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Conserved domains on  [gi|493538075|ref|WP_006491972|]
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MULTISPECIES: elongation factor G [Mesotoga]

Protein Classification

elongation factor G( domain architecture ID 11422284)

elongation factor G catalyzes the translocation step of protein synthesis in bacteria and mitochondria

Gene Ontology:  GO:0006414|GO:0005525
PubMed:  17214893|11916378

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
1-686 0e+00

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: 969.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075   1 MDKIPVDAKRDIVLIGHHGSGKTQIVDAMLFNAKLIDRIGILA-----TDSEEVEKEKKASFSMGVTSLPHNDKRIYVID 75
Cdd:COG0480    1 MAEYPLEKIRNIGIVAHIDAGKTTLTERILFYTGAIHRIGEVHdgntvMDWMPEEQERGITITSAATTCEWKGHKINIID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  76 TPGMSDFYAETANGIFASENVVAVINSTAGLEIQTERFGSIAKELKKGIIAFFNMLDKERAGYEETLSDLADTFERTPVL 155
Cdd:COG0480   81 TPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQLKERLGANPVP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 156 VQLPIGREADFRGIVDLVKMKAYIYENEG--AFKEEDIPADLKSAAEESRTKMIEDIVQNDEELMMKYLEGEELSTEELI 233
Cdd:COG0480  161 LQLPIGAEDDFKGVIDLVTMKAYVYDDELgaKYEEEEIPAELKEEAEEAREELIEAVAETDDELMEKYLEGEELTEEEIK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 234 TALRKAYLANEVIPVLLGSAGKNIGISQLLDFVSAVGKGPSEASPKAATLL-SGEKIDVVPAEEEPLVAYIFKSVVDPFV 312
Cdd:COG0480  241 AGLRKATLAGKIVPVLCGSAFKNKGVQPLLDAVVDYLPSPLDVPAIKGVDPdTGEEVERKPDDDEPFSALVFKTMTDPFV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 313 GKLTFMKLLSGTLKQGDSFYVVDQDSSEKVGHVMLPEGTKEIEVDEATVGDIVKLSKLKKSAAGNTVAHKDRQLKLDLPV 392
Cdd:COG0480  321 GKLSFFRVYSGTLKSGSTVYNSTKGKKERIGRLLRMHGNKREEVDEAGAGDIVAVVKLKDTTTGDTLCDEDHPIVLEPIE 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 393 MPEPMISKSIQPKSKGDIDKISGGLARLAESDPTFKWENDPETNETVISGLGSVHLDIMIERLKKLFSVDVEVGKPKIAY 472
Cdd:COG0480  401 FPEPVISVAIEPKTKADEDKLSTALAKLAEEDPTFRVETDEETGQTIISGMGELHLEIIVDRLKREFGVEVNVGKPQVAY 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 473 RETVRKTVEAEYKHKKQTGGHGQYGHVQIKIEPNERGAGFEFIDKIVGGVVPKNYIPAVEKGIVEAMKKGVLASYPVVDA 552
Cdd:COG0480  481 RETIRKKAEAEGKHKKQSGGHGQYGDVWIEIEPLPRGEGFEFVDKIVGGVIPKEYIPAVEKGIREAMEKGVLAGYPVVDV 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 553 KVTLFYGSYHDVDSSDMSFQIAARQAFKNGMAEANPVILEPLMDVEVFVPEESTGDIMGEITSRRGRPMGMEPQGkGTSK 632
Cdd:COG0480  561 KVTLYDGSYHPVDSSEMAFKIAASMAFKEAAKKAKPVLLEPIMKVEVTVPEEYMGDVMGDLNSRRGRILGMESRG-GAQV 639
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493538075 633 VVAQVPLAEMLDFANKLSSITSGRGYFTMKFSGYQETPPDVQQKIILERQRELE 686
Cdd:COG0480  640 IKAEVPLAEMFGYATDLRSLTQGRGSFTMEFSHYEEVPANVAEKIIAKRKAEKE 693
 
Name Accession Description Interval E-value
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
1-686 0e+00

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: 969.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075   1 MDKIPVDAKRDIVLIGHHGSGKTQIVDAMLFNAKLIDRIGILA-----TDSEEVEKEKKASFSMGVTSLPHNDKRIYVID 75
Cdd:COG0480    1 MAEYPLEKIRNIGIVAHIDAGKTTLTERILFYTGAIHRIGEVHdgntvMDWMPEEQERGITITSAATTCEWKGHKINIID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  76 TPGMSDFYAETANGIFASENVVAVINSTAGLEIQTERFGSIAKELKKGIIAFFNMLDKERAGYEETLSDLADTFERTPVL 155
Cdd:COG0480   81 TPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQLKERLGANPVP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 156 VQLPIGREADFRGIVDLVKMKAYIYENEG--AFKEEDIPADLKSAAEESRTKMIEDIVQNDEELMMKYLEGEELSTEELI 233
Cdd:COG0480  161 LQLPIGAEDDFKGVIDLVTMKAYVYDDELgaKYEEEEIPAELKEEAEEAREELIEAVAETDDELMEKYLEGEELTEEEIK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 234 TALRKAYLANEVIPVLLGSAGKNIGISQLLDFVSAVGKGPSEASPKAATLL-SGEKIDVVPAEEEPLVAYIFKSVVDPFV 312
Cdd:COG0480  241 AGLRKATLAGKIVPVLCGSAFKNKGVQPLLDAVVDYLPSPLDVPAIKGVDPdTGEEVERKPDDDEPFSALVFKTMTDPFV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 313 GKLTFMKLLSGTLKQGDSFYVVDQDSSEKVGHVMLPEGTKEIEVDEATVGDIVKLSKLKKSAAGNTVAHKDRQLKLDLPV 392
Cdd:COG0480  321 GKLSFFRVYSGTLKSGSTVYNSTKGKKERIGRLLRMHGNKREEVDEAGAGDIVAVVKLKDTTTGDTLCDEDHPIVLEPIE 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 393 MPEPMISKSIQPKSKGDIDKISGGLARLAESDPTFKWENDPETNETVISGLGSVHLDIMIERLKKLFSVDVEVGKPKIAY 472
Cdd:COG0480  401 FPEPVISVAIEPKTKADEDKLSTALAKLAEEDPTFRVETDEETGQTIISGMGELHLEIIVDRLKREFGVEVNVGKPQVAY 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 473 RETVRKTVEAEYKHKKQTGGHGQYGHVQIKIEPNERGAGFEFIDKIVGGVVPKNYIPAVEKGIVEAMKKGVLASYPVVDA 552
Cdd:COG0480  481 RETIRKKAEAEGKHKKQSGGHGQYGDVWIEIEPLPRGEGFEFVDKIVGGVIPKEYIPAVEKGIREAMEKGVLAGYPVVDV 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 553 KVTLFYGSYHDVDSSDMSFQIAARQAFKNGMAEANPVILEPLMDVEVFVPEESTGDIMGEITSRRGRPMGMEPQGkGTSK 632
Cdd:COG0480  561 KVTLYDGSYHPVDSSEMAFKIAASMAFKEAAKKAKPVLLEPIMKVEVTVPEEYMGDVMGDLNSRRGRILGMESRG-GAQV 639
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493538075 633 VVAQVPLAEMLDFANKLSSITSGRGYFTMKFSGYQETPPDVQQKIILERQRELE 686
Cdd:COG0480  640 IKAEVPLAEMFGYATDLRSLTQGRGSFTMEFSHYEEVPANVAEKIIAKRKAEKE 693
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
15-678 0e+00

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 861.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  15 IGHHGSGKTQIVDAMLFNAKLIDRIGILA-----TDSEEVEKEKKASFSMGVTSLPHNDKRIYVIDTPGMSDFYAETANG 89
Cdd:PRK12740   1 VGHSGAGKTTLTEAILFYTGAIHRIGEVEdgtttMDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVERA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  90 IFASENVVAVINSTAGLEIQTERFGSIAKELKKGIIAFFNMLDKERAGYEETLSDLADTFERTPVLVQLPIGREADFRGI 169
Cdd:PRK12740  81 LRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRAGADFFRVLAQLQEKLGAPVVPLQLPIGEGDDFTGV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 170 VDLVKMKAYIYENEGAFKEEDIPADLKSAAEESRTKMIEDIVQNDEELMMKYLEGEELSTEELITALRKAYLANEVIPVL 249
Cdd:PRK12740 161 VDLLSMKAYRYDEGGPSEEIEIPAELLDRAEEAREELLEALAEFDDELMEKYLEGEELSEEEIKAGLRKATLAGEIVPVF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 250 LGSAGKNIGISQLLDFVSAVGKGPSEAsPKAATLLSGEKIDVVPAEEEPLVAYIFKSVVDPFVGKLTFMKLLSGTLKQGD 329
Cdd:PRK12740 241 CGSALKNKGVQRLLDAVVDYLPSPLEV-PPVDGEDGEEGAELAPDPDGPLVALVFKTMDDPFVGKLSLVRVYSGTLKKGD 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 330 SFYVVDQDSSEKVGHVMLPEGTKEIEVDEATVGDIVKLSKLKKSAAGNTVAHKDRQLKLDLPVMPEPMISKSIQPKSKGD 409
Cdd:PRK12740 320 TLYNSGTGKKERVGRLYRMHGKQREEVDEAVAGDIVAVAKLKDAATGDTLCDKGDPILLEPMEFPEPVISLAIEPKDKGD 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 410 IDKISGGLARLAESDPTFKWENDPETNETVISGLGSVHLDIMIERLKKLFSVDVEVGKPKIAYRETVRKTVEAEYKHKKQ 489
Cdd:PRK12740 400 EEKLSEALGKLAEEDPTLRVERDEETGQTILSGMGELHLDVALERLKREYGVEVETGPPQVPYRETIRKKAEGHGRHKKQ 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 490 TGGHGQYGHVQIKIEPNERGAGFEFIDKIVGGVVPKNYIPAVEKGIVEAMKKGVLASYPVVDAKVTLFYGSYHDVDSSDM 569
Cdd:PRK12740 480 SGGHGQFGDVWLEVEPLPRGEGFEFVDKVVGGAVPRQYIPAVEKGVREALEKGVLAGYPVVDVKVTLTDGSYHSVDSSEM 559
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 570 SFQIAARQAFKNGMAEANPVILEPLMDVEVFVPEESTGDIMGEITSRRGRPMGMEPQGKGTsKVVAQVPLAEMLDFANKL 649
Cdd:PRK12740 560 AFKIAARLAFREALPKAKPVLLEPIMKVEVSVPEEFVGDVIGDLSSRRGRILGMESRGGGD-VVRAEVPLAEMFGYATDL 638
                        650       660
                 ....*....|....*....|....*....
gi 493538075 650 SSITSGRGYFTMKFSGYQETPPDVQQKII 678
Cdd:PRK12740 639 RSLTQGRGSFSMEFSHYEEVPGNVAEKVI 667
EF-G TIGR00484
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ...
3-682 0e+00

