NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1720420193|ref|XP_030097803|]
View 

elongation factor-like GTPase 1 isoform X1 [Mus musculus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK13351 super family cl46912
elongation factor G-like protein;
2-836 1.84e-116

elongation factor G-like protein;


The actual alignment was detected with superfamily member PTZ00416:

Pssm-ID: 481252 [Multi-domain]  Cd Length: 836  Bit Score: 374.00  E-value: 1.84e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193   2 KAKKIMKVDQ-AKGKKPL--FVQLILENIWSLYDAVLKKDKEKIDKIVTSLGLKIGArEARHSDPKVQINAICSQWLPIS 78
Cdd:PTZ00416  247 KTKKWIKDETnAQGKKLKraFCQFILDPICQLFDAVMNEDKEKYDKMLKSLNISLTG-EDKELTGKPLLKAVMQKWLPAA 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193  79 HAVLAMVCHKLPSPLDMTSERVEKLlctgsqtFESlpPETQALKAAFMKCGSEdtAPVIIFVSKMFavdvkalpqnkprp 158
Cdd:PTZ00416  326 DTLLEMIVDHLPSPKEAQKYRVENL-------YEG--PMDDEAANAIRNCDPN--GPLMMYISKMV-------------- 380

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 159 ltqeemaqrrerarqrhaeklaaaqgqtsqgPTQDGGAletsphedeprgdepdvasvsrqpvsqeessqeaFIAFARVF 238
Cdd:PTZ00416  381 -------------------------------PTSDKGR----------------------------------FYAFGRVF 395

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 239 SGIARRGKKIFVLGPKYSPvdflqrvplgfsAPLEDLppvphmACCTLENLYLLMGRELEDLEEVPPGNVLGIGGLQDFV 318
Cdd:PTZ00416  396 SGTVATGQKVRIQGPNYVP------------GKKEDL------FEKNIQRTVLMMGRYVEQIEDVPCGNTVGLVGVDQYL 457

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 319 LKSATLCSLPSCPPFIPLNFEATPIVRVAVEPKHPSEMPQLVKGMKLLNQADPCVQVLIQETGEHVLVTAGEVHLQRCLD 398
Cdd:PTZ00416  458 VKSGTITTSETAHNIRDMKYSVSPVVRVAVEPKNPKDLPKLVEGLKRLAKSDPLVVCTTEESGEHIVAGCGELHVEICLK 537

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 399 DLRERFAKIHISVSEPIIPFRETITkppkvdmvneeigrqqkvavihqtkeEQSKIpegihvdsdgLITIPTPNKLATLS 478
Cdd:PTZ00416  538 DLEDDYANIDIIVSDPVVSYRETVT--------------------------EESSQ----------TCLSKSPNKHNRLY 581

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 479 VRAIPLPEEvtrileensdlirsmelLTSSLNEGRNTQAIHQKTQEKIWEfkgklEKHltgrKW-RNTVDQIWSFGPRKC 557
Cdd:PTZ00416  582 MKAEPLTEE-----------------LAEAIEEGKVGPEDDPKERANFLA-----DKY----EWdKNDARKIWCFGPENK 635

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 558 GPNILVSRSEDFQNSvwsgpagRESKEasrfrdfgnSIVSGFQLATLSGPMCEEPLMGVCFVLEKWELNkcaeqgaSDKQ 637
Cdd:PTZ00416  636 GPNVLVDVTKGVQYM-------NEIKD---------SCVSAFQWATKEGVLCDENMRGIRFNILDVTLH-------ADAI 692

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 638 HQGqcdlagegqgggktchvgdenqeqqdvcsepfeetsqkgdspvidcygpfSGQLIATMKEaCRYALQVKPQ-RLMAA 716
Cdd:PTZ00416  693 HRG--------------------------------------------------AGQIIPTARR-VFYACELTASpRLLEP 721

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 717 MYTCDIMATSDVLGRVYAVLSKREGRVLQEEMKEGTDMFIIKAVLPVAESFGFADEIRKRTSGLASPQLVFSHWEVIPSD 796
Cdd:PTZ00416  722 MFLVDITAPEDAMGGIYSVLNRRRGVVIGEEQRPGTPLSNIKAYLPVAESFGFTAALRAATSGQAFPQCVFDHWQVVPGD 801

                         810       820       830       840
                  ....*....|....*....|....*....|....*....|
gi 1720420193 797 PFwvptteeeylhfgekaDSENQARKYMNAVRKRKGLYVE 836
Cdd:PTZ00416  802 PL----------------EPGSKANEIVLSIRKRKGLKPE 825
 
Name Accession Description Interval E-value
PTZ00416 PTZ00416
elongation factor 2; Provisional
 2-836 1.84e-116

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 374.00  E-value: 1.84e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193   2 KAKKIMKVDQ-AKGKKPL--FVQLILENIWSLYDAVLKKDKEKIDKIVTSLGLKIGArEARHSDPKVQINAICSQWLPIS 78
Cdd:PTZ00416  247 KTKKWIKDETnAQGKKLKraFCQFILDPICQLFDAVMNEDKEKYDKMLKSLNISLTG-EDKELTGKPLLKAVMQKWLPAA 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193  79 HAVLAMVCHKLPSPLDMTSERVEKLlctgsqtFESlpPETQALKAAFMKCGSEdtAPVIIFVSKMFavdvkalpqnkprp 158
Cdd:PTZ00416  326 DTLLEMIVDHLPSPKEAQKYRVENL-------YEG--PMDDEAANAIRNCDPN--GPLMMYISKMV-------------- 380

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 159 ltqeemaqrrerarqrhaeklaaaqgqtsqgPTQDGGAletsphedeprgdepdvasvsrqpvsqeessqeaFIAFARVF 238
Cdd:PTZ00416  381 -------------------------------PTSDKGR----------------------------------FYAFGRVF 395

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 239 SGIARRGKKIFVLGPKYSPvdflqrvplgfsAPLEDLppvphmACCTLENLYLLMGRELEDLEEVPPGNVLGIGGLQDFV 318
Cdd:PTZ00416  396 SGTVATGQKVRIQGPNYVP------------GKKEDL------FEKNIQRTVLMMGRYVEQIEDVPCGNTVGLVGVDQYL 457

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 319 LKSATLCSLPSCPPFIPLNFEATPIVRVAVEPKHPSEMPQLVKGMKLLNQADPCVQVLIQETGEHVLVTAGEVHLQRCLD 398
Cdd:PTZ00416  458 VKSGTITTSETAHNIRDMKYSVSPVVRVAVEPKNPKDLPKLVEGLKRLAKSDPLVVCTTEESGEHIVAGCGELHVEICLK 537

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 399 DLRERFAKIHISVSEPIIPFRETITkppkvdmvneeigrqqkvavihqtkeEQSKIpegihvdsdgLITIPTPNKLATLS 478
Cdd:PTZ00416  538 DLEDDYANIDIIVSDPVVSYRETVT--------------------------EESSQ----------TCLSKSPNKHNRLY 581

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 479 VRAIPLPEEvtrileensdlirsmelLTSSLNEGRNTQAIHQKTQEKIWEfkgklEKHltgrKW-RNTVDQIWSFGPRKC 557
Cdd:PTZ00416  582 MKAEPLTEE-----------------LAEAIEEGKVGPEDDPKERANFLA-----DKY----EWdKNDARKIWCFGPENK 635

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 558 GPNILVSRSEDFQNSvwsgpagRESKEasrfrdfgnSIVSGFQLATLSGPMCEEPLMGVCFVLEKWELNkcaeqgaSDKQ 637
Cdd:PTZ00416  636 GPNVLVDVTKGVQYM-------NEIKD---------SCVSAFQWATKEGVLCDENMRGIRFNILDVTLH-------ADAI 692

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 638 HQGqcdlagegqgggktchvgdenqeqqdvcsepfeetsqkgdspvidcygpfSGQLIATMKEaCRYALQVKPQ-RLMAA 716
Cdd:PTZ00416  693 HRG--------------------------------------------------AGQIIPTARR-VFYACELTASpRLLEP 721

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 717 MYTCDIMATSDVLGRVYAVLSKREGRVLQEEMKEGTDMFIIKAVLPVAESFGFADEIRKRTSGLASPQLVFSHWEVIPSD 796
Cdd:PTZ00416  722 MFLVDITAPEDAMGGIYSVLNRRRGVVIGEEQRPGTPLSNIKAYLPVAESFGFTAALRAATSGQAFPQCVFDHWQVVPGD 801

                         810       820       830       840
                  ....*....|....*....|....*....|....*....|
gi 1720420193 797 PFwvptteeeylhfgekaDSENQARKYMNAVRKRKGLYVE 836
Cdd:PTZ00416  802 PL----------------EPGSKANEIVLSIRKRKGLKPE 825
aeEF2_snRNP_like_IV cd01681
This family represents domain IV of archaeal and eukaryotic elongation factor 2 (aeEF-2) and ...
 413-719 7.81e-48

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: 167.75  E-value: 7.81e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 413 EPIIPFRETITKPpkvdmvneeigrqqkvavihqtkeeqskipegihvdSDGLITIPTPNKLATLSVRAIPLPEEVTRIL 492
Cdd:cd01681     1 DPVVSFRETVVET------------------------------------SSGTCLAKSPNKHNRLYMRAEPLPEELIEDI 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 493 EENSDLIRsmelltsslnegrntqaihqktqekiWEFKGKLEKHLTGRKWRNT-VDQIWSFGPRKCGPNILVSRSEDFQN 571
Cdd:cd01681    45 EKGKITLK--------------------------DDKKKRARILLDKYGWDKLaARKIWAFGPDRTGPNILVDDTKGVQY 98

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 572 SVwsgpagreskeaSRFRDFGNSIVSGFQLATLSGPMCEEPLMGVCFVLEKWELnkcaeqgasdkqHQgqcdlagegqgg 651
Cdd:cd01681    99 DK------------SLLNEIKDSIVAGFQWATKEGPLCEEPMRGVKFKLEDATL------------HA------------ 142

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720420193 652 gktchvgdenqeqqdvcsepfeetsqkgdspviDCYGPFSGQLIATMKEACRYALQVKPQRLMAAMYT 719
Cdd:cd01681   143 ---------------------------------DAIHRGGGQIIPAARRACYAAFLLASPRLMEPMYL 177
EFG_C smart00838
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ...
 713-798 5.86e-21

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: 87.94  E-value: 5.86e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193  713 LMAAMYTCDIMATSDVLGRVYAVLSKREGRVlqEEMKEGTDMFIIKAVLPVAESFGFADEIRKRTSGLASPQLVFSHWEV 792
Cdd:smart00838   1 LLEPIMKVEVTVPEEYMGDVIGDLNSRRGKI--EGMEQRGGAQVIKAKVPLSEMFGYATDLRSATQGRATWSMEFSHYEE 78


                   ....*.
gi 1720420193  793 IPSDPF 798
Cdd:smart00838  79 VPKSIA 84
EFG_C pfam00679
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ...
 712-798 9.42e-21

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: 87.22  E-value: 9.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 712 RLMAAMYTCDIMATSDVLGRVYAVLSKREGRVlQEEMKEGTDMFIIKAVLPVAESFGFADEIRKRTSGLASPQLVFSHWE 791
Cdd:pfam00679   1 VLLEPIEKVTIDVPEEYVGDVISDLNSRRGEI-LDMDPDDGGRVVIEAEVPLAELFGFATELRSLTKGRGSFSMEFSGYQ 79


                  ....*..
gi 1720420193 792 VIPSDPF 798
Cdd:pfam00679  80 PVPGDIL 86
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 289-429 2.93e-15

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: 80.09  E-value: 2.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 289 LYLLMGRELEDLEEVPPGNVLGIGGLQDfVLKSATLCSlPSCP-PFIPLNFeATPIVRVAVEPKHPSEMPQLVKGMKLLN 367
Cdd:COG0480   353 LLRMHGNKREEVDEAGAGDIVAVVKLKD-TTTGDTLCD-EDHPiVLEPIEF-PEPVISVAIEPKTKADEDKLSTALAKLA 429

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720420193 368 QADPCVQVLI-QETGEHVLVTAGEVHLQRCLDDLRERFaKIHISVSEPIIPFRETITKPPKVD 429
Cdd:COG0480   430 EEDPTFRVETdEETGQTIISGMGELHLEIIVDRLKREF-GVEVNVGKPQVAYRETIRKKAEAE 491
 
Name Accession Description Interval E-value
PTZ00416 PTZ00416
elongation factor 2; Provisional
 2-836 1.84e-116

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 374.00  E-value: 1.84e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193   2 KAKKIMKVDQ-AKGKKPL--FVQLILENIWSLYDAVLKKDKEKIDKIVTSLGLKIGArEARHSDPKVQINAICSQWLPIS 78
Cdd:PTZ00416  247 KTKKWIKDETnAQGKKLKraFCQFILDPICQLFDAVMNEDKEKYDKMLKSLNISLTG-EDKELTGKPLLKAVMQKWLPAA 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193  79 HAVLAMVCHKLPSPLDMTSERVEKLlctgsqtFESlpPETQALKAAFMKCGSEdtAPVIIFVSKMFavdvkalpqnkprp 158
Cdd:PTZ00416  326 DTLLEMIVDHLPSPKEAQKYRVENL-------YEG--PMDDEAANAIRNCDPN--GPLMMYISKMV-------------- 380

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 159 ltqeemaqrrerarqrhaeklaaaqgqtsqgPTQDGGAletsphedeprgdepdvasvsrqpvsqeessqeaFIAFARVF 238
Cdd:PTZ00416  381 -------------------------------PTSDKGR----------------------------------FYAFGRVF 395

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 239 SGIARRGKKIFVLGPKYSPvdflqrvplgfsAPLEDLppvphmACCTLENLYLLMGRELEDLEEVPPGNVLGIGGLQDFV 318
Cdd:PTZ00416  396 SGTVATGQKVRIQGPNYVP------------GKKEDL------FEKNIQRTVLMMGRYVEQIEDVPCGNTVGLVGVDQYL 457

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 319 LKSATLCSLPSCPPFIPLNFEATPIVRVAVEPKHPSEMPQLVKGMKLLNQADPCVQVLIQETGEHVLVTAGEVHLQRCLD 398
Cdd:PTZ00416  458 VKSGTITTSETAHNIRDMKYSVSPVVRVAVEPKNPKDLPKLVEGLKRLAKSDPLVVCTTEESGEHIVAGCGELHVEICLK 537

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 399 DLRERFAKIHISVSEPIIPFRETITkppkvdmvneeigrqqkvavihqtkeEQSKIpegihvdsdgLITIPTPNKLATLS 478
Cdd:PTZ00416  538 DLEDDYANIDIIVSDPVVSYRETVT--------------------------EESSQ----------TCLSKSPNKHNRLY 581

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 479 VRAIPLPEEvtrileensdlirsmelLTSSLNEGRNTQAIHQKTQEKIWEfkgklEKHltgrKW-RNTVDQIWSFGPRKC 557
Cdd:PTZ00416  582 MKAEPLTEE-----------------LAEAIEEGKVGPEDDPKERANFLA-----DKY----EWdKNDARKIWCFGPENK 635

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 558 GPNILVSRSEDFQNSvwsgpagRESKEasrfrdfgnSIVSGFQLATLSGPMCEEPLMGVCFVLEKWELNkcaeqgaSDKQ 637
Cdd:PTZ00416  636 GPNVLVDVTKGVQYM-------NEIKD---------SCVSAFQWATKEGVLCDENMRGIRFNILDVTLH-------ADAI 692

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 638 HQGqcdlagegqgggktchvgdenqeqqdvcsepfeetsqkgdspvidcygpfSGQLIATMKEaCRYALQVKPQ-RLMAA 716
Cdd:PTZ00416  693 HRG--------------------------------------------------AGQIIPTARR-VFYACELTASpRLLEP 721

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 717 MYTCDIMATSDVLGRVYAVLSKREGRVLQEEMKEGTDMFIIKAVLPVAESFGFADEIRKRTSGLASPQLVFSHWEVIPSD 796
Cdd:PTZ00416  722 MFLVDITAPEDAMGGIYSVLNRRRGVVIGEEQRPGTPLSNIKAYLPVAESFGFTAALRAATSGQAFPQCVFDHWQVVPGD 801

                         810       820       830       840
                  ....*....|....*....|....*....|....*....|
gi 1720420193 797 PFwvptteeeylhfgekaDSENQARKYMNAVRKRKGLYVE 836
Cdd:PTZ00416  802 PL----------------EPGSKANEIVLSIRKRKGLKPE 825
PLN00116 PLN00116
translation elongation factor EF-2 subunit; Provisional
 19-833 2.23e-93

translation elongation factor EF-2 subunit; Provisional


Pssm-ID: 177730 [Multi-domain]  Cd Length: 843  Bit Score: 312.43  E-value: 2.23e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193  19 FVQLILENIWSLYDAVLKKDKEKIDKIVTSLGLKIGAREARHSDpKVQINAICSQWLPISHAVLAMVCHKLPSPLDMTSE 98
Cdd:PLN00116  271 FVQFCYEPIKQIINTCMNDQKDKLWPMLEKLGVTLKSDEKELMG-KALMKRVMQTWLPASDALLEMIIFHLPSPAKAQRY 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193  99 RVEKLlctgsqtFESlpPETQALKAAFMKCGSEdtAPVIIFVSKMFavdvkalpqnkprpltqeemaqrrerarqrhaek 178
Cdd:PLN00116  350 RVENL-------YEG--PLDDKYATAIRNCDPN--GPLMLYVSKMI---------------------------------- 384

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 179 laaaqgqtsqgPTQDGGAletsphedeprgdepdvasvsrqpvsqeessqeaFIAFARVFSGIARRGKKIFVLGPKYSP- 257
Cdd:PLN00116  385 -----------PASDKGR----------------------------------FFAFGRVFSGTVATGMKVRIMGPNYVPg 419

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 258 ------VDFLQRVplgfsapledlppvphmacctlenlYLLMGRELEDLEEVPPGNVLGIGGLQDFVLKSATLC--SLPS 329
Cdd:PLN00116  420 ekkdlyVKSVQRT-------------------------VIWMGKKQESVEDVPCGNTVAMVGLDQFITKNATLTneKEVD 474

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 330 CPPFIPLNFEATPIVRVAVEPKHPSEMPQLVKGMKLLNQADPCVQVLIQETGEHVLVTAGEVHLQRCLDDLRERF-AKIH 408
Cdd:PLN00116  475 AHPIKAMKFSVSPVVRVAVQCKNASDLPKLVEGLKRLAKSDPMVQCTIEESGEHIIAGAGELHLEICLKDLQDDFmGGAE 554

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 409 ISVSEPIIPFRETitkppkvdmVNEEigrqqkvavihqtkeeqskipegihvdSDGLITIPTPNKLATLSVRAIPLPEEv 488
Cdd:PLN00116  555 IKVSDPVVSFRET---------VLEK---------------------------SCRTVMSKSPNKHNRLYMEARPLEEG- 597

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 489 trileensdlirsmelLTSSLNEGRNTQAIHQKTQEKIWEfkgklEKHltgrKW-RNTVDQIWSFGPRKCGPNILVSRSE 567
Cdd:PLN00116  598 ----------------LAEAIDDGRIGPRDDPKIRSKILA-----EEF----GWdKDLAKKIWCFGPETTGPNMVVDMCK 652

