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Conserved domains on  [gi|1017207214|ref|NP_001309773|]
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elongation factor-like GTPase 1 isoform 3 [Homo sapiens]

Protein Classification

elongation factor 2 family protein( domain architecture ID 999991)

elongation factor 2 (EF-2) family protein simmilar to EF-2 that catalyzes the GTP-dependent ribosomal translocation step during translation elongation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13351 super family cl46912
elongation factor G-like protein;
1-840 6.11e-123

elongation factor G-like protein;


The actual alignment was detected with superfamily member PTZ00416:

Pssm-ID: 481252 [Multi-domain]  Cd Length: 836  Bit Score: 390.95  E-value: 6.11e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214   1 MKTLWGDYYINMKAKKIMK---GDQAKGKKPLFVQLILENIWSLYDAVLKKDKDKIDKIVTSLGLKIGArEARHSDPKVQ 77
Cdd:PTZ00416  235 MERLWGDNFFDAKTKKWIKdetNAQGKKLKRAFCQFILDPICQLFDAVMNEDKEKYDKMLKSLNISLTG-EDKELTGKPL 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214  78 INAICSQWLPISHAVLAMVCQKLPSPLDITAERVERLMcTGsqtfdsfpPETQALKAAFMKCGSEdtAPVIIFVSKMFav 157
Cdd:PTZ00416  314 LKAVMQKWLPAADTLLEMIVDHLPSPKEAQKYRVENLY-EG--------PMDDEAANAIRNCDPN--GPLMMYISKMV-- 380

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 158 dakalpqnkprpltqeeiaqrrerarqrhaeklaaaqgqaplePTQDgsaietcpKGEeprgdeqqvesmtpkpvlqeen 237
Cdd:PTZ00416  381 -------------------------------------------PTSD--------KGR---------------------- 387

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 238 nqesFIAFARVFSGVARRGKKIFVLGPKYSPLEflrrvplgfsapPDGLPQVPhmaycaLENLYLLMGRELEYLEEVPPG 317
Cdd:PTZ00416  388 ----FYAFGRVFSGTVATGQKVRIQGPNYVPGK------------KEDLFEKN------IQRTVLMMGRYVEQIEDVPCG 445

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 318 NVLGIGGLQDFVLKSATLCSLPSCPPFIPLNFEATPIVRVAVEPKHPSEMPQLVKGMKLLNQADPCVQILIQETGEHVLV 397
Cdd:PTZ00416  446 NTVGLVGVDQYLVKSGTITTSETAHNIRDMKYSVSPVVRVAVEPKNPKDLPKLVEGLKRLAKSDPLVVCTTEESGEHIVA 525

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 398 TAGEVHLQRCLDDLKERFAKIHISVSEPIIPFRETITkppkvdmvneEIGKQQKVAvihqmkedqskipegiqvdsdgli 477
Cdd:PTZ00416  526 GCGELHVEICLKDLEDDYANIDIIVSDPVVSYRETVT----------EESSQTCLS------------------------ 571

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 478 tiTTPNKLATLSVRAMPLPEEVTQILEENsdlirsmeQLTSSLNEGENTHMIHQKTQekiWEfkgkleqhltgrrwRNIV 557
Cdd:PTZ00416  572 --KSPNKHNRLYMKAEPLTEELAEAIEEG--------KVGPEDDPKERANFLADKYE---WD--------------KNDA 624

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 558 DQIWSFGPRKCGPNILVNKSEDFQNSvwtgpadKASKEasryrdlgnSIVSGFQLATLSGPMCEEPLMGVCFVLEKWDLS 637
Cdd:PTZ00416  625 RKIWCFGPENKGPNVLVDVTKGVQYM-------NEIKD---------SCVSAFQWATKEGVLCDENMRGIRFNILDVTLH 688

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 638 kfeeqgaSDLAKEGqeenetcsggnenqelqdgcseafekrtsqkgespltdcygpfSGQLIATMKEaCRYALQVKPQ-R 716
Cdd:PTZ00416  689 -------ADAIHRG-------------------------------------------AGQIIPTARR-VFYACELTASpR 717

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 717 LMAAMYTCDIMATGDVLGRVYAVLSKREGRVLQEEMKEGTDMFIIKAVLPVAESFGFADEIRKRTSGLASPQLVFSHWEI 796
Cdd:PTZ00416  718 LLEPMFLVDITAPEDAMGGIYSVLNRRRGVVIGEEQRPGTPLSNIKAYLPVAESFGFTAALRAATSGQAFPQCVFDHWQV 797

                         810       820       830       840
                  ....*....|....*....|....*....|....*....|....
gi 1017207214 797 IPSDPFwvptteeeylhfgekaDSENQARKYMNAVRKRKGLYVE 840
Cdd:PTZ00416  798 VPGDPL----------------EPGSKANEIVLSIRKRKGLKPE 825
 
Name Accession Description Interval E-value
PTZ00416 PTZ00416
elongation factor 2; Provisional
 1-840 6.11e-123

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 390.95  E-value: 6.11e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214   1 MKTLWGDYYINMKAKKIMK---GDQAKGKKPLFVQLILENIWSLYDAVLKKDKDKIDKIVTSLGLKIGArEARHSDPKVQ 77
Cdd:PTZ00416  235 MERLWGDNFFDAKTKKWIKdetNAQGKKLKRAFCQFILDPICQLFDAVMNEDKEKYDKMLKSLNISLTG-EDKELTGKPL 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214  78 INAICSQWLPISHAVLAMVCQKLPSPLDITAERVERLMcTGsqtfdsfpPETQALKAAFMKCGSEdtAPVIIFVSKMFav 157
Cdd:PTZ00416  314 LKAVMQKWLPAADTLLEMIVDHLPSPKEAQKYRVENLY-EG--------PMDDEAANAIRNCDPN--GPLMMYISKMV-- 380

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 158 dakalpqnkprpltqeeiaqrrerarqrhaeklaaaqgqaplePTQDgsaietcpKGEeprgdeqqvesmtpkpvlqeen 237
Cdd:PTZ00416  381 -------------------------------------------PTSD--------KGR---------------------- 387

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 238 nqesFIAFARVFSGVARRGKKIFVLGPKYSPLEflrrvplgfsapPDGLPQVPhmaycaLENLYLLMGRELEYLEEVPPG 317
Cdd:PTZ00416  388 ----FYAFGRVFSGTVATGQKVRIQGPNYVPGK------------KEDLFEKN------IQRTVLMMGRYVEQIEDVPCG 445

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 318 NVLGIGGLQDFVLKSATLCSLPSCPPFIPLNFEATPIVRVAVEPKHPSEMPQLVKGMKLLNQADPCVQILIQETGEHVLV 397
Cdd:PTZ00416  446 NTVGLVGVDQYLVKSGTITTSETAHNIRDMKYSVSPVVRVAVEPKNPKDLPKLVEGLKRLAKSDPLVVCTTEESGEHIVA 525

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 398 TAGEVHLQRCLDDLKERFAKIHISVSEPIIPFRETITkppkvdmvneEIGKQQKVAvihqmkedqskipegiqvdsdgli 477
Cdd:PTZ00416  526 GCGELHVEICLKDLEDDYANIDIIVSDPVVSYRETVT----------EESSQTCLS------------------------ 571

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 478 tiTTPNKLATLSVRAMPLPEEVTQILEENsdlirsmeQLTSSLNEGENTHMIHQKTQekiWEfkgkleqhltgrrwRNIV 557
Cdd:PTZ00416  572 --KSPNKHNRLYMKAEPLTEELAEAIEEG--------KVGPEDDPKERANFLADKYE---WD--------------KNDA 624

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 558 DQIWSFGPRKCGPNILVNKSEDFQNSvwtgpadKASKEasryrdlgnSIVSGFQLATLSGPMCEEPLMGVCFVLEKWDLS 637
Cdd:PTZ00416  625 RKIWCFGPENKGPNVLVDVTKGVQYM-------NEIKD---------SCVSAFQWATKEGVLCDENMRGIRFNILDVTLH 688

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 638 kfeeqgaSDLAKEGqeenetcsggnenqelqdgcseafekrtsqkgespltdcygpfSGQLIATMKEaCRYALQVKPQ-R 716
Cdd:PTZ00416  689 -------ADAIHRG-------------------------------------------AGQIIPTARR-VFYACELTASpR 717

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 717 LMAAMYTCDIMATGDVLGRVYAVLSKREGRVLQEEMKEGTDMFIIKAVLPVAESFGFADEIRKRTSGLASPQLVFSHWEI 796
Cdd:PTZ00416  718 LLEPMFLVDITAPEDAMGGIYSVLNRRRGVVIGEEQRPGTPLSNIKAYLPVAESFGFTAALRAATSGQAFPQCVFDHWQV 797

                         810       820       830       840
                  ....*....|....*....|....*....|....*....|....
gi 1017207214 797 IPSDPFwvptteeeylhfgekaDSENQARKYMNAVRKRKGLYVE 840
Cdd:PTZ00416  798 VPGDPL----------------EPGSKANEIVLSIRKRKGLKPE 825
aeEF2_snRNP_like_IV cd01681
This family represents domain IV of archaeal and eukaryotic elongation factor 2 (aeEF-2) and ...
 424-723 5.87e-51

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: 176.61  E-value: 5.87e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 424 EPIIPFRETITKPpkvdmvneeigkqqkvavihqmkedqskipegiqvdSDGLITITTPNKLATLSVRAMPLPEEVTQIL 503
Cdd:cd01681     1 DPVVSFRETVVET------------------------------------SSGTCLAKSPNKHNRLYMRAEPLPEELIEDI 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 504 EENSDLIRsmeqltsslnegenthmihqktqekiWEFKGKLEQHLTGRRW-RNIVDQIWSFGPRKCGPNILVNKSEDFQN 582
Cdd:cd01681    45 EKGKITLK--------------------------DDKKKRARILLDKYGWdKLAARKIWAFGPDRTGPNILVDDTKGVQY 98

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 583 SVwtgpadkaskeaSRYRDLGNSIVSGFQLATLSGPMCEEPLMGVCFVLEKWDLSkfeeqgasdlakegqeenetcsggn 662
Cdd:cd01681    99 DK------------SLLNEIKDSIVAGFQWATKEGPLCEEPMRGVKFKLEDATLH------------------------- 141

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1017207214 663 enqelqdgcseafekrtsqkgesplTDCYGPFSGQLIATMKEACRYALQVKPQRLMAAMYT 723
Cdd:cd01681   142 -------------------------ADAIHRGGGQIIPAARRACYAAFLLASPRLMEPMYL 177
EFG_C smart00838
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ...
 717-802 1.86e-20

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: 86.40  E-value: 1.86e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214  717 LMAAMYTCDIMATGDVLGRVYAVLSKREGRVlqEEMKEGTDMFIIKAVLPVAESFGFADEIRKRTSGLASPQLVFSHWEI 796
Cdd:smart00838   1 LLEPIMKVEVTVPEEYMGDVIGDLNSRRGKI--EGMEQRGGAQVIKAKVPLSEMFGYATDLRSATQGRATWSMEFSHYEE 78


                   ....*.
gi 1017207214  797 IPSDPF 802
Cdd:smart00838  79 VPKSIA 84
EFG_C pfam00679
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ...
 716-802 3.13e-20

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: 85.68  E-value: 3.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 716 RLMAAMYTCDIMATGDVLGRVYAVLSKREGRVlQEEMKEGTDMFIIKAVLPVAESFGFADEIRKRTSGLASPQLVFSHWE 795
Cdd:pfam00679   1 VLLEPIEKVTIDVPEEYVGDVISDLNSRRGEI-LDMDPDDGGRVVIEAEVPLAELFGFATELRSLTKGRGSFSMEFSGYQ 79


                  ....*..
gi 1017207214 796 IIPSDPF 802
Cdd:pfam00679  80 PVPGDIL 86
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 300-440 1.13e-13

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: 75.08  E-value: 1.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 300 LYLLMGRELEYLEEVPPGNVLGIGGLQDfVLKSATLCSlPSCP-PFIPLNFeATPIVRVAVEPKHPSEMPQLVKGMKLLN 378
Cdd:COG0480   353 LLRMHGNKREEVDEAGAGDIVAVVKLKD-TTTGDTLCD-EDHPiVLEPIEF-PEPVISVAIEPKTKADEDKLSTALAKLA 429

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1017207214 379 QADPCVQILI-QETGEHVLVTAGEVHLQRCLDDLKERFaKIHISVSEPIIPFRETITKPPKVD 440
Cdd:COG0480   430 EEDPTFRVETdEETGQTIISGMGELHLEIIVDRLKREF-GVEVNVGKPQVAYRETIRKKAEAE 491
 
Name Accession Description Interval E-value
PTZ00416 PTZ00416
elongation factor 2; Provisional
 1-840 6.11e-123

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 390.95  E-value: 6.11e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214   1 MKTLWGDYYINMKAKKIMK---GDQAKGKKPLFVQLILENIWSLYDAVLKKDKDKIDKIVTSLGLKIGArEARHSDPKVQ 77
Cdd:PTZ00416  235 MERLWGDNFFDAKTKKWIKdetNAQGKKLKRAFCQFILDPICQLFDAVMNEDKEKYDKMLKSLNISLTG-EDKELTGKPL 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214  78 INAICSQWLPISHAVLAMVCQKLPSPLDITAERVERLMcTGsqtfdsfpPETQALKAAFMKCGSEdtAPVIIFVSKMFav 157
Cdd:PTZ00416  314 LKAVMQKWLPAADTLLEMIVDHLPSPKEAQKYRVENLY-EG--------PMDDEAANAIRNCDPN--GPLMMYISKMV-- 380

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 158 dakalpqnkprpltqeeiaqrrerarqrhaeklaaaqgqaplePTQDgsaietcpKGEeprgdeqqvesmtpkpvlqeen 237
Cdd:PTZ00416  381 -------------------------------------------PTSD--------KGR---------------------- 387

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 238 nqesFIAFARVFSGVARRGKKIFVLGPKYSPLEflrrvplgfsapPDGLPQVPhmaycaLENLYLLMGRELEYLEEVPPG 317
Cdd:PTZ00416  388 ----FYAFGRVFSGTVATGQKVRIQGPNYVPGK------------KEDLFEKN------IQRTVLMMGRYVEQIEDVPCG 445

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 318 NVLGIGGLQDFVLKSATLCSLPSCPPFIPLNFEATPIVRVAVEPKHPSEMPQLVKGMKLLNQADPCVQILIQETGEHVLV 397
Cdd:PTZ00416  446 NTVGLVGVDQYLVKSGTITTSETAHNIRDMKYSVSPVVRVAVEPKNPKDLPKLVEGLKRLAKSDPLVVCTTEESGEHIVA 525

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 398 TAGEVHLQRCLDDLKERFAKIHISVSEPIIPFRETITkppkvdmvneEIGKQQKVAvihqmkedqskipegiqvdsdgli 477
Cdd:PTZ00416  526 GCGELHVEICLKDLEDDYANIDIIVSDPVVSYRETVT----------EESSQTCLS------------------------ 571

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 478 tiTTPNKLATLSVRAMPLPEEVTQILEENsdlirsmeQLTSSLNEGENTHMIHQKTQekiWEfkgkleqhltgrrwRNIV 557
Cdd:PTZ00416  572 --KSPNKHNRLYMKAEPLTEELAEAIEEG--------KVGPEDDPKERANFLADKYE---WD--------------KNDA 624

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 558 DQIWSFGPRKCGPNILVNKSEDFQNSvwtgpadKASKEasryrdlgnSIVSGFQLATLSGPMCEEPLMGVCFVLEKWDLS 637
Cdd:PTZ00416  625 RKIWCFGPENKGPNVLVDVTKGVQYM-------NEIKD---------SCVSAFQWATKEGVLCDENMRGIRFNILDVTLH 688

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 638 kfeeqgaSDLAKEGqeenetcsggnenqelqdgcseafekrtsqkgespltdcygpfSGQLIATMKEaCRYALQVKPQ-R 716
Cdd:PTZ00416  689 -------ADAIHRG-------------------------------------------AGQIIPTARR-VFYACELTASpR 717

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 717 LMAAMYTCDIMATGDVLGRVYAVLSKREGRVLQEEMKEGTDMFIIKAVLPVAESFGFADEIRKRTSGLASPQLVFSHWEI 796
Cdd:PTZ00416  718 LLEPMFLVDITAPEDAMGGIYSVLNRRRGVVIGEEQRPGTPLSNIKAYLPVAESFGFTAALRAATSGQAFPQCVFDHWQV 797

                         810       820       830       840
                  ....*....|....*....|....*....|....*....|....
gi 1017207214 797 IPSDPFwvptteeeylhfgekaDSENQARKYMNAVRKRKGLYVE 840
Cdd:PTZ00416  798 VPGDPL----------------EPGSKANEIVLSIRKRKGLKPE 825
PLN00116 PLN00116
translation elongation factor EF-2 subunit; Provisional
 1-837 6.87e-94

translation elongation factor EF-2 subunit; Provisional


Pssm-ID: 177730 [Multi-domain]  Cd Length: 843  Bit Score: 313.58  E-value: 6.87e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214   1 MKTLWGDYYINMKAKKIMKGDQAKGK-KPLFVQLILENIWSLYDAVLKKDKDKIDKIVTSLGLKIGAREARHSDpKVQIN 79
Cdd:PLN00116  241 MERLWGENFFDPATKKWTTKNTGSPTcKRGFVQFCYEPIKQIINTCMNDQKDKLWPMLEKLGVTLKSDEKELMG-KALMK 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214  80 AICSQWLPISHAVLAMVCQKLPSPLDITAERVERLmctgsqtFDSfpPETQALKAAFMKCGSEdtAPVIIFVSKMFavda 159
Cdd:PLN00116  320 RVMQTWLPASDALLEMIIFHLPSPAKAQRYRVENL-------YEG--PLDDKYATAIRNCDPN--GPLMLYVSKMI---- 384

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 160 kalpqnkprpltqeeiaqrrerarqrhaeklaaaqgqaplePTQDgsaietcpKGEeprgdeqqvesmtpkpvlqeennq 239
Cdd:PLN00116  385 -----------------------------------------PASD--------KGR------------------------ 391

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 240 esFIAFARVFSGVARRGKKIFVLGPKYSPLE----FLRRVplgfsappdglpqvphmaycalENLYLLMGRELEYLEEVP 315
Cdd:PLN00116  392 --FFAFGRVFSGTVATGMKVRIMGPNYVPGEkkdlYVKSV----------------------QRTVIWMGKKQESVEDVP 447

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 316 PGNVLGIGGLQDFVLKSATLC--SLPSCPPFIPLNFEATPIVRVAVEPKHPSEMPQLVKGMKLLNQADPCVQILIQETGE 393
Cdd:PLN00116  448 CGNTVAMVGLDQFITKNATLTneKEVDAHPIKAMKFSVSPVVRVAVQCKNASDLPKLVEGLKRLAKSDPMVQCTIEESGE 527

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 394 HVLVTAGEVHLQRCLDDLKERF-AKIHISVSEPIIPFRETitkppkvdmVNEEigkqqkvavihqmkedqskipegiqvd 472
Cdd:PLN00116  528 HIIAGAGELHLEICLKDLQDDFmGGAEIKVSDPVVSFRET---------VLEK--------------------------- 571

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 473 SDGLITITTPNKLATLSVRAMPLPEEvtqileensdlirsmeqLTSSLNEGENTHMIHQKTQEKIW--EFKgkleqhltg 550
Cdd:PLN00116  572 SCRTVMSKSPNKHNRLYMEARPLEEG-----------------LAEAIDDGRIGPRDDPKIRSKILaeEFG--------- 625

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 551 rrW-RNIVDQIWSFGPRKCGPNILVNKSEDFQnsvwtgpadkaskeasrYRD-LGNSIVSGFQLATLSGPMCEEPLMGVC 628
Cdd:PLN00116  626 --WdKDLAKKIWCFGPETTGPNMVVDMCKGVQ-----------------YLNeIKDSVVAGFQWATKEGALAEENMRGIC 686

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 629 FVLEKWDLSkfeeqgaSDLAKEGqeenetcsggnenqelqdgcseafekrtsqkgespltdcygpfSGQLIATMKEACrY 708
Cdd:PLN00116  687 FEVCDVVLH-------ADAIHRG-------------------------------------------GGQIIPTARRVI-Y 715

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 709 ALQV--KPqRLMAAMYTCDIMATGDVLGRVYAVLSKREGRVLQEEMKEGTDMFIIKAVLPVAESFGFADEIRKRTSGLAS 786
Cdd:PLN00116  716 ASQLtaKP-RLLEPVYLVEIQAPEQALGGIYSVLNQKRGHVFEEMQRPGTPLYNIKAYLPVIESFGFSGTLRAATSGQAF 794

                         810       820       830       840       850
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1017207214 787 PQLVFSHWEIIPSDPFwvptteeeylhfgekaDSENQARKYMNAVRKRKGL 837
Cdd:PLN00116  795 PQCVFDHWDMMSSDPL----------------EAGSQAAQLVADIRKRKGL 829
aeEF2_snRNP_like_IV cd01681
This family represents domain IV of archaeal and eukaryotic elongation factor 2 (aeEF-2) and ...
 424-723 5.87e-51

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: 176.61  E-value: 5.87e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 424 EPIIPFRETITKPpkvdmvneeigkqqkvavihqmkedqskipegiqvdSDGLITITTPNKLATLSVRAMPLPEEVTQIL 503
Cdd:cd01681     1 DPVVSFRETVVET------------------------------------SSGTCLAKSPNKHNRLYMRAEPLPEELIEDI 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 504 EENSDLIRsmeqltsslnegenthmihqktqekiWEFKGKLEQHLTGRRW-RNIVDQIWSFGPRKCGPNILVNKSEDFQN 582
Cdd:cd01681    45 EKGKITLK--------------------------DDKKKRARILLDKYGWdKLAARKIWAFGPDRTGPNILVDDTKGVQY 98

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 583 SVwtgpadkaskeaSRYRDLGNSIVSGFQLATLSGPMCEEPLMGVCFVLEKWDLSkfeeqgasdlakegqeenetcsggn 662
Cdd:cd01681    99 DK------------SLLNEIKDSIVAGFQWATKEGPLCEEPMRGVKFKLEDATLH------------------------- 141

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1017207214 663 enqelqdgcseafekrtsqkgesplTDCYGPFSGQLIATMKEACRYALQVKPQRLMAAMYT 723
Cdd:cd01681   142 -------------------------ADAIHRGGGQIIPAARRACYAAFLLASPRLMEPMYL 177
PRK07560 PRK07560
elongation factor EF-2; Reviewed
 243-846 3.99e-47

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 180.06  E-value: 3.99e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 243 IAFARVFSGVARRGKKIFVLGpkyspleflrrvplgfSAPPDGLPQVphmaycalenlYLLMGRELEYLEEVPPGNVLGI 322
Cdd:PRK07560  307 VATGRVFSGTLRKGQEVYLVG----------------AKKKNRVQQV-----------GIYMGPEREEVEEIPAGNIAAV 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 323 GGLQDFVLKSaTLCSLPSCPPFIPLNFEATPIVRVAVEPKHPSEMPQLVKGMKLLNQADPCVQILI-QETGEHVLVTAGE 401
Cdd:PRK07560  360 TGLKDARAGE-TVVSVEDMTPFESLKHISEPVVTVAIEAKNPKDLPKLIEVLRQLAKEDPTLVVKInEETGEHLLSGMGE 438

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 402 VHLQRCLDDLKERFaKIHISVSEPIIPFRETITKppkvdmvneeigkqqkvavihqmkedQSKIPEGIqvdsdglititT 481
Cdd:PRK07560  439 LHLEVITYRIKRDY-GIEVVTSEPIVVYRETVRG--------------------------KSQVVEGK-----------S 480

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 482 PNKLATLSVRAMPLPEEVTqileensDLIRsmeqltsslnEGEnthmIHQKTQEKiwEFKgKLEQHLTGRRW-RNIVDQI 560
Cdd:PRK07560  481 PNKHNRFYISVEPLEEEVI-------EAIK----------EGE----ISEDMDKK--EAK-ILREKLIEAGMdKDEAKRV 536

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 561 WSFgprkCGPNILVNKSEDFQ--NSVwtgpadkaskeasryRDLgnsIVSGFQLATLSGPMCEEPLMGVCFVLekWDlSK 638
Cdd:PRK07560  537 WAI----YNGNVFIDMTKGIQylNEV---------------MEL---IIEGFREAMKEGPLAAEPVRGVKVRL--HD-AK 591

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 639 FEEQGAsdlakegqeenetcsggnenqelqdgcseafeKRtsqkgespltdcyGPfsGQLIATMKEACRYA-LQVKPqRL 717
Cdd:PRK07560  592 LHEDAI--------------------------------HR-------------GP--AQVIPAVRNAIFAAmLTAKP-TL 623

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 718 MAAMYTCDIMATGDVLGRVYAVLSKREGRVLqeEMKEGTDMFIIKAVLPVAESFGFADEIRKRTSGLASPQLVFSHWEII 797
Cdd:PRK07560  624 LEPIQKVDINVPQDYMGAVTREIQGRRGKIL--DMEQEGDMAIIEAEAPVAEMFGFAGEIRSATEGRALWSTEFAGFEPV 701

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*....
gi 1017207214 798 PsdpfwvptteeeylhfgekadsENQARKYMNAVRKRKGLYVEEKIVEH 846
Cdd:PRK07560  702 P----------------------DSLQLDIVRQIRERKGLKPELPKPED 728
eEF2_snRNP_like_C cd04096
eEF2_snRNP_like_C: this family represents a C-terminal domain of eukaryotic elongation factor ...
 720-798 3.08e-42

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: 148.07  E-value: 3.08e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1017207214 720 AMYTCDIMATGDVLGRVYAVLSKREGRVLQEEMKEGTDMFIIKAVLPVAESFGFADEIRKRTSGLASPQLVFSHWEIIP 798
Cdd:cd04096     2 PIYLVEIQCPEDALGKVYSVLSKRRGHVLSEEPKEGTPLFEIKAYLPVIESFGFETDLRSATSGQAFPQLVFSHWEIVP 80
EF2_snRNP_III cd16261
Domain III of Elongation Factor 2 (EF2); This model represents domain III of Elongation factor ...
 353-424 7.28e-36

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: 129.61  E-value: 7.28e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1017207214 353 PIVRVAVEPKHPSEMPQLVKGMKLLNQADPCVQILIQETGEHVLVTAGEVHLQRCLDDLKERFAKIHISVSE 424
Cdd:cd16261     1 PVVRVAVEPKNPSDLPKLVEGLKKLAKSDPTVQVKIEEEGEHLIAGAGELHLEICLKDLKEDFAGIEIKVSD 72
EF2_II cd16268
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 ...
 239-337 1.98e-29

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: 112.31  E-value: 1.98e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 239 QESFIAFARVFSGVARRGKKIFVLGPKYSPleflrrvplgfsappdglPQVPHMAYCALENLYLLMGRELEYLEEVPPGN 318
Cdd:cd16268    15 GAGFVAFGRVFSGTVRRGQEVYILGPKYVP------------------GKKDDLKKKRIQQTYLMMGREREPVDEVPAGN 76

                          90
                  ....*....|....*....
gi 1017207214 319 VLGIGGLQDFVLKSATLCS 337
Cdd:cd16268    77 IVGLVGLDDFLAKSGTTTS 95
Elongation_Factor_C cd01514
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ...
 721-798 4.78e-25

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: 99.09  E-value: 4.78e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1017207214 721 MYTCDIMATGDVLGRVYAVLSKREGRVLQEEMKeGTDMFIIKAVLPVAESFGFADEIRKRTSGLASPQLVFSHWEIIP 798
Cdd:cd01514     3 IMKVEITVPEEYLGAVIGDLSKRRGEILGMEPR-GTGRVVIKAELPLAEMFGFATDLRSLTQGRASFSMEFSHYEPVP 79
EFG_C smart00838
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ...
 717-802 1.86e-20

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: 86.40  E-value: 1.86e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214  717 LMAAMYTCDIMATGDVLGRVYAVLSKREGRVlqEEMKEGTDMFIIKAVLPVAESFGFADEIRKRTSGLASPQLVFSHWEI 796
Cdd:smart00838   1 LLEPIMKVEVTVPEEYMGDVIGDLNSRRGKI--EGMEQRGGAQVIKAKVPLSEMFGYATDLRSATQGRATWSMEFSHYEE 78


                   ....*.
gi 1017207214  797 IPSDPF 802
Cdd:smart00838  79 VPKSIA 84
EFG_C pfam00679
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ...
 716-802 3.13e-20

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: 85.68  E-value: 3.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 716 RLMAAMYTCDIMATGDVLGRVYAVLSKREGRVlQEEMKEGTDMFIIKAVLPVAESFGFADEIRKRTSGLASPQLVFSHWE 795
Cdd:pfam00679   1 VLLEPIEKVTIDVPEEYVGDVISDLNSRRGEI-LDMDPDDGGRVVIEAEVPLAELFGFATELRSLTKGRGSFSMEFSGYQ 79


                  ....*..
gi 1017207214 796 IIPSDPF 802
Cdd:pfam00679  80 PVPGDIL 86
eEF2_C_snRNP cd04098
eEF2_C_snRNP: This family includes a C-terminal portion of the spliceosomal human 116kD U5 ...
 721-798 7.52e-19

