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Conserved domains on  [gi|75756276|gb|ABA27171|]
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mRNA splicing factor U5 snRNP [Bigelowiella natans]

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

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List of domain hits

 Name Accession Description Interval E-value
PRK13351 super family cl46912
elongation factor G-like protein;
60-883 9.95e-46

elongation factor G-like protein;


The actual alignment was detected with superfamily member PTZ00416:

Pssm-ID: 481252 [Multi-domain]  Cd Length: 836  Bit Score: 177.16  E-value: 9.95e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276   60 SIDEffIYKMIDNERQIRTISVAGSINSGKSSFLTS------IISFNSPylKDSIYKHMRTDEDIMKTTIimtpllKS-- 131
Cdd:PTZ00416   5 TVDQ--IREIMDNPDQIRNMSVIAHVDHGKSTLTDSlvckagIISSKNA--GDARFTDTRADEQERGITI------KStg 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  132 --------IRKNNKYNTYYF--LDTPGHSNLFQDFNLALCISDGVIITIDSIEGVTLQTKKIINSCLYTKKKIFILITKI 201
Cdd:PTZ00416  75 islyyehdLEDGDDKQPFLInlIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  202 DRLISELRLPPSTFYDKIQSIIFDVNLIIKNSNKKQ--DY-FSFSKSNIGILSAEIGLFLTSEILNKLYHSIYPTIFKLF 278
Cdd:PTZ00416 155 DRAILELQLDPEEIYQNFVKTIENVNVIIATYNDELmgDVqVYPEKGTVAFGSGLQGWAFTLTTFARIYAKKFGVEESKM 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  279 FPKEWiwhTENFIVGKNilKSNPKEPGSHNPIIFFAIIPI------YKLYSFCLSENPLKIMQFIHKTNFSNTLLNLNFP 352
Cdd:PTZ00416 235 MERLW---GDNFFDAKT--KKWIKDETNAQGKKLKRAFCQfildpiCQLFDAVMNEDKEKYDKMLKSLNISLTGEDKELT 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  353 LKNLMKFVFKSVFDYPQSTYEKFSEYFESSKHLNQLFTNsmskqsskkssifshtaknHFYDKYMEKKVFLGI------- 425
Cdd:PTZ00416 310 GKPLLKAVMQKWLPAADTLLEMIVDHLPSPKEAQKYRVE-------------------NLYEGPMDDEAANAIrncdpng 370

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  426 -------KFFPNSYGKKFLLFGRILNGKIVN---------------NDSLYAKNfnnivhnfkINHFFLINCFQLKRIKS 483
Cdd:PTZ00416 371 plmmyisKMVPTSDKGRFYAFGRVFSGTVATgqkvriqgpnyvpgkKEDLFEKN---------IQRTVLMMGRYVEQIED 441

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  484 IKKGN-CLVIEENNNLNEIPILITEESkvyesnPFIDKNLLKNTYP-LKITIEPAYSMDLTKLLSGIQKYLKTSKNTIAS 561
Cdd:PTZ00416 442 VPCGNtVGLVGVDQYLVKSGTITTSET------AHNIRDMKYSVSPvVRVAVEPKNPKDLPKLVEGLKRLAKSDPLVVCT 515

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  562 VQESGTVQISGIGEFALNLMIKEICDFFSLLKVKVSNPFISLKETIECSSkfkSISIAQKS-----RIYM--EIMTEKIN 634
Cdd:PTZ00416 516 TEESGEHIVAGCGELHVEICLKDLEDDYANIDIIVSDPVVSYRETVTEES---SQTCLSKSpnkhnRLYMkaEPLTEELA 592

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  635 LIKEKNEITKKYlsyQNDEMKHFYTQEYIMEKvkisNLSNNLWSYQVHDGFLNILSEyKTSynDKQILK-IRSTLIKAFL 713
Cdd:PTZ00416 593 EAIEEGKVGPED---DPKERANFLADKYEWDK----NDARKIWCFGPENKGPNVLVD-VTK--GVQYMNeIKDSCVSAFQ 662

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  714 MACRTGPICMEPVVNINFAIQEIK-SIEKIQ----QIfkkeISSCmKKLCHSSILISTPRILEPYSEIEVVTPFESSKMI 788
Cdd:PTZ00416 663 WATKEGVLCDENMRGIRFNILDVTlHADAIHrgagQI----IPTA-RRVFYACELTASPRLLEPMFLVDITAPEDAMGGI 737

                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  789 FNILLNRRAIILNDMPIQGTLHYRILFLIPTINTIGLETDIRYHTQGQSLIIGFFKGWYIVPGYPISnqnnikKNNIAHN 868
Cdd:PTZ00416 738 YSVLNRRRGVVIGEEQRPGTPLSNIKAYLPVAESFGFTAALRAATSGQAFPQCVFDHWQVVPGDPLE------PGSKANE 811

                        890
                 ....*....|....*
gi 75756276  869 YMKKIRRKKGMSEKI 883
Cdd:PTZ00416 812 IVLSIRKRKGLKPEI 826
 
Name Accession Description Interval E-value
PTZ00416 PTZ00416
elongation factor 2; Provisional
 60-883 9.95e-46