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 568 DFQ--NsvwsgpagrESKEasrfrdfgnSIVSGFQLATLSGPMCEEPLMGVCFVLEKWELNkcaeqgaSDKQHQGqcdla 645
Cdd:PLN00116  653 GVQylN---------EIKD---------SVVAGFQWATKEGALAEENMRGICFEVCDVVLH-------ADAIHRG----- 702

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 646 gegqgggktchvgdenqeqqdvcsepfeetsqkgdspvidcygpfSGQLIATMKEACrYALQV--KPqRLMAAMYTCDIM 723
Cdd:PLN00116  703 ---------------------------------------------GGQIIPTARRVI-YASQLtaKP-RLLEPVYLVEIQ 735

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 724 ATSDVLGRVYAVLSKREGRVLQEEMKEGTDMFIIKAVLPVAESFGFADEIRKRTSGLASPQLVFSHWEVIPSDPFwvptt 803
Cdd:PLN00116  736 APEQALGGIYSVLNQKRGHVFEEMQRPGTPLYNIKAYLPVIESFGFSGTLRAATSGQAFPQCVFDHWDMMSSDPL----- 810

                         810       820       830
                  ....*....|....*....|....*....|
gi 1720420193 804 eeeylhfgekaDSENQARKYMNAVRKRKGL 833
Cdd:PLN00116  811 -----------EAGSQAAQLVADIRKRKGL 829
PRK07560 PRK07560
elongation factor EF-2; Reviewed
 232-842 1.48e-48

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 184.30  E-value: 1.48e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 232 IAFARVFSGIARRGKKIFVLGPKYSpvdflQRVplgfsapledlppvphmacctlENLYLLMGRELEDLEEVPPGNVLGI 311
Cdd:PRK07560  307 VATGRVFSGTLRKGQEVYLVGAKKK-----NRV----------------------QQVGIYMGPEREEVEEIPAGNIAAV 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 312 GGLQDFVLKSaTLCSLPSCPPFIPLNFEATPIVRVAVEPKHPSEMPQLVKGMKLLNQADPCVQVLI-QETGEHVLVTAGE 390
Cdd:PRK07560  360 TGLKDARAGE-TVVSVEDMTPFESLKHISEPVVTVAIEAKNPKDLPKLIEVLRQLAKEDPTLVVKInEETGEHLLSGMGE 438

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 391 VHLQRCLDDLRERFaKIHISVSEPIIPFRETITKppkvdmvneeigrqqkvavihqtkeeQSKIPEGIhvdsdglitipT 470
Cdd:PRK07560  439 LHLEVITYRIKRDY-GIEVVTSEPIVVYRETVRG--------------------------KSQVVEGK-----------S 480

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 471 PNKLATLSVRAIPLPEEVTrileensDLIRSMELltsslnegrntqaihqkTQEKIWEFKGKLEKHLTGRKW-RNTVDQI 549
Cdd:PRK07560  481 PNKHNRFYISVEPLEEEVI-------EAIKEGEI-----------------SEDMDKKEAKILREKLIEAGMdKDEAKRV 536

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 550 WSFgprkCGPNILVSRSEDFQNSvwsgpagRESKEasrfrdfgnSIVSGFQLATLSGPMCEEPLMGVCFVLEKWELNKca 629
Cdd:PRK07560  537 WAI----YNGNVFIDMTKGIQYL-------NEVME---------LIIEGFREAMKEGPLAAEPVRGVKVRLHDAKLHE-- 594

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 630 eqgasDKQHQGqcdlagegqgggktchvgdenqeqqdvcsePfeetsqkgdspvidcygpfsGQLIATMKEACRYA-LQV 708
Cdd:PRK07560  595 -----DAIHRG------------------------------P--------------------AQVIPAVRNAIFAAmLTA 619

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 709 KPqRLMAAMYTCDIMATSDVLGRVYAVLSKREGRVLqeEMKEGTDMFIIKAVLPVAESFGFADEIRKRTSGLASPQLVFS 788
Cdd:PRK07560  620 KP-TLLEPIQKVDINVPQDYMGAVTREIQGRRGKIL--DMEQEGDMAIIEAEAPVAEMFGFAGEIRSATEGRALWSTEFA 696

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720420193 789 HWEVIPsdpfwvptteeeylhfgekadsENQARKYMNAVRKRKGLYVEEKIVEH 842
Cdd:PRK07560  697 GFEPVP----------------------DSLQLDIVRQIRERKGLKPELPKPED 728
aeEF2_snRNP_like_IV cd01681
This family represents domain IV of archaeal and eukaryotic elongation factor 2 (aeEF-2) and ...
 413-719 7.81e-48

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: 167.75  E-value: 7.81e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 413 EPIIPFRETITKPpkvdmvneeigrqqkvavihqtkeeqskipegihvdSDGLITIPTPNKLATLSVRAIPLPEEVTRIL 492
Cdd:cd01681     1 DPVVSFRETVVET------------------------------------SSGTCLAKSPNKHNRLYMRAEPLPEELIEDI 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 493 EENSDLIRsmelltsslnegrntqaihqktqekiWEFKGKLEKHLTGRKWRNT-VDQIWSFGPRKCGPNILVSRSEDFQN 571
Cdd:cd01681    45 EKGKITLK--------------------------DDKKKRARILLDKYGWDKLaARKIWAFGPDRTGPNILVDDTKGVQY 98

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 572 SVwsgpagreskeaSRFRDFGNSIVSGFQLATLSGPMCEEPLMGVCFVLEKWELnkcaeqgasdkqHQgqcdlagegqgg 651
Cdd:cd01681    99 DK------------SLLNEIKDSIVAGFQWATKEGPLCEEPMRGVKFKLEDATL------------HA------------ 142

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720420193 652 gktchvgdenqeqqdvcsepfeetsqkgdspviDCYGPFSGQLIATMKEACRYALQVKPQRLMAAMYT 719
Cdd:cd01681   143 ---------------------------------DAIHRGGGQIIPAARRACYAAFLLASPRLMEPMYL 177
eEF2_snRNP_like_C cd04096
eEF2_snRNP_like_C: this family represents a C-terminal domain of eukaryotic elongation factor ...
 716-794 4.88e-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: 147.69  E-value: 4.88e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720420193 716 AMYTCDIMATSDVLGRVYAVLSKREGRVLQEEMKEGTDMFIIKAVLPVAESFGFADEIRKRTSGLASPQLVFSHWEVIP 794
Cdd:cd04096     2 PIYLVEIQCPEDALGKVYSVLSKRRGHVLSEEPKEGTPLFEIKAYLPVIESFGFETDLRSATSGQAFPQLVFSHWEIVP 80
EF2_snRNP_III cd16261
Domain III of Elongation Factor 2 (EF2); This model represents domain III of Elongation factor ...
 342-413 1.06e-35

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: 129.23  E-value: 1.06e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720420193 342 PIVRVAVEPKHPSEMPQLVKGMKLLNQADPCVQVLIQETGEHVLVTAGEVHLQRCLDDLRERFAKIHISVSE 413
Cdd:cd16261     1 PVVRVAVEPKNPSDLPKLVEGLKKLAKSDPTVQVKIEEEGEHLIAGAGELHLEICLKDLKEDFAGIEIKVSD 72
EF2_II cd16268
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 ...
 231-326 3.11e-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: 111.92  E-value: 3.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 231 FIAFARVFSGIARRGKKIFVLGPKYSPvdflqrvplgfsapledlPPVPHMACCTLENLYLLMGRELEDLEEVPPGNVLG 310
Cdd:cd16268    18 FVAFGRVFSGTVRRGQEVYILGPKYVP------------------GKKDDLKKKRIQQTYLMMGREREPVDEVPAGNIVG 79

                          90
                  ....*....|....*.
gi 1720420193 311 IGGLQDFVLKSATLCS 326
Cdd:cd16268    80 LVGLDDFLAKSGTTTS 95
Elongation_Factor_C cd01514
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ...
 717-794 6.29e-26

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


Pssm-ID: 238772 [Multi-domain]  Cd Length: 79  Bit Score: 101.79  E-value: 6.29e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720420193 717 MYTCDIMATSDVLGRVYAVLSKREGRVLQEEMKeGTDMFIIKAVLPVAESFGFADEIRKRTSGLASPQLVFSHWEVIP 794
Cdd:cd01514     3 IMKVEITVPEEYLGAVIGDLSKRRGEILGMEPR-GTGRVVIKAELPLAEMFGFATDLRSLTQGRASFSMEFSHYEPVP 79
EFG_C smart00838
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ...
 713-798 5.86e-21

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: 87.94  E-value: 5.86e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193  713 LMAAMYTCDIMATSDVLGRVYAVLSKREGRVlqEEMKEGTDMFIIKAVLPVAESFGFADEIRKRTSGLASPQLVFSHWEV 792
Cdd:smart00838   1 LLEPIMKVEVTVPEEYMGDVIGDLNSRRGKI--EGMEQRGGAQVIKAKVPLSEMFGYATDLRSATQGRATWSMEFSHYEE 78


                   ....*.
gi 1720420193  793 IPSDPF 798
Cdd:smart00838  79 VPKSIA 84
EFG_C pfam00679
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ...
 712-798 9.42e-21

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: 87.22  E-value: 9.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 712 RLMAAMYTCDIMATSDVLGRVYAVLSKREGRVlQEEMKEGTDMFIIKAVLPVAESFGFADEIRKRTSGLASPQLVFSHWE 791
Cdd:pfam00679   1 VLLEPIEKVTIDVPEEYVGDVISDLNSRRGEI-LDMDPDDGGRVVIEAEVPLAELFGFATELRSLTKGRGSFSMEFSGYQ 79


                  ....*..
gi 1720420193 792 VIPSDPF 798
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 ...
 717-794 2.06e-18

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: 80.37  E-value: 2.06e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720420193 717 MYTCDIMATSDVLGRVYAVLSKREGRVLQEEMKEGTDMFIIKAVLPVAESFGFADEIRKRTSGLASPQLVFSHWEVIP 794
Cdd:cd04098     3 IYEVEITCPADAVSAVYEVLSRRRGHVIYDTPIPGTPLYEVKAFIPVIESFGFETDLRVHTQGQAFCQSVFDHWQIVP 80
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
200-429 9.24e-18

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 87.87  E-value: 9.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 200 SPHEDEPRGDEPDVASVSRQPVSQEESSQEAF----------IAFARVFSGIARRGKKIFVLGPKyspvdflQRVPLGfs 269
Cdd:PRK12740  263 SPLEVPPVDGEDGEEGAELAPDPDGPLVALVFktmddpfvgkLSLVRVYSGTLKKGDTLYNSGTG-------KKERVG-- 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 270 apledlppvphmacctleNLYLLMGRELEDLEEVPPGNVLGIGGLQDfVLKSATLCSlPSCP-PFIPLNFeATPIVRVAV 348
Cdd:PRK12740  334 ------------------RLYRMHGKQREEVDEAVAGDIVAVAKLKD-AATGDTLCD-KGDPiLLEPMEF-PEPVISLAI 392

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 349 EPKHPSEMPQLVKGMKLLNQADPCVQVLI-QETGEHVLVTAGEVHLQRCLDDLRERFaKIHISVSEPIIPFRETITKPPK 427
Cdd:PRK12740  393 EPKDKGDEEKLSEALGKLAEEDPTLRVERdEETGQTILSGMGELHLDVALERLKREY-GVEVETGPPQVPYRETIRKKAE 471


                  ..
gi 1720420193 428 VD 429
Cdd:PRK12740  472 GH 473
PRK13351 PRK13351
elongation factor G-like protein;
200-425 1.50e-16

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 84.23  E-value: 1.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 200 SPHEDEP-RGDEPDVASVSRQPVSQEESSQEAF----------IAFARVFSGIARRGKKIFVLGPKyspvdflQRVPLGf 268
Cdd:PRK13351  279 SPLEVPPpRGSKDNGKPVKVDPDPEKPLLALVFkvqydpyagkLTYLRVYSGTLRAGSQLYNGTGG-------KREKVG- 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 269 sapledlppvphmacctleNLYLLMGRELEDLEEVPPGNVLGIGGLqDFVLKSATLCSLPSCPPFIPLNFeATPIVRVAV 348
Cdd:PRK13351  351 -------------------RLFRLQGNKREEVDRAKAGDIVAVAGL-KELETGDTLHDSADPVLLELLTF-PEPVVSLAV 409

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720420193 349 EPKHPSEMPQLVKGMKLLNQADPCVQVLI-QETGEHVLVTAGEVHLQRCLDDLRERFaKIHISVSEPIIPFRETITKP 425
Cdd:PRK13351  410 EPERRGDEQKLAEALEKLVWEDPSLRVEEdEETGQTILSGMGELHLEVALERLRREF-KLEVNTGKPQVAYRETIRKM 486
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 289-429 2.93e-15

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: 80.09  E-value: 2.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 289 LYLLMGRELEDLEEVPPGNVLGIGGLQDfVLKSATLCSlPSCP-PFIPLNFeATPIVRVAVEPKHPSEMPQLVKGMKLLN 367
Cdd:COG0480   353 LLRMHGNKREEVDEAGAGDIVAVVKLKD-TTTGDTLCD-EDHPiVLEPIEF-PEPVISVAIEPKTKADEDKLSTALAKLA 429

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720420193 368 QADPCVQVLI-QETGEHVLVTAGEVHLQRCLDDLRERFaKIHISVSEPIIPFRETITKPPKVD 429
Cdd:COG0480   430 EEDPTFRVETdEETGQTIISGMGELHLEIIVDRLKREF-GVEVNVGKPQVAYRETIRKKAEAE 491
EF2_II_snRNP cd04090
Domain II of the spliceosomal 116kD U5 small nuclear ribonucleoprotein (snRNP) component; This ...
 229-326 1.86e-14

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: 69.57  E-value: 1.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 229 EAFIAFARVFSGIARRGKKIFVLGPKYSPVDflqrvplgfsapLEDlppvphMACCTLENLYLLMGRELEDLEEVPPGNV 308
Cdd:cd04090    15 GSFWALGRIYSGTLRKGQKVKVLGENYSLED------------EED------MTVCTVGRLWILGARYKYEVNSAPAGNW 76

                          90
                  ....*....|....*...
gi 1720420193 309 LGIGGLQDFVLKSATLCS 326
Cdd:cd04090    77 VLIKGIDQSIVKTATITS 94
snRNP_III cd16264
Domain III of the spliceosomal 116kD U5 small nuclear ribonucleoprotein (snRNP) component; ...
 342-413 2.30e-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: 65.60  E-value: 2.30e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720420193 342 PIVRVAVEPKHPSEMPQLVKGMKLLNQADPCVQVLIQETGEHVLVTAGEVHLQRCLDDLRERFAKIHISVSE 413
Cdd:cd16264     1 SVFKIAVEPLNPSELPKMLDGLRKVNKSYPLLITKVEESGEHVILGTGELYMDCVMHDLRKMYSEIEIKVAD 72
EFG_III-like cd16257
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G ...
 342-404 1.46e-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: 57.74  E-value: 1.46e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720420193 342 PIVRVAVEPKHPSEMPQLVKGMKLLNQADPCVQVLIQE-TGEHVLVTAGEVHLQRCLDDLRERF 404
Cdd:cd16257     1 PVVFVTVEVKNPLDQEKLLEGLERLSEEDPALQVYREEsTGEFILSGLGELHLEIIVARLEREY 64
EFG_mtEFG_C cd03713
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational ...
 721-794 1.71e-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: 57.92  E-value: 1.71e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720420193 721 DIMATSDVLGRVYAVLSKREGRVLQEEMKEGTDmfIIKAVLPVAESFGFADEIRKRTSGLASPQLVFSHWEVIP 794
Cdd:cd03713     7 EVTVPEEYMGDVIGDLSSRRGQILGTESRGGWK--VIKAEVPLAEMFGYSTDLRSLTQGRGSFTMEFSHYEEVP 78
EF2_snRNP_like_II cd03700
Domain II of elongation factor 2 and C-terminal domain of the spliceosomal human 116kD U5 ...
 231-324 2.89e-10

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: 57.62  E-value: 2.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 231 FIAFARVFSGIARRGKKIFVLGPKYSPVDflqrvplgfsapLEDLPPVphmaccTLENLYLLMGRELEDLEEVPPGNVLG 310
Cdd:cd03700    17 FYAFGRVFAGTVHAGQKVRILGPNYTPGK------------KEDLRIK------AIQRLWLMMGRYVEEINDVPAGNIVG 78

                          90
                  ....*....|....
gi 1720420193 311 IGGLQDFVLKSATL 324
Cdd:cd03700    79 LVGIDQFLQKTGTT 92
EF2_IV_snRNP cd01683
EF-2_domain IV_snRNP domain is a part of 116kD U5-specific protein of the U5 small ...
 470-620 5.44e-09

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: 56.53  E-value: 5.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420193 470 TPNKLATLSVRAIPLPEEVTRILEensdlirsmelltsslnegrNTQAIHQKTQEKIWEFKgkLEKHltgrKW-----RN 544
Cdd:cd01683    22 TPNKKNKITMIAEPLDKGLAEDIE--------------------NGQLKLSWNRKKLGKFL--RTKY----GWdalaaRS 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720420193 545 tvdqIWSFGPRKCGPNILVSRSEDfqnsvwsgpagrESKEASRFRDFGNSIVSGFQLATLSGPMCEEPLMGVCFVL 620
Cdd:cd01683    76 ----IWAFGPDTKGPNVLIDDTLP------------EEVDKNLLNSVKESIVQGFQWAVREGPLCEEPIRNVKFKL 135
EFG_III pfam14492
Elongation Factor G, domain III; This domain is found in Elongation Factor G. It shares a ...
 342-404 1.45e-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: 1.45e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720420193 342 PIVRVAVEPKHPSEMPQLVKGMKLLNQADPCVQVLI-QETGEHVLVTAGEVHLQRCLDDLRERF 404
Cdd:pfam14492   4 PVISVAIEPKTKGDEDKLSKALNRLLEEDPTLRVERdEETGETILSGMGELHLEIVVDRLKRKY 67
EFG_IV smart00889
Elongation factor G, domain IV; Translation elongation factors are responsible for two main ...
 549-620 6.59e-05

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: 43.30  E-value: 6.59e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720420193  549 IWSFGPRKCGPNILvsrsedFQNSVwsgPAGRESKEasrfrdFGNSIVSGFQLATLSGPMCEEPLMGVCFVL 620
Cdd:smart00889  33 ILEVEPLERGSGFE------FDDTI---VGGVIPKE------YIPAVEKGFREALEEGPLAGYPVVDVKVTL 89
EFG_III cd16262
Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial ...
 342-414 1.67e-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: 40.90  E-value: 1.67e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720420193 342 PIVRVAVEPKHPSEMPQLVKGMKLLNQADPCVQVLI-QETGEHVLVTAGEVHLQRCLDDLRERFaKIHISVSEP 414
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 ...
 722-792 1.52e-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: 1.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720420193 722 IMATSDVLGRVYAVLSKREGRVLQEEMKEgtDMFIIKAVLPVAESFGFADEIRKRTSGLASPQLVFSHWEV 792
Cdd:cd03711     8 LEVPQDALGRAMSDLAKMGATFEDPQIKG--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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH