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Conserved domains on  [gi|41386743|ref|NP_956752|]
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elongation factor 2b [Danio rerio]

Protein Classification

elongation factor 2( domain architecture ID 11488498)

elongation factor 2 catalyzes the GTP-dependent ribosomal translocation step during translation elongation, and is a component of the mRNA surveillance SURF complex

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTZ00416 PTZ00416
elongation factor 2; Provisional
1-858 0e+00

elongation factor 2; Provisional


:

Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 1601.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743    1 MVNFTVDQIRAIMDKKSNIRNMSVIAHVDHGKSTLTDSLVSKAGIIASARAGETRFTDTRKDEQERCITIKSTAISMYYE 80
Cdd:PTZ00416   1 MVNFTVDQIREIMDNPDQIRNMSVIAHVDHGKSTLTDSLVCKAGIISSKNAGDARFTDTRADEQERGITIKSTGISLYYE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   81 LTENDlafikqCKDGSGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKM 160
Cdd:PTZ00416  81 HDLED------GDDKQPFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  161 DRALLELQLEPEELYQTFQRIVENVNVIISTYGEDeggPMGNIMIDPVIGTVGFGSGLHGWAFTLKQFAEMYVAKFASKg 240
Cdd:PTZ00416 155 DRAILELQLDPEEIYQNFVKTIENVNVIIATYNDE---LMGDVQVYPEKGTVAFGSGLQGWAFTLTTFARIYAKKFGVE- 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  241 eaqlspadrckkVEDMMKKLWGDRYFDPAGGKFTKTANGPDGKKYPRTFAQLILDPIFKVFDAIMNFKKEETAKLIEKLD 320
Cdd:PTZ00416 231 ------------ESKMMERLWGDNFFDAKTKKWIKDETNAQGKKLKRAFCQFILDPICQLFDAVMNEDKEKYDKMLKSLN 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  321 IKLDTEDKDKEGKPLLKAVMRRWLPAGEALLQMITIHLPSPVTAQKYRCELLYEGPGDDEAAMGIKNCDPKGPLMMYISK 400
Cdd:PTZ00416 299 ISLTGEDKELTGKPLLKAVMQKWLPAADTLLEMIVDHLPSPKEAQKYRVENLYEGPMDDEAANAIRNCDPNGPLMMYISK 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  401 MVPTTDKGRFYAFGRVFSGVVSTGLKVRIMGPNYTPGKKEDLYLKPIQRTILMMGRYVEPIEDVPCGNIVGLVGVDQFLV 480
Cdd:PTZ00416 379 MVPTSDKGRFYAFGRVFSGTVATGQKVRIQGPNYVPGKKEDLFEKNIQRTVLMMGRYVEQIEDVPCGNTVGLVGVDQYLV 458
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  481 KTGTITTFDQAHNMRVMKFSVSPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCIIEESGEHIIAGAGELHLEICLKD 560
Cdd:PTZ00416 459 KSGTITTSETAHNIRDMKYSVSPVVRVAVEPKNPKDLPKLVEGLKRLAKSDPLVVCTTEESGEHIVAGCGELHVEICLKD 538
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  561 LEEDHACIPLKKSDPVVSYRETVSAESDQMCLSKSPNKHNRLYMKARPFPDGLAEDIDKGDVSSRQELKTRARYLADKYE 640
Cdd:PTZ00416 539 LEDDYANIDIIVSDPVVSYRETVTEESSQTCLSKSPNKHNRLYMKAEPLTEELAEAIEEGKVGPEDDPKERANFLADKYE 618
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  641 WEVTEARKIWCFGPDGTGPNMLVDVTKGVQYLNEIKDSVVAGFQWATKEGALCEENMRAVRFDIHDVTLHTDAIHRGGGQ 720
Cdd:PTZ00416 619 WDKNDARKIWCFGPENKGPNVLVDVTKGVQYMNEIKDSCVSAFQWATKEGVLCDENMRGIRFNILDVTLHADAIHRGAGQ 698
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  721 IIPTARRVLYACQLTAEPRLMEPIYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQVMGTPMFVVKAYLPVNESFGFTADL 800
Cdd:PTZ00416 699 IIPTARRVFYACELTASPRLLEPMFLVDITAPEDAMGGIYSVLNRRRGVVIGEEQRPGTPLSNIKAYLPVAESFGFTAAL 778
                        810       820       830       840       850
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 41386743  801 RSNTGGQAFPQCVFDHWQILPGDPKDAASKPCQIVADTRKRKGLKEGIPALDNFLDKL 858
Cdd:PTZ00416 779 RAATSGQAFPQCVFDHWQVVPGDPLEPGSKANEIVLSIRKRKGLKPEIPDLDNYLDKL 836
 
Name Accession Description Interval E-value
PTZ00416 PTZ00416
elongation factor 2; Provisional
1-858 0e+00

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 1601.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743    1 MVNFTVDQIRAIMDKKSNIRNMSVIAHVDHGKSTLTDSLVSKAGIIASARAGETRFTDTRKDEQERCITIKSTAISMYYE 80
Cdd:PTZ00416   1 MVNFTVDQIREIMDNPDQIRNMSVIAHVDHGKSTLTDSLVCKAGIISSKNAGDARFTDTRADEQERGITIKSTGISLYYE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   81 LTENDlafikqCKDGSGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKM 160
Cdd:PTZ00416  81 HDLED------GDDKQPFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  161 DRALLELQLEPEELYQTFQRIVENVNVIISTYGEDeggPMGNIMIDPVIGTVGFGSGLHGWAFTLKQFAEMYVAKFASKg 240
Cdd:PTZ00416 155 DRAILELQLDPEEIYQNFVKTIENVNVIIATYNDE---LMGDVQVYPEKGTVAFGSGLQGWAFTLTTFARIYAKKFGVE- 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  241 eaqlspadrckkVEDMMKKLWGDRYFDPAGGKFTKTANGPDGKKYPRTFAQLILDPIFKVFDAIMNFKKEETAKLIEKLD 320
Cdd:PTZ00416 231 ------------ESKMMERLWGDNFFDAKTKKWIKDETNAQGKKLKRAFCQFILDPICQLFDAVMNEDKEKYDKMLKSLN 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  321 IKLDTEDKDKEGKPLLKAVMRRWLPAGEALLQMITIHLPSPVTAQKYRCELLYEGPGDDEAAMGIKNCDPKGPLMMYISK 400
Cdd:PTZ00416 299 ISLTGEDKELTGKPLLKAVMQKWLPAADTLLEMIVDHLPSPKEAQKYRVENLYEGPMDDEAANAIRNCDPNGPLMMYISK 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  401 MVPTTDKGRFYAFGRVFSGVVSTGLKVRIMGPNYTPGKKEDLYLKPIQRTILMMGRYVEPIEDVPCGNIVGLVGVDQFLV 480
Cdd:PTZ00416 379 MVPTSDKGRFYAFGRVFSGTVATGQKVRIQGPNYVPGKKEDLFEKNIQRTVLMMGRYVEQIEDVPCGNTVGLVGVDQYLV 458
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  481 KTGTITTFDQAHNMRVMKFSVSPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCIIEESGEHIIAGAGELHLEICLKD 560
Cdd:PTZ00416 459 KSGTITTSETAHNIRDMKYSVSPVVRVAVEPKNPKDLPKLVEGLKRLAKSDPLVVCTTEESGEHIVAGCGELHVEICLKD 538
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  561 LEEDHACIPLKKSDPVVSYRETVSAESDQMCLSKSPNKHNRLYMKARPFPDGLAEDIDKGDVSSRQELKTRARYLADKYE 640
Cdd:PTZ00416 539 LEDDYANIDIIVSDPVVSYRETVTEESSQTCLSKSPNKHNRLYMKAEPLTEELAEAIEEGKVGPEDDPKERANFLADKYE 618
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  641 WEVTEARKIWCFGPDGTGPNMLVDVTKGVQYLNEIKDSVVAGFQWATKEGALCEENMRAVRFDIHDVTLHTDAIHRGGGQ 720
Cdd:PTZ00416 619 WDKNDARKIWCFGPENKGPNVLVDVTKGVQYMNEIKDSCVSAFQWATKEGVLCDENMRGIRFNILDVTLHADAIHRGAGQ 698
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  721 IIPTARRVLYACQLTAEPRLMEPIYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQVMGTPMFVVKAYLPVNESFGFTADL 800
Cdd:PTZ00416 699 IIPTARRVFYACELTASPRLLEPMFLVDITAPEDAMGGIYSVLNRRRGVVIGEEQRPGTPLSNIKAYLPVAESFGFTAAL 778
                        810       820       830       840       850
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 41386743  801 RSNTGGQAFPQCVFDHWQILPGDPKDAASKPCQIVADTRKRKGLKEGIPALDNFLDKL 858
Cdd:PTZ00416 779 RAATSGQAFPQCVFDHWQVVPGDPLEPGSKANEIVLSIRKRKGLKPEIPDLDNYLDKL 836
aEF-2 TIGR00490
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ...
6-845 2.23e-160

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: 485.17  E-value: 2.23e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743     6 VDQIRAIMDKKSNIRNMSVIAHVDHGKSTLTDSLVSKAGIIASARAGETRFTDTRKDEQERCITIKSTAISMYYELTEND 85
Cdd:TIGR00490   6 IDKIKELMWKPKFIRNIGIVAHIDHGKTTLSDNLLAGAGMISEELAGQQLYLDFDEQEQERGITINAANVSMVHEYEGNE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743    86 lafikqckdgsgFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALL 165
Cdd:TIGR00490  86 ------------YLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKPVLFINKVDRLIN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   166 ELQLEPEELYQTFQRIVENVNVIISTYGEDEGgpMGNIMIDPVIGTVGFGSGLHGWAFTLkqfaemyvakfaskgeaqls 245
Cdd:TIGR00490 154 ELKLTPQELQERFIKIITEVNKLIKAMAPEEF--RDKWKVRVEDGSVAFGSAYYNWAISV-------------------- 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   246 padrckkvedmmkklwgdryfdpaggkftktangPDGKKYPRTFAQLIldpifkvfdaimnfkkeetakliekldiKLDT 325
Cdd:TIGR00490 212 ----------------------------------PSMKKTGIGFKDIY----------------------------KYCK 229
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   326 EDKDKEgkpLLKAVmrrwlPAGEALLQMITIHLPSPVTAQKYRCELLYEGPGDDEAAMGIKNCDPKGPLMMYISKMVPTT 405
Cdd:TIGR00490 230 EDKQKE---LAKKS-----PLHQVVLDMVIRHLPSPIEAQKYRIPVIWKGDLNSEVGKAMLNCDPKGPLALMITKIVVDK 301
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   406 DKGRFyAFGRVFSGVVSTGLKVRIMGpNYTPGKkedlylkpIQRTILMMGRYVEPIEDVPCGNIVGLVGVDQFLVKTGTI 485
Cdd:TIGR00490 302 HAGEV-AVGRLYSGTIRPGMEVYIVD-RKAKAR--------IQQVGVYMGPERVEVDEIPAGNIVAVIGLKDAVAGETIC 371
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   486 TTFDQAHNMRVMKFSVSPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCII-EESGEHIIAGAGELHLEICLKDLEED 564
Cdd:TIGR00490 372 TTVENITPFESIKHISEPVVTVAIEAKNTKDLPKLIEVLRQVAKEDPTVHVEInEETGEHLISGMGELHLEIIVEKIRED 451
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   565 HAcIPLKKSDPVVSYRETVSAESdQMCLSKSPNKHNRLYMKARPFPDGLAEDIDKGDVSSRQELKTRARYLADKYEWEVT 644
Cdd:TIGR00490 452 YG-LDVETSPPIVVYRETVTGTS-PVVEGKSPNKHNRFYIVVEPLEESVIQAFKEGKIVDMKMKKKERRRLLIEAGMDSE 529
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   645 EARKIWCFGPDgtgpNMLVDVTKGVQYLNEIKDSVVAGFQWATKEGALCEENMRAVRFDIHDVTLHTDAIHRGGGQIIPT 724
Cdd:TIGR00490 530 EAARVEEYYEG----NLFINMTRGIQYLDETKELILEGFREAMRNGPIAREKCMGVKVKLMDAKLHEDAVHRGPAQVIPA 605
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   725 ARRVLYACQLTAEPRLMEPIYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQvmGTPMFVVKAYLPVNESFGFTADLRSNT 804
Cdd:TIGR00490 606 VRSGIFAAMMQAKPVLLEPYQKVFINVPQDMMGAATREIQNRRGQILEMKQ--EGDMVTIIAKAPVAEMFGFAGAIRGAT 683
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|.
gi 41386743   805 GGQAFPQCVFDHWQILPGDPKDaaskpcQIVADTRKRKGLK 845
Cdd:TIGR00490 684 SGRCLWSTEHAGFELVPQNLQQ------EFVMEVRKRKGLK 718
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
20-233 1.06e-109

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: 335.36  E-value: 1.06e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  20 RNMSVIAHVDHGKSTLTDSLVSKAGIIASARAGETRFTDTRKDEQERCITIKSTAISMYYELTENDLafikqckDGSGFL 99
Cdd:cd01885   1 RNICIIAHVDHGKTTLSDSLLASAGIISEKLAGKARYLDTREDEQERGITIKSSAISLYFEYEEEKM-------DGNDYL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 100 INLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALLELQLEPEELYQTFQ 179
Cdd:cd01885  74 INLIDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDRLILELKLSPEEAYQRLL 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 41386743 180 RIVENVNVIISTYGEDEGGPmGNIMIDPVIGTVGFGSGLHGWAFTLKQFAEMYV 233
Cdd:cd01885 154 RIVEDVNAIIETYAPEEFKQ-EKWKFSPQKGNVAFGSALDGWGFTIIKFADIYA 206
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
17-823 8.89e-64

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: 227.62  E-value: 8.89e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  17 SNIRNMSVIAHVDHGKSTLTDSLVSKAGIIAsaRAGE----TRFTDTRKDEQERCITIKSTAISMYYeltendlafiKQC 92
Cdd:COG0480   7 EKIRNIGIVAHIDAGKTTLTERILFYTGAIH--RIGEvhdgNTVMDWMPEEQERGITITSAATTCEW----------KGH 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  93 KdgsgflINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALLElqlepe 172
Cdd:COG0480  75 K------INIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGAD------ 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 173 elyqtFQRIVE------NVNVIISTYgedeggPMGNimidpvigtvgfGSGLHGwaftlkqfaemyvakfaskgeaqlsp 246
Cdd:COG0480 143 -----FDRVLEqlkerlGANPVPLQL------PIGA------------EDDFKG-------------------------- 173
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 247 adrckkVEDM--MKKLwgdrYFDPAGGKFTKTANGPDG-----KKYpRtfAQLIldpifkvfDAIMNFKKEetakLIEKL 319
Cdd:COG0480 174 ------VIDLvtMKAY----VYDDELGAKYEEEEIPAElkeeaEEA-R--EELI--------EAVAETDDE----LMEKY 228
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 320 --DIKLDTEDkdkegkplLKAVMRRWLPAGE----------------ALLQMITIHLPSPVTAQKYRCELLyegpgDDEA 381
Cdd:COG0480 229 leGEELTEEE--------IKAGLRKATLAGKivpvlcgsafknkgvqPLLDAVVDYLPSPLDVPAIKGVDP-----DTGE 295
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 382 AMGIKnCDPKGPLMMYISKMVptTDK--GRfYAFGRVFSGVVSTGLKVRimgpNYTPGKKEDlylkpIQRTILMMGRYVE 459
Cdd:COG0480 296 EVERK-PDDDEPFSALVFKTM--TDPfvGK-LSFFRVYSGTLKSGSTVY----NSTKGKKER-----IGRLLRMHGNKRE 362
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 460 PIEDVPCGNIVGLVGVDQflVKTG-TITtfDQAHNMRV--MKFSVsPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQC 536
Cdd:COG0480 363 EVDEAGAGDIVAVVKLKD--TTTGdTLC--DEDHPIVLepIEFPE-PVISVAIEPKTKADEDKLSTALAKLAEEDPTFRV 437
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 537 II-EESGEHIIAGAGELHLEICLKDLEEDHAcIPLKKSDPVVSYRETVSAESDQMclskspNKHNR----------LYMK 605
Cdd:COG0480 438 ETdEETGQTIISGMGELHLEIIVDRLKREFG-VEVNVGKPQVAYRETIRKKAEAE------GKHKKqsgghgqygdVWIE 510
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 606 ARPFPDGlaedidkgdvssrqelktrarylaDKYEWEvtearkiwcfgpDgtgpnmlvDVTKGV---QYLNeikdSVVAG 682
Cdd:COG0480 511 IEPLPRG------------------------EGFEFV------------D--------KIVGGVipkEYIP----AVEKG 542
                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 683 FQWATKEGALCE---ENMRAVRFD--IHDVtlhtD--------AihrgggqiiptARRVLYACQLTAEPRLMEPIYLVEI 749
Cdd:COG0480 543 IREAMEKGVLAGypvVDVKVTLYDgsYHPV----DssemafkiA-----------ASMAFKEAAKKAKPVLLEPIMKVEV 607
                       810       820       830       840       850       860       870
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41386743 750 QCPEQVVGGIYGVLNRKRGhvfeesQVMGT----PMFVVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQILPGD 823
Cdd:COG0480 608 TVPEEYMGDVMGDLNSRRG------RILGMesrgGAQVIKAEVPLAEMFGYATDLRSLTQGRGSFTMEFSHYEEVPAN 679
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
18-224 7.93e-60

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: 201.60  E-value: 7.93e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743    18 NIRNMSVIAHVDHGKSTLTDSLVSKAGIIASA---RAGETRFTDTRKDEQERCITIKSTAISMYYEltendlafikqckd 94
Cdd:pfam00009   2 RHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRgevKGEGEAGLDNLPEERERGITIKSAAVSFETK-------------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743    95 gsGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRAllelqlepeeL 174
Cdd:pfam00009  68 --DYLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRV----------D 135
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 41386743   175 YQTFQRIVENVNviiSTYGEDEGGPMGNImidPVIgtvgFGSGLHGWAFT 224
Cdd:pfam00009 136 GAELEEVVEEVS---RELLEKYGEDGEFV---PVV----PGSALKGEGVQ 175
EFG_IV smart00889
Elongation factor G, domain IV; Translation elongation factors are responsible for two main ...
625-737 3.73e-29

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: 112.25  E-value: 3.73e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743    625 RQELKTRARYLADKYEWEVTEARKIWCFGPDGTGPNMLVDVTK--GVQYLnEIKDSVVAGFQWATKEGALCEENMRAVRF 702
Cdd:smart00889   9 TKPVKEAEGKHKKQSGGDGQYARVILEVEPLERGSGFEFDDTIvgGVIPK-EYIPAVEKGFREALEEGPLAGYPVVDVKV 87
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 41386743    703 DIHDVTLHTDaIHRGGGqIIPTARRVLYACQLTAE 737
Cdd:smart00889  88 TLLDGSYHEV-DSSEMA-FKPAARRAFKEALLKAG 120
 
Name Accession Description Interval E-value
PTZ00416 PTZ00416
elongation factor 2; Provisional
1-858 0e+00

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 1601.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743    1 MVNFTVDQIRAIMDKKSNIRNMSVIAHVDHGKSTLTDSLVSKAGIIASARAGETRFTDTRKDEQERCITIKSTAISMYYE 80
Cdd:PTZ00416   1 MVNFTVDQIREIMDNPDQIRNMSVIAHVDHGKSTLTDSLVCKAGIISSKNAGDARFTDTRADEQERGITIKSTGISLYYE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   81 LTENDlafikqCKDGSGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKM 160
Cdd:PTZ00416  81 HDLED------GDDKQPFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  161 DRALLELQLEPEELYQTFQRIVENVNVIISTYGEDeggPMGNIMIDPVIGTVGFGSGLHGWAFTLKQFAEMYVAKFASKg 240
Cdd:PTZ00416 155 DRAILELQLDPEEIYQNFVKTIENVNVIIATYNDE---LMGDVQVYPEKGTVAFGSGLQGWAFTLTTFARIYAKKFGVE- 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  241 eaqlspadrckkVEDMMKKLWGDRYFDPAGGKFTKTANGPDGKKYPRTFAQLILDPIFKVFDAIMNFKKEETAKLIEKLD 320
Cdd:PTZ00416 231 ------------ESKMMERLWGDNFFDAKTKKWIKDETNAQGKKLKRAFCQFILDPICQLFDAVMNEDKEKYDKMLKSLN 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  321 IKLDTEDKDKEGKPLLKAVMRRWLPAGEALLQMITIHLPSPVTAQKYRCELLYEGPGDDEAAMGIKNCDPKGPLMMYISK 400
Cdd:PTZ00416 299 ISLTGEDKELTGKPLLKAVMQKWLPAADTLLEMIVDHLPSPKEAQKYRVENLYEGPMDDEAANAIRNCDPNGPLMMYISK 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  401 MVPTTDKGRFYAFGRVFSGVVSTGLKVRIMGPNYTPGKKEDLYLKPIQRTILMMGRYVEPIEDVPCGNIVGLVGVDQFLV 480
Cdd:PTZ00416 379 MVPTSDKGRFYAFGRVFSGTVATGQKVRIQGPNYVPGKKEDLFEKNIQRTVLMMGRYVEQIEDVPCGNTVGLVGVDQYLV 458
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  481 KTGTITTFDQAHNMRVMKFSVSPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCIIEESGEHIIAGAGELHLEICLKD 560
Cdd:PTZ00416 459 KSGTITTSETAHNIRDMKYSVSPVVRVAVEPKNPKDLPKLVEGLKRLAKSDPLVVCTTEESGEHIVAGCGELHVEICLKD 538
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  561 LEEDHACIPLKKSDPVVSYRETVSAESDQMCLSKSPNKHNRLYMKARPFPDGLAEDIDKGDVSSRQELKTRARYLADKYE 640
Cdd:PTZ00416 539 LEDDYANIDIIVSDPVVSYRETVTEESSQTCLSKSPNKHNRLYMKAEPLTEELAEAIEEGKVGPEDDPKERANFLADKYE 618
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  641 WEVTEARKIWCFGPDGTGPNMLVDVTKGVQYLNEIKDSVVAGFQWATKEGALCEENMRAVRFDIHDVTLHTDAIHRGGGQ 720
Cdd:PTZ00416 619 WDKNDARKIWCFGPENKGPNVLVDVTKGVQYMNEIKDSCVSAFQWATKEGVLCDENMRGIRFNILDVTLHADAIHRGAGQ 698
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  721 IIPTARRVLYACQLTAEPRLMEPIYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQVMGTPMFVVKAYLPVNESFGFTADL 800
Cdd:PTZ00416 699 IIPTARRVFYACELTASPRLLEPMFLVDITAPEDAMGGIYSVLNRRRGVVIGEEQRPGTPLSNIKAYLPVAESFGFTAAL 778
                        810       820       830       840       850
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 41386743  801 RSNTGGQAFPQCVFDHWQILPGDPKDAASKPCQIVADTRKRKGLKEGIPALDNFLDKL 858
Cdd:PTZ00416 779 RAATSGQAFPQCVFDHWQVVPGDPLEPGSKANEIVLSIRKRKGLKPEIPDLDNYLDKL 836
PLN00116 PLN00116
translation elongation factor EF-2 subunit; Provisional
1-858 0e+00