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 177.16  E-value: 9.95e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276   60 SIDEffIYKMIDNERQIRTISVAGSINSGKSSFLTS------IISFNSPylKDSIYKHMRTDEDIMKTTIimtpllKS-- 131
Cdd:PTZ00416   5 TVDQ--IREIMDNPDQIRNMSVIAHVDHGKSTLTDSlvckagIISSKNA--GDARFTDTRADEQERGITI------KStg 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  132 --------IRKNNKYNTYYF--LDTPGHSNLFQDFNLALCISDGVIITIDSIEGVTLQTKKIINSCLYTKKKIFILITKI 201
Cdd:PTZ00416  75 islyyehdLEDGDDKQPFLInlIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  202 DRLISELRLPPSTFYDKIQSIIFDVNLIIKNSNKKQ--DY-FSFSKSNIGILSAEIGLFLTSEILNKLYHSIYPTIFKLF 278
Cdd:PTZ00416 155 DRAILELQLDPEEIYQNFVKTIENVNVIIATYNDELmgDVqVYPEKGTVAFGSGLQGWAFTLTTFARIYAKKFGVEESKM 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  279 FPKEWiwhTENFIVGKNilKSNPKEPGSHNPIIFFAIIPI------YKLYSFCLSENPLKIMQFIHKTNFSNTLLNLNFP 352
Cdd:PTZ00416 235 MERLW---GDNFFDAKT--KKWIKDETNAQGKKLKRAFCQfildpiCQLFDAVMNEDKEKYDKMLKSLNISLTGEDKELT 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  353 LKNLMKFVFKSVFDYPQSTYEKFSEYFESSKHLNQLFTNsmskqsskkssifshtaknHFYDKYMEKKVFLGI------- 425
Cdd:PTZ00416 310 GKPLLKAVMQKWLPAADTLLEMIVDHLPSPKEAQKYRVE-------------------NLYEGPMDDEAANAIrncdpng 370

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  426 -------KFFPNSYGKKFLLFGRILNGKIVN---------------NDSLYAKNfnnivhnfkINHFFLINCFQLKRIKS 483
Cdd:PTZ00416 371 plmmyisKMVPTSDKGRFYAFGRVFSGTVATgqkvriqgpnyvpgkKEDLFEKN---------IQRTVLMMGRYVEQIED 441

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  484 IKKGN-CLVIEENNNLNEIPILITEESkvyesnPFIDKNLLKNTYP-LKITIEPAYSMDLTKLLSGIQKYLKTSKNTIAS 561
Cdd:PTZ00416 442 VPCGNtVGLVGVDQYLVKSGTITTSET------AHNIRDMKYSVSPvVRVAVEPKNPKDLPKLVEGLKRLAKSDPLVVCT 515

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  562 VQESGTVQISGIGEFALNLMIKEICDFFSLLKVKVSNPFISLKETIECSSkfkSISIAQKS-----RIYM--EIMTEKIN 634
Cdd:PTZ00416 516 TEESGEHIVAGCGELHVEICLKDLEDDYANIDIIVSDPVVSYRETVTEES---SQTCLSKSpnkhnRLYMkaEPLTEELA 592

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  635 LIKEKNEITKKYlsyQNDEMKHFYTQEYIMEKvkisNLSNNLWSYQVHDGFLNILSEyKTSynDKQILK-IRSTLIKAFL 713
Cdd:PTZ00416 593 EAIEEGKVGPED---DPKERANFLADKYEWDK----NDARKIWCFGPENKGPNVLVD-VTK--GVQYMNeIKDSCVSAFQ 662

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  714 MACRTGPICMEPVVNINFAIQEIK-SIEKIQ----QIfkkeISSCmKKLCHSSILISTPRILEPYSEIEVVTPFESSKMI 788
Cdd:PTZ00416 663 WATKEGVLCDENMRGIRFNILDVTlHADAIHrgagQI----IPTA-RRVFYACELTASPRLLEPMFLVDITAPEDAMGGI 737

                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  789 FNILLNRRAIILNDMPIQGTLHYRILFLIPTINTIGLETDIRYHTQGQSLIIGFFKGWYIVPGYPISnqnnikKNNIAHN 868
Cdd:PTZ00416 738 YSVLNRRRGVVIGEEQRPGTPLSNIKAYLPVAESFGFTAALRAATSGQAFPQCVFDHWQVVPGDPLE------PGSKANE 811

                        890
                 ....*....|....*
gi 75756276  869 YMKKIRRKKGMSEKI 883
Cdd:PTZ00416 812 IVLSIRKRKGLKPEI 826
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 78-256 3.53e-38

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


Pssm-ID: 206647 [Multi-domain]  Cd Length: 183  Bit Score: 140.51  E-value: 3.53e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  78 TISVAGSINSGKSSFLTSIISFNSPYLKDSIYK----HMRTDEDIMKTTIIMTPLLKSIRKNNkyntYYFLDTPGHSNLF 153
Cdd:cd00881   1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKetflDTLKEERERGITIKTGVVEFEWPKRR----INFIDTPGHEDFS 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276 154 QDFNLALCISDGVIITIDSIEGVTLQTKKIINSCLYTKKKIFILITKIDRLIselrlpPSTFYDKIQSIIFDVNLIIKNs 233
Cdd:cd00881  77 KETVRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVG------EEDFDEVLREIKELLKLIGFT- 149

                       170       180
                ....*....|....*....|...
gi 75756276 234 nkkqdYFSFSKSNIGILSAEIGL 256
Cdd:cd00881 150 -----FLKGKDVPIIPISALTGE 167
EFG_C pfam00679
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ...
 768-853 7.19e-13

