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Conserved domains on  [gi|1021452772|gb|ANA43489|]
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elongation factor G [Borrelia hermsii HS1]

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;
1-669 0e+00

elongation factor G-like protein;


:

Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 1007.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   1 MEIRNIGIMAHIDAGKTTTTERIIYYTGKTHKIGDVDSGNTVTDWMTQEQDRGITISSAAITCYWKDHQINIIDTPGHVD 80
Cdd:PRK13351    6 MQIRNIGILAHIDAGKTTLTERILFYTGKIHKMGEVEDGTTVTDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHID 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  81 FTAEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYVNKMDRVGANFFKVVEDIRNKFGIVPIVLQIPIG 160
Cdd:PRK13351   86 FTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLFKVLEDIEERFGKRPLPLQLPIG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 161 SENNFEGVIDIIRNKELHFELRDGKPIVLEDVVREEFVENVKIFKENLIDSLSNFSERITELFLENSVIDDSLIIEEIRR 240
Cdd:PRK13351  166 SEDGFEGVVDLITEPELHFSEGDGGSTVEEGPIPEELLEEVEEAREKLIEALAEFDDELLELYLEGEELSAEQLRAPLRE 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 241 CTISGFIIPVLMGTSLKNIGIEPLIDAIVDYLPSPFEKKINAYSLKTDRSVSIEPKDEKRLSALVFKVQYFSAIaAHLYF 320
Cdd:PRK13351  246 GTRSGHLVPVLFGSALKNIGIEPLLDAVVDYLPSPLEVPPPRGSKDNGKPVKVDPDPEKPLLALVFKVQYDPYA-GKLTY 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 321 IRVYSGELSSSKRVLNIAKNKREKFTRIFRVFSNKNEQIDEVKAGDIGAVIGLKYSITGDTLVEEGNEIMLEPLVFPEPV 400
Cdd:PRK13351  325 LRVYSGTLRAGSQLYNGTGGKREKVGRLFRLQGNKREEVDRAKAGDIVAVAGLKELETGDTLHDSADPVLLELLTFPEPV 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 401 VLISIEPERASDDGRLKEVLEIITKEDPTFSYKESKETGQLLVSGMGELHLEIIVMRIRDDFKLNVYTGKPQVSYRESLS 480
Cdd:PRK13351  405 VSLAVEPERRGDEQKLAEALEKLVWEDPSLRVEEDEETGQTILSGMGELHLEVALERLRREFKLEVNTGKPQVAYRETIR 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 481 VTVNDVFEFVNMFAGKELNLKIGMIVSPLMRGEGnKIEFECNVE----PLFKAAILRGITSSFSSGII-GYPIIDVGVKI 555
Cdd:PRK13351  485 KMAEGVYRHKKQFGGKGQFGEVHLRVEPLERGAG-FIFVSKVVGgaipEELIPAVEKGIREALASGPLaGYPVTDLRVTV 563
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 556 TSLDYDKSKVNESVIESIAGLAFNEFFKRANPIKLEPIMILEIRTPIEYTGEVVSTLNFVGGMIHSISNIEDYEI-IKAE 634
Cdd:PRK13351  564 LDGKYHPVDSSESAFKAAARKAFLEAFRKANPVLLEPIMELEITVPTEHVGDVLGDLSQRRGRIEGTEPRGDGEVlVKAE 643
                         650       660       670
                  ....*....|....*....|....*....|....*
gi 1021452772 635 AAFEKLFGYTSILRSATKGRGVFTMEFSYFKEKCE 669
Cdd:PRK13351  644 APLAELFGYATRLRSMTKGRGSFTMEFSHFDPVPP 678
 
Name Accession Description Interval E-value
PRK13351 PRK13351
elongation factor G-like protein;
1-669 0e+00

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 1007.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   1 MEIRNIGIMAHIDAGKTTTTERIIYYTGKTHKIGDVDSGNTVTDWMTQEQDRGITISSAAITCYWKDHQINIIDTPGHVD 80
Cdd:PRK13351    6 MQIRNIGILAHIDAGKTTLTERILFYTGKIHKMGEVEDGTTVTDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHID 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  81 FTAEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYVNKMDRVGANFFKVVEDIRNKFGIVPIVLQIPIG 160
Cdd:PRK13351   86 FTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLFKVLEDIEERFGKRPLPLQLPIG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 161 SENNFEGVIDIIRNKELHFELRDGKPIVLEDVVREEFVENVKIFKENLIDSLSNFSERITELFLENSVIDDSLIIEEIRR 240
Cdd:PRK13351  166 SEDGFEGVVDLITEPELHFSEGDGGSTVEEGPIPEELLEEVEEAREKLIEALAEFDDELLELYLEGEELSAEQLRAPLRE 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 241 CTISGFIIPVLMGTSLKNIGIEPLIDAIVDYLPSPFEKKINAYSLKTDRSVSIEPKDEKRLSALVFKVQYFSAIaAHLYF 320
Cdd:PRK13351  246 GTRSGHLVPVLFGSALKNIGIEPLLDAVVDYLPSPLEVPPPRGSKDNGKPVKVDPDPEKPLLALVFKVQYDPYA-GKLTY 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 321 IRVYSGELSSSKRVLNIAKNKREKFTRIFRVFSNKNEQIDEVKAGDIGAVIGLKYSITGDTLVEEGNEIMLEPLVFPEPV 400
Cdd:PRK13351  325 LRVYSGTLRAGSQLYNGTGGKREKVGRLFRLQGNKREEVDRAKAGDIVAVAGLKELETGDTLHDSADPVLLELLTFPEPV 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 401 VLISIEPERASDDGRLKEVLEIITKEDPTFSYKESKETGQLLVSGMGELHLEIIVMRIRDDFKLNVYTGKPQVSYRESLS 480
Cdd:PRK13351  405 VSLAVEPERRGDEQKLAEALEKLVWEDPSLRVEEDEETGQTILSGMGELHLEVALERLRREFKLEVNTGKPQVAYRETIR 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 481 VTVNDVFEFVNMFAGKELNLKIGMIVSPLMRGEGnKIEFECNVE----PLFKAAILRGITSSFSSGII-GYPIIDVGVKI 555
Cdd:PRK13351  485 KMAEGVYRHKKQFGGKGQFGEVHLRVEPLERGAG-FIFVSKVVGgaipEELIPAVEKGIREALASGPLaGYPVTDLRVTV 563
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 556 TSLDYDKSKVNESVIESIAGLAFNEFFKRANPIKLEPIMILEIRTPIEYTGEVVSTLNFVGGMIHSISNIEDYEI-IKAE 634
Cdd:PRK13351  564 LDGKYHPVDSSESAFKAAARKAFLEAFRKANPVLLEPIMELEITVPTEHVGDVLGDLSQRRGRIEGTEPRGDGEVlVKAE 643
                         650       660       670
                  ....*....|....*....|....*....|....*
gi 1021452772 635 AAFEKLFGYTSILRSATKGRGVFTMEFSYFKEKCE 669
Cdd:PRK13351  644 APLAELFGYATRLRSMTKGRGSFTMEFSHFDPVPP 678
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
3-666 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: 768.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   3 IRNIGIMAHIDAGKTTTTERIIYYTGKTHKIGDVDSGNTVTDWMTQEQDRGITISSAAITCYWKDHQINIIDTPGHVDFT 82
Cdd:COG0480     9 IRNIGIVAHIDAGKTTLTERILFYTGAIHRIGEVHDGNTVMDWMPEEQERGITITSAATTCEWKGHKINIIDTPGHVDFT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  83 AEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYVNKMDRVGANFFKVVEDIRNKFGIVPIVLQIPIGSE 162
Cdd:COG0480    89 GEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQLKERLGANPVPLQLPIGAE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 163 NNFEGVIDIIRNKELHFELRDGKPIVLEDvVREEFVENVKIFKENLIDSLSNFSERITELFLENSVIDDSLIIEEIRRCT 242
Cdd:COG0480   169 DDFKGVIDLVTMKAYVYDDELGAKYEEEE-IPAELKEEAEEAREELIEAVAETDDELMEKYLEGEELTEEEIKAGLRKAT 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 243 ISGFIIPVLMGTSLKNIGIEPLIDAIVDYLPSPFEKK-INAYSLKTDRSVSIEPKDEKRLSALVFKVQY--FsaiAAHLY 319
Cdd:COG0480   248 LAGKIVPVLCGSAFKNKGVQPLLDAVVDYLPSPLDVPaIKGVDPDTGEEVERKPDDDEPFSALVFKTMTdpF---VGKLS 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 320 FIRVYSGELSSSKRVLNIAKNKREKFTRIFRVFSNKNEQIDEVKAGDIGAVIGLKYSITGDTLVEEGNEIMLEPLVFPEP 399
Cdd:COG0480   325 FFRVYSGTLKSGSTVYNSTKGKKERIGRLLRMHGNKREEVDEAGAGDIVAVVKLKDTTTGDTLCDEDHPIVLEPIEFPEP 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 400 VVLISIEPERASDDGRLKEVLEIITKEDPTFSYKESKETGQLLVSGMGELHLEIIVMRIRDDFKLNVYTGKPQVSYRESL 479
Cdd:COG0480   405 VISVAIEPKTKADEDKLSTALAKLAEEDPTFRVETDEETGQTIISGMGELHLEIIVDRLKREFGVEVNVGKPQVAYRETI 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 480 SVTVN----------------DVFefvnmfagkelnlkigMIVSPLMRGEGnkIEFECNV-------EplFKAAILRGIT 536
Cdd:COG0480   485 RKKAEaegkhkkqsgghgqygDVW----------------IEIEPLPRGEG--FEFVDKIvggvipkE--YIPAVEKGIR 544
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 537 SSFSSGII-GYPIIDVGVKItsldYDKS-----------KvnesviesIAG-LAFNEFFKRANPIKLEPIMILEIRTPIE 603
Cdd:COG0480   545 EAMEKGVLaGYPVVDVKVTL----YDGSyhpvdssemafK--------IAAsMAFKEAAKKAKPVLLEPIMKVEVTVPEE 612
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1021452772 604 YTGEVVSTLNFVGGMIHSISNIEDYEIIKAEAAFEKLFGYTSILRSATKGRGVFTMEFSYFKE 666
Cdd:COG0480   613 YMGDVMGDLNSRRGRILGMESRGGAQVIKAEVPLAEMFGYATDLRSLTQGRGSFTMEFSHYEE 675
EF-G TIGR00484
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ...
3-666 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: 652.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   3 IRNIGIMAHIDAGKTTTTERIIYYTGKTHKIGDVDSGNTVTDWMTQEQDRGITISSAAITCYWKDHQINIIDTPGHVDFT 82
Cdd:TIGR00484  10 FRNIGISAHIDAGKTTTTERILFYTGRIHKIGEVHDGAATMDWMEQEKERGITITSAATTVFWKGHRINIIDTPGHVDFT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  83 AEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYVNKMDRVGANFFKVVEDIRNKFGIVPIVLQIPIGSE 162
Cdd:TIGR00484  90 VEVERSLRVLDGAVAVLDAVGGVQPQSETVWRQANRYEVPRIAFVNKMDKTGANFLRVVNQIKQRLGANAVPIQLPIGAE 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 163 NNFEGVIDIIRNKELHFELRDGKPIVLEDvVREEFVENVKIFKENLIDSLSNFSERITELFLENSVIDDSLIIEEIRRCT 242
Cdd:TIGR00484 170 DNFIGVIDLVEMKAYFFNGDKGTKAIEKE-IPSDLLEQAKELRENLVEAVAEFDEELMEKYLEGEELTIEEIKNAIRKGV 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 243 ISGFIIPVLMGTSLKNIGIEPLIDAIVDYLPSPFE-KKINAYSLKTDRSVSIEPKDEKRLSALVFKVQYfSAIAAHLYFI 321
Cdd:TIGR00484 249 LNCEFFPVLCGSAFKNKGVQLLLDAVVDYLPSPTDvPAIKGIDPDTEKEIERKASDDEPFSALAFKVAT-DPFVGQLTFV 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 322 RVYSGELSSSKRVLNIAKNKREKFTRIFRVFSNKNEQIDEVKAGDIGAVIGLKYSITGDTLVEEGNEIMLEPLVFPEPVV 401
Cdd:TIGR00484 328 RVYSGVLKSGSYVKNSRKNKKERVGRLVKMHANNREEIKEVRAGDICAAIGLKDTTTGDTLCDPKIDVILERMEFPEPVI 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 402 LISIEPERASDDGRLKEVLEIITKEDPTFSYKESKETGQLLVSGMGELHLEIIVMRIRDDFKLNVYTGKPQVSYRESLSV 481
Cdd:TIGR00484 408 SLAVEPKTKADQEKMGIALGKLAEEDPTFRTFTDPETGQTIIAGMGELHLDIIVDRMKREFKVEANVGAPQVAYRETIRS 487
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 482 TVNDVFEFVNMFAGKElnlKIGMIVSPLMRGEGNKIEFE----CNVEPL-FKAAILRGITSSFSSG-IIGYPIIDVGVKI 555
Cdd:TIGR00484 488 KVEVEGKHAKQSGGRG---QYGHVKIRFEPLEPKGYEFVneikGGVIPReYIPAVDKGLQEAMESGpLAGYPVVDIKATL 564
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 556 TSLDYDKSKVNESVIESIAGLAFNEFFKRANPIKLEPIMILEIRTPIEYTGEVVSTLNFVGGMIHSISNIEDYEIIKAEA 635
Cdd:TIGR00484 565 FDGSYHDVDSSEMAFKLAASLAFKEAGKKANPVLLEPIMKVEVEVPEEYMGDVMGDLSSRRGIIEGMEARGNVQKIKAEV 644
                         650       660       670
                  ....*....|....*....|....*....|.
gi 1021452772 636 AFEKLFGYTSILRSATKGRGVFTMEFSYFKE 666
Cdd:TIGR00484 645 PLSEMFGYATDLRSFTQGRGTYSMEFLHYGE 675
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
5-275 1.04e-164

