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Conserved domains on  [gi|78194975|gb|ABB32742|]
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translation elongation factor G [Geobacter metallireducens GS-15]

Protein Classification

elongation factor G( domain architecture ID 11486585)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK13351 PRK13351
elongation factor G-like protein;
3-687 0e+00

elongation factor G-like protein;


:

Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 1031.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975    3 HPPLDSIRNIGIISHIDAGKTTVSERILFYTGETHKIGEVHDGEAVMDWMPQEQERGITITSTATVCRWGAWWINLIDTP 82
Cdd:PRK13351   2 EMPLMQIRNIGILAHIDAGKTTLTERILFYTGKIHKMGEVEDGTTVTDWMPQEQERGITIESAATSCDWDNHRINLIDTP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   83 GHIDFTIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRICFINKMDRVGADYRETLRQMEEKLGARPVLLQ 162
Cdd:PRK13351  82 GHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLFKVLEDIEERFGKRPLPLQ 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  163 LPVGVEASFAGVVDLIAGEFLTFSEADQGSTVERHPIPAEIAGEAMAVREELIEAAADFDDAILADFLEGTAIAAERIRA 242
Cdd:PRK13351 162 LPIGSEDGFEGVVDLITEPELHFSEGDGGSTVEEGPIPEELLEEVEEAREKLIEALAEFDDELLELYLEGEELSAEQLRA 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  243 AIRKGTIACRIVPVFLGTALRNRGIQPLLDAVAAYLPSPRDIPPVTGQRPDGEAVDsLPCDPAGPLCALAFKVQADEG-R 321
Cdd:PRK13351 242 PLREGTRSGHLVPVLFGSALKNIGIEPLLDAVVDYLPSPLEVPPPRGSKDNGKPVK-VDPDPEKPLLALVFKVQYDPYaG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  322 KLTYLRIYSGTVKAGGALWNSNRGCFEKAARLFRMHAHKREPIDEALAGDIVAAIGLKEVLTGDTLCDPAHKVLLSGLTV 401
Cdd:PRK13351 321 KLTYLRVYSGTLRAGSQLYNGTGGKREKVGRLFRLQGNKREEVDRAKAGDIVAVAGLKELETGDTLHDSADPVLLELLTF 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  402 PEPVVALAVEPRGVDDRDKLLPALEKLQWEDPTFRVHEDEETGQTILTGMGELHLEVVTDRLGREFGVQVKTGRPQVVYR 481
Cdd:PRK13351 401 PEPVVSLAVEPERRGDEQKLAEALEKLVWEDPSLRVEEDEETGQTILSGMGELHLEVALERLRREFKLEVNTGKPQVAYR 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  482 ETITRPAERQEVFRTEFEGKVQGGEVHLRLAPLHRGEGvRIVVPPAEVLGITRELHTALTESLTRGASTGCVTGYPLTDL 561
Cdd:PRK13351 481 ETIRKMAEGVYRHKKQFGGKGQFGEVHLRVEPLERGAG-FIFVSKVVGGAIPEELIPAVEKGIREALASGPLAGYPVTDL 559
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  562 EVRVITVPVEQGVTTEGGVRAAAGRGLMRAARDGAPTLLEPLMDLEIITPTEYAGKVLGSVQQKRGRVEGIITQGNTE-A 640
Cdd:PRK13351 560 RVTVLDGKYHPVDSSESAFKAAARKAFLEAFRKANPVLLEPIMELEITVPTEHVGDVLGDLSQRRGRIEGTEPRGDGEvL 639
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|....*..
gi 78194975  641 IRALVPLAEMFGYMTELRSATKGRGGFTMEFSRFDQAPASVLQQFGL 687
Cdd:PRK13351 640 VKAEAPLAELFGYATRLRSMTKGRGSFTMEFSHFDPVPPAVQKKVGS 686
 
Name Accession Description Interval E-value
PRK13351 PRK13351
elongation factor G-like protein;
3-687 0e+00

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 1031.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975    3 HPPLDSIRNIGIISHIDAGKTTVSERILFYTGETHKIGEVHDGEAVMDWMPQEQERGITITSTATVCRWGAWWINLIDTP 82
Cdd:PRK13351   2 EMPLMQIRNIGILAHIDAGKTTLTERILFYTGKIHKMGEVEDGTTVTDWMPQEQERGITIESAATSCDWDNHRINLIDTP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   83 GHIDFTIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRICFINKMDRVGADYRETLRQMEEKLGARPVLLQ 162
Cdd:PRK13351  82 GHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLFKVLEDIEERFGKRPLPLQ 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  163 LPVGVEASFAGVVDLIAGEFLTFSEADQGSTVERHPIPAEIAGEAMAVREELIEAAADFDDAILADFLEGTAIAAERIRA 242
Cdd:PRK13351 162 LPIGSEDGFEGVVDLITEPELHFSEGDGGSTVEEGPIPEELLEEVEEAREKLIEALAEFDDELLELYLEGEELSAEQLRA 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  243 AIRKGTIACRIVPVFLGTALRNRGIQPLLDAVAAYLPSPRDIPPVTGQRPDGEAVDsLPCDPAGPLCALAFKVQADEG-R 321
Cdd:PRK13351 242 PLREGTRSGHLVPVLFGSALKNIGIEPLLDAVVDYLPSPLEVPPPRGSKDNGKPVK-VDPDPEKPLLALVFKVQYDPYaG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  322 KLTYLRIYSGTVKAGGALWNSNRGCFEKAARLFRMHAHKREPIDEALAGDIVAAIGLKEVLTGDTLCDPAHKVLLSGLTV 401
Cdd:PRK13351 321 KLTYLRVYSGTLRAGSQLYNGTGGKREKVGRLFRLQGNKREEVDRAKAGDIVAVAGLKELETGDTLHDSADPVLLELLTF 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  402 PEPVVALAVEPRGVDDRDKLLPALEKLQWEDPTFRVHEDEETGQTILTGMGELHLEVVTDRLGREFGVQVKTGRPQVVYR 481
Cdd:PRK13351 401 PEPVVSLAVEPERRGDEQKLAEALEKLVWEDPSLRVEEDEETGQTILSGMGELHLEVALERLRREFKLEVNTGKPQVAYR 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  482 ETITRPAERQEVFRTEFEGKVQGGEVHLRLAPLHRGEGvRIVVPPAEVLGITRELHTALTESLTRGASTGCVTGYPLTDL 561
Cdd:PRK13351 481 ETIRKMAEGVYRHKKQFGGKGQFGEVHLRVEPLERGAG-FIFVSKVVGGAIPEELIPAVEKGIREALASGPLAGYPVTDL 559
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  562 EVRVITVPVEQGVTTEGGVRAAAGRGLMRAARDGAPTLLEPLMDLEIITPTEYAGKVLGSVQQKRGRVEGIITQGNTE-A 640
Cdd:PRK13351 560 RVTVLDGKYHPVDSSESAFKAAARKAFLEAFRKANPVLLEPIMELEITVPTEHVGDVLGDLSQRRGRIEGTEPRGDGEvL 639
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|....*..
gi 78194975  641 IRALVPLAEMFGYMTELRSATKGRGGFTMEFSRFDQAPASVLQQFGL 687
Cdd:PRK13351 640 VKAEAPLAELFGYATRLRSMTKGRGSFTMEFSHFDPVPPAVQKKVGS 686
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
1-684 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: 920.60  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   1 MQHPPLDSIRNIGIISHIDAGKTTVSERILFYTGETHKIGEVHDGEAVMDWMPQEQERGITITSTATVCRWGAWWINLID 80
Cdd:COG0480   1 MAEYPLEKIRNIGIVAHIDAGKTTLTERILFYTGAIHRIGEVHDGNTVMDWMPEEQERGITITSAATTCEWKGHKINIID 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  81 TPGHIDFTIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRICFINKMDRVGADYRETLRQMEEKLGARPVL 160
Cdd:COG0480  81 TPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQLKERLGANPVP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 161 LQLPVGVEASFAGVVDLIAGEFLTFSEaDQGSTVERHPIPAEIAGEAMAVREELIEAAADFDDAILADFLEGTAIAAERI 240
Cdd:COG0480 161 LQLPIGAEDDFKGVIDLVTMKAYVYDD-ELGAKYEEEEIPAELKEEAEEAREELIEAVAETDDELMEKYLEGEELTEEEI 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 241 RAAIRKGTIACRIVPVFLGTALRNRGIQPLLDAVAAYLPSPRDIPPVTGQRPDGEAVDSLPCDPAGPLCALAFKVQADE- 319
Cdd:COG0480 240 KAGLRKATLAGKIVPVLCGSAFKNKGVQPLLDAVVDYLPSPLDVPAIKGVDPDTGEEVERKPDDDEPFSALVFKTMTDPf 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 320 GRKLTYLRIYSGTVKAGGALWNSNRGCFEKAARLFRMHAHKREPIDEALAGDIVAAIGLKEVLTGDTLCDPAHKVLLSGL 399
Cdd:COG0480 320 VGKLSFFRVYSGTLKSGSTVYNSTKGKKERIGRLLRMHGNKREEVDEAGAGDIVAVVKLKDTTTGDTLCDEDHPIVLEPI 399
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 400 TVPEPVVALAVEPRGVDDRDKLLPALEKLQWEDPTFRVHEDEETGQTILTGMGELHLEVVTDRLGREFGVQVKTGRPQVV 479
Cdd:COG0480 400 EFPEPVISVAIEPKTKADEDKLSTALAKLAEEDPTFRVETDEETGQTIISGMGELHLEIIVDRLKREFGVEVNVGKPQVA 479
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 480 YRETITRPAERQEVFRTEFEGKVQGGEVHLRLAPLHRGEGV----RIV---VP----PAeVL-GItRElhtALTEsltrg 547
Cdd:COG0480 480 YRETIRKKAEAEGKHKKQSGGHGQYGDVWIEIEPLPRGEGFefvdKIVggvIPkeyiPA-VEkGI-RE---AMEK----- 549
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 548 astGCVTGYPLTDLEVRVItvpveqgvtteGG----V-------RAAAGRGLMRAARDGAPTLLEPLMDLEIITPTEYAG 616
Cdd:COG0480 550 ---GVLAGYPVVDVKVTLY-----------DGsyhpVdssemafKIAASMAFKEAAKKAKPVLLEPIMKVEVTVPEEYMG 615
                       650       660       670       680       690       700
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78194975 617 KVLGSVQQKRGRVEGIITQGNTEAIRALVPLAEMFGYMTELRSATKGRGGFTMEFSRFDQAPASVLQQ 684
Cdd:COG0480 616 DVMGDLNSRRGRILGMESRGGAQVIKAEVPLAEMFGYATDLRSLTQGRGSFTMEFSHYEEVPANVAEK 683
EF-G TIGR00484
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ...
5-684 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: 756.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975     5 PLDSIRNIGIISHIDAGKTTVSERILFYTGETHKIGEVHDGEAVMDWMPQEQERGITITSTATVCRWGAWWINLIDTPGH 84
Cdd:TIGR00484   6 DLNRFRNIGISAHIDAGKTTTTERILFYTGRIHKIGEVHDGAATMDWMEQEKERGITITSAATTVFWKGHRINIIDTPGH 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975    85 IDFTIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRICFINKMDRVGADYRETLRQMEEKLGARPVLLQLP 164
Cdd:TIGR00484  86 VDFTVEVERSLRVLDGAVAVLDAVGGVQPQSETVWRQANRYEVPRIAFVNKMDKTGANFLRVVNQIKQRLGANAVPIQLP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   165 VGVEASFAGVVDLIAGEFLTFsEADQGSTVERHPIPAEIAGEAMAVREELIEAAADFDDAILADFLEGTAIAAERIRAAI 244
Cdd:TIGR00484 166 IGAEDNFIGVIDLVEMKAYFF-NGDKGTKAIEKEIPSDLLEQAKELRENLVEAVAEFDEELMEKYLEGEELTIEEIKNAI 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   245 RKGTIACRIVPVFLGTALRNRGIQPLLDAVAAYLPSPRDIPPVTGQRPDGEAVDSLPCDPAGPLCALAFKVQADE-GRKL 323
Cdd:TIGR00484 245 RKGVLNCEFFPVLCGSAFKNKGVQLLLDAVVDYLPSPTDVPAIKGIDPDTEKEIERKASDDEPFSALAFKVATDPfVGQL 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   324 TYLRIYSGTVKAGGALWNSNRGCFEKAARLFRMHAHKREPIDEALAGDIVAAIGLKEVLTGDTLCDPAHKVLLSGLTVPE 403
Cdd:TIGR00484 325 TFVRVYSGVLKSGSYVKNSRKNKKERVGRLVKMHANNREEIKEVRAGDICAAIGLKDTTTGDTLCDPKIDVILERMEFPE 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   404 PVVALAVEPRGVDDRDKLLPALEKLQWEDPTFRVHEDEETGQTILTGMGELHLEVVTDRLGREFGVQVKTGRPQVVYRET 483
Cdd:TIGR00484 405 PVISLAVEPKTKADQEKMGIALGKLAEEDPTFRTFTDPETGQTIIAGMGELHLDIIVDRMKREFKVEANVGAPQVAYRET 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   484 ITRPAERQEVFRTEFEGKVQGGEVHLRLAPLHRgEGVRIVvppAEVLG--ITRELHTALTESLTRGASTGCVTGYPLTDL 561
Cdd:TIGR00484 485 IRSKVEVEGKHAKQSGGRGQYGHVKIRFEPLEP-KGYEFV---NEIKGgvIPREYIPAVDKGLQEAMESGPLAGYPVVDI 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   562 EVRVITVPVEQGVTTEGGVRAAAGRGLMRAARDGAPTLLEPLMDLEIITPTEYAGKVLGSVQQKRGRVEGIITQGNTEAI 641
Cdd:TIGR00484 561 KATLFDGSYHDVDSSEMAFKLAASLAFKEAGKKANPVLLEPIMKVEVEVPEEYMGDVMGDLSSRRGIIEGMEARGNVQKI 640
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|...
gi 78194975   642 RALVPLAEMFGYMTELRSATKGRGGFTMEFSRFDQAPASVLQQ 684
Cdd:TIGR00484 641 KAEVPLSEMFGYATDLRSFTQGRGTYSMEFLHYGEVPSSVANE 683
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
11-281 3.27e-158