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: 64.87  E-value: 7.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276   768 RILEPYSEIEVVTPFESSKMIFNILLNRRAIILNDMPIQGTLHyRILFLIPTINTIGLETDIRYHTQGQSLIIGFFKGWY 847
Cdd:pfam00679   1 VLLEPIEKVTIDVPEEYVGDVISDLNSRRGEILDMDPDDGGRV-VIEAEVPLAELFGFATELRSLTKGRGSFSMEFSGYQ 79


                  ....*.
gi 75756276   848 IVPGYP 853
Cdd:pfam00679  80 PVPGDI 85
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 75-203 4.25e-05

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: 47.35  E-value: 4.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  75 QIRTISVAGSINSGKSSfLTSIISFNSpylkDSIYKHMRTDE-----DIM------KTTIimTPLLKSIR-KNNKYNtyy 142
Cdd:COG0480   8 KIRNIGIVAHIDAGKTT-LTERILFYT----GAIHRIGEVHDgntvmDWMpeeqerGITI--TSAATTCEwKGHKIN--- 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75756276 143 FLDTPGHSNLFQDFNLALCISDGVIITIDSIEGVTLQTKKIINSClyTKKKI--FILITKIDR 203
Cdd:COG0480  78 IIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQA--DKYGVprIVFVNKMDR 138
EFG_C smart00838
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ...
 769-850 6.67e-05

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: 42.11  E-value: 6.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276    769 ILEPYSEIEVVTPFEsskMIFNI---LLNRRAIILnDMPIQGTLHyRILFLIPTINTIGLETDIRYHTQGQSLIIGFFKG 845
Cdd:smart00838   1 LLEPIMKVEVTVPEE---YMGDVigdLNSRRGKIE-GMEQRGGAQ-VIKAKVPLSEMFGYATDLRSATQGRATWSMEFSH 75


                   ....*
gi 75756276    846 WYIVP 850
Cdd:smart00838  76 YEEVP 80
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 79-202 3.03e-04

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


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 42.36  E-value: 3.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276    79 ISVAGSINSGKSSfLTSIISFNspylKDSI--YKHMRTDEDIMKttiimtpllkSIRKNNKYNTYYFLDTPGH------- 149
Cdd:TIGR00231   4 IVIVGHPNVGKST-LLNSLLGN----KGSIteYYPGTTRNYVTT----------VIEEDGKTYKFNLLDTAGQedydair 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 75756276   150 SNLFQDFNLALCISDGVIITIDSIEGVTLQTKKIINSCLYtKKKIFILITKID 202
Cdd:TIGR00231  69 RLYYPQVERSLRVFDIVILVLDVEEILEKQTKEIIHHADS-GVPIILVGNKID 120
 
Name Accession Description Interval E-value
PTZ00416 PTZ00416
elongation factor 2; Provisional
 60-883 9.95e-46

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 177.16  E-value: 9.95e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276   60 SIDEffIYKMIDNERQIRTISVAGSINSGKSSFLTS------IISFNSPylKDSIYKHMRTDEDIMKTTIimtpllKS-- 131
Cdd:PTZ00416   5 TVDQ--IREIMDNPDQIRNMSVIAHVDHGKSTLTDSlvckagIISSKNA--GDARFTDTRADEQERGITI------KStg 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  132 --------IRKNNKYNTYYF--LDTPGHSNLFQDFNLALCISDGVIITIDSIEGVTLQTKKIINSCLYTKKKIFILITKI 201
Cdd:PTZ00416  75 islyyehdLEDGDDKQPFLInlIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  202 DRLISELRLPPSTFYDKIQSIIFDVNLIIKNSNKKQ--DY-FSFSKSNIGILSAEIGLFLTSEILNKLYHSIYPTIFKLF 278
Cdd:PTZ00416 155 DRAILELQLDPEEIYQNFVKTIENVNVIIATYNDELmgDVqVYPEKGTVAFGSGLQGWAFTLTTFARIYAKKFGVEESKM 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  279 FPKEWiwhTENFIVGKNilKSNPKEPGSHNPIIFFAIIPI------YKLYSFCLSENPLKIMQFIHKTNFSNTLLNLNFP 352
Cdd:PTZ00416 235 MERLW---GDNFFDAKT--KKWIKDETNAQGKKLKRAFCQfildpiCQLFDAVMNEDKEKYDKMLKSLNISLTGEDKELT 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  353 LKNLMKFVFKSVFDYPQSTYEKFSEYFESSKHLNQLFTNsmskqsskkssifshtaknHFYDKYMEKKVFLGI------- 425
Cdd:PTZ00416 310 GKPLLKAVMQKWLPAADTLLEMIVDHLPSPKEAQKYRVE-------------------NLYEGPMDDEAANAIrncdpng 370

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  426 -------KFFPNSYGKKFLLFGRILNGKIVN---------------NDSLYAKNfnnivhnfkINHFFLINCFQLKRIKS 483
Cdd:PTZ00416 371 plmmyisKMVPTSDKGRFYAFGRVFSGTVATgqkvriqgpnyvpgkKEDLFEKN---------IQRTVLMMGRYVEQIED 441

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  484 IKKGN-CLVIEENNNLNEIPILITEESkvyesnPFIDKNLLKNTYP-LKITIEPAYSMDLTKLLSGIQKYLKTSKNTIAS 561
Cdd:PTZ00416 442 VPCGNtVGLVGVDQYLVKSGTITTSET------AHNIRDMKYSVSPvVRVAVEPKNPKDLPKLVEGLKRLAKSDPLVVCT 515