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: 472.75  E-value: 1.04e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   5 NIGIMAHIDAGKTTTTERIIYYTGKTHKIGDVDSGNTVTDWMTQEQDRGITISSAAITCYWKDHQINIIDTPGHVDFTAE 84
Cdd:cd01886     1 NIGIIAHIDAGKTTTTERILYYTGRIHKIGEVHGGGATMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDFTIE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  85 VERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYVNKMDRVGANFFKVVEDIRNKFGIVPIVLQIPIGSENN 164
Cdd:cd01886    81 VERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQIREKLGANPVPLQLPIGAEDD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 165 FEGVIDIIRNKELHFELRDGKPIVLEDvVREEFVENVKIFKENLIDSLSNFSERITELFLENSVIDDSLIIEEIRRCTIS 244
Cdd:cd01886   161 FEGVVDLIEMKALYWDGELGEKIEETD-IPEDLLEEAEEAREELIETLAEVDDELMEKYLEGEEITEEEIKAAIRKGTIA 239
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1021452772 245 GFIIPVLMGTSLKNIGIEPLIDAIVDYLPSP 275
Cdd:cd01886   240 NKIVPVLCGSAFKNKGVQPLLDAVVDYLPSP 270
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
2-148 1.54e-71

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: 229.72  E-value: 1.54e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   2 EIRNIGIMAHIDAGKTTTTERIIYYTGKTHKIGDVD-SGNTVTDWMTQEQDRGITISSAAITCYWKDHQINIIDTPGHVD 80
Cdd:pfam00009   2 RHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKgEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVD 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021452772  81 FTAEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYVNKMDRV-GANFFKVVEDIRNKF 148
Cdd:pfam00009  82 FVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVdGAELEEVVEEVSREL 150
EFG_C smart00838
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ...
590-666 5.15e-19

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: 81.78  E-value: 5.15e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1021452772  590 LEPIMILEIRTPIEYTGEVVSTLNFVGGMIHSISNIEDYEIIKAEAAFEKLFGYTSILRSATKGRGVFTMEFSYFKE 666
Cdd:smart00838   2 LEPIMKVEVTVPEEYMGDVIGDLNSRRGKIEGMEQRGGAQVIKAKVPLSEMFGYATDLRSATQGRATWSMEFSHYEE 78
 
Name Accession Description Interval E-value
PRK13351 PRK13351
elongation factor G-like protein;
1-669 0e+00

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 1007.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   1 MEIRNIGIMAHIDAGKTTTTERIIYYTGKTHKIGDVDSGNTVTDWMTQEQDRGITISSAAITCYWKDHQINIIDTPGHVD 80
Cdd:PRK13351    6 MQIRNIGILAHIDAGKTTLTERILFYTGKIHKMGEVEDGTTVTDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHID 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  81 FTAEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYVNKMDRVGANFFKVVEDIRNKFGIVPIVLQIPIG 160
Cdd:PRK13351   86 FTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLFKVLEDIEERFGKRPLPLQLPIG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 161 SENNFEGVIDIIRNKELHFELRDGKPIVLEDVVREEFVENVKIFKENLIDSLSNFSERITELFLENSVIDDSLIIEEIRR 240
Cdd:PRK13351  166 SEDGFEGVVDLITEPELHFSEGDGGSTVEEGPIPEELLEEVEEAREKLIEALAEFDDELLELYLEGEELSAEQLRAPLRE 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 241 CTISGFIIPVLMGTSLKNIGIEPLIDAIVDYLPSPFEKKINAYSLKTDRSVSIEPKDEKRLSALVFKVQYFSAIaAHLYF 320
Cdd:PRK13351  246 GTRSGHLVPVLFGSALKNIGIEPLLDAVVDYLPSPLEVPPPRGSKDNGKPVKVDPDPEKPLLALVFKVQYDPYA-GKLTY 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 321 IRVYSGELSSSKRVLNIAKNKREKFTRIFRVFSNKNEQIDEVKAGDIGAVIGLKYSITGDTLVEEGNEIMLEPLVFPEPV 400
Cdd:PRK13351  325 LRVYSGTLRAGSQLYNGTGGKREKVGRLFRLQGNKREEVDRAKAGDIVAVAGLKELETGDTLHDSADPVLLELLTFPEPV 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 401 VLISIEPERASDDGRLKEVLEIITKEDPTFSYKESKETGQLLVSGMGELHLEIIVMRIRDDFKLNVYTGKPQVSYRESLS 480
Cdd:PRK13351  405 VSLAVEPERRGDEQKLAEALEKLVWEDPSLRVEEDEETGQTILSGMGELHLEVALERLRREFKLEVNTGKPQVAYRETIR 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 481 VTVNDVFEFVNMFAGKELNLKIGMIVSPLMRGEGnKIEFECNVE----PLFKAAILRGITSSFSSGII-GYPIIDVGVKI 555
Cdd:PRK13351  485 KMAEGVYRHKKQFGGKGQFGEVHLRVEPLERGAG-FIFVSKVVGgaipEELIPAVEKGIREALASGPLaGYPVTDLRVTV 563
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 556 TSLDYDKSKVNESVIESIAGLAFNEFFKRANPIKLEPIMILEIRTPIEYTGEVVSTLNFVGGMIHSISNIEDYEI-IKAE 634
Cdd:PRK13351  564 LDGKYHPVDSSESAFKAAARKAFLEAFRKANPVLLEPIMELEITVPTEHVGDVLGDLSQRRGRIEGTEPRGDGEVlVKAE 643
                         650       660       670
                  ....*....|....*....|....*....|....*
gi 1021452772 635 AAFEKLFGYTSILRSATKGRGVFTMEFSYFKEKCE 669
Cdd:PRK13351  644 APLAELFGYATRLRSMTKGRGSFTMEFSHFDPVPP 678
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
3-666 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: 768.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   3 IRNIGIMAHIDAGKTTTTERIIYYTGKTHKIGDVDSGNTVTDWMTQEQDRGITISSAAITCYWKDHQINIIDTPGHVDFT 82
Cdd:COG0480     9 IRNIGIVAHIDAGKTTLTERILFYTGAIHRIGEVHDGNTVMDWMPEEQERGITITSAATTCEWKGHKINIIDTPGHVDFT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  83 AEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYVNKMDRVGANFFKVVEDIRNKFGIVPIVLQIPIGSE 162
Cdd:COG0480    89 GEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQLKERLGANPVPLQLPIGAE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 163 NNFEGVIDIIRNKELHFELRDGKPIVLEDvVREEFVENVKIFKENLIDSLSNFSERITELFLENSVIDDSLIIEEIRRCT 242
Cdd:COG0480   169 DDFKGVIDLVTMKAYVYDDELGAKYEEEE-IPAELKEEAEEAREELIEAVAETDDELMEKYLEGEELTEEEIKAGLRKAT 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 243 ISGFIIPVLMGTSLKNIGIEPLIDAIVDYLPSPFEKK-INAYSLKTDRSVSIEPKDEKRLSALVFKVQY--FsaiAAHLY 319
Cdd:COG0480   248 LAGKIVPVLCGSAFKNKGVQPLLDAVVDYLPSPLDVPaIKGVDPDTGEEVERKPDDDEPFSALVFKTMTdpF---VGKLS 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 320 FIRVYSGELSSSKRVLNIAKNKREKFTRIFRVFSNKNEQIDEVKAGDIGAVIGLKYSITGDTLVEEGNEIMLEPLVFPEP 399
Cdd:COG0480   325 FFRVYSGTLKSGSTVYNSTKGKKERIGRLLRMHGNKREEVDEAGAGDIVAVVKLKDTTTGDTLCDEDHPIVLEPIEFPEP 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 400 VVLISIEPERASDDGRLKEVLEIITKEDPTFSYKESKETGQLLVSGMGELHLEIIVMRIRDDFKLNVYTGKPQVSYRESL 479
Cdd:COG0480   405 VISVAIEPKTKADEDKLSTALAKLAEEDPTFRVETDEETGQTIISGMGELHLEIIVDRLKREFGVEVNVGKPQVAYRETI 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 480 SVTVN----------------DVFefvnmfagkelnlkigMIVSPLMRGEGnkIEFECNV-------EplFKAAILRGIT 536
Cdd:COG0480   485 RKKAEaegkhkkqsgghgqygDVW----------------IEIEPLPRGEG--FEFVDKIvggvipkE--YIPAVEKGIR 544
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 537 SSFSSGII-GYPIIDVGVKItsldYDKS-----------KvnesviesIAG-LAFNEFFKRANPIKLEPIMILEIRTPIE 603
Cdd:COG0480   545 EAMEKGVLaGYPVVDVKVTL----YDGSyhpvdssemafK--------IAAsMAFKEAAKKAKPVLLEPIMKVEVTVPEE 612
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1021452772 604 YTGEVVSTLNFVGGMIHSISNIEDYEIIKAEAAFEKLFGYTSILRSATKGRGVFTMEFSYFKE 666
Cdd:COG0480   613 YMGDVMGDLNSRRGRILGMESRGGAQVIKAEVPLAEMFGYATDLRSLTQGRGSFTMEFSHYEE 675
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
9-666 0e+00

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 670.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   9 MAHIDAGKTTTTERIIYYTGKTHKIGDVDSGNTVTDWMTQEQDRGITISSAAITCYWKDHQINIIDTPGHVDFTAEVERS 88
Cdd:PRK12740    1 VGHSGAGKTTLTEAILFYTGAIHRIGEVEDGTTTMDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVERA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  89 LRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYVNKMDRVGANFFKVVEDIRNKFGIVPIVLQIPIGSENNFEGV 168
Cdd:PRK12740   81 LRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRAGADFFRVLAQLQEKLGAPVVPLQLPIGEGDDFTGV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 169 IDIIRNKELHFelRDGKPIVLEDvVREEFVENVKIFKENLIDSLSNFSERITELFLENSVIDDSLIIEEIRRCTISGFII 248
Cdd:PRK12740  161 VDLLSMKAYRY--DEGGPSEEIE-IPAELLDRAEEAREELLEALAEFDDELMEKYLEGEELSEEEIKAGLRKATLAGEIV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 249 PVLMGTSLKNIGIEPLIDAIVDYLPSPFEKKiNAYSLKTDRSVSIEPKDEKRLSALVFKV---QYFSAIAahlyFIRVYS 325
Cdd:PRK12740  238 PVFCGSALKNKGVQRLLDAVVDYLPSPLEVP-PVDGEDGEEGAELAPDPDGPLVALVFKTmddPFVGKLS----LVRVYS 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 326 GELSSSKRVLNIAKNKREKFTRIFRVFSNKNEQIDEVKAGDIGAVIGLKYSITGDTLVEEGNEIMLEPLVFPEPVVLISI 405
Cdd:PRK12740  313 GTLKKGDTLYNSGTGKKERVGRLYRMHGKQREEVDEAVAGDIVAVAKLKDAATGDTLCDKGDPILLEPMEFPEPVISLAI 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 406 EPERASDDGRLKEVLEIITKEDPTFSYKESKETGQLLVSGMGELHLEIIVMRIRDDFKLNVYTGKPQVSYRESLSVTVND 485
Cdd:PRK12740  393 EPKDKGDEEKLSEALGKLAEEDPTLRVERDEETGQTILSGMGELHLDVALERLKREYGVEVETGPPQVPYRETIRKKAEG 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 486 VFEFVNM------FAgkelnlKIGMIVSPLMRGEGnkIEFECNV-------EplFKAAILRGITSSFSSGII-GYPIIDV 551
Cdd:PRK12740  473 HGRHKKQsgghgqFG------DVWLEVEPLPRGEG--FEFVDKVvggavprQ--YIPAVEKGVREALEKGVLaGYPVVDV 542
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 552 GVKITSLDYDkskvneSVIES-----IAG-LAFNEFFKRANPIKLEPIMILEIRTPIEYTGEVVSTLNFVGGMIHSISNI 625
Cdd:PRK12740  543 KVTLTDGSYH------SVDSSemafkIAArLAFREALPKAKPVLLEPIMKVEVSVPEEFVGDVIGDLSSRRGRILGMESR 616
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|.
gi 1021452772 626 EDYEIIKAEAAFEKLFGYTSILRSATKGRGVFTMEFSYFKE 666
Cdd:PRK12740  617 GGGDVVRAEVPLAEMFGYATDLRSLTQGRGSFSMEFSHYEE 657
EF-G TIGR00484
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ...
3-666 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: 652.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   3 IRNIGIMAHIDAGKTTTTERIIYYTGKTHKIGDVDSGNTVTDWMTQEQDRGITISSAAITCYWKDHQINIIDTPGHVDFT 82
Cdd:TIGR00484  10 FRNIGISAHIDAGKTTTTERILFYTGRIHKIGEVHDGAATMDWMEQEKERGITITSAATTVFWKGHRINIIDTPGHVDFT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  83 AEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYVNKMDRVGANFFKVVEDIRNKFGIVPIVLQIPIGSE 162
Cdd:TIGR00484  90 VEVERSLRVLDGAVAVLDAVGGVQPQSETVWRQANRYEVPRIAFVNKMDKTGANFLRVVNQIKQRLGANAVPIQLPIGAE 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 163 NNFEGVIDIIRNKELHFELRDGKPIVLEDvVREEFVENVKIFKENLIDSLSNFSERITELFLENSVIDDSLIIEEIRRCT 242
Cdd:TIGR00484 170 DNFIGVIDLVEMKAYFFNGDKGTKAIEKE-IPSDLLEQAKELRENLVEAVAEFDEELMEKYLEGEELTIEEIKNAIRKGV 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 243 ISGFIIPVLMGTSLKNIGIEPLIDAIVDYLPSPFE-KKINAYSLKTDRSVSIEPKDEKRLSALVFKVQYfSAIAAHLYFI 321
Cdd:TIGR00484 249 LNCEFFPVLCGSAFKNKGVQLLLDAVVDYLPSPTDvPAIKGIDPDTEKEIERKASDDEPFSALAFKVAT-DPFVGQLTFV 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 322 RVYSGELSSSKRVLNIAKNKREKFTRIFRVFSNKNEQIDEVKAGDIGAVIGLKYSITGDTLVEEGNEIMLEPLVFPEPVV 401
Cdd:TIGR00484 328 RVYSGVLKSGSYVKNSRKNKKERVGRLVKMHANNREEIKEVRAGDICAAIGLKDTTTGDTLCDPKIDVILERMEFPEPVI 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 402 LISIEPERASDDGRLKEVLEIITKEDPTFSYKESKETGQLLVSGMGELHLEIIVMRIRDDFKLNVYTGKPQVSYRESLSV 481
Cdd:TIGR00484 408 SLAVEPKTKADQEKMGIALGKLAEEDPTFRTFTDPETGQTIIAGMGELHLDIIVDRMKREFKVEANVGAPQVAYRETIRS 487
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 482 TVNDVFEFVNMFAGKElnlKIGMIVSPLMRGEGNKIEFE----CNVEPL-FKAAILRGITSSFSSG-IIGYPIIDVGVKI 555
Cdd:TIGR00484 488 KVEVEGKHAKQSGGRG---QYGHVKIRFEPLEPKGYEFVneikGGVIPReYIPAVDKGLQEAMESGpLAGYPVVDIKATL 564
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 556 TSLDYDKSKVNESVIESIAGLAFNEFFKRANPIKLEPIMILEIRTPIEYTGEVVSTLNFVGGMIHSISNIEDYEIIKAEA 635
Cdd:TIGR00484 565 FDGSYHDVDSSEMAFKLAASLAFKEAGKKANPVLLEPIMKVEVEVPEEYMGDVMGDLSSRRGIIEGMEARGNVQKIKAEV 644
                         650       660       670
                  ....*....|....*....|....*....|.
gi 1021452772 636 AFEKLFGYTSILRSATKGRGVFTMEFSYFKE 666
Cdd:TIGR00484 645 PLSEMFGYATDLRSFTQGRGTYSMEFLHYGE 675
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
5-275 1.04e-164

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: 472.75  E-value: 1.04e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   5 NIGIMAHIDAGKTTTTERIIYYTGKTHKIGDVDSGNTVTDWMTQEQDRGITISSAAITCYWKDHQINIIDTPGHVDFTAE 84
Cdd:cd01886     1 NIGIIAHIDAGKTTTTERILYYTGRIHKIGEVHGGGATMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDFTIE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  85 VERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYVNKMDRVGANFFKVVEDIRNKFGIVPIVLQIPIGSENN 164
Cdd:cd01886    81 VERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQIREKLGANPVPLQLPIGAEDD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 165 FEGVIDIIRNKELHFELRDGKPIVLEDvVREEFVENVKIFKENLIDSLSNFSERITELFLENSVIDDSLIIEEIRRCTIS 244
Cdd:cd01886   161 FEGVVDLIEMKALYWDGELGEKIEETD-IPEDLLEEAEEAREELIETLAEVDDELMEKYLEGEEITEEEIKAAIRKGTIA 239
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1021452772 245 GFIIPVLMGTSLKNIGIEPLIDAIVDYLPSP 275
Cdd:cd01886   240 NKIVPVLCGSAFKNKGVQPLLDAVVDYLPSP 270
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
5-275 4.34e-81

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: 257.91  E-value: 4.34e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   5 NIGIMAHIDAGKTTTTERIIYYTGKTHKIGDVDSGNTVTDWMTQEQDRGITISSAAITCYWKDHQINIIDTPGHVDFTAE 84
Cdd:cd04170     1 NIALVGHSGSGKTTLAEALLYATGAIDRLGRVEDGNTVSDYDPEEKKRKMSIETSVAPLEWNGHKINLIDTPGYADFVGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  85 VERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYVNKMDRVGANFFKVVEDIRNKFGIVPIVLQIPIGSENN 164
Cdd:cd04170    81 TLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRARADFDKTLAALREAFGRPVVPIQLPIGEGDE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 165 FEGVIDIIRNKELHFelRDGKPIVLEDvVREEFVENVKIFKENLIDSLSNFSERITELFLENSVIDDSLIIEEIRRCTIS 244
Cdd:cd04170   161 FTGVVDLLSEKAYRY--DPGEPSVEIE-IPEELKEKVAEAREELLEAVAETDEELMEKYLEEGELTEEELRAGLRRALRA 237
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1021452772 245 GFIIPVLMGTSLKNIGIEPLIDAIVDYLPSP 275
Cdd:cd04170   238 GLIVPVFFGSALTGIGVRRLLDALVELAPSP 268
PRK07560 PRK07560
elongation factor EF-2; Reviewed
3-665 7.91e-77

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 260.18  E-value: 7.91e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   3 IRNIGIMAHIDAGKTTTTERIIYYTGKthkIGDVDSGNT-VTDWMTQEQDRGITISSAAITCYW----KDHQINIIDTPG 77
Cdd:PRK07560   20 IRNIGIIAHIDHGKTTLSDNLLAGAGM---ISEELAGEQlALDFDEEEQARGITIKAANVSMVHeyegKEYLINLIDTPG 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  78 HVDFTAEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYVNKMDR-----------VGANFFKVVEDI-- 144
Cdd:PRK07560   97 HVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKPVLFINKVDRlikelkltpqeMQQRLLKIIKDVnk 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 145 ----------------------------RNKFGI-VPIVLQIPIgsenNFEGVIDIIRNKELHfELRDGKPI---VLEDV 192
Cdd:PRK07560  177 likgmapeefkekwkvdvedgtvafgsaLYNWAIsVPMMQKTGI----KFKDIIDYYEKGKQK-ELAEKAPLhevVLDMV 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 193 VReeFVEN---------VKIFKENLidslsnfseritelfleNSVIDDSLIieeirRCTISGfiipvlmgtslknigieP 263
Cdd:PRK07560  252 VK--HLPNpieaqkyriPKIWKGDL-----------------NSEVGKAML-----NCDPNG-----------------P 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 264 LIDAIVDylpspfekkinayslktdrsVSIEPKdekrlSALVfkvqyfsAIAahlyfiRVYSGELSSSKRV--LNIAKNK 341
Cdd:PRK07560  291 LVMMVTD--------------------IIVDPH-----AGEV-------ATG------RVFSGTLRKGQEVylVGAKKKN 332
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 342 REKFTRIFrvFSNKNEQIDEVKAGDIGAVIGLKYSITGDTLVEEGNEIMLEPLV-FPEPVVLISIEPERASDDGRLKEVL 420
Cdd:PRK07560  333 RVQQVGIY--MGPEREEVEEIPAGNIAAVTGLKDARAGETVVSVEDMTPFESLKhISEPVVTVAIEAKNPKDLPKLIEVL 410
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 421 EIITKEDPTFSYKESKETGQLLVSGMGELHLEIIVMRIRDDFKLNVYTGKPQVSYRESLSVTVnDVFEfvnmfaGKELNL 500
Cdd:PRK07560  411 RQLAKEDPTLVVKINEETGEHLLSGMGELHLEVITYRIKRDYGIEVVTSEPIVVYRETVRGKS-QVVE------GKSPNK 483
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 501 --KIGMIVSPL------MRGEGN------KIEFECNVEPLFKAA----------------------------------IL 532
Cdd:PRK07560  484 hnRFYISVEPLeeevieAIKEGEisedmdKKEAKILREKLIEAGmdkdeakrvwaiyngnvfidmtkgiqylnevmelII 563
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 533 RGITSSFSSG-IIGYPIIdvGVKITSLDydkSKVNE--------SVIESIAGLAFNEFFKrANPIKLEPIMILEIRTPIE 603
Cdd:PRK07560  564 EGFREAMKEGpLAAEPVR--GVKVRLHD---AKLHEdaihrgpaQVIPAVRNAIFAAMLT-AKPTLLEPIQKVDINVPQD 637
                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1021452772 604 YTGEVVSTLNFVGGMIHSISNIEDYEIIKAEAAFEKLFGYTSILRSATKGRGVFTMEFSYFK 665
Cdd:PRK07560  638 YMGAVTREIQGRRGKILDMEQEGDMAIIEAEAPVAEMFGFAGEIRSATEGRALWSTEFAGFE 699
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
5-275 3.40e-73

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: 235.98  E-value: 3.40e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   5 NIGIMAHIDAGKTTTTERIIYYTGKTHKIGDVDSGNTVTDWMTQEQDRGITISSAAITCYWKDHQINIIDTPGHVDFTAE 84
Cdd:cd04168     1 NIGILAHVDAGKTTLTESLLYTSGAIRELGSVDKGTTRTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  85 VERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYVNKMDRVGANFFKVVEDIRNKFgivpivlqipigsenn 164
Cdd:cd04168    81 VERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTIIFVNKIDRAGADLEKVYQEIKEKL---------------- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 165 fegvidiirnkelhfelrDGKPIVLEDVVREEFVENVKIFKENLIDSLSNFSERITELFLENSVIDDSLIIEEIRRCTIS 244
Cdd:cd04168   145 ------------------SPDIVPMQKVGLYPNICDTNNIDDEQIETVAEGNDELLEKYLSGGPLEELELDNELSARIQK 206
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1021452772 245 GFIIPVLMGTSLKNIGIEPLIDAIVDYLPSP 275
Cdd:cd04168   207 ASLFPVYHGSALKGIGIDELLEGITNLFPTS 237
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
2-148 1.54e-71

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: 229.72  E-value: 1.54e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   2 EIRNIGIMAHIDAGKTTTTERIIYYTGKTHKIGDVD-SGNTVTDWMTQEQDRGITISSAAITCYWKDHQINIIDTPGHVD 80
Cdd:pfam00009   2 RHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKgEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVD 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021452772  81 FTAEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYVNKMDRV-GANFFKVVEDIRNKF 148
Cdd:pfam00009  82 FVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVdGAELEEVVEEVSREL 150
aEF-2 TIGR00490
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ...
3-665 2.14e-66

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: 231.71  E-value: 2.14e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   3 IRNIGIMAHIDAGKTTTTERIIYYTGKTHKigDVDSGNTVTDWMTQEQDRGITISSAAITCYW----KDHQINIIDTPGH 78
Cdd:TIGR00490  19 IRNIGIVAHIDHGKTTLSDNLLAGAGMISE--ELAGQQLYLDFDEQEQERGITINAANVSMVHeyegNEYLINLIDTPGH 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  79 VDFTAEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYVNKMDRvganffkvvedIRNKFGIVPIVLQip 158
Cdd:TIGR00490  97 VDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKPVLFINKVDR-----------LINELKLTPQELQ-- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 159 igsennfEGVIDIIRNkeLHFELRDGKPivledvvrEEFVENVKIFKEN----LIDSLSNFSerITELFLENSVIDDSLI 234
Cdd:TIGR00490 164 -------ERFIKIITE--VNKLIKAMAP--------EEFRDKWKVRVEDgsvaFGSAYYNWA--ISVPSMKKTGIGFKDI 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 235 IEEIRRCTISGFiipvlmgtSLKNIGIEPLIDAIVDYLPSPFEKK------INAYSLKTDRSVSIEPKDEKRLSALVFKV 308
Cdd:TIGR00490 225 YKYCKEDKQKEL--------AKKSPLHQVVLDMVIRHLPSPIEAQkyripvIWKGDLNSEVGKAMLNCDPKGPLALMITK 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 309 QYFSAIAAHLYFIRVYSGELSSSKRVLNIAKNKREKFTRIFRVFSNKNEQIDEVKAGDIGAVIGLKYSITGDTLVEEGNE 388
Cdd:TIGR00490 297 IVVDKHAGEVAVGRLYSGTIRPGMEVYIVDRKAKARIQQVGVYMGPERVEVDEIPAGNIVAVIGLKDAVAGETICTTVEN 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 389 IM-LEPLV-FPEPVVLISIEPERASDDGRLKEVLEIITKEDPTFSYKESKETGQLLVSGMGELHLEIIVMRIRDDFKLNV 466
Cdd:TIGR00490 377 ITpFESIKhISEPVVTVAIEAKNTKDLPKLIEVLRQVAKEDPTVHVEINEETGEHLISGMGELHLEIIVEKIREDYGLDV 456
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 467 YTGKPQVSYRESLSVTV-----------NDVFEFVNMFAGKELN-LKIGMIVSPLMRGEGNKIEF-ECNVEP-------- 525
Cdd:TIGR00490 457 ETSPPIVVYRETVTGTSpvvegkspnkhNRFYIVVEPLEESVIQaFKEGKIVDMKMKKKERRRLLiEAGMDSeeaarvee 536
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 526 -----LF-------------KAAILRGITSSFSSGIIGY-PIIDVGVKITSLDYDKSKVNESVIESIAGLAFNEF--FKR 584
Cdd:TIGR00490 537 yyegnLFinmtrgiqyldetKELILEGFREAMRNGPIAReKCMGVKVKLMDAKLHEDAVHRGPAQVIPAVRSGIFaaMMQ 616
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 585 ANPIKLEPIMILEIRTPIEYTGEVVSTLNFVGGMIHSISNIEDYEIIKAEAAFEKLFGYTSILRSATKGRGVFTMEFSYF 664
Cdd:TIGR00490 617 AKPVLLEPYQKVFINVPQDMMGAATREIQNRRGQILEMKQEGDMVTIIAKAPVAEMFGFAGAIRGATSGRCLWSTEHAGF 696

                  .
gi 1021452772 665 K 665
Cdd:TIGR00490 697 E 697
RF3 cd04169
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ...
4-275 1.16e-49

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: 174.32  E-value: 1.16e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   4 RNIGIMAHIDAGKTTTTERIIYYTGKTHKIGDV----DSGNTVTDWMTQEQDRGITISSAAITCYWKDHQINIIDTPGHV 79
Cdd:cd04169     3 RTFAIISHPDAGKTTLTEKLLLFGGAIQEAGAVkarkSRKHATSDWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  80 DFTAEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYVNKMDRVGANFFKVVEDIRNKFGIVPIVLQIPI 159
Cdd:cd04169    83 DFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDREGRDPLELLDEIENELGIDCAPMTWPI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 160 GSENNFEGVIDiIRNKELHFELRD--GKPIVLEDVVREEFVENVKIFKENLIDSLsnfserITELFLENSVIDDsLIIEE 237
Cdd:cd04169   163 GMGKDFKGVYD-RYDKEIYLYERGagGAIKAPEETKGLDDPKLDELLGEDLAEQL------REELELVEGAGPE-FDKEL 234
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1021452772 238 IRRCTISgfiiPVLMGTSLKNIGIEPLIDAIVDYLPSP 275
Cdd:cd04169   235 FLAGELT----PVFFGSALNNFGVQELLDAFVKLAPAP 268
PrfC COG4108
Peptide chain release factor RF-3 [Translation, ribosomal structure and biogenesis]; Peptide ...
4-397 5.03e-49

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: 179.88  E-value: 5.03e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   4 RNIGIMAHIDAGKTTTTERIIYYTGKTHKIGDV----DSGNTVTDWMTQEQDRGITISSAAITCYWKDHQINIIDTPGHV 79
Cdd:COG4108    11 RTFAIISHPDAGKTTLTEKLLLFGGAIQLAGAVkarkARRHATSDWMEIEKQRGISVTSSVMQFEYRGYVINLLDTPGHE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  80 DFTaevERSLRVL---DGGIVVFSAVDGIQAQTE---TVWRQAskyGIPRLAYVNKMDRVGANFFKVVEDIRNKFGIVPI 153
Cdd:COG4108    91 DFS---EDTYRTLtavDSAVMVIDAAKGVEPQTRklfEVCRLR---GIPIITFINKLDREGRDPLELLDEIEEVLGIDCA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 154 VLQIPIGSENNFEGVIDIIRNKELHFELRDGKpivledvVREEFVEnvkifkenlIDSLSN--FSERITELFLENSVIDD 231
Cdd:COG4108   165 PMTWPIGMGKDFKGVYDRYTDEVHLFERGAGG-------ATEAPEE---------IEGLDDpeLDELLGEDLAEQLREEI 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 232 SLI--------IEEIRRCTISgfiiPVLMGTSLKNIGIEPLIDAIVDYLPSPFEKKinayslKTDRSVsiEPkDEKRLSA 303
Cdd:COG4108   229 ELLdgagpefdLEAFLAGELT----PVFFGSALNNFGVRELLDAFVELAPPPRPRE------ADEREV--EP-TEEKFSG 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 304 LVFKVQyfsaiA----AH---LYFIRVYSGELSSSKRVLNIAKNKREKFTRIFRVFSNKNEQIDEVKAGDIgavIGL--- 373
Cdd:COG4108   296 FVFKIQ-----AnmdpAHrdrIAFMRICSGKFERGMKVKHVRTGKKIRLSNPQQFFAQDRETVEEAYPGDI---IGLhnh 367
                         410       420
                  ....*....|....*....|....*
gi 1021452772 374 -KYSItGDTLVEEgneimlEPLVFP 397
Cdd:COG4108   368 gTLRI-GDTLTEG------EKLEFT 385
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
5-154 1.34e-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: 165.55  E-value: 1.34e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   5 NIGIMAHIDAGKTTTTERIIYYTGKTHKIGDVDsgNTVTDWMTQEQDRGITISSAAITCYWKDHQINIIDTPGHVDFTAE 84
Cdd:cd00881     1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRK--ETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKE 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1021452772  85 VERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYVNKMDRVG-ANFFKVVEDIRNKFGIVPIV 154
Cdd:cd00881    79 TVRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGeEDFDEVLREIKELLKLIGFT 149
PTZ00416 PTZ00416
elongation factor 2; Provisional
3-653 6.38e-44

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 169.07  E-value: 6.38e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   3 IRNIGIMAHIDAGKTTTTERIIyytGKTHKIGDVDSGNT-VTDWMTQEQDRGITISSAAITCYW----------KDHQIN 71
Cdd:PTZ00416   19 IRNMSVIAHVDHGKSTLTDSLV---CKAGIISSKNAGDArFTDTRADEQERGITIKSTGISLYYehdledgddkQPFLIN 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  72 IIDTPGHVDFTAEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYVNKMDRVGANFFKVVEDIRNKF-GI 150
Cdd:PTZ00416   96 LIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKVDRAILELQLDPEEIYQNFvKT 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 151 VPIVLQIpIGSENNfegviDIIRNKELHFEL--------RDGKPIVLEDVVReEFVENVKIFKENLIDSL--SNFSERIT 220
Cdd:PTZ00416  176 IENVNVI-IATYND-----ELMGDVQVYPEKgtvafgsgLQGWAFTLTTFAR-IYAKKFGVEESKMMERLwgDNFFDAKT 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 221 ELFLENSVIDDSliiEEIRRCTISGFIIPVLMGTS-------------LKNIGIE----------------------PLI 265
Cdd:PTZ00416  249 KKWIKDETNAQG---KKLKRAFCQFILDPICQLFDavmnedkekydkmLKSLNISltgedkeltgkpllkavmqkwlPAA 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 266 DA----IVDYLPSPFE----KKINAYSLKTDR--SVSIEPKD-EKRLSALVFKVQYFSAIAAHLYFIRVYSGELSSSKRV 334
Cdd:PTZ00416  326 DTllemIVDHLPSPKEaqkyRVENLYEGPMDDeaANAIRNCDpNGPLMMYISKMVPTSDKGRFYAFGRVFSGTVATGQKV 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 335 LNIAKN-----KREKF----TRIFRVFSNKNEQIDEVKAGDIGAVIGL-KYSITGDTLVEEGNEIMLEPLVFP-EPVVLI 403
Cdd:PTZ00416  406 RIQGPNyvpgkKEDLFekniQRTVLMMGRYVEQIEDVPCGNTVGLVGVdQYLVKSGTITTSETAHNIRDMKYSvSPVVRV 485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 404 SIEPERASDDGRLKEVLEIITKEDPTFSYkESKETGQLLVSGMGELHLEIIVMRIRDDF-KLNVYTGKPQVSYREslsvT 482
Cdd:PTZ00416  486 AVEPKNPKDLPKLVEGLKRLAKSDPLVVC-TTEESGEHIVAGCGELHVEICLKDLEDDYaNIDIIVSDPVVSYRE----T 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 483 VNDVFEFVNMfaGKELNL--KIGMIVSPLMRGEGNKIE---FECNVEPLFKAAIL-----------RGITSSFSSGIIGY 546
Cdd:PTZ00416  561 VTEESSQTCL--SKSPNKhnRLYMKAEPLTEELAEAIEegkVGPEDDPKERANFLadkyewdkndaRKIWCFGPENKGPN 638
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 547 PIIDVGVKITSLDYDKSKVN--------ESVI--ESIAGLAFN-----------------------EFFK----RANPIK 589
Cdd:PTZ00416  639 VLVDVTKGVQYMNEIKDSCVsafqwatkEGVLcdENMRGIRFNildvtlhadaihrgagqiiptarRVFYacelTASPRL 718
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 590 LEPIMILEIRTPIEYTGEVVSTLNFVGGMIHSisniEDYE------IIKAEAAFEKLFGYTSILRSATKG 653
Cdd:PTZ00416  719 LEPMFLVDITAPEDAMGGIYSVLNRRRGVVIG----EEQRpgtplsNIKAYLPVAESFGFTAALRAATSG 784
prfC PRK00741
peptide chain release factor 3; Provisional
4-384 1.22e-43

peptide chain release factor 3; Provisional


Pssm-ID: 179105 [Multi-domain]  Cd Length: 526  Bit Score: 164.54  E-value: 1.22e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   4 RNIGIMAHIDAGKTTTTERIIYYTGKTHKIGDVD---SGNTVT-DWMTQEQDRGITISSAAITCYWKDHQINIIDTPGHV 79
Cdd:PRK00741   11 RTFAIISHPDAGKTTLTEKLLLFGGAIQEAGTVKgrkSGRHATsDWMEMEKQRGISVTSSVMQFPYRDCLINLLDTPGHE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  80 DFTAEVERSLRVLDGGIVVFSAVDGIQAQTET---VWRQAskyGIPRLAYVNKMDRVGANFFKVVEDIRNKFGIVPIVLQ 156
Cdd:PRK00741   91 DFSEDTYRTLTAVDSALMVIDAAKGVEPQTRKlmeVCRLR---DTPIFTFINKLDRDGREPLELLDEIEEVLGIACAPIT 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 157 IPIGSENNFEGVIDIiRNKELH-FELRDGKPIvledvvreefvENVKIFKENLIDSLSnfsERITELFLENSVIDDSLI- 234
Cdd:PRK00741  168 WPIGMGKRFKGVYDL-YNDEVElYQPGEGHTI-----------QEVEIIKGLDNPELD---ELLGEDLAEQLREELELVq 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 235 -------IEEIrrctISGFIIPVLMGTSLKNIGIEPLIDAIVDYLPSPFEKKinayslKTDRSVsiEPKDEKrLSALVFK 307
Cdd:PRK00741  233 gasnefdLEAF----LAGELTPVFFGSALNNFGVQEFLDAFVEWAPAPQPRQ------TDEREV--EPTEEK-FSGFVFK 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 308 VQyfsA---------IAahlyFIRVYSGELSSSKRVLNIAKNKREKFTRIFRVFSNKNEQIDEVKAGDIgavIGL----K 374
Cdd:PRK00741  300 IQ---AnmdpkhrdrIA----FVRVCSGKFEKGMKVRHVRTGKDVRISNALTFMAQDREHVEEAYAGDI---IGLhnhgT 369
                         410
                  ....*....|
gi 1021452772 375 YSItGDTLVE 384
Cdd:PRK00741  370 IQI-GDTFTQ 378
prfC TIGR00503
peptide chain release factor 3; This translation releasing factor, RF-3 (prfC) was originally ...
4-462 2.78e-42

peptide chain release factor 3; This translation releasing factor, RF-3 (prfC) was originally described as stop codon-independent, in contrast to peptide chain release factor 1 (RF-1, prfA) and RF-2 (prfB). RF-1 and RF-2 are closely related to each other, while RF-3 is similar to elongation factors EF-Tu and EF-G; RF-1 is active at UAA and UAG and RF-2 is active at UAA and UGA. More recently, RF-3 was shown to be active primarily at UGA stop codons in E. coli. All bacteria and organelles have RF-1. The Mycoplasmas and organelles, which translate UGA as Trp rather than as a stop codon, lack RF-2. RF-3, in contrast, seems to be rare among bacteria and is found so far only in Escherichia coli and some other gamma subdivision Proteobacteria, in Synechocystis PCC6803, and in Staphylococcus aureus. [Protein synthesis, Translation factors]


Pssm-ID: 129594 [Multi-domain]  Cd Length: 527  Bit Score: 160.84  E-value: 2.78e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   4 RNIGIMAHIDAGKTTTTERIIYYTGKTHKIGDV----DSGNTVTDWMTQEQDRGITISSAAITCYWKDHQINIIDTPGHV 79
Cdd:TIGR00503  12 RTFAIISHPDAGKTTITEKVLLYGGAIQTAGAVkgrgSQRHAKSDWMEMEKQRGISITTSVMQFPYRDCLVNLLDTPGHE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  80 DFTAEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYVNKMDRVGANFFKVVEDIRNKFGIVPIVLQIPI 159
Cdd:TIGR00503  92 DFSEDTYRTLTAVDNCLMVIDAAKGVETRTRKLMEVTRLRDTPIFTFMNKLDRDIRDPLELLDEVENELKINCAPITWPI 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 160 GSENNFEGVIDIIRNKELHFELRDGKPIvledvvreEFVENVKIFKENLIDSLsnFSERITELFLENSVIDDSLIIEEIR 239
Cdd:TIGR00503 172 GCGKLFKGVYHLLKDETYLYQSGTGGTI--------QAVRQVKGLNNPALDSA--VGSDLAQQLRDELELVEGASNEFDL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 240 RCTISGFIIPVLMGTSLKNIGIEPLIDAIVDYLPSPFEKkinayslKTDRSvSIEPKDEKrLSALVFKVQ------YFSA 313
Cdd:TIGR00503 242 AAFHGGEMTPVFFGTALGNFGVDHFLDGLLQWAPKPEAR-------QSDTR-TVEPTEEK-FSGFVFKIQanmdpkHRDR 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 314 IAahlyFIRVYSGELSSSKRVLNIAKNKREKFTRIFRVFSNKNEQIDEVKAGDIgavIGLKYSIT---GDTlVEEGNEIM 390
Cdd:TIGR00503 313 VA----FMRVVSGKYEKGMKLKHVRTGKDVVISDALTFMAGDREHVEEAYAGDI---IGLHNHGTiqiGDT-FTQGEKIK 384
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021452772 391 LEPLVFPEPVVLISIepeRASDDGRLKEVLEIITK--EDPTFSYKESKETGQLLVSGMGELHLEIIVMRIRDDF 462
Cdd:TIGR00503 385 FTGIPNFAPELFRRI---RLKDPLKQKQLLKGLVQlsEEGAVQVFRPLDNNDLIVGAVGVLQFDVVVYRLKEEY 455
lepA TIGR01393
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a ...
3-476 6.79e-42

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


Pssm-ID: 130460 [Multi-domain]  Cd Length: 595  Bit Score: 160.57  E-value: 6.79e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   3 IRNIGIMAHIDAGKTTTTERIIYYTGKthkIGDVDSGNTVTDWMTQEQDRGITISSAAITCYWKD-----HQINIIDTPG 77
Cdd:TIGR01393   3 IRNFSIIAHIDHGKSTLADRLLEYTGA---ISEREMREQVLDSMDLERERGITIKAQAVRLNYKAkdgetYVLNLIDTPG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  78 HVDFTAEVERSLRVLDGGIVVFSAVDGIQAQTEtvwrqaskygiprlayvnkmdrvgANFFKVVEdirNKFGIVPIVLQI 157
Cdd:TIGR01393  80 HVDFSYEVSRSLAACEGALLLVDAAQGIEAQTL------------------------ANVYLALE---NDLEIIPVINKI 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 158 PIGSENnfegvidiirnkelhfelrdgkpivledvvreefVENVKIFKENLIDslsnfseritelflensvIDDSLIIee 237
Cdd:TIGR01393 133 DLPSAD----------------------------------PERVKKEIEEVIG------------------LDASEAI-- 158
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 238 irRCtisgfiipvlmgtSLKN-IGIEPLIDAIVDYLPSPfekkinayslktdrsvsiEPKDEKRLSALVFKvQYFSAIAA 316
Cdd:TIGR01393 159 --LA-------------SAKTgIGIEEILEAIVKRVPPP------------------KGDPDAPLKALIFD-SHYDNYRG 204
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 317 HLYFIRVYSGELSSSKRVLNIAKNKREKFTRIFrVFSNKNEQIDEVKAGDIGAVI-GLKYSI---TGDTLVEEGNEImLE 392
Cdd:TIGR01393 205 VVALVRVFEGTIKPGDKIRFMSTGKEYEVDEVG-VFTPKLTKTDELSAGEVGYIIaGIKDVSdvrVGDTITHVKNPA-KE 282
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 393 PLV-FPE--PVVLISIEPERASDDGRLKEVLEIITKEDPTFSYKesKETGQLLVSG-----MGELHLEIIVMRIRDDFKL 464
Cdd:TIGR01393 283 PLPgFKEvkPMVFAGLYPIDTEDYEDLRDALEKLKLNDASLTYE--PESSPALGFGfrcgfLGLLHMEIIQERLEREFNL 360
                         490
                  ....*....|..
gi 1021452772 465 NVYTGKPQVSYR 476
Cdd:TIGR01393 361 DLITTAPSVIYR 372
PLN00116 PLN00116
translation elongation factor EF-2 subunit; Provisional
3-485 7.15e-40

translation elongation factor EF-2 subunit; Provisional


Pssm-ID: 177730 [Multi-domain]  Cd Length: 843  Bit Score: 156.81  E-value: 7.15e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   3 IRNIGIMAHIDAGKTTTTERIIYYTGKTHKigDVDSGNTVTDWMTQEQDRGITISSAAITCYW----------------K 66
Cdd:PLN00116   19 IRNMSVIAHVDHGKSTLTDSLVAAAGIIAQ--EVAGDVRMTDTRADEAERGITIKSTGISLYYemtdeslkdfkgerdgN 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  67 DHQINIIDTPGHVDFTAEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYVNKMDR------VGA----- 135
Cdd:PLN00116   97 EYLINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTETVLRQALGERIRPVLTVNKMDRcflelqVDGeeayq 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 136 NFFKVVEDirnkfgivpiVLQIPIGSENNFEGVIDIIRNKE-------LHfelrdGKPIVLEDVVReEFVENVKIFKENL 208
Cdd:PLN00116  177 TFSRVIEN----------ANVIMATYEDPLLGDVQVYPEKGtvafsagLH-----GWAFTLTNFAK-MYASKFGVDESKM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 209 IDSL--SNFSERITELFLENSVIDDSL-------IIEEIRRctisgfIIPVLMGTS-------LKNIGIE---------- 262
Cdd:PLN00116  241 MERLwgENFFDPATKKWTTKNTGSPTCkrgfvqfCYEPIKQ------IINTCMNDQkdklwpmLEKLGVTlksdekelmg 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 263 ----------------PLIDAIVDYLPSPFekKINAYSLKT-------DR-SVSIEPKDEK-RLSALVFKVQYFSAIAAH 317
Cdd:PLN00116  315 kalmkrvmqtwlpasdALLEMIIFHLPSPA--KAQRYRVENlyegpldDKyATAIRNCDPNgPLMLYVSKMIPASDKGRF 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 318 LYFIRVYSGELSSSKRVLNIAKN-----KREKFT----RIFRVFSNKNEQIDEVKAGDIGAVIGLKYSITGD-TLVEEGN 387
Cdd:PLN00116  393 FAFGRVFSGTVATGMKVRIMGPNyvpgeKKDLYVksvqRTVIWMGKKQESVEDVPCGNTVAMVGLDQFITKNaTLTNEKE 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 388 EIM--LEPLVFP-EPVVLISIEPERASDDGRLKEVLEIITKEDP-TFSYKEskETGQLLVSGMGELHLEIIVMRIRDDFK 463
Cdd:PLN00116  473 VDAhpIKAMKFSvSPVVRVAVQCKNASDLPKLVEGLKRLAKSDPmVQCTIE--ESGEHIIAGAGELHLEICLKDLQDDFM 550
                         570       580
                  ....*....|....*....|....
gi 1021452772 464 --LNVYTGKPQVSYREslsvTVND 485
Cdd:PLN00116  551 ggAEIKVSDPVVSFRE----TVLE 570
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
4-132 4.46e-38

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: 140.83  E-value: 4.46e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   4 RNIGIMAHIDAGKTTTTERIIYYTGkthkIGDVDSGNTV--TDWMTQEQDRGITISSAAITCYW---------KDHQINI 72
Cdd:cd01885     1 RNICIIAHVDHGKTTLSDSLLASAG----IISEKLAGKAryLDTREDEQERGITIKSSAISLYFeyeeekmdgNDYLINL 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  73 IDTPGHVDFTAEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYVNKMDR 132
Cdd:cd01885    77 IDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDR 136
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
1-477 1.61e-33

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


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 135.92  E-value: 1.61e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   1 MEIRNIGIMAHIDAGKTTTTERIIYYTGKTHKIGDVDsgNTVTDWMTQEQDRGITISSAAITCYWKDHQINIIDTPGHVD 80
Cdd:COG1217     4 EDIRNIAIIAHVDHGKTTLVDALLKQSGTFRENQEVA--ERVMDSNDLERERGITILAKNTAVRYKGVKINIVDTPGHAD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  81 FTAEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYVNKMDRVGAnffkvvedirnkfgivpivlqipig 160
Cdd:COG1217    82 FGGEVERVLSMVDGVLLLVDAFEGPMPQTRFVLKKALELGLKPIVVINKIDRPDA------------------------- 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 161 sennfegvidiirnkelhfelrdgkpivledvvREEFVENvKIFkenlidslsnfseritELFLENSVIDDSLiieeirr 240
Cdd:COG1217   137 ---------------------------------RPDEVVD-EVF----------------DLFIELGATDEQL------- 159
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 241 ctisGFiiPVL--------MGTSLKNIG--IEPLIDAIVDYLPSPfekkinayslktdrsvsiEPKDEKRLSALVFKVQY 310
Cdd:COG1217   160 ----DF--PVVyasarngwASLDLDDPGedLTPLFDTILEHVPAP------------------EVDPDGPLQMLVTNLDY 215
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 311 FS-----AIAahlyfiRVYSGELSSSKRVLNIAKN---KREKFTRIFRVFSNKNEQIDEVKAGDIGAVIGL-KYSItGDT 381
Cdd:COG1217   216 SDyvgriAIG------RIFRGTIKKGQQVALIKRDgkvEKGKITKLFGFEGLERVEVEEAEAGDIVAIAGIeDINI-GDT 288
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 382 LVEEGNeimleplvfPEPVVLISIEPER------------ASDDGR------LKEVLEiitKE---DPTFSYKESKETGQ 440
Cdd:COG1217   289 ICDPEN---------PEALPPIKIDEPTlsmtfsvndspfAGREGKfvtsrqIRERLE---KEletNVALRVEETDSPDA 356
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 1021452772 441 LLVSGMGELHLEIIV--MRiRDDFKLNVytGKPQVSYRE 477
Cdd:COG1217   357 FKVSGRGELHLSILIetMR-REGYELQV--SRPEVIFKE 392
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
4-150 3.93e-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: 125.34  E-value: 3.93e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   4 RNIGIMAHIDAGKTTTTERIIYYTGKthkIGDVDSGNTVTDWMTQEQDRGITISSAAITCYWK-----DHQINIIDTPGH 78
Cdd:cd01890     1 RNFSIIAHIDHGKSTLADRLLELTGT---VSEREMKEQVLDSMDLERERGITIKAQAVRLFYKakdgeEYLLNLIDTPGH 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1021452772  79 VDFTAEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYVNKMDRVGANFFKVVEDIRNKFGI 150
Cdd:cd01890    78 VDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVKQEIEDVLGL 149
LepA COG0481
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ...
3-532 4.70e-33

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


Pssm-ID: 440249 [Multi-domain]  Cd Length: 598  Bit Score: 134.76  E-value: 4.70e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   3 IRNIGIMAHIDAGKTTTTERIIYYTGKthkIGDVDSGNTVTDWMTQEQDRGITISSAAITCYWK-----DHQINIIDTPG 77
Cdd:COG0481     6 IRNFSIIAHIDHGKSTLADRLLELTGT---LSEREMKEQVLDSMDLERERGITIKAQAVRLNYKakdgeTYQLNLIDTPG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  78 HVDFTAEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYG---IPRLayvNKMDRVGANFFKVVEDIRNKFGIVPiv 154
Cdd:COG0481    83 HVDFSYEVSRSLAACEGALLVVDASQGVEAQTLANVYLALENDleiIPVI---NKIDLPSADPERVKQEIEDIIGIDA-- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 155 lqipigsennfegvidiirnkelhfelrdgkpivlEDVVReefvenvkifkenlidslsnfseritelflensviddsli 234
Cdd:COG0481   158 -----------------------------------SDAIL---------------------------------------- 162
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 235 ieeirrctISGfiipvlmgtslKN-IGIEPLIDAIVDYLPSPfekkinayslktdrsvsiEPKDEKRLSALVFKVQYFS- 312
Cdd:COG0481   163 --------VSA-----------KTgIGIEEILEAIVERIPPP------------------KGDPDAPLQALIFDSWYDSy 205
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 313 --AIAahlyFIRVYSGELSSSKRVLNIAKNKREKFTRIFrVFSNKNEQIDEVKAGDIGAVI-GLKySIT----GDTLVEE 385
Cdd:COG0481   206 rgVVV----YVRVFDGTLKKGDKIKMMSTGKEYEVDEVG-VFTPKMTPVDELSAGEVGYIIaGIK-DVRdarvGDTITLA 279
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 386 GNEiMLEPLV-F--PEPVVLISIEPERASDDGRLKEVLEIITKEDPTFSYKesKETGQLLVSG-----MGELHLEIIVMR 457
Cdd:COG0481   280 KNP-AAEPLPgFkeVKPMVFAGLYPVDSDDYEDLRDALEKLQLNDASLTYE--PETSAALGFGfrcgfLGLLHMEIIQER 356
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021452772 458 IRDDFKLNVYTGKPQVSYReslsvtvndvfefVNMFAGKELnlkigMIVSPLMRGEGNKI-EFEcnvEPLFKAAIL 532
Cdd:COG0481   357 LEREFDLDLITTAPSVVYE-------------VTLTDGEVI-----EVDNPSDLPDPGKIeEIE---EPIVKATII 411
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
2-144 9.96e-33

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: 124.63  E-value: 9.96e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   2 EIRNIGIMAHIDAGKTTTTERIIYYTGKTHKIGDVdsGNTVTDWMTQEQDRGITISSAAITCYWKDHQINIIDTPGHVDF 81
Cdd:cd01891     1 KIRNIAIIAHVDHGKTTLVDALLKQSGTFRENEEV--GERVMDSNDLERERGITILAKNTAITYKDTKINIIDTPGHADF 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1021452772  82 TAEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYVNKMDRVGANFFKVVEDI 144
Cdd:cd01891    79 GGEVERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDRPDARPEEVVDEV 141
EFG_mtEFG_II cd04088
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation ...
301-384 7.00e-31