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: 624.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075    3 KIPVDAKRDIVLIGHHGSGKTQIVDAMLFNAKLIDRI-----GILATDSEEVEKEKKASFSMGVTSLPHNDKRIYVIDTP 77
Cdd:TIGR00484   4 TTDLNRFRNIGISAHIDAGKTTTTERILFYTGRIHKIgevhdGAATMDWMEQEKERGITITSAATTVFWKGHRINIIDTP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075   78 GMSDFYAETANGIFASENVVAVINSTAGLEIQTERFGSIAKELKKGIIAFFNMLDKERAGYEETLSDLADTFERTPVLVQ 157
Cdd:TIGR00484  84 GHVDFTVEVERSLRVLDGAVAVLDAVGGVQPQSETVWRQANRYEVPRIAFVNKMDKTGANFLRVVNQIKQRLGANAVPIQ 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  158 LPIGREADFRGIVDLVKMKAYIYE-NEGA-FKEEDIPADLKSAAEESRTKMIEDIVQNDEELMMKYLEGEELSTEELITA 235
Cdd:TIGR00484 164 LPIGAEDNFIGVIDLVEMKAYFFNgDKGTkAIEKEIPSDLLEQAKELRENLVEAVAEFDEELMEKYLEGEELTIEEIKNA 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  236 LRKAYLANEVIPVLLGSAGKNIGISQLLDFVSAVGKGPSEASPKAATLLSGEK-IDVVPAEEEPLVAYIFKSVVDPFVGK 314
Cdd:TIGR00484 244 IRKGVLNCEFFPVLCGSAFKNKGVQLLLDAVVDYLPSPTDVPAIKGIDPDTEKeIERKASDDEPFSALAFKVATDPFVGQ 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  315 LTFMKLLSGTLKQGDSFYVVDQDSSEKVGHVMLPEGTKEIEVDEATVGDIVKLSKLKKSAAGNTVAHKDRQLKLDLPVMP 394
Cdd:TIGR00484 324 LTFVRVYSGVLKSGSYVKNSRKNKKERVGRLVKMHANNREEIKEVRAGDICAAIGLKDTTTGDTLCDPKIDVILERMEFP 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  395 EPMISKSIQPKSKGDIDKISGGLARLAESDPTFKWENDPETNETVISGLGSVHLDIMIERLKKLFSVDVEVGKPKIAYRE 474
Cdd:TIGR00484 404 EPVISLAVEPKTKADQEKMGIALGKLAEEDPTFRTFTDPETGQTIIAGMGELHLDIIVDRMKREFKVEANVGAPQVAYRE 483
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  475 TVRKTVEAEYKHKKQTGGHGQYGHVQIKIEPNERGaGFEFIDKIVGGVVPKNYIPAVEKGIVEAMKKGVLASYPVVDAKV 554
Cdd:TIGR00484 484 TIRSKVEVEGKHAKQSGGRGQYGHVKIRFEPLEPK-GYEFVNEIKGGVIPREYIPAVDKGLQEAMESGPLAGYPVVDIKA 562
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  555 TLFYGSYHDVDSSDMSFQIAARQAFKNGMAEANPVILEPLMDVEVFVPEESTGDIMGEITSRRGRPMGMEPQGkGTSKVV 634
Cdd:TIGR00484 563 TLFDGSYHDVDSSEMAFKLAASLAFKEAGKKANPVLLEPIMKVEVEVPEEYMGDVMGDLSSRRGIIEGMEARG-NVQKIK 641
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*...
gi 493538075  635 AQVPLAEMLDFANKLSSITSGRGYFTMKFSGYQETPPDVQQKIILERQ 682
Cdd:TIGR00484 642 AEVPLSEMFGYATDLRSFTQGRGTYSMEFLHYGEVPSSVANEIIEKRK 689
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
12-273 1.07e-86

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: 272.93  E-value: 1.07e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  12 IVLIGHHGSGKTQIVDAMLFNAKLIDRIGIL-----ATDSEEVEKEKKASFSMGVTSLPHNDKRIYVIDTPGMSDFYAET 86
Cdd:cd04170    2 IALVGHSGSGKTTLAEALLYATGAIDRLGRVedgntVSDYDPEEKKRKMSIETSVAPLEWNGHKINLIDTPGYADFVGET 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  87 ANGIFASENVVAVINSTAGLEIQTERFGSIAKELKKGIIAFFNMLDKERAGYEETLSDLADTFERTPVLVQLPIGREADF 166
Cdd:cd04170   82 LSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRARADFDKTLAALREAFGRPVVPIQLPIGEGDEF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 167 RGIVDLVKMKAYIYENEGAFKEEDIPADLKSAAEESRTKMIEDIVQNDEELMMKYLEGEELSTEELITALRKAYLANEVI 246
Cdd:cd04170  162 TGVVDLLSEKAYRYDPGEPSVEIEIPEELKEKVAEAREELLEAVAETDEELMEKYLEEGELTEEELRAGLRRALRAGLIV 241
                        250       260
                 ....*....|....*....|....*..
gi 493538075 247 PVLLGSAGKNIGISQLLDFVSAVGKGP 273
Cdd:cd04170  242 PVFFGSALTGIGVRRLLDALVELAPSP 268
EFG_IV pfam03764
Elongation factor G, domain IV; This domain is found in elongation factor G, elongation factor ...
468-587 3.34e-58

Elongation factor G, domain IV; This domain is found in elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopts a ribosomal protein S5 domain 2-like fold.


Pssm-ID: 397710 [Multi-domain]  Cd Length: 121  Bit Score: 192.43  E-value: 3.34e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  468 PKIAYRETVRKTVEA-EYKHKKQTGGHGQYGHVQIKIEPNERGAGFEFIDKIVGGVVPKNYIPAVEKGIVEAMKKGVLAS 546
Cdd:pfam03764   1 PQVAYRETIRKPVKErAYKHKKQSGGDGQYARVILRIEPLPPGSGNEFVDETVGGQIPKEFIPAVEKGFQEAMKEGPLAG 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 493538075  547 YPVVDAKVTLFYGSYHDVDSSDMSFQIAARQAFKNGMAEAN 587
Cdd:pfam03764  81 EPVTDVKVTLLDGSYHEVDSSEAAFIPAARRAFREALLKAS 121
EFG_IV smart00889
Elongation factor G, domain IV; Translation elongation factors are responsible for two main ...
469-587 1.22e-56

Elongation factor G, domain IV; Translation elongation factors are responsible for two main processes during protein synthesis on the ribosome. EF1A (or EF-Tu) is responsible for the selection and binding of the cognate aminoacyl-tRNA to the A-site (acceptor site) of the ribosome. EF2 (or EF-G) is responsible for the translocation of the peptidyl-tRNA from the A-site to the P-site (peptidyl-tRNA site) of the ribosome, thereby freeing the A-site for the next aminoacyl-tRNA to bind. Elongation factors are responsible for achieving accuracy of translation and both EF1A and EF2 are remarkably conserved throughout evolution. Elongation factor EF2 (EF-G) is a G-protein. It brings about the translocation of peptidyl-tRNA and mRNA through a ratchet-like mechanism: the binding of GTP-EF2 to the ribosome causes a counter-clockwise rotation in the small ribosomal subunit; the hydrolysis of GTP to GDP by EF2 and the subsequent release of EF2 causes a clockwise rotation of the small subunit back to the starting position. This twisting action destabilises tRNA-ribosome interactions, freeing the tRNA to translocate along the ribosome upon GTP-hydrolysis by EF2. EF2 binding also affects the entry and exit channel openings for the mRNA, widening it when bound to enable the mRNA to translocate along the ribosome. EF2 has five domains. This entry represents domain IV found in EF2 (or EF-G) of both prokaryotes and eukaryotes. The EF2-GTP-ribosome complex undergoes extensive structural rearrangement for tRNA-mRNA movement to occur. Domain IV, which extends from the 'body' of the EF2 molecule much like a lever arm, appears to be essential for the structural transition to take place.


Pssm-ID: 214887 [Multi-domain]  Cd Length: 120  Bit Score: 188.14  E-value: 1.22e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075   469 KIAYRETVRKTV-EAEYKHKKQTGGHGQYGHVQIKIEPNERGAGFEFIDKIVGGVVPKNYIPAVEKGIVEAMKKGVLASY 547
Cdd:smart00889   1 QVAYRETITKPVkEAEGKHKKQSGGDGQYARVILEVEPLERGSGFEFDDTIVGGVIPKEYIPAVEKGFREALEEGPLAGY 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 493538075   548 PVVDAKVTLFYGSYHDVDSSDMSFQIAARQAFKNGMAEAN 587
Cdd:smart00889  81 PVVDVKVTLLDGSYHEVDSSEMAFKPAARRAFKEALLKAG 120
 
Name Accession Description Interval E-value
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
1-686 0e+00

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: 969.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075   1 MDKIPVDAKRDIVLIGHHGSGKTQIVDAMLFNAKLIDRIGILA-----TDSEEVEKEKKASFSMGVTSLPHNDKRIYVID 75
Cdd:COG0480    1 MAEYPLEKIRNIGIVAHIDAGKTTLTERILFYTGAIHRIGEVHdgntvMDWMPEEQERGITITSAATTCEWKGHKINIID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  76 TPGMSDFYAETANGIFASENVVAVINSTAGLEIQTERFGSIAKELKKGIIAFFNMLDKERAGYEETLSDLADTFERTPVL 155
Cdd:COG0480   81 TPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQLKERLGANPVP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 156 VQLPIGREADFRGIVDLVKMKAYIYENEG--AFKEEDIPADLKSAAEESRTKMIEDIVQNDEELMMKYLEGEELSTEELI 233
Cdd:COG0480  161 LQLPIGAEDDFKGVIDLVTMKAYVYDDELgaKYEEEEIPAELKEEAEEAREELIEAVAETDDELMEKYLEGEELTEEEIK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 234 TALRKAYLANEVIPVLLGSAGKNIGISQLLDFVSAVGKGPSEASPKAATLL-SGEKIDVVPAEEEPLVAYIFKSVVDPFV 312
Cdd:COG0480  241 AGLRKATLAGKIVPVLCGSAFKNKGVQPLLDAVVDYLPSPLDVPAIKGVDPdTGEEVERKPDDDEPFSALVFKTMTDPFV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 313 GKLTFMKLLSGTLKQGDSFYVVDQDSSEKVGHVMLPEGTKEIEVDEATVGDIVKLSKLKKSAAGNTVAHKDRQLKLDLPV 392
Cdd:COG0480  321 GKLSFFRVYSGTLKSGSTVYNSTKGKKERIGRLLRMHGNKREEVDEAGAGDIVAVVKLKDTTTGDTLCDEDHPIVLEPIE 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 393 MPEPMISKSIQPKSKGDIDKISGGLARLAESDPTFKWENDPETNETVISGLGSVHLDIMIERLKKLFSVDVEVGKPKIAY 472
Cdd:COG0480  401 FPEPVISVAIEPKTKADEDKLSTALAKLAEEDPTFRVETDEETGQTIISGMGELHLEIIVDRLKREFGVEVNVGKPQVAY 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 473 RETVRKTVEAEYKHKKQTGGHGQYGHVQIKIEPNERGAGFEFIDKIVGGVVPKNYIPAVEKGIVEAMKKGVLASYPVVDA 552
Cdd:COG0480  481 RETIRKKAEAEGKHKKQSGGHGQYGDVWIEIEPLPRGEGFEFVDKIVGGVIPKEYIPAVEKGIREAMEKGVLAGYPVVDV 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 553 KVTLFYGSYHDVDSSDMSFQIAARQAFKNGMAEANPVILEPLMDVEVFVPEESTGDIMGEITSRRGRPMGMEPQGkGTSK 632
Cdd:COG0480  561 KVTLYDGSYHPVDSSEMAFKIAASMAFKEAAKKAKPVLLEPIMKVEVTVPEEYMGDVMGDLNSRRGRILGMESRG-GAQV 639
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493538075 633 VVAQVPLAEMLDFANKLSSITSGRGYFTMKFSGYQETPPDVQQKIILERQRELE 686
Cdd:COG0480  640 IKAEVPLAEMFGYATDLRSLTQGRGSFTMEFSHYEEVPANVAEKIIAKRKAEKE 693
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
15-678 0e+00

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 861.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  15 IGHHGSGKTQIVDAMLFNAKLIDRIGILA-----TDSEEVEKEKKASFSMGVTSLPHNDKRIYVIDTPGMSDFYAETANG 89
Cdd:PRK12740   1 VGHSGAGKTTLTEAILFYTGAIHRIGEVEdgtttMDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVERA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  90 IFASENVVAVINSTAGLEIQTERFGSIAKELKKGIIAFFNMLDKERAGYEETLSDLADTFERTPVLVQLPIGREADFRGI 169
Cdd:PRK12740  81 LRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRAGADFFRVLAQLQEKLGAPVVPLQLPIGEGDDFTGV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 170 VDLVKMKAYIYENEGAFKEEDIPADLKSAAEESRTKMIEDIVQNDEELMMKYLEGEELSTEELITALRKAYLANEVIPVL 249
Cdd:PRK12740 161 VDLLSMKAYRYDEGGPSEEIEIPAELLDRAEEAREELLEALAEFDDELMEKYLEGEELSEEEIKAGLRKATLAGEIVPVF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 250 LGSAGKNIGISQLLDFVSAVGKGPSEAsPKAATLLSGEKIDVVPAEEEPLVAYIFKSVVDPFVGKLTFMKLLSGTLKQGD 329
Cdd:PRK12740 241 CGSALKNKGVQRLLDAVVDYLPSPLEV-PPVDGEDGEEGAELAPDPDGPLVALVFKTMDDPFVGKLSLVRVYSGTLKKGD 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 330 SFYVVDQDSSEKVGHVMLPEGTKEIEVDEATVGDIVKLSKLKKSAAGNTVAHKDRQLKLDLPVMPEPMISKSIQPKSKGD 409
Cdd:PRK12740 320 TLYNSGTGKKERVGRLYRMHGKQREEVDEAVAGDIVAVAKLKDAATGDTLCDKGDPILLEPMEFPEPVISLAIEPKDKGD 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 410 IDKISGGLARLAESDPTFKWENDPETNETVISGLGSVHLDIMIERLKKLFSVDVEVGKPKIAYRETVRKTVEAEYKHKKQ 489
Cdd:PRK12740 400 EEKLSEALGKLAEEDPTLRVERDEETGQTILSGMGELHLDVALERLKREYGVEVETGPPQVPYRETIRKKAEGHGRHKKQ 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 490 TGGHGQYGHVQIKIEPNERGAGFEFIDKIVGGVVPKNYIPAVEKGIVEAMKKGVLASYPVVDAKVTLFYGSYHDVDSSDM 569
Cdd:PRK12740 480 SGGHGQFGDVWLEVEPLPRGEGFEFVDKVVGGAVPRQYIPAVEKGVREALEKGVLAGYPVVDVKVTLTDGSYHSVDSSEM 559
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 570 SFQIAARQAFKNGMAEANPVILEPLMDVEVFVPEESTGDIMGEITSRRGRPMGMEPQGKGTsKVVAQVPLAEMLDFANKL 649
Cdd:PRK12740 560 AFKIAARLAFREALPKAKPVLLEPIMKVEVSVPEEFVGDVIGDLSSRRGRILGMESRGGGD-VVRAEVPLAEMFGYATDL 638
                        650       660
                 ....*....|....*....|....*....
gi 493538075 650 SSITSGRGYFTMKFSGYQETPPDVQQKII 678
Cdd:PRK12740 639 RSLTQGRGSFSMEFSHYEEVPGNVAEKVI 667
PRK13351 PRK13351
elongation factor G-like protein;
5-680 0e+00

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 674.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075   5 PVDAKRDIVLIGHHGSGKTQIVDAMLFNAKLIDRIGIL-----ATDSEEVEKEKKASFSMGVTSLPHNDKRIYVIDTPGM 79
Cdd:PRK13351   4 PLMQIRNIGILAHIDAGKTTLTERILFYTGKIHKMGEVedgttVTDWMPQEQERGITIESAATSCDWDNHRINLIDTPGH 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  80 SDFYAETANGIFASENVVAVINSTAGLEIQTERFGSIAKELKKGIIAFFNMLDKERAGYEETLSDLADTFERTPVLVQLP 159
Cdd:PRK13351  84 IDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLFKVLEDIEERFGKRPLPLQLP 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 160 IGREADFRGIVDLVKMKAYIYENEGA---FKEEDIPADLKSAAEESRTKMIEDIVQNDEELMMKYLEGEELSTEELITAL 236
Cdd:PRK13351 164 IGSEDGFEGVVDLITEPELHFSEGDGgstVEEGPIPEELLEEVEEAREKLIEALAEFDDELLELYLEGEELSAEQLRAPL 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 237 RKAYLANEVIPVLLGSAGKNIGISQLLDFVSAVGKGPSEASPKAATLLSGEKIDVVPAEEEPLVAYIFKSVVDPFVGKLT 316
Cdd:PRK13351 244 REGTRSGHLVPVLFGSALKNIGIEPLLDAVVDYLPSPLEVPPPRGSKDNGKPVKVDPDPEKPLLALVFKVQYDPYAGKLT 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 317 FMKLLSGTLKQGDSFYVVDQDSSEKVGHVMLPEGTKEIEVDEATVGDIVKLSKLKKSAAGNTVAHKDRQLKLDLPVMPEP 396
Cdd:PRK13351 324 YLRVYSGTLRAGSQLYNGTGGKREKVGRLFRLQGNKREEVDRAKAGDIVAVAGLKELETGDTLHDSADPVLLELLTFPEP 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 397 MISKSIQPKSKGDIDKISGGLARLAESDPTFKWENDPETNETVISGLGSVHLDIMIERLKKLFSVDVEVGKPKIAYRETV 476
Cdd:PRK13351 404 VVSLAVEPERRGDEQKLAEALEKLVWEDPSLRVEEDEETGQTILSGMGELHLEVALERLRREFKLEVNTGKPQVAYRETI 483
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 477 RKTVEAEYKHKKQTGGHGQYGHVQIKIEPNERGAGFEFIDKIVGGVVPKNYIPAVEKGIVEAMKKGVLASYPVVDAKVTL 556
Cdd:PRK13351 484 RKMAEGVYRHKKQFGGKGQFGEVHLRVEPLERGAGFIFVSKVVGGAIPEELIPAVEKGIREALASGPLAGYPVTDLRVTV 563
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 557 FYGSYHDVDSSDMSFQIAARQAFKNGMAEANPVILEPLMDVEVFVPEESTGDIMGEITSRRGRPMGMEPQGKGTSKVVAQ 636
Cdd:PRK13351 564 LDGKYHPVDSSESAFKAAARKAFLEAFRKANPVLLEPIMELEITVPTEHVGDVLGDLSQRRGRIEGTEPRGDGEVLVKAE 643
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|....
gi 493538075 637 VPLAEMLDFANKLSSITSGRGYFTMKFSGYQETPPDVQQKIILE 680
Cdd:PRK13351 644 APLAELFGYATRLRSMTKGRGSFTMEFSHFDPVPPAVQKKVGSK 687
EF-G TIGR00484
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ...
3-682 0e+00