translation elongation factor EF-2 subunit; Provisional


Pssm-ID: 177730 [Multi-domain]  Cd Length: 843  Bit Score: 1498.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743    1 MVNFTVDQIRAIMDKKSNIRNMSVIAHVDHGKSTLTDSLVSKAGIIASARAGETRFTDTRKDEQERCITIKSTAISMYYE 80
Cdd:PLN00116   1 MVKFTAEELRRIMDKKHNIRNMSVIAHVDHGKSTLTDSLVAAAGIIAQEVAGDVRMTDTRADEAERGITIKSTGISLYYE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   81 LTENDLAFIKQCKDGSGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKM 160
Cdd:PLN00116  81 MTDESLKDFKGERDGNEYLINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTETVLRQALGERIRPVLTVNKM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  161 DRALLELQLEPEELYQTFQRIVENVNVIISTYgEDEGgpMGNIMIDPVIGTVGFGSGLHGWAFTLKQFAEMYVAKFASKG 240
Cdd:PLN00116 161 DRCFLELQVDGEEAYQTFSRVIENANVIMATY-EDPL--LGDVQVYPEKGTVAFSAGLHGWAFTLTNFAKMYASKFGVDE 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  241 EAqlspadrckkvedMMKKLWGDRYFDPAGGKFTKTANGpdGKKYPRTFAQLILDPIFKVFDAIMNFKKEETAKLIEKLD 320
Cdd:PLN00116 238 SK-------------MMERLWGENFFDPATKKWTTKNTG--SPTCKRGFVQFCYEPIKQIINTCMNDQKDKLWPMLEKLG 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  321 IKLDTEDKDKEGKPLLKAVMRRWLPAGEALLQMITIHLPSPVTAQKYRCELLYEGPGDDEAAMGIKNCDPKGPLMMYISK 400
Cdd:PLN00116 303 VTLKSDEKELMGKALMKRVMQTWLPASDALLEMIIFHLPSPAKAQRYRVENLYEGPLDDKYATAIRNCDPNGPLMLYVSK 382
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  401 MVPTTDKGRFYAFGRVFSGVVSTGLKVRIMGPNYTPGKKEDLYLKPIQRTILMMGRYVEPIEDVPCGNIVGLVGVDQFLV 480
Cdd:PLN00116 383 MIPASDKGRFFAFGRVFSGTVATGMKVRIMGPNYVPGEKKDLYVKSVQRTVIWMGKKQESVEDVPCGNTVAMVGLDQFIT 462
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  481 KTGTITT--FDQAHNMRVMKFSVSPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCIIEESGEHIIAGAGELHLEICL 558
Cdd:PLN00116 463 KNATLTNekEVDAHPIKAMKFSVSPVVRVAVQCKNASDLPKLVEGLKRLAKSDPMVQCTIEESGEHIIAGAGELHLEICL 542
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  559 KDLEEDH-ACIPLKKSDPVVSYRETVSAESDQMCLSKSPNKHNRLYMKARPFPDGLAEDIDKGDVSSRQELKTRARYLAD 637
Cdd:PLN00116 543 KDLQDDFmGGAEIKVSDPVVSFRETVLEKSCRTVMSKSPNKHNRLYMEARPLEEGLAEAIDDGRIGPRDDPKIRSKILAE 622
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  638 KYEWEVTEARKIWCFGPDGTGPNMLVDVTKGVQYLNEIKDSVVAGFQWATKEGALCEENMRAVRFDIHDVTLHTDAIHRG 717
Cdd:PLN00116 623 EFGWDKDLAKKIWCFGPETTGPNMVVDMCKGVQYLNEIKDSVVAGFQWATKEGALAEENMRGICFEVCDVVLHADAIHRG 702
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  718 GGQIIPTARRVLYACQLTAEPRLMEPIYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQVMGTPMFVVKAYLPVNESFGFT 797
Cdd:PLN00116 703 GGQIIPTARRVIYASQLTAKPRLLEPVYLVEIQAPEQALGGIYSVLNQKRGHVFEEMQRPGTPLYNIKAYLPVIESFGFS 782
                        810       820       830       840       850       860
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41386743  798 ADLRSNTGGQAFPQCVFDHWQILPGDPKDAASKPCQIVADTRKRKGLKEGIPALDNFLDKL 858
Cdd:PLN00116 783 GTLRAATSGQAFPQCVFDHWDMMSSDPLEAGSQAAQLVADIRKRKGLKEQMPPLSEYEDKL 843
PRK07560 PRK07560
elongation factor EF-2; Reviewed
5-856 0e+00

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 648.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743    5 TVDQIRAIMDKKSNIRNMSVIAHVDHGKSTLTDSLVSKAGIIASARAGETRFTDTRKDEQERCITIKSTAISMYYELten 84
Cdd:PRK07560   6 MVEKILELMKNPEQIRNIGIIAHIDHGKTTLSDNLLAGAGMISEELAGEQLALDFDEEEQARGITIKAANVSMVHEY--- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   85 dlafikqckDGSGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRAL 164
Cdd:PRK07560  83 ---------EGKEYLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKPVLFINKVDRLI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  165 LELQLEPEELYQTFQRIVENVNVIISTYGEDEGgpMGNIMIDPVIGTVGFGSGLHGWAFTLkqfaemyvakfaskgeaql 244
Cdd:PRK07560 154 KELKLTPQEMQQRLLKIIKDVNKLIKGMAPEEF--KEKWKVDVEDGTVAFGSALYNWAISV------------------- 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  245 spadrckkveDMMKKlwgdryfdpAGGKFTKtangpdgkkyprtfaqlildpifkVFDAIMNFKKEETAKLIekldikld 324
Cdd:PRK07560 213 ----------PMMQK---------TGIKFKD------------------------IIDYYEKGKQKELAEKA-------- 241
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  325 tedkdkegkpllkavmrrwlPAGEALLQMITIHLPSPVTAQKYRCELLYEGPGDDEAAMGIKNCDPKGPLMMYISKMVpt 404
Cdd:PRK07560 242 --------------------PLHEVVLDMVVKHLPNPIEAQKYRIPKIWKGDLNSEVGKAMLNCDPNGPLVMMVTDII-- 299
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  405 TDK-GRFYAFGRVFSGVVSTGLKVRIMGpnyTPGKKEdlylkpIQRTILMMGRYVEPIEDVPCGNIVGLVGVDQF----- 478
Cdd:PRK07560 300 VDPhAGEVATGRVFSGTLRKGQEVYLVG---AKKKNR------VQQVGIYMGPEREEVEEIPAGNIAAVTGLKDAraget 370
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  479 LVKTGTITTFDQahnmrvMKFSVSPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCII-EESGEHIIAGAGELHLEIC 557
Cdd:PRK07560 371 VVSVEDMTPFES------LKHISEPVVTVAIEAKNPKDLPKLIEVLRQLAKEDPTLVVKInEETGEHLLSGMGELHLEVI 444
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  558 LKDLEEDHAcIPLKKSDPVVSYRETVSAESdQMCLSKSPNKHNRLYMKARPFPDGLAEDIDKGDVSSRQ---ELKTRARY 634
Cdd:PRK07560 445 TYRIKRDYG-IEVVTSEPIVVYRETVRGKS-QVVEGKSPNKHNRFYISVEPLEEEVIEAIKEGEISEDMdkkEAKILREK 522
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  635 LAdKYEWEVTEARKIWCFgpdgTGPNMLVDVTKGVQYLNEIKDSVVAGFQWATKEGALCEENMRAVRFDIHDVTLHTDAI 714
Cdd:PRK07560 523 LI-EAGMDKDEAKRVWAI----YNGNVFIDMTKGIQYLNEVMELIIEGFREAMKEGPLAAEPVRGVKVRLHDAKLHEDAI 597
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  715 HRGGGQIIPTARRVLYACQLTAEPRLMEPIYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQvMGTpMFVVKAYLPVNESF 794
Cdd:PRK07560 598 HRGPAQVIPAVRNAIFAAMLTAKPTLLEPIQKVDINVPQDYMGAVTREIQGRRGKILDMEQ-EGD-MAIIEAEAPVAEMF 675
                        810       820       830       840       850       860
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41386743  795 GFTADLRSNTGGQAFPQCVFDHWQILPGDPKDaaskpcQIVADTRKRKGLKEGIPALDNFLD 856
Cdd:PRK07560 676 GFAGEIRSATEGRALWSTEFAGFEPVPDSLQL------DIVRQIRERKGLKPELPKPEDFLS 731
aEF-2 TIGR00490
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ...
6-845 2.23e-160

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: 485.17  E-value: 2.23e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743     6 VDQIRAIMDKKSNIRNMSVIAHVDHGKSTLTDSLVSKAGIIASARAGETRFTDTRKDEQERCITIKSTAISMYYELTEND 85
Cdd:TIGR00490   6 IDKIKELMWKPKFIRNIGIVAHIDHGKTTLSDNLLAGAGMISEELAGQQLYLDFDEQEQERGITINAANVSMVHEYEGNE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743    86 lafikqckdgsgFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALL 165
Cdd:TIGR00490  86 ------------YLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKPVLFINKVDRLIN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   166 ELQLEPEELYQTFQRIVENVNVIISTYGEDEGgpMGNIMIDPVIGTVGFGSGLHGWAFTLkqfaemyvakfaskgeaqls 245
Cdd:TIGR00490 154 ELKLTPQELQERFIKIITEVNKLIKAMAPEEF--RDKWKVRVEDGSVAFGSAYYNWAISV-------------------- 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   246 padrckkvedmmkklwgdryfdpaggkftktangPDGKKYPRTFAQLIldpifkvfdaimnfkkeetakliekldiKLDT 325
Cdd:TIGR00490 212 ----------------------------------PSMKKTGIGFKDIY----------------------------KYCK 229
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   326 EDKDKEgkpLLKAVmrrwlPAGEALLQMITIHLPSPVTAQKYRCELLYEGPGDDEAAMGIKNCDPKGPLMMYISKMVPTT 405
Cdd:TIGR00490 230 EDKQKE---LAKKS-----PLHQVVLDMVIRHLPSPIEAQKYRIPVIWKGDLNSEVGKAMLNCDPKGPLALMITKIVVDK 301
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   406 DKGRFyAFGRVFSGVVSTGLKVRIMGpNYTPGKkedlylkpIQRTILMMGRYVEPIEDVPCGNIVGLVGVDQFLVKTGTI 485
Cdd:TIGR00490 302 HAGEV-AVGRLYSGTIRPGMEVYIVD-RKAKAR--------IQQVGVYMGPERVEVDEIPAGNIVAVIGLKDAVAGETIC 371
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   486 TTFDQAHNMRVMKFSVSPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCII-EESGEHIIAGAGELHLEICLKDLEED 564
Cdd:TIGR00490 372 TTVENITPFESIKHISEPVVTVAIEAKNTKDLPKLIEVLRQVAKEDPTVHVEInEETGEHLISGMGELHLEIIVEKIRED 451
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   565 HAcIPLKKSDPVVSYRETVSAESdQMCLSKSPNKHNRLYMKARPFPDGLAEDIDKGDVSSRQELKTRARYLADKYEWEVT 644
Cdd:TIGR00490 452 YG-LDVETSPPIVVYRETVTGTS-PVVEGKSPNKHNRFYIVVEPLEESVIQAFKEGKIVDMKMKKKERRRLLIEAGMDSE 529
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   645 EARKIWCFGPDgtgpNMLVDVTKGVQYLNEIKDSVVAGFQWATKEGALCEENMRAVRFDIHDVTLHTDAIHRGGGQIIPT 724
Cdd:TIGR00490 530 EAARVEEYYEG----NLFINMTRGIQYLDETKELILEGFREAMRNGPIAREKCMGVKVKLMDAKLHEDAVHRGPAQVIPA 605
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   725 ARRVLYACQLTAEPRLMEPIYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQvmGTPMFVVKAYLPVNESFGFTADLRSNT 804
Cdd:TIGR00490 606 VRSGIFAAMMQAKPVLLEPYQKVFINVPQDMMGAATREIQNRRGQILEMKQ--EGDMVTIIAKAPVAEMFGFAGAIRGAT 683
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|.
gi 41386743   805 GGQAFPQCVFDHWQILPGDPKDaaskpcQIVADTRKRKGLK 845
Cdd:TIGR00490 684 SGRCLWSTEHAGFELVPQNLQQ------EFVMEVRKRKGLK 718
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
20-233 1.06e-109

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: 335.36  E-value: 1.06e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  20 RNMSVIAHVDHGKSTLTDSLVSKAGIIASARAGETRFTDTRKDEQERCITIKSTAISMYYELTENDLafikqckDGSGFL 99
Cdd:cd01885   1 RNICIIAHVDHGKTTLSDSLLASAGIISEKLAGKARYLDTREDEQERGITIKSSAISLYFEYEEEKM-------DGNDYL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 100 INLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALLELQLEPEELYQTFQ 179
Cdd:cd01885  74 INLIDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDRLILELKLSPEEAYQRLL 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 41386743 180 RIVENVNVIISTYGEDEGGPmGNIMIDPVIGTVGFGSGLHGWAFTLKQFAEMYV 233
Cdd:cd01885 154 RIVEDVNAIIETYAPEEFKQ-EKWKFSPQKGNVAFGSALDGWGFTIIKFADIYA 206
aeEF2_snRNP_like_IV cd01681
This family represents domain IV of archaeal and eukaryotic elongation factor 2 (aeEF-2) and ...
574-746 1.34e-105

This family represents domain IV of archaeal and eukaryotic elongation factor 2 (aeEF-2) and of an evolutionarily conserved U5 snRNP-specific protein. U5 snRNP is a GTP-binding factor closely related to the ribosomal translocase EF-2. 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 of the small subunit of ribosome and the mRNA is shifted one codon relative to the ribosome. It has been shown that EF-2_IV domain mimics the shape of anticodon arm of the tRNA in the structurally homologous ternary complex of Phe-tRNA, EF-1 (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-2 displaces the A-site tRNA to the P-site by physical interaction with the anticodon arm.