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: 456.95  E-value: 3.27e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  11 NIGIISHIDAGKTTVSERILFYTGETHKIGEVHDGEAVMDWMPQEQERGITITSTATVCRWGAWWINLIDTPGHIDFTIE 90
Cdd:cd01886   1 NIGIIAHIDAGKTTTTERILYYTGRIHKIGEVHGGGATMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDFTIE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  91 VERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRICFINKMDRVGADYRETLRQMEEKLGARPVLLQLPVGVEAS 170
Cdd:cd01886  81 VERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQIREKLGANPVPLQLPIGAEDD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 171 FAGVVDLIAGEFLTFSEaDQGSTVERHPIPAEIAGEAMAVREELIEAAADFDDAILADFLEGTAIAAERIRAAIRKGTIA 250
Cdd:cd01886 161 FEGVVDLIEMKALYWDG-ELGEKIEETDIPEDLLEEAEEAREELIETLAEVDDELMEKYLEGEEITEEEIKAAIRKGTIA 239
                       250       260       270
                ....*....|....*....|....*....|.
gi 78194975 251 CRIVPVFLGTALRNRGIQPLLDAVAAYLPSP 281
Cdd:cd01886 240 NKIVPVLCGSAFKNKGVQPLLDAVVDYLPSP 270
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
9-154 1.48e-69

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: 224.71  E-value: 1.48e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975     9 IRNIGIISHIDAGKTTVSERILFYTGETHKIGEVH-DGEAVMDWMPQEQERGITITSTATVCRWGAWWINLIDTPGHIDF 87
Cdd:pfam00009   3 HRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKgEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVDF 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78194975    88 TIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRICFINKMDRV-GADYRETLRQMEEKL 154
Cdd:pfam00009  83 VKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVdGAELEEVVEEVSREL 150
EFG_C smart00838
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ...
599-683 4.81e-35

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: 127.62  E-value: 4.81e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975    599 LLEPLMDLEIITPTEYAGKVLGSVQQKRGRVEGIITQGNTEAIRALVPLAEMFGYMTELRSATKGRGGFTMEFSRFDQAP 678
Cdd:smart00838   1 LLEPIMKVEVTVPEEYMGDVIGDLNSRRGKIEGMEQRGGAQVIKAKVPLSEMFGYATDLRSATQGRATWSMEFSHYEEVP 80

                   ....*
gi 78194975    679 ASVLQ 683
Cdd:smart00838  81 KSIAE 85
 
Name Accession Description Interval E-value
PRK13351 PRK13351
elongation factor G-like protein;
3-687 0e+00

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 1031.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975    3 HPPLDSIRNIGIISHIDAGKTTVSERILFYTGETHKIGEVHDGEAVMDWMPQEQERGITITSTATVCRWGAWWINLIDTP 82
Cdd:PRK13351   2 EMPLMQIRNIGILAHIDAGKTTLTERILFYTGKIHKMGEVEDGTTVTDWMPQEQERGITIESAATSCDWDNHRINLIDTP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   83 GHIDFTIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRICFINKMDRVGADYRETLRQMEEKLGARPVLLQ 162
Cdd:PRK13351  82 GHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLFKVLEDIEERFGKRPLPLQ 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  163 LPVGVEASFAGVVDLIAGEFLTFSEADQGSTVERHPIPAEIAGEAMAVREELIEAAADFDDAILADFLEGTAIAAERIRA 242
Cdd:PRK13351 162 LPIGSEDGFEGVVDLITEPELHFSEGDGGSTVEEGPIPEELLEEVEEAREKLIEALAEFDDELLELYLEGEELSAEQLRA 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  243 AIRKGTIACRIVPVFLGTALRNRGIQPLLDAVAAYLPSPRDIPPVTGQRPDGEAVDsLPCDPAGPLCALAFKVQADEG-R 321
Cdd:PRK13351 242 PLREGTRSGHLVPVLFGSALKNIGIEPLLDAVVDYLPSPLEVPPPRGSKDNGKPVK-VDPDPEKPLLALVFKVQYDPYaG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  322 KLTYLRIYSGTVKAGGALWNSNRGCFEKAARLFRMHAHKREPIDEALAGDIVAAIGLKEVLTGDTLCDPAHKVLLSGLTV 401
Cdd:PRK13351 321 KLTYLRVYSGTLRAGSQLYNGTGGKREKVGRLFRLQGNKREEVDRAKAGDIVAVAGLKELETGDTLHDSADPVLLELLTF 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  402 PEPVVALAVEPRGVDDRDKLLPALEKLQWEDPTFRVHEDEETGQTILTGMGELHLEVVTDRLGREFGVQVKTGRPQVVYR 481
Cdd:PRK13351 401 PEPVVSLAVEPERRGDEQKLAEALEKLVWEDPSLRVEEDEETGQTILSGMGELHLEVALERLRREFKLEVNTGKPQVAYR 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  482 ETITRPAERQEVFRTEFEGKVQGGEVHLRLAPLHRGEGvRIVVPPAEVLGITRELHTALTESLTRGASTGCVTGYPLTDL 561
Cdd:PRK13351 481 ETIRKMAEGVYRHKKQFGGKGQFGEVHLRVEPLERGAG-FIFVSKVVGGAIPEELIPAVEKGIREALASGPLAGYPVTDL 559
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  562 EVRVITVPVEQGVTTEGGVRAAAGRGLMRAARDGAPTLLEPLMDLEIITPTEYAGKVLGSVQQKRGRVEGIITQGNTE-A 640
Cdd:PRK13351 560 RVTVLDGKYHPVDSSESAFKAAARKAFLEAFRKANPVLLEPIMELEITVPTEHVGDVLGDLSQRRGRIEGTEPRGDGEvL 639
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|....*..
gi 78194975  641 IRALVPLAEMFGYMTELRSATKGRGGFTMEFSRFDQAPASVLQQFGL 687
Cdd:PRK13351 640 VKAEAPLAELFGYATRLRSMTKGRGSFTMEFSHFDPVPPAVQKKVGS 686
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
1-684 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: 920.60  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   1 MQHPPLDSIRNIGIISHIDAGKTTVSERILFYTGETHKIGEVHDGEAVMDWMPQEQERGITITSTATVCRWGAWWINLID 80
Cdd:COG0480   1 MAEYPLEKIRNIGIVAHIDAGKTTLTERILFYTGAIHRIGEVHDGNTVMDWMPEEQERGITITSAATTCEWKGHKINIID 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  81 TPGHIDFTIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRICFINKMDRVGADYRETLRQMEEKLGARPVL 160
Cdd:COG0480  81 TPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQLKERLGANPVP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 161 LQLPVGVEASFAGVVDLIAGEFLTFSEaDQGSTVERHPIPAEIAGEAMAVREELIEAAADFDDAILADFLEGTAIAAERI 240
Cdd:COG0480 161 LQLPIGAEDDFKGVIDLVTMKAYVYDD-ELGAKYEEEEIPAELKEEAEEAREELIEAVAETDDELMEKYLEGEELTEEEI 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 241 RAAIRKGTIACRIVPVFLGTALRNRGIQPLLDAVAAYLPSPRDIPPVTGQRPDGEAVDSLPCDPAGPLCALAFKVQADE- 319
Cdd:COG0480 240 KAGLRKATLAGKIVPVLCGSAFKNKGVQPLLDAVVDYLPSPLDVPAIKGVDPDTGEEVERKPDDDEPFSALVFKTMTDPf 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 320 GRKLTYLRIYSGTVKAGGALWNSNRGCFEKAARLFRMHAHKREPIDEALAGDIVAAIGLKEVLTGDTLCDPAHKVLLSGL 399
Cdd:COG0480 320 VGKLSFFRVYSGTLKSGSTVYNSTKGKKERIGRLLRMHGNKREEVDEAGAGDIVAVVKLKDTTTGDTLCDEDHPIVLEPI 399
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 400 TVPEPVVALAVEPRGVDDRDKLLPALEKLQWEDPTFRVHEDEETGQTILTGMGELHLEVVTDRLGREFGVQVKTGRPQVV 479
Cdd:COG0480 400 EFPEPVISVAIEPKTKADEDKLSTALAKLAEEDPTFRVETDEETGQTIISGMGELHLEIIVDRLKREFGVEVNVGKPQVA 479
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 480 YRETITRPAERQEVFRTEFEGKVQGGEVHLRLAPLHRGEGV----RIV---VP----PAeVL-GItRElhtALTEsltrg 547
Cdd:COG0480 480 YRETIRKKAEAEGKHKKQSGGHGQYGDVWIEIEPLPRGEGFefvdKIVggvIPkeyiPA-VEkGI-RE---AMEK----- 549
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 548 astGCVTGYPLTDLEVRVItvpveqgvtteGG----V-------RAAAGRGLMRAARDGAPTLLEPLMDLEIITPTEYAG 616
Cdd:COG0480 550 ---GVLAGYPVVDVKVTLY-----------DGsyhpVdssemafKIAASMAFKEAAKKAKPVLLEPIMKVEVTVPEEYMG 615
                       650       660       670       680       690       700
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78194975 617 KVLGSVQQKRGRVEGIITQGNTEAIRALVPLAEMFGYMTELRSATKGRGGFTMEFSRFDQAPASVLQQ 684
Cdd:COG0480 616 DVMGDLNSRRGRILGMESRGGAQVIKAEVPLAEMFGYATDLRSLTQGRGSFTMEFSHYEEVPANVAEK 683
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
15-684 0e+00

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 786.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   15 ISHIDAGKTTVSERILFYTGETHKIGEVHDGEAVMDWMPQEQERGITITSTATVCRWGAWWINLIDTPGHIDFTIEVERS 94
Cdd:PRK12740   1 VGHSGAGKTTLTEAILFYTGAIHRIGEVEDGTTTMDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVERA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   95 LRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRICFINKMDRVGADYRETLRQMEEKLGARPVLLQLPVGVEASFAGV 174
Cdd:PRK12740  81 LRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRAGADFFRVLAQLQEKLGAPVVPLQLPIGEGDDFTGV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  175 VDLIAGEFLTFseaDQGSTVERHPIPAEIAGEAMAVREELIEAAADFDDAILADFLEGTAIAAERIRAAIRKGTIACRIV 254
Cdd:PRK12740 161 VDLLSMKAYRY---DEGGPSEEIEIPAELLDRAEEAREELLEALAEFDDELMEKYLEGEELSEEEIKAGLRKATLAGEIV 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  255 PVFLGTALRNRGIQPLLDAVAAYLPSPRDIPPVTGqrPDGEAVDSLPCDPAGPLCALAFKVQADE-GRKLTYLRIYSGTV 333
Cdd:PRK12740 238 PVFCGSALKNKGVQRLLDAVVDYLPSPLEVPPVDG--EDGEEGAELAPDPDGPLVALVFKTMDDPfVGKLSLVRVYSGTL 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  334 KAGGALWNSNRGCFEKAARLFRMHAHKREPIDEALAGDIVAAIGLKEVLTGDTLCDPAHKVLLSGLTVPEPVVALAVEPR 413
Cdd:PRK12740 316 KKGDTLYNSGTGKKERVGRLYRMHGKQREEVDEAVAGDIVAVAKLKDAATGDTLCDKGDPILLEPMEFPEPVISLAIEPK 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  414 GVDDRDKLLPALEKLQWEDPTFRVHEDEETGQTILTGMGELHLEVVTDRLGREFGVQVKTGRPQVVYRETITRPAERQEV 493
Cdd:PRK12740 396 DKGDEEKLSEALGKLAEEDPTLRVERDEETGQTILSGMGELHLDVALERLKREYGVEVETGPPQVPYRETIRKKAEGHGR 475
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  494 FRTEFEGKVQGGEVHLRLAPLHRGEGVRIVvppAEVLG--ITRELHTA----LTESLTRGAstgcVTGYPLTDLEVRVI- 566
Cdd:PRK12740 476 HKKQSGGHGQFGDVWLEVEPLPRGEGFEFV---DKVVGgaVPRQYIPAvekgVREALEKGV----LAGYPVVDVKVTLTd 548
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  567 --TVPVEqgvTTEGGVRAAAGRGLMRAARDGAPTLLEPLMDLEIITPTEYAGKVLGSVQQKRGRVEGIITQGNTEAIRAL 644
Cdd:PRK12740 549 gsYHSVD---SSEMAFKIAARLAFREALPKAKPVLLEPIMKVEVSVPEEFVGDVIGDLSSRRGRILGMESRGGGDVVRAE 625
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|
gi 78194975  645 VPLAEMFGYMTELRSATKGRGGFTMEFSRFDQAPASVLQQ 684
Cdd:PRK12740 626 VPLAEMFGYATDLRSLTQGRGSFSMEFSHYEEVPGNVAEK 665
EF-G TIGR00484
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ...
5-684 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: 756.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975     5 PLDSIRNIGIISHIDAGKTTVSERILFYTGETHKIGEVHDGEAVMDWMPQEQERGITITSTATVCRWGAWWINLIDTPGH 84
Cdd:TIGR00484   6 DLNRFRNIGISAHIDAGKTTTTERILFYTGRIHKIGEVHDGAATMDWMEQEKERGITITSAATTVFWKGHRINIIDTPGH 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975    85 IDFTIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRICFINKMDRVGADYRETLRQMEEKLGARPVLLQLP 164
Cdd:TIGR00484  86 VDFTVEVERSLRVLDGAVAVLDAVGGVQPQSETVWRQANRYEVPRIAFVNKMDKTGANFLRVVNQIKQRLGANAVPIQLP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   165 VGVEASFAGVVDLIAGEFLTFsEADQGSTVERHPIPAEIAGEAMAVREELIEAAADFDDAILADFLEGTAIAAERIRAAI 244
Cdd:TIGR00484 166 IGAEDNFIGVIDLVEMKAYFF-NGDKGTKAIEKEIPSDLLEQAKELRENLVEAVAEFDEELMEKYLEGEELTIEEIKNAI 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   245 RKGTIACRIVPVFLGTALRNRGIQPLLDAVAAYLPSPRDIPPVTGQRPDGEAVDSLPCDPAGPLCALAFKVQADE-GRKL 323
Cdd:TIGR00484 245 RKGVLNCEFFPVLCGSAFKNKGVQLLLDAVVDYLPSPTDVPAIKGIDPDTEKEIERKASDDEPFSALAFKVATDPfVGQL 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   324 TYLRIYSGTVKAGGALWNSNRGCFEKAARLFRMHAHKREPIDEALAGDIVAAIGLKEVLTGDTLCDPAHKVLLSGLTVPE 403
Cdd:TIGR00484 325 TFVRVYSGVLKSGSYVKNSRKNKKERVGRLVKMHANNREEIKEVRAGDICAAIGLKDTTTGDTLCDPKIDVILERMEFPE 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   404 PVVALAVEPRGVDDRDKLLPALEKLQWEDPTFRVHEDEETGQTILTGMGELHLEVVTDRLGREFGVQVKTGRPQVVYRET 483
Cdd:TIGR00484 405 PVISLAVEPKTKADQEKMGIALGKLAEEDPTFRTFTDPETGQTIIAGMGELHLDIIVDRMKREFKVEANVGAPQVAYRET 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   484 ITRPAERQEVFRTEFEGKVQGGEVHLRLAPLHRgEGVRIVvppAEVLG--ITRELHTALTESLTRGASTGCVTGYPLTDL 561
Cdd:TIGR00484 485 IRSKVEVEGKHAKQSGGRGQYGHVKIRFEPLEP-KGYEFV---NEIKGgvIPREYIPAVDKGLQEAMESGPLAGYPVVDI 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   562 EVRVITVPVEQGVTTEGGVRAAAGRGLMRAARDGAPTLLEPLMDLEIITPTEYAGKVLGSVQQKRGRVEGIITQGNTEAI 641
Cdd:TIGR00484 561 KATLFDGSYHDVDSSEMAFKLAASLAFKEAGKKANPVLLEPIMKVEVEVPEEYMGDVMGDLSSRRGIIEGMEARGNVQKI 640
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|...
gi 78194975   642 RALVPLAEMFGYMTELRSATKGRGGFTMEFSRFDQAPASVLQQ 684
Cdd:TIGR00484 641 KAEVPLSEMFGYATDLRSFTQGRGTYSMEFLHYGEVPSSVANE 683
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
11-281 3.27e-158

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: 456.95  E-value: 3.27e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  11 NIGIISHIDAGKTTVSERILFYTGETHKIGEVHDGEAVMDWMPQEQERGITITSTATVCRWGAWWINLIDTPGHIDFTIE 90
Cdd:cd01886   1 NIGIIAHIDAGKTTTTERILYYTGRIHKIGEVHGGGATMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDFTIE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  91 VERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRICFINKMDRVGADYRETLRQMEEKLGARPVLLQLPVGVEAS 170
Cdd:cd01886  81 VERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQIREKLGANPVPLQLPIGAEDD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 171 FAGVVDLIAGEFLTFSEaDQGSTVERHPIPAEIAGEAMAVREELIEAAADFDDAILADFLEGTAIAAERIRAAIRKGTIA 250
Cdd:cd01886 161 FEGVVDLIEMKALYWDG-ELGEKIEETDIPEDLLEEAEEAREELIETLAEVDDELMEKYLEGEEITEEEIKAAIRKGTIA 239
                       250       260       270
                ....*....|....*....|....*....|.
gi 78194975 251 CRIVPVFLGTALRNRGIQPLLDAVAAYLPSP 281
Cdd:cd01886 240 NKIVPVLCGSAFKNKGVQPLLDAVVDYLPSP 270
PRK07560 PRK07560
elongation factor EF-2; Reviewed
1-685 7.33e-111

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 351.09  E-value: 7.33e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975    1 MQHPplDSIRNIGIISHIDAGKTTVSERILFYTGethKIGEVHDGEA-VMDWMPQEQERGITITStATVCRWGAW----- 74
Cdd:PRK07560  14 MKNP--EQIRNIGIIAHIDHGKTTLSDNLLAGAG---MISEELAGEQlALDFDEEEQARGITIKA-ANVSMVHEYegkey 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   75 WINLIDTPGHIDFTIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRICFINKMDRVGADYRETLRQMEEKL 154
Cdd:PRK07560  88 LINLIDTPGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKPVLFINKVDRLIKELKLTPQEMQQRL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  155 GarpvllqlpvgveasfagvvdliagefltfseadqgstverhpipaEIAGEAmavrEELIEAAAD--FDDAILADFLEG 232
Cdd:PRK07560 168 L----------------------------------------------KIIKDV----NKLIKGMAPeeFKEKWKVDVEDG 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  233 TaiaaeriraairkgtiacrivpVFLGTALRNRGIQ------------------------------PL----LDAVAAYL 278
Cdd:PRK07560 198 T----------------------VAFGSALYNWAISvpmmqktgikfkdiidyyekgkqkelaekaPLhevvLDMVVKHL 255
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  279 PSPRD-----IPPVTGQRPDGEAVDS-LPCDPAGPLCALAFKVQADEGRKLTYL-RIYSGTVKAGGALWNSNRGCFEKAA 351
Cdd:PRK07560 256 PNPIEaqkyrIPKIWKGDLNSEVGKAmLNCDPNGPLVMMVTDIIVDPHAGEVATgRVFSGTLRKGQEVYLVGAKKKNRVQ 335
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  352 RLFRMHAHKREPIDEALAGDIVAAIGLKEVLTGDTLCDPAHKVLLSGLT-VPEPVVALAVEPRGVDDRDKLLPALEKLQW 430
Cdd:PRK07560 336 QVGIYMGPEREEVEEIPAGNIAAVTGLKDARAGETVVSVEDMTPFESLKhISEPVVTVAIEAKNPKDLPKLIEVLRQLAK 415
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  431 EDPTFRVHEDEETGQTILTGMGELHLEVVTDRLGREFGVQVKTGRPQVVYRETITRPAErqevfrtEFEGK--------- 501
Cdd:PRK07560 416 EDPTLVVKINEETGEHLLSGMGELHLEVITYRIKRDYGIEVVTSEPIVVYRETVRGKSQ-------VVEGKspnkhnrfy 488
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  502 -------------VQGGEVHLRLAPLHRG--------------EGVRIV-VPPAEVL-----GI-----TREL-HTALTE 542
Cdd:PRK07560 489 isvepleeevieaIKEGEISEDMDKKEAKilreklieagmdkdEAKRVWaIYNGNVFidmtkGIqylneVMELiIEGFRE 568
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  543 SLTRGastgcvtgyPLTDLEVRVITV----------PVEQGvttEGGVRAAAGRGLMRAARDGAPTLLEPLMDLEIITPT 612
Cdd:PRK07560 569 AMKEG---------PLAAEPVRGVKVrlhdaklhedAIHRG---PAQVIPAVRNAIFAAMLTAKPTLLEPIQKVDINVPQ 636
                        730       740       750       760       770       780       790
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 78194975  613 EYAGKVLGSVQQKRGRVEGIITQGNTEAIRALVPLAEMFGYMTELRSATKGRGGFTMEFSRFDQAPASVLQQF 685
Cdd:PRK07560 637 DYMGAVTREIQGRRGKILDMEQEGDMAIIEAEAPVAEMFGFAGEIRSATEGRALWSTEFAGFEPVPDSLQLDI 709
aEF-2 TIGR00490
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ...
1-685 1.05e-91

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


Pssm-ID: 129581 [Multi-domain]  Cd Length: 720  Bit Score: 300.27  E-value: 1.05e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975     1 MQHPplDSIRNIGIISHIDAGKTTVSERILFYTGETHKigEVHDGEAVMDWMPQEQERGITI----TSTATVCRWGAWWI 76
Cdd:TIGR00490  13 MWKP--KFIRNIGIVAHIDHGKTTLSDNLLAGAGMISE--ELAGQQLYLDFDEQEQERGITInaanVSMVHEYEGNEYLI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975    77 NLIDTPGHIDFTIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRICFINKMDRVGADYRETLRQMEEKLga 156
Cdd:TIGR00490  89 NLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKPVLFINKVDRLINELKLTPQELQERF-- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   157 rpvllqlpvgveasfagvVDLIAgefltfseadQGSTVERHPIPAEIAGEAMaVREELIEAA---ADFDDAILADFLEGT 233
Cdd:TIGR00490 167 ------------------IKIIT----------EVNKLIKAMAPEEFRDKWK-VRVEDGSVAfgsAYYNWAISVPSMKKT 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   234 AIAAERIRAAIRKGTIA--CRIVPVFlgtalrnrgiQPLLDAVAAYLPSPRD-----IPPV-TGQRPDGEAVDSLPCDPA 305
Cdd:TIGR00490 218 GIGFKDIYKYCKEDKQKelAKKSPLH----------QVVLDMVIRHLPSPIEaqkyrIPVIwKGDLNSEVGKAMLNCDPK 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   306 GPLCALAFKVQAD-EGRKLTYLRIYSGTVKAGGALWNSNRGCFEKAARLFRMHAHKREPIDEALAGDIVAAIGLKEVLTG 384
Cdd:TIGR00490 288 GPLALMITKIVVDkHAGEVAVGRLYSGTIRPGMEVYIVDRKAKARIQQVGVYMGPERVEVDEIPAGNIVAVIGLKDAVAG 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   385 DTLCDPAHKVL-LSGLT-VPEPVVALAVEPRGVDDRDKLLPALEKLQWEDPTFRVHEDEETGQTILTGMGELHLEVVTDR 462
Cdd:TIGR00490 368 ETICTTVENITpFESIKhISEPVVTVAIEAKNTKDLPKLIEVLRQVAKEDPTVHVEINEETGEHLISGMGELHLEIIVEK 447
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   463 LGREFGVQVKTGRPQVVYRETIT---------------------RPAErQEVFRTEFEGKVQGGEV-------HLRLAPL 514
Cdd:TIGR00490 448 IREDYGLDVETSPPIVVYRETVTgtspvvegkspnkhnrfyivvEPLE-ESVIQAFKEGKIVDMKMkkkerrrLLIEAGM 526
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   515 HRGEGVRI--VVPPAEVLGITR------ELHTALTESLTRGASTGCVTGYPLTDLEVRVITVPVEQGVTTEG--GVRAAA 584
Cdd:TIGR00490 527 DSEEAARVeeYYEGNLFINMTRgiqyldETKELILEGFREAMRNGPIAREKCMGVKVKLMDAKLHEDAVHRGpaQVIPAV 606
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   585 GRGLMRAARDGAPTLLEPLMDLEIITPTEYAGKVLGSVQQKRGRVEGIITQGNTEAIRALVPLAEMFGYMTELRSATKGR 664
Cdd:TIGR00490 607 RSGIFAAMMQAKPVLLEPYQKVFINVPQDMMGAATREIQNRRGQILEMKQEGDMVTIIAKAPVAEMFGFAGAIRGATSGR 686
                         730       740
                  ....*....|....*....|.
gi 78194975   665 GGFTMEFSRFDQAPASVLQQF 685
Cdd:TIGR00490 687 CLWSTEHAGFELVPQNLQQEF 707
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
11-281 1.20e-78

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: 251.74  E-value: 1.20e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  11 NIGIISHIDAGKTTVSERILFYTGETHKIGEVHDGEAVMDWMPQEQERGITITSTATVCRWGAWWINLIDTPGHIDFTIE 90
Cdd:cd04170   1 NIALVGHSGSGKTTLAEALLYATGAIDRLGRVEDGNTVSDYDPEEKKRKMSIETSVAPLEWNGHKINLIDTPGYADFVGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  91 VERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRICFINKMDRVGADYRETLRQMEEKLGARPVLLQLPVGVEAS 170
Cdd:cd04170  81 TLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRARADFDKTLAALREAFGRPVVPIQLPIGEGDE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 171 FAGVVDLIAGEFLTFSEadqGSTVERHPIPAEIAGEAMAVREELIEAAADFDDAILADFLEGTAIAAERIRAAIRKGTIA 250
Cdd:cd04170 161 FTGVVDLLSEKAYRYDP---GEPSVEIEIPEELKEKVAEAREELLEAVAETDEELMEKYLEEGELTEEELRAGLRRALRA 237
                       250       260       270
                ....*....|....*....|....*....|.
gi 78194975 251 CRIVPVFLGTALRNRGIQPLLDAVAAYLPSP 281
Cdd:cd04170 238 GLIVPVFFGSALTGIGVRRLLDALVELAPSP 268
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
9-154 1.48e-69

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: 224.71  E-value: 1.48e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975     9 IRNIGIISHIDAGKTTVSERILFYTGETHKIGEVH-DGEAVMDWMPQEQERGITITSTATVCRWGAWWINLIDTPGHIDF 87
Cdd:pfam00009   3 HRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKgEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVDF 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78194975    88 TIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRICFINKMDRV-GADYRETLRQMEEKL 154
Cdd:pfam00009  83 VKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVdGAELEEVVEEVSREL 150
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
11-281 5.86e-66

Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.


Pssm-ID: 206731 [Multi-domain]  Cd Length: 237  Bit Score: 217.10  E-value: 5.86e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  11 NIGIISHIDAGKTTVSERILFYTGETHKIGEVHDGEAVMDWMPQEQERGITITSTATVCRWGAWWINLIDTPGHIDFTIE 90
Cdd:cd04168   1 NIGILAHVDAGKTTLTESLLYTSGAIRELGSVDKGTTRTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIAE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  91 VERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRICFINKMDRVGADYRETLRQMEEKLGARPVLLQLPVGVEas 170
Cdd:cd04168  81 VERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTIIFVNKIDRAGADLEKVYQEIKEKLSPDIVPMQKVGLYP-- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 171 fagvvdliagefltfseadqgSTVERHPIPaeiageamavrEELIEAAADFDDAILADFLEGTAIAAERIRAAIRKGTIA 250
Cdd:cd04168 159 ---------------------NICDTNNID-----------DEQIETVAEGNDELLEKYLSGGPLEELELDNELSARIQK 206
                       250       260       270
                ....*....|....*....|....*....|.
gi 78194975 251 CRIVPVFLGTALRNRGIQPLLDAVAAYLPSP 281
Cdd:cd04168 207 ASLFPVYHGSALKGIGIDELLEGITNLFPTS 237
PrfC COG4108
Peptide chain release factor RF-3 [Translation, ribosomal structure and biogenesis]; Peptide ...
10-471 6.26e-58

Peptide chain release factor RF-3 [Translation, ribosomal structure and biogenesis]; Peptide chain release factor RF-3 is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 443284 [Multi-domain]  Cd Length: 528  Bit Score: 204.53  E-value: 6.26e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  10 RNIGIISHIDAGKTTVSERILFYTGETHKIGEVH----DGEAVMDWMPQEQERGITITSTatV-------CRwgawwINL 78
Cdd:COG4108  11 RTFAIISHPDAGKTTLTEKLLLFGGAIQLAGAVKarkaRRHATSDWMEIEKQRGISVTSS--VmqfeyrgYV-----INL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  79 IDTPGHIDFTievE---RSLRALDGAVAIFSAVEGVQPQSE---SVWRQADryqVPRICFINKMDRVGADYRETLRQMEE 152
Cdd:COG4108  84 LDTPGHEDFS---EdtyRTLTAVDSAVMVIDAAKGVEPQTRklfEVCRLRG---IPIITFINKLDREGRDPLELLDEIEE 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 153 KLGARPVLLQLPVGVEASFAGVVDLIAGEFLTFSEADQGSTVER-------HPIPAEIAGEAMA--VRE--ELIEAA-AD 220
Cdd:COG4108 158 VLGIDCAPMTWPIGMGKDFKGVYDRYTDEVHLFERGAGGATEAPeeiegldDPELDELLGEDLAeqLREeiELLDGAgPE 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 221 FDdaiLADFLEGtaiaaeriraairkgtiacRIVPVFLGTALRNRGIQPLLDAVAAYLPSPRDIPPVTGQ-RPDGEavds 299
Cdd:COG4108 238 FD---LEAFLAG-------------------ELTPVFFGSALNNFGVRELLDAFVELAPPPRPREADEREvEPTEE---- 291
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 300 lpcdpagPLCALAFKVQA-------DegrKLTYLRIYSGTVKAGGALWNSNRGcfekaaRLFRMH------AHKREPIDE 366
Cdd:COG4108 292 -------KFSGFVFKIQAnmdpahrD---RIAFMRICSGKFERGMKVKHVRTG------KKIRLSnpqqffAQDRETVEE 355
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 367 ALAGDIvaaIGLKEVLT---GDTLCDPaHKVLLSGLtvpePVVA---LA-VEPRGVDDRDKLLPALEKLQWEDPT--FRV 437
Cdd:COG4108 356 AYPGDI---IGLHNHGTlriGDTLTEG-EKLEFTGI----PSFApelFRrVRLKDPMKAKQLRKGLEQLAEEGAVqvFRP 427
                       490       500       510
                ....*....|....*....|....*....|....
gi 78194975 438 HEDEEtgqTILTGMGELHLEVVTDRLGREFGVQV 471
Cdd:COG4108 428 LDGND---PILGAVGQLQFEVVQYRLKNEYGVEV 458
RF3 cd04169
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ...
10-281 1.48e-56

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: 193.20  E-value: 1.48e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  10 RNIGIISHIDAGKTTVSERILFYTGETHKIGEVH----DGEAVMDWMPQEQERGITITSTATVCRWGAWWINLIDTPGHI 85
Cdd:cd04169   3 RTFAIISHPDAGKTTLTEKLLLFGGAIQEAGAVKarksRKHATSDWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  86 DFTIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRICFINKMDRVGADYRETLRQMEEKLGARPVLLQLPV 165
Cdd:cd04169  83 DFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDREGRDPLELLDEIENELGIDCAPMTWPI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 166 GVEASFAGVVDLIAGEFLTFSEADQGSTVER-------HPIPAEIAGEAMA--VRE--ELIEAA-ADFDdaiLADFLEGT 233
Cdd:cd04169 163 GMGKDFKGVYDRYDKEIYLYERGAGGAIKAPeetkgldDPKLDELLGEDLAeqLREelELVEGAgPEFD---KELFLAGE 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 78194975 234 aiaaeriraairkgtiacrIVPVFLGTALRNRGIQPLLDAVAAYLPSP 281
Cdd:cd04169 240 -------------------LTPVFFGSALNNFGVQELLDAFVKLAPAP 268
PTZ00416 PTZ00416
elongation factor 2; Provisional
1-684 1.06e-55

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 204.13  E-value: 1.06e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975    1 MQHPplDSIRNIGIISHIDAGKTTVSERILFYTGethKIGEVHDGEA-VMDWMPQEQERGITITSTA----------TVC 69
Cdd:PTZ00416  13 MDNP--DQIRNMSVIAHVDHGKSTLTDSLVCKAG---IISSKNAGDArFTDTRADEQERGITIKSTGislyyehdleDGD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   70 RWGAWWINLIDTPGHIDFTIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRICFINKMDRV-------GAD 142
Cdd:PTZ00416  88 DKQPFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKVDRAilelqldPEE 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  143 YRETLRQMEEKLGA----------RPVLLQLPVGVEA-------------SFA-------GV--------------VDLI 178
Cdd:PTZ00416 168 IYQNFVKTIENVNViiatyndelmGDVQVYPEKGTVAfgsglqgwaftltTFAriyakkfGVeeskmmerlwgdnfFDAK 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  179 AGEFLTFSEADQGSTVER-------HPIpaeiageamavrEELIEAAADFDDAILADFLEGTAIAAERIRAAIRKGTIAC 251
Cdd:PTZ00416 248 TKKWIKDETNAQGKKLKRafcqfilDPI------------CQLFDAVMNEDKEKYDKMLKSLNISLTGEDKELTGKPLLK 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  252 RIVPVFLGTAlrnrgiQPLLDAVAAYLPSPRDIPP------VTGQRPDGEAVDSLPCDPAGPLCALAFKV--QADEGRKL 323
Cdd:PTZ00416 316 AVMQKWLPAA------DTLLEMIVDHLPSPKEAQKyrvenlYEGPMDDEAANAIRNCDPNGPLMMYISKMvpTSDKGRFY 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  324 TYLRIYSGTVKAG------GALW--NSNRGCFEKA-ARLFRMHAHKREPIDEALAGDIVAAIGLKEVL--TGD-TLCDPA 391
Cdd:PTZ00416 390 AFGRVFSGTVATGqkvriqGPNYvpGKKEDLFEKNiQRTVLMMGRYVEQIEDVPCGNTVGLVGVDQYLvkSGTiTTSETA 469
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  392 HKVLLSGLTVpEPVVALAVEPRGVDDRDKLLPALEKLQWEDPTFRVhEDEETGQTILTGMGELHLEVVTDRLGREF-GVQ 470
Cdd:PTZ00416 470 HNIRDMKYSV-SPVVRVAVEPKNPKDLPKLVEGLKRLAKSDPLVVC-TTEESGEHIVAGCGELHVEICLKDLEDDYaNID 547
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  471 VKTGRPQVVYRETITRPAERQEVFRTEFEgkvqggevHLRL----APLHRGEGVRI----VVPPAEVLGITRELHTAL-- 540
Cdd:PTZ00416 548 IIVSDPVVSYRETVTEESSQTCLSKSPNK--------HNRLymkaEPLTEELAEAIeegkVGPEDDPKERANFLADKYew 619
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  541 --TESL--------TRGAS-----TGCVTGYPltdlEVRVITVPVEQGVTTEG--------GVRA----------AAGRG 587
Cdd:PTZ00416 620 dkNDARkiwcfgpeNKGPNvlvdvTKGVQYMN----EIKDSCVSAFQWATKEGvlcdenmrGIRFnildvtlhadAIHRG 695
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  588 ---LMRAARDG--------APTLLEPLMDLEIITPTEYAGKVLGSVQQKRGRVegiITQGNTEA-----IRALVPLAEMF 651
Cdd:PTZ00416 696 agqIIPTARRVfyaceltaSPRLLEPMFLVDITAPEDAMGGIYSVLNRRRGVV---IGEEQRPGtplsnIKAYLPVAESF 772
                        810       820       830
                 ....*....|....*....|....*....|...
gi 78194975  652 GYMTELRSATKGRGGFTMEFSRFDQAPASVLQQ 684
Cdd:PTZ00416 773 GFTAALRAATSGQAFPQCVFDHWQVVPGDPLEP 805
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
7-482 1.28e-49

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


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 183.30  E-value: 1.28e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   7 DSIRNIGIISHIDAGKTTVSERILFYTGETHKIGEVhdGEAVMDWMPQEQERGITITSTATVCRWGAWWINLIDTPGHID 86
Cdd:COG1217   4 EDIRNIAIIAHVDHGKTTLVDALLKQSGTFRENQEV--AERVMDSNDLERERGITILAKNTAVRYKGVKINIVDTPGHAD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  87 FTIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRICFINKMDRVGADYRETLRQMEE---KLGARPVLLQL 163
Cdd:COG1217  82 FGGEVERVLSMVDGVLLLVDAFEGPMPQTRFVLKKALELGLKPIVVINKIDRPDARPDEVVDEVFDlfiELGATDEQLDF 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 164 PVgVEASfagvvdliagefltfseADQGstverhpipaeIAGEAMAVREElieaaadfddailadflegtaiaaeriraa 243
Cdd:COG1217 162 PV-VYAS-----------------ARNG-----------WASLDLDDPGE------------------------------ 182
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 244 irkgtiacrivpvflgtalrnrGIQPLLDAVAAYLPSPrdippvtgqrpdgeavdslPCDPAGPLCALAFKVQADE--GR 321
Cdd:COG1217 183 ----------------------DLTPLFDTILEHVPAP-------------------EVDPDGPLQMLVTNLDYSDyvGR 221
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 322 KLTyLRIYSGTVKAGGALWNSNR-GCFEKA--ARLFRMHAHKREPIDEALAGDIVAAIGLKEVLTGDTLCDPAHKVLLSG 398
Cdd:COG1217 222 IAI-GRIFRGTIKKGQQVALIKRdGKVEKGkiTKLFGFEGLERVEVEEAEAGDIVAIAGIEDINIGDTICDPENPEALPP 300
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 399 LTVPEPVVALAVeprGVDD----------------RDKLLPALEKlqweDPTFRVHEDEETGQTILTGMGELHLEVVTDR 462
Cdd:COG1217 301 IKIDEPTLSMTF---SVNDspfagregkfvtsrqiRERLEKELET----NVALRVEETDSPDAFKVSGRGELHLSILIET 373
                       490       500
                ....*....|....*....|.
gi 78194975 463 LGRE-FGVQVktGRPQVVYRE 482
Cdd:COG1217 374 MRREgYELQV--SRPEVIFKE 392
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
11-160 6.35e-47

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: 164.01  E-value: 6.35e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  11 NIGIISHIDAGKTTVSERILFYTGETHKIGEVHdgEAVMDWMPQEQERGITITSTATVCRWGAWWINLIDTPGHIDFTIE 90
Cdd:cd00881   1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRK--ETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKE 78
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 78194975  91 VERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRICFINKMDRVG-ADYRETLRQMEEKLGARPVL 160
Cdd:cd00881  79 TVRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGeEDFDEVLREIKELLKLIGFT 149
prfC PRK00741
peptide chain release factor 3; Provisional
10-471 6.52e-47

peptide chain release factor 3; Provisional


Pssm-ID: 179105 [Multi-domain]  Cd Length: 526  Bit Score: 174.17  E-value: 6.52e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   10 RNIGIISHIDAGKTTVSERILFYTGETHKIGEV-------HdgeAVMDWMPQEQERGITITStaTV-------CRwgaww 75
Cdd:PRK00741  11 RTFAIISHPDAGKTTLTEKLLLFGGAIQEAGTVkgrksgrH---ATSDWMEMEKQRGISVTS--SVmqfpyrdCL----- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   76 INLIDTPGHIDFTIEVERSLRALDGAVAIFSAVEGVQPQSE---SVWRQADryqVPRICFINKMDRVGADYRETLRQMEE 152
Cdd:PRK00741  81 INLLDTPGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTRklmEVCRLRD---TPIFTFINKLDRDGREPLELLDEIEE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  153 KLGARPVLLQLPVGVEASFAGVVDLIAGEFLTFsEADQGSTVE-------------RHPIPAEIAGEAmavREEL---IE 216
Cdd:PRK00741 158 VLGIACAPITWPIGMGKRFKGVYDLYNDEVELY-QPGEGHTIQeveiikgldnpelDELLGEDLAEQL---REELelvQG 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  217 AAADFDdaiLADFLEGtaiaaeriraairkgtiacRIVPVFLGTALRNRGIQPLLDAVAAYLPSPRdiPPVTGQRPdgea 296
Cdd:PRK00741 234 ASNEFD---LEAFLAG-------------------ELTPVFFGSALNNFGVQEFLDAFVEWAPAPQ--PRQTDERE---- 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  297 VDslPCDPagPLCALAFKVQA-------DegrKLTYLRIYSGTVKAGGALWNSNRGcfeKAARLFR----MhAHKREPID 365
Cdd:PRK00741 286 VE--PTEE--KFSGFVFKIQAnmdpkhrD---RIAFVRVCSGKFEKGMKVRHVRTG---KDVRISNaltfM-AQDREHVE 354
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  366 EALAGDIvaaIGLKEVLT---GDTLCDpAHKVLLSGLTVPEPVVALAVEPRGVDDRDKLLPALEKLQWEDPTfRVHEDEE 442
Cdd:PRK00741 355 EAYAGDI---IGLHNHGTiqiGDTFTQ-GEKLKFTGIPNFAPELFRRVRLKNPLKQKQLQKGLVQLSEEGAV-QVFRPLD 429
                        490       500
                 ....*....|....*....|....*....
gi 78194975  443 TGQTILTGMGELHLEVVTDRLGREFGVQV 471
Cdd:PRK00741 430 NNDLILGAVGQLQFEVVAHRLKNEYNVEA 458
PLN00116 PLN00116
translation elongation factor EF-2 subunit; Provisional
7-664 1.48e-44

translation elongation factor EF-2 subunit; Provisional


Pssm-ID: 177730 [Multi-domain]  Cd Length: 843  Bit Score: 171.45  E-value: 1.48e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975    7 DSIRNIGIISHIDAGKTTVSERILFYTGethKIGEVHDGEA-VMDWMPQEQERGITITST----------------ATVC 69
Cdd:PLN00116  17 HNIRNMSVIAHVDHGKSTLTDSLVAAAG---IIAQEVAGDVrMTDTRADEAERGITIKSTgislyyemtdeslkdfKGER 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   70 RWGAWWINLIDTPGHIDFTIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRICFINKMDR------VGAD- 142
Cdd:PLN00116  94 DGNEYLINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTETVLRQALGERIRPVLTVNKMDRcflelqVDGEe 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  143 -YRETLRQME-----------EKLGarPVLLQLPVGVEASFAGV----------VDLIAGEFLT---------------- 184
Cdd:PLN00116 174 aYQTFSRVIEnanvimatyedPLLG--DVQVYPEKGTVAFSAGLhgwaftltnfAKMYASKFGVdeskmmerlwgenffd 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  185 -----FSEADQGS-TVER-------HPIpAEIAGEAMAVR-EELIEAAADFDDAILADFLEgtaiaaeriraairkgtia 250
Cdd:PLN00116 252 patkkWTTKNTGSpTCKRgfvqfcyEPI-KQIINTCMNDQkDKLWPMLEKLGVTLKSDEKE------------------- 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  251 crivpvFLGTALRNRGIQPLLDAVAA-------YLPSprdipPVTGQR---------P--DGEAVDSLPCDPAGPLCALA 312
Cdd:PLN00116 312 ------LMGKALMKRVMQTWLPASDAllemiifHLPS-----PAKAQRyrvenlyegPldDKYATAIRNCDPNGPLMLYV 380
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  313 FKV--QADEGRKLTYLRIYSGTVKAG------GA---------LWNSNrgcfekAARLFRMHAHKREPIDEALAGDIVAA 375
Cdd:PLN00116 381 SKMipASDKGRFFAFGRVFSGTVATGmkvrimGPnyvpgekkdLYVKS------VQRTVIWMGKKQESVEDVPCGNTVAM 454
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  376 IGLKEVLT-----GDTLCDPAHKVLLSGLTVpEPVVALAVEPRGVDDRDKLLPALEKLQWEDPTFrVHEDEETGQTILTG 450
Cdd:PLN00116 455 VGLDQFITknatlTNEKEVDAHPIKAMKFSV-SPVVRVAVQCKNASDLPKLVEGLKRLAKSDPMV-QCTIEESGEHIIAG 532
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  451 MGELHLEVVTDRLGREF--GVQVKTGRPQVVYRETITRPAERQEVF-------RTEFEGK---------VQGGEVHLRLA 512
Cdd:PLN00116 533 AGELHLEICLKDLQDDFmgGAEIKVSDPVVSFRETVLEKSCRTVMSkspnkhnRLYMEARpleeglaeaIDDGRIGPRDD 612
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  513 PLHRGegvRIVvppAEVLGITRELHTA------------LTESLTRGAS------TGCVTGY-------PLTDLEVR--- 564
Cdd:PLN00116 613 PKIRS---KIL---AEEFGWDKDLAKKiwcfgpettgpnMVVDMCKGVQylneikDSVVAGFqwatkegALAEENMRgic 686
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  565 --VITVPVEQGVTTEGG--VRAAAGRGLMRAARDGAPTLLEPLMDLEIITPTEYAGKVLGSVQQKRGRVEGIITQGNTE- 639
Cdd:PLN00116 687 feVCDVVLHADAIHRGGgqIIPTARRVIYASQLTAKPRLLEPVYLVEIQAPEQALGGIYSVLNQKRGHVFEEMQRPGTPl 766
                        810       820
                 ....*....|....*....|....*.
gi 78194975  640 -AIRALVPLAEMFGYMTELRSATKGR 664
Cdd:PLN00116 767 yNIKAYLPVIESFGFSGTLRAATSGQ 792
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
10-138 3.90e-39

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: 143.91  E-value: 3.90e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  10 RNIGIISHIDAGKTTVSERILFYTGethKIGEVHDGEA-VMDWMPQEQERGITITSTATVCRW---------GAWWINLI 79
Cdd:cd01885   1 RNICIIAHVDHGKTTLSDSLLASAG---IISEKLAGKArYLDTREDEQERGITIKSSAISLYFeyeeekmdgNDYLINLI 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 78194975  80 DTPGHIDFTIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRICFINKMDR 138
Cdd:cd01885  78 DSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDR 136
EFG_like_IV cd01680
Elongation Factor G-like domain IV. This family includes the translational elongation factor ...
480-596 2.97e-38

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: 137.76  E-value: 2.97e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 480 YRETITRPAERQEVFRTEFEGKVQGGEVHLRLAPLHRGEGVRIVVPPAEVLGItRELHTALTESLTRGASTGCVTGYPLT 559
Cdd:cd01680   1 YRETIRKSVEATGEFERELGGKPQFGEVTLRVEPLERGSGVRVVDPVDEELLP-AELKEAVEEGIRDACASGPLTGYPLT 79
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 78194975 560 DLEVRVITVPVEQGVTTEGGVRAAAGRGLMRAARDGA 596
Cdd:cd01680  80 DVRVTVLDVPYHEGVSTEAGFRAAAGRAFESAAQKAG 116
EFG_mtEFG_II cd04088
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation ...
308-389 3.08e-36

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: 130.72  E-value: 3.08e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 308 LCALAFKVQADEGR-KLTYLRIYSGTVKAGGALWNSNRGCFEKAARLFRMHAHKREPIDEALAGDIVAAIGLKEVLTGDT 386
Cdd:cd04088   1 FSALVFKTMADPFVgKLTFFRVYSGTLKSGSTVYNSTKGKKERVGRLLRMHGKKREEVEELGAGDIGAVVGLKDTRTGDT 80

                ...
gi 78194975 387 LCD 389
Cdd:cd04088  81 LCD 83
EFG_III cd16262
Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial ...
402-477 7.36e-36

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: 129.50  E-value: 7.36e-36
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78194975 402 PEPVVALAVEPRGVDDRDKLLPALEKLQWEDPTFRVHEDEETGQTILTGMGELHLEVVTDRLGREFGVQVKTGRPQ 477
Cdd:cd16262   1 PEPVISLAIEPKTKADEDKLSKALARLAEEDPTLRVSRDEETGQTILSGMGELHLEIIVERLKREYGVEVEVGKPQ 76
EFG_III pfam14492
Elongation Factor G, domain III; This domain is found in Elongation Factor G. It shares a ...
401-475 1.05e-35

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: 129.14  E-value: 1.05e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78194975   401 VPEPVVALAVEPRGVDDRDKLLPALEKLQWEDPTFRVHEDEETGQTILTGMGELHLEVVTDRLGREFGVQVKTGR 475
Cdd:pfam14492   1 FPEPVISVAIEPKTKGDEDKLSKALNRLLEEDPTLRVERDEETGETILSGMGELHLEIVVDRLKRKYGVEVELGP 75
LepA COG0481
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ...
5-677 1.35e-35

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


Pssm-ID: 440249 [Multi-domain]  Cd Length: 598  Bit Score: 142.47  E-value: 1.35e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   5 PLDSIRNIGIISHIDAGKTTVSERILFYTGethKIGEVHDGEAVMDWMPQEQERGITITSTATVCRWGAW-----WINLI 79
Cdd:COG0481   2 DQKNIRNFSIIAHIDHGKSTLADRLLELTG---TLSEREMKEQVLDSMDLERERGITIKAQAVRLNYKAKdgetyQLNLI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  80 DTPGHIDFTIEVERSLRALDGAVAIFSAVEGVQPQSesvwrQADRYQ--------VPricFINKMDRVGADYRETLRQME 151
Cdd:COG0481  79 DTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQT-----LANVYLalendleiIP---VINKIDLPSADPERVKQEIE 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 152 EKLGarpvllqlpvgveasfagvvdliagefltfseadqgstverhpIPAEiageamavreelieaaadfdDAILADFLE 231
Cdd:COG0481 151 DIIG-------------------------------------------IDAS--------------------DAILVSAKT 167
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 232 GTaiaaeriraairkgtiacrivpvflgtalrnrGIQPLLDAVAAYLPSPRdippvtgqrpdgeavdslpCDPAGPLCAL 311
Cdd:COG0481 168 GI--------------------------------GIEEILEAIVERIPPPK-------------------GDPDAPLQAL 196
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 312 AFKVQADEGRK-LTYLRIYSGTVKAG--------GALWNSNR-GCFekaarlfrmhAHKREPIDEALAGD---IVAAI-G 377
Cdd:COG0481 197 IFDSWYDSYRGvVVYVRVFDGTLKKGdkikmmstGKEYEVDEvGVF----------TPKMTPVDELSAGEvgyIIAGIkD 266
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 378 LKEVLTGDTLCDPAH--KVLLSGLTVPEPVVALAVEPRGVDDRDKLLPALEKLQWEDPTFrVHEdEETGQTILTG----- 450
Cdd:COG0481 267 VRDARVGDTITLAKNpaAEPLPGFKEVKPMVFAGLYPVDSDDYEDLRDALEKLQLNDASL-TYE-PETSAALGFGfrcgf 344
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 451 MGELHLEVVTDRLGREFGVQVKTGRPQVVYretitrpaerqevfrtefegkvqggEVHLRlaplhRGEgVRIVVPPAEVl 530
Cdd:COG0481 345 LGLLHMEIIQERLEREFDLDLITTAPSVVY-------------------------EVTLT-----DGE-VIEVDNPSDL- 392
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 531 gitrelhtaltesltrgastgcvtgYPLTDLEvrvitvpveqgvtteggvraaagrglmraardgapTLLEPLMDLEIIT 610
Cdd:COG0481 393 -------------------------PDPGKIE-----------------------------------EIEEPIVKATIIT 412
                       650       660       670       680       690       700
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78194975 611 PTEYAGKVLGSVQQKRGRVEGIITQGNTEA-IRALVPLAE-MFGYMTELRSATKGRGGFTMEFSRFDQA 677
Cdd:COG0481 413 PSEYVGAVMELCQEKRGVQKNMEYLGENRVeLTYELPLAEiVFDFFDRLKSITRGYASLDYEFIGYRES 481
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
8-165 4.23e-35

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: 131.56  E-value: 4.23e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   8 SIRNIGIISHIDAGKTTVSERILFYTGETHKIGEVhdGEAVMDWMPQEQERGITITSTATVCRWGAWWINLIDTPGHIDF 87
Cdd:cd01891   1 KIRNIAIIAHVDHGKTTLVDALLKQSGTFRENEEV--GERVMDSNDLERERGITILAKNTAITYKDTKINIIDTPGHADF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  88 TIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRICFINKMDRVGADYRETLRQMEE---KLGARPVLLQLP 164
Cdd:cd01891  79 GGEVERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDRPDARPEEVVDEVFDlflELNATDEQLDFP 158

                .
gi 78194975 165 V 165
Cdd:cd01891 159 I 159
EFG_C smart00838
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ...
599-683 4.81e-35