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: 624.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075    3 KIPVDAKRDIVLIGHHGSGKTQIVDAMLFNAKLIDRI-----GILATDSEEVEKEKKASFSMGVTSLPHNDKRIYVIDTP 77
Cdd:TIGR00484   4 TTDLNRFRNIGISAHIDAGKTTTTERILFYTGRIHKIgevhdGAATMDWMEQEKERGITITSAATTVFWKGHRINIIDTP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075   78 GMSDFYAETANGIFASENVVAVINSTAGLEIQTERFGSIAKELKKGIIAFFNMLDKERAGYEETLSDLADTFERTPVLVQ 157
Cdd:TIGR00484  84 GHVDFTVEVERSLRVLDGAVAVLDAVGGVQPQSETVWRQANRYEVPRIAFVNKMDKTGANFLRVVNQIKQRLGANAVPIQ 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  158 LPIGREADFRGIVDLVKMKAYIYE-NEGA-FKEEDIPADLKSAAEESRTKMIEDIVQNDEELMMKYLEGEELSTEELITA 235
Cdd:TIGR00484 164 LPIGAEDNFIGVIDLVEMKAYFFNgDKGTkAIEKEIPSDLLEQAKELRENLVEAVAEFDEELMEKYLEGEELTIEEIKNA 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  236 LRKAYLANEVIPVLLGSAGKNIGISQLLDFVSAVGKGPSEASPKAATLLSGEK-IDVVPAEEEPLVAYIFKSVVDPFVGK 314
Cdd:TIGR00484 244 IRKGVLNCEFFPVLCGSAFKNKGVQLLLDAVVDYLPSPTDVPAIKGIDPDTEKeIERKASDDEPFSALAFKVATDPFVGQ 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  315 LTFMKLLSGTLKQGDSFYVVDQDSSEKVGHVMLPEGTKEIEVDEATVGDIVKLSKLKKSAAGNTVAHKDRQLKLDLPVMP 394
Cdd:TIGR00484 324 LTFVRVYSGVLKSGSYVKNSRKNKKERVGRLVKMHANNREEIKEVRAGDICAAIGLKDTTTGDTLCDPKIDVILERMEFP 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  395 EPMISKSIQPKSKGDIDKISGGLARLAESDPTFKWENDPETNETVISGLGSVHLDIMIERLKKLFSVDVEVGKPKIAYRE 474
Cdd:TIGR00484 404 EPVISLAVEPKTKADQEKMGIALGKLAEEDPTFRTFTDPETGQTIIAGMGELHLDIIVDRMKREFKVEANVGAPQVAYRE 483
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  475 TVRKTVEAEYKHKKQTGGHGQYGHVQIKIEPNERGaGFEFIDKIVGGVVPKNYIPAVEKGIVEAMKKGVLASYPVVDAKV 554
Cdd:TIGR00484 484 TIRSKVEVEGKHAKQSGGRGQYGHVKIRFEPLEPK-GYEFVNEIKGGVIPREYIPAVDKGLQEAMESGPLAGYPVVDIKA 562
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  555 TLFYGSYHDVDSSDMSFQIAARQAFKNGMAEANPVILEPLMDVEVFVPEESTGDIMGEITSRRGRPMGMEPQGkGTSKVV 634
Cdd:TIGR00484 563 TLFDGSYHDVDSSEMAFKLAASLAFKEAGKKANPVLLEPIMKVEVEVPEEYMGDVMGDLSSRRGIIEGMEARG-NVQKIK 641
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*...
gi 493538075  635 AQVPLAEMLDFANKLSSITSGRGYFTMKFSGYQETPPDVQQKIILERQ 682
Cdd:TIGR00484 642 AEVPLSEMFGYATDLRSFTQGRGTYSMEFLHYGEVPSSVANEIIEKRK 689
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
12-273 1.07e-86

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: 272.93  E-value: 1.07e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  12 IVLIGHHGSGKTQIVDAMLFNAKLIDRIGIL-----ATDSEEVEKEKKASFSMGVTSLPHNDKRIYVIDTPGMSDFYAET 86
Cdd:cd04170    2 IALVGHSGSGKTTLAEALLYATGAIDRLGRVedgntVSDYDPEEKKRKMSIETSVAPLEWNGHKINLIDTPGYADFVGET 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  87 ANGIFASENVVAVINSTAGLEIQTERFGSIAKELKKGIIAFFNMLDKERAGYEETLSDLADTFERTPVLVQLPIGREADF 166
Cdd:cd04170   82 LSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRARADFDKTLAALREAFGRPVVPIQLPIGEGDEF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 167 RGIVDLVKMKAYIYENEGAFKEEDIPADLKSAAEESRTKMIEDIVQNDEELMMKYLEGEELSTEELITALRKAYLANEVI 246
Cdd:cd04170  162 TGVVDLLSEKAYRYDPGEPSVEIEIPEELKEKVAEAREELLEAVAETDEELMEKYLEEGELTEEELRAGLRRALRAGLIV 241
                        250       260
                 ....*....|....*....|....*..
gi 493538075 247 PVLLGSAGKNIGISQLLDFVSAVGKGP 273
Cdd:cd04170  242 PVFFGSALTGIGVRRLLDALVELAPSP 268
EFG_mtEFG1_IV cd01434
EFG_mtEFG1_IV: domains similar to domain IV of the bacterial translational elongation factor ...
472-587 1.82e-71

EFG_mtEFG1_IV: domains similar to domain IV of the bacterial translational elongation factor (EF) EF-G. Included in this group is a domain of mitochondrial Elongation factor G1 (mtEFG1) proteins homologous to domain IV of EF-G. 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. There are two forms of mtEFG present in mammals (designated mtEFG1s and mtEFG2s) mtEFG2s are not present in this group.


Pssm-ID: 238715 [Multi-domain]  Cd Length: 116  Bit Score: 227.32  E-value: 1.82e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 472 YRETVRKTVEAEYKHKKQTGGHGQYGHVQIKIEPNERGAGFEFIDKIVGGVVPKNYIPAVEKGIVEAMKKGVLASYPVVD 551
Cdd:cd01434    1 YRETITKPAEFEYRHKKQSGGAGQYGHVVLEIEPLPRGSGFEFVNKIVGGAIPKEYIPAVEKGFREALEKGPLAGYPVVD 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 493538075 552 AKVTLFYGSYHDVDSSDMSFQIAARQAFKNGMAEAN 587
Cdd:cd01434   81 VKVTLYDGSYHDVDSSEMAFKIAARMAFKEAFKKAK 116
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
12-266 3.25e-61

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: 205.80  E-value: 3.25e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  12 IVLIGHHGSGKTQIVDAMLFNAKLIDRIGIL-----ATDSEEVEKEKKASFSMGVTSLPHNDKRIYVIDTPGMSDFYAET 86
Cdd:cd01886    2 IGIIAHIDAGKTTTTERILYYTGRIHKIGEVhgggaTMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDFTIEV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  87 ANGIFASENVVAVINSTAGLEIQTERFGSIAKELKKGIIAFFNMLDKERAGYEETLSDLADTFERTPVLVQLPIGREADF 166
Cdd:cd01886   82 ERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQIREKLGANPVPLQLPIGAEDDF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 167 RGIVDLVKMKAYIYENEGAFK--EEDIPADLKSAAEESRTKMIEDIVQNDEELMMKYLEGEELSTEELITALRKAYLANE 244
Cdd:cd01886  162 EGVVDLIEMKALYWDGELGEKieETDIPEDLLEEAEEAREELIETLAEVDDELMEKYLEGEEITEEEIKAAIRKGTIANK 241
                        250       260
                 ....*....|....*....|..
gi 493538075 245 VIPVLLGSAGKNIGISQLLDFV 266
Cdd:cd01886  242 IVPVLCGSAFKNKGVQPLLDAV 263
PRK07560 PRK07560
elongation factor EF-2; Reviewed
298-683 6.37e-59

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 211.65  E-value: 6.37e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 298 PLVAYIFKSVVDPFVGKLTFMKLLSGTLKQGDSFYVVDQDSSEKVGHVMLPEGTKEIEVDEATVGDIVKLSKLKKSAAGN 377
Cdd:PRK07560 290 PLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLVGAKKKNRVQQVGIYMGPEREEVEEIPAGNIAAVTGLKDARAGE 369
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 378 TVAhkdrqlklDLPVMP---------EPMISKSIQPKSKGDIDKISGGLARLAESDPTFKWENDPETNETVISGLGSVHL 448
Cdd:PRK07560 370 TVV--------SVEDMTpfeslkhisEPVVTVAIEAKNPKDLPKLIEVLRQLAKEDPTLVVKINEETGEHLLSGMGELHL 441
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 449 DIMIERLKKLFSVDVEVGKPKIAYRETVRKT---VEAEY--KHKK-------------QTGGHGQYGHVQIKIEPNER-- 508
Cdd:PRK07560 442 EVITYRIKRDYGIEVVTSEPIVVYRETVRGKsqvVEGKSpnKHNRfyisvepleeeviEAIKEGEISEDMDKKEAKILre 521
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 509 ---GAGFE---------------FIDKIVGGVVPKNYIPAVEKGIVEAMKKGVLASYPVVDAKVTLfygsyHDVDSSDMS 570
Cdd:PRK07560 522 kliEAGMDkdeakrvwaiyngnvFIDMTKGIQYLNEVMELIIEGFREAMKEGPLAAEPVRGVKVRL-----HDAKLHEDA 596
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 571 F-----QI--AARQAFKNGMAEANPVILEPLMDVEVFVPEESTGDIMGEITSRRGRPMGMEPQGkGTSKVVAQVPLAEML 643
Cdd:PRK07560 597 IhrgpaQVipAVRNAIFAAMLTAKPTLLEPIQKVDINVPQDYMGAVTREIQGRRGKILDMEQEG-DMAIIEAEAPVAEMF 675
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 493538075 644 DFANKLSSITSGRGYFTMKFSGYQETPPDVQQKIILE-RQR 683
Cdd:PRK07560 676 GFAGEIRSATEGRALWSTEFAGFEPVPDSLQLDIVRQiRER 716
EFG_IV pfam03764
Elongation factor G, domain IV; This domain is found in elongation factor G, elongation factor ...
468-587 3.34e-58

Elongation factor G, domain IV; This domain is found in elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopts a ribosomal protein S5 domain 2-like fold.


Pssm-ID: 397710 [Multi-domain]  Cd Length: 121  Bit Score: 192.43  E-value: 3.34e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  468 PKIAYRETVRKTVEA-EYKHKKQTGGHGQYGHVQIKIEPNERGAGFEFIDKIVGGVVPKNYIPAVEKGIVEAMKKGVLAS 546
Cdd:pfam03764   1 PQVAYRETIRKPVKErAYKHKKQSGGDGQYARVILRIEPLPPGSGNEFVDETVGGQIPKEFIPAVEKGFQEAMKEGPLAG 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 493538075  547 YPVVDAKVTLFYGSYHDVDSSDMSFQIAARQAFKNGMAEAN 587
Cdd:pfam03764  81 EPVTDVKVTLLDGSYHEVDSSEAAFIPAARRAFREALLKAS 121
EFG_IV smart00889
Elongation factor G, domain IV; Translation elongation factors are responsible for two main ...
469-587 1.22e-56

Elongation factor G, domain IV; Translation elongation factors are responsible for two main processes during protein synthesis on the ribosome. EF1A (or EF-Tu) is responsible for the selection and binding of the cognate aminoacyl-tRNA to the A-site (acceptor site) of the ribosome. EF2 (or EF-G) is responsible for the translocation of the peptidyl-tRNA from the A-site to the P-site (peptidyl-tRNA site) of the ribosome, thereby freeing the A-site for the next aminoacyl-tRNA to bind. Elongation factors are responsible for achieving accuracy of translation and both EF1A and EF2 are remarkably conserved throughout evolution. Elongation factor EF2 (EF-G) is a G-protein. It brings about the translocation of peptidyl-tRNA and mRNA through a ratchet-like mechanism: the binding of GTP-EF2 to the ribosome causes a counter-clockwise rotation in the small ribosomal subunit; the hydrolysis of GTP to GDP by EF2 and the subsequent release of EF2 causes a clockwise rotation of the small subunit back to the starting position. This twisting action destabilises tRNA-ribosome interactions, freeing the tRNA to translocate along the ribosome upon GTP-hydrolysis by EF2. EF2 binding also affects the entry and exit channel openings for the mRNA, widening it when bound to enable the mRNA to translocate along the ribosome. EF2 has five domains. This entry represents domain IV found in EF2 (or EF-G) of both prokaryotes and eukaryotes. The EF2-GTP-ribosome complex undergoes extensive structural rearrangement for tRNA-mRNA movement to occur. Domain IV, which extends from the 'body' of the EF2 molecule much like a lever arm, appears to be essential for the structural transition to take place.


Pssm-ID: 214887 [Multi-domain]  Cd Length: 120  Bit Score: 188.14  E-value: 1.22e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075   469 KIAYRETVRKTV-EAEYKHKKQTGGHGQYGHVQIKIEPNERGAGFEFIDKIVGGVVPKNYIPAVEKGIVEAMKKGVLASY 547
Cdd:smart00889   1 QVAYRETITKPVkEAEGKHKKQSGGDGQYARVILEVEPLERGSGFEFDDTIVGGVIPKEYIPAVEKGFREALEEGPLAGY 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 493538075   548 PVVDAKVTLFYGSYHDVDSSDMSFQIAARQAFKNGMAEAN 587
Cdd:smart00889  81 PVVDVKVTLLDGSYHEVDSSEMAFKPAARRAFKEALLKAG 120
EFG_mtEFG_C cd03713
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational ...
592-670 2.66e-33

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: 122.25  E-value: 2.66e-33
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493538075 592 EPLMDVEVFVPEESTGDIMGEITSRRGRPMGMEPQGkGTSKVVAQVPLAEMLDFANKLSSITSGRGYFTMKFSGYQETP 670
Cdd:cd03713    1 EPIMKVEVTVPEEYMGDVIGDLSSRRGQILGTESRG-GWKVIKAEVPLAEMFGYSTDLRSLTQGRGSFTMEFSHYEEVP 78
EFG_III cd16262
Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial ...
394-469 1.01e-31

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: 117.94  E-value: 1.01e-31
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493538075 394 PEPMISKSIQPKSKGDIDKISGGLARLAESDPTFKWENDPETNETVISGLGSVHLDIMIERLKKLFSVDVEVGKPK 469
Cdd:cd16262    1 PEPVISLAIEPKTKADEDKLSKALARLAEEDPTLRVSRDEETGQTILSGMGELHLEIIVERLKREYGVEVEVGKPQ 76
EFG_like_IV cd01680
Elongation Factor G-like domain IV. This family includes the translational elongation factor ...
472-586 1.32e-31

Elongation Factor G-like domain IV. This family includes the translational elongation factor termed EF-2 (for Archaea and Eukarya) and EF-G (for Bacteria), ribosomal protection proteins that mediate tetracycline resistance and, an evolutionarily conserved U5 snRNP-specific protein (U5-116kD). In complex with GTP, EF-G/EF-2 promotes the translocation step of translation. During translocation the peptidyl-tRNA is moved from the A site to the P site of the small subunit of ribosome and the mRNA is shifted one codon relative to the ribosome. It has been shown that EF-G/EF-2_IV domain mimics the shape of anticodon arm of the tRNA in the structurally homologous ternary complex of Petra, EF-Tu (another transcriptional elongation factor) and GTP analog. The tip portion of this domain is found in a position that overlaps the anticodon arm of the A-site tRNA, implying that EF-G/EF-2 displaces the A-site tRNA to the P-site by physical interaction with the anticodon arm.


Pssm-ID: 238838 [Multi-domain]  Cd Length: 116  Bit Score: 118.88  E-value: 1.32e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 472 YRETVRKTVEAEYKHKKQTGGHGQYGHVQIKIEPNERGAGFEFIDKIVGGVVPKNYIPAVEKGIVEAMKKGVLASYPVVD 551
Cdd:cd01680    1 YRETIRKSVEATGEFERELGGKPQFGEVTLRVEPLERGSGVRVVDPVDEELLPAELKEAVEEGIRDACASGPLTGYPLTD 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 493538075 552 AKVTLFYGSYHDVDSSDMSFQIAARQAFKNGMAEA 586
Cdd:cd01680   81 VRVTVLDVPYHEGVSTEAGFRAAAGRAFESAAQKA 115
EFG_III pfam14492
Elongation Factor G, domain III; This domain is found in Elongation Factor G. It shares a ...
393-467 1.80e-30

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: 114.12  E-value: 1.80e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493538075  393 MPEPMISKSIQPKSKGDIDKISGGLARLAESDPTFKWENDPETNETVISGLGSVHLDIMIERLKKLFSVDVEVGK 467
Cdd:pfam14492   1 FPEPVISVAIEPKTKGDEDKLSKALNRLLEEDPTLRVERDEETGETILSGMGELHLEIVVDRLKRKYGVEVELGP 75
EFG_C pfam00679
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ...
589-676 2.30e-30

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: 114.18  E-value: 2.30e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  589 VILEPLMDVEVFVPEESTGDIMGEITSRRGRPMGMEPQGKGTSKVVAQVPLAEMLDFANKLSSITSGRGYFTMKFSGYQE 668
Cdd:pfam00679   1 VLLEPIEKVTIDVPEEYVGDVISDLNSRRGEILDMDPDDGGRVVIEAEVPLAELFGFATELRSLTKGRGSFSMEFSGYQP 80

                  ....*...
gi 493538075  669 TPPDVQQK 676
Cdd:pfam00679  81 VPGDILDR 88
EFG_C smart00838
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ...
590-675 2.80e-30

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: 114.14  E-value: 2.80e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075   590 ILEPLMDVEVFVPEESTGDIMGEITSRRGRPMGMEPQGkGTSKVVAQVPLAEMLDFANKLSSITSGRGYFTMKFSGYQET 669
Cdd:smart00838   1 LLEPIMKVEVTVPEEYMGDVIGDLNSRRGKIEGMEQRG-GAQVIKAKVPLSEMFGYATDLRSATQGRATWSMEFSHYEEV 79

                   ....*.
gi 493538075   670 PPDVQQ 675
Cdd:smart00838  80 PKSIAE 85
Elongation_Factor_C cd01514
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ...
592-670 3.39e-28

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: 107.95  E-value: 3.39e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493538075 592 EPLMDVEVFVPEESTGDIMGEITSRRGRPMGMEPQGKGTSKVVAQVPLAEMLDFANKLSSITSGRGYFTMKFSGYQETP 670
Cdd:cd01514    1 EPIMKVEITVPEEYLGAVIGDLSKRRGEILGMEPRGTGRVVIKAELPLAEMFGFATDLRSLTQGRASFSMEFSHYEPVP 79
RF3 cd04169
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ...
15-273 1.04e-25

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: 106.91  E-value: 1.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  15 IGHHGSGKTQIVDAMLFNAKLI--------DRIGILAT-DSEEVEKEKKASFSMGVTSLPHNDKRIYVIDTPGMSDFYAE 85
Cdd:cd04169    8 ISHPDAGKTTLTEKLLLFGGAIqeagavkaRKSRKHATsDWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHEDFSED 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  86 TANGIFASENVVAVINSTAGLEIQTERFGSIAKELKKGIIAFFNMLDKEraGYE--ETLSDLADTFERTPVLVQLPIGRE 163
Cdd:cd04169   88 TYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDRE--GRDplELLDEIENELGIDCAPMTWPIGMG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 164 ADFRGIVDLVKMKAYIYEN--EGAFKEEDIPADLKSAA------EESRTKMIEDIvqndeELMMKylEGEELSTEElita 235
Cdd:cd04169  166 KDFKGVYDRYDKEIYLYERgaGGAIKAPEETKGLDDPKldellgEDLAEQLREEL-----ELVEG--AGPEFDKEL---- 234
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 493538075 236 lrkaYLANEVIPVLLGSAGKNIGISQLLDFVSAVGKGP 273
Cdd:cd04169  235 ----FLAGELTPVFFGSALNNFGVQELLDAFVKLAPAP 268
EFG_mtEFG_II cd04088
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation ...
299-381 2.71e-22

Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation factors G1 and G2; This family represents the domain II of bacterial Elongation factor G (EF-G)and mitochondrial Elongation factors G1 (mtEFG1) and G2 (mtEFG2). 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 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 in the yeast homolog of mtEFG2, MEF2.