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: 115.70  E-value: 7.00e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 301 LSALVFKVQYfSAIAAHLYFIRVYSGELSSSKRVLNIAKNKREKFTRIFRVFSNKNEQIDEVKAGDIGAVIGLKYSITGD 380
Cdd:cd04088     1 FSALVFKTMA-DPFVGKLTFFRVYSGTLKSGSTVYNSTKGKKERVGRLLRMHGKKREEVEELGAGDIGAVVGLKDTRTGD 79

                  ....
gi 1021452772 381 TLVE 384
Cdd:cd04088    80 TLCD 83
EFG_III cd16262
Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial ...
397-472 3.80e-29

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: 110.24  E-value: 3.80e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021452772 397 PEPVVLISIEPERASDDGRLKEVLEIITKEDPTFSYKESKETGQLLVSGMGELHLEIIVMRIRDDFKLNVYTGKPQ 472
Cdd:cd16262     1 PEPVISLAIEPKTKADEDKLSKALARLAEEDPTLRVSRDEETGQTILSGMGELHLEIIVERLKREYGVEVEVGKPQ 76
PRK10218 PRK10218
translational GTPase TypA;
3-477 3.47e-28

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 119.81  E-value: 3.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   3 IRNIGIMAHIDAGKTTTTERIIYYTGKTHkiGDVDSGNTVTDWMTQEQDRGITISSAAITCYWKDHQINIIDTPGHVDFT 82
Cdd:PRK10218    5 LRNIAIIAHVDHGKTTLVDKLLQQSGTFD--SRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  83 AEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYVNKMDRVGAnffkvvedirnkfgivpivlqipigse 162
Cdd:PRK10218   83 GEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGA--------------------------- 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 163 nnfegvidiirnkelhfelrdgkpivledvvREEFVenvkifkenlidslsnfSERITELFLENSVIDDSLIIEEIRRCT 242
Cdd:PRK10218  136 -------------------------------RPDWV-----------------VDQVFDLFVNLDATDEQLDFPIVYASA 167
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 243 ISGfiipvLMGTSLKNIG--IEPLIDAIVDYLPSPfekkinayslktdrSVSIEPKDEKRLSALVFKvQYFSAIAAHlyf 320
Cdd:PRK10218  168 LNG-----IAGLDHEDMAedMTPLYQAIVDHVPAP--------------DVDLDGPFQMQISQLDYN-SYVGVIGIG--- 224
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 321 iRVYSGELSSSKRVLNIAKNKREKFTRIFRVFSNKN-EQIDE--VKAGDIGAVIGLKYSITGDTLVEEGNEIMLEPLVFP 397
Cdd:PRK10218  225 -RIKRGKVKPNQQVTIIDSEGKTRNAKVGKVLGHLGlERIETdlAEAGDIVAITGLGELNISDTVCDTQNVEALPALSVD 303
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 398 EPVV----LISIEPeRASDDGRL---KEVLEIITKE---DPTFSYKESKETGQLLVSGMGELHLEIIV--MRiRDDFKLN 465
Cdd:PRK10218  304 EPTVsmffCVNTSP-FCGKEGKFvtsRQILDRLNKElvhNVALRVEETEDADAFRVSGRGELHLSVLIenMR-REGFELA 381
                         490
                  ....*....|..
gi 1021452772 466 VytGKPQVSYRE 477
Cdd:PRK10218  382 V--SRPKVIFRE 391
EFG_III pfam14492
Elongation Factor G, domain III; This domain is found in Elongation Factor G. It shares a ...
396-470 5.11e-26

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: 101.40  E-value: 5.11e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1021452772 396 FPEPVVLISIEPERASDDGRLKEVLEIITKEDPTFSYKESKETGQLLVSGMGELHLEIIVMRIRDDFKLNVYTGK 470
Cdd:pfam14492   1 FPEPVISVAIEPKTKGDEDKLSKALNRLLEEDPTLRVERDEETGETILSGMGELHLEIVVDRLKRKYGVEVELGP 75
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
4-132 3.22e-25

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: 103.89  E-value: 3.22e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   4 RNIGIMAHIDAGKTTTTERIIYYTGK-THKIGDVDSGNTVTDWMTQEQDRGITISSAAITCYW-----KDHQINIIDTPG 77
Cdd:cd04167     1 RNVCIAGHLHHGKTSLLDMLIEQTHKrTPSVKLGWKPLRYTDTRKDEQERGISIKSNPISLVLedskgKSYLINIIDTPG 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1021452772  78 HVDFTAEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYVNKMDR 132
Cdd:cd04167    81 HVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDR 135
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
3-174 7.07e-25

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: 101.29  E-value: 7.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   3 IRNIGIMAHIDAGKTTTTERIIYYTGKTHKIGdvdSGNTVTDWMTQEQDRGITIssaaitcywkdhQINIIDTPGHVDF- 81
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYY---PGTTRNYVTTVIEEDGKTY------------KFNLLDTAGQEDYd 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  82 ------TAEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQAsKYGIPRLAYVNKMDRVGANFFKVVEDIRNKFGIVPIVl 155
Cdd:TIGR00231  66 airrlyYPQVERSLRVFDIVILVLDVEEILEKQTKEIIHHA-DSGVPIILVGNKIDLKDADLKTHVASEFAKLNGEPII- 143
                         170
                  ....*....|....*....
gi 1021452772 156 QIPIGSENNFEGVIDIIRN 174
Cdd:TIGR00231 144 PLSAETGKNIDSAFKIVEA 162
EFG_mtEFG_C cd03713
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational ...
591-666 1.93e-23

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: 94.13  E-value: 1.93e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021452772 591 EPIMILEIRTPIEYTGEVVSTLNFVGGMIHSISNIEDYEIIKAEAAFEKLFGYTSILRSATKGRGVFTMEFSYFKE 666
Cdd:cd03713     1 EPIMKVEVTVPEEYMGDVIGDLSSRRGQILGTESRGGWKVIKAEVPLAEMFGYSTDLRSLTQGRGSFTMEFSHYEE 76
EFG_like_IV cd01680
Elongation Factor G-like domain IV. This family includes the translational elongation factor ...
475-585 3.19e-19

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: 83.45  E-value: 3.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 475 YRESLSVTVNDVFEFVNMFAGKELNLKIGMIVSPLMRGEGNKIEFECNVEPL---FKAAILRGITSSFSSGI-IGYPIID 550
Cdd:cd01680     1 YRETIRKSVEATGEFERELGGKPQFGEVTLRVEPLERGSGVRVVDPVDEELLpaeLKEAVEEGIRDACASGPlTGYPLTD 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1021452772 551 VGVKITSLDYDKSKVNESVIESIAGLAFNEFFKRA 585
Cdd:cd01680    81 VRVTVLDVPYHEGVSTEAGFRAAAGRAFESAAQKA 115
EFG_C smart00838
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ...
590-666 5.15e-19

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: 81.78  E-value: 5.15e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1021452772  590 LEPIMILEIRTPIEYTGEVVSTLNFVGGMIHSISNIEDYEIIKAEAAFEKLFGYTSILRSATKGRGVFTMEFSYFKE 666
Cdd:smart00838   2 LEPIMKVEVTVPEEYMGDVIGDLNSRRGKIEGMEQRGGAQVIKAKVPLSEMFGYATDLRSATQGRATWSMEFSHYEE 78
mtEFG1_C cd04097
mtEFG1_C: C-terminus of mitochondrial Elongation factor G1 (mtEFG1)-like proteins found in ...
591-662 6.08e-18

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: 78.52  E-value: 6.08e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1021452772 591 EPIMILEIRTPIEYTGEVVSTLNFVGGMIHSISNIEDYEIIKAEAAFEKLFGYTSILRSATKGRGVFTMEFS 662
Cdd:cd04097     1 EPIMKVEVTAPTEFQGNVIGLLNKRKGTIVDTDTGEDEFTLEAEVPLNDMFGYSTELRSMTQGKGEFSMEFS 72
mtEFG2_II_like cd04092
Domain II of mitochondrial elongation factor G2-like proteins found in eukaryotes; Eukaryotic ...
301-383 1.19e-17

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: 78.13  E-value: 1.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 301 LSALVFKVQYfSAIAAHLYFIRVYSGELSSSKRVLNIAKNKREKFTRIFRVFSNKNEQIDEVKAGDIGAVIGLKYSITGD 380
Cdd:cd04092     1 LCALAFKVIH-DPQRGPLVFVRVYSGTLKAGSNVYNTTTGKKERISRLLKMHADQTEEVDSLSAGNIGVITGLKVTSTGD 79

                  ...
gi 1021452772 381 TLV 383
Cdd:cd04092    80 TLV 82
EF2_snRNP_III cd16261
Domain III of Elongation Factor 2 (EF2); This model represents domain III of Elongation factor ...
399-462 1.31e-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: 71.83  E-value: 1.31e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021452772 399 PVVLISIEPERASDDGRLKEVLEIITKEDPTFSYKeSKETGQLLVSGMGELHLEIIVMRIRDDF 462
Cdd:cd16261     1 PVVRVAVEPKNPSDLPKLVEGLKKLAKSDPTVQVK-IEEEGEHLIAGAGELHLEICLKDLKEDF 63
EFG_C pfam00679
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ...
588-666 2.75e-15

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: 71.42  E-value: 2.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 588 IKLEPIMILEIRTPIEYTGEVVSTLNFVGG-MIHSISNIEDYEIIKAEAAFEKLFGYTSILRSATKGRGVFTMEFSYFKE 666
Cdd:pfam00679   1 VLLEPIEKVTIDVPEEYVGDVISDLNSRRGeILDMDPDDGGRVVIEAEVPLAELFGFATELRSLTKGRGSFSMEFSGYQP 80
Elongation_Factor_C cd01514
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ...
591-666 4.07e-15

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: 70.59  E-value: 4.07e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1021452772 591 EPIMILEIRTPIEYTGEVVSTLNFVGGMIHSISNIE-DYEIIKAEAAFEKLFGYTSILRSATKGRGVFTMEFSYFKE 666
Cdd:cd01514     1 EPIMKVEITVPEEYLGAVIGDLSKRRGEILGMEPRGtGRVVIKAELPLAEMFGFATDLRSLTQGRASFSMEFSHYEP 77
PLN03127 PLN03127
Elongation factor Tu; Provisional
5-133 5.86e-13

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 71.39  E-value: 5.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   5 NIGIMAHIDAGKTTTTERIiyytgkTHKIGDVDSGNTVT----DWMTQEQDRGITISSAAITCYWKDHQINIIDTPGHVD 80
Cdd:PLN03127   63 NVGTIGHVDHGKTTLTAAI------TKVLAEEGKAKAVAfdeiDKAPEEKARGITIATAHVEYETAKRHYAHVDCPGHAD 136
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1021452772  81 FTAEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLA-YVNKMDRV 133
Cdd:PLN03127  137 YVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVvFLNKVDVV 190
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
5-134 1.45e-12

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: 69.96  E-value: 1.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   5 NIGIMAHIDAGKTTTTERIIYYTG-------KTHKIGDVDSGNT------VTDWMTQEQDRGITISSAAITCYWKDHQIN 71
Cdd:COG5256     9 NLVVIGHVDHGKSTLVGRLLYETGaidehiiEKYEEEAEKKGKEsfkfawVMDRLKEERERGVTIDLAHKKFETDKYYFT 88
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021452772  72 IIDTPGHVDFTAEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLA-YVNKMDRVG 134
Cdd:COG5256    89 IIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIvAVNKMDAVN 152
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
5-154 2.80e-12

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: 66.07  E-value: 2.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   5 NIGIMAHIDAGKTTTTERIIYY-----TGKTHKIGDVDSGntvtdwmTQEQDRGITISSAAI-----TCYWKdHqiniID 74
Cdd:cd01884     4 NVGTIGHVDHGKTTLTAAITKVlakkgGAKAKKYDEIDKA-------PEEKARGITINTAHVeyetaNRHYA-H----VD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  75 TPGHVDF-------TAEverslrvLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLA-YVNKMDRVG-ANFFKVVE-DI 144
Cdd:cd01884    72 CPGHADYiknmitgAAQ-------MDGAILVVSATDGPMPQTREHLLLARQVGVPYIVvFLNKADMVDdEELLELVEmEV 144
                         170
                  ....*....|....*..
gi 1021452772 145 R---NKFGI----VPIV 154
Cdd:cd01884   145 RellSKYGFdgddTPIV 161
EFG_III-like cd16257
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G ...
399-464 2.18e-11

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: 59.67  E-value: 2.18e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021452772 399 PVVLISIEPERASDDGRLKEVLEIITKEDPTFSYKESKETGQLLVSGMGELHLEIIVMRIRDDFKL 464
Cdd:cd16257     1 PVVFVTVEVKNPLDQEKLLEGLERLSEEDPALQVYREESTGEFILSGLGELHLEIIVARLEREYGV 66
PLN03126 PLN03126
Elongation factor Tu; Provisional
5-133 2.29e-11

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 66.56  E-value: 2.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   5 NIGIMAHIDAGKTTTTERIIYY-----TGKTHKIGDVDSGntvtdwmTQEQDRGITISSAAITCYWKDHQINIIDTPGHV 79
Cdd:PLN03126   83 NIGTIGHVDHGKTTLTAALTMAlasmgGSAPKKYDEIDAA-------PEERARGITINTATVEYETENRHYAHVDCPGHA 155
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1021452772  80 DFTAEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRL-AYVNKMDRV 133
Cdd:PLN03126  156 DYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMvVFLNKQDQV 210
mtEFG1_II_like cd04091
Domain II of mitochondrial elongation factor G1-like proteins found in eukaryotes; Eukaryotic ...
318-383 2.57e-11

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: 59.99  E-value: 2.57e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021452772 318 LYFIRVYSGELSSSKRVLNIAKNKREKFTRIFRVFSNKNEQIDEVKAGDIGAVIGLKYSiTGDTLV 383
Cdd:cd04091    16 LTYMRVYQGVLRKGDTIYNVRTGKKVRVPRLVRMHSDEMEDIEEVYAGDICALFGIDCA-SGDTFT 80
PRK12736 PRK12736
elongation factor Tu; Reviewed
5-134 6.94e-11

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 64.58  E-value: 6.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   5 NIGIMAHIDAGKTTTTERIIYYTGKThkigdvdSGNTVTDW-----MTQEQDRGITISSAAITCYWKDHQINIIDTPGHV 79
Cdd:PRK12736   14 NIGTIGHVDHGKTTLTAAITKVLAER-------GLNQAKDYdsidaAPEEKERGITINTAHVEYETEKRHYAHVDCPGHA 86
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1021452772  80 DFTAEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRL-AYVNKMDRVG 134
Cdd:PRK12736   87 DYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLvVFLNKVDLVD 142
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
5-133 7.32e-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: 64.41  E-value: 7.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   5 NIGIMAHIDAGKTTTTERII-----YYTGKTHKIGDVDSGntvtdwmTQEQDRGITISSAAITCYWKDHQINIIDTPGHV 79
Cdd:TIGR00485  14 NVGTIGHVDHGKTTLTAAITtvlakEGGAAARAYDQIDNA-------PEEKARGITINTAHVEYETETRHYAHVDCPGHA 86
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1021452772  80 DFTAEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRL-AYVNKMDRV 133
Cdd:TIGR00485  87 DYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIvVFLNKCDMV 141
EFG_IV pfam03764
Elongation factor G, domain IV; This domain is found in elongation factor G, elongation factor ...
471-586 9.15e-11

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: 59.54  E-value: 9.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 471 PQVSYRESLSVTVNDV-FEFVNMFAGKELNLKIGMIVSPLMRGEGNkiEFE-----CNVEPLFKAAILRGITSSFSSGII 544
Cdd:pfam03764   1 PQVAYRETIRKPVKERaYKHKKQSGGDGQYARVILRIEPLPPGSGN--EFVdetvgGQIPKEFIPAVEKGFQEAMKEGPL 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1021452772 545 -GYPIIDVGVKITSLDYDKSKVNESVIESIAGLAFNEFFKRAN 586
Cdd:pfam03764  79 aGEPVTDVKVTLLDGSYHEVDSSEAAFIPAARRAFREALLKAS 121
infB CHL00189
translation initiation factor 2; Provisional
6-172 1.20e-10

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 64.85  E-value: 1.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   6 IGIMAHIDAGKTTTTERIiyytgkthkigdvdsGNTVTdwmTQEQDRGITISSAAITCYWK----DHQINIIDTPGHVDF 81
Cdd:CHL00189  247 VTILGHVDHGKTTLLDKI---------------RKTQI---AQKEAGGITQKIGAYEVEFEykdeNQKIVFLDTPGHEAF 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  82 TAEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYVNKMDRVGANFFKVVEDIrNKFGIVPI-----VLQ 156
Cdd:CHL00189  309 SSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANTERIKQQL-AKYNLIPEkwggdTPM 387
                         170
                  ....*....|....*...
gi 1021452772 157 IPIGS--ENNFEGVIDII 172
Cdd:CHL00189  388 IPISAsqGTNIDKLLETI 405
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
8-152 1.75e-10

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: 60.18  E-value: 1.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   8 IMAHIDAGKTTTTERIiyytGKThKIGDVDSGntvtdwmtqeqdrGIT--ISSAAITCYWKDHQINIIDTPGHVDFTAEV 85
Cdd:cd01887     5 VMGHVDHGKTTLLDKI----RKT-NVAAGEAG-------------GITqhIGAYQVPIDVKIPGITFIDTPGHEAFTNMR 66
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  86 ERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYVNKMDR---VGANFFKVVEDIrNKFGIVP 152
Cdd:cd01887    67 ARGASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKpygTEADPERVKNEL-SELGLVG 135
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
5-133 2.59e-10

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 63.02  E-value: 2.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   5 NIGIMAHIDAGKTTTTERIIYYTG-------KTHKIGDVDSGNT------VTDWMTQEQDRGITISSAAITCYWKDHQIN 71
Cdd:PRK12317    8 NLAVIGHVDHGKSTLVGRLLYETGaidehiiEELREEAKEKGKEsfkfawVMDRLKEERERGVTIDLAHKKFETDKYYFT 87
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021452772  72 IIDTPGHVDFTAEVERSLRVLDGGIVVFSAVD--GIQAQT-ETVWrQASKYGIPRLA-YVNKMDRV 133
Cdd:PRK12317   88 IVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTrEHVF-LARTLGINQLIvAINKMDAV 152
tufA CHL00071
elongation factor Tu
5-133 3.92e-10

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 62.28  E-value: 3.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   5 NIGIMAHIDAGKTTTTERIIYY-----TGKTHKIGDVDSGntvtdwmTQEQDRGITISSAAITCYWKDHQINIIDTPGHV 79
Cdd:CHL00071   14 NIGTIGHVDHGKTTLTAAITMTlaakgGAKAKKYDEIDSA-------PEEKARGITINTAHVEYETENRHYAHVDCPGHA 86
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1021452772  80 DFTAEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRL-AYVNKMDRV 133
Cdd:CHL00071   87 DYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIvVFLNKEDQV 141
EFG_IV smart00889
Elongation factor G, domain IV; Translation elongation factors are responsible for two main ...
472-586 1.54e-09

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: 56.01  E-value: 1.54e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  472 QVSYRESLSVTVNDV-FEFVNMFAGKELNLKIGMIVSPLMRGEGNKIEFEC--NVEPL-FKAAILRGITSSFSSGII-GY 546
Cdd:smart00889   1 QVAYRETITKPVKEAeGKHKKQSGGDGQYARVILEVEPLERGSGFEFDDTIvgGVIPKeYIPAVEKGFREALEEGPLaGY 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1021452772  547 PIIDVGVKITSLDYDKSKVNESVIESIAGLAFNEFFKRAN 586
Cdd:smart00889  81 PVVDVKVTLLDGSYHEVDSSEMAFKPAARRAFKEALLKAG 120
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
6-148 2.56e-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 bacterial SelBs, as well as, one from archaea.


Pssm-ID: 206734 [Multi-domain]  Cd Length: 170  Bit Score: 56.84  E-value: 2.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   6 IGIMAHIDAGKTTTTERIiyyTGKThkigdvdsgntvTDWMTQEQDRGITIS-SAAITCYWKDHQINIIDTPGHVDFTAE 84
Cdd:cd04171     2 IGTAGHIDHGKTTLIKAL---TGIE------------TDRLPEEKKRGITIDlGFAYLDLPDGKRLGFIDVPGHEKFVKN 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021452772  85 VERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYV-NKMDRVGANFF-KVVEDIRNKF 148
Cdd:cd04171    67 MLAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVlTKADLVDEDRLeLVEEEILELL 132
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
5-142 4.78e-09

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: 59.50  E-value: 4.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   5 NIGIMAHIDAGKTTTTERIiyyTGkthkigdvdsgnTVTDWMTQEQDRGITISSAAITCYWKDHQINIIDTPGHVDFTAE 84
Cdd:TIGR00475   2 IIATAGHVDHGKTTLLKAL---TG------------IAADRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISN 66
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1021452772  85 VERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRL-AYVNKMDRVGANFFKVVE 142
Cdd:TIGR00475  67 AIAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTiVVITKADRVNEEEIKRTE 125
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
5-133 7.44e-09

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: 58.24  E-value: 7.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   5 NIGIMAHIDAGKTTTTERIIYYTGKTH-----KIGDVDSGntvtdwmTQEQDRGITISSAAITcYWKD-----HqiniID 74
Cdd:COG0050    14 NIGTIGHVDHGKTTLTAAITKVLAKKGgakakAYDQIDKA-------PEEKERGITINTSHVE-YETEkrhyaH----VD 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1021452772  75 TPGHVDF-------TAEverslrvLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLA-YVNKMDRV 133
Cdd:COG0050    82 CPGHADYvknmitgAAQ-------MDGAILVVSATDGPMPQTREHILLARQVGVPYIVvFLNKCDMV 141
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
11-159 1.16e-08

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: 55.65  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  11 HIDAGKTTTTERIIY-----YTGKTHKIGDVDSGNT---------VTDWMTQEQDRGITISSAAITCYWKDHQINIIDTP 76
Cdd:cd04166     7 SVDDGKSTLIGRLLYdsksiFEDQLAALERSKSSGTqgekldlalLVDGLQAEREQGITIDVAYRYFSTPKRKFIIADTP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  77 GHVDFTAEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAY-VNKMDRVG---ANFFKVVEDIR---NKFG 149
Cdd:cd04166    87 GHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVaVNKMDLVDydeEVFEEIKADYLafaASLG 166
                         170
                  ....*....|
gi 1021452772 150 IVPIVLqIPI 159
Cdd:cd04166   167 IEDITF-IPI 175
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
5-137 3.25e-08

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: 54.42  E-value: 3.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   5 NIGIMAHIDAGKTTTTERIIYytgkthKIGDVDSGNT-------------------VTDWMTQEQDRGITISSAAITCYW 65
Cdd:cd01883     1 NLVVIGHVDAGKSTLTGHLLY------KLGGVDKRTIekyekeakemgkesfkyawVLDKLKEERERGVTIDVGLAKFET 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  66 KDHQINIIDTPGHVDF-------TAEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLA-YVNKMDRVGANF 137
Cdd:cd01883    75 EKYRFTIIDAPGHRDFvknmitgASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIvAVNKMDDVTVNW 154
PRK00049 PRK00049
elongation factor Tu; Reviewed
5-133 3.59e-08

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 55.97  E-value: 3.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   5 NIGIMAHIDAGKTTTTERIIYYTGKTH-----KIGDVDSGntvtdwmTQEQDRGITISSAAITcYWKD-----HqiniID 74
Cdd:PRK00049   14 NVGTIGHVDHGKTTLTAAITKVLAKKGgaeakAYDQIDKA-------PEEKARGITINTAHVE-YETEkrhyaH----VD 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021452772  75 TPGHVDFTAEVERSLRVLDGGIVVFSAVDGIQAQTetvwRQ----ASKYGIPRL-AYVNKMDRV 133
Cdd:PRK00049   82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQT----REhillARQVGVPYIvVFLNKCDMV 141
Tet_II cd03690
Domain II of ribosomal protection proteins Tet(M) and Tet(O); This subfamily represents domain ...
298-382 5.59e-08

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: 50.70  E-value: 5.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 298 EKRLSALVFKVQYFSAiAAHLYFIRVYSGELSSSKRVLNIAKNKREKFTRIFRVFSNKNEQIDEVKAGDIGAVIGLKYSI 377
Cdd:cd03690     1 ESELSGTVFKIEYDPK-GERLAYLRLYSGTLRLRDSVRVSGEEEKIKITELRTFENGELVKVDRVYAGDIAILVGLKSLR 79

                  ....*
gi 1021452772 378 TGDTL 382
Cdd:cd03690    80 VGDVL 84
PRK12735 PRK12735
elongation factor Tu; Reviewed
5-133 1.48e-07

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 54.07  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   5 NIGIMAHIDAGKTTTTERIIYYTGKTHKIGDVDSGNtvTDWMTQEQDRGITISSAAITcYWKD-----HqiniIDTPGHV 79
Cdd:PRK12735   14 NVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQ--IDNAPEEKARGITINTSHVE-YETAnrhyaH----VDCPGHA 86
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1021452772  80 DFTAEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRL-AYVNKMDRV 133
Cdd:PRK12735   87 DYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIvVFLNKCDMV 141
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
5-137 5.30e-07

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 52.44  E-value: 5.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   5 NIGIMAHIDAGKTTTTERIIYytgkthKIGDVDSGNT-------------------VTDWMTQEQDRGITISSAaitcYW 65
Cdd:PTZ00141    9 NLVVIGHVDSGKSTTTGHLIY------KCGGIDKRTIekfekeaaemgkgsfkyawVLDKLKAERERGITIDIA----LW 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  66 K----DHQINIIDTPGHVDF-------TAEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAY-VNKMDRV 133
Cdd:PTZ00141   79 KfetpKYYFTIIDAPGHRDFiknmitgTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVcINKMDDK 158

                  ....
gi 1021452772 134 GANF 137
Cdd:PTZ00141  159 TVNY 162
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
7-154 1.73e-06

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: 48.22  E-value: 1.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   7 GIMAHIDAGKTTTTERIIYytgktHKIGDVDSGNTVTdwmtqeqdrgITISSAAITCYWKDHQINIIDTPGHVDF----- 81
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLG-----GEVGEVSDVPGTT----------RDPDVYVKELDKGKVKLVLVDTPGLDEFgglgr 65
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1021452772  82 TAEVERSLRVLDGGIVVFSAVDG--IQAQTETVWRQASKYGIPRLAYVNKMDRVGAN--FFKVVEDIRNKFGIVPIV 154
Cdd:cd00882    66 EELARLLLRGADLILLVVDSTDResEEDAKLLILRRLRKEGIPIILVGNKIDLLEERevEELLRLEELAKILGVPVF 142
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
320-383 8.22e-06

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


Pssm-ID: 427163 [Multi-domain]  Cd Length: 73  Bit Score: 44.18  E-value: 8.22e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021452772 320 FIRVYSGELSSSKRVLNIA-----KNKREKFTRIFRVFSNKNEQIDEVKAGDIGAVIGLKYSITGDTLV 383
Cdd:pfam03144   5 TGRVESGTLKKGDKVRILPngtgkKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
mtEFG2_like_IV cd01693
mtEF-G2 domain IV. This subfamily is a part the of mitochondrial transcriptional elongation ...
473-560 2.86e-05

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: 43.92  E-value: 2.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 473 VSYRESLSVTVNDVFEFVNMFAGKELNLKIGMIVSPLMRGEGNKIEFEC-----NVEPL-FKAAILRGITSSFSSG-IIG 545
Cdd:cd01693     1 IAYRETILEPARATDTLEKVIGDKKHSVTVTMEVRPNQASSSPVELIELansaiEVLLKrIQEAVENGVHSALLQGpLLG 80
                          90
                  ....*....|....*
gi 1021452772 546 YPIIDVGVKITSLDY 560
Cdd:cd01693    81 FPVQDVAITLHSLTI 95
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
5-109 3.36e-05

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: 45.05  E-value: 3.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   5 NIGIMAHIDAGKTTTTeRIIYYTGKThkigdvdsgnTVTDWMTQEQDRGITI----SS-------AAITCYWKDH---QI 70
Cdd:cd01889     2 NVGLLGHVDSGKTSLA-KALSEIAST----------AAFDKNPQSQERGITLdlgfSSfevdkpkHLEDNENPQIenyQI 70
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1021452772  71 NIIDTPGHVDFTAEVERSLRVLDGGIVVFSAVDGIQAQT 109
Cdd:cd01889    71 TLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQT 109
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
5-179 3.70e-05

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 46.62  E-value: 3.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   5 NIGIMAHIDAGKTTTTERIIYYTGKTHK---------IGDVDSGNT----VTDWMTQEQDRGITISSAAITCYWKDHQIN 71
Cdd:PLN00043    9 NIVVIGHVDSGKSTTTGHLIYKLGGIDKrvierfekeAAEMNKRSFkyawVLDKLKAERERGITIDIALWKFETTKYYCT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  72 IIDTPGHVDF-------TAEVERSLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRL-AYVNKMDRV-----GANFF 138
Cdd:PLN00043   89 VIDAPGHRDFiknmitgTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMiCCCNKMDATtpkysKARYD 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1021452772 139 KVVEDIRN---KFGIVPIvlQIPIGSENNFEGVIDIIRNKELHF 179
Cdd:PLN00043  169 EIVKEVSSylkKVGYNPD--KIPFVPISGFEGDNMIERSTNLDW 210
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
49-159 4.28e-05

Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and metabolism]; Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 442140 [Multi-domain]  Cd Length: 430  Bit Score: 46.23  E-value: 4.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  49 EQDRGITISSAAItcYW---KDHQInIIDTPGHVDFT---------AEVerslrvldgGIVVFSAVDGIQAQTetvwRQ- 115
Cdd:COG2895    76 EREQGITIDVAYR--YFstpKRKFI-IADTPGHEQYTrnmvtgastADL---------AILLIDARKGVLEQT----RRh 139
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1021452772 116 ---ASKYGIPR--LAyVNKMDRVG---ANFFKVVEDIR---NKFGIVPIVLqIPI 159
Cdd:COG2895   140 syiASLLGIRHvvVA-VNKMDLVDyseEVFEEIVADYRafaAKLGLEDITF-IPI 192
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
8-152 5.99e-05

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


Pssm-ID: 440298 [Multi-domain]  Cd Length: 502  Bit Score: 46.16  E-value: 5.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   8 IMAHIDAGKTTTTERIIyytgKThKIGDVDSGntvtdwmtqeqdrGITISSAAITCYWKDHQINIIDTPGHVDFTAEVER 87
Cdd:COG0532     9 VMGHVDHGKTSLLDAIR----KT-NVAAGEAG-------------GITQHIGAYQVETNGGKITFLDTPGHEAFTAMRAR 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1021452772  88 SLRVLDGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAYVNKMDRVGANffkvVEDIRN---KFGIVP 152
Cdd:COG0532    71 GAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVPIIVAINKIDKPGAN----PDRVKQelaEHGLVP 134
Tet_C cd03711
Tet_C: C-terminus of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology ...
591-662 2.46e-04

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: 39.91  E-value: 2.46e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1021452772 591 EPIMILEIRTPIEYTGEVVSTLNFVGGMIHSISNIEDYEIIKAEAAFEKLFGYTSILRSATKGRGVFTMEFS 662
Cdd:cd03711     1 EPYLRFELEVPQDALGRAMSDLAKMGATFEDPQIKGDEVTLEGTIPVATSQDYQSELPSYTHGEGVLETEFK 72
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
6-109 3.58e-04

Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 442507 [Multi-domain]  Cd Length: 630  Bit Score: 43.75  E-value: 3.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772   6 IGIMAHIDAGKTTTTERIiyyTGkthkigdVDsgntvTDWMTQEQDRGITI--SSAaitcYWK---DHQINIIDTPGHvd 80
Cdd:COG3276     3 IGTAGHIDHGKTTLVKAL---TG-------ID-----TDRLKEEKKRGITIdlGFA----YLPlpdGRRLGFVDVPGH-- 61
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1021452772  81 ftaevERSLR-VLDG--GI-----VVfSAVDGIQAQT 109
Cdd:COG3276    62 -----EKFIKnMLAGagGIdlvllVV-AADEGVMPQT 92
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
301-383 5.19e-04

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: 39.17  E-value: 5.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 301 LSALVFKVQYFSAIAAhLYFIRVYSGELSSSKRVLNIAKNKREKFTRIFRvfsnKNEQIDEVKAGDIGAVIGLKYS--IT 378
Cdd:cd01342     1 LVMQVFKVFYIPGRGR-VAGGRVESGTLKVGDEIRILPKGITGRVTSIER----FHEEVDEAKAGDIVGIGILGVKdiLT 75

                  ....*
gi 1021452772 379 GDTLV 383
Cdd:cd01342    76 GDTLT 80
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
53-129 5.78e-04

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: 39.91  E-value: 5.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  53 GITISSAAITCYWKDHQINIIDTPGHVDFTAE---VERSLRVL---DGGIVVFSAVDGIQAQTETVWRQASKYGIPRLAY 126
Cdd:pfam01926  31 GTTRDPNEGRLELKGKQIILVDTPGLIEGASEgegLGRAFLAIieaDLILFVVDSEEGITPLDEELLELLRENKKPIILV 110

                  ...
gi 1021452772 127 VNK 129
Cdd:pfam01926 111 LNK 113
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
11-109 6.51e-04

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 42.73  E-value: 6.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  11 HIDAGKTTTTERIiyyTGkthkigdVDsgntvTDWMTQEQDRGITISSAaiTCYWKDHQ---INIIDTPGHVDFTAEVER 87
Cdd:PRK10512    8 HVDHGKTTLLQAI---TG-------VN-----ADRLPEEKKRGMTIDLG--YAYWPQPDgrvLGFIDVPGHEKFLSNMLA 70
                          90       100
                  ....*....|....*....|..
gi 1021452772  88 SLRVLDGGIVVFSAVDGIQAQT 109
Cdd:PRK10512   71 GVGGIDHALLVVACDDGVMAQT 92
Tet_III cd16258
Domain III of Tetracycline resistance protein Tet; Tetracycline resistance proteins, including ...
399-466 2.31e-03

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: 36.92  E-value: 2.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1021452772 399 PVVLISIEPERASDDGRLKEVLEIITKEDPTFSYKESKETGQLLVSGMGELHLEIIVMRIRDDFKLNV 466
Cdd:cd16258     1 PMLQTTIRPRKPEQRERLLDALTELSDEDPLLKYRVDSTTHEIILSLYGEVQMEVISALLEEKYGVEV 68
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
33-173 2.61e-03

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 39.19  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  33 IGDVDSGNT------VTDWMTQEQD---RGITISSAAITCYWKDHQINIIDTPGHVDFTAE---VERSLRVLDGGIVVFS 100
Cdd:COG1100     9 VGTGGVGKTslvnrlVGDIFSLEKYlstNGVTIDKKELKLDGLDVDLVIWDTPGQDEFRETrqfYARQLTGASLYLFVVD 88
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021452772 101 AVDGIQAQTETVWRQ--ASKYGIPRLAYV-NKMDRVGANFFKVVEDIRNKFGIVPIVLQIPIGSENNfEGVIDIIR 173
Cdd:COG1100    89 GTREETLQSLYELLEslRRLGKKSPIILVlNKIDLYDEEEIEDEERLKEALSEDNIVEVVATSAKTG-EGVEELFA 163
BipA_TypA_C cd03710
BipA_TypA_C: a C-terminal portion of BipA or TypA having homology to the C terminal domains of ...
591-662 4.44e-03

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


Pssm-ID: 239681 [Multi-domain]  Cd Length: 79  Bit Score: 36.33  E-value: 4.44e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1021452772 591 EPIMILEIRTPIEYTGEVVSTLNFVGG-MIHSISNIEDYEIIKAEAAFEKLFGYTSILRSATKGRGVFTMEFS 662
Cdd:cd03710     1 EPIEELTIDVPEEYSGAVIEKLGKRKGeMVDMEPDGNGRTRLEFKIPSRGLIGFRSEFLTDTRGTGIMNHVFD 73
RalA_RalB cd04139
Ral (Ras-like) family containing highly homologous RalA and RalB; The Ral (Ras-like) subfamily ...
64-131 5.31e-03

Ral (Ras-like) family containing highly homologous RalA and RalB; The Ral (Ras-like) subfamily consists of the highly homologous RalA and RalB. Ral proteins are believed to play a crucial role in tumorigenesis, metastasis, endocytosis, and actin cytoskeleton dynamics. Despite their high sequence similarity (>80% sequence identity), nonoverlapping and opposing functions have been assigned to RalA and RalBs in tumor migration. In human bladder and prostate cancer cells, RalB promotes migration while RalA inhibits it. A Ral-specific set of GEFs has been identified that are activated by Ras binding. This RalGEF activity is enhanced by Ras binding to another of its target proteins, phosphatidylinositol 3-kinase (PI3K). Ral effectors include RLIP76/RalBP1, a Rac/cdc42 GAP, and the exocyst (Sec6/8) complex, a heterooctomeric protein complex that is involved in tethering vesicles to specific sites on the plasma membrane prior to exocytosis. In rat kidney cells, RalB is required for functional assembly of the exocyst and for localizing the exocyst to the leading edge of migrating cells. In human cancer cells, RalA is required to support anchorage-independent proliferation and RalB is required to suppress apoptosis. RalA has been shown to localize to the plasma membrane while RalB is localized to the intracellular vesicles. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206710 [Multi-domain]  Cd Length: 163  Bit Score: 38.18  E-value: 5.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  64 YWK-------DHQINIIDTPGHVDFTAEVERSLRVLDGGIVVFS-----AVDGIQAQTETVWRQASKYGIPRLAYVNKMD 131
Cdd:cd04139    37 YRKkvvldgeEVQLNILDTAGQEDYAAIRDNYFRSGEGFLLVFSitdmeSFTALAEFREQILRVKEDDNVPLLLVGNKCD 116
Tet_like_IV cd01684
EF-G_domain IV_RPP domain is a part of bacterial ribosomal protected proteins (RPP) family. ...
502-557 8.37e-03

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: 36.50  E-value: 8.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1021452772 502 IGMIVSPLMRGEGNKIEFECNVEPL---FKAAILRGITSSFSSGIIGYPIIDVGVKITS 557
Cdd:cd01684    28 VGLRVEPLPRGSGLQYESEVSLGSLprsFQNAVEETVRETLQQGLYGWEVTDCKVTLTY 86
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
53-154 9.21e-03

EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. 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. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.


Pssm-ID: 206682 [Multi-domain]  Cd Length: 174  Bit Score: 37.80  E-value: 9.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772  53 GITISSAAITCYWKDHQINIIDTPG-----HVDFTAE---VERSLRVLDGG---IVVFSAVDGIQAQTETVWRQASKYGI 121
Cdd:cd01895    35 GTTRDSIDVPFEYDGQKYTLIDTAGirkkgKVTEGIEkysVLRTLKAIERAdvvLLVLDASEGITEQDLRIAGLILEEGK 114
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1021452772 122 PRLAYVNKMDRVGAN---FFKVVEDIRNKFGI---VPIV 154
Cdd:cd01895   115 ALIIVVNKWDLVEKDektMKEFEKELRRKLPFldyAPIV 153
RF3_II cd03689
Domain II of bacterial Release Factor 3; This subfamily represents domain II of bacterial ...
301-384 9.35e-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: 35.71  E-value: 9.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021452772 301 LSALVFKVQ------YFSAIAahlyFIRVYSGELSSSKRVLNIAKNKREKFTRIFRVFSNKNEQIDEVKAGDIgavIGL- 373
Cdd:cd03689     1 FSGFVFKIQanmdpkHRDRIA----FLRVCSGKFERGMKVKHVRTGKEVRLSNATTFMAQDRETVEEAYPGDI---IGLp 73
                          90
                  ....*....|....
gi 1021452772 374 ---KYSItGDTLVE 384
Cdd:cd03689    74 nhgTFQI-GDTFTE 86
 
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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