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: 127.62  E-value: 4.81e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975    599 LLEPLMDLEIITPTEYAGKVLGSVQQKRGRVEGIITQGNTEAIRALVPLAEMFGYMTELRSATKGRGGFTMEFSRFDQAP 678
Cdd:smart00838   1 LLEPIMKVEVTVPEEYMGDVIGDLNSRRGKIEGMEQRGGAQVIKAKVPLSEMFGYATDLRSATQGRATWSMEFSHYEEVP 80

                   ....*
gi 78194975    679 ASVLQ 683
Cdd:smart00838  81 KSIAE 85
EFG_mtEFG_C cd03713
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational ...
601-678 7.45e-35

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: 126.87  E-value: 7.45e-35
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78194975 601 EPLMDLEIITPTEYAGKVLGSVQQKRGRVEGIITQGNTEAIRALVPLAEMFGYMTELRSATKGRGGFTMEFSRFDQAP 678
Cdd:cd03713   1 EPIMKVEVTVPEEYMGDVIGDLSSRRGQILGTESRGGWKVIKAEVPLAEMFGYSTDLRSLTQGRGSFTMEFSHYEEVP 78
PRK10218 PRK10218
translational GTPase TypA;
6-504 1.44e-34

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 139.46  E-value: 1.44e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975    6 LDSIRNIGIISHIDAGKTTVSERILFYTGETHKIGEVHdgEAVMDWMPQEQERGITITSTATVCRWGAWWINLIDTPGHI 85
Cdd:PRK10218   2 IEKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQ--ERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   86 DFTIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRICFINKMDRVgadyretlrqmeeklGARPvllqlpv 165
Cdd:PRK10218  80 DFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRP---------------GARP------- 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  166 gveasfAGVVDLIAGEFLTFSEADqgstvERHPIPaeiageamAVREELIEAAADFDDAILADflegtaiaaeriraair 245
Cdd:PRK10218 138 ------DWVVDQVFDLFVNLDATD-----EQLDFP--------IVYASALNGIAGLDHEDMAE----------------- 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  246 kgtiacrivpvflgtalrnrGIQPLLDAVAAYLPSPrDIppvtgqrpdgeavdslpcDPAGPLcalafKVQADEGRKLTY 325
Cdd:PRK10218 182 --------------------DMTPLYQAIVDHVPAP-DV------------------DLDGPF-----QMQISQLDYNSY 217
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  326 L------RIYSGTVKAGGALWNSNRGCFEKAARLFRMHAH---KREPIDEALAGDIVAAIGLKEVLTGDTLCDPAHKVLL 396
Cdd:PRK10218 218 VgvigigRIKRGKVKPNQQVTIIDSEGKTRNAKVGKVLGHlglERIETDLAEAGDIVAITGLGELNISDTVCDTQNVEAL 297
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  397 SGLTVPEPVVAL----------AVEPRGVDDRdKLLPALEKLQWEDPTFRVHEDEETGQTILTGMGELHLEVVTDRLGRE 466
Cdd:PRK10218 298 PALSVDEPTVSMffcvntspfcGKEGKFVTSR-QILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRRE 376
                        490       500       510
                 ....*....|....*....|....*....|....*...
gi 78194975  467 fGVQVKTGRPQVVYRETITRPAERQEVFRTEFEGKVQG 504
Cdd:PRK10218 377 -GFELAVSRPKVIFREIDGRKQEPYENVTLDVEEQHQG 413
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
10-158 1.70e-33

LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.


Pssm-ID: 206677 [Multi-domain]  Cd Length: 179  Bit Score: 126.49  E-value: 1.70e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  10 RNIGIISHIDAGKTTVSERILFYTGethKIGEVHDGEAVMDWMPQEQERGITITSTATVCRWGA-----WWINLIDTPGH 84
Cdd:cd01890   1 RNFSIIAHIDHGKSTLADRLLELTG---TVSEREMKEQVLDSMDLERERGITIKAQAVRLFYKAkdgeeYLLNLIDTPGH 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78194975  85 IDFTIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRICFINKMDRVGADYRETLRQMEEKLGARP 158
Cdd:cd01890  78 VDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVKQEIEDVLGLDA 151
EFG_C pfam00679
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ...
599-684 1.22e-29

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: 112.25  E-value: 1.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   599 LLEPLMDLEIITPTEYAGKVLGSVQQKRGRVEGIITQGNTEA-IRALVPLAEMFGYMTELRSATKGRGGFTMEFSRFDQA 677
Cdd:pfam00679   2 LLEPIEKVTIDVPEEYVGDVISDLNSRRGEILDMDPDDGGRVvIEAEVPLAELFGFATELRSLTKGRGSFSMEFSGYQPV 81

                  ....*..
gi 78194975   678 PASVLQQ 684
Cdd:pfam00679  82 PGDILDR 88
Elongation_Factor_C cd01514
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ...
601-678 1.02e-26

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


Pssm-ID: 238772 [Multi-domain]  Cd Length: 79  Bit Score: 103.72  E-value: 1.02e-26
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78194975 601 EPLMDLEIITPTEYAGKVLGSVQQKRGRVEGIITQGNTEA-IRALVPLAEMFGYMTELRSATKGRGGFTMEFSRFDQAP 678
Cdd:cd01514   1 EPIMKVEITVPEEYLGAVIGDLSKRRGEILGMEPRGTGRVvIKAELPLAEMFGFATDLRSLTQGRASFSMEFSHYEPVP 79
mtEFG2_II_like cd04092
Domain II of mitochondrial elongation factor G2-like proteins found in eukaryotes; Eukaryotic ...
308-387 1.72e-23

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: 94.69  E-value: 1.72e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 308 LCALAFKVQADEGR-KLTYLRIYSGTVKAGGALWNSNRGCFEKAARLFRMHAHKREPIDEALAGDIVAAIGLKEVLTGDT 386
Cdd:cd04092   1 LCALAFKVIHDPQRgPLVFVRVYSGTLKAGSNVYNTTTGKKERISRLLKMHADQTEEVDSLSAGNIGVITGLKVTSTGDT 80

                .
gi 78194975 387 L 387
Cdd:cd04092  81 L 81
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
10-138 1.90e-23

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: 98.88  E-value: 1.90e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  10 RNIGIISHIDAGKTTVSERILFYTGEthKIGEVHDGEAVMDWMPQ---EQERGITITST-----ATVCRWGAWWINLIDT 81
Cdd:cd04167   1 RNVCIAGHLHHGKTSLLDMLIEQTHK--RTPSVKLGWKPLRYTDTrkdEQERGISIKSNpislvLEDSKGKSYLINIIDT 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 78194975  82 PGHIDFTIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRICFINKMDR 138
Cdd:cd04167  79 PGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDR 135
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
9-178 2.29e-23

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: 97.06  E-value: 2.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975     9 IRNIGIISHIDAGKTTVSERILFYTGETHKIGEvhdGEAVMDWMPQEQERGITITstatvcrwgawwINLIDTPGHIDF- 87
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYP---GTTRNYVTTVIEEDGKTYK------------FNLLDTAGQEDYd 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975    88 ------TIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADrYQVPRICFINKMDRVGADYRETLRQMEEKLGARPVlL 161
Cdd:TIGR00231  66 airrlyYPQVERSLRVFDIVILVLDVEEILEKQTKEIIHHAD-SGVPIILVGNKIDLKDADLKTHVASEFAKLNGEPI-I 143
                         170
                  ....*....|....*..
gi 78194975   162 QLPVGVEASFAGVVDLI 178
Cdd:TIGR00231 144 PLSAETGKNIDSAFKIV 160
mtEFG1_C cd04097
mtEFG1_C: C-terminus of mitochondrial Elongation factor G1 (mtEFG1)-like proteins found in ...
601-680 1.60e-22

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: 91.61  E-value: 1.60e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 601 EPLMDLEIITPTEYAGKVLGSVQQKRGRVEGIITQGNTEAIRALVPLAEMFGYMTELRSATKGRGGFTMEFSRFdqAPAS 680
Cdd:cd04097   1 EPIMKVEVTAPTEFQGNVIGLLNKRKGTIVDTDTGEDEFTLEAEVPLNDMFGYSTELRSMTQGKGEFSMEFSRY--APVP 78
EFG_IV smart00889
Elongation factor G, domain IV; Translation elongation factors are responsible for two main ...
477-593 6.06e-21

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: 88.76  E-value: 6.06e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975    477 QVVYRETITRPA-ERQEVFRTEFEGKVQGGEVHLRLAPLHRGEGVRIVVppaEVLG--ITRELHTALTESLTRGASTGCV 553
Cdd:smart00889   1 QVAYRETITKPVkEAEGKHKKQSGGDGQYARVILEVEPLERGSGFEFDD---TIVGgvIPKEYIPAVEKGFREALEEGPL 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 78194975    554 TGYPLTDLEVRVITVPVEQGVTTEGGVRAAAGRGLMRAAR 593
Cdd:smart00889  78 AGYPVVDVKVTLLDGSYHEVDSSEMAFKPAARRAFKEALL 117
mtEFG1_II_like cd04091
Domain II of mitochondrial elongation factor G1-like proteins found in eukaryotes; Eukaryotic ...
308-389 5.10e-18

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: 78.87  E-value: 5.10e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 308 LCALAFKVQADEGRKLTYLRIYSGTVKAGGALWNSNRGCFEKAARLFRMHAHKREPIDEALAGDIVAAIGLkEVLTGDTL 387
Cdd:cd04091   1 FVGLAFKLEEGRFGQLTYMRVYQGVLRKGDTIYNVRTGKKVRVPRLVRMHSDEMEDIEEVYAGDICALFGI-DCASGDTF 79

                ..
gi 78194975 388 CD 389
Cdd:cd04091  80 TD 81
EFG_III-like cd16257
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G ...
404-472 8.30e-17

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: 75.08  E-value: 8.30e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78194975 404 PVVALAVEPRGVDDRDKLLPALEKLQWEDPTFRVHEDEETGQTILTGMGELHLEVVTDRLGREFGVQVK 472
Cdd:cd16257   1 PVVFVTVEVKNPLDQEKLLEGLERLSEEDPALQVYREESTGEFILSGLGELHLEIIVARLEREYGVELV 69
EF2_snRNP_III cd16261
Domain III of Elongation Factor 2 (EF2); This model represents domain III of Elongation factor ...
404-474 6.19e-15

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: 69.91  E-value: 6.19e-15
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78194975 404 PVVALAVEPRGVDDRDKLLPALEKLQWEDPTFRVhEDEETGQTILTGMGELHLEVVTDRLGREF-GVQVKTG 474
Cdd:cd16261   1 PVVRVAVEPKNPSDLPKLVEGLKKLAKSDPTVQV-KIEEEGEHLIAGAGELHLEICLKDLKEDFaGIEIKVS 71
eEF2_snRNP_like_C cd04096
eEF2_snRNP_like_C: this family represents a C-terminal domain of eukaryotic elongation factor ...
601-675 3.93e-13

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: 64.87  E-value: 3.93e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78194975 601 EPLMDLEIITPTEYAGKVLGSVQQKRGRV--EGIITQGNTEAIRALVPLAEMFGYMTELRSATKGRGGFTMEFSRFD 675
Cdd:cd04096   1 EPIYLVEIQCPEDALGKVYSVLSKRRGHVlsEEPKEGTPLFEIKAYLPVIESFGFETDLRSATSGQAFPQLVFSHWE 77
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
11-154 4.12e-13

Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 444074 [Multi-domain]  Cd Length: 423  Bit Score: 71.89  E-value: 4.12e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  11 NIGIISHIDAGKTTVSERILFYTGE-THKIGEVHDGEA------------VMDWMPQEQERGITITSTATVCRWGAWWIN 77
Cdd:COG5256   9 NLVVIGHVDHGKSTLVGRLLYETGAiDEHIIEKYEEEAekkgkesfkfawVMDRLKEERERGVTIDLAHKKFETDKYYFT 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  78 LIDTPGHIDFTIEVERSLRALDGAVAIFSAVEGVQPQS-ESVW--RQADRYQVprICFINKMDRVGAD---YRETLRQME 151
Cdd:COG5256  89 IIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTrEHAFlaRTLGINQL--IVAVNKMDAVNYSekrYEEVKEEVS 166

                ...
gi 78194975 152 EKL 154
Cdd:COG5256 167 KLL 169
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
11-145 4.44e-12

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 68.41  E-value: 4.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   11 NIGIISHIDAGKTTVSERILFYTGET-HKIGEVHDGEA------------VMDWMPQEQERGITITSTATVCRWGAWWIN 77
Cdd:PRK12317   8 NLAVIGHVDHGKSTLVGRLLYETGAIdEHIIEELREEAkekgkesfkfawVMDRLKEERERGVTIDLAHKKFETDKYYFT 87
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 78194975   78 LIDTPGHIDFTIEVERSLRALDGAVAIFSA--VEGVQPQS-ESVW--RQADRYQVprICFINKMDRVgaDYRE 145
Cdd:PRK12317  88 IVDCPGHRDFVKNMITGASQADAAVLVVAAddAGGVMPQTrEHVFlaRTLGINQL--IVAINKMDAV--NYDE 156
PLN03127 PLN03127
Elongation factor Tu; Provisional
11-151 1.00e-11

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 67.54  E-value: 1.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   11 NIGIISHIDAGKTTVSERILFYTGETHKIGEVHDGEavMDWMPQEQERGITITST----ATVCRWGAWwinlIDTPGHID 86
Cdd:PLN03127  63 NVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDE--IDKAPEEKARGITIATAhveyETAKRHYAH----VDCPGHAD 136
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78194975   87 FTIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRI-CFINKMDRVGADYRETLRQME 151
Cdd:PLN03127 137 YVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLvVFLNKVDVVDDEELLELVEME 202
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
11-151 4.48e-11

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


Pssm-ID: 129576 [Multi-domain]  Cd Length: 394  Bit Score: 65.18  E-value: 4.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975    11 NIGIISHIDAGKTTVSERIlfytgeTHKIGEVHDGEAV----MDWMPQEQERGITItSTATV-----CRWGAWwinlIDT 81
Cdd:TIGR00485  14 NVGTIGHVDHGKTTLTAAI------TTVLAKEGGAAARaydqIDNAPEEKARGITI-NTAHVeyeteTRHYAH----VDC 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 78194975    82 PGHIDFTIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRI-CFINKMDRVGADYRETLRQME 151
Cdd:TIGR00485  83 PGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIvVFLNKCDMVDDEELLELVEME 153
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
323-388 5.59e-11

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: 58.82  E-value: 5.59e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 78194975   323 LTYLRIYSGTVKAGGALWNSN-----RGCFEKAARLFRMHAHKREPIDEALAGDIVAAIGLKEVLTGDTLC 388
Cdd:pfam03144   3 VATGRVESGTLKKGDKVRILPngtgkKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
11-139 7.19e-11

Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.


Pssm-ID: 206671 [Multi-domain]  Cd Length: 195  Bit Score: 61.83  E-value: 7.19e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  11 NIGIISHIDAGKTTVSERILFYTGETHKiGEVHDGEAVmDWMPQEQERGITItSTATV------CRWGAwwinlIDTPGH 84
Cdd:cd01884   4 NVGTIGHVDHGKTTLTAAITKVLAKKGG-AKAKKYDEI-DKAPEEKARGITI-NTAHVeyetanRHYAH-----VDCPGH 75
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 78194975  85 IDFTIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRI-CFINKMDRV 139
Cdd:cd01884  76 ADYIKNMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIvVFLNKADMV 131
BipA_TypA_II cd03691
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ...
327-392 2.61e-10

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: 57.58  E-value: 2.61e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78194975 327 RIYSGTVKAGGALWNSNRGCFEKAARLFRMHAH---KREPIDEALAGDIVAAIGLKEVLTGDTLCDPAH 392
Cdd:cd03691  21 RIFSGTVKVGQQVTVVDEDGKIEKGRVTKLFGFeglERVEVEEAEAGDIVAIAGLEDITIGDTICDPEV 89
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
11-146 4.21e-10

Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.


Pssm-ID: 206670 [Multi-domain]  Cd Length: 219  Bit Score: 60.20  E-value: 4.21e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  11 NIGIISHIDAGKTTVSERILFYTGETHK-IGEVHDGEA------------VMDWMPQEQERGITItstaTVCRW----GA 73
Cdd:cd01883   1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKrTIEKYEKEAkemgkesfkyawVLDKLKEERERGVTI----DVGLAkfetEK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  74 WWINLIDTPGHIDFTIEverslrALDGA----VAI---------FSAVEGVQPQS-ESVW--RQADRYQVprICFINKMD 137
Cdd:cd01883  77 YRFTIIDAPGHRDFVKN------MITGAsqadVAVlvvsarkgeFEAGFEKGGQTrEHALlaRTLGVKQL--IVAVNKMD 148

                ....*....
gi 78194975 138 RVGADYRET 146
Cdd:cd01883 149 DVTVNWSQE 157
Tet_C cd03711
Tet_C: C-terminus of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology ...
601-678 4.82e-10

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: 56.09  E-value: 4.82e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78194975 601 EPLMDLEIITPTEYAGKVLGSVQQKRGRVEGIITQGNTEAIRALVPLAEMFGYMTELRSATKGRGGFTMEFSRFDQAP 678
Cdd:cd03711   1 EPYLRFELEVPQDALGRAMSDLAKMGATFEDPQIKGDEVTLEGTIPVATSQDYQSELPSYTHGEGVLETEFKGYRPCH 78
EFG_IV pfam03764
Elongation factor G, domain IV; This domain is found in elongation factor G, elongation factor ...
476-595 6.13e-10

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: 57.23  E-value: 6.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   476 PQVVYRETITRPAE-RQEVFRTEFEGKVQGGEVHLRLAPLHRGEGVRIVvppAEVLG--ITRELHTALTESLTRGASTGC 552
Cdd:pfam03764   1 PQVAYRETIRKPVKeRAYKHKKQSGGDGQYARVILRIEPLPPGSGNEFV---DETVGgqIPKEFIPAVEKGFQEAMKEGP 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 78194975   553 VTGYPLTDLEVRVITVPVEQGVTTEGGVRAAAGRGLMRAARDG 595
Cdd:pfam03764  78 LAGEPVTDVKVTLLDGSYHEVDSSEAAFIPAARRAFREALLKA 120
PLN03126 PLN03126
Elongation factor Tu; Provisional
11-151 6.27e-10

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 61.94  E-value: 6.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   11 NIGIISHIDAGKTTVSERIlfytgeTHKIGEVHDGEAV----MDWMPQEQERGITItSTATV-----CRWGAWwinlIDT 81
Cdd:PLN03126  83 NIGTIGHVDHGKTTLTAAL------TMALASMGGSAPKkydeIDAAPEERARGITI-NTATVeyeteNRHYAH----VDC 151
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 78194975   82 PGHIDFTIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPR-ICFINKMDRVgaDYRETLRQME 151
Cdd:PLN03126 152 PGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNmVVFLNKQDQV--DDEELLELVE 220
lepA_C cd03709
lepA_C: This family represents the C-terminal region of LepA, a GTP-binding protein localized ...
601-677 8.00e-10

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: 55.58  E-value: 8.00e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 601 EPLMDLEIITPTEYAGKVLGSVQQKRGrvegiiTQGNTEAI---RALV----PLAEM-FGYMTELRSATKGRGGFTMEFS 672
Cdd:cd03709   1 EPFVKATIITPSEYLGAIMELCQERRG------VQKDMEYLdanRVMLtyelPLAEIvYDFFDKLKSISKGYASLDYELI 74

                ....*
gi 78194975 673 RFDQA 677
Cdd:cd03709  75 GYRES 79
Tet_II cd03690
Domain II of ribosomal protection proteins Tet(M) and Tet(O); This subfamily represents domain ...
306-387 8.47e-10

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: 55.71  E-value: 8.47e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 306 GPLCALAFKVQADE-GRKLTYLRIYSGTVKAGGALWNSNRGCFEKAARLFRMHAHKREPIDEALAGDIVAAIGLKEVLTG 384
Cdd:cd03690   2 SELSGTVFKIEYDPkGERLAYLRLYSGTLRLRDSVRVSGEEEKIKITELRTFENGELVKVDRVYAGDIAILVGLKSLRVG 81

                ...
gi 78194975 385 DTL 387
Cdd:cd03690  82 DVL 84
PRK12736 PRK12736
elongation factor Tu; Reviewed
11-151 9.43e-10

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 61.11  E-value: 9.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   11 NIGIISHIDAGKTTVSERIlfytgeTHKIGEVHDGEAV----MDWMPQEQERGITItSTA-----TVCRWGAWwinlIDT 81
Cdd:PRK12736  14 NIGTIGHVDHGKTTLTAAI------TKVLAERGLNQAKdydsIDAAPEEKERGITI-NTAhveyeTEKRHYAH----VDC 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 78194975   82 PGHIDFTIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRI-CFINKMDRVGADYRETLRQME 151
Cdd:PRK12736  83 PGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLvVFLNKVDLVDDEELLELVEME 153
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
308-388 2.45e-09

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: 54.19  E-value: 2.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 308 LCALAFKVQADEGR-KLTYLRIYSGTVKAGGALWNSNRGCFEKAARLFRMHahkrEPIDEALAGDIVA--AIGLKEVLTG 384
Cdd:cd01342   1 LVMQVFKVFYIPGRgRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFH----EEVDEAKAGDIVGigILGVKDILTG 76

                ....
gi 78194975 385 DTLC 388
Cdd:cd01342  77 DTLT 80
PRK12735 PRK12735
elongation factor Tu; Reviewed
11-139 4.05e-09

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 59.08  E-value: 4.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   11 NIGIISHIDAGKTTVSERIlfytgeTHKIGEVHDGEAV----MDWMPQEQERGITItSTA-----TVCRWGAwwinLIDT 81
Cdd:PRK12735  14 NVGTIGHVDHGKTTLTAAI------TKVLAKKGGGEAKaydqIDNAPEEKARGITI-NTShveyeTANRHYA----HVDC 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 78194975   82 PGHIDFTIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRI-CFINKMDRV 139
Cdd:PRK12735  83 PGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIvVFLNKCDMV 141
tufA CHL00071
elongation factor Tu
11-139 4.77e-09

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 58.82  E-value: 4.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   11 NIGIISHIDAGKTTVSERI-----LFYTGETHKIGEVhdgeavmDWMPQEQERGITItSTA-----TVCRWGAWwinlID 80
Cdd:CHL00071  14 NIGTIGHVDHGKTTLTAAItmtlaAKGGAKAKKYDEI-------DSAPEEKARGITI-NTAhveyeTENRHYAH----VD 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   81 TPGHIDFTIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRI-CFINKMDRV 139
Cdd:CHL00071  82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIvVFLNKEDQV 141
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
14-138 7.82e-09

Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.


Pssm-ID: 206674 [Multi-domain]  Cd Length: 169  Bit Score: 55.56  E-value: 7.82e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  14 IISHIDAGKTTvserILFYTGETHkigeVHDGEAvmdwmpqeqeRGITITSTATVCRWGAW--WINLIDTPGHIDFTiev 91
Cdd:cd01887   5 VMGHVDHGKTT----LLDKIRKTN----VAAGEA----------GGITQHIGAYQVPIDVKipGITFIDTPGHEAFT--- 63
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 78194975  92 erSLRALDGAVA-----IFSAVEGVQPQSESVWRQADRYQVPRICFINKMDR 138
Cdd:cd01887  64 --NMRARGASVTdiailVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDK 113
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
11-154 8.31e-09

SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.


Pssm-ID: 206676 [Multi-domain]  Cd Length: 192  Bit Score: 55.83  E-value: 8.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  11 NIGIISHIDAGKTTVSeRILFYTGEThkigevhdgeAVMDWMPQEQERGITIT---STATVCRWGAWW-----------I 76
Cdd:cd01889   2 NVGLLGHVDSGKTSLA-KALSEIAST----------AAFDKNPQSQERGITLDlgfSSFEVDKPKHLEdnenpqienyqI 70
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78194975  77 NLIDTPGHIDFTIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRICFINKMDRVGADYRE-TLRQMEEKL 154
Cdd:cd01889  71 TLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDLIPEEERKrKIEKMKKRL 149
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
11-139 1.35e-08

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


Pssm-ID: 439820 [Multi-domain]  Cd Length: 396  Bit Score: 57.47  E-value: 1.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  11 NIGIISHIDAGKTTVSERIlfytgeTHKIGEVHDGEAV----MDWMPQEQERGITItSTA-----TVCRWGAwwinLIDT 81
Cdd:COG0050  14 NIGTIGHVDHGKTTLTAAI------TKVLAKKGGAKAKaydqIDKAPEEKERGITI-NTShveyeTEKRHYA----HVDC 82
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 78194975  82 PGHIDFTIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRI-CFINKMDRV 139
Cdd:COG0050  83 PGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIvVFLNKCDMV 141
PRK00049 PRK00049
elongation factor Tu; Reviewed
11-139 1.90e-08

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 57.12  E-value: 1.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   11 NIGIISHIDAGKTTVSERILFYTGETHKiGEVHDGEAVmDWMPQEQERGITItSTA-----TVCRWGAwwinLIDTPGHI 85
Cdd:PRK00049  14 NVGTIGHVDHGKTTLTAAITKVLAKKGG-AEAKAYDQI-DKAPEEKARGITI-NTAhveyeTEKRHYA----HVDCPGHA 86
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 78194975   86 DFTIEVERSLRALDGAVAIFSAVEGVQPQS-ESVW--RQAdryQVPRI-CFINKMDRV 139
Cdd:PRK00049  87 DYVKNMITGAAQMDGAILVVSAADGPMPQTrEHILlaRQV---GVPYIvVFLNKCDMV 141
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
11-154 2.73e-08

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


Pssm-ID: 129567 [Multi-domain]  Cd Length: 581  Bit Score: 57.19  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975    11 NIGIISHIDAGKTTVSERIlfyTGEThkigevhdgeavMDWMPQEQERGITITSTATVCRWGAWWINLIDTPGHIDFTIE 90
Cdd:TIGR00475   2 IIATAGHVDHGKTTLLKAL---TGIA------------ADRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISN 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78194975    91 VERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPR-ICFINKMDRVG-ADYRETLRQMEEKL 154
Cdd:TIGR00475  67 AIAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHtIVVITKADRVNeEEIKRTEMFMKQIL 132
infB CHL00189
translation initiation factor 2; Provisional
2-155 5.58e-08

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 55.99  E-value: 5.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975    2 QHPPLdsirnIGIISHIDAGKTTVSERILFYT-------GETHKIG--EVhdgeavmDWMPQEQERGITitstatvcrwg 72
Cdd:CHL00189 242 NRPPI-----VTILGHVDHGKTTLLDKIRKTQiaqkeagGITQKIGayEV-------EFEYKDENQKIV----------- 298
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   73 awwinLIDTPGHIDFTIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRICFINKMDRVGADYrETLRQ--- 149
Cdd:CHL00189 299 -----FLDTPGHEAFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANT-ERIKQqla 372
                        170
                 ....*....|
gi 78194975  150 ----MEEKLG 155
Cdd:CHL00189 373 kynlIPEKWG 382
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
12-157 6.03e-08