Pssm-ID: 293905 [Multi-domain]  Cd Length: 83  Bit Score: 91.04  E-value: 2.71e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 299 LVAYIFKSVVDPFVGKLTFMKLLSGTLKQGDSFYVVDQDSSEKVGHVMLPEGTKEIEVDEATVGDIVKLSKLKKSAAGNT 378
Cdd:cd04088    1 FSALVFKTMADPFVGKLTFFRVYSGTLKSGSTVYNSTKGKKERVGRLLRMHGKKREEVEELGAGDIGAVVGLKDTRTGDT 80

                 ...
gi 493538075 379 VAH 381
Cdd:cd04088   81 LCD 83
PTZ00416 PTZ00416
elongation factor 2; Provisional
10-683 1.48e-20

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 96.66  E-value: 1.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  10 RDIVLIGHHGSGKTQIVDAmlfnakLIDRIGILA---------TDSEEVEKE-----KKASFSM--GVTSLPHNDKR--- 70
Cdd:PTZ00416  20 RNMSVIAHVDHGKSTLTDS------LVCKAGIISsknagdarfTDTRADEQErgitiKSTGISLyyEHDLEDGDDKQpfl 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  71 IYVIDTPGMSDFYAETANGIFASENVVAVINSTAGLEIQTERFGSIAKELKKGIIAFFNMLDkeRAGYEETLS--DLADT 148
Cdd:PTZ00416  94 INLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKVD--RAILELQLDpeEIYQN 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 149 FERT-----------------PVLVQLPIGREADFRGI-------------------VDLVKMKAYIYEN------EGAF 186
Cdd:PTZ00416 172 FVKTienvnviiatyndelmgDVQVYPEKGTVAFGSGLqgwaftlttfariyakkfgVEESKMMERLWGDnffdakTKKW 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 187 KEEDIPADLKSAAE-------ESRTKMIEDIVQNDEELMMKYL---------EGEELSTEELITALRKAYLanevipvll 250
Cdd:PTZ00416 252 IKDETNAQGKKLKRafcqfilDPICQLFDAVMNEDKEKYDKMLkslnisltgEDKELTGKPLLKAVMQKWL--------- 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 251 gSAGknigiSQLLDFVSAVGKGPSEASP-KAATLLSGEKIDVVPA------EEEPLVAYIFKSVvdPFVGK---LTFMKL 320
Cdd:PTZ00416 323 -PAA-----DTLLEMIVDHLPSPKEAQKyRVENLYEGPMDDEAANairncdPNGPLMMYISKMV--PTSDKgrfYAFGRV 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 321 LSGTLKQGDSF------YVV--DQDSSEK-VGHVMLPEGTKEIEVDEATVGDIVKL----SKLKKSAAGNT--VAHKDRQ 385
Cdd:PTZ00416 395 FSGTVATGQKVriqgpnYVPgkKEDLFEKnIQRTVLMMGRYVEQIEDVPCGNTVGLvgvdQYLVKSGTITTseTAHNIRD 474
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 386 LKLDLpvmpEPMISKSIQPKSKGDIDKISGGLARLAESDPTFKWENDpETNETVISGLGSVHLDIMIERLKKLFS-VDVE 464
Cdd:PTZ00416 475 MKYSV----SPVVRVAVEPKNPKDLPKLVEGLKRLAKSDPLVVCTTE-ESGEHIVAGCGELHVEICLKDLEDDYAnIDII 549
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 465 VGKPKIAYRETVRKT------VEAEYKHKK----------QTGGHGQYGHVQIKIEPNERG----AGFEFiDK------- 517
Cdd:PTZ00416 550 VSDPVVSYRETVTEEssqtclSKSPNKHNRlymkaeplteELAEAIEEGKVGPEDDPKERAnflaDKYEW-DKndarkiw 628
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 518 -----------IVGGVVPKNYIPAVEKGIVEAM----KKGVLASYPVVDAKVTLFYGSYHDVDSSDMSFQI--AARQAFK 580
Cdd:PTZ00416 629 cfgpenkgpnvLVDVTKGVQYMNEIKDSCVSAFqwatKEGVLCDENMRGIRFNILDVTLHADAIHRGAGQIipTARRVFY 708
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 581 NGMAEANPVILEPLMDVEVFVPEESTGDIMGEITSRRGRPMGMEP-QGKGTSKVVAQVPLAEMLDFANKLSSITSGRGYF 659
Cdd:PTZ00416 709 ACELTASPRLLEPMFLVDITAPEDAMGGIYSVLNRRRGVVIGEEQrPGTPLSNIKAYLPVAESFGFTAALRAATSGQAFP 788
                        810       820       830
                 ....*....|....*....|....*....|.
gi 493538075 660 TMKFSGYQETPPDV------QQKIILE-RQR 683
Cdd:PTZ00416 789 QCVFDHWQVVPGDPlepgskANEIVLSiRKR 819
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
12-159 2.20e-19

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: 86.19  E-value: 2.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  12 IVLIGHHGSGKTQIVDAMLFNAKLIDRIGILA---TDSEEVEKEKKASFSMGVTSLPHNDKRIYVIDTPGMSDFYAETAN 88
Cdd:cd00881    2 VGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKetfLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETVR 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493538075  89 GIFASENVVAVINSTAGLEIQTERFGSIAKELKKGIIAFFNMLDKE-RAGYEETLSDLADTFERTPVLVQLP 159
Cdd:cd00881   82 GLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVgEEDFDEVLREIKELLKLIGFTFLKG 153
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
10-149 1.33e-18

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: 84.11  E-value: 1.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075   10 RDIVLIGHHGSGKTQIVDAMLFNAKLIDRIGILA------TDSEEVEKEKKASFSMGVTSLPHNDKRIYVIDTPGMSDFY 83
Cdd:pfam00009   4 RNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKgegeagLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVDFV 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493538075   84 AETANGIFASENVVAVINSTAGLEIQTERFGSIAKELKKGIIAFFNMLDK-ERAGYEETLSDLADTF 149
Cdd:pfam00009  84 KEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRvDGAELEEVVEEVSREL 150
PLN00116 PLN00116
translation elongation factor EF-2 subunit; Provisional
298-658 2.58e-18

translation elongation factor EF-2 subunit; Provisional


Pssm-ID: 177730 [Multi-domain]  Cd Length: 843  Bit Score: 89.40  E-value: 2.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 298 PLVAYIFKSVVDPFVGK-LTFMKLLSGTLKQG------DSFYVVDQDSS---EKVGHVMLPEGTKEIEVDEATVGDIVKL 367
Cdd:PLN00116 375 PLMLYVSKMIPASDKGRfFAFGRVFSGTVATGmkvrimGPNYVPGEKKDlyvKSVQRTVIWMGKKQESVEDVPCGNTVAM 454
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 368 SKLK----KSA----AGNTVAHKDRQLKLDLpvmpEPMISKSIQPKSKGDIDKISGGLARLAESDPTFKWENDpETNETV 439
Cdd:PLN00116 455 VGLDqfitKNAtltnEKEVDAHPIKAMKFSV----SPVVRVAVQCKNASDLPKLVEGLKRLAKSDPMVQCTIE-ESGEHI 529
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 440 ISGLGSVHLDIMIERLKKLF--SVDVEVGKPKIAYRETVRK----TVEAEY--KHKK--------QTG----------GH 493
Cdd:PLN00116 530 IAGAGELHLEICLKDLQDDFmgGAEIKVSDPVVSFRETVLEkscrTVMSKSpnKHNRlymearplEEGlaeaiddgriGP 609
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 494 GQYGHVQIKIEPNERGAGFEFIDKI-------------VGGVVPKNYIPAVEKGIVEAM----KKGVLA-------SYPV 549
Cdd:PLN00116 610 RDDPKIRSKILAEEFGWDKDLAKKIwcfgpettgpnmvVDMCKGVQYLNEIKDSVVAGFqwatKEGALAeenmrgiCFEV 689
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 550 VDakVTLFYGSYHDVDSsdmsfQI--AARQAFKNGMAEANPVILEPLMDVEVFVPEESTGDIMGEITSRRGRPMgMEPQG 627
Cdd:PLN00116 690 CD--VVLHADAIHRGGG-----QIipTARRVIYASQLTAKPRLLEPVYLVEIQAPEQALGGIYSVLNQKRGHVF-EEMQR 761
                        410       420       430
                 ....*....|....*....|....*....|...
gi 493538075 628 KGT--SKVVAQVPLAEMLDFANKLSSITSGRGY 658
Cdd:PLN00116 762 PGTplYNIKAYLPVIESFGFSGTLRAATSGQAF 794
mtEFG1_C cd04097
mtEFG1_C: C-terminus of mitochondrial Elongation factor G1 (mtEFG1)-like proteins found in ...
592-670 3.19e-16

mtEFG1_C: C-terminus of mitochondrial Elongation factor G1 (mtEFG1)-like proteins found in eukaryotes. 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. Eukaryotic EF-2 operates in the cytosolic protein synthesis machinery of eukaryotes, EF-Gs in protein synthesis in bacteria. 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. There are two forms of mtEFG present in mammals (designated mtEFG1s and mtEFG2s) mtEFG2s are not present in this group.


Pssm-ID: 239764 [Multi-domain]  Cd Length: 78  Bit Score: 73.89  E-value: 3.19e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493538075 592 EPLMDVEVFVPEESTGDIMGEITSRRGRPMGMEpQGKGTSKVVAQVPLAEMLDFANKLSSITSGRGYFTMKFSGYQETP 670
Cdd:cd04097    1 EPIMKVEVTAPTEFQGNVIGLLNKRKGTIVDTD-TGEDEFTLEAEVPLNDMFGYSTELRSMTQGKGEFSMEFSRYAPVP 78
EFG_III-like cd16257
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G ...
396-466 1.81e-15

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: 71.23  E-value: 1.81e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493538075 396 PMISKSIQPKSKGDIDKISGGLARLAESDPTFKWENDPETNETVISGLGSVHLDIMIERLKKLFSVDVEVG 466
Cdd:cd16257    1 PVVFVTVEVKNPLDQEKLLEGLERLSEEDPALQVYREESTGEFILSGLGELHLEIIVARLEREYGVELVVS 71
prfC PRK00741
peptide chain release factor 3; Provisional
6-305 9.18e-14

peptide chain release factor 3; Provisional


Pssm-ID: 179105 [Multi-domain]  Cd Length: 526  Bit Score: 74.40  E-value: 9.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075   6 VDAKRDIVLIGHHGSGKTQIVDAMLFNAKLIDRIGIL--------AT-DSEEVEKEKKASFSMGVTSLPHNDKRIYVIDT 76
Cdd:PRK00741   7 VAKRRTFAIISHPDAGKTTLTEKLLLFGGAIQEAGTVkgrksgrhATsDWMEMEKQRGISVTSSVMQFPYRDCLINLLDT 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  77 PGMSDFYAETANGIFASENVVAVINSTAGLEIQTERFGSIAKELKKGIIAFFNMLDkeRAGYE--ETLSDLADTFERTPV 154
Cdd:PRK00741  87 PGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTRKLMEVCRLRDTPIFTFINKLD--RDGREplELLDEIEEVLGIACA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 155 LVQLPIGREADFRGIVDLVKMKAYIYEnegafkeedipadlksAAEESRTKMIEDIVQNDEELMMKYLeGEELSTE---- 230
Cdd:PRK00741 165 PITWPIGMGKRFKGVYDLYNDEVELYQ----------------PGEGHTIQEVEIIKGLDNPELDELL-GEDLAEQlree 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 231 -ELITAL-----RKAYLANEVIPVLLGSAGKNIGISQLLD-FVsavgkgpsEASPKAATLLSGEKidVVPAEEEPLVAYI 303
Cdd:PRK00741 228 lELVQGAsnefdLEAFLAGELTPVFFGSALNNFGVQEFLDaFV--------EWAPAPQPRQTDER--EVEPTEEKFSGFV 297

                 ..
gi 493538075 304 FK 305
Cdd:PRK00741 298 FK 299
Tet_like_IV cd01684
EF-G_domain IV_RPP domain is a part of bacterial ribosomal protected proteins (RPP) family. ...
470-587 1.89e-13

EF-G_domain IV_RPP domain is a part of bacterial ribosomal protected proteins (RPP) family. RPPs such as tetracycline resistance proteins Tet(M) and Tet(O) mediate tetracycline resistance in both gram-positive and -negative species. Tetracyclines inhibit the accommodation of aminoacyl-tRNA into ribosomal A site and therefore prevent the addition of new amino acids to the growing polypeptide. RPPs Tet(M) confer tetracycline resistance by releasing tetracycline from the ribosome and thereby freeing the ribosome from inhibitory effects of the drug, such that aa-tRNA can bind to the A site and protein synthesis can continue.


Pssm-ID: 238841 [Multi-domain]  Cd Length: 115  Bit Score: 67.31  E-value: 1.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 470 IAYRETVRKTVEAeYKHKkQTGGHGQYGHVQIKIEPNERGAGFEFIDKIVGGVVPKNYIPAVEKGIVEAMKKGVLASyPV 549
Cdd:cd01684    1 VIYKERPLGTGEG-VEHI-EVPPNPFWATVGLRVEPLPRGSGLQYESEVSLGSLPRSFQNAVEETVRETLQQGLYGW-EV 77
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 493538075 550 VDAKVTLFYGSYHDVDSSDMSFQIAARQAFKNGMAEAN 587
Cdd:cd01684   78 TDCKVTLTYGRYHSPVSTAADFRELTPRVLRQALKKAG 115
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
10-149 9.28e-13

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: 67.23  E-value: 9.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  10 RDIVLIGHHGSGKTQIVDAML-----F--NAKLIDRIgilaTDSEEVEKEKKASFSMGVTSLPHNDKRIYVIDTPGMSDF 82
Cdd:cd01891    3 RNIAIIAHVDHGKTTLVDALLkqsgtFreNEEVGERV----MDSNDLERERGITILAKNTAITYKDTKINIIDTPGHADF 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493538075  83 YAETANGIFASENVVAVINSTAGLEIQTeRFgSIAKELKKGI--IAFFNMLDKERAGYEETLSDLADTF 149
Cdd:cd01891   79 GGEVERVLSMVDGVLLLVDASEGPMPQT-RF-VLKKALEAGLkpIVVINKIDRPDARPEEVVDEVFDLF 145
mtEFG2_II_like cd04092
Domain II of mitochondrial elongation factor G2-like proteins found in eukaryotes; Eukaryotic ...
299-379 1.54e-11

Domain II of mitochondrial elongation factor G2-like proteins found in eukaryotes; 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. Eukaryotic EF-2 operates in the cytosolic protein synthesis machinery of eukaryotes, EF-Gs in protein synthesis in bacteria. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. No clear phenotype has been found for mutants in the yeast homolog of mtEFG2, MEF2. There are two forms of mtEFG present in mammals (designated mtEFG1s and mtEFG2s); mtEFG1s are not present in this group.


Pssm-ID: 293909 [Multi-domain]  Cd Length: 83  Bit Score: 60.79  E-value: 1.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 299 LVAYIFKSVVDPFVGKLTFMKLLSGTLKQGDSFYVVDQDSSEKVGHVMLPEGTKEIEVDEATVGDIVKLSKLKKSAAGNT 378
Cdd:cd04092    1 LCALAFKVIHDPQRGPLVFVRVYSGTLKAGSNVYNTTTGKKERISRLLKMHADQTEEVDSLSAGNIGVITGLKVTSTGDT 80

                 .
gi 493538075 379 V 379
Cdd:cd04092   81 L 81
Tet_C cd03711
Tet_C: C-terminus of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology ...
592-670 7.35e-11

Tet_C: C-terminus of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology to the C terminal domains of the elongation factors EF-G and EF-2. Tet(M) and Tet(O) catalyze the release of tetracycline (Tc) from the ribosome in a GTP-dependent manner thereby mediating Tc resistance. Tcs are broad-spectrum antibiotics. Typical Tcs bind to the ribosome and inhibit the elongation phase of protein synthesis, by inhibiting the occupation of site A by aminoacyl-tRNA.


Pssm-ID: 239682 [Multi-domain]  Cd Length: 78  Bit Score: 58.40  E-value: 7.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 592 EPLMDVEVFVPEESTGDIMGEITSRRGRPMgmEPQGKGTSKVV-AQVPLAEMLDFANKLSSITSGRGYFTMKFSGYQETP 670
Cdd:cd03711    1 EPYLRFELEVPQDALGRAMSDLAKMGATFE--DPQIKGDEVTLeGTIPVATSQDYQSELPSYTHGEGVLETEFKGYRPCH 78
lepA_C cd03709
lepA_C: This family represents the C-terminal region of LepA, a GTP-binding protein localized ...
592-669 7.85e-11

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: 58.66  E-value: 7.85e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493538075 592 EPLMDVEVFVPEESTGDIMGEITSRRGRPMGMEPQGKGTSKVVAQVPLAEM-LDFANKLSSITSGRGYFTMKFSGYQET 669
Cdd:cd03709    1 EPFVKATIITPSEYLGAIMELCQERRGVQKDMEYLDANRVMLTYELPLAEIvYDFFDKLKSISKGYASLDYELIGYRES 79
Tet_II cd03690
Domain II of ribosomal protection proteins Tet(M) and Tet(O); This subfamily represents domain ...
296-371 1.20e-09

Domain II of ribosomal protection proteins Tet(M) and Tet(O); This subfamily represents domain II of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology to domain II of the elongation factors EF-G and EF-2. Tet(M) and Tet(O) catalyze the release of tetracycline (Tc) from the ribosome in a GTP-dependent manner thereby mediating Tc resistance. Tcs are broad-spectrum antibiotics. Typical Tcs bind to the ribosome and inhibit the elongation phase of protein synthesis, by inhibiting the occupation of site A by aminoacyl-tRNA.


Pssm-ID: 293891 [Multi-domain]  Cd Length: 86  Bit Score: 55.32  E-value: 1.20e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493538075 296 EEPLVAYIFKSVVDPFVGKLTFMKLLSGTLKQGDSFYVVDQDSSEKVGHVMLPEGTKEIEVDEATVGDIVKLSKLK 371
Cdd:cd03690    1 ESELSGTVFKIEYDPKGERLAYLRLYSGTLRLRDSVRVSGEEEKIKITELRTFENGELVKVDRVYAGDIAILVGLK 76
mtEFG2_like_IV cd01693
mtEF-G2 domain IV. This subfamily is a part the of mitochondrial transcriptional elongation ...
470-586 1.38e-09

mtEF-G2 domain IV. This subfamily is a part the of mitochondrial transcriptional elongation factor, mtEF-G2. Mitochondrial translation is crucial for maintaining mitochondrial function and mutations in this system lead to a breakdown in the respiratory chain-oxidative phosphorylation system and to impaired maintenance of mitochondrial DNA. In complex with GTP, EF-G promotes the translocation step of translation. During translocation the peptidyl-tRNA is moved from the A site to the P site of the small subunit of ribosome and the mRNA is shifted one codon relative to the ribosome.


Pssm-ID: 238842 [Multi-domain]  Cd Length: 120  Bit Score: 56.25  E-value: 1.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 470 IAYRETVRKTVEAEYKHKKQTGGHGQYGHVQIKIEPNE--RGAGFEF-IDKIVGGVVPKNYIPAVEKGIVEAMKKGVLAS 546
Cdd:cd01693    1 IAYRETILEPARATDTLEKVIGDKKHSVTVTMEVRPNQasSSPVELIeLANSAIEVLLKRIQEAVENGVHSALLQGPLLG 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 493538075 547 YPVVDAKVTLFYGSYHDvDSSDMSFQIAARQAFKNGMAEA 586
Cdd:cd01693   81 FPVQDVAITLHSLTIGP-GTSPTMISACASQCVQKALKSA 119
BipA_TypA_II cd03691
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ...
309-383 2.13e-09

Domain II of BipA; BipA (also called TypA) 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. The domain II of BipA shows similarity to the domain II of the elongation factors (EFs) EF-G and EF-Tu.


Pssm-ID: 293892 [Multi-domain]  Cd Length: 94  Bit Score: 54.89  E-value: 2.13e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493538075 309 DPFVGKLTFMKLLSGTLKQGDSFYVVDQDSSE---KVGHVMLPEGTKEIEVDEATVGDIVKLSKLKKSAAGNTVAHKD 383
Cdd:cd03691   11 DDYLGRIAIGRIFSGTVKVGQQVTVVDEDGKIekgRVTKLFGFEGLERVEVEEAEAGDIVAIAGLEDITIGDTICDPE 88
BipA_TypA_C cd03710
BipA_TypA_C: a C-terminal portion of BipA or TypA having homology to the C terminal domains of ...
592-667 4.08e-09

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: 53.66  E-value: 4.08e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493538075 592 EPLMDVEVFVPEESTGDIMGEITSRRGRPMGMEPQGKGTSKVVAQVPLAEMLDFANKLSSITSGRGYFTMKFSGYQ 667
Cdd:cd03710    1 EPIEELTIDVPEEYSGAVIEKLGKRKGEMVDMEPDGNGRTRLEFKIPSRGLIGFRSEFLTDTRGTGIMNHVFDGYE 76
EF2_snRNP_III cd16261
Domain III of Elongation Factor 2 (EF2); This model represents domain III of Elongation factor ...
396-467 5.59e-09

Domain III of Elongation Factor 2 (EF2); This model represents domain III of Elongation factor 2 (EF2) found in eukaryotes and archaea, and the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and its yeast counterpart Snu114p. 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. This translocation step is catalyzed by EF-2_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. Yeast Snu114p is essential for cell viability and for splicing in vivo. U5-116 kD binds GTP. Experiments suggest that GTP binding and probably GTP hydrolysis are important for the function of the U5-116 kD/Snu114p.


Pssm-ID: 293918 [Multi-domain]  Cd Length: 72  Bit Score: 52.96  E-value: 5.59e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493538075 396 PMISKSIQPKSKGDIDKISGGLARLAESDPTFKWENDpETNETVISGLGSVHLDIMIERLKKLFS-VDVEVGK 467
Cdd:cd16261    1 PVVRVAVEPKNPSDLPKLVEGLKKLAKSDPTVQVKIE-EEGEHLIAGAGELHLEICLKDLKEDFAgIEIKVSD 72
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
10-112 1.08e-08

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


Pssm-ID: 206730 [Multi-domain]  Cd Length: 213  Bit Score: 55.74  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  10 RDIVLIGHHGSGKTQIVDAMLFNAKLIDRIGIL------ATDSEEVEKEKKASFSMGVTSLPHNDKR-----IYVIDTPG 78
Cdd:cd04167    1 RNVCIAGHLHHGKTSLLDMLIEQTHKRTPSVKLgwkplrYTDTRKDEQERGISIKSNPISLVLEDSKgksylINIIDTPG 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 493538075  79 MSDFYAETANGIFASENVVAVINSTAGLEIQTER 112
Cdd:cd04167   81 HVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTER 114
PRK10218 PRK10218
translational GTPase TypA;
6-474 1.37e-08

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 58.18  E-value: 1.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075   6 VDAKRDIVLIGHHGSGKTQIVDAML-----FNAKLIDRIGILatDSEEVEKEKKASFSMGVTSLPHNDKRIYVIDTPGMS 80
Cdd:PRK10218   2 IEKLRNIAIIAHVDHGKTTLVDKLLqqsgtFDSRAETQERVM--DSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  81 DFYAETANGIFASENVVAVINSTAGLEIQTeRFGSiAKELKKGI--IAFFNMLDKERAGYEETLSDLADTF---ERTPVL 155
Cdd:PRK10218  80 DFGGEVERVMSMVDSVLLVVDAFDGPMPQT-RFVT-KKAFAYGLkpIVVINKVDRPGARPDWVVDQVFDLFvnlDATDEQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 156 VQLPIGREADFRGIVDLvkmkayiyenegafKEEDIPADLksaaeesrtkmiedivqndeelmmkylegeelsteeliTA 235
Cdd:PRK10218 158 LDFPIVYASALNGIAGL--------------DHEDMAEDM--------------------------------------TP 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 236 LRKAylanevipvllgsagknigisqLLDFVSAvgkgpseaspkaatllsgEKIDVvpaeEEPLVAYIFKSVVDPFVGKL 315
Cdd:PRK10218 186 LYQA----------------------IVDHVPA------------------PDVDL----DGPFQMQISQLDYNSYVGVI 221
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 316 TFMKLLSGTLKQGDSFYVVDQDSSE---KVGHVMLPEGTKEIEVDEATVGDIVKLSKLKKSAAGNTVAHKDRQLKLDLPV 392
Cdd:PRK10218 222 GIGRIKRGKVKPNQQVTIIDSEGKTrnaKVGKVLGHLGLERIETDLAEAGDIVAITGLGELNISDTVCDTQNVEALPALS 301
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 393 MPEPMISK----SIQP--KSKGDIDKISGGLARLAES---DPTFKWENDPETNETVISGLGSVHLDIMIERLKKLfSVDV 463
Cdd:PRK10218 302 VDEPTVSMffcvNTSPfcGKEGKFVTSRQILDRLNKElvhNVALRVEETEDADAFRVSGRGELHLSVLIENMRRE-GFEL 380
                        490
                 ....*....|.
gi 493538075 464 EVGKPKIAYRE 474
Cdd:PRK10218 381 AVSRPKVIFRE 391
eEF2_snRNP_like_C cd04096
eEF2_snRNP_like_C: this family represents a C-terminal domain of eukaryotic elongation factor ...
592-667 1.59e-08

eEF2_snRNP_like_C: this family represents a C-terminal domain of eukaryotic elongation factor 2 (eEF-2) and a homologous domain of the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and, its yeast counterpart Snu114p. Yeast Snu114p is essential for cell viability and for splicing in vivo. U5-116 kD binds GTP. Experiments suggest that GTP binding and probably GTP hydrolysis is important for the function of the U5-116 kD/Snu114p. In complex with GTP, EF-2 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.


Pssm-ID: 239763 [Multi-domain]  Cd Length: 80  Bit Score: 52.16  E-value: 1.59e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493538075 592 EPLMDVEVFVPEESTGDIMGEITSRRGRPMGMEPQ-GKGTSKVVAQVPLAEMLDFANKLSSITSGRGYFTMKFSGYQ 667
Cdd:cd04096    1 EPIYLVEIQCPEDALGKVYSVLSKRRGHVLSEEPKeGTPLFEIKAYLPVIESFGFETDLRSATSGQAFPQLVFSHWE 77
mtEFG1_II_like cd04091
Domain II of mitochondrial elongation factor G1-like proteins found in eukaryotes; Eukaryotic ...
299-381 4.27e-08

Domain II of mitochondrial elongation factor G1-like proteins found in eukaryotes; 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. Eukaryotic EF-2 operates in the cytosolic protein synthesis machinery of eukaryotes, EF-Gs in protein synthesis in bacteria. 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. There are two forms of mtEFG present in mammals (designated mtEFG1s and mtEFG2s); mtEFG2s are not present in this group.


Pssm-ID: 293908 [Multi-domain]  Cd Length: 81  Bit Score: 50.75  E-value: 4.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 299 LVAYIFKSVVDPFvGKLTFMKLLSGTLKQGDSFYVVDQDSSEKVGHVMLPEGTKEIEVDEATVGDIVKLSKLkKSAAGNT 378
Cdd:cd04091    1 FVGLAFKLEEGRF-GQLTYMRVYQGVLRKGDTIYNVRTGKKVRVPRLVRMHSDEMEDIEEVYAGDICALFGI-DCASGDT 78

                 ...
gi 493538075 379 VAH 381
Cdd:cd04091   79 FTD 81
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
299-373 5.67e-08

Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.


Pssm-ID: 293888 [Multi-domain]  Cd Length: 80  Bit Score: 50.34  E-value: 5.67e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493538075 299 LVAYIFKSVVDPFVGKLTFMKLLSGTLKQGDSFYVVDQDSSEKVGHVmlpeGTKEIEVDEATVGDIVKLSKLKKS 373
Cdd:cd01342    1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSI----ERFHEEVDEAKAGDIVGIGILGVK 71
Tet_III cd16258
Domain III of Tetracycline resistance protein Tet; Tetracycline resistance proteins, including ...
396-465 1.19e-06

Domain III of Tetracycline resistance protein Tet; Tetracycline resistance proteins, including TetM and TetO, catalyze the release of tetracycline (Tc) from the ribosome in a GTP-dependent manner thereby mediating Tc resistance. Tcs are broad-spectrum antibiotics. Typical Tcs bind to the ribosome and inhibit the elongation phase of protein synthesis, by inhibiting the occupation of site A by aminoacyl-tRNA.


Pssm-ID: 293915 [Multi-domain]  Cd Length: 71  Bit Score: 46.55  E-value: 1.19e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075 396 PMISKSIQPKSKGDIDKISGGLARLAESDPTFKWENDPETNETVISGLGSVHLDIMIERLKKLFSVDVEV 465
Cdd:cd16258    1 PMLQTTIRPRKPEQRERLLDALTELSDEDPLLKYRVDSTTHEIILSLYGEVQMEVISALLEEKYGVEVEF 70
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
313-380 2.07e-06

Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.


Pssm-ID: 427163 [Multi-domain]  Cd Length: 73  Bit Score: 45.72  E-value: 2.07e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493538075  313 GKLTFMKLLSGTLKQGDSFYVVDQDSSEK-----VGHVMLPEGTKEIEVDEATVGDIVKLSKLKKSAAGNTVA 380
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGTGKKkivtrVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
10-111 1.08e-05

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: 47.23  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  10 RDIVLIGHHGSGKTQIVDAMLFNAKLI--DRIG-ILATDSEEVEKEK----KAS-----FSMGVTSLPHNDKRIYVIDTP 77
Cdd:cd01885    1 RNICIIAHVDHGKTTLSDSLLASAGIIseKLAGkARYLDTREDEQERgitiKSSaislyFEYEEEKMDGNDYLINLIDSP 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 493538075  78 GMSDFYAETANGIFASENVVAVINSTAGLEIQTE 111
Cdd:cd01885   81 GHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTE 114
EF4_III cd16260
Domain III of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly ...
396-463 4.16e-03

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: 36.32  E-value: 4.16e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493538075 396 PMISKSIQPKSKGDIDKISGGLARLAESDPTFKWEndPETNETVISG-----LGSVHLDIMIERLKKLFSVDV 463
Cdd:cd16260    1 PMVFAGLYPVDGSDYEELRDALEKLTLNDASVTFE--PETSSALGFGfrcgfLGLLHMEVFQERLEREYGLDL 71
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
12-174 5.28e-03

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: 38.12  E-value: 5.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075   12 IVLIGHHGSGKTQIVDAMLFNAKLIDRI--GILATDSEEVEKEKkasfsmGVTslphndKRIYVIDTPGMSDF------- 82
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLLGNKGSITEYypGTTRNYVTTVIEED------GKT------YKFNLLDTAGQEDYdairrly 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075   83 YAETANGIFASENVVAVINSTAGLEIQTErfgSIAKELKKG--IIAFFNMLDKERAGYEETLSDLADTFERTPVlVQLPI 160
Cdd:TIGR00231  72 YPQVERSLRVFDIVILVLDVEEILEKQTK---EIIHHADSGvpIILVGNKIDLKDADLKTHVASEFAKLNGEPI-IPLSA 147
                         170
                  ....*....|....
gi 493538075  161 GREADFRGIVDLVK 174
Cdd:TIGR00231 148 ETGKNIDSAFKIVE 161
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
12-181 6.65e-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 bacterial SelBs, as well as, one from archaea.


Pssm-ID: 206734 [Multi-domain]  Cd Length: 170  Bit Score: 37.97  E-value: 6.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  12 IVLIGHHGSGKTQivdamlfnakLIDRIGILATDSEEVEKEKKASFSMGVTSLP-HNDKRIYVIDTPGMSDFYAETANGI 90
Cdd:cd04171    2 IGTAGHIDHGKTT----------LIKALTGIETDRLPEEKKRGITIDLGFAYLDlPDGKRLGFIDVPGHEKFVKNMLAGA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493538075  91 FASENVVAVINSTAGLEIQTERFGSIAK--ELKKGIIAF--FNMLDKERAG--YEETLSDLADTF-ERTPVLvqlpIGRE 163
Cdd:cd04171   72 GGIDAVLLVVAADEGIMPQTREHLEILEllGIKKGLVVLtkADLVDEDRLElvEEEILELLAGTFlADAPIF----PVSS 147
                        170
                 ....*....|....*...
gi 493538075 164 ADFRGIVDLvkmKAYIYE 181
Cdd:cd04171  148 VTGEGIEEL---KNYLDE 162
 
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.
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