Pssm-ID: 238839 [Multi-domain]  Cd Length: 177  Bit Score: 322.98  E-value: 1.34e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 574 DPVVSYRETVSAESDQMCLSKSPNKHNRLYMKARPFPDGLAEDIDKGDVSSRQELKTRARYLADKYEWEVTEARKIWCFG 653
Cdd:cd01681   1 DPVVSFRETVVETSSGTCLAKSPNKHNRLYMRAEPLPEELIEDIEKGKITLKDDKKKRARILLDKYGWDKLAARKIWAFG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 654 PDGTGPNMLVDVTKGVQY----LNEIKDSVVAGFQWATKEGALCEENMRAVRFDIHDVTLHTDAIHRGGGQIIPTARRVL 729
Cdd:cd01681  81 PDRTGPNILVDDTKGVQYdkslLNEIKDSIVAGFQWATKEGPLCEEPMRGVKFKLEDATLHADAIHRGGGQIIPAARRAC 160
                       170
                ....*....|....*..
gi 41386743 730 YACQLTAEPRLMEPIYL 746
Cdd:cd01681 161 YAAFLLASPRLMEPMYL 177
EF2_IV_snRNP cd01683
EF-2_domain IV_snRNP domain is a part of 116kD U5-specific protein of the U5 small ...
574-747 1.78e-67

EF-2_domain IV_snRNP domain is a part of 116kD U5-specific protein of the U5 small nucleoprotein (snRNP) particle, essential component of the spliceosome. The protein is structurally closely related to the eukaryotic translational elongation factor EF2. This domain has been also identified in 114kD U5-specific protein of Saccharomyces cerevisiae and may play an important role either in splicing process itself or the recycling of spliceosomal snRNP.


Pssm-ID: 238840 [Multi-domain]  Cd Length: 178  Bit Score: 221.78  E-value: 1.78e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 574 DPVVSYRETVSAESDQMCLSKSPNKHNRLYMKARPFPDGLAEDIDKGDVSSRQELKTRARYLADKYEWEVTEARKIWCFG 653
Cdd:cd01683   1 DPVVTFCETVVETSSAKCFAETPNKKNKITMIAEPLDKGLAEDIENGQLKLSWNRKKLGKFLRTKYGWDALAARSIWAFG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 654 PDGTGPNMLVDVT----KGVQYLNEIKDSVVAGFQWATKEGALCEENMRAVRFDIHDVTLHTDAIHRGGGQIIPTARRVL 729
Cdd:cd01683  81 PDTKGPNVLIDDTlpeeVDKNLLNSVKESIVQGFQWAVREGPLCEEPIRNVKFKLLDADIASEPIDRGGGQIIPTARRAC 160
                       170
                ....*....|....*...
gi 41386743 730 YACQLTAEPRLMEPIYLV 747
Cdd:cd01683 161 YSAFLLATPRLMEPIYEV 178
PRK13351 PRK13351
elongation factor G-like protein;
17-822 1.82e-65

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 232.15  E-value: 1.82e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   17 SNIRNMSVIAHVDHGKSTLTDSLVSKAGiiASARAGE----TRFTDTRKDEQERCITIKSTAISMYYEltendlafikqc 92
Cdd:PRK13351   6 MQIRNIGILAHIDAGKTTLTERILFYTG--KIHKMGEvedgTTVTDWMPQEQERGITIESAATSCDWD------------ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   93 kdgsGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALlelqlepe 172
Cdd:PRK13351  72 ----NHRINLIDTPGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVG-------- 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  173 elyQTFQRIVENVnviistygEDEGGPmgnimiDPVI--GTVGFGSGLHGwaftlkqfaemYVAKFASKgEAQLSPADRC 250
Cdd:PRK13351 140 ---ADLFKVLEDI--------EERFGK------RPLPlqLPIGSEDGFEG-----------VVDLITEP-ELHFSEGDGG 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  251 KKVEdmmKKLWGDRYFDPAggkftktangpdgkkypRTFAQLILDPIFKVFDAIMNFKKEETAKLIEKLDIKLDTEDKDK 330
Cdd:PRK13351 191 STVE---EGPIPEELLEEV-----------------EEAREKLIEALAEFDDELLELYLEGEELSAEQLRAPLREGTRSG 250
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  331 EGKPLLKAVMRRwlPAG-EALLQMITIHLPSPVTAQKYRcelLYEGPGDDEAAmgikNCDPKGPLMMYISKMVPTTDKGR 409
Cdd:PRK13351 251 HLVPVLFGSALK--NIGiEPLLDAVVDYLPSPLEVPPPR---GSKDNGKPVKV----DPDPEKPLLALVFKVQYDPYAGK 321
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  410 FYAFgRVFSGVVSTGLKVRimgpNYTPGKKEDLYlkpiqRTILMMGRYVEPIEDVPCGNIVGLVGVDQflVKTGTiTTFD 489
Cdd:PRK13351 322 LTYL-RVYSGTLRAGSQLY----NGTGGKREKVG-----RLFRLQGNKREEVDRAKAGDIVAVAGLKE--LETGD-TLHD 388
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  490 QAHNMRV--MKFsVSPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQC-IIEESGEHIIAGAGELHLEICLKDLEEDHA 566
Cdd:PRK13351 389 SADPVLLelLTF-PEPVVSLAVEPERRGDEQKLAEALEKLVWEDPSLRVeEDEETGQTILSGMGELHLEVALERLRREFK 467
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  567 cIPLKKSDPVVSYRETVsaesdqmclSKSPNKHNRlYMKArpfpDGLAedIDKGDVSSRqeLKTRARyladkyewevtea 646
Cdd:PRK13351 468 -LEVNTGKPQVAYRETI---------RKMAEGVYR-HKKQ----FGGK--GQFGEVHLR--VEPLER------------- 515
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  647 rkiwcfgpdGTGPNmLVDVTKGVQYLNEIKDSVVAGFQWATKEGALCEENMRAVRFDIHDVTLHTDAIHRGGGQIIptAR 726
Cdd:PRK13351 516 ---------GAGFI-FVSKVVGGAIPEELIPAVEKGIREALASGPLAGYPVTDLRVTVLDGKYHPVDSSESAFKAA--AR 583
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  727 RVLYACQLTAEPRLMEPIYLVEIQCPEQVVGGIYGVLNRKRGHVfEESQVMGTPMFVVKAYLPVNESFGFTADLRSNTGG 806
Cdd:PRK13351 584 KAFLEAFRKANPVLLEPIMELEITVPTEHVGDVLGDLSQRRGRI-EGTEPRGDGEVLVKAEAPLAELFGYATRLRSMTKG 662
                        810
                 ....*....|....*.
gi 41386743  807 QAFPQCVFDHWQILPG 822
Cdd:PRK13351 663 RGSFTMEFSHFDPVPP 678
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
17-823 8.89e-64

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: 227.62  E-value: 8.89e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  17 SNIRNMSVIAHVDHGKSTLTDSLVSKAGIIAsaRAGE----TRFTDTRKDEQERCITIKSTAISMYYeltendlafiKQC 92
Cdd:COG0480   7 EKIRNIGIVAHIDAGKTTLTERILFYTGAIH--RIGEvhdgNTVMDWMPEEQERGITITSAATTCEW----------KGH 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  93 KdgsgflINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALLElqlepe 172
Cdd:COG0480  75 K------INIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGAD------ 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 173 elyqtFQRIVE------NVNVIISTYgedeggPMGNimidpvigtvgfGSGLHGwaftlkqfaemyvakfaskgeaqlsp 246
Cdd:COG0480 143 -----FDRVLEqlkerlGANPVPLQL------PIGA------------EDDFKG-------------------------- 173
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 247 adrckkVEDM--MKKLwgdrYFDPAGGKFTKTANGPDG-----KKYpRtfAQLIldpifkvfDAIMNFKKEetakLIEKL 319
Cdd:COG0480 174 ------VIDLvtMKAY----VYDDELGAKYEEEEIPAElkeeaEEA-R--EELI--------EAVAETDDE----LMEKY 228
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 320 --DIKLDTEDkdkegkplLKAVMRRWLPAGE----------------ALLQMITIHLPSPVTAQKYRCELLyegpgDDEA 381
Cdd:COG0480 229 leGEELTEEE--------IKAGLRKATLAGKivpvlcgsafknkgvqPLLDAVVDYLPSPLDVPAIKGVDP-----DTGE 295
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 382 AMGIKnCDPKGPLMMYISKMVptTDK--GRfYAFGRVFSGVVSTGLKVRimgpNYTPGKKEDlylkpIQRTILMMGRYVE 459
Cdd:COG0480 296 EVERK-PDDDEPFSALVFKTM--TDPfvGK-LSFFRVYSGTLKSGSTVY----NSTKGKKER-----IGRLLRMHGNKRE 362
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 460 PIEDVPCGNIVGLVGVDQflVKTG-TITtfDQAHNMRV--MKFSVsPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQC 536
Cdd:COG0480 363 EVDEAGAGDIVAVVKLKD--TTTGdTLC--DEDHPIVLepIEFPE-PVISVAIEPKTKADEDKLSTALAKLAEEDPTFRV 437
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 537 II-EESGEHIIAGAGELHLEICLKDLEEDHAcIPLKKSDPVVSYRETVSAESDQMclskspNKHNR----------LYMK 605
Cdd:COG0480 438 ETdEETGQTIISGMGELHLEIIVDRLKREFG-VEVNVGKPQVAYRETIRKKAEAE------GKHKKqsgghgqygdVWIE 510
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 606 ARPFPDGlaedidkgdvssrqelktrarylaDKYEWEvtearkiwcfgpDgtgpnmlvDVTKGV---QYLNeikdSVVAG 682
Cdd:COG0480 511 IEPLPRG------------------------EGFEFV------------D--------KIVGGVipkEYIP----AVEKG 542
                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 683 FQWATKEGALCE---ENMRAVRFD--IHDVtlhtD--------AihrgggqiiptARRVLYACQLTAEPRLMEPIYLVEI 749
Cdd:COG0480 543 IREAMEKGVLAGypvVDVKVTLYDgsYHPV----DssemafkiA-----------ASMAFKEAAKKAKPVLLEPIMKVEV 607
                       810       820       830       840       850       860       870
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41386743 750 QCPEQVVGGIYGVLNRKRGhvfeesQVMGT----PMFVVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQILPGD 823
Cdd:COG0480 608 TVPEEYMGDVMGDLNSRRG------RILGMesrgGAQVIKAEVPLAEMFGYATDLRSLTQGRGSFTMEFSHYEEVPAN 679
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
25-823 2.41e-60

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 217.30  E-value: 2.41e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   25 IAHVDHGKSTLTDSLVSKAGIIAsaRAGE----TRFTDTRKDEQERCITIKSTAISMYYEltendlafikqckdgsGFLI 100
Cdd:PRK12740   1 VGHSGAGKTTLTEAILFYTGAIH--RIGEvedgTTTMDFMPEERERGISITSAATTCEWK----------------GHKI 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  101 NLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALLElqlepeelyqtFQR 180
Cdd:PRK12740  63 NLIDTPGHVDFTGEVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRAGAD-----------FFR 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  181 IVE------NVNVIISTYGEDEGgpmgnimiDPVIGTVGFgsglhgwaFTLKQFaemyvaKFASKGEAQLS--PADRCKK 252
Cdd:PRK12740 132 VLAqlqeklGAPVVPLQLPIGEG--------DDFTGVVDL--------LSMKAY------RYDEGGPSEEIeiPAELLDR 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  253 VEDMmkklwgdRyfdpaggkftktangpdgkkyprtfAQLIldpifkvfDAIMNFKKEETAKLIEklDIKLDTEDkdkeg 332
Cdd:PRK12740 190 AEEA-------R-------------------------EELL--------EALAEFDDELMEKYLE--GEELSEEE----- 222
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  333 kplLKAVMRRWLPAGE----------------ALLQMITIHLPSPVTAQKyrcellyeGPGDDEAAMGIKNCDPKGPLMM 396
Cdd:PRK12740 223 ---IKAGLRKATLAGEivpvfcgsalknkgvqRLLDAVVDYLPSPLEVPP--------VDGEDGEEGAELAPDPDGPLVA 291
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  397 YISKMVPTTDKGRfYAFGRVFSGVVSTGLKVRimgpNYTPGKKEDlylkpIQRTILMMGRYVEPIEDVPCGNIVGLVGVD 476
Cdd:PRK12740 292 LVFKTMDDPFVGK-LSLVRVYSGTLKKGDTLY----NSGTGKKER-----VGRLYRMHGKQREEVDEAVAGDIVAVAKLK 361
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  477 QflVKTG-TITtfDQAHNMRV--MKFSVsPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQciIE---ESGEHIIAGAG 550
Cdd:PRK12740 362 D--AATGdTLC--DKGDPILLepMEFPE-PVISLAIEPKDKGDEEKLSEALGKLAEEDPTLR--VErdeETGQTILSGMG 434
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  551 ELHLEICLKDLEEDHAcIPLKKSDPVVSYRETVSAESDQMClskspnKHnrlymkarpfpdglaediDK--------GDV 622
Cdd:PRK12740 435 ELHLDVALERLKREYG-VEVETGPPQVPYRETIRKKAEGHG------RH------------------KKqsgghgqfGDV 489
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  623 ssrqelktraryladKYEWEVtearkiwcfGPDGTGpNMLVD-VTKGV---QYLneikDSVVAGFQWATKEGALCEENMR 698
Cdd:PRK12740 490 ---------------WLEVEP---------LPRGEG-FEFVDkVVGGAvprQYI----PAVEKGVREALEKGVLAGYPVV 540
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  699 AVRFDIHDVTLHT----DAihrgggqiiptarrvlyACQL-----------TAEPRLMEPIYLVEIQCPEQVVGGIYGVL 763
Cdd:PRK12740 541 DVKVTLTDGSYHSvdssEM-----------------AFKIaarlafrealpKAKPVLLEPIMKVEVSVPEEFVGDVIGDL 603
                        810       820       830       840       850       860
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41386743  764 NRKRGhvfeesQVMGT----PMFVVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQILPGD 823
Cdd:PRK12740 604 SSRRG------RILGMesrgGGDVVRAEVPLAEMFGYATDLRSLTQGRGSFSMEFSHYEEVPGN 661
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
18-224 7.93e-60

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: 201.60  E-value: 7.93e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743    18 NIRNMSVIAHVDHGKSTLTDSLVSKAGIIASA---RAGETRFTDTRKDEQERCITIKSTAISMYYEltendlafikqckd 94
Cdd:pfam00009   2 RHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRgevKGEGEAGLDNLPEERERGITIKSAAVSFETK-------------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743    95 gsGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRAllelqlepeeL 174
Cdd:pfam00009  68 --DYLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRV----------D 135
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 41386743   175 YQTFQRIVENVNviiSTYGEDEGGPMGNImidPVIgtvgFGSGLHGWAFT 224
Cdd:pfam00009 136 GAELEEVVEEVS---RELLEKYGEDGEFV---PVV----PGSALKGEGVQ 175
EF-G TIGR00484
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ...
18-821 2.11e-57

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: 209.28  E-value: 2.11e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743    18 NIRNMSVIAHVDHGKSTLTDSLVSKAGIIAsaRAGETR----FTDTRKDEQERCITIKSTAISMYYeltendlafikqck 93
Cdd:TIGR00484   9 RFRNIGISAHIDAGKTTTTERILFYTGRIH--KIGEVHdgaaTMDWMEQEKERGITITSAATTVFW-------------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743    94 dgSGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALLelqlepee 173
Cdd:TIGR00484  73 --KGHRINIIDTPGHVDFTVEVERSLRVLDGAVAVLDAVGGVQPQSETVWRQANRYEVPRIAFVNKMDKTGA-------- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   174 lyqTFQRIVENVNVIISTYGEDEGGPMG-----NIMIDPVIGTVGFGSGLHGWAFTLKQFAEMYVAKFASKGEAQLSPAd 248
Cdd:TIGR00484 143 ---NFLRVVNQIKQRLGANAVPIQLPIGaednfIGVIDLVEMKAYFFNGDKGTKAIEKEIPSDLLEQAKELRENLVEAV- 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   249 rCKKVEDMMKKLWGdryfdpaggkftktangpdGKKYPrtfaqlildpifkvFDAIMNFKKEETAKLiEKLDIKLDTEDK 328
Cdd:TIGR00484 219 -AEFDEELMEKYLE-------------------GEELT--------------IEEIKNAIRKGVLNC-EFFPVLCGSAFK 263
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   329 DKEGKPLLKAVMRrwlpageallqmitiHLPSPVTAQKYRcellyeGPGDDEAAMGIKNCDPKGPLMMYISKMVPTTDKG 408
Cdd:TIGR00484 264 NKGVQLLLDAVVD---------------YLPSPTDVPAIK------GIDPDTEKEIERKASDDEPFSALAFKVATDPFVG 322
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   409 RFyAFGRVFSGVVSTGLKVRimgpNYTPGKKEDlylkpIQRTILMMGRYVEPIEDVPCGNIVGLVGVDQflVKTG-TITT 487
Cdd:TIGR00484 323 QL-TFVRVYSGVLKSGSYVK----NSRKNKKER-----VGRLVKMHANNREEIKEVRAGDICAAIGLKD--TTTGdTLCD 390
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   488 FDQAHNMRVMKFSvSPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCII-EESGEHIIAGAGELHLEICLKDLEEDHA 566
Cdd:TIGR00484 391 PKIDVILERMEFP-EPVISLAVEPKTKADQEKMGIALGKLAEEDPTFRTFTdPETGQTIIAGMGELHLDIIVDRMKREFK 469
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   567 cIPLKKSDPVVSYRET----VSAESDQMCLSKSPNKHNRLYMKARPFPDGLAEDID--KGDVSSRQELKTraryladkye 640
Cdd:TIGR00484 470 -VEANVGAPQVAYRETirskVEVEGKHAKQSGGRGQYGHVKIRFEPLEPKGYEFVNeiKGGVIPREYIPA---------- 538
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   641 wevtearkiwcfgpdgtgpnmlvdVTKGVQylNEIKDSVVAGFQWAtkegalceeNMRAVRFD--IHDVTLHTDAIHRGG 718
Cdd:TIGR00484 539 ------------------------VDKGLQ--EAMESGPLAGYPVV---------DIKATLFDgsYHDVDSSEMAFKLAA 583
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   719 GQIIPTARRVlyacqltAEPRLMEPIYLVEIQCPEQVVGGIYGVLNRKRGHVfeESQVMGTPMFVVKAYLPVNESFGFTA 798
Cdd:TIGR00484 584 SLAFKEAGKK-------ANPVLLEPIMKVEVEVPEEYMGDVMGDLSSRRGII--EGMEARGNVQKIKAEVPLSEMFGYAT 654
                         810       820
                  ....*....|....*....|...
gi 41386743   799 DLRSNTGGQAFPQCVFDHWQILP 821
Cdd:TIGR00484 655 DLRSFTQGRGTYSMEFLHYGEVP 677
EF2_snRNP_like_II cd03700
Domain II of elongation factor 2 and C-terminal domain of the spliceosomal human 116kD U5 ...
394-488 3.01e-50

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: 171.26  E-value: 3.01e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 394 LMMYISKMVPTTDKGRFYAFGRVFSGVVSTGLKVRIMGPNYTPGKKEDLYLKPIQRTILMMGRYVEPIEDVPCGNIVGLV 473
Cdd:cd03700   1 LMVYSSKMVPTSDKGRFYAFGRVFAGTVHAGQKVRILGPNYTPGKKEDLRIKAIQRLWLMMGRYVEEINDVPAGNIVGLV 80
                        90
                ....*....|....*
gi 41386743 474 GVDQFLVKTGTITTF 488
Cdd:cd03700  81 GIDQFLQKTGTTTTI 95
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
20-232 5.89e-50

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: 175.15  E-value: 5.89e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  20 RNMSVIAHVDHGKSTLTDSLVSKA-GIIASARAGE--TRFTDTRKDEQERCITIKSTAISMYYELTEndlafikqckdGS 96
Cdd:cd04167   1 RNVCIAGHLHHGKTSLLDMLIEQThKRTPSVKLGWkpLRYTDTRKDEQERGISIKSNPISLVLEDSK-----------GK 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  97 GFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALLELQLEPEELYQ 176
Cdd:cd04167  70 SYLINIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDRLILELKLPPTDAYY 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 41386743 177 TFQRIVENVNVIISTYGEDEggpmgNIMIDPVIGTVGFGSGLHGWAFTLKQFAEMY 232
Cdd:cd04167 150 KLRHTIDEINNYIASFSTTE-----GFLVSPELGNVLFASSKFGFCFTLESFAKKY 200
eEF2_snRNP_like_C cd04096
eEF2_snRNP_like_C: this family represents a C-terminal domain of eukaryotic elongation factor ...
742-821 8.89e-49

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: 166.56  E-value: 8.89e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 742 EPIYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQVMGTPMFVVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQILP 821
Cdd:cd04096   1 EPIYLVEIQCPEDALGKVYSVLSKRRGHVLSEEPKEGTPLFEIKAYLPVIESFGFETDLRSATSGQAFPQLVFSHWEIVP 80
EF2_II cd16268
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 ...
393-488 3.71e-47

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: 162.77  E-value: 3.71e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 393 PLMMYISKMVPTTDKGRFYAFGRVFSGVVSTGLKVRIMGPNYTPGKKEDLYLKPIQRTILMMGRYVEPIEDVPCGNIVGL 472
Cdd:cd16268   1 PLVMYVSKMVPTDKGAGFVAFGRVFSGTVRRGQEVYILGPKYVPGKKDDLKKKRIQQTYLMMGREREPVDEVPAGNIVGL 80
                        90
                ....*....|....*.
gi 41386743 473 VGVDQFLVKTGTITTF 488
Cdd:cd16268  81 VGLDDFLAKSGTTTSS 96
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
21-224 4.27e-47

GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function.


Pssm-ID: 206647 [Multi-domain]  Cd Length: 183  Bit Score: 165.93  E-value: 4.27e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  21 NMSVIAHVDHGKSTLTDSLVSKAGIIASARAGETRFTDTRKDEQERCITIKSTAISMYYEltendlafikqckdgsGFLI 100
Cdd:cd00881   1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWP----------------KRRI 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 101 NLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRAllelqlEPEELYQTFQR 180
Cdd:cd00881  65 NFIDTPGHEDFSKETVRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRV------GEEDFDEVLRE 138
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 41386743 181 IVENVNVIISTYGEDEGGPmgnimidpvigtVGFGSGLHGWAFT 224
Cdd:cd00881 139 IKELLKLIGFTFLKGKDVP------------IIPISALTGEGIE 170
EF2_snRNP_III cd16261
Domain III of Elongation Factor 2 (EF2); This model represents domain III of Elongation factor ...
503-574 1.02e-41

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: 146.56  E-value: 1.02e-41
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41386743 503 PVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCIIEESGEHIIAGAGELHLEICLKDLEEDHACIPLKKSD 574
Cdd:cd16261   1 PVVRVAVEPKNPSDLPKLVEGLKKLAKSDPTVQVKIEEEGEHLIAGAGELHLEICLKDLKEDFAGIEIKVSD 72
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
20-161 2.69e-40

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: 146.52  E-value: 2.69e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  20 RNMSVIAHVDHGKSTLTDSLVSKAGIIaSARAGETRFTDTRKDEQERCITIKSTAISMYYeltendlafikQCKDGSGFL 99
Cdd:cd01890   1 RNFSIIAHIDHGKSTLADRLLELTGTV-SEREMKEQVLDSMDLERERGITIKAQAVRLFY-----------KAKDGEEYL 68
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41386743 100 INLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIaER---IKPVLmmNKMD 161
Cdd:cd01890  69 LNLIDTPGHVDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLAL-ENnleIIPVI--NKID 130
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
18-162 1.91e-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: 130.41  E-value: 1.91e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  18 NIRNMSVIAHVDHGKSTLTDSLVSKAGIIASARAGETRFTDTRKDEQERCITIKSTAISMYYEltendlafikqckdgsG 97
Cdd:cd01891   1 KIRNIAIIAHVDHGKTTLVDALLKQSGTFRENEEVGERVMDSNDLERERGITILAKNTAITYK----------------D 64
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41386743  98 FLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDR 162
Cdd:cd01891  65 TKINIIDTPGHADFGGEVERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDR 129
EFG_IV pfam03764
Elongation factor G, domain IV; This domain is found in elongation factor G, elongation factor ...
620-737 3.10e-34

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: 126.95  E-value: 3.10e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   620 GDVSSRQEL----KTRARYLADKYEWEVTEARKIWCFGPDGTG-PNMLVDVTKGVQYLNEIKDSVVAGFQWATKEGALCE 694
Cdd:pfam03764   1 PQVAYRETIrkpvKERAYKHKKQSGGDGQYARVILRIEPLPPGsGNEFVDETVGGQIPKEFIPAVEKGFQEAMKEGPLAG 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 41386743   695 ENMRAVRFDIHDVTLHtdAIHRGGGQIIPTARRVLYACQLTAE 737
Cdd:pfam03764  81 EPVTDVKVTLLDGSYH--EVDSSEAAFIPAARRAFREALLKAS 121
lepA TIGR01393
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a ...
17-161 3.31e-32