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: 81.52  E-value: 7.52e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1017207214 721 MYTCDIMATGDVLGRVYAVLSKREGRVLQEEMKEGTDMFIIKAVLPVAESFGFADEIRKRTSGLASPQLVFSHWEIIP 798
Cdd:cd04098     3 IYEVEITCPADAVSAVYEVLSRRRGHVIYDTPIPGTPLYEVKAFIPVIESFGFETDLRVHTQGQAFCQSVFDHWQIVP 80
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
243-440 6.89e-16

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 82.10  E-value: 6.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 243 IAFARVFSGVARRGKKIFVLGpkyspleflRRVPLGFSAppdglpqvphmaycalenLYLLMGRELEYLEEVPPGNVLGI 322
Cdd:PRK12740  305 LSLVRVYSGTLKKGDTLYNSG---------TGKKERVGR------------------LYRMHGKQREEVDEAVAGDIVAV 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 323 GGLQDfVLKSATLCSlPSCP-PFIPLNFeATPIVRVAVEPKHPSEMPQLVKGMKLLNQADPCVQILI-QETGEHVLVTAG 400
Cdd:PRK12740  358 AKLKD-AATGDTLCD-KGDPiLLEPMEF-PEPVISLAIEPKDKGDEEKLSEALGKLAEEDPTLRVERdEETGQTILSGMG 434

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1017207214 401 EVHLQRCLDDLKERFaKIHISVSEPIIPFRETITKPPKVD 440
Cdd:PRK12740  435 ELHLDVALERLKREY-GVEVETGPPQVPYRETIRKKAEGH 473
PRK13351 PRK13351
elongation factor G-like protein;
243-436 8.75e-14

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 75.37  E-value: 8.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 243 IAFARVFSGVARRGKKIFVLGPKyspleflRRVPLGfsappdglpqvphmaycaleNLYLLMGRELEYLEEVPPGNVLGI 322
Cdd:PRK13351  322 LTYLRVYSGTLRAGSQLYNGTGG-------KREKVG--------------------RLFRLQGNKREEVDRAKAGDIVAV 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 323 GGLqDFVLKSATLCSLPSCPPFIPLNFeATPIVRVAVEPKHPSEMPQLVKGMKLLNQADPCVQILI-QETGEHVLVTAGE 401
Cdd:PRK13351  375 AGL-KELETGDTLHDSADPVLLELLTF-PEPVVSLAVEPERRGDEQKLAEALEKLVWEDPSLRVEEdEETGQTILSGMGE 452

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1017207214 402 VHLQRCLDDLKERFaKIHISVSEPIIPFRETITKP 436
Cdd:PRK13351  453 LHLEVALERLRREF-KLEVNTGKPQVAYRETIRKM 486
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 300-440 1.13e-13

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: 75.08  E-value: 1.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 300 LYLLMGRELEYLEEVPPGNVLGIGGLQDfVLKSATLCSlPSCP-PFIPLNFeATPIVRVAVEPKHPSEMPQLVKGMKLLN 378
Cdd:COG0480   353 LLRMHGNKREEVDEAGAGDIVAVVKLKD-TTTGDTLCD-EDHPiVLEPIEF-PEPVISVAIEPKTKADEDKLSTALAKLA 429

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1017207214 379 QADPCVQILI-QETGEHVLVTAGEVHLQRCLDDLKERFaKIHISVSEPIIPFRETITKPPKVD 440
Cdd:COG0480   430 EEDPTFRVETdEETGQTIISGMGELHLEIIVDRLKREF-GVEVNVGKPQVAYRETIRKKAEAE 491
snRNP_III cd16264
Domain III of the spliceosomal 116kD U5 small nuclear ribonucleoprotein (snRNP) component; ...
 353-424 6.70e-13

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: 64.44  E-value: 6.70e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1017207214 353 PIVRVAVEPKHPSEMPQLVKGMKLLNQADPCVQILIQETGEHVLVTAGEVHLQRCLDDLKERFAKIHISVSE 424
Cdd:cd16264     1 SVFKIAVEPLNPSELPKMLDGLRKVNKSYPLLITKVEESGEHVILGTGELYMDCVMHDLRKMYSEIEIKVAD 72
EF2_IV_snRNP cd01683
EF-2_domain IV_snRNP domain is a part of 116kD U5-specific protein of the U5 small ...
 481-631 2.67e-12

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: 66.16  E-value: 2.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 481 TPNKLATLSVRAMPLPEEVTQILEEnsdlirsmEQLTSSLNEGenthmihqktqeKIWEFkgkLEQHLTgrrW-----RN 555
Cdd:cd01683    22 TPNKKNKITMIAEPLDKGLAEDIEN--------GQLKLSWNRK------------KLGKF---LRTKYG---WdalaaRS 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1017207214 556 ivdqIWSFGPRKCGPNILVNKsedfqnsvwTGPADKASKEASRYRDlgnSIVSGFQLATLSGPMCEEPLMGVCFVL 631
Cdd:cd01683    76 ----IWAFGPDTKGPNVLIDD---------TLPEEVDKNLLNSVKE---SIVQGFQWAVREGPLCEEPIRNVKFKL 135
EF2_II_snRNP cd04090
Domain II of the spliceosomal 116kD U5 small nuclear ribonucleoprotein (snRNP) component; This ...
 240-337 3.69e-11

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: 60.33  E-value: 3.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 240 ESFIAFARVFSGVARRGKKIFVLGPKYSPleflrrvplgfSAPPDglpqvphMAYCALENLYLLMGRELEYLEEVPPGNV 319
Cdd:cd04090    15 GSFWALGRIYSGTLRKGQKVKVLGENYSL-----------EDEED-------MTVCTVGRLWILGARYKYEVNSAPAGNW 76

                          90
                  ....*....|....*...
gi 1017207214 320 LGIGGLQDFVLKSATLCS 337
Cdd:cd04090    77 VLIKGIDQSIVKTATITS 94
EFG_mtEFG_C cd03713
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational ...
 717-798 2.15e-10

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: 57.54  E-value: 2.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 717 LMAAMYTCDIMATGDVLGrvyaVLSKREGRVLQEEMKEGTDmfIIKAVLPVAESFGFADEIRKRTSGLASPQLVFSHWEI 796
Cdd:cd03713     3 IMKVEVTVPEEYMGDVIG----DLSSRRGQILGTESRGGWK--VIKAEVPLAEMFGYSTDLRSLTQGRGSFTMEFSHYEE 76


                  ..
gi 1017207214 797 IP 798
Cdd:cd03713    77 VP 78
EFG_III-like cd16257
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G ...
 353-415 3.98e-10

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: 56.59  E-value: 3.98e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1017207214 353 PIVRVAVEPKHPSEMPQLVKGMKLLNQADPCVQILIQE-TGEHVLVTAGEVHLQRCLDDLKERF 415
Cdd:cd16257     1 PVVFVTVEVKNPLDQEKLLEGLERLSEEDPALQVYREEsTGEFILSGLGELHLEIIVARLEREY 64
EF2_snRNP_like_II cd03700
Domain II of elongation factor 2 and C-terminal domain of the spliceosomal human 116kD U5 ...
 242-335 1.68e-09

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: 55.70  E-value: 1.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017207214 242 FIAFARVFSGVARRGKKIFVLGPKYSP--LEFLRRVplgfsappdglpqvphmaycALENLYLLMGRELEYLEEVPPGNV 319
Cdd:cd03700    17 FYAFGRVFAGTVHAGQKVRILGPNYTPgkKEDLRIK--------------------AIQRLWLMMGRYVEEINDVPAGNI 76

                          90
                  ....*....|....*.
gi 1017207214 320 LGIGGLQDFVLKSATL 335
Cdd:cd03700    77 VGLVGIDQFLQKTGTT 92
EFG_III pfam14492
Elongation Factor G, domain III; This domain is found in Elongation Factor G. It shares a ...
 353-415 1.44e-06

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: 46.71  E-value: 1.44e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1017207214 353 PIVRVAVEPKHPSEMPQLVKGMKLLNQADPCVQILI-QETGEHVLVTAGEVHLQRCLDDLKERF 415
Cdd:pfam14492   4 PVISVAIEPKTKGDEDKLSKALNRLLEEDPTLRVERdEETGETILSGMGELHLEIVVDRLKRKY 67
EFG_IV smart00889
Elongation factor G, domain IV; Translation elongation factors are responsible for two main ...
 560-631 1.07e-04

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: 42.53  E-value: 1.07e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1017207214  560 IWSFGPRKCGPNILvnksedFQNSVwtgpadkasKEASRYRDLGNSIVSGFQLATLSGPMCEEPLMGVCFVL 631
Cdd:smart00889  33 ILEVEPLERGSGFE------FDDTI---------VGGVIPKEYIPAVEKGFREALEEGPLAGYPVVDVKVTL 89
EFG_III cd16262
Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial ...
 353-425 2.46e-04

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: 40.13  E-value: 2.46e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1017207214 353 PIVRVAVEPKHPSEMPQLVKGMKLLNQADPCVQILI-QETGEHVLVTAGEVHLQRCLDDLKERFaKIHISVSEP 425
Cdd:cd16262     3 PVISLAIEPKTKADEDKLSKALARLAEEDPTLRVSRdEETGQTILSGMGELHLEIIVERLKREY-GVEVEVGKP 75
Tet_C cd03711
Tet_C: C-terminus of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology ...
 731-796 1.48e-03

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: 37.99  E-value: 1.48e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1017207214 731 DVLGRVYAVLSKREGRVLQEEMKEgtDMFIIKAVLPVAESFGFADEIRKRTSGLASPQLVFSHWEI 796
Cdd:cd03711    13 DALGRAMSDLAKMGATFEDPQIKG--DEVTLEGTIPVATSQDYQSELPSYTHGEGVLETEFKGYRP 76
 
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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