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  562 VQESGTVQISGIGEFALNLMIKEICDFFSLLKVKVSNPFISLKETIECSSkfkSISIAQKS-----RIYM--EIMTEKIN 634
Cdd:PTZ00416 516 TEESGEHIVAGCGELHVEICLKDLEDDYANIDIIVSDPVVSYRETVTEES---SQTCLSKSpnkhnRLYMkaEPLTEELA 592

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  635 LIKEKNEITKKYlsyQNDEMKHFYTQEYIMEKvkisNLSNNLWSYQVHDGFLNILSEyKTSynDKQILK-IRSTLIKAFL 713
Cdd:PTZ00416 593 EAIEEGKVGPED---DPKERANFLADKYEWDK----NDARKIWCFGPENKGPNVLVD-VTK--GVQYMNeIKDSCVSAFQ 662

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  714 MACRTGPICMEPVVNINFAIQEIK-SIEKIQ----QIfkkeISSCmKKLCHSSILISTPRILEPYSEIEVVTPFESSKMI 788
Cdd:PTZ00416 663 WATKEGVLCDENMRGIRFNILDVTlHADAIHrgagQI----IPTA-RRVFYACELTASPRLLEPMFLVDITAPEDAMGGI 737

                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  789 FNILLNRRAIILNDMPIQGTLHYRILFLIPTINTIGLETDIRYHTQGQSLIIGFFKGWYIVPGYPISnqnnikKNNIAHN 868
Cdd:PTZ00416 738 YSVLNRRRGVVIGEEQRPGTPLSNIKAYLPVAESFGFTAALRAATSGQAFPQCVFDHWQVVPGDPLE------PGSKANE 811

                        890
                 ....*....|....*
gi 75756276  869 YMKKIRRKKGMSEKI 883
Cdd:PTZ00416 812 IVLSIRKRKGLKPEI 826
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 78-256 3.53e-38

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


Pssm-ID: 206647 [Multi-domain]  Cd Length: 183  Bit Score: 140.51  E-value: 3.53e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  78 TISVAGSINSGKSSFLTSIISFNSPYLKDSIYK----HMRTDEDIMKTTIIMTPLLKSIRKNNkyntYYFLDTPGHSNLF 153
Cdd:cd00881   1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKetflDTLKEERERGITIKTGVVEFEWPKRR----INFIDTPGHEDFS 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276 154 QDFNLALCISDGVIITIDSIEGVTLQTKKIINSCLYTKKKIFILITKIDRLIselrlpPSTFYDKIQSIIFDVNLIIKNs 233
Cdd:cd00881  77 KETVRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVG------EEDFDEVLREIKELLKLIGFT- 149

                       170       180
                ....*....|....*....|...
gi 75756276 234 nkkqdYFSFSKSNIGILSAEIGL 256
Cdd:cd00881 150 -----FLKGKDVPIIPISALTGE 167
PLN00116 PLN00116
translation elongation factor EF-2 subunit; Provisional
 60-883 3.56e-36

translation elongation factor EF-2 subunit; Provisional


Pssm-ID: 177730 [Multi-domain]  Cd Length: 843  Bit Score: 147.56  E-value: 3.56e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276   60 SIDEffIYKMIDNERQIRTISVAGSINSGKSSFLTS------IISFNSPylKDSIYKHMRTDED----IMKTTII----- 124
Cdd:PLN00116   5 TAEE--LRRIMDKKHNIRNMSVIAHVDHGKSTLTDSlvaaagIIAQEVA--GDVRMTDTRADEAergiTIKSTGIslyye 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  125 MTP-LLKSIRKNNKYNTYY--FLDTPGHSNLFQDFNLALCISDGVIITIDSIEGVTLQTKKIINSCLYTKKKIFILITKI 201
Cdd:PLN00116  81 MTDeSLKDFKGERDGNEYLinLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTETVLRQALGERIRPVLTVNKM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  202 DRLISELRLPPSTFYDKIQSIIFDVNLIIKNSNKK--QDYFSFSKSNIGILSAeiGL----FLTSEIlNKLYHSIYPTIF 275
Cdd:PLN00116 161 DRCFLELQVDGEEAYQTFSRVIENANVIMATYEDPllGDVQVYPEKGTVAFSA--GLhgwaFTLTNF-AKMYASKFGVDE 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  276 KLFFPKEWiwhTENFI--VGKNILKSNPKEPGSHNPIIFFAIIPIYKLYSFCLSENPLKIMQFIHKtnFSNTLLNLNFPL 353
Cdd:PLN00116 238 SKMMERLW---GENFFdpATKKWTTKNTGSPTCKRGFVQFCYEPIKQIINTCMNDQKDKLWPMLEK--LGVTLKSDEKEL 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  354 --KNLMKFVFKSVFDYPQSTYEKFSEYFESSkhlnqlftnsmskqsskkssifsHTAKNH----FYDKYMEKKVFLGI-- 425
Cdd:PLN00116 313 mgKALMKRVMQTWLPASDALLEMIIFHLPSP-----------------------AKAQRYrvenLYEGPLDDKYATAIrn 369

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  426 ------------KFFPNSYGKKFLLFGRILNGKIVN---------------NDSLYAKNFNNIVhnfkinhffLINCFQL 478
Cdd:PLN00116 370 cdpngplmlyvsKMIPASDKGRFFAFGRVFSGTVATgmkvrimgpnyvpgeKKDLYVKSVQRTV---------IWMGKKQ 440

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  479 KRIKSIKKGN-CLVIEENNNLNEIPILITEEskvyESNPFIDKNLLKNTYPL-KITIEPAYSMDLTKLLSGIQKYLKTSK 556
Cdd:PLN00116 441 ESVEDVPCGNtVAMVGLDQFITKNATLTNEK----EVDAHPIKAMKFSVSPVvRVAVQCKNASDLPKLVEGLKRLAKSDP 516

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  557 NTIASVQESGTVQISGIGEFALnlmikEIC------DFFSLLKVKVSNPFISLKETIE------CSSKfksiSIAQKSRI 624
Cdd:PLN00116 517 MVQCTIEESGEHIIAGAGELHL-----EIClkdlqdDFMGGAEIKVSDPVVSFRETVLekscrtVMSK----SPNKHNRL 587

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  625 YMEI--MTEKINLIKEKNEITKKylsyqnDEMK---HFYTQEYIMEKvkisNLSNNLWSYQVHDGFLNILSEYKTSYNdk 699
Cdd:PLN00116 588 YMEArpLEEGLAEAIDDGRIGPR------DDPKirsKILAEEFGWDK----DLAKKIWCFGPETTGPNMVVDMCKGVQ-- 655

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  700 QILKIRSTLIKAFLMACRTGPICMEPVVNINFAIQEI----KSIEK-IQQIfkkeISSCmKKLCHSSILISTPRILEPYS 774
Cdd:PLN00116 656 YLNEIKDSVVAGFQWATKEGALAEENMRGICFEVCDVvlhaDAIHRgGGQI----IPTA-RRVIYASQLTAKPRLLEPVY 730

                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  775 EIEVVTPFESSKMIFNILLNRRAIILNDMPIQGTLHYRILFLIPTINTIGLETDIRYHTQGQSLIIGFFKGWYIVPGYPI 854
Cdd:PLN00116 731 LVEIQAPEQALGGIYSVLNQKRGHVFEEMQRPGTPLYNIKAYLPVIESFGFSGTLRAATSGQAFPQCVFDHWDMMSSDPL 810

                        890       900
                 ....*....|....*....|....*....
gi 75756276  855 SnqnnikKNNIAHNYMKKIRRKKGMSEKI 883
Cdd:PLN00116 811 E------AGSQAAQLVADIRKRKGLKEQM 833
eEF2_C_snRNP cd04098
eEF2_C_snRNP: This family includes a C-terminal portion of the spliceosomal human 116kD U5 ...
 771-850 3.60e-35

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: 128.13  E-value: 3.60e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276 771 EPYSEIEVVTPFESSKMIFNILLNRRAIILNDMPIQGTLHYRILFLIPTINTIGLETDIRYHTQGQSLIIGFFKGWYIVP 850
Cdd:cd04098   1 EPIYEVEITCPADAVSAVYEVLSRRRGHVIYDTPIPGTPLYEVKAFIPVIESFGFETDLRVHTQGQAFCQSVFDHWQIVP 80
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
 77-267 1.22e-32

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


Pssm-ID: 206730 [Multi-domain]  Cd Length: 213  Bit Score: 125.84  E-value: 1.22e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  77 RTISVAGSINSGKSSFLTSIISFNSPYLKDSI-------YKHMRTDEDIMKTTIIMTPLlKSIRKNNKYNTYYF--LDTP 147
Cdd:cd04167   1 RNVCIAGHLHHGKTSLLDMLIEQTHKRTPSVKlgwkplrYTDTRKDEQERGISIKSNPI-SLVLEDSKGKSYLIniIDTP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276 148 GHSNLFQDFNLALCISDGVIITIDSIEGVTLQTKKIINSCLYTKKKIFILITKIDRLISELRLPPSTFYDKIQSIIFDVN 227
Cdd:cd04167  80 GHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDRLILELKLPPTDAYYKLRHTIDEIN 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 75756276 228 LIIKNSNKKQDY-FSFSKSNIGILSAEIGLFLTSEILNKLY 267
Cdd:cd04167 160 NYIASFSTTEGFlVSPELGNVLFASSKFGFCFTLESFAKKY 200
eEF2_snRNP_like_C cd04096
eEF2_snRNP_like_C: this family represents a C-terminal domain of eukaryotic elongation factor ...
 771-850 2.28e-25

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: 100.31  E-value: 2.28e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276 771 EPYSEIEVVTPFESSKMIFNILLNRRAIILNDMPIQGTLHYRILFLIPTINTIGLETDIRYHTQGQSLIIGFFKGWYIVP 850
Cdd:cd04096   1 EPIYLVEIQCPEDALGKVYSVLSKRRGHVLSEEPKEGTPLFEIKAYLPVIESFGFETDLRSATSGQAFPQLVFSHWEIVP 80
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
 77-252 4.95e-17

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


Pssm-ID: 206672 [Multi-domain]  Cd Length: 218  Bit Score: 80.74  E-value: 4.95e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  77 RTISVAGSINSGKSSFLTSIISFNSPYLKDSIYK--HMRTDED------IMKTTII--MTPLLKSIRKNNKY--NtyyFL 144
Cdd:cd01885   1 RNICIIAHVDHGKTTLSDSLLASAGIISEKLAGKarYLDTREDeqergiTIKSSAIslYFEYEEEKMDGNDYliN---LI 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276 145 DTPGHSNLFQDFNLALCISDGVIITIDSIEGVTLQTKKIINSCLYTKKKIFILITKIDRLISELRLPPSTFYDKIQSIIF 224
Cdd:cd01885  78 DSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDRLILELKLSPEEAYQRLLRIVE 157

                       170       180       190
                ....*....|....*....|....*....|...
gi 75756276 225 DVNLIIK---NSNKKQD--YFSFSKSNIGILSA 252
Cdd:cd01885 158 DVNAIIEtyaPEEFKQEkwKFSPQKGNVAFGSA 190
PRK07560 PRK07560
elongation factor EF-2; Reviewed
 531-883 3.43e-16

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 83.37  E-value: 3.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  531 ITIEPAYSMDLTKLLSGIQKYLK---TSKNTIAsvQESGTVQISGIGEFALNLMIKEICDFFSLlKVKVSNPFISLKETI 607
Cdd:PRK07560 393 VAIEAKNPKDLPKLIEVLRQLAKedpTLVVKIN--EETGEHLLSGMGELHLEVITYRIKRDYGI-EVVTSEPIVVYRETV 469

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  608 -ECSSKFKSISIAQKSRIYMEI--MTEK-INLIKEkNEITKKylsyqNDEMKHFYTQEYIMEKVKISNLSNNLWSYQVHD 683
Cdd:PRK07560 470 rGKSQVVEGKSPNKHNRFYISVepLEEEvIEAIKE-GEISED-----MDKKEAKILREKLIEAGMDKDEAKRVWAIYNGN 543

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  684 GFLNilseyKTSynDKQILK-IRSTLIKAFLMACRTGPICMEPVVNINFAIQEIKSIEKI-----QQIFkkeisSCMKKL 757
Cdd:PRK07560 544 VFID-----MTK--GIQYLNeVMELIIEGFREAMKEGPLAAEPVRGVKVRLHDAKLHEDAihrgpAQVI-----PAVRNA 611

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  758 CHSSILISTPRILEPYSEIEVVTPFESSKMIFNILLNRRAIILnDMPIQGTLhYRILFLIPTINTIGLETDIRYHTQGQS 837
Cdd:PRK07560 612 IFAAMLTAKPTLLEPIQKVDINVPQDYMGAVTREIQGRRGKIL-DMEQEGDM-AIIEAEAPVAEMFGFAGEIRSATEGRA 689

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 75756276  838 LIIGFFKGWYIVPgypisnqnnikkNNIAHNYMKKIRRKKGMSEKI 883
Cdd:PRK07560 690 LWSTEFAGFEPVP------------DSLQLDIVRQIRERKGLKPEL 723
aeEF2_snRNP_like_IV cd01681
This family represents domain IV of archaeal and eukaryotic elongation factor 2 (aeEF-2) and ...
 599-773 8.70e-15

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: 73.37  E-value: 8.70e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276 599 PFISLKETIECSS--KFKSISIAQKSRIYMEI--MTEKINLIKEKNEITKKylSYQNDEMKHFyTQEYIMEKvkisNLSN 674
Cdd:cd01681   2 PVVSFRETVVETSsgTCLAKSPNKHNRLYMRAepLPEELIEDIEKGKITLK--DDKKKRARIL-LDKYGWDK----LAAR 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276 675 NLWSYQVHDGFLNIL-SEYKTSYNDKQIL-KIRSTLIKAFLMACRTGPICMEPVVNINFAIQEIKSIEKIQQIFKKEISS 752
Cdd:cd01681  75 KIWAFGPDRTGPNILvDDTKGVQYDKSLLnEIKDSIVAGFQWATKEGPLCEEPMRGVKFKLEDATLHADAIHRGGGQIIP 154

                       170       180
                ....*....|....*....|.
gi 75756276 753 CMKKLCHSSILISTPRILEPY 773
Cdd:cd01681 155 AARRACYAAFLLASPRLMEPM 175
EFG_C pfam00679
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ...
 768-853 7.19e-13

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: 64.87  E-value: 7.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276   768 RILEPYSEIEVVTPFESSKMIFNILLNRRAIILNDMPIQGTLHyRILFLIPTINTIGLETDIRYHTQGQSLIIGFFKGWY 847
Cdd:pfam00679   1 VLLEPIEKVTIDVPEEYVGDVISDLNSRRGEILDMDPDDGGRV-VIEAEVPLAELFGFATELRSLTKGRGSFSMEFSGYQ 79


                  ....*.
gi 75756276   848 IVPGYP 853
Cdd:pfam00679  80 PVPGDI 85
EF2_IV_snRNP cd01683
EF-2_domain IV_snRNP domain is a part of 116kD U5-specific protein of the U5 small ...
 599-776 8.24e-13

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: 67.70  E-value: 8.24e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276 599 PFISLKETIECSSKFKSISIAQ--KSRIYM--EIMTEKINLIKEKNEITkkyLSYQNDEMKHFYTQEYIMEKVKisnlSN 674
Cdd:cd01683   2 PVVTFCETVVETSSAKCFAETPnkKNKITMiaEPLDKGLAEDIENGQLK---LSWNRKKLGKFLRTKYGWDALA----AR 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276 675 NLWSYQVHDGFLNIL------SEYktsynDKQIL-KIRSTLIKAFLMACRTGPICMEPVVNINFAIQEIKSIEKIQQIFK 747
Cdd:cd01683  75 SIWAFGPDTKGPNVLiddtlpEEV-----DKNLLnSVKESIVQGFQWAVREGPLCEEPIRNVKFKLLDADIASEPIDRGG 149

                       170       180
                ....*....|....*....|....*....
gi 75756276 748 KEISSCMKKLCHSSILISTPRILEPYSEI 776
Cdd:cd01683 150 GQIIPTARRACYSAFLLATPRLMEPIYEV 178
Elongation_Factor_C cd01514
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ...
 771-850 2.74e-12

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: 62.88  E-value: 2.74e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276 771 EPYSEIEVVTPFESSKMIFNILLNRRAIILNDMPIqGTLHYRILFLIPTINTIGLETDIRYHTQGQSLIIGFFKGWYIVP 850
Cdd:cd01514   1 EPIMKVEITVPEEYLGAVIGDLSKRRGEILGMEPR-GTGRVVIKAELPLAEMFGFATDLRSLTQGRASFSMEFSHYEPVP 79
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 75-219 2.92e-12

Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.