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: 52.99  E-value: 6.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  12 IGIISHIDAGKTTVSERIlfyTG-EThkigevhdgeavmDWMPQEQERGITITstatvcrWGAWWINL--------IDTP 82
Cdd:cd04171   2 IGTAGHIDHGKTTLIKAL---TGiET-------------DRLPEEKKRGITID-------LGFAYLDLpdgkrlgfIDVP 58
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78194975  83 GHIDFTIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPR-ICFINKMDRVGADyreTLRQMEEKLGAR 157
Cdd:cd04171  59 GHEKFVKNMLAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKgLVVLTKADLVDED---RLELVEEEILEL 131
EFG_mtEFG1_IV cd01434
EFG_mtEFG1_IV: domains similar to domain IV of the bacterial translational elongation factor ...
480-566 8.86e-08

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: 50.90  E-value: 8.86e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 480 YRETITRPAERQEVFRTEFEGKVQGGEVHLRLAPLHRGEGVRIVvppAEVLG--ITRELHTALTESLTRGASTGCVTGYP 557
Cdd:cd01434   1 YRETITKPAEFEYRHKKQSGGAGQYGHVVLEIEPLPRGSGFEFV---NKIVGgaIPKEYIPAVEKGFREALEKGPLAGYP 77

                ....*....
gi 78194975 558 LTDLEVRVI 566
Cdd:cd01434  78 VVDVKVTLY 86
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
11-145 1.08e-05

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 48.59  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   11 NIGIISHIDAGKTTVSERILFYTG------------ETHKIGEVHDGEA-VMDWMPQEQERGITITSTATVCRWGAWWIN 77
Cdd:PTZ00141   9 NLVVIGHVDSGKSTTTGHLIYKCGgidkrtiekfekEAAEMGKGSFKYAwVLDKLKAERERGITIDIALWKFETPKYYFT 88
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78194975   78 LIDTPGHIDF-------TIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPR-ICFINKMDRVGADYRE 145
Cdd:PTZ00141  89 IIDAPGHRDFiknmitgTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQmIVCINKMDDKTVNYSQ 164
EF4_III cd16260
Domain III of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly ...
404-471 1.44e-05

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: 43.64  E-value: 1.44e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 78194975 404 PVVALAVEPRGVDDRDKLLPALEKLQWEDPTFRVHEdeETGQTILTG-----MGELHLEVVTDRLGREFGVQV 471
Cdd:cd16260   1 PMVFAGLYPVDGSDYEELRDALEKLTLNDASVTFEP--ETSSALGFGfrcgfLGLLHMEVFQERLEREYGLDL 71
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
11-143 1.72e-05

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 47.78  E-value: 1.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975   11 NIGIISHIDAGKTTVSERILFYTGETHK-IGEVHDGEA------------VMDWMPQEQERGITITSTATVCRWGAWWIN 77
Cdd:PLN00043   9 NIVVIGHVDSGKSTTTGHLIYKLGGIDKrVIERFEKEAaemnkrsfkyawVLDKLKAERERGITIDIALWKFETTKYYCT 88
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78194975   78 LIDTPGHIDFTIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQV--------PRICFINKMDRVGADY 143
Cdd:PLN00043  89 VIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALlaftlgvkQMICCCNKMDATTPKY 162
Tet_III cd16258
Domain III of Tetracycline resistance protein Tet; Tetracycline resistance proteins, including ...
404-471 1.77e-05

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: 43.09  E-value: 1.77e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78194975 404 PVVALAVEPRGVDDRDKLLPALEKLQWEDPTFRVHEDEETGQTILTGMGELHLEVVTDRLGREFGVQV 471
Cdd:cd16258   1 PMLQTTIRPRKPEQRERLLDALTELSDEDPLLKYRVDSTTHEIILSLYGEVQMEVISALLEEKYGVEV 68
eEF2_C_snRNP cd04098
eEF2_C_snRNP: This family includes a C-terminal portion of the spliceosomal human 116kD U5 ...
601-678 4.81e-05

eEF2_C_snRNP: This family includes a C-terminal portion of the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and, its yeast counterpart Snu114p. This domain is homologous to the C-terminal domain of the eukaryotic translational elongation factor EF-2. 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: 239765 [Multi-domain]  Cd Length: 80  Bit Score: 42.23  E-value: 4.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 601 EPLMDLEIITPTEYAGKVLGSVQQKRGRVEG-IITQGNT-EAIRALVPLAEMFGYMTELRSATKGRGGFTMEFSRFDQAP 678
Cdd:cd04098   1 EPIYEVEITCPADAVSAVYEVLSRRRGHVIYdTPIPGTPlYEVKAFIPVIESFGFETDLRVHTQGQAFCQSVFDHWQIVP 80
Tet_like_IV cd01684
EF-G_domain IV_RPP domain is a part of bacterial ribosomal protected proteins (RPP) family. ...
478-593 2.90e-04

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: 40.73  E-value: 2.90e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 478 VVYRETITRPAERQEVFrtEFEGKVQGGEVHLRLAPLHRGEGVRIVvppAEV-LG-ITRELHTALTESLTRGASTGcVTG 555
Cdd:cd01684   1 VIYKERPLGTGEGVEHI--EVPPNPFWATVGLRVEPLPRGSGLQYE---SEVsLGsLPRSFQNAVEETVRETLQQG-LYG 74
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 78194975 556 YPLTDLEVRVITVPVEQGVTTEGGVRAAAGRGLMRAAR 593
Cdd:cd01684  75 WEVTDCKVTLTYGRYHSPVSTAADFRELTPRVLRQALK 112
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
17-159 3.00e-04

CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN.


Pssm-ID: 206729 [Multi-domain]  Cd Length: 209  Bit Score: 42.56  E-value: 3.00e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  17 HIDAGKTTVSERILFYTG-------ETHKIGEVHDGEA-------VMDWMPQEQERGITITST----ATVCRWgawWInL 78
Cdd:cd04166   7 SVDDGKSTLIGRLLYDSKsifedqlAALERSKSSGTQGekldlalLVDGLQAEREQGITIDVAyryfSTPKRK---FI-I 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  79 IDTPGHIDFTIEVERSLRALDGAVAIFSAVEGVQPQSESVWRQADRYQVPRICF-INKMDRVG----------ADYRETL 147
Cdd:cd04166  83 ADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVaVNKMDLVDydeevfeeikADYLAFA 162
                       170
                ....*....|..
gi 78194975 148 rqmeEKLGARPV 159
Cdd:cd04166 163 ----ASLGIEDI 170
PRK04004 PRK04004
translation initiation factor IF-2; Validated
79-139 4.62e-04

translation initiation factor IF-2; Validated


Pssm-ID: 235195 [Multi-domain]  Cd Length: 586  Bit Score: 43.24  E-value: 4.62e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78194975   79 IDTPGHIDFTieverSLRALDGAVA-----IFSAVEGVQPQSESVWRQADRYQVPRICFINKMDRV 139
Cdd:PRK04004  76 IDTPGHEAFT-----NLRKRGGALAdiailVVDINEGFQPQTIEAINILKRRKTPFVVAANKIDRI 136
EF2_II cd16268
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 ...
327-389 1.12e-03

Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 (EF-2) found in eukaryotes and archaea. 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.


Pssm-ID: 293913 [Multi-domain]  Cd Length: 96  Bit Score: 38.74  E-value: 1.12e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78194975 327 RIYSGTVKAGGALW--------NSNRGCFEKAA-RLFRMHAHKREPIDEALAGDIVAAIGLKEVL--TGDTLCD 389
Cdd:cd16268  23 RVFSGTVRRGQEVYilgpkyvpGKKDDLKKKRIqQTYLMMGREREPVDEVPAGNIVGLVGLDDFLakSGTTTSS 96
PRK14845 PRK14845
translation initiation factor IF-2; Provisional
79-139 1.18e-03

translation initiation factor IF-2; Provisional


Pssm-ID: 237833 [Multi-domain]  Cd Length: 1049  Bit Score: 42.18  E-value: 1.18e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78194975    79 IDTPGHIDFTieverSLRALDGAVAIFSAV-----EGVQPQSESVWRQADRYQVPRICFINKMDRV 139
Cdd:PRK14845  531 IDTPGHEAFT-----SLRKRGGSLADLAVLvvdinEGFKPQTIEAINILRQYKTPFVVAANKIDLI 591
mtEFG2_like_IV cd01693
mtEF-G2 domain IV. This subfamily is a part the of mitochondrial transcriptional elongation ...
478-591 1.25e-03

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: 39.30  E-value: 1.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 478 VVYRETITRPAerQEVFRTEFE--GKVQGGEVHLRLAPL--HRGEGVRIVVPPAEVLGITRELHTALTESLTRGASTGCV 553
Cdd:cd01693   1 IAYRETILEPA--RATDTLEKVigDKKHSVTVTMEVRPNqaSSSPVELIELANSAIEVLLKRIQEAVENGVHSALLQGPL 78
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 78194975 554 TGYPLTDLEVRVITVPVEQGvTTEGGVRAAAGRGLMRA 591
Cdd:cd01693  79 LGFPVQDVAITLHSLTIGPG-TSPTMISACASQCVQKA 115
RF3_II cd03689
Domain II of bacterial Release Factor 3; This subfamily represents domain II of bacterial ...
310-388 2.18e-03

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


Pssm-ID: 293890 [Multi-domain]  Cd Length: 87  Bit Score: 37.64  E-value: 2.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975 310 ALAFKVQADEGRK----LTYLRIYSGTVKAGGALWNSNRGCFEKAARLFRMHAHKREPIDEALAGDIVAAIGLKEVLTGD 385
Cdd:cd03689   3 GFVFKIQANMDPKhrdrIAFLRVCSGKFERGMKVKHVRTGKEVRLSNATTFMAQDRETVEEAYPGDIIGLPNHGTFQIGD 82

                ...
gi 78194975 386 TLC 388
Cdd:cd03689  83 TFT 85
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
19-154 2.47e-03

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


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 39.36  E-value: 2.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  19 DAGKTTVSERILfytgeTHKIGEVHDgeavmdwmpqeqERGITITSTATVCRWGAWW--INLIDTPGHIDF-----TIEV 91
Cdd:cd00882   7 GVGKSSLLNALL-----GGEVGEVSD------------VPGTTRDPDVYVKELDKGKvkLVLVDTPGLDEFgglgrEELA 69
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78194975  92 ERSLRALDGAVAIFSAVEG--VQPQSESVWRQADRYQVPRICFINKMDRVGADYRETLRQMEEKL 154
Cdd:cd00882  70 RLLLRGADLILLVVDSTDResEEDAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELA 134
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
17-142 3.87e-03

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


Pssm-ID: 440298 [Multi-domain]  Cd Length: 502  Bit Score: 40.38  E-value: 3.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  17 HIDAGKTTvserILFYTGETHkigeVHDGEAvmdwmpqeqeRGIT--ItstatvcrwGAW-------WINLIDTPGHIDF 87
Cdd:COG0532  12 HVDHGKTS----LLDAIRKTN----VAAGEA----------GGITqhI---------GAYqvetnggKITFLDTPGHEAF 64
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  88 TieverSLRAL-----DGAVAIFSAVEGVQPQSESVWRQADRYQVPRICFINKMDRVGAD 142
Cdd:COG0532  65 T-----AMRARgaqvtDIVILVVAADDGVMPQTIEAINHAKAAGVPIIVAINKIDKPGAN 119
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
59-135 4.09e-03

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 37.60  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975    59 GITITSTATVCRWGAWWINLIDTPGHIDFTIE---VERSLRAL---DGAVAIFSAVEGVQPQSESVWRQADRYQVPRICF 132
Cdd:pfam01926  31 GTTRDPNEGRLELKGKQIILVDTPGLIEGASEgegLGRAFLAIieaDLILFVVDSEEGITPLDEELLELLRENKKPIILV 110

                  ...
gi 78194975   133 INK 135
Cdd:pfam01926 111 LNK 113
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
20-181 7.23e-03

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 38.04  E-value: 7.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  20 AGKTTVSERILFytgethkigevhdgeavmDWMPQEQE---RGITITSTATVCRWGAWWINLIDTPGHIDFTIEVERSLR 96
Cdd:COG1100  14 VGKTSLVNRLVG------------------DIFSLEKYlstNGVTIDKKELKLDGLDVDLVIWDTPGQDEFRETRQFYAR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  97 ALDGA-VAIFsAVEGVQP---QSESVWRQADRY---QVPRICFINKMDRVGADYRETLRQMEEKLGARPVLLQLPV---- 165
Cdd:COG1100  76 QLTGAsLYLF-VVDGTREetlQSLYELLESLRRlgkKSPIILVLNKIDLYDEEEIEDEERLKEALSEDNIVEVVATsakt 154
                       170
                ....*....|....*...
gi 78194975 166 --GVEASFAGVVDLIAGE 181
Cdd:COG1100 155 geGVEELFAALAEILRGE 172
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
76-154 8.65e-03

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 37.61  E-value: 8.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78194975  76 INLIDTPGhIDFTIE-----VERSLRALDGA-VAIFsAVEGVQPQSESVWRQAD--RYQVPRICFINKMDRVGADYRETL 147
Cdd:cd00880  48 VVLIDTPG-LDEEGGlgrerVEEARQVADRAdLVLL-VVDSDLTPVEEEAKLGLlrERGKPVLLVLNKIDLVPESEEEEL 125

                ....*..
gi 78194975 148 RQMEEKL 154
Cdd:cd00880 126 LRERKLE 132
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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