|
Name |
Accession |
Description |
Interval |
E-value |
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
1-605 |
0e+00 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 1257.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 1 MIEKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHAD 80
Cdd:COG1217 2 MREDIRNIAIIAHVDHGKTTLVDALLKQSGTFRENQEVAERVMDSNDLERERGITILAKNTAVRYKGVKINIVDTPGHAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 81 FGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDF 160
Cdd:COG1217 82 FGGEVERVLSMVDGVLLLVDAFEGPMPQTRFVLKKALELGLKPIVVINKIDRPDARPDEVVDEVFDLFIELGATDEQLDF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 161 PIVYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTII 240
Cdd:COG1217 162 PVVYASARNGWASLDLDDPGEDLTPLFDTILEHVPAPEVDPDGPLQMLVTNLDYSDYVGRIAIGRIFRGTIKKGQQVALI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 241 DSEGKTRNAKVGKVLGHLGLERIETDLAEAGDIVAITGLGELNISDTVCDTQNVEALPALSVDEPTVSMFFCVNTSPFCG 320
Cdd:COG1217 242 KRDGKVEKGKITKLFGFEGLERVEVEEAEAGDIVAIAGIEDINIGDTICDPENPEALPPIKIDEPTLSMTFSVNDSPFAG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 321 KEGKFVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRREGFELAVSRPKVIFREIDGRKQEPY 400
Cdd:COG1217 322 REGKFVTSRQIRERLEKELETNVALRVEETDSPDAFKVSGRGELHLSILIETMRREGYELQVSRPEVIFKEIDGKKLEPI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 401 ENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDVRpGEV 480
Cdd:COG1217 402 EELTIDVPEEYSGAVIEKLGQRKGEMTNMEPDGGGRVRLEFLIPSRGLIGFRTEFLTDTRGTGIMNHVFDGYEPYK-GEI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 481 GQRQNGVLISNGQGKAVAFALFGLQDRGKLFLGHGAEVYEGQIIGIHSRSNDLTVNCLTGKKLTNMRASGTDEAVVLVPP 560
Cdd:COG1217 481 PGRRNGSLISMETGKATAYALFNLQERGTLFIGPGTEVYEGMIVGEHSRDNDLVVNVCKEKKLTNMRