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Conserved domains on  [gi|1718559237|ref|WP_144958240|]
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MULTISPECIES: elongation factor G [Pseudomonas]

Protein Classification

elongation factor G( domain architecture ID 11422284)

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
1-700 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: 1308.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237   1 MArTTAINRYRNIGICAHVDAGKTTTTERILFYTGVNHKMGEVHDGAATMDWMVQEQERGITITSAATTAFWSGstkqyd 80
Cdd:COG0480     1 MA-EYPLEKIRNIGIVAHIDAGKTTLTERILFYTGAIHRIGEVHDGNTVMDWMPEEQERGITITSAATTCEWKG------ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  81 kYRVNIIDTPGHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDRAGANFLRVVEQIKK 160
Cdd:COG0480    74 -HKINIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQLKE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 161 RLGHTPVPVQLAIGAEENFQGQIDLLKMKAIFWnDDDQGMTYREEEIPADMLADAEQWRSNMVEAAAEANEELMNKYLEE 240
Cdd:COG0480   153 RLGANPVPLQLPIGAEDDFKGVIDLVTMKAYVY-DDELGAKYEEEEIPAELKEEAEEAREELIEAVAETDDELMEKYLEG 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 241 GELSIDEIKAGLRQRTIACEIVPAVCGSSFKNKGVPLVLDAVIDFLPAPIEIPAIKGTNPDNEEiTDERHADDNEPFSAL 320
Cdd:COG0480   232 EELTEEEIKAGLRKATLAGKIVPVLCGSAFKNKGVQPLLDAVVDYLPSPLDVPAIKGVDPDTGE-EVERKPDDDEPFSAL 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 321 AFKIATDPFVGTLTFARVYSGVLSSGDSVINSVKGKKERVGRMVQMHANTREEIKEVRAGDIAALIGMKDVTTGDTLCSI 400
Cdd:COG0480   311 VFKTMTDPFVGKLSFFRVYSGTLKSGSTVYNSTKGKKERIGRLLRMHGNKREEVDEAGAGDIVAVVKLKDTTTGDTLCDE 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 401 EKPIILERMDFPEPVISVAVEPKTKADQEKMGIALGKLAQEDPSFRVKTDEESGQTIISGMGELHLDILVDRMKREFGVE 480
Cdd:COG0480   391 DHPIVLEPIEFPEPVISVAIEPKTKADEDKLSTALAKLAEEDPTFRVETDEETGQTIISGMGELHLEIIVDRLKREFGVE 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 481 ANIGKPQVAYRETIRNTCEIEGKFVRQSGGRGQFGHCWIRFAPADEGqEGLEFVSEVVGGVIPKEYIPAIQKGIEEQMKN 560
Cdd:COG0480   471 VNVGKPQVAYRETIRKKAEAEGKHKKQSGGHGQYGDVWIEIEPLPRG-EGFEFVDKIVGGVIPKEYIPAVEKGIREAMEK 549
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 561 GIVAGYPLLGLKAAVFDGSYHDVDSNEMAFKIAASMATKQLTQKGGAVLLEPIMKVEVVTPEDYMGDVMGDLNRRRGLIQ 640
Cdd:COG0480   550 GVLAGYPVVDVKVTLYDGSYHPVDSSEMAFKIAASMAFKEAAKKAKPVLLEPIMKVEVTVPEEYMGDVMGDLNSRRGRIL 629
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 641 GMEDTVTGKVIRAEVPLGEMFGYATDVRSMSQGRASYSMEFSKYAEAPSNIAEAIIKKQA 700
Cdd:COG0480   630 GMESRGGAQVIKAEVPLAEMFGYATDLRSLTQGRGSFTMEFSHYEEVPANVAEKIIAKRK 689
 
Name Accession Description Interval E-value
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
1-700 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: 1308.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237   1 MArTTAINRYRNIGICAHVDAGKTTTTERILFYTGVNHKMGEVHDGAATMDWMVQEQERGITITSAATTAFWSGstkqyd 80
Cdd:COG0480     1 MA-EYPLEKIRNIGIVAHIDAGKTTLTERILFYTGAIHRIGEVHDGNTVMDWMPEEQERGITITSAATTCEWKG------ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  81 kYRVNIIDTPGHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDRAGANFLRVVEQIKK 160
Cdd:COG0480    74 -HKINIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQLKE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 161 RLGHTPVPVQLAIGAEENFQGQIDLLKMKAIFWnDDDQGMTYREEEIPADMLADAEQWRSNMVEAAAEANEELMNKYLEE 240
Cdd:COG0480   153 RLGANPVPLQLPIGAEDDFKGVIDLVTMKAYVY-DDELGAKYEEEEIPAELKEEAEEAREELIEAVAETDDELMEKYLEG 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 241 GELSIDEIKAGLRQRTIACEIVPAVCGSSFKNKGVPLVLDAVIDFLPAPIEIPAIKGTNPDNEEiTDERHADDNEPFSAL 320
Cdd:COG0480   232 EELTEEEIKAGLRKATLAGKIVPVLCGSAFKNKGVQPLLDAVVDYLPSPLDVPAIKGVDPDTGE-EVERKPDDDEPFSAL 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 321 AFKIATDPFVGTLTFARVYSGVLSSGDSVINSVKGKKERVGRMVQMHANTREEIKEVRAGDIAALIGMKDVTTGDTLCSI 400
Cdd:COG0480   311 VFKTMTDPFVGKLSFFRVYSGTLKSGSTVYNSTKGKKERIGRLLRMHGNKREEVDEAGAGDIVAVVKLKDTTTGDTLCDE 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 401 EKPIILERMDFPEPVISVAVEPKTKADQEKMGIALGKLAQEDPSFRVKTDEESGQTIISGMGELHLDILVDRMKREFGVE 480
Cdd:COG0480   391 DHPIVLEPIEFPEPVISVAIEPKTKADEDKLSTALAKLAEEDPTFRVETDEETGQTIISGMGELHLEIIVDRLKREFGVE 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 481 ANIGKPQVAYRETIRNTCEIEGKFVRQSGGRGQFGHCWIRFAPADEGqEGLEFVSEVVGGVIPKEYIPAIQKGIEEQMKN 560
Cdd:COG0480   471 VNVGKPQVAYRETIRKKAEAEGKHKKQSGGHGQYGDVWIEIEPLPRG-EGFEFVDKIVGGVIPKEYIPAVEKGIREAMEK 549
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 561 GIVAGYPLLGLKAAVFDGSYHDVDSNEMAFKIAASMATKQLTQKGGAVLLEPIMKVEVVTPEDYMGDVMGDLNRRRGLIQ 640
Cdd:COG0480   550 GVLAGYPVVDVKVTLYDGSYHPVDSSEMAFKIAASMAFKEAAKKAKPVLLEPIMKVEVTVPEEYMGDVMGDLNSRRGRIL 629
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 641 GMEDTVTGKVIRAEVPLGEMFGYATDVRSMSQGRASYSMEFSKYAEAPSNIAEAIIKKQA 700
Cdd:COG0480   630 GMESRGGAQVIKAEVPLAEMFGYATDLRSLTQGRGSFTMEFSHYEEVPANVAEKIIAKRK 689
EF-G TIGR00484
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ...
1-698 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: 1176.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237   1 MARTTAINRYRNIGICAHVDAGKTTTTERILFYTGVNHKMGEVHDGAATMDWMVQEQERGITITSAATTAFWSGstkqyd 80
Cdd:TIGR00484   1 MARTTDLNRFRNIGISAHIDAGKTTTTERILFYTGRIHKIGEVHDGAATMDWMEQEKERGITITSAATTVFWKG------ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  81 kYRVNIIDTPGHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDRAGANFLRVVEQIKK 160
Cdd:TIGR00484  75 -HRINIIDTPGHVDFTVEVERSLRVLDGAVAVLDAVGGVQPQSETVWRQANRYEVPRIAFVNKMDKTGANFLRVVNQIKQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 161 RLGHTPVPVQLAIGAEENFQGQIDLLKMKAIFWNDDdQGMTYREEEIPADMLADAEQWRSNMVEAAAEANEELMNKYLEE 240
Cdd:TIGR00484 154 RLGANAVPIQLPIGAEDNFIGVIDLVEMKAYFFNGD-KGTKAIEKEIPSDLLEQAKELRENLVEAVAEFDEELMEKYLEG 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 241 GELSIDEIKAGLRQRTIACEIVPAVCGSSFKNKGVPLVLDAVIDFLPAPIEIPAIKGTNPDNEEiTDERHADDNEPFSAL 320
Cdd:TIGR00484 233 EELTIEEIKNAIRKGVLNCEFFPVLCGSAFKNKGVQLLLDAVVDYLPSPTDVPAIKGIDPDTEK-EIERKASDDEPFSAL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 321 AFKIATDPFVGTLTFARVYSGVLSSGDSVINSVKGKKERVGRMVQMHANTREEIKEVRAGDIAALIGMKDVTTGDTLCSI 400
Cdd:TIGR00484 312 AFKVATDPFVGQLTFVRVYSGVLKSGSYVKNSRKNKKERVGRLVKMHANNREEIKEVRAGDICAAIGLKDTTTGDTLCDP 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 401 EKPIILERMDFPEPVISVAVEPKTKADQEKMGIALGKLAQEDPSFRVKTDEESGQTIISGMGELHLDILVDRMKREFGVE 480
Cdd:TIGR00484 392 KIDVILERMEFPEPVISLAVEPKTKADQEKMGIALGKLAEEDPTFRTFTDPETGQTIIAGMGELHLDIIVDRMKREFKVE 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 481 ANIGKPQVAYRETIRNTCEIEGKFVRQSGGRGQFGHCWIRFAPADEgqEGLEFVSEVVGGVIPKEYIPAIQKGIEEQMKN 560
Cdd:TIGR00484 472 ANVGAPQVAYRETIRSKVEVEGKHAKQSGGRGQYGHVKIRFEPLEP--KGYEFVNEIKGGVIPREYIPAVDKGLQEAMES 549
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 561 GIVAGYPLLGLKAAVFDGSYHDVDSNEMAFKIAASMATKQLTQKGGAVLLEPIMKVEVVTPEDYMGDVMGDLNRRRGLIQ 640
Cdd:TIGR00484 550 GPLAGYPVVDIKATLFDGSYHDVDSSEMAFKLAASLAFKEAGKKANPVLLEPIMKVEVEVPEEYMGDVMGDLSSRRGIIE 629
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1718559237 641 GMEDTVTGKVIRAEVPLGEMFGYATDVRSMSQGRASYSMEFSKYAEAPSNIAEAIIKK 698
Cdd:TIGR00484 630 GMEARGNVQKIKAEVPLSEMFGYATDLRSFTQGRGTYSMEFLHYGEVPSSVANEIIEK 687
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
17-697 0e+00

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 1102.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  17 AHVDAGKTTTTERILFYTGVNHKMGEVHDGAATMDWMVQEQERGITITSAATTAFWSGstkqydkYRVNIIDTPGHVDFT 96
Cdd:PRK12740    2 GHSGAGKTTLTEAILFYTGAIHRIGEVEDGTTTMDFMPEERERGISITSAATTCEWKG-------HKINLIDTPGHVDFT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  97 IEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDRAGANFLRVVEQIKKRLGHTPVPVQLAIGAE 176
Cdd:PRK12740   75 GEVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRAGADFFRVLAQLQEKLGAPVVPLQLPIGEG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 177 ENFQGQIDLLKMKAIFWnddDQGMTYREEEIPADMLADAEQWRSNMVEAAAEANEELMNKYLEEGELSIDEIKAGLRQRT 256
Cdd:PRK12740  155 DDFTGVVDLLSMKAYRY---DEGGPSEEIEIPAELLDRAEEAREELLEALAEFDDELMEKYLEGEELSEEEIKAGLRKAT 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 257 IACEIVPAVCGSSFKNKGVPLVLDAVIDFLPAPIEIPAIKGTNPDNEEitdERHADDNEPFSALAFKIATDPFVGTLTFA 336
Cdd:PRK12740  232 LAGEIVPVFCGSALKNKGVQRLLDAVVDYLPSPLEVPPVDGEDGEEGA---ELAPDPDGPLVALVFKTMDDPFVGKLSLV 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 337 RVYSGVLSSGDSVINSVKGKKERVGRMVQMHANTREEIKEVRAGDIAALIGMKDVTTGDTLCSIEKPIILERMDFPEPVI 416
Cdd:PRK12740  309 RVYSGTLKKGDTLYNSGTGKKERVGRLYRMHGKQREEVDEAVAGDIVAVAKLKDAATGDTLCDKGDPILLEPMEFPEPVI 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 417 SVAVEPKTKADQEKMGIALGKLAQEDPSFRVKTDEESGQTIISGMGELHLDILVDRMKREFGVEANIGKPQVAYRETIRN 496
Cdd:PRK12740  389 SLAIEPKDKGDEEKLSEALGKLAEEDPTLRVERDEETGQTILSGMGELHLDVALERLKREYGVEVETGPPQVPYRETIRK 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 497 TCEIEGKFVRQSGGRGQFGHCWIRFAPADEGqEGLEFVSEVVGGVIPKEYIPAIQKGIEEQMKNGIVAGYPLLGLKAAVF 576
Cdd:PRK12740  469 KAEGHGRHKKQSGGHGQFGDVWLEVEPLPRG-EGFEFVDKVVGGAVPRQYIPAVEKGVREALEKGVLAGYPVVDVKVTLT 547
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 577 DGSYHDVDSNEMAFKIAASMATKQLTQKGGAVLLEPIMKVEVVTPEDYMGDVMGDLNRRRGLIQGMEDTVTGKVIRAEVP 656
Cdd:PRK12740  548 DGSYHSVDSSEMAFKIAARLAFREALPKAKPVLLEPIMKVEVSVPEEFVGDVIGDLSSRRGRILGMESRGGGDVVRAEVP 627
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|.
gi 1718559237 657 LGEMFGYATDVRSMSQGRASYSMEFSKYAEAPSNIAEAIIK 697
Cdd:PRK12740  628 LAEMFGYATDLRSLTQGRGSFSMEFSHYEEVPGNVAEKVIA 668
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
12-289 2.52e-170

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: 488.15  E-value: 2.52e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  12 NIGICAHVDAGKTTTTERILFYTGVNHKMGEVHDGAATMDWMVQEQERGITITSAATTAFWSGstkqydkYRVNIIDTPG 91
Cdd:cd01886     1 NIGIIAHIDAGKTTTTERILYYTGRIHKIGEVHGGGATMDWMEQERERGITIQSAATTCFWKD-------HRINIIDTPG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  92 HVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDRAGANFLRVVEQIKKRLGHTPVPVQL 171
Cdd:cd01886    74 HVDFTIEVERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQIREKLGANPVPLQL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 172 AIGAEENFQGQIDLLKMKAIFWNDDDqGMTYREEEIPADMLADAEQWRSNMVEAAAEANEELMNKYLEEGELSIDEIKAG 251
Cdd:cd01886   154 PIGAEDDFEGVVDLIEMKALYWDGEL-GEKIEETDIPEDLLEEAEEAREELIETLAEVDDELMEKYLEGEEITEEEIKAA 232
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1718559237 252 LRQRTIACEIVPAVCGSSFKNKGVPLVLDAVIDFLPAP 289
Cdd:cd01886   233 IRKGTIANKIVPVLCGSAFKNKGVQPLLDAVVDYLPSP 270
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
8-288 1.41e-73

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: 235.88  E-value: 1.41e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237   8 NRYRNIGICAHVDAGKTTTTERILFYTGVNHKMGEVH-DGAATMDWMVQEQERGITITSAATTAFWsgstkqyDKYRVNI 86
Cdd:pfam00009   1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKgEGEAGLDNLPEERERGITIKSAAVSFET-------KDYLINL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  87 IDTPGHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDRA-GANFLRVVEQIKKRlght 165
Cdd:pfam00009  74 IDTPGHVDFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVdGAELEEVVEEVSRE---- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 166 pvpvqlaigaeenfqgqidllkmkaifwndddqgmtyreeeipadmladaeqwrsnmveaaaeaneeLMNKYLEEGelsi 245
Cdd:pfam00009 150 -------------------------------------------------------------------LLEKYGEDG---- 158
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1718559237 246 deikaglrqrtiacEIVPAVCGSSFKNKGVPLVLDAVIDFLPA 288
Cdd:pfam00009 159 --------------EFVPVVPGSALKGEGVQTLLDALDEYLPS 187
EFG_IV smart00889
Elongation factor G, domain IV; Translation elongation factors are responsible for two main ...
487-606 8.78e-51

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: 172.34  E-value: 8.78e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  487 QVAYRETIRNTC-EIEGKFVRQSGGRGQFGHCWIRFAPADEGqEGLEFVSEVVGGVIPKEYIPAIQKGIEEQMKNGIVAG 565
Cdd:smart00889   1 QVAYRETITKPVkEAEGKHKKQSGGDGQYARVILEVEPLERG-SGFEFDDTIVGGVIPKEYIPAVEKGFREALEEGPLAG 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1718559237  566 YPLLGLKAAVFDGSYHDVDSNEMAFKIAASMATKQLTQKGG 606
Cdd:smart00889  80 YPVVDVKVTLLDGSYHEVDSSEMAFKPAARRAFKEALLKAG 120
 
Name Accession Description Interval E-value
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
1-700 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: 1308.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237   1 MArTTAINRYRNIGICAHVDAGKTTTTERILFYTGVNHKMGEVHDGAATMDWMVQEQERGITITSAATTAFWSGstkqyd 80
Cdd:COG0480     1 MA-EYPLEKIRNIGIVAHIDAGKTTLTERILFYTGAIHRIGEVHDGNTVMDWMPEEQERGITITSAATTCEWKG------ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  81 kYRVNIIDTPGHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDRAGANFLRVVEQIKK 160
Cdd:COG0480    74 -HKINIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQLKE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 161 RLGHTPVPVQLAIGAEENFQGQIDLLKMKAIFWnDDDQGMTYREEEIPADMLADAEQWRSNMVEAAAEANEELMNKYLEE 240
Cdd:COG0480   153 RLGANPVPLQLPIGAEDDFKGVIDLVTMKAYVY-DDELGAKYEEEEIPAELKEEAEEAREELIEAVAETDDELMEKYLEG 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 241 GELSIDEIKAGLRQRTIACEIVPAVCGSSFKNKGVPLVLDAVIDFLPAPIEIPAIKGTNPDNEEiTDERHADDNEPFSAL 320
Cdd:COG0480   232 EELTEEEIKAGLRKATLAGKIVPVLCGSAFKNKGVQPLLDAVVDYLPSPLDVPAIKGVDPDTGE-EVERKPDDDEPFSAL 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 321 AFKIATDPFVGTLTFARVYSGVLSSGDSVINSVKGKKERVGRMVQMHANTREEIKEVRAGDIAALIGMKDVTTGDTLCSI 400
Cdd:COG0480   311 VFKTMTDPFVGKLSFFRVYSGTLKSGSTVYNSTKGKKERIGRLLRMHGNKREEVDEAGAGDIVAVVKLKDTTTGDTLCDE 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 401 EKPIILERMDFPEPVISVAVEPKTKADQEKMGIALGKLAQEDPSFRVKTDEESGQTIISGMGELHLDILVDRMKREFGVE 480
Cdd:COG0480   391 DHPIVLEPIEFPEPVISVAIEPKTKADEDKLSTALAKLAEEDPTFRVETDEETGQTIISGMGELHLEIIVDRLKREFGVE 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 481 ANIGKPQVAYRETIRNTCEIEGKFVRQSGGRGQFGHCWIRFAPADEGqEGLEFVSEVVGGVIPKEYIPAIQKGIEEQMKN 560
Cdd:COG0480   471 VNVGKPQVAYRETIRKKAEAEGKHKKQSGGHGQYGDVWIEIEPLPRG-EGFEFVDKIVGGVIPKEYIPAVEKGIREAMEK 549
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 561 GIVAGYPLLGLKAAVFDGSYHDVDSNEMAFKIAASMATKQLTQKGGAVLLEPIMKVEVVTPEDYMGDVMGDLNRRRGLIQ 640
Cdd:COG0480   550 GVLAGYPVVDVKVTLYDGSYHPVDSSEMAFKIAASMAFKEAAKKAKPVLLEPIMKVEVTVPEEYMGDVMGDLNSRRGRIL 629
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 641 GMEDTVTGKVIRAEVPLGEMFGYATDVRSMSQGRASYSMEFSKYAEAPSNIAEAIIKKQA 700
Cdd:COG0480   630 GMESRGGAQVIKAEVPLAEMFGYATDLRSLTQGRGSFTMEFSHYEEVPANVAEKIIAKRK 689
EF-G TIGR00484
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ...
1-698 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: 1176.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237   1 MARTTAINRYRNIGICAHVDAGKTTTTERILFYTGVNHKMGEVHDGAATMDWMVQEQERGITITSAATTAFWSGstkqyd 80
Cdd:TIGR00484   1 MARTTDLNRFRNIGISAHIDAGKTTTTERILFYTGRIHKIGEVHDGAATMDWMEQEKERGITITSAATTVFWKG------ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  81 kYRVNIIDTPGHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDRAGANFLRVVEQIKK 160
Cdd:TIGR00484  75 -HRINIIDTPGHVDFTVEVERSLRVLDGAVAVLDAVGGVQPQSETVWRQANRYEVPRIAFVNKMDKTGANFLRVVNQIKQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 161 RLGHTPVPVQLAIGAEENFQGQIDLLKMKAIFWNDDdQGMTYREEEIPADMLADAEQWRSNMVEAAAEANEELMNKYLEE 240
Cdd:TIGR00484 154 RLGANAVPIQLPIGAEDNFIGVIDLVEMKAYFFNGD-KGTKAIEKEIPSDLLEQAKELRENLVEAVAEFDEELMEKYLEG 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 241 GELSIDEIKAGLRQRTIACEIVPAVCGSSFKNKGVPLVLDAVIDFLPAPIEIPAIKGTNPDNEEiTDERHADDNEPFSAL 320
Cdd:TIGR00484 233 EELTIEEIKNAIRKGVLNCEFFPVLCGSAFKNKGVQLLLDAVVDYLPSPTDVPAIKGIDPDTEK-EIERKASDDEPFSAL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 321 AFKIATDPFVGTLTFARVYSGVLSSGDSVINSVKGKKERVGRMVQMHANTREEIKEVRAGDIAALIGMKDVTTGDTLCSI 400
Cdd:TIGR00484 312 AFKVATDPFVGQLTFVRVYSGVLKSGSYVKNSRKNKKERVGRLVKMHANNREEIKEVRAGDICAAIGLKDTTTGDTLCDP 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 401 EKPIILERMDFPEPVISVAVEPKTKADQEKMGIALGKLAQEDPSFRVKTDEESGQTIISGMGELHLDILVDRMKREFGVE 480
Cdd:TIGR00484 392 KIDVILERMEFPEPVISLAVEPKTKADQEKMGIALGKLAEEDPTFRTFTDPETGQTIIAGMGELHLDIIVDRMKREFKVE 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 481 ANIGKPQVAYRETIRNTCEIEGKFVRQSGGRGQFGHCWIRFAPADEgqEGLEFVSEVVGGVIPKEYIPAIQKGIEEQMKN 560
Cdd:TIGR00484 472 ANVGAPQVAYRETIRSKVEVEGKHAKQSGGRGQYGHVKIRFEPLEP--KGYEFVNEIKGGVIPREYIPAVDKGLQEAMES 549
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 561 GIVAGYPLLGLKAAVFDGSYHDVDSNEMAFKIAASMATKQLTQKGGAVLLEPIMKVEVVTPEDYMGDVMGDLNRRRGLIQ 640
Cdd:TIGR00484 550 GPLAGYPVVDIKATLFDGSYHDVDSSEMAFKLAASLAFKEAGKKANPVLLEPIMKVEVEVPEEYMGDVMGDLSSRRGIIE 629
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1718559237 641 GMEDTVTGKVIRAEVPLGEMFGYATDVRSMSQGRASYSMEFSKYAEAPSNIAEAIIKK 698
Cdd:TIGR00484 630 GMEARGNVQKIKAEVPLSEMFGYATDLRSFTQGRGTYSMEFLHYGEVPSSVANEIIEK 687
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
17-697 0e+00

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 1102.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  17 AHVDAGKTTTTERILFYTGVNHKMGEVHDGAATMDWMVQEQERGITITSAATTAFWSGstkqydkYRVNIIDTPGHVDFT 96
Cdd:PRK12740    2 GHSGAGKTTLTEAILFYTGAIHRIGEVEDGTTTMDFMPEERERGISITSAATTCEWKG-------HKINLIDTPGHVDFT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  97 IEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDRAGANFLRVVEQIKKRLGHTPVPVQLAIGAE 176
Cdd:PRK12740   75 GEVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRAGADFFRVLAQLQEKLGAPVVPLQLPIGEG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 177 ENFQGQIDLLKMKAIFWnddDQGMTYREEEIPADMLADAEQWRSNMVEAAAEANEELMNKYLEEGELSIDEIKAGLRQRT 256
Cdd:PRK12740  155 DDFTGVVDLLSMKAYRY---DEGGPSEEIEIPAELLDRAEEAREELLEALAEFDDELMEKYLEGEELSEEEIKAGLRKAT 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 257 IACEIVPAVCGSSFKNKGVPLVLDAVIDFLPAPIEIPAIKGTNPDNEEitdERHADDNEPFSALAFKIATDPFVGTLTFA 336
Cdd:PRK12740  232 LAGEIVPVFCGSALKNKGVQRLLDAVVDYLPSPLEVPPVDGEDGEEGA---ELAPDPDGPLVALVFKTMDDPFVGKLSLV 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 337 RVYSGVLSSGDSVINSVKGKKERVGRMVQMHANTREEIKEVRAGDIAALIGMKDVTTGDTLCSIEKPIILERMDFPEPVI 416
Cdd:PRK12740  309 RVYSGTLKKGDTLYNSGTGKKERVGRLYRMHGKQREEVDEAVAGDIVAVAKLKDAATGDTLCDKGDPILLEPMEFPEPVI 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 417 SVAVEPKTKADQEKMGIALGKLAQEDPSFRVKTDEESGQTIISGMGELHLDILVDRMKREFGVEANIGKPQVAYRETIRN 496
Cdd:PRK12740  389 SLAIEPKDKGDEEKLSEALGKLAEEDPTLRVERDEETGQTILSGMGELHLDVALERLKREYGVEVETGPPQVPYRETIRK 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 497 TCEIEGKFVRQSGGRGQFGHCWIRFAPADEGqEGLEFVSEVVGGVIPKEYIPAIQKGIEEQMKNGIVAGYPLLGLKAAVF 576
Cdd:PRK12740  469 KAEGHGRHKKQSGGHGQFGDVWLEVEPLPRG-EGFEFVDKVVGGAVPRQYIPAVEKGVREALEKGVLAGYPVVDVKVTLT 547
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 577 DGSYHDVDSNEMAFKIAASMATKQLTQKGGAVLLEPIMKVEVVTPEDYMGDVMGDLNRRRGLIQGMEDTVTGKVIRAEVP 656
Cdd:PRK12740  548 DGSYHSVDSSEMAFKIAARLAFREALPKAKPVLLEPIMKVEVSVPEEFVGDVIGDLSSRRGRILGMESRGGGDVVRAEVP 627
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|.
gi 1718559237 657 LGEMFGYATDVRSMSQGRASYSMEFSKYAEAPSNIAEAIIK 697
Cdd:PRK12740  628 LAEMFGYATDLRSLTQGRGSFSMEFSHYEEVPGNVAEKVIA 668
PRK13351 PRK13351
elongation factor G-like protein;
7-698 0e+00

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 908.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237   7 INRYRNIGICAHVDAGKTTTTERILFYTGVNHKMGEVHDGAATMDWMVQEQERGITITSAATTAFWsgstkqyDKYRVNI 86
Cdd:PRK13351    5 LMQIRNIGILAHIDAGKTTLTERILFYTGKIHKMGEVEDGTTVTDWMPQEQERGITIESAATSCDW-------DNHRINL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  87 IDTPGHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDRAGANFLRVVEQIKKRLGHTP 166
Cdd:PRK13351   78 IDTPGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLFKVLEDIEERFGKRP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 167 VPVQLAIGAEENFQGQIDLLKMKAIFWNDDDQGMTYREEEIPADMLADAEQWRSNMVEAAAEANEELMNKYLEEGELSID 246
Cdd:PRK13351  158 LPLQLPIGSEDGFEGVVDLITEPELHFSEGDGGSTVEEGPIPEELLEEVEEAREKLIEALAEFDDELLELYLEGEELSAE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 247 EIKAGLRQRTIACEIVPAVCGSSFKNKGVPLVLDAVIDFLPAPIEIPAIKGTNPDNEEITdeRHADDNEPFSALAFKIAT 326
Cdd:PRK13351  238 QLRAPLREGTRSGHLVPVLFGSALKNIGIEPLLDAVVDYLPSPLEVPPPRGSKDNGKPVK--VDPDPEKPLLALVFKVQY 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 327 DPFVGTLTFARVYSGVLSSGDSVINSVKGKKERVGRMVQMHANTREEIKEVRAGDIAALIGMKDVTTGDTLCSIEKPIIL 406
Cdd:PRK13351  316 DPYAGKLTYLRVYSGTLRAGSQLYNGTGGKREKVGRLFRLQGNKREEVDRAKAGDIVAVAGLKELETGDTLHDSADPVLL 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 407 ERMDFPEPVISVAVEPKTKADQEKMGIALGKLAQEDPSFRVKTDEESGQTIISGMGELHLDILVDRMKREFGVEANIGKP 486
Cdd:PRK13351  396 ELLTFPEPVVSLAVEPERRGDEQKLAEALEKLVWEDPSLRVEEDEETGQTILSGMGELHLEVALERLRREFKLEVNTGKP 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 487 QVAYRETIRNTCEIEGKFVRQSGGRGQFGHCWIRFAPADEGqEGLEFVSEVVGGVIPKEYIPAIQKGIEEQMKNGIVAGY 566
Cdd:PRK13351  476 QVAYRETIRKMAEGVYRHKKQFGGKGQFGEVHLRVEPLERG-AGFIFVSKVVGGAIPEELIPAVEKGIREALASGPLAGY 554
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 567 PLLGLKAAVFDGSYHDVDSNEMAFKIAASMATKQLTQKGGAVLLEPIMKVEVVTPEDYMGDVMGDLNRRRGLIQGMEDTV 646
Cdd:PRK13351  555 PVTDLRVTVLDGKYHPVDSSESAFKAAARKAFLEAFRKANPVLLEPIMELEITVPTEHVGDVLGDLSQRRGRIEGTEPRG 634
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1718559237 647 TGKV-IRAEVPLGEMFGYATDVRSMSQGRASYSMEFSKYAEAPSNIAEAIIKK 698
Cdd:PRK13351  635 DGEVlVKAEAPLAELFGYATRLRSMTKGRGSFTMEFSHFDPVPPAVQKKVGSK 687
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
12-289 2.52e-170

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: 488.15  E-value: 2.52e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  12 NIGICAHVDAGKTTTTERILFYTGVNHKMGEVHDGAATMDWMVQEQERGITITSAATTAFWSGstkqydkYRVNIIDTPG 91
Cdd:cd01886     1 NIGIIAHIDAGKTTTTERILYYTGRIHKIGEVHGGGATMDWMEQERERGITIQSAATTCFWKD-------HRINIIDTPG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  92 HVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDRAGANFLRVVEQIKKRLGHTPVPVQL 171
Cdd:cd01886    74 HVDFTIEVERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQIREKLGANPVPLQL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 172 AIGAEENFQGQIDLLKMKAIFWNDDDqGMTYREEEIPADMLADAEQWRSNMVEAAAEANEELMNKYLEEGELSIDEIKAG 251
Cdd:cd01886   154 PIGAEDDFEGVVDLIEMKALYWDGEL-GEKIEETDIPEDLLEEAEEAREELIETLAEVDDELMEKYLEGEEITEEEIKAA 232
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1718559237 252 LRQRTIACEIVPAVCGSSFKNKGVPLVLDAVIDFLPAP 289
Cdd:cd01886   233 IRKGTIANKIVPVLCGSAFKNKGVQPLLDAVVDYLPSP 270
PRK07560 PRK07560
elongation factor EF-2; Reviewed
7-698 1.46e-122

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 382.29  E-value: 1.46e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237   7 INRYRNIGICAHVDAGKTTTTERILFYTGVNHKmgEVHDGAATMDWMVQEQERGITITSAATTAfwsgsTKQYD--KYRV 84
Cdd:PRK07560   17 PEQIRNIGIIAHIDHGKTTLSDNLLAGAGMISE--ELAGEQLALDFDEEEQARGITIKAANVSM-----VHEYEgkEYLI 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  85 NIIDTPGHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDRAgANFLRVV-EQIKKRLG 163
Cdd:PRK07560   90 NLIDTPGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKPVLFINKVDRL-IKELKLTpQEMQQRLL 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 164 htpvpvqlAIGAEENfqgqiDLLKMkaifwndddqgmtYREEEIPADMLADAE-----------QWRSNMveaaaeaneE 232
Cdd:PRK07560  169 --------KIIKDVN-----KLIKG-------------MAPEEFKEKWKVDVEdgtvafgsalyNWAISV---------P 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 233 LMNK----------YLEEGElsIDEikagLRQRTiaceivpavcgssfknkgvPL---VLDAVIDFLPAPIE-----IPA 294
Cdd:PRK07560  214 MMQKtgikfkdiidYYEKGK--QKE----LAEKA-------------------PLhevVLDMVVKHLPNPIEaqkyrIPK 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 295 I-KGtNPDNEEITDERHADDNEPFSALAFKIATDPFVGTLTFARVYSGVLSSGDSVINSVKGKKERVGRMVQMHANTREE 373
Cdd:PRK07560  269 IwKG-DLNSEVGKAMLNCDPNGPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLVGAKKKNRVQQVGIYMGPEREE 347
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 374 IKEVRAGDIAALIGMKDVTTGDTLCSIEKPIILERMD-FPEPVISVAVEPKTKADQEKMGIALGKLAQEDPSFRVKTDEE 452
Cdd:PRK07560  348 VEEIPAGNIAAVTGLKDARAGETVVSVEDMTPFESLKhISEPVVTVAIEAKNPKDLPKLIEVLRQLAKEDPTLVVKINEE 427
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 453 SGQTIISGMGELHLDILVDRMKREFGVEANIGKPQVAYRETIRNTC-EIEGKfvrqSGGRgqfgH--CWIRFAPADEG-- 527
Cdd:PRK07560  428 TGEHLLSGMGELHLEVITYRIKRDYGIEVVTSEPIVVYRETVRGKSqVVEGK----SPNK----HnrFYISVEPLEEEvi 499
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 528 ---QEGlefvsEVVGGVIPKEY-------------------IPAIQ---------KGI--------------EEQMKNGI 562
Cdd:PRK07560  500 eaiKEG-----EISEDMDKKEAkilreklieagmdkdeakrVWAIYngnvfidmtKGIqylnevmeliiegfREAMKEGP 574
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 563 VAGYPLLGLKAAVFDGSYHDvDSNE---------MAFKIAASMATkqltqkGGAVLLEPIMKVEVVTPEDYMGDVMGDLN 633
Cdd:PRK07560  575 LAAEPVRGVKVRLHDAKLHE-DAIHrgpaqvipaVRNAIFAAMLT------AKPTLLEPIQKVDINVPQDYMGAVTREIQ 647
                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1718559237 634 RRRGLIQGMEDTVTGKVIRAEVPLGEMFGYATDVRSMSQGRASYSMEFSKYAEAPSNIAEAIIKK 698
Cdd:PRK07560  648 GRRGKILDMEQEGDMAIIEAEAPVAEMFGFAGEIRSATEGRALWSTEFAGFEPVPDSLQLDIVRQ 712
aEF-2 TIGR00490
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ...
9-698 2.60e-98

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: 318.38  E-value: 2.60e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237   9 RYRNIGICAHVDAGKTTTTERILFYTGVNHKmgEVHDGAATMDWMVQEQERGITITSAATTAFwsgSTKQYDKYRVNIID 88
Cdd:TIGR00490  18 FIRNIGIVAHIDHGKTTLSDNLLAGAGMISE--ELAGQQLYLDFDEQEQERGITINAANVSMV---HEYEGNEYLINLID 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  89 TPGHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDRAGANFLRVVEQIKKRLGHTPVP 168
Cdd:TIGR00490  93 TPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKPVLFINKVDRLINELKLTPQELQERFIKIITE 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 169 VQLAIG--AEENFQG--QIDLLKMKAIFwndddqGMTYREEEIPADMLADAEQWRSNMVeaaaeaneelmnKYLEEGels 244
Cdd:TIGR00490 173 VNKLIKamAPEEFRDkwKVRVEDGSVAF------GSAYYNWAISVPSMKKTGIGFKDIY------------KYCKED--- 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 245 ideikaglRQRTIAceivpavcgssfknKGVPL---VLDAVIDFLPAPIE-----IPAIKGTNPDNEEITDERHADDNEP 316
Cdd:TIGR00490 232 --------KQKELA--------------KKSPLhqvVLDMVIRHLPSPIEaqkyrIPVIWKGDLNSEVGKAMLNCDPKGP 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 317 FSALAFKIATDPFVGTLTFARVYSGVLSSGDSVINSVKGKKERVGRMVQMHANTREEIKEVRAGDIAALIGMKDVTTGDT 396
Cdd:TIGR00490 290 LALMITKIVVDKHAGEVAVGRLYSGTIRPGMEVYIVDRKAKARIQQVGVYMGPERVEVDEIPAGNIVAVIGLKDAVAGET 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 397 LCSIEKPII-LERMD-FPEPVISVAVEPKTKADQEKMGIALGKLAQEDPSFRVKTDEESGQTIISGMGELHLDILVDRMK 474
Cdd:TIGR00490 370 ICTTVENITpFESIKhISEPVVTVAIEAKNTKDLPKLIEVLRQVAKEDPTVHVEINEETGEHLISGMGELHLEIIVEKIR 449
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 475 REFGVEANIGKPQVAYRETIRNTCEI----------------------------EGKFVRQSGGRGQFGHCWIR------ 520
Cdd:TIGR00490 450 EDYGLDVETSPPIVVYRETVTGTSPVvegkspnkhnrfyivvepleesviqafkEGKIVDMKMKKKERRRLLIEagmdse 529
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 521 -FAPADEGQEGLEFVSEVVGGVIPKEYIPAIQKGIEEQMKNGIVAGYPLLGLKAAVFDGSYHD--VDSNEMAFKIAASMA 597
Cdd:TIGR00490 530 eAARVEEYYEGNLFINMTRGIQYLDETKELILEGFREAMRNGPIAREKCMGVKVKLMDAKLHEdaVHRGPAQVIPAVRSG 609
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 598 TKQLTQKGGAVLLEPIMKVEVVTPEDYMGDVMGDLNRRRGLIQGMEDTVTGKVIRAEVPLGEMFGYATDVRSMSQGRASY 677
Cdd:TIGR00490 610 IFAAMMQAKPVLLEPYQKVFINVPQDMMGAATREIQNRRGQILEMKQEGDMVTIIAKAPVAEMFGFAGAIRGATSGRCLW 689
                         730       740
                  ....*....|....*....|.
gi 1718559237 678 SMEFSKYAEAPSNIAEAIIKK 698
Cdd:TIGR00490 690 STEHAGFELVPQNLQQEFVME 710
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
12-289 5.85e-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: 258.29  E-value: 5.85e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  12 NIGICAHVDAGKTTTTERILFYTGVNHKMGEVHDGAATMDWMVQEQERGITITSaaTTAFWsgstkQYDKYRVNIIDTPG 91
Cdd:cd04170     1 NIALVGHSGSGKTTLAEALLYATGAIDRLGRVEDGNTVSDYDPEEKKRKMSIET--SVAPL-----EWNGHKINLIDTPG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  92 HVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDRAGANFLRVVEQIKKRLGHTPVPVQL 171
Cdd:cd04170    74 YADFVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRARADFDKTLAALREAFGRPVVPIQL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 172 AIGAEENFQGQIDLLKMKAIFWNDddqGMTYREEEIPADMLADAEQWRSNMVEAAAEANEELMNKYLEEGELSIDEIKAG 251
Cdd:cd04170   154 PIGEGDEFTGVVDLLSEKAYRYDP---GEPSVEIEIPEELKEKVAEAREELLEAVAETDEELMEKYLEEGELTEEELRAG 230
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1718559237 252 LRQRTIACEIVPAVCGSSFKNKGVPLVLDAVIDFLPAP 289
Cdd:cd04170   231 LRRALRAGLIVPVFFGSALTGIGVRRLLDALVELAPSP 268
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
8-288 1.41e-73

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: 235.88  E-value: 1.41e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237   8 NRYRNIGICAHVDAGKTTTTERILFYTGVNHKMGEVH-DGAATMDWMVQEQERGITITSAATTAFWsgstkqyDKYRVNI 86
Cdd:pfam00009   1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKgEGEAGLDNLPEERERGITIKSAAVSFET-------KDYLINL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  87 IDTPGHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDRA-GANFLRVVEQIKKRlght 165
Cdd:pfam00009  74 IDTPGHVDFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVdGAELEEVVEEVSRE---- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 166 pvpvqlaigaeenfqgqidllkmkaifwndddqgmtyreeeipadmladaeqwrsnmveaaaeaneeLMNKYLEEGelsi 245
Cdd:pfam00009 150 -------------------------------------------------------------------LLEKYGEDG---- 158
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1718559237 246 deikaglrqrtiacEIVPAVCGSSFKNKGVPLVLDAVIDFLPA 288
Cdd:pfam00009 159 --------------EFVPVVPGSALKGEGVQTLLDALDEYLPS 187
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
12-289 2.43e-66

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


Pssm-ID: 206731 [Multi-domain]  Cd Length: 237  Bit Score: 218.64  E-value: 2.43e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  12 NIGICAHVDAGKTTTTERILFYTGVNHKMGEVHDGAATMDWMVQEQERGITITSAATTAFWSGStkqydkyRVNIIDTPG 91
Cdd:cd04168     1 NIGILAHVDAGKTTLTESLLYTSGAIRELGSVDKGTTRTDSMELERQRGITIFSAVASFQWEDT-------KVNIIDTPG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  92 HVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDRAGANFLRVVEQIKKRLGHTPVPVQl 171
Cdd:cd04168    74 HMDFIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTIIFVNKIDRAGADLEKVYQEIKEKLSPDIVPMQ- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 172 AIGAEENFQGqidllkmkaifwnDDDQGMTYREEEIPADmladaeqwrsnmveaaaeanEELMNKYLEEGELSIDEIKAG 251
Cdd:cd04168   153 KVGLYPNICD-------------TNNIDDEQIETVAEGN--------------------DELLEKYLSGGPLEELELDNE 199
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1718559237 252 LRQRTIACEIVPAVCGSSFKNKGVPLVLDAVIDFLPAP 289
Cdd:cd04168   200 LSARIQKASLFPVYHGSALKGIGIDELLEGITNLFPTS 237
PTZ00416 PTZ00416
elongation factor 2; Provisional
8-694 1.94e-63

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 226.08  E-value: 1.94e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237   8 NRYRNIGICAHVDAGKTTTTERILFYTGVnHKMGEVHDgAATMDWMVQEQERGITITSAATTAFW-----SGSTKQydKY 82
Cdd:PTZ00416   17 DQIRNMSVIAHVDHGKSTLTDSLVCKAGI-ISSKNAGD-ARFTDTRADEQERGITIKSTGISLYYehdleDGDDKQ--PF 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  83 RVNIIDTPGHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDRA-----------GANF 151
Cdd:PTZ00416   93 LINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKVDRAilelqldpeeiYQNF 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 152 LRVVEQI--------KKRLGHTPVPVQL---AIGAeeNFQG----------------QIDLLKMKAIFWND---DDQGMT 201
Cdd:PTZ00416  173 VKTIENVnviiatynDELMGDVQVYPEKgtvAFGS--GLQGwaftlttfariyakkfGVEESKMMERLWGDnffDAKTKK 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 202 YREEEIPAD-----------MLADAEQWRSNMVEAAAEANEELMNKY-----LEEGELSIDE-IKAGLRqrtiaceivpa 264
Cdd:PTZ00416  251 WIKDETNAQgkklkrafcqfILDPICQLFDAVMNEDKEKYDKMLKSLnisltGEDKELTGKPlLKAVMQ----------- 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 265 vcgssfknKGVPL---VLDAVIDFLPAPIEIPAIKGTN----P-DNEEITDERHADDNEPFSALAFKIatdpfVGT---- 332
Cdd:PTZ00416  320 --------KWLPAadtLLEMIVDHLPSPKEAQKYRVENlyegPmDDEAANAIRNCDPNGPLMMYISKM-----VPTsdkg 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 333 --LTFARVYSGVLSSGDSV----INSVKGKKE-----RVGRMVQMHANTREEIKEVRAGDIAALIGMKD--VTTGdTLCS 399
Cdd:PTZ00416  387 rfYAFGRVFSGTVATGQKVriqgPNYVPGKKEdlfekNIQRTVLMMGRYVEQIEDVPCGNTVGLVGVDQylVKSG-TITT 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 400 IEKPIILERMDFP-EPVISVAVEPKTKADQEKMGIALGKLAQEDPSFRVKTdEESGQTIISGMGELHLDILVDRMKREF- 477
Cdd:PTZ00416  466 SETAHNIRDMKYSvSPVVRVAVEPKNPKDLPKLVEGLKRLAKSDPLVVCTT-EESGEHIVAGCGELHVEICLKDLEDDYa 544
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 478 GVEANIGKPQVAYRETIRN----TC------------------------EIEGKFVRQ---SGGRGQF---GHCWIR--- 520
Cdd:PTZ00416  545 NIDIIVSDPVVSYRETVTEessqTClskspnkhnrlymkaeplteelaeAIEEGKVGPeddPKERANFladKYEWDKnda 624
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 521 -----FAPADEGQeglEFVSEVVGGVipkEYIPAIQKGIEEQM----KNGIVAGYPLLGLKAAVFDGSYHDVDSNEMAFK 591
Cdd:PTZ00416  625 rkiwcFGPENKGP---NVLVDVTKGV---QYMNEIKDSCVSAFqwatKEGVLCDENMRGIRFNILDVTLHADAIHRGAGQ 698
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 592 IAAS----MATKQLTqkGGAVLLEPIMKVEVVTPEDYMGDVMGDLNRRRGLIQGmEDTVTGK---VIRAEVPLGEMFGYA 664
Cdd:PTZ00416  699 IIPTarrvFYACELT--ASPRLLEPMFLVDITAPEDAMGGIYSVLNRRRGVVIG-EEQRPGTplsNIKAYLPVAESFGFT 775
                         810       820       830
                  ....*....|....*....|....*....|
gi 1718559237 665 TDVRSMSQGRASYSMEFSKYAEAPSNIAEA 694
Cdd:PTZ00416  776 AALRAATSGQAFPQCVFDHWQVVPGDPLEP 805
EFG_mtEFG1_IV cd01434
EFG_mtEFG1_IV: domains similar to domain IV of the bacterial translational elongation factor ...
490-606 1.83e-60

EFG_mtEFG1_IV: domains similar to domain IV of the bacterial translational elongation factor (EF) EF-G. Included in this group is a domain of mitochondrial Elongation factor G1 (mtEFG1) proteins homologous to domain IV of EF-G. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. In bacteria this translocation step is catalyzed by EF-G_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. There are two forms of mtEFG present in mammals (designated mtEFG1s and mtEFG2s) mtEFG2s are not present in this group.


Pssm-ID: 238715 [Multi-domain]  Cd Length: 116  Bit Score: 198.43  E-value: 1.83e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 490 YRETIRNTCEIEGKFVRQSGGRGQFGHCWIRFAPADEGqEGLEFVSEVVGGVIPKEYIPAIQKGIEEQMKNGIVAGYPLL 569
Cdd:cd01434     1 YRETITKPAEFEYRHKKQSGGAGQYGHVVLEIEPLPRG-SGFEFVNKIVGGAIPKEYIPAVEKGFREALEKGPLAGYPVV 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1718559237 570 GLKAAVFDGSYHDVDSNEMAFKIAASMATKQLTQKGG 606
Cdd:cd01434    80 DVKVTLYDGSYHDVDSSEMAFKIAARMAFKEAFKKAK 116
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
11-492 1.03e-53

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


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 194.85  E-value: 1.03e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  11 RNIGICAHVDAGKTTTTERILFYTGVNHKMGEVHDGAatMDWMVQEQERGITITSAATTAFWSGstkqydkYRVNIIDTP 90
Cdd:COG1217     7 RNIAIIAHVDHGKTTLVDALLKQSGTFRENQEVAERV--MDSNDLERERGITILAKNTAVRYKG-------VKINIVDTP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  91 GHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDRAGANFLRVVEQIkkrlghtpvpvq 170
Cdd:COG1217    78 GHADFGGEVERVLSMVDGVLLLVDAFEGPMPQTRFVLKKALELGLKPIVVINKIDRPDARPDEVVDEV------------ 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 171 laigaeenfqgqIDLLkmkaifwndddqgmtyreeeipADMLADAEQwrsnmveaaaeaneelmnkyLE---------EG 241
Cdd:COG1217   146 ------------FDLF----------------------IELGATDEQ--------------------LDfpvvyasarNG 171
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 242 --ELSIDEIKAGLRqrtiaceivpavcgssfknkgvPLvLDAVIDFLPAPieipaikgtnpdneeitderHADDNEPFSA 319
Cdd:COG1217   172 waSLDLDDPGEDLT----------------------PL-FDTILEHVPAP--------------------EVDPDGPLQM 208
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 320 LAFKIATDPFVGTLTFARVYSGVLSSGDSV-INSVKGKKE--RVGRMVQMHANTREEIKEVRAGDIAALIGMKDVTTGDT 396
Cdd:COG1217   209 LVTNLDYSDYVGRIAIGRIFRGTIKKGQQVaLIKRDGKVEkgKITKLFGFEGLERVEVEEAEAGDIVAIAGIEDINIGDT 288
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 397 LCSIEKPIILERMDFPEPVISVAVEPKTK--ADQEkmgialGK----------LAQE---DPSFRVKTDEESGQTIISGM 461
Cdd:COG1217   289 ICDPENPEALPPIKIDEPTLSMTFSVNDSpfAGRE------GKfvtsrqirerLEKEletNVALRVEETDSPDAFKVSGR 362
                         490       500       510
                  ....*....|....*....|....*....|.
gi 1718559237 462 GELHLDILVDRMKREfGVEANIGKPQVAYRE 492
Cdd:COG1217   363 GELHLSILIETMRRE-GYELQVSRPEVIFKE 392
PLN00116 PLN00116
translation elongation factor EF-2 subunit; Provisional
11-675 1.46e-52

translation elongation factor EF-2 subunit; Provisional


Pssm-ID: 177730 [Multi-domain]  Cd Length: 843  Bit Score: 195.33  E-value: 1.46e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  11 RNIGICAHVDAGKTTTTERILFYTGVNHKmgEVHDGAATMDWMVQEQERGITITSAATTAFW---SGSTKQY------DK 81
Cdd:PLN00116   20 RNMSVIAHVDHGKSTLTDSLVAAAGIIAQ--EVAGDVRMTDTRADEAERGITIKSTGISLYYemtDESLKDFkgerdgNE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  82 YRVNIIDTPGHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDR-----------AGAN 150
Cdd:PLN00116   98 YLINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTETVLRQALGERIRPVLTVNKMDRcflelqvdgeeAYQT 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 151 FLRVVEQIK--------KRLGHTPV-PVQLAIGAEENFQGQIDLL----KMKAIFWNDDDQGMTyreEEIPADMLADAE- 216
Cdd:PLN00116  178 FSRVIENANvimatyedPLLGDVQVyPEKGTVAFSAGLHGWAFTLtnfaKMYASKFGVDESKMM---ERLWGENFFDPAt 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 217 -QWRSN----------MVEAAAEANEELMNKYLEEGElsiDEIKAGLRQrtIACEIVPAvcgsSFKNKGVPL-------- 277
Cdd:PLN00116  255 kKWTTKntgsptckrgFVQFCYEPIKQIINTCMNDQK---DKLWPMLEK--LGVTLKSD----EKELMGKALmkrvmqtw 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 278 ------VLDAVIDFLPAPIEIPAIKGTN----P-DNEEITDERHADDNEPFSALAFKI--ATDP--FVGtltFARVYSGV 342
Cdd:PLN00116  326 lpasdaLLEMIIFHLPSPAKAQRYRVENlyegPlDDKYATAIRNCDPNGPLMLYVSKMipASDKgrFFA---FGRVFSGT 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 343 LSSGDSV----INSVKGKK-----ERVGRMVQMHANTREEIKEVRAGDIAALIGM-----KDVTTGDTLCSIEKPIilER 408
Cdd:PLN00116  403 VATGMKVrimgPNYVPGEKkdlyvKSVQRTVIWMGKKQESVEDVPCGNTVAMVGLdqfitKNATLTNEKEVDAHPI--KA 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 409 MDFP-EPVISVAVEPKTKADQEKMGIALGKLAQEDPSFRVKTdEESGQTIISGMGELHLDILVDRMKREF--GVEANIGK 485
Cdd:PLN00116  481 MKFSvSPVVRVAVQCKNASDLPKLVEGLKRLAKSDPMVQCTI-EESGEHIIAGAGELHLEICLKDLQDDFmgGAEIKVSD 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 486 PQVAYRETI-----------------------------------------RNTCEIEGKFVRQSGG--RGQFGHCWIrFA 522
Cdd:PLN00116  560 PVVSFRETVlekscrtvmskspnkhnrlymearpleeglaeaiddgrigpRDDPKIRSKILAEEFGwdKDLAKKIWC-FG 638
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 523 PadEGQeGLEFVSEVVGGVipkEYIPAIQK----GIEEQMKNGIVAGYPLLGLKAAVFDGSYH-DVDSNEMAFKIAAS-- 595
Cdd:PLN00116  639 P--ETT-GPNMVVDMCKGV---QYLNEIKDsvvaGFQWATKEGALAEENMRGICFEVCDVVLHaDAIHRGGGQIIPTArr 712
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 596 -MATKQLTQKGGavLLEPIMKVEVVTPEDYMGDVMGDLNRRRG-LIQGMEDTVTGKV-IRAEVPLGEMFGYATDVRSMSQ 672
Cdd:PLN00116  713 vIYASQLTAKPR--LLEPVYLVEIQAPEQALGGIYSVLNQKRGhVFEEMQRPGTPLYnIKAYLPVIESFGFSGTLRAATS 790

                  ...
gi 1718559237 673 GRA 675
Cdd:PLN00116  791 GQA 793
EFG_IV smart00889
Elongation factor G, domain IV; Translation elongation factors are responsible for two main ...
487-606 8.78e-51

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: 172.34  E-value: 8.78e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  487 QVAYRETIRNTC-EIEGKFVRQSGGRGQFGHCWIRFAPADEGqEGLEFVSEVVGGVIPKEYIPAIQKGIEEQMKNGIVAG 565
Cdd:smart00889   1 QVAYRETITKPVkEAEGKHKKQSGGDGQYARVILEVEPLERG-SGFEFDDTIVGGVIPKEYIPAVEKGFREALEEGPLAG 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1718559237  566 YPLLGLKAAVFDGSYHDVDSNEMAFKIAASMATKQLTQKGG 606
Cdd:smart00889  80 YPVVDVKVTLLDGSYHEVDSSEMAFKPAARRAFKEALLKAG 120
EFG_IV pfam03764
Elongation factor G, domain IV; This domain is found in elongation factor G, elongation factor ...
486-606 1.18e-50

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: 172.02  E-value: 1.18e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 486 PQVAYRETIRNTCE-IEGKFVRQSGGRGQFGHCWIRFAPADEGqEGLEFVSEVVGGVIPKEYIPAIQKGIEEQMKNGIVA 564
Cdd:pfam03764   1 PQVAYRETIRKPVKeRAYKHKKQSGGDGQYARVILRIEPLPPG-SGNEFVDETVGGQIPKEFIPAVEKGFQEAMKEGPLA 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1718559237 565 GYPLLGLKAAVFDGSYHDVDSNEMAFKIAASMATKQLTQKGG 606
Cdd:pfam03764  80 GEPVTDVKVTLLDGSYHEVDSSEAAFIPAARRAFREALLKAS 121
EFG_C smart00838
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ...
609-693 2.13e-50

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: 169.99  E-value: 2.13e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  609 LLEPIMKVEVVTPEDYMGDVMGDLNRRRGLIQGMEDTVTGKVIRAEVPLGEMFGYATDVRSMSQGRASYSMEFSKYAEAP 688
Cdd:smart00838   1 LLEPIMKVEVTVPEEYMGDVIGDLNSRRGKIEGMEQRGGAQVIKAKVPLSEMFGYATDLRSATQGRATWSMEFSHYEEVP 80

                   ....*
gi 1718559237  689 SNIAE 693
Cdd:smart00838  81 KSIAE 85
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
12-169 6.09e-49

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: 169.78  E-value: 6.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  12 NIGICAHVDAGKTTTTERILFYTGVNHKMGEVHDgaATMDWMVQEQERGITITSAATTAFWsgstkqyDKYRVNIIDTPG 91
Cdd:cd00881     1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKE--TFLDTLKEERERGITIKTGVVEFEW-------PKRRINFIDTPG 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1718559237  92 HVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDRAG-ANFLRVVEQIKKRLGHTPVPV 169
Cdd:cd00881    72 HEDFSKETVRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGeEDFDEVLREIKELLKLIGFTF 150
RF3 cd04169
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ...
9-289 6.65e-46

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: 164.31  E-value: 6.65e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237   9 RYRNIGICAHVDAGKTTTTERILFYTGVNHKMGEVH----DGAATMDWMVQEQERGITITSAATTaFwsgstkQYDKYRV 84
Cdd:cd04169     1 RRRTFAIISHPDAGKTTLTEKLLLFGGAIQEAGAVKarksRKHATSDWMEIEKQRGISVTSSVMQ-F------EYKGCVI 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  85 NIIDTPGHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDRAGANFLRVVEQIKKRLGH 164
Cdd:cd04169    74 NLLDTPGHEDFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDREGRDPLELLDEIENELGI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 165 TPVPVQLAIGAEENFQGQIDLLKMKAIFWNDDDQGMTYREEEIpaDMLADAEqwrsnmveAAAEANEELMNKYLEEGELs 244
Cdd:cd04169   154 DCAPMTWPIGMGKDFKGVYDRYDKEIYLYERGAGGAIKAPEET--KGLDDPK--------LDELLGEDLAEQLREELEL- 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1718559237 245 IDEIKAGLRQRTI-ACEIVPAVCGSSFKNKGVPLVLDAVIDFLPAP 289
Cdd:cd04169   223 VEGAGPEFDKELFlAGELTPVFFGSALNNFGVQELLDAFVKLAPAP 268
EFG_III cd16262
Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial ...
412-487 4.81e-45

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: 154.92  E-value: 4.81e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1718559237 412 PEPVISVAVEPKTKADQEKMGIALGKLAQEDPSFRVKTDEESGQTIISGMGELHLDILVDRMKREFGVEANIGKPQ 487
Cdd:cd16262     1 PEPVISLAIEPKTKADEDKLSKALARLAEEDPTLRVSRDEETGQTILSGMGELHLEIIVERLKREYGVEVEVGKPQ 76
lepA TIGR01393
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a ...
9-687 7.98e-45

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: 169.43  E-value: 7.98e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237   9 RYRNIGICAHVDAGKTTTTERILFYTGVnhkMGEVHDGAATMDWMVQEQERGITITSAATTAFWSgsTKQYDKYRVNIID 88
Cdd:TIGR01393   2 NIRNFSIIAHIDHGKSTLADRLLEYTGA---ISEREMREQVLDSMDLERERGITIKAQAVRLNYK--AKDGETYVLNLID 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  89 TPGHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQseTVwrqANKYG--------VPRIvyvNKMDRAGANFLRVVEQIKK 160
Cdd:TIGR01393  77 TPGHVDFSYEVSRSLAACEGALLLVDAAQGIEAQ--TL---ANVYLalendleiIPVI---NKIDLPSADPERVKKEIEE 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 161 RLGhtpvpvqlaigaeenfqgqidllkmkaifwndddqgmtyreeeipadmladaeqwrsnmveaaaeaneelmnkyLEE 240
Cdd:TIGR01393 149 VIG--------------------------------------------------------------------------LDA 154
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 241 GElsideikaglrqrtiaceivpAVCGSSFKNKGVPLVLDAVIDFLPAPieipaiKGtnpdneeitderhaDDNEPFSAL 320
Cdd:TIGR01393 155 SE---------------------AILASAKTGIGIEEILEAIVKRVPPP------KG--------------DPDAPLKAL 193
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 321 AFKIATDPFVGTLTFARVYSGVLSSGDSVINSVKGKKERVGRMVQMHANTREEiKEVRAGD----IAALIGMKDVTTGDT 396
Cdd:TIGR01393 194 IFDSHYDNYRGVVALVRVFEGTIKPGDKIRFMSTGKEYEVDEVGVFTPKLTKT-DELSAGEvgyiIAGIKDVSDVRVGDT 272
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 397 LCSIEKPIILERMDFPE--PVISVAVEPKTKADQEKMGIALGKLAQEDPS--FRVKTDEESGQTIISG-MGELHLDILVD 471
Cdd:TIGR01393 273 ITHVKNPAKEPLPGFKEvkPMVFAGLYPIDTEDYEDLRDALEKLKLNDASltYEPESSPALGFGFRCGfLGLLHMEIIQE 352
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 472 RMKREFGVEANIGKPQVAYRETIRNTCEIEgkfVRQsggrgqfghcwirfaPADegqeglefvsevvggvipkeyipaiq 551
Cdd:TIGR01393 353 RLEREFNLDLITTAPSVIYRVYLTNGEVIE---VDN---------------PSD-------------------------- 388
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 552 kgieeqmkngivagYPLLGLKAAVfdgsyhdvdsnemafkiaasmatkqltqkggavlLEPIMKVEVVTPEDYMGDVMGD 631
Cdd:TIGR01393 389 --------------LPDPGKIEHV----------------------------------EEPYVKATIITPTEYLGPIMTL 420
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1718559237 632 LNRRRGLIQGMEDTVTGKV-IRAEVPLGE-MFGYATDVRSMSQGRASYSMEFSKYAEA 687
Cdd:TIGR01393 421 CQEKRGVQTNMEYLDPNRVeLIYEMPLAEiVYDFFDKLKSISRGYASFDYELIGYRPS 478
prfC PRK00741
peptide chain release factor 3; Provisional
6-481 1.16e-43

peptide chain release factor 3; Provisional


Pssm-ID: 179105 [Multi-domain]  Cd Length: 526  Bit Score: 164.92  E-value: 1.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237   6 AINRYRNIGICAHVDAGKTTTTERILFYTGVNHKMGEV-------HdgaATMDWMVQEQERGITITSaattafwsgSTKQ 78
Cdd:PRK00741    6 EVAKRRTFAIISHPDAGKTTLTEKLLLFGGAIQEAGTVkgrksgrH---ATSDWMEMEKQRGISVTS---------SVMQ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  79 --YDKYRVNIIDTPGHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSET---VWRQANkygVPRIVYVNKMDRAGANFLR 153
Cdd:PRK00741   74 fpYRDCLINLLDTPGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTRKlmeVCRLRD---TPIFTFINKLDRDGREPLE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 154 VVEQIKKRLGHTPVPVQLAIGAEENFQGQIDLLKMKAIFWNDDDQGMTYREEEIPAdmLADAEqwrsnmveAAAEANEEL 233
Cdd:PRK00741  151 LLDEIEEVLGIACAPITWPIGMGKRFKGVYDLYNDEVELYQPGEGHTIQEVEIIKG--LDNPE--------LDELLGEDL 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 234 MNKYLEEGEL--------SIDEIKAGlrqrtiacEIVPAVCGSSFKNKGVPLVLDAVIDFLPAPIEIPAIKGT-NPDNEE 304
Cdd:PRK00741  221 AEQLREELELvqgasnefDLEAFLAG--------ELTPVFFGSALNNFGVQEFLDAFVEWAPAPQPRQTDEREvEPTEEK 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 305 itderhaddnepFSALAFKIAT--DP-------FVgtltfaRVYSGVLSSGDSVINSVKGKKERVGRMVQMHANTREEIK 375
Cdd:PRK00741  293 ------------FSGFVFKIQAnmDPkhrdriaFV------RVCSGKFEKGMKVRHVRTGKDVRISNALTFMAQDREHVE 354
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 376 EVRAGDIaalIGMKDVTT---GDTLCSIEKpiiLERMDFPE--PVISVAVEPK--TKADQEKMGIAlgKLAQEDpSFRVK 448
Cdd:PRK00741  355 EAYAGDI---IGLHNHGTiqiGDTFTQGEK---LKFTGIPNfaPELFRRVRLKnpLKQKQLQKGLV--QLSEEG-AVQVF 425
                         490       500       510
                  ....*....|....*....|....*....|...
gi 1718559237 449 TDEESGQTIISGMGELHLDILVDRMKREFGVEA 481
Cdd:PRK00741  426 RPLDNNDLILGAVGQLQFEVVAHRLKNEYNVEA 458
EFG_mtEFG_C cd03713
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational ...
611-688 4.55e-43

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: 149.60  E-value: 4.55e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718559237 611 EPIMKVEVVTPEDYMGDVMGDLNRRRGLIQGMEDTVTGKVIRAEVPLGEMFGYATDVRSMSQGRASYSMEFSKYAEAP 688
Cdd:cd03713     1 EPIMKVEVTVPEEYMGDVIGDLSSRRGQILGTESRGGWKVIKAEVPLAEMFGYSTDLRSLTQGRGSFTMEFSHYEEVP 78
EFG_mtEFG_II cd04088
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation ...
317-398 5.73e-43

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: 149.59  E-value: 5.73e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 317 FSALAFKIATDPFVGTLTFARVYSGVLSSGDSVINSVKGKKERVGRMVQMHANTREEIKEVRAGDIAALIGMKDVTTGDT 396
Cdd:cd04088     1 FSALVFKTMADPFVGKLTFFRVYSGTLKSGSTVYNSTKGKKERVGRLLRMHGKKREEVEELGAGDIGAVVGLKDTRTGDT 80

                  ..
gi 1718559237 397 LC 398
Cdd:cd04088    81 LC 82
EFG_III pfam14492
Elongation Factor G, domain III; This domain is found in Elongation Factor G. It shares a ...
411-485 1.40e-42

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: 148.40  E-value: 1.40e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1718559237 411 FPEPVISVAVEPKTKADQEKMGIALGKLAQEDPSFRVKTDEESGQTIISGMGELHLDILVDRMKREFGVEANIGK 485
Cdd:pfam14492   1 FPEPVISVAIEPKTKGDEDKLSKALNRLLEEDPTLRVERDEETGETILSGMGELHLEIVVDRLKRKYGVEVELGP 75
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
11-158 4.24e-39

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


Pssm-ID: 206672 [Multi-domain]  Cd Length: 218  Bit Score: 143.91  E-value: 4.24e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  11 RNIGICAHVDAGKTTTTERILFYTGV--NHKMGEvhdgAATMDWMVQEQERGITITSAATTAFWSGSTKQYDK--YRVNI 86
Cdd:cd01885     1 RNICIIAHVDHGKTTLSDSLLASAGIisEKLAGK----ARYLDTREDEQERGITIKSSAISLYFEYEEEKMDGndYLINL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  87 IDTPGHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDR-----------AGANFLRVV 155
Cdd:cd01885    77 IDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDRlilelklspeeAYQRLLRIV 156

                  ...
gi 1718559237 156 EQI 158
Cdd:cd01885   157 EDV 159
EFG_C pfam00679
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ...
608-693 4.96e-36

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: 130.36  E-value: 4.96e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 608 VLLEPIMKVEVVTPEDYMGDVMGDLNRRRGLIQGMEDTVTG-KVIRAEVPLGEMFGYATDVRSMSQGRASYSMEFSKYAE 686
Cdd:pfam00679   1 VLLEPIEKVTIDVPEEYVGDVISDLNSRRGEILDMDPDDGGrVVIEAEVPLAELFGFATELRSLTKGRGSFSMEFSGYQP 80

                  ....*..
gi 1718559237 687 APSNIAE 693
Cdd:pfam00679  81 VPGDILD 87
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
11-158 1.39e-34

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: 130.02  E-value: 1.39e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  11 RNIGICAHVDAGKTTTTERILFYTGVNHKMGEVHDGAatMDWMVQEQERGITITSAATTAFWSGstkqydkYRVNIIDTP 90
Cdd:cd01891     3 RNIAIIAHVDHGKTTLVDALLKQSGTFRENEEVGERV--MDSNDLERERGITILAKNTAITYKD-------TKINIIDTP 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718559237  91 GHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDRAGANFLRVVEQI 158
Cdd:cd01891    74 GHADFGGEVERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDRPDARPEEVVDEV 141
Elongation_Factor_C cd01514
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ...
611-688 5.51e-33

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: 121.44  E-value: 5.51e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1718559237 611 EPIMKVEVVTPEDYMGDVMGDLNRRRGLIQGMEDTVTGKV-IRAEVPLGEMFGYATDVRSMSQGRASYSMEFSKYAEAP 688
Cdd:cd01514     1 EPIMKVEITVPEEYLGAVIGDLSKRRGEILGMEPRGTGRVvIKAELPLAEMFGFATDLRSLTQGRASFSMEFSHYEPVP 79
LepA COG0481
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ...
11-687 5.54e-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: 5.54e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  11 RNIGICAHVDAGKTTTTERILFYTGV--NHKMGE-VHDgaaTMDWmvqEQERGITITSAATTAFWsgstKQYD--KYRVN 85
Cdd:COG0481     7 RNFSIIAHIDHGKSTLADRLLELTGTlsEREMKEqVLD---SMDL---ERERGITIKAQAVRLNY----KAKDgeTYQLN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  86 IIDTPGHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQseTVwrqANKY-----GVPRIVYVNKMDRAGANFLRVVEQIKK 160
Cdd:COG0481    77 LIDTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQ--TL---ANVYlalenDLEIIPVINKIDLPSADPERVKQEIED 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 161 RLGhtpvpvqlaIGAEEnfqgqidllkmkAIfwndddqgmtyreeeipadmLADAeqwrsnmveaaaeaneelmnkylee 240
Cdd:COG0481   152 IIG---------IDASD------------AI--------------------LVSA------------------------- 165
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 241 gelsideiKAGLrqrtiaceivpavcgssfknkGVPLVLDAVIDFLPAPieipaiKGtnpdneeitderhaDDNEPFSAL 320
Cdd:COG0481   166 --------KTGI---------------------GIEEILEAIVERIPPP------KG--------------DPDAPLQAL 196
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 321 AFKIATDPFVGTLTFARVYSGVLSSGDSVINSVKGKK---ERVGRMvqmhANTREEIKEVRAGDIAALI-GMKDVT---T 393
Cdd:COG0481   197 IFDSWYDSYRGVVVYVRVFDGTLKKGDKIKMMSTGKEyevDEVGVF----TPKMTPVDELSAGEVGYIIaGIKDVRdarV 272
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 394 GDTLCSIEKPiilerMDFP----EPVISV---AVEPKTKADQEKMGIALGKLAQEDPSFRVKtdEESGQTIISG-----M 461
Cdd:COG0481   273 GDTITLAKNP-----AAEPlpgfKEVKPMvfaGLYPVDSDDYEDLRDALEKLQLNDASLTYE--PETSAALGFGfrcgfL 345
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 462 GELHLDILVDRMKREFGVEANIGKPQVAYRETIRNTCEIEgkfvrqsggrgqfghcwIRfAPADegqeglefvsevvggv 541
Cdd:COG0481   346 GLLHMEIIQERLEREFDLDLITTAPSVVYEVTLTDGEVIE-----------------VD-NPSD---------------- 391
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 542 ipkeyIPAIQKgIEEqmkngivagypllglkaavfdgsyhdvdsnemafkiaasmatkqltqkggavLLEPIMKVEVVTP 621
Cdd:COG0481   392 -----LPDPGK-IEE----------------------------------------------------IEEPIVKATIITP 413
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718559237 622 EDYMGDVMGDLNRRRGLIQGMEDTVTGKV-IRAEVPLGE-MFGYATDVRSMSQGRASYSMEFSKYAEA 687
Cdd:COG0481   414 SEYVGAVMELCQEKRGVQKNMEYLGENRVeLTYELPLAEiVFDFFDRLKSITRGYASLDYEFIGYRES 481
PRK10218 PRK10218
translational GTPase TypA;
7-492 4.36e-32

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 132.14  E-value: 4.36e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237   7 INRYRNIGICAHVDAGKTTTTERILFYTGVNHKMGEVHDgaATMDWMVQEQERGITITSAATTAFWsgstkqyDKYRVNI 86
Cdd:PRK10218    2 IEKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQE--RVMDSNDLEKERGITILAKNTAIKW-------NDYRINI 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  87 IDTPGHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDRAGANFLRVVEQIkkrlghtp 166
Cdd:PRK10218   73 VDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQV-------- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 167 vpvqlaigaeenfqgqIDLlkmkaiFWNDDdqgmtyreeeipadmlADAEQWRSNMVEAAaeaneelmnkyleegelSID 246
Cdd:PRK10218  145 ----------------FDL------FVNLD----------------ATDEQLDFPIVYAS-----------------ALN 169
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 247 EIkAGLRQRTIACEIVPavcgssfknkgvplVLDAVIDFLPAPieipaikgtnpdneeitderHADDNEPFSALAFKIAT 326
Cdd:PRK10218  170 GI-AGLDHEDMAEDMTP--------------LYQAIVDHVPAP--------------------DVDLDGPFQMQISQLDY 214
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 327 DPFVGTLTFARVYSGVLSSGD--SVINSV-KGKKERVGRMVQMHANTREEIKEVRAGDIAALIGMKDVTTGDTLCSIEKP 403
Cdd:PRK10218  215 NSYVGVIGIGRIKRGKVKPNQqvTIIDSEgKTRNAKVGKVLGHLGLERIETDLAEAGDIVAITGLGELNISDTVCDTQNV 294
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 404 IILERMDFPEPVISVAVEPKTKADQEKMGI------ALGKLAQE---DPSFRVKTDEESGQTIISGMGELHLDILVDRMK 474
Cdd:PRK10218  295 EALPALSVDEPTVSMFFCVNTSPFCGKEGKfvtsrqILDRLNKElvhNVALRVEETEDADAFRVSGRGELHLSVLIENMR 374
                         490
                  ....*....|....*...
gi 1718559237 475 REfGVEANIGKPQVAYRE 492
Cdd:PRK10218  375 RE-GFELAVSRPKVIFRE 391
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
11-163 1.72e-31

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: 120.72  E-value: 1.72e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  11 RNIGICAHVDAGKTTTTERILFYTGV---NHKMGEVhdgaatMDWMVQEQERGITITSAATTAFWSGSTKQydKYRVNII 87
Cdd:cd01890     1 RNFSIIAHIDHGKSTLADRLLELTGTvseREMKEQV------LDSMDLERERGITIKAQAVRLFYKAKDGE--EYLLNLI 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1718559237  88 DTPGHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDRAGANFLRVVEQIKKRLG 163
Cdd:cd01890    73 DTPGHVDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVKQEIEDVLG 148
mtEFG1_C cd04097
mtEFG1_C: C-terminus of mitochondrial Elongation factor G1 (mtEFG1)-like proteins found in ...
611-688 3.94e-30

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: 113.57  E-value: 3.94e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718559237 611 EPIMKVEVVTPEDYMGDVMGDLNRRRGLIQGMEDTVTGKVIRAEVPLGEMFGYATDVRSMSQGRASYSMEFSKYAEAP 688
Cdd:cd04097     1 EPIMKVEVTAPTEFQGNVIGLLNKRKGTIVDTDTGEDEFTLEAEVPLNDMFGYSTELRSMTQGKGEFSMEFSRYAPVP 78
mtEFG2_II_like cd04092
Domain II of mitochondrial elongation factor G2-like proteins found in eukaryotes; Eukaryotic ...
319-399 1.81e-27

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: 105.86  E-value: 1.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 319 ALAFKIATDPFVGTLTFARVYSGVLSSGDSVINSVKGKKERVGRMVQMHANTREEIKEVRAGDIAALIGMKDVTTGDTLC 398
Cdd:cd04092     3 ALAFKVIHDPQRGPLVFVRVYSGTLKAGSNVYNTTTGKKERISRLLKMHADQTEEVDSLSAGNIGVITGLKVTSTGDTLV 82

                  .
gi 1718559237 399 S 399
Cdd:cd04092    83 S 83
EFG_like_IV cd01680
Elongation Factor G-like domain IV. This family includes the translational elongation factor ...
490-606 2.38e-26

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: 103.86  E-value: 2.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 490 YRETIRNTCEIEGKFVRQSGGRGQFGHCWIRFAPADEGqEGLEFVSEVVGGVIPKEYIPAIQKGIEEQMKNGIVAGYPLL 569
Cdd:cd01680     1 YRETIRKSVEATGEFERELGGKPQFGEVTLRVEPLERG-SGVRVVDPVDEELLPAELKEAVEEGIRDACASGPLTGYPLT 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1718559237 570 GLKAAVFDGSYHDVDSNEMAFKIAASMATKQLTQKGG 606
Cdd:cd01680    80 DVRVTVLDVPYHEGVSTEAGFRAAAGRAFESAAQKAG 116
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
11-146 1.35e-23

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


Pssm-ID: 206730 [Multi-domain]  Cd Length: 213  Bit Score: 99.26  E-value: 1.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  11 RNIGICAHVDAGKTTTTERILFYTgvnHKM-GEVHDGAAT---MDWMVQEQERGITITSAATTAFWSGStkQYDKYRVNI 86
Cdd:cd04167     1 RNVCIAGHLHHGKTSLLDMLIEQT---HKRtPSVKLGWKPlryTDTRKDEQERGISIKSNPISLVLEDS--KGKSYLINI 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  87 IDTPGHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDR 146
Cdd:cd04167    76 IDTPGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDR 135
mtEFG1_II_like cd04091
Domain II of mitochondrial elongation factor G1-like proteins found in eukaryotes; Eukaryotic ...
317-399 1.46e-23

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: 94.66  E-value: 1.46e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 317 FSALAFKIATDPFvGTLTFARVYSGVLSSGDSVINSVKGKKERVGRMVQMHANTREEIKEVRAGDIAALIGMkDVTTGDT 396
Cdd:cd04091     1 FVGLAFKLEEGRF-GQLTYMRVYQGVLRKGDTIYNVRTGKKVRVPRLVRMHSDEMEDIEEVYAGDICALFGI-DCASGDT 78

                  ...
gi 1718559237 397 LCS 399
Cdd:cd04091    79 FTD 81
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
10-187 1.74e-23

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


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 97.44  E-value: 1.74e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  10 YRNIGICAHVDAGKTTTTERILFYTGVNHKMGEvhdGAATMDWMVQEQERGITitsaattafwsgstkqydkYRVNIIDT 89
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYP---GTTRNYVTTVIEEDGKT-------------------YKFNLLDT 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  90 PGHVDF-------TIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQAnKYGVPRIVYVNKMDRAGANFLRVVEQIKKRL 162
Cdd:TIGR00231  59 AGQEDYdairrlyYPQVERSLRVFDIVILVLDVEEILEKQTKEIIHHA-DSGVPIILVGNKIDLKDADLKTHVASEFAKL 137
                         170       180
                  ....*....|....*....|....*
gi 1718559237 163 GHTPVpVQLAIGAEENFQGQIDLLK 187
Cdd:TIGR00231 138 NGEPI-IPLSAETGKNIDSAFKIVE 161
EFG_III-like cd16257
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G ...
414-484 3.84e-22

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: 90.49  E-value: 3.84e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1718559237 414 PVISVAVEPKTKADQEKMGIALGKLAQEDPSFRVKTDEESGQTIISGMGELHLDILVDRMKREFGVEANIG 484
Cdd:cd16257     1 PVVFVTVEVKNPLDQEKLLEGLERLSEEDPALQVYREESTGEFILSGLGELHLEIIVARLEREYGVELVVS 71
EF2_snRNP_III cd16261
Domain III of Elongation Factor 2 (EF2); This model represents domain III of Elongation factor ...
414-485 2.19e-17

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: 76.84  E-value: 2.19e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1718559237 414 PVISVAVEPKTKADQEKMGIALGKLAQEDPSFRVKTDEEsGQTIISGMGELHLDILVDRMKREF-GVEANIGK 485
Cdd:cd16261     1 PVVRVAVEPKNPSDLPKLVEGLKKLAKSDPTVQVKIEEE-GEHLIAGAGELHLEICLKDLKEDFaGIEIKVSD 72
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
331-398 3.29e-15

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: 70.76  E-value: 3.29e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1718559237 331 GTLTFARVYSGVLSSGDSVIN-----SVKGKKERVGRMVQMHANTREEIKEVRAGDIAALIGMKDVTTGDTLC 398
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRIlpngtGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
12-162 5.10e-14

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: 74.58  E-value: 5.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  12 NIGICAHVDAGKTTTTERILFYTGV--NHKMGEVHDGAAT-----------MDWMVQEQERGITItSAATTAFwsgstkQ 78
Cdd:COG5256     9 NLVVIGHVDHGKSTLVGRLLYETGAidEHIIEKYEEEAEKkgkesfkfawvMDRLKEERERGVTI-DLAHKKF------E 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  79 YDKYRVNIIDTPGHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPR-IVYVNKMDRAG---ANFLRV 154
Cdd:COG5256    82 TDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQlIVAVNKMDAVNyseKRYEEV 161

                  ....*...
gi 1718559237 155 VEQIKKRL 162
Cdd:COG5256   162 KEEVSKLL 169
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
12-162 2.21e-13

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 72.65  E-value: 2.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  12 NIGICAHVDAGKTTTTERILFYTG-VNHKMGEVHDGAA------------TMDWMVQEQERGITItSAATTAFwsgstkQ 78
Cdd:PRK12317    8 NLAVIGHVDHGKSTLVGRLLYETGaIDEHIIEELREEAkekgkesfkfawVMDRLKEERERGVTI-DLAHKKF------E 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  79 YDKYRVNIIDTPGHVDFTIEVERSLRVLDGAVVVFCG--TSGVEPQS-ETVWrQANKYGVPR-IVYVNKMDRAG---ANF 151
Cdd:PRK12317   81 TDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAAddAGGVMPQTrEHVF-LARTLGINQlIVAINKMDAVNydeKRY 159
                         170
                  ....*....|.
gi 1718559237 152 LRVVEQIKKRL 162
Cdd:PRK12317  160 EEVKEEVSKLL 170
BipA_TypA_II cd03691
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ...
317-403 2.95e-13

Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios and is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion. The domain II of BipA shows similarity to the domain II of the elongation factors (EFs) EF-G and EF-Tu.


Pssm-ID: 293892 [Multi-domain]  Cd Length: 94  Bit Score: 66.06  E-value: 2.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 317 FSALAFKIATDPFVGTLTFARVYSGVLSSGDSVINSVKGKKERVGRMVQMHA---NTREEIKEVRAGDIAALIGMKDVTT 393
Cdd:cd03691     1 FQMLVTTLDYDDYLGRIAIGRIFSGTVKVGQQVTVVDEDGKIEKGRVTKLFGfegLERVEVEEAEAGDIVAIAGLEDITI 80
                          90
                  ....*....|
gi 1718559237 394 GDTLCSIEKP 403
Cdd:cd03691    81 GDTICDPEVP 90
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
12-151 4.24e-13

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: 69.06  E-value: 4.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  12 NIGICAHVDAGKTTTTERILFYTGV--NHKMGEVHDGAAT-----------MDWMVQEQERGITItSAATTAFwsgstkQ 78
Cdd:cd01883     1 NLVVIGHVDAGKSTLTGHLLYKLGGvdKRTIEKYEKEAKEmgkesfkyawvLDKLKEERERGVTI-DVGLAKF------E 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  79 YDKYRVNIIDTPGHVDF-------TIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPR-IVYVNKMDRAGAN 150
Cdd:cd01883    74 TEKYRFTIIDAPGHRDFvknmitgASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQlIVAVNKMDDVTVN 153

                  .
gi 1718559237 151 F 151
Cdd:cd01883   154 W 154
eEF2_snRNP_like_C cd04096
eEF2_snRNP_like_C: this family represents a C-terminal domain of eukaryotic elongation factor ...
611-682 5.01e-12

eEF2_snRNP_like_C: this family represents a C-terminal domain of eukaryotic elongation factor 2 (eEF-2) and a homologous domain of the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and, its yeast counterpart Snu114p. Yeast Snu114p is essential for cell viability and for splicing in vivo. U5-116 kD binds GTP. Experiments suggest that GTP binding and probably GTP hydrolysis is important for the function of the U5-116 kD/Snu114p. In complex with GTP, EF-2 promotes the translocation step of translation. During translocation the peptidyl-tRNA is moved from the A site to the P site, the uncharged tRNA from the P site to the E-site and, the mRNA is shifted one codon relative to the ribosome.


Pssm-ID: 239763 [Multi-domain]  Cd Length: 80  Bit Score: 61.79  E-value: 5.01e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1718559237 611 EPIMKVEVVTPEDYMGDVMGDLNRRRGLIQGmEDTVTGK---VIRAEVPLGEMFGYATDVRSMSQGRASYSMEFS 682
Cdd:cd04096     1 EPIYLVEIQCPEDALGKVYSVLSKRRGHVLS-EEPKEGTplfEIKAYLPVIESFGFETDLRSATSGQAFPQLVFS 74
lepA_C cd03709
lepA_C: This family represents the C-terminal region of LepA, a GTP-binding protein localized ...
611-687 1.20e-11

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


Pssm-ID: 239680 [Multi-domain]  Cd Length: 80  Bit Score: 60.97  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 611 EPIMKVEVVTPEDYMGDVMGDLNRRRGLIQGMEdTVTGK--VIRAEVPLGEM-FGYATDVRSMSQGRASYSMEFSKYAEA 687
Cdd:cd03709     1 EPFVKATIITPSEYLGAIMELCQERRGVQKDME-YLDANrvMLTYELPLAEIvYDFFDKLKSISKGYASLDYELIGYRES 79
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
12-145 5.21e-11

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


Pssm-ID: 129576 [Multi-domain]  Cd Length: 394  Bit Score: 65.18  E-value: 5.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  12 NIGICAHVDAGKTTTTERIlfyTGVNHKMGevhdGAATMDW-----MVQEQERGITITSAatTAFWSGSTKQYDKyrvni 86
Cdd:TIGR00485  14 NVGTIGHVDHGKTTLTAAI---TTVLAKEG----GAAARAYdqidnAPEEKARGITINTA--HVEYETETRHYAH----- 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  87 IDTPGHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRI-VYVNKMD 145
Cdd:TIGR00485  80 VDCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIvVFLNKCD 139
infB CHL00189
translation initiation factor 2; Provisional
5-160 6.31e-11

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 65.62  E-value: 6.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237   5 TAINRYRNIGICAHVDAGKTTTTERILFYTGVNHKMGevhdgaatmdwmvqeqerGITITSAATTAFWsgstkQYDKYRV 84
Cdd:CHL00189  239 NSINRPPIVTILGHVDHGKTTLLDKIRKTQIAQKEAG------------------GITQKIGAYEVEF-----EYKDENQ 295
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718559237  85 NII--DTPGHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDRAGANFLRVVEQIKK 160
Cdd:CHL00189  296 KIVflDTPGHEAFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANTERIKQQLAK 373
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
317-398 7.21e-11

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: 58.82  E-value: 7.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 317 FSALAFKIATDPFVGTLTFARVYSGVLSSGDSVINSVKGKKERVGRMVQMHantrEEIKEVRAGDIAAL--IGMKDVTTG 394
Cdd:cd01342     1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFH----EEVDEAKAGDIVGIgiLGVKDILTG 76

                  ....
gi 1718559237 395 DTLC 398
Cdd:cd01342    77 DTLT 80
PLN03126 PLN03126
Elongation factor Tu; Provisional
12-156 7.73e-11

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 65.02  E-value: 7.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  12 NIGICAHVDAGKTTTTERI-LFYTGVNHKMGEVHDgaaTMDWMVQEQERGITITSAatTAFWSGSTKQYDKyrvniIDTP 90
Cdd:PLN03126   83 NIGTIGHVDHGKTTLTAALtMALASMGGSAPKKYD---EIDAAPEERARGITINTA--TVEYETENRHYAH-----VDCP 152
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718559237  91 GHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPR-IVYVNKMDRA-GANFLRVVE 156
Cdd:PLN03126  153 GHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNmVVFLNKQDQVdDEELLELVE 220
IF-2 TIGR00487
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ...
13-160 2.03e-10

translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]


Pssm-ID: 273102 [Multi-domain]  Cd Length: 587  Bit Score: 64.02  E-value: 2.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  13 IGICAHVDAGKTTTTERILfYTGVNHKmgevhdgaatmdwmvqeQERGITITSAATTafwsgsTKQYDKYRVNIIDTPGH 92
Cdd:TIGR00487  90 VTIMGHVDHGKTSLLDSIR-KTKVAQG-----------------EAGGITQHIGAYH------VENEDGKMITFLDTPGH 145
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718559237  93 VDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDRAGANFLRVVEQIKK 160
Cdd:TIGR00487 146 EAFTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVPIIVAINKIDKPEANPDRVKQELSE 213
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
12-145 1.95e-09

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: 57.59  E-value: 1.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  12 NIGICAHVDAGKTTTTERIlfyTGVNHKMG--EVHDGAAtMDWMVQEQERGITItsAATTAFWSGSTKQYDKyrvniIDT 89
Cdd:cd01884     4 NVGTIGHVDHGKTTLTAAI---TKVLAKKGgaKAKKYDE-IDKAPEEKARGITI--NTAHVEYETANRHYAH-----VDC 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1718559237  90 PGHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRI-VYVNKMD 145
Cdd:cd01884    73 PGHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIvVFLNKAD 129
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
18-160 2.71e-09

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


Pssm-ID: 206674 [Multi-domain]  Cd Length: 169  Bit Score: 56.71  E-value: 2.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  18 HVDAGKTTTTERIlfyTGVNhkmgevhdgaatmdwmVQEQE-RGITITSAATTAFWSGSTKqydkyRVNIIDTPGHVDFT 96
Cdd:cd01887     8 HVDHGKTTLLDKI---RKTN----------------VAAGEaGGITQHIGAYQVPIDVKIP-----GITFIDTPGHEAFT 63
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1718559237  97 IEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDR---AGANFLRVVEQIKK 160
Cdd:cd01887    64 NMRARGASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKpygTEADPERVKNELSE 130
Tet_C cd03711
Tet_C: C-terminus of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology ...
611-688 3.98e-09

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: 53.78  E-value: 3.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 611 EPIMKVEVVTPEDYMGDVMGDLNRRRG---LIQGMEDTVTgkvIRAEVPLGEMFGYATDVRSMSQGRASYSMEFSKYAEA 687
Cdd:cd03711     1 EPYLRFELEVPQDALGRAMSDLAKMGAtfeDPQIKGDEVT---LEGTIPVATSQDYQSELPSYTHGEGVLETEFKGYRPC 77

                  .
gi 1718559237 688 P 688
Cdd:cd03711    78 H 78
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
12-166 5.48e-09

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 58.99  E-value: 5.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  12 NIGICAHVDAGKTTTTERILFYTG-VNHKMGEVHDGAAT------------MDWMVQEQERGITITsaatTAFWSGSTKq 78
Cdd:PTZ00141    9 NLVVIGHVDSGKSTTTGHLIYKCGgIDKRTIEKFEKEAAemgkgsfkyawvLDKLKAERERGITID----IALWKFETP- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  79 ydKYRVNIIDTPGHVDF-------TIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPR-IVYVNKMDRAGAN 150
Cdd:PTZ00141   84 --KYYFTIIDAPGHRDFiknmitgTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQmIVCINKMDDKTVN 161
                         170       180
                  ....*....|....*....|....
gi 1718559237 151 FLR-----VVEQIK---KRLGHTP 166
Cdd:PTZ00141  162 YSQerydeIKKEVSaylKKVGYNP 185
PLN03127 PLN03127
Elongation factor Tu; Provisional
1-145 6.42e-09

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 58.68  E-value: 6.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237   1 MARTTAINRYRNIGICAHVDAGKTTTTERIlfyTGVNHKMGEVHDGA-ATMDWMVQEQERGITITSAATTafWSGSTKQY 79
Cdd:PLN03127   52 MATFTRTKPHVNVGTIGHVDHGKTTLTAAI---TKVLAEEGKAKAVAfDEIDKAPEEKARGITIATAHVE--YETAKRHY 126
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1718559237  80 DKyrvniIDTPGHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIV-YVNKMD 145
Cdd:PLN03127  127 AH-----VDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVvFLNKVD 188
Tet_II cd03690
Domain II of ribosomal protection proteins Tet(M) and Tet(O); This subfamily represents domain ...
315-397 6.58e-09

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


Pssm-ID: 293891 [Multi-domain]  Cd Length: 86  Bit Score: 53.40  E-value: 6.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 315 EPFSALAFKIATDPFVGTLTFARVYSGVLSSGDSVINSVKGKKERVGRMVQMHANTREEIKEVRAGDIAALIGMKDVTTG 394
Cdd:cd03690     2 SELSGTVFKIEYDPKGERLAYLRLYSGTLRLRDSVRVSGEEEKIKITELRTFENGELVKVDRVYAGDIAILVGLKSLRVG 81

                  ...
gi 1718559237 395 DTL 397
Cdd:cd03690    82 DVL 84
PRK12736 PRK12736
elongation factor Tu; Reviewed
12-145 1.57e-08

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 57.26  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  12 NIGICAHVDAGKTTTTERIlfyTGVNHKMGEVHDGA-ATMDWMVQEQERGITITSAATTafWSGSTKQYDKyrvniIDTP 90
Cdd:PRK12736   14 NIGTIGHVDHGKTTLTAAI---TKVLAERGLNQAKDyDSIDAAPEEKERGITINTAHVE--YETEKRHYAH-----VDCP 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1718559237  91 GHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRI-VYVNKMD 145
Cdd:PRK12736   84 GHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLvVFLNKVD 139
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
12-160 1.90e-08

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


Pssm-ID: 129567 [Multi-domain]  Cd Length: 581  Bit Score: 57.58  E-value: 1.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  12 NIGICAHVDAGKTTTTERIlfyTGVNhkmgevhdgaatMDWMVQEQERGITITSAatTAFWSgstkqYDKYRVNIIDTPG 91
Cdd:TIGR00475   2 IIATAGHVDHGKTTLLKAL---TGIA------------ADRLPEEKKRGMTIDLG--FAYFP-----LPDYRLGFIDVPG 59
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  92 HVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPR-IVYVNKMDRAGANFLRVVEQIKK 160
Cdd:TIGR00475  60 HEKFISNAIAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHtIVVITKADRVNEEEIKRTEMFMK 129
BipA_TypA_C cd03710
BipA_TypA_C: a C-terminal portion of BipA or TypA having homology to the C terminal domains of ...
611-685 2.24e-08

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: 51.35  E-value: 2.24e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1718559237 611 EPIMKVEVVTPEDYMGDVMGDLNRRRGLIQGMEDTVTGKV-IRAEVPLGEMFGYATDVRSMSQGRASYSMEFSKYA 685
Cdd:cd03710     1 EPIEELTIDVPEEYSGAVIEKLGKRKGEMVDMEPDGNGRTrLEFKIPSRGLIGFRSEFLTDTRGTGIMNHVFDGYE 76
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
14-169 3.38e-08

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: 53.23  E-value: 3.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  14 GICAHVDAGKTTTTERIL--FYTGVNHKMGEvhdgaatmdwmvqeqergititsaaTTAFWSGS-TKQYDKYRVNIIDTP 90
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLggEVGEVSDVPGT-------------------------TRDPDVYVkELDKGKVKLVLVDTP 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  91 GHVDF-----TIEVERSLRVLDGAVVVFCGTSG--VEPQSETVWRQANKYGVPRIVYVNKMDRAGANFLRVVEQIKKRLG 163
Cdd:cd00882    56 GLDEFgglgrEELARLLLRGADLILLVVDSTDResEEDAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELAK 135

                  ....*.
gi 1718559237 164 HTPVPV 169
Cdd:cd00882   136 ILGVPV 141
EF2_II cd16268
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 ...
324-399 3.99e-08

Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 (EF-2) found in eukaryotes and archaea. During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. This translocation step is catalyzed by EF-2_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site.


Pssm-ID: 293913 [Multi-domain]  Cd Length: 96  Bit Score: 51.45  E-value: 3.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 324 IATDPFVGTLTFARVYSGVLSSGDSV----INSVKGKKE-----RVGRMVQMHANTREEIKEVRAGDIAALIGMKD--VT 392
Cdd:cd16268    10 VPTDKGAGFVAFGRVFSGTVRRGQEVyilgPKYVPGKKDdlkkkRIQQTYLMMGREREPVDEVPAGNIVGLVGLDDflAK 89

                  ....*..
gi 1718559237 393 TGDTLCS 399
Cdd:cd16268    90 SGTTTSS 96
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
13-166 4.85e-08

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


Pssm-ID: 206734 [Multi-domain]  Cd Length: 170  Bit Score: 52.99  E-value: 4.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  13 IGICAHVDAGKTTTTERIlfyTGVNhkmgevhdgaatMDWMVQEQERGITIT-SAATTAFWSGStkqydkyRVNIIDTPG 91
Cdd:cd04171     2 IGTAGHIDHGKTTLIKAL---TGIE------------TDRLPEEKKRGITIDlGFAYLDLPDGK-------RLGFIDVPG 59
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1718559237  92 HVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPR-IVYVNKMDRAGANFL-RVVEQIKKRLGHTP 166
Cdd:cd04171    60 HEKFVKNMLAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKgLVVLTKADLVDEDRLeLVEEEILELLAGTF 136
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
15-167 1.59e-07

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: 52.57  E-value: 1.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  15 ICAHVDAGKTTTTERILFYTG--------------VNHKMGEVHDGAATMDWMVQEQERGITITSA----ATtafwsgst 76
Cdd:cd04166     4 TCGSVDDGKSTLIGRLLYDSKsifedqlaalerskSSGTQGEKLDLALLVDGLQAEREQGITIDVAyryfST-------- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  77 kqyDKYRVNIIDTPGHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVY-VNKMDRAG---ANFL 152
Cdd:cd04166    76 ---PKRKFIIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVaVNKMDLVDydeEVFE 152
                         170
                  ....*....|....*...
gi 1718559237 153 RVVEQIK---KRLGHTPV 167
Cdd:cd04166   153 EIKADYLafaASLGIEDI 170
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
12-165 2.00e-07

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: 51.98  E-value: 2.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  12 NIGICAHVDAGKTTTTeRILfytgvnhkmGEVHDGAAtMDWMVQEQERGITI--------TSAATTAFWSGStKQYDKYR 83
Cdd:cd01889     2 NVGLLGHVDSGKTSLA-KAL---------SEIASTAA-FDKNPQSQERGITLdlgfssfeVDKPKHLEDNEN-PQIENYQ 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  84 VNIIDTPGHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDRAGANFLRV-VEQIKKRL 162
Cdd:cd01889    70 ITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDLIPEEERKRkIEKMKKRL 149

                  ...
gi 1718559237 163 GHT 165
Cdd:cd01889   150 QKT 152
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
12-145 2.46e-07

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: 53.62  E-value: 2.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  12 NIGICAHVDAGKTTTTERIlfyTGVNHKMGEVHDGA-ATMDWMVQEQERGITITSAAT---TAfwsgsTKQYDKyrvniI 87
Cdd:COG0050    14 NIGTIGHVDHGKTTLTAAI---TKVLAKKGGAKAKAyDQIDKAPEEKERGITINTSHVeyeTE-----KRHYAH-----V 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718559237  88 DTPGHVDFtieverslrV---------LDGAVVVFCGTSGVEPQSETVWRQANKYGVPRI-VYVNKMD 145
Cdd:COG0050    81 DCPGHADY---------VknmitgaaqMDGAILVVSATDGPMPQTREHILLARQVGVPYIvVFLNKCD 139
PRK12735 PRK12735
elongation factor Tu; Reviewed
12-145 4.52e-07

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 52.53  E-value: 4.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  12 NIGICAHVDAGKTTTTERIlfyTGVNHKMGevhdGAATMDW-----MVQEQERGITITSAATTafWSGSTKQYDKyrvni 86
Cdd:PRK12735   14 NVGTIGHVDHGKTTLTAAI---TKVLAKKG----GGEAKAYdqidnAPEEKARGITINTSHVE--YETANRHYAH----- 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  87 IDTPGHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRI-VYVNKMD 145
Cdd:PRK12735   80 VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIvVFLNKCD 139
PRK00049 PRK00049
elongation factor Tu; Reviewed
12-145 6.12e-07

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 52.11  E-value: 6.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  12 NIGICAHVDAGKTTTTERIlfyTGVNHKMGevhdGAATMDW-----MVQEQERGITITSAAT---TAfwsgsTKQYDKyr 83
Cdd:PRK00049   14 NVGTIGHVDHGKTTLTAAI---TKVLAKKG----GAEAKAYdqidkAPEEKARGITINTAHVeyeTE-----KRHYAH-- 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1718559237  84 vniIDTPGHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQS-ETVW--RQAnkyGVPRI-VYVNKMD 145
Cdd:PRK00049   80 ---VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTrEHILlaRQV---GVPYIvVFLNKCD 139
Tet_III cd16258
Domain III of Tetracycline resistance protein Tet; Tetracycline resistance proteins, including ...
414-481 1.02e-06

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


Pssm-ID: 293915 [Multi-domain]  Cd Length: 71  Bit Score: 46.55  E-value: 1.02e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718559237 414 PVISVAVEPKTKADQEKMGIALGKLAQEDPSFRVKTDEESGQTIISGMGELHLDILVDRMKREFGVEA 481
Cdd:cd16258     1 PMLQTTIRPRKPEQRERLLDALTELSDEDPLLKYRVDSTTHEIILSLYGEVQMEVISALLEEKYGVEV 68
eEF2_C_snRNP cd04098
eEF2_C_snRNP: This family includes a C-terminal portion of the spliceosomal human 116kD U5 ...
611-688 1.12e-06

eEF2_C_snRNP: This family includes a C-terminal portion of the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and, its yeast counterpart Snu114p. This domain is homologous to the C-terminal domain of the eukaryotic translational elongation factor EF-2. Yeast Snu114p is essential for cell viability and for splicing in vivo. U5-116 kD binds GTP. Experiments suggest that GTP binding and probably GTP hydrolysis is important for the function of the U5-116 kD/Snu114p. In complex with GTP, EF-2 promotes the translocation step of translation. During translocation the peptidyl-tRNA is moved from the A site to the P site, the uncharged tRNA from the P site to the E-site and, the mRNA is shifted one codon relative to the ribosome.


Pssm-ID: 239765 [Multi-domain]  Cd Length: 80  Bit Score: 46.86  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 611 EPIMKVEVVTPEDYMGDVMGDLNRRRG-LIQGMEDTVTGKV-IRAEVPLGEMFGYATDVRSMSQGRASYSMEFSKYAEAP 688
Cdd:cd04098     1 EPIYEVEITCPADAVSAVYEVLSRRRGhVIYDTPIPGTPLYeVKAFIPVIESFGFETDLRVHTQGQAFCQSVFDHWQIVP 80
tufA CHL00071
elongation factor Tu
12-145 1.71e-06

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 50.73  E-value: 1.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  12 NIGICAHVDAGKTTTTERI-----LFYTGVNHKMGEVhDGAAtmdwmvQEQERGITITSAATTafWSGSTKQYDKyrvni 86
Cdd:CHL00071   14 NIGTIGHVDHGKTTLTAAItmtlaAKGGAKAKKYDEI-DSAP------EEKARGITINTAHVE--YETENRHYAH----- 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  87 IDTPGHVDFTIEVERSLRVLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRI-VYVNKMD 145
Cdd:CHL00071   80 VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIvVFLNKED 139
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
12-118 2.51e-06

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 50.47  E-value: 2.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  12 NIGICAHVDAGKTTTTERILF-YTGVNHKMGEVHDGAAT------------MDWMVQEQERGITITsaatTAFWSGSTKq 78
Cdd:PLN00043    9 NIVVIGHVDSGKSTTTGHLIYkLGGIDKRVIERFEKEAAemnkrsfkyawvLDKLKAERERGITID----IALWKFETT- 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1718559237  79 ydKYRVNIIDTPGHVDFTIEVERSLRVLDGAVVVFCGTSG 118
Cdd:PLN00043   84 --KYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTG 121
PRK04004 PRK04004
translation initiation factor IF-2; Validated
18-146 3.07e-05

translation initiation factor IF-2; Validated


Pssm-ID: 235195 [Multi-domain]  Cd Length: 586  Bit Score: 47.10  E-value: 3.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  18 HVDAGKTTTTERILFYTGVNHKMGEV--HDGAATMDWMVQEQErgititsaattafwSGSTKQYDKYRVNI-----IDTP 90
Cdd:PRK04004   14 HVDHGKTTLLDKIRGTAVAAKEAGGItqHIGATEVPIDVIEKI--------------AGPLKKPLPIKLKIpgllfIDTP 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1718559237  91 GHVDFTieverSLR-----VLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDR 146
Cdd:PRK04004   80 GHEAFT-----NLRkrggaLADIAILVVDINEGFQPQTIEAINILKRRKTPFVVAANKIDR 135
RF3_II cd03689
Domain II of bacterial Release Factor 3; This subfamily represents domain II of bacterial ...
317-399 6.94e-05

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: 41.87  E-value: 6.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 317 FSALAFKIAT--DP-FVGTLTFARVYSGVLSSGDSVINSVKGKKERVGRMVQMHANTREEIKEVRAGDIAALIGMKDVTT 393
Cdd:cd03689     1 FSGFVFKIQAnmDPkHRDRIAFLRVCSGKFERGMKVKHVRTGKEVRLSNATTFMAQDRETVEEAYPGDIIGLPNHGTFQI 80

                  ....*.
gi 1718559237 394 GDTLCS 399
Cdd:cd03689    81 GDTFTE 86
mtEFG2_like_IV cd01693
mtEF-G2 domain IV. This subfamily is a part the of mitochondrial transcriptional elongation ...
488-606 8.63e-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: 42.38  E-value: 8.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237 488 VAYRETIRNTCEIEGKFVRQSGGRGQFGHCWIRFAPADE---GQEGLEFvSEVVGGVIPKEYIPAIQKGIEEQMKNGIVA 564
Cdd:cd01693     1 IAYRETILEPARATDTLEKVIGDKKHSVTVTMEVRPNQAsssPVELIEL-ANSAIEVLLKRIQEAVENGVHSALLQGPLL 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1718559237 565 GYPLLGLKAAVFDGSYHDVDSNEMaFKIAASMATKQLTQKGG 606
Cdd:cd01693    80 GFPVQDVAITLHSLTIGPGTSPTM-ISACASQCVQKALKSAG 120
EF4_III cd16260
Domain III of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly ...
414-480 1.17e-04

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


Pssm-ID: 293917 [Multi-domain]  Cd Length: 76  Bit Score: 40.95  E-value: 1.17e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1718559237 414 PVISVAVEPKTKADQEKMGIALGKLAQEDPSFRVKtdEESGQTIISG-----MGELHLDILVDRMKREFGVE 480
Cdd:cd16260     1 PMVFAGLYPVDGSDYEELRDALEKLTLNDASVTFE--PETSSALGFGfrcgfLGLLHMEVFQERLEREYGLD 70
BipA_III cd16263
Domain III of GTP-binding protein BipA (TypA); BipA (also called TypA) is a highly conserved ...
435-484 1.30e-04

Domain III of GTP-binding protein BipA (TypA); BipA (also called TypA) is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios. It 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: 293920 [Multi-domain]  Cd Length: 79  Bit Score: 40.76  E-value: 1.30e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1718559237 435 LGKLAQEDPSFRVKTDEESGQTIISGMGELHLDILVDRMKREfGVEANIG 484
Cdd:cd16263    31 LEKELETNVALRVEETESPDSFIVSGRGELHLSILIETMRRE-GFELQVS 79
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
87-157 2.09e-04

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: 44.23  E-value: 2.09e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1718559237  87 IDTPGHVDFTieverSLR-----VLDGAVVVFCGTSGVEPQSETVWRQANKYGVPRIVYVNKMDRAGANFLRVVEQ 157
Cdd:COG0532    56 LDTPGHEAFT-----AMRargaqVTDIVILVVAADDGVMPQTIEAINHAKAAGVPIIVAINKIDKPGANPDRVKQE 126
snRNP_III cd16264
Domain III of the spliceosomal 116kD U5 small nuclear ribonucleoprotein (snRNP) component; ...
414-477 2.62e-04

Domain III of the spliceosomal 116kD U5 small nuclear ribonucleoprotein (snRNP) component; Domain III of the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and its yeast counterpart Snu114p is homologous to domain III of the eukaryotic translational elongation factor EF-2. U5-116 kD is a GTPase component of the spliceosome complex which functions in the processing of precursor mRNAs to produce mature mRNAs.


Pssm-ID: 293921 [Multi-domain]  Cd Length: 72  Bit Score: 39.79  E-value: 2.62e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1718559237 414 PVISVAVEPKTKADQEKMGIALGKLAQEDPSFRVKTdEESGQTIISGMGELHLDILVDRMKREF 477
Cdd:cd16264     1 SVFKIAVEPLNPSELPKMLDGLRKVNKSYPLLITKV-EESGEHVILGTGELYMDCVMHDLRKMY 63
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
73-191 3.32e-04

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


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 41.85  E-value: 3.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  73 SGSTKQYDKYRVNIIDTPGhVDFTIE-----VERSLRVL---DGAVVVFCGTSGVEPQSETVwRQANKYGVPRIVYVNKM 144
Cdd:cd00880    37 RKEWELLPLGPVVLIDTPG-LDEEGGlgrerVEEARQVAdraDLVLLVVDSDLTPVEEEAKL-GLLRERGKPVLLVLNKI 114
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1718559237 145 DRAGANFLRVVEQIKKRLGHTPVPVqLAIGAEEnfQGQIDLLKMKAI 191
Cdd:cd00880   115 DLVPESEEEELLRERKLELLPDLPV-IAVSALP--GEGIDELRKKIA 158
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
15-169 3.43e-04

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


Pssm-ID: 442140 [Multi-domain]  Cd Length: 430  Bit Score: 43.54  E-value: 3.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  15 ICAHVDAGKTTTTERILFYTG---------VnHKMGEVHdGAATMDW------MVQEQERGITITSA----ATtafwsgs 75
Cdd:COG2895    22 TCGSVDDGKSTLIGRLLYDTKsifedqlaaL-ERDSKKR-GTQEIDLalltdgLQAEREQGITIDVAyryfST------- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  76 tkqyDKYRVNIIDTPGHVDFTieverslRVL-------DGAVVVFCGTSGVEPQSEtvwRQAnkY-----GVPRIVY-VN 142
Cdd:COG2895    93 ----PKRKFIIADTPGHEQYT-------RNMvtgastaDLAILLIDARKGVLEQTR---RHS--YiasllGIRHVVVaVN 156
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1718559237 143 KMDRAG---ANFLRVVEQIK---KRLG---HTPVPV 169
Cdd:COG2895   157 KMDLVDyseEVFEEIVADYRafaAKLGledITFIPI 192
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
67-143 1.33e-03

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


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 39.14  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  67 ATTAFWSGSTK-------QYDKYRVNIIDTPGHVDFTIE---VERSLRVL---DGAVVVFCGTSGVEPQSETVWRQANKY 133
Cdd:pfam01926  24 AIVSDYPGTTRdpnegrlELKGKQIILVDTPGLIEGASEgegLGRAFLAIieaDLILFVVDSEEGITPLDEELLELLREN 103
                          90
                  ....*....|
gi 1718559237 134 GVPRIVYVNK 143
Cdd:pfam01926 104 KKPIILVLNK 113
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
13-166 2.40e-03

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: 41.05  E-value: 2.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  13 IGICAHVDAGKTTTTeRILfyTGVNhkmgevhdgaaTmDWMVQEQERGITITSaattafwsG--STKQYDKYRVNIIDTP 90
Cdd:COG3276     3 IGTAGHIDHGKTTLV-KAL--TGID-----------T-DRLKEEKKRGITIDL--------GfaYLPLPDGRRLGFVDVP 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  91 GHvdftievERSLR-VLDGA----VVVFC--GTSGVEPQSE---TVWRQAnkyGVPR-IVYVNKMDRAGANFL-RVVEQI 158
Cdd:COG3276    60 GH-------EKFIKnMLAGAggidLVLLVvaADEGVMPQTRehlAILDLL---GIKRgIVVLTKADLVDEEWLeLVEEEI 129

                  ....*...
gi 1718559237 159 KKRLGHTP 166
Cdd:COG3276   130 RELLAGTF 137
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
13-164 2.80e-03

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 40.80  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718559237  13 IGICAHVDAGKTTTTERIlfyTGVNhkmgevhdgaatMDWMVQEQERGITITSAatTAFWSgstkQYDKYRVNIIDTPGH 92
Cdd:PRK10512    3 IATAGHVDHGKTTLLQAI---TGVN------------ADRLPEEKKRGMTIDLG--YAYWP----QPDGRVLGFIDVPGH 61
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1718559237  93 VDFTIEVERSLRVLDGAVVVFCGTSGVEPQSE---TVWRQAnkyGVPRI-VYVNKMDR-AGANFLRVVEQIKKRLGH 164
Cdd:PRK10512   62 EKFLSNMLAGVGGIDHALLVVACDDGVMAQTRehlAILQLT---GNPMLtVALTKADRvDEARIAEVRRQVKAVLRE 135
EF2_snRNP_like_II cd03700
Domain II of elongation factor 2 and C-terminal domain of the spliceosomal human 116kD U5 ...
335-388 2.98e-03

Domain II of elongation factor 2 and C-terminal domain of the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein; This subfamily represents domain II of elongation factor (EF) EF-2 found in eukaryotes and archaea, and the C-terminal portion of 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 is important for the function of U5-116 kD/Snu114p.


Pssm-ID: 293901 [Multi-domain]  Cd Length: 95  Bit Score: 37.59  E-value: 2.98e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1718559237 335 FARVYSGVLSSGDSV----INSVKGKKE-----RVGRMVQMHANTREEIKEVRAGDIAALIGM 388
Cdd:cd03700    20 FGRVFAGTVHAGQKVrilgPNYTPGKKEdlrikAIQRLWLMMGRYVEEINDVPAGNIVGLVGI 82
 
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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