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: 133.22  E-value: 3.31e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743    17 SNIRNMSVIAHVDHGKSTLTDSLVSKAGIIaSARAGETRFTDTRKDEQERCITIKSTAISMYYeltendlafikQCKDGS 96
Cdd:TIGR01393   1 KNIRNFSIIAHIDHGKSTLADRLLEYTGAI-SEREMREQVLDSMDLERERGITIKAQAVRLNY-----------KAKDGE 68
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41386743    97 GFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIaER---IKPVLmmNKMD 161
Cdd:TIGR01393  69 TYVLNLIDTPGHVDFSYEVSRSLAACEGALLLVDAAQGIEAQTLANVYLAL-ENdleIIPVI--NKID 133
eEF2_C_snRNP cd04098
eEF2_C_snRNP: This family includes a C-terminal portion of the spliceosomal human 116kD U5 ...
742-821 6.62e-32

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: 118.89  E-value: 6.62e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 742 EPIYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQVMGTPMFVVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQILP 821
Cdd:cd04098   1 EPIYEVEITCPADAVSAVYEVLSRRRGHVIYDTPIPGTPLYEVKAFIPVIESFGFETDLRVHTQGQAFCQSVFDHWQIVP 80
LepA COG0481
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ...
15-161 9.50e-32

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


Pssm-ID: 440249 [Multi-domain]  Cd Length: 598  Bit Score: 131.68  E-value: 9.50e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  15 KKSNIRNMSVIAHVDHGKSTLTDSLVSKAGIIaSARAGETRFTDTRKDEQERCITIKSTAISMYYeltendlafikQCKD 94
Cdd:COG0481   2 DQKNIRNFSIIAHIDHGKSTLADRLLELTGTL-SEREMKEQVLDSMDLERERGITIKAQAVRLNY-----------KAKD 69
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  95 GSGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIaER---IKPVLmmNKMD 161
Cdd:COG0481  70 GETYQLNLIDTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTLANVYLAL-ENdleIIPVI--NKID 136
Elongation_Factor_C cd01514
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ...
742-821 2.45e-31

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: 117.20  E-value: 2.45e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 742 EPIYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQvMGTPMFVVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQILP 821
Cdd:cd01514   1 EPIMKVEITVPEEYLGAVIGDLSKRRGEILGMEP-RGTGRVVIKAELPLAEMFGFATDLRSLTQGRASFSMEFSHYEPVP 79
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
21-162 7.93e-31

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: 122.22  E-value: 7.93e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  21 NMSVIAHVDHGKSTLTDSLVSKAGIIAsaRAGETRFTDTRKD----EQERCITIKSTAISMYYEltendlafikqckdgs 96
Cdd:cd01886   1 NIGIIAHIDAGKTTTTERILYYTGRIH--KIGEVHGGGATMDwmeqERERGITIQSAATTCFWK---------------- 62
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41386743  97 GFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDR 162
Cdd:cd01886  63 DHRINIIDTPGHVDFTIEVERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDR 128
TypA_BipA TIGR01394
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ...
19-162 1.94e-30

GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, a GTP-binding protein, is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways, but the precise function is unknown. [Regulatory functions, Other, Cellular processes, Adaptations to atypical conditions, Protein synthesis, Translation factors]


Pssm-ID: 273597 [Multi-domain]  Cd Length: 594  Bit Score: 127.42  E-value: 1.94e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743    19 IRNMSVIAHVDHGKSTLTDSLVSKAGIIASARAGETRFTDTRKDEQERCITI--KSTAIsMYyeltendlafikqckdgS 96
Cdd:TIGR01394   1 IRNIAIIAHVDHGKTTLVDALLKQSGTFRANEAVAERVMDSNDLERERGITIlaKNTAI-RY-----------------N 62
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41386743    97 GFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDR 162
Cdd:TIGR01394  63 GTKINIVDTPGHADFGGEVERVLGMVDGVLLLVDASEGPMPQTRFVLKKALELGLKPIVVINKIDR 128
EFG_IV smart00889
Elongation factor G, domain IV; Translation elongation factors are responsible for two main ...
625-737 3.73e-29

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: 112.25  E-value: 3.73e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743    625 RQELKTRARYLADKYEWEVTEARKIWCFGPDGTGPNMLVDVTK--GVQYLnEIKDSVVAGFQWATKEGALCEENMRAVRF 702
Cdd:smart00889   9 TKPVKEAEGKHKKQSGGDGQYARVILEVEPLERGSGFEFDDTIvgGVIPK-EYIPAVEKGFREALEEGPLAGYPVVDVKV 87
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 41386743    703 DIHDVTLHTDaIHRGGGqIIPTARRVLYACQLTAE 737
Cdd:smart00889  88 TLLDGSYHEV-DSSEMA-FKPAARRAFKEALLKAG 120
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
15-162 8.51e-29

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


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 122.44  E-value: 8.51e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  15 KKSNIRNMSVIAHVDHGKSTLTDSLVSKAGIIASARAGETRFTDTRKDEQERCITIKSTAISMYYEltendlafikqckd 94
Cdd:COG1217   2 MREDIRNIAIIAHVDHGKTTLVDALLKQSGTFRENQEVAERVMDSNDLERERGITILAKNTAVRYK-------------- 67
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41386743  95 gsGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDR 162
Cdd:COG1217  68 --GVKINIVDTPGHADFGGEVERVLSMVDGVLLLVDAFEGPMPQTRFVLKKALELGLKPIVVINKIDR 133
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
21-163 5.46e-28

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: 113.10  E-value: 5.46e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  21 NMSVIAHVDHGKSTLTDSLVSKAGIIA---SARAGETrFTDTRKDEQERCITIKSTAISMYYELTEndlafikqckdgsg 97
Cdd:cd04168   1 NIGILAHVDAGKTTLTESLLYTSGAIRelgSVDKGTT-RTDSMELERQRGITIFSAVASFQWEDTK-------------- 65
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41386743  98 flINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRA 163
Cdd:cd04168  66 --VNIIDTPGHMDFIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTIIFVNKIDRA 129
EFG_C pfam00679
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ...
739-826 7.13e-27

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: 104.55  E-value: 7.13e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   739 RLMEPIYLVEIQCPEQVVGGIYGVLNRKRGHVfEESQVMGTPMFVVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQ 818
Cdd:pfam00679   1 VLLEPIEKVTIDVPEEYVGDVISDLNSRRGEI-LDMDPDDGGRVVIEAEVPLAELFGFATELRSLTKGRGSFSMEFSGYQ 79

                  ....*...
gi 41386743   819 ILPGDPKD 826
Cdd:pfam00679  80 PVPGDILD 87
EF2_II_snRNP cd04090
Domain II of the spliceosomal 116kD U5 small nuclear ribonucleoprotein (snRNP) component; This ...
394-487 7.47e-26

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


Pssm-ID: 293907 [Multi-domain]  Cd Length: 94  Bit Score: 101.93  E-value: 7.47e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 394 LMMYISKMVPTTDKGRFYAFGRVFSGVVSTGLKVRIMGPNYTPGKKEDLYLKPIQRTILMMGRYVEPIEDVPCGNIVGLV 473
Cdd:cd04090   1 LVVHVTKLYSSSDGGSFWALGRIYSGTLRKGQKVKVLGENYSLEDEEDMTVCTVGRLWILGARYKYEVNSAPAGNWVLIK 80
                        90
                ....*....|....
gi 41386743 474 GVDQFLVKTGTITT 487
Cdd:cd04090  81 GIDQSIVKTATITS 94
EFG_III-like cd16257
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G ...
503-573 1.12e-24

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: 97.80  E-value: 1.12e-24
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41386743 503 PVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCIIEES-GEHIIAGAGELHLEICLKDLEEDhACIPLKKS 573
Cdd:cd16257   1 PVVFVTVEVKNPLDQEKLLEGLERLSEEDPALQVYREEStGEFILSGLGELHLEIIVARLERE-YGVELVVS 71
EFG_C smart00838
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ...
740-821 1.79e-23

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: 94.88  E-value: 1.79e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743    740 LMEPIYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQvmGTPMFVVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQI 819
Cdd:smart00838   1 LLEPIMKVEVTVPEEYMGDVIGDLNSRRGKIEGMEQ--RGGAQVIKAKVPLSEMFGYATDLRSATQGRATWSMEFSHYEE 78

                   ..
gi 41386743    820 LP 821
Cdd:smart00838  79 VP 80
PRK10218 PRK10218
translational GTPase TypA;
18-162 2.88e-23

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 105.18  E-value: 2.88e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   18 NIRNMSVIAHVDHGKSTLTDSLVSKAGIIASARAGETRFTDTRKDEQERCITI--KSTAISMyyelteNDlafikqckdg 95
Cdd:PRK10218   4 KLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITIlaKNTAIKW------ND---------- 67
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41386743   96 sgFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDR 162
Cdd:PRK10218  68 --YRINIVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDR 132
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
21-163 1.77e-22

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: 98.05  E-value: 1.77e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  21 NMSVIAHVDHGKSTLTDSLVSKAGIIAsaRAG----ETRFTDTRKDEQERCITIKSTAISMYYEltendlafikqckdgs 96
Cdd:cd04170   1 NIALVGHSGSGKTTLAEALLYATGAID--RLGrvedGNTVSDYDPEEKKRKMSIETSVAPLEWN---------------- 62
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41386743  97 GFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRA 163
Cdd:cd04170  63 GHKINLIDTPGYADFVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRA 129
RF3 cd04169
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ...
20-162 1.03e-17

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: 84.18  E-value: 1.03e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  20 RNMSVIAHVDHGKSTLTDSLVSKAGIIASARA----GETRFT--DTRKDEQERCITIKSTAISMYYEltendlafikqck 93
Cdd:cd04169   3 RTFAIISHPDAGKTTLTEKLLLFGGAIQEAGAvkarKSRKHAtsDWMEIEKQRGISVTSSVMQFEYK------------- 69
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41386743  94 dgsGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDR 162
Cdd:cd04169  70 ---GCVINLLDTPGHEDFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDR 135
EFG_mtEFG_C cd03713
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational ...
742-821 4.80e-17

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: 76.41  E-value: 4.80e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 742 EPIYLVEIQCPEQVVGGIYGVLNRKRGHVfeESQVMGTPMFVVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQILP 821
Cdd:cd03713   1 EPIMKVEVTVPEEYMGDVIGDLSSRRGQI--LGTESRGGWKVIKAEVPLAEMFGYSTDLRSLTQGRGSFTMEFSHYEEVP 78
snRNP_III cd16264
Domain III of the spliceosomal 116kD U5 small nuclear ribonucleoprotein (snRNP) component; ...
503-574 3.11e-16

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: 74.07  E-value: 3.11e-16
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41386743 503 PVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCIIEESGEHIIAGAGELHLEICLKDLEEDHACIPLKKSD 574
Cdd:cd16264   1 SVFKIAVEPLNPSELPKMLDGLRKVNKSYPLLITKVEESGEHVILGTGELYMDCVMHDLRKMYSEIEIKVAD 72
EFG_III pfam14492
Elongation Factor G, domain III; This domain is found in Elongation Factor G. It shares a ...
503-556 4.72e-14

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: 67.89  E-value: 4.72e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 41386743   503 PVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCII-EESGEHIIAGAGELHLEI 556
Cdd:pfam14492   4 PVISVAIEPKTKGDEDKLSKALNRLLEEDPTLRVERdEETGETILSGMGELHLEI 58
EFG_III cd16262
Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial ...
503-556 2.49e-12

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: 62.86  E-value: 2.49e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 41386743 503 PVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCII-EESGEHIIAGAGELHLEI 556
Cdd:cd16262   3 PVISLAIEPKTKADEDKLSKALARLAEEDPTLRVSRdEETGQTILSGMGELHLEI 57
EFG_like_IV cd01680
Elongation Factor G-like domain IV. This family includes the translational elongation factor ...
579-733 3.29e-12

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: 63.80  E-value: 3.29e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 579 YRETVSAESDqmCLSKSPN------KHNRLYMKARPFPDGlaedidkgdvssrqelktraryladkyewevtearkiwcf 652
Cdd:cd01680   1 YRETIRKSVE--ATGEFERelggkpQFGEVTLRVEPLERG---------------------------------------- 38
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 653 gpdgtGPNMLVDVTKGVQYLNEIKDSVVAGFQWATKEGALCEENMRAVRFDIHDVTLHTDAihRGGGQIIPTARRVLY-A 731
Cdd:cd01680  39 -----SGVRVVDPVDEELLPAELKEAVEEGIRDACASGPLTGYPLTDVRVTVLDVPYHEGV--STEAGFRAAAGRAFEsA 111

                ..
gi 41386743 732 CQ 733
Cdd:cd01680 112 AQ 113
prfC PRK00741
peptide chain release factor 3; Provisional
20-162 9.79e-12

peptide chain release factor 3; Provisional


Pssm-ID: 179105 [Multi-domain]  Cd Length: 526  Bit Score: 68.24  E-value: 9.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   20 RNMSVIAHVDHGKSTLTDSL------VSKAGIIASARAGetRF--TDTRKDEQERCITIKSTAISMYYEltendlafikq 91
Cdd:PRK00741  11 RTFAIISHPDAGKTTLTEKLllfggaIQEAGTVKGRKSG--RHatSDWMEMEKQRGISVTSSVMQFPYR----------- 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41386743   92 ckdgsGFLINLIDSPGHVDFSSE----VTAAlrvtDGALVVVDCVSGVCVQTET---VLRQaiaeRIKPVL-MMNKMDR 162
Cdd:PRK00741  78 -----DCLINLLDTPGHEDFSEDtyrtLTAV----DSALMVIDAAKGVEPQTRKlmeVCRL----RDTPIFtFINKLDR 143
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
19-161 1.62e-11

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: 63.16  E-value: 1.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743    19 IRNMSVIAHVDHGKSTLTDSLVSKAGIIASARAGETRftdtrkDEQERCITIkstaismyyeltendlafikqckDGSGF 98
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTR------NYVTTVIEE-----------------------DGKTY 51
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743    99 LINLIDSPGHVDFSS-------EVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAErIKPVLMMNKMD 161
Cdd:TIGR00231  52 KFNLLDTAGQEDYDAirrlyypQVERSLRVFDIVILVLDVEEILEKQTKEIIHHADSG-VPIILVGNKID 120
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
13-161 3.51e-10

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: 63.03  E-value: 3.51e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  13 MDKKSNIrNMSVIAHVDHGKSTLTDSLVSKAGII----------ASARAGETRFT-----DTRKDEQERCITIkstaism 77
Cdd:COG5256   2 ASEKPHL-NLVVIGHVDHGKSTLVGRLLYETGAIdehiiekyeeEAEKKGKESFKfawvmDRLKEERERGVTI------- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  78 yyeltenDLAFIKQCKDGSGFLInlIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQT-ETVL-------RQAIae 149
Cdd:COG5256  74 -------DLAHKKFETDKYYFTI--IDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTrEHAFlartlgiNQLI-- 142
                       170
                ....*....|..
gi 41386743 150 rikpvLMMNKMD 161
Cdd:COG5256 143 -----VAVNKMD 149
PLN03126 PLN03126
Elongation factor Tu; Provisional
4-162 1.12e-09

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 61.55  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743    4 FTVDQIRAIMDKKSNIRNMSVIAHVDHGKSTLTDSLVSKAGIIASARAGETRFTDTRKDEQERCITIKSTAISmyYELTE 83
Cdd:PLN03126  66 FTVRAARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVE--YETEN 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   84 NDLAFikqckdgsgflinlIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQT-ETVLrqaIAERI---KPVLMMNK 159
Cdd:PLN03126 144 RHYAH--------------VDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTkEHIL---LAKQVgvpNMVVFLNK 206

                 ...
gi 41386743  160 MDR 162
Cdd:PLN03126 207 QDQ 209
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
410-480 1.13e-09

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: 55.35  E-value: 1.13e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41386743   410 FYAFGRVFSGVVSTGLKVRIMgPNYTPGKKEDLYLKPIQRtilMMGRYVEPIEDVPCGNIVGLVGVDQFLV 480
Cdd:pfam03144   2 TVATGRVESGTLKKGDKVRIL-PNGTGKKKIVTRVTSLLM---FHAPLREAVAGDNAGLILAGVGLEDIRV 68
mtEFG1_C cd04097
mtEFG1_C: C-terminus of mitochondrial Elongation factor G1 (mtEFG1)-like proteins found in ...
742-808 1.89e-09

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: 55.02  E-value: 1.89e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41386743 742 EPIYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQVMGTpmFVVKAYLPVNESFGFTADLRSNTGGQA 808
Cdd:cd04097   1 EPIMKVEVTAPTEFQGNVIGLLNKRKGTIVDTDTGEDE--FTLEAEVPLNDMFGYSTELRSMTQGKG 65
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
27-197 2.07e-09

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


Pssm-ID: 129567 [Multi-domain]  Cd Length: 581  Bit Score: 61.04  E-value: 2.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743    27 HVDHGKSTLTDSLVSKAgiiasaragetrfTDTRKDEQERCITIkstaismyyeltenDLAFIKQCKDgsGFLINLIDSP 106
Cdd:TIGR00475   8 HVDHGKTTLLKALTGIA-------------ADRLPEEKKRGMTI--------------DLGFAYFPLP--DYRLGFIDVP 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   107 GHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKP-VLMMNKMDRALLELQLEPEELYQTFQR---IV 182
Cdd:TIGR00475  59 GHEKFISNAIAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHtIVVITKADRVNEEEIKRTEMFMKQILNsyiFL 138
                         170
                  ....*....|....*
gi 41386743   183 ENVNVIISTYGEDEG 197
Cdd:TIGR00475 139 KNAKIFKTSAKTGQG 153
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
27-163 2.49e-09

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


Pssm-ID: 206734 [Multi-domain]  Cd Length: 170  Bit Score: 57.23  E-value: 2.49e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  27 HVDHGKSTLTDSLVSKAgiiasaragetrfTDTRKDEQERCITIkstaismyyeltenDLAFiKQCKDGSGFLINLIDSP 106
Cdd:cd04171   7 HIDHGKTTLIKALTGIE-------------TDRLPEEKKRGITI--------------DLGF-AYLDLPDGKRLGFIDVP 58
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41386743 107 GHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLM-MNKMDRA 163
Cdd:cd04171  59 GHEKFVKNMLAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVvLTKADLV 116
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
21-134 3.33e-09

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: 57.89  E-value: 3.33e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  21 NMSVIAHVDHGKSTLTDSLVSKAGII----------ASARAGETRFT-----DTRKDEQERCITIkstAISMYYELTENd 85
Cdd:cd01883   1 NLVVIGHVDAGKSTLTGHLLYKLGGVdkrtiekyekEAKEMGKESFKyawvlDKLKEERERGVTI---DVGLAKFETEK- 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 41386743  86 lafikqckdgsgFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSG 134
Cdd:cd01883  77 ------------YRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKG 113
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
21-161 4.87e-09

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


Pssm-ID: 206676 [Multi-domain]  Cd Length: 192  Bit Score: 56.99  E-value: 4.87e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  21 NMSVIAHVDHGKSTLTDSLVSkagiIASARAgetrfTDTRKDEQERCITI----KSTAISMYYELTENDLAFIKQCKdgs 96
Cdd:cd01889   2 NVGLLGHVDSGKTSLAKALSE----IASTAA-----FDKNPQSQERGITLdlgfSSFEVDKPKHLEDNENPQIENYQ--- 69
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41386743  97 gflINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLrqAIAE--RIKPVLMMNKMD 161
Cdd:cd01889  70 ---ITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECL--VIGEllCKPLIVVLNKID 131
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
13-141 5.69e-09

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 59.17  E-value: 5.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   13 MDKKSNIrNMSVIAHVDHGKSTLTDSLVSKAG-----IIASAR-----AGETRFT-----DTRKDEQERCITIkstaism 77
Cdd:PRK12317   1 AKEKPHL-NLAVIGHVDHGKSTLVGRLLYETGaidehIIEELReeakeKGKESFKfawvmDRLKEERERGVTI------- 72
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41386743   78 yyeltenDLAFIKqcKDGSGFLINLIDSPGHVDF-SSEVTAALRvTDGALVVVDCVSGVCVQTET 141
Cdd:PRK12317  73 -------DLAHKK--FETDKYYFTIVDCPGHRDFvKNMITGASQ-ADAAVLVVAADDAGGVMPQT 127
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
13-134 2.64e-08

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 57.06  E-value: 2.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   13 MDK-KSNIrNMSVIAHVDHGKSTLTDSLVSKAGII----------ASARAGETRFT-----DTRKDEQERCITIkstais 76
Cdd:PTZ00141   1 MGKeKTHI-NLVVIGHVDSGKSTTTGHLIYKCGGIdkrtiekfekEAAEMGKGSFKyawvlDKLKAERERGITI------ 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 41386743   77 myyeltenDLAFIKqcKDGSGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSG 134
Cdd:PTZ00141  74 --------DIALWK--FETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAG 121
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
21-161 3.56e-08

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: 54.51  E-value: 3.56e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  21 NMSVIAHVDHGKSTLTDSL--VSKAGIIASARAGETrfTDTRKDEQERCITIKSTAISmyYELTENDLAFikqckdgsgf 98
Cdd:cd01884   4 NVGTIGHVDHGKTTLTAAItkVLAKKGGAKAKKYDE--IDKAPEEKARGITINTAHVE--YETANRHYAH---------- 69
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41386743  99 linlIDSPGHVDF-SSEVTAALRVtDGALVVVDCVSGVCVQT-ETVL--RQAIAERIkpVLMMNKMD 161
Cdd:cd01884  70 ----VDCPGHADYiKNMITGAAQM-DGAILVVSATDGPMPQTrEHLLlaRQVGVPYI--VVFLNKAD 129
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
24-208 7.05e-08

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: 52.86  E-value: 7.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  24 VIAHVDHGKSTLTDSLVSKAgiIASARAGEtrftdtrkdeqercIT--IKSTAISMyyeltendlafikqckDGSGFLIN 101
Cdd:cd01887   5 VMGHVDHGKTTLLDKIRKTN--VAAGEAGG--------------ITqhIGAYQVPI----------------DVKIPGIT 52
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 102 LIDSPGHVDFSsevtaALR-----VTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRallelqlepeelYQ 176
Cdd:cd01887  53 FIDTPGHEAFT-----NMRargasVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDK------------PY 115
                       170       180       190
                ....*....|....*....|....*....|....*
gi 41386743 177 TFQRIVENVNVIISTY---GEDEGgpmGNIMIDPV 208
Cdd:cd01887 116 GTEADPERVKNELSELglvGEEWG---GDVSIVPI 147
eif2g_arch TIGR03680
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ...
21-161 8.75e-08

translation initiation factor 2 subunit gamma; This model represents the archaeal translation initiation factor 2 subunit gamma and is found in all known archaea. eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.


Pssm-ID: 274720 [Multi-domain]  Cd Length: 406  Bit Score: 55.44  E-value: 8.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743    21 NMSVIAHVDHGKSTLTDSLVSKagiiasaragetrFTDTRKDEQERCITIK----STAISMYYELTENDlAFIKQ----- 91
Cdd:TIGR03680   6 NIGMVGHVDHGKTTLTKALTGV-------------WTDTHSEELKRGISIRlgyaDAEIYKCPECDGPE-CYTTEpvcpn 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41386743    92 CKDGSGFL--INLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGvCVQTETVLRQAIAERI---KPVLMMNKMD 161
Cdd:TIGR03680  72 CGSETELLrrVSFVDAPGHETLMATMLSGAALMDGALLVIAANEP-CPQPQTKEHLMALEIIgikNIVIVQNKID 145
PLN03127 PLN03127
Elongation factor Tu; Provisional
21-161 1.51e-07

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 54.83  E-value: 1.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   21 NMSVIAHVDHGKSTLTDSLVSKAGIIASARAGETRFTDTRKDEQERCITIKSTAISmyYELTENDLAFikqckdgsgfli 100
Cdd:PLN03127  63 NVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVE--YETAKRHYAH------------ 128
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41386743  101 nlIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQT-ETVL--RQAIAERIkpVLMMNKMD 161
Cdd:PLN03127 129 --VDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMPQTkEHILlaRQVGVPSL--VVFLNKVD 188
Tet_C cd03711
Tet_C: C-terminus of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology ...
742-821 2.55e-07

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: 48.77  E-value: 2.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 742 EPIYLVEIQCPEQVVGGIYGVLNRKRGhVFEESQvMGTPMFVVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQILP 821
Cdd:cd03711   1 EPYLRFELEVPQDALGRAMSDLAKMGA-TFEDPQ-IKGDEVTLEGTIPVATSQDYQSELPSYTHGEGVLETEFKGYRPCH 78
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
21-161 3.25e-07

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: 53.63  E-value: 3.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743    21 NMSVIAHVDHGKSTLTDSLVSKAGIIASARAGETRFTDTRKDEQERCITIKSTAISmyYELTENDLAFikqckdgsgfli 100
Cdd:TIGR00485  14 NVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVE--YETETRHYAH------------ 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41386743   101 nlIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQT-ETVL--RQAIAERIkpVLMMNKMD 161
Cdd:TIGR00485  80 --VDCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTrEHILlaRQVGVPYI--VVFLNKCD 139
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
21-161 6.76e-07

Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.


Pssm-ID: 206675 [Multi-domain]  Cd Length: 197  Bit Score: 50.73  E-value: 6.76e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  21 NMSVIAHVDHGKSTLTDSLvskAGIiasaragetrFTDTRKDEQERCITIK----STAISMYYELT--ENDLAFIKQCKD 94
Cdd:cd01888   2 NIGTIGHVAHGKTTLVKAL---SGV----------WTVRHKEELKRNITIKlgyaNAKIYKCPNCGcpRPYDTPECECPG 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  95 GSG-----FLINLIDSPGHvdfssEVTAALRVT-----DGALVVVDcVSGVCVQTETVLRQAIAERIKP---VLMMNKMD 161
Cdd:cd01888  69 CGGetklvRHVSFVDCPGH-----EILMATMLSgaavmDGALLLIA-ANEPCPQPQTSEHLAALEIMGLkhiIILQNKID 142
PRK12736 PRK12736
elongation factor Tu; Reviewed
21-161 1.12e-06

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 51.87  E-value: 1.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   21 NMSVIAHVDHGKSTLTDSLVSKAGIIASARAGETRFTDTRKDEQERCITIkSTAiSMYYELTENDLAFikqckdgsgfli 100
Cdd:PRK12736  14 NIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITI-NTA-HVEYETEKRHYAH------------ 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41386743  101 nlIDSPGHVDF-SSEVTAALRVtDGALVVVDCVSGVCVQT-ETVL--RQAIAERIkpVLMMNKMD 161
Cdd:PRK12736  80 --VDCPGHADYvKNMITGAAQM-DGAILVVAATDGPMPQTrEHILlaRQVGVPYL--VVFLNKVD 139
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
21-161 3.76e-06

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: 50.15  E-value: 3.76e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  21 NMSVIAHVDHGKSTLTdslvskAGI-IASARAGETRFT-----DTRKDEQERCITIKSTAISmyYElTEN-DLAFikqck 93
Cdd:COG0050  14 NIGTIGHVDHGKTTLT------AAItKVLAKKGGAKAKaydqiDKAPEEKERGITINTSHVE--YE-TEKrHYAH----- 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41386743  94 dgsgflinlIDSPGHVDF-SSEVTAALRVtDGALVVVDCVSGVCVQT-ETVL--RQAIAERIkpVLMMNKMD 161
Cdd:COG0050  80 ---------VDCPGHADYvKNMITGAAQM-DGAILVVSATDGPMPQTrEHILlaRQVGVPYI--VVFLNKCD 139
PRK12735 PRK12735
elongation factor Tu; Reviewed
21-161 4.25e-06

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 49.84  E-value: 4.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   21 NMSVIAHVDHGKSTLTDSL---VSKAGiIASARAGETrfTDTRKDEQERCITIKSTAISmyYElTEN-DLAFikqckdgs 96
Cdd:PRK12735  14 NVGTIGHVDHGKTTLTAAItkvLAKKG-GGEAKAYDQ--IDNAPEEKARGITINTSHVE--YE-TANrHYAH-------- 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41386743   97 gflinlIDSPGHVDF-SSEVTAALRVtDGALVVVDCVSGVCVQT-ETVL--RQAIAERIkpVLMMNKMD 161
Cdd:PRK12735  80 ------VDCPGHADYvKNMITGAAQM-DGAILVVSAADGPMPQTrEHILlaRQVGVPYI--VVFLNKCD 139
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
27-139 5.40e-06

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: 49.91  E-value: 5.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  27 HVDHGKSTLTdslvsKA--GIiasaragEtrfTDTRKDEQERCITIkstaismyyeltenDL--AFIKQckdGSGFLINL 102
Cdd:COG3276   8 HIDHGKTTLV-----KAltGI-------D---TDRLKEEKKRGITI--------------DLgfAYLPL---PDGRRLGF 55
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 41386743 103 IDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQT 139
Cdd:COG3276  56 VDVPGHEKFIKNMLAGAGGIDLVLLVVAADEGVMPQT 92
tufA CHL00071
elongation factor Tu
10-161 6.57e-06

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 49.57  E-value: 6.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   10 RAIMDKKSNIRNMSVIAHVDHGKSTLTDSLVSKAGIIASARAGETRFTDTRKDEQERCITIKSTAISmyYELTENDLAFi 89
Cdd:CHL00071   3 REKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVE--YETENRHYAH- 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41386743   90 kqckdgsgflinlIDSPGHVDF-SSEVTAALRVtDGALVVVDCVSGVCVQT-ETVL--RQAIAERIkpVLMMNKMD 161
Cdd:CHL00071  80 -------------VDCPGHADYvKNMITGAAQM-DGAILVVSAADGPMPQTkEHILlaKQVGVPNI--VVFLNKED 139
infB CHL00189
translation initiation factor 2; Provisional
23-163 6.98e-06

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 49.83  E-value: 6.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   23 SVIAHVDHGKSTLTDSLvsKAGIIASARAGEtrftdtrkdeqercITIKSTAISMYYEltendlafikqcKDGSGFLINL 102
Cdd:CHL00189 248 TILGHVDHGKTTLLDKI--RKTQIAQKEAGG--------------ITQKIGAYEVEFE------------YKDENQKIVF 299
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41386743  103 IDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRA 163
Cdd:CHL00189 300 LDTPGHEAFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKA 360
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
394-485 9.39e-06

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: 44.56  E-value: 9.39e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743 394 LMMYISKMVPTTDKGRFyAFGRVFSGVVSTGLKVRIMGPNYTpGKKEDLYLKPiqrtilmmgryvEPIEDVPCGNIVGLV 473
Cdd:cd01342   1 LVMQVFKVFYIPGRGRV-AGGRVESGTLKVGDEIRILPKGIT-GRVTSIERFH------------EEVDEAKAGDIVGIG 66
                        90
                ....*....|..
gi 41386743 474 GVDQFLVKTGTI 485
Cdd:cd01342  67 ILGVKDILTGDT 78
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
21-130 1.03e-05

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 48.69  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   21 NMSVIAHVDHGKSTLTDSLvskAGIiasaragetrFTDTRKDEQERCITIK----STAISMYYELTENDLAFIK----QC 92
Cdd:PRK04000  11 NIGMVGHVDHGKTTLVQAL---TGV----------WTDRHSEELKRGITIRlgyaDATIRKCPDCEEPEAYTTEpkcpNC 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 41386743   93 KDGSGFL--INLIDSPGHvdfssEVT-------AALrvTDGALVVVD 130
Cdd:PRK04000  78 GSETELLrrVSFVDAPGH-----ETLmatmlsgAAL--MDGAILVIA 117
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
27-161 1.05e-05

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: 47.18  E-value: 1.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  27 HVDHGKSTLTDSLV--SK-------AGIIASARAGETR-------FTDTRKDEQERCITIkstaismyyeltenDLAFIK 90
Cdd:cd04166   7 SVDDGKSTLIGRLLydSKsifedqlAALERSKSSGTQGekldlalLVDGLQAEREQGITI--------------DVAYRY 72
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41386743  91 QCKDGSGFLInlIDSPGHVDFSSE-VTAALRvTDGALVVVDCVSGVCVQTEtvlRQA-IAE--RIKP-VLMMNKMD 161
Cdd:cd04166  73 FSTPKRKFII--ADTPGHEQYTRNmVTGAST-ADLAILLVDARKGVLEQTR---RHSyIASllGIRHvVVAVNKMD 142
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
24-162 1.27e-05

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: 46.30  E-value: 1.27e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  24 VIAHVDHGKSTLTDSLVSKAGIIASARAGETRftdtrkDEQERCITIkstaismyyeltendlafikqckDGSGFLINLI 103
Cdd:cd00882   2 VVGRGGVGKSSLLNALLGGEVGEVSDVPGTTR------DPDVYVKEL-----------------------DKGKVKLVLV 52
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41386743 104 DSPGHVDFS-----SEVTAALRVTDGALVVVDCVSGVCV--QTETVLRQAIAERIKPVLMMNKMDR 162
Cdd:cd00882  53 DTPGLDEFGglgreELARLLLRGADLILLVVDSTDRESEedAKLLILRRLRKEGIPIILVGNKIDL 118
PRK00049 PRK00049
elongation factor Tu; Reviewed
21-161 1.36e-05

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 48.26  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   21 NMSVIAHVDHGKSTLTDSL---VSKAGiIASARAGETrfTDTRKDEQERCITIkSTAiSMYYElTEN-DLAFikqckdgs 96
Cdd:PRK00049  14 NVGTIGHVDHGKTTLTAAItkvLAKKG-GAEAKAYDQ--IDKAPEEKARGITI-NTA-HVEYE-TEKrHYAH-------- 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41386743   97 gflinlIDSPGHVDF-SSEVTAALRVtDGALVVVDCVSGVCVQT-ETVL--RQAIAERIkpVLMMNKMD 161
Cdd:PRK00049  80 ------VDCPGHADYvKNMITGAAQM-DGAILVVSAADGPMPQTrEHILlaRQVGVPYI--VVFLNKCD 139
aIF-2 TIGR00491
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ...
22-162 2.05e-05

translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic orthologs of bacterial IF-2. Like IF-2, it helps convey the initiator tRNA to the ribosome, although the initiator is N-formyl-Met in bacteria and Met here. This protein is not closely related to the subunits of eIF-2 of eukaryotes, which is also involved in the initiation of translation. The aIF-2 of Methanococcus jannaschii contains a large intein interrupting a region of very strongly conserved sequence very near the amino end; the alignment generated by this model does not correctly align the sequences from Methanococcus jannaschii and Pyrococcus horikoshii in this region. [Protein synthesis, Translation factors]


Pssm-ID: 273104 [Multi-domain]  Cd Length: 591  Bit Score: 48.27  E-value: 2.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743    22 MSVIAHVDHGKSTLTDSLVSKAgiIASARAGEtrftdtrkdeqercitikstaISMYYELTENDLAFIKQ-CKD-GSGFL 99
Cdd:TIGR00491   7 VVVLGHVDHGKTTLLDKIRGTA--VVKKEAGG---------------------ITQHIGASEVPTDVIEKiCGDlLKSFK 63
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   100 INL-------IDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDR 162
Cdd:TIGR00491  64 IKLkipgllfIDTPGHEAFTNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTPFVVAANKIDR 133
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
27-139 3.89e-05

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 47.35  E-value: 3.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   27 HVDHGKSTLTDSLvskAGIIAsaragetrftDTRKDEQERCITIkstaismyyeltenDL--AFIKQcKDGSgfLINLID 104
Cdd:PRK10512   8 HVDHGKTTLLQAI---TGVNA----------DRLPEEKKRGMTI--------------DLgyAYWPQ-PDGR--VLGFID 57
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 41386743  105 SPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQT 139
Cdd:PRK10512  58 VPGHEKFLSNMLAGVGGIDHALLVVACDDGVMAQT 92
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
31-159 4.38e-05

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: 43.38  E-value: 4.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743    31 GKSTLTDSLVSKAGIIaSARAGETRftdtrkDEQERCITIKstaismyyeltendlafikqckdgsGFLINLIDSPGHVD 110
Cdd:pfam01926  11 GKSTLINALTGAKAIV-SDYPGTTR------DPNEGRLELK-------------------------GKQIILVDTPGLIE 58
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 41386743   111 FSSE------VTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNK 159
Cdd:pfam01926  59 GASEgeglgrAFLAIIEADLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
13-134 1.01e-04

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 45.85  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743   13 MDKKSNIRNMSVIAHVDHGKSTLTDSLVSKAGII----------ASARAGETRFT-----DTRKDEQERCITIkstaism 77
Cdd:PLN00043   1 MGKEKVHINIVVIGHVDSGKSTTTGHLIYKLGGIdkrvierfekEAAEMNKRSFKyawvlDKLKAERERGITI------- 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 41386743   78 yyeltenDLAFIKqcKDGSGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSG 134
Cdd:PLN00043  74 -------DIALWK--FETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTG 121
GCD11 COG5257
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ...
21-130 3.64e-03

Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal structure and biogenesis]; Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 444075 [Multi-domain]  Cd Length: 408  Bit Score: 40.59  E-value: 3.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386743  21 NMSVIAHVDHGKSTLTDSLvskAGIiasaragetrFTDTRKDEQERCITIK---STAISMYYELTENDLAFI-----KQC 92
Cdd:COG5257   7 NIGVVGHVDHGKTTLVQAL---TGV----------WTDRHSEELKRGITIRlgyADATFYKCPNCEPPEAYTtepkcPNC 73
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 41386743  93 KDGSGFL--INLIDSPGHvdfssEVT-------AALrvTDGALVVVD 130
Cdd:COG5257  74 GSETELLrrVSFVDAPGH-----ETLmatmlsgAAL--MDGAILVIA 113
 
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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