Pssm-ID: 425418 [Multi-domain]  Cd Length: 187  Bit Score: 66.01  E-value: 2.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276    75 QIRTISVAGSINSGKSSFLTSIISfnspYLKDSIYKHMRTDE-----DIMKT------TI------IMTpllksirKNNK 137
Cdd:pfam00009   2 RHRNIGIIGHVDHGKTTLTDRLLY----YTGAISKRGEVKGEgeaglDNLPEerergiTIksaavsFET-------KDYL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276   138 YNtyyFLDTPGHsnlfQDFN------LALCisDGVIITIDSIEGVTLQTKKIINSCLYTKKKIFILITKIDRL-ISELRL 210
Cdd:pfam00009  71 IN---LIDTPGH----VDFVkevirgLAQA--DGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVdGAELEE 141


                  ....*....
gi 75756276   211 PPSTFYDKI 219
Cdd:pfam00009 142 VVEEVSREL 150
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 81-204 6.73e-08

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 52.84  E-value: 6.73e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  81 VAGSINSGKSSFLTSIisfnspylkdsIYKHMRTDEDIMKTTIimTPLLKSIRKNNKYNTYYFLDTPGH-----SNLFQD 155
Cdd:cd00882   2 VVGRGGVGKSSLLNAL-----------LGGEVGEVSDVPGTTR--DPDVYVKELDKGKVKLVLVDTPGLdefggLGREEL 68

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 75756276 156 FNLALCISDGVIITIDSIEGVTL--QTKKIINSCLYTKKKIFILITKIDRL 204
Cdd:cd00882  69 ARLLLRGADLILLVVDSTDRESEedAKLLILRRLRKEGIPIILVGNKIDLL 119
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
 78-203 1.02e-06

Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.


Pssm-ID: 206733 [Multi-domain]  Cd Length: 268  Bit Score: 51.05  E-value: 1.02e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  78 TISVAGSINSGKSS------FLTSIIS-FNSPYLKDSIYKHmrTDEDI-MKTTIIMTPLlksirkNNKYNTY--YFLDTP 147
Cdd:cd04170   1 NIALVGHSGSGKTTlaeallYATGAIDrLGRVEDGNTVSDY--DPEEKkRKMSIETSVA------PLEWNGHkiNLIDTP 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 75756276 148 GHSNLFQDFNLALCISDGVIITIDSIEGVTLQTKKIINSCLYTKKKIFILITKIDR 203
Cdd:cd04170  73 GYADFVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDR 128
PRK13351 PRK13351
elongation factor G-like protein;
75-209 1.55e-06

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 51.88  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276   75 QIRTISVAGSINSGKSSFLTSIIsfnspYLKDSIYKHMRTDE-----DIM----KTTIIMTPLLKSIRknnkYNTY--YF 143
Cdd:PRK13351   7 QIRNIGILAHIDAGKTTLTERIL-----FYTGKIHKMGEVEDgttvtDWMpqeqERGITIESAATSCD----WDNHriNL 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75756276  144 LDTPGHSNLFQDFNLALCISDGVIITIDSIEGVTLQTKKIINSCLYTKKKIFILITKIDRLISELR 209
Cdd:PRK13351  78 IDTPGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLF 143
PRK10218 PRK10218
translational GTPase TypA;
69-239 2.43e-05

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 48.17  E-value: 2.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276   69 MIDNerqIRTISVAGSINSGKSSFLTSIISFNSPYLKDSIYKHMRTDEDIMKTTIIMTPLLKSIRKnnKYNTYYF--LDT 146
Cdd:PRK10218   1 MIEK---LRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAI--KWNDYRIniVDT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  147 PGHSNLFQDFNLALCISDGVIITIDSIEGVTLQTKKIINSCLYTKKKIFILITKIDRliselrlpPSTFYDKIQSIIFDV 226
Cdd:PRK10218  76 PGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDR--------PGARPDWVVDQVFDL 147

                        170
                 ....*....|...
gi 75756276  227 NLIIKNSNKKQDY 239
Cdd:PRK10218 148 FVNLDATDEQLDF 160
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
 144-203 2.77e-05

Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity.


Pssm-ID: 206678 [Multi-domain]  Cd Length: 194  Bit Score: 46.05  E-value: 2.77e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75756276 144 LDTPGHSnlfqDFN----LALCISDGVIITIDSIEGVTLQTKKIINSCLYTKKKIFILITKIDR 203
Cdd:cd01891  70 IDTPGHA----DFGgeveRVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDR 129
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 78-200 3.13e-05

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


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 44.15  E-value: 3.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276    78 TISVAGSINSGKSSFLTSIISfnspylkdsiyKHMRTdEDIMKTTIimTPLLKSIRKNNKynTYYFLDTPG-------HS 150
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTG-----------AKAIV-SDYPGTTR--DPNEGRLELKGK--QIILVDTPGliegaseGE 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 75756276   151 NLFQDFnLALCISDGVIITIDSIEGVTLQTKKIINSCLYTKKKIFILITK 200
Cdd:pfam01926  65 GLGRAF-LAIIEADLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
134-203 3.26e-05

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 47.81  E-value: 3.26e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75756276  134 KNNKYNtyyFLDTPGHSNLFQDFNLALCISDGVIITIDSIEGVTLQTKKIINSClyTKKKI--FILITKIDR 203
Cdd:PRK12740  58 KGHKIN---LIDTPGHVDFTGEVERALRVLDGAVVVVCAVGGVEPQTETVWRQA--EKYGVprIIFVNKMDR 124
snRNP_III cd16264
Domain III of the spliceosomal 116kD U5 small nuclear ribonucleoprotein (snRNP) component; ...
 529-598 4.16e-05

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: 42.49  E-value: 4.16e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276 529 LKITIEPAYSMDLTKLLSGIQKYLKTSKNTIASVQESGTVQISGIGEFALNLMIKEICDFFSLLKVKVSN 598
Cdd:cd16264   3 FKIAVEPLNPSELPKMLDGLRKVNKSYPLLITKVEESGEHVILGTGELYMDCVMHDLRKMYSEIEIKVAD 72
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 75-203 4.25e-05

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: 47.35  E-value: 4.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  75 QIRTISVAGSINSGKSSfLTSIISFNSpylkDSIYKHMRTDE-----DIM------KTTIimTPLLKSIR-KNNKYNtyy 142
Cdd:COG0480   8 KIRNIGIVAHIDAGKTT-LTERILFYT----GAIHRIGEVHDgntvmDWMpeeqerGITI--TSAATTCEwKGHKIN--- 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75756276 143 FLDTPGHSNLFQDFNLALCISDGVIITIDSIEGVTLQTKKIINSClyTKKKI--FILITKIDR 203
Cdd:COG0480  78 IIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQA--DKYGVprIVFVNKMDR 138
RF3 cd04169
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ...
 138-203 4.33e-05

Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.


Pssm-ID: 206732 [Multi-domain]  Cd Length: 268  Bit Score: 46.05  E-value: 4.33e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75756276 138 YNTYYF--LDTPGHSNLFQDFNLALCISDGVIITIDSIEGVTLQTKKIINSCLYTKKKIFILITKIDR 203
Cdd:cd04169  68 YKGCVInlLDTPGHEDFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDR 135
EFG_C smart00838
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ...
 769-850 6.67e-05

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: 42.11  E-value: 6.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276    769 ILEPYSEIEVVTPFEsskMIFNI---LLNRRAIILnDMPIQGTLHyRILFLIPTINTIGLETDIRYHTQGQSLIIGFFKG 845
Cdd:smart00838   1 LLEPIMKVEVTVPEE---YMGDVigdLNSRRGKIE-GMEQRGGAQ-VIKAKVPLSEMFGYATDLRSATQGRATWSMEFSH 75


                   ....*
gi 75756276    846 WYIVP 850
Cdd:smart00838  76 YEEVP 80
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 79-202 3.03e-04

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


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 42.36  E-value: 3.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276    79 ISVAGSINSGKSSfLTSIISFNspylKDSI--YKHMRTDEDIMKttiimtpllkSIRKNNKYNTYYFLDTPGH------- 149
Cdd:TIGR00231   4 IVIVGHPNVGKST-LLNSLLGN----KGSIteYYPGTTRNYVTT----------VIEEDGKTYKFNLLDTAGQedydair 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 75756276   150 SNLFQDFNLALCISDGVIITIDSIEGVTLQTKKIINSCLYtKKKIFILITKID 202
Cdd:TIGR00231  69 RLYYPQVERSLRVFDIVILVLDVEEILEKQTKEIIHHADS-GVPIILVGNKID 120
EF2_snRNP_III cd16261
Domain III of Elongation Factor 2 (EF2); This model represents domain III of Elongation factor ...
 529-597 6.24e-04

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: 39.09  E-value: 6.24e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75756276 529 LKITIEPAYSMDLTKLLSGIQKYLKTSKNTIASVQESGTVQISGIGEFALNLMIKEICDFFSLLKVKVS 597
Cdd:cd16261   3 VRVAVEPKNPSDLPKLVEGLKKLAKSDPTVQVKIEEEGEHLIAGAGELHLEICLKDLKEDFAGIEIKVS 71
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 143-204 1.41e-03

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


Pssm-ID: 206674 [Multi-domain]  Cd Length: 169  Bit Score: 40.53  E-value: 1.41e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75756276 143 FLDTPGH---SNL-FQDFNLAlcisDGVIITIDSIEGVTLQTKKIINSCLYTKKKIFILITKIDRL 204
Cdd:cd01887  53 FIDTPGHeafTNMrARGASVT----DIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKP 114
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 81-204 2.32e-03

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


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 39.54  E-value: 2.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756276  81 VAGSINSGKSSFLTSIIsfNSPYLKDSiykhmrtdeDIMKTTiiMTPLLKSIRKNNKYNtYYFLDTPG-------HSNLF 153
Cdd:cd00880   2 IFGRPNVGKSSLLNALL--GQNVGIVS---------PIPGTT--RDPVRKEWELLPLGP-VVLIDTPGldeegglGRERV 67

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 75756276 154 QDFNLALCISDGVIITIDSIEGVTLQTKKIINScLYTKKKIFILITKIDRL 204
Cdd:cd00880  68 EEARQVADRADLVLLVVDSDLTPVEEEAKLGLL-RERGKPVLLVLNKIDLV 117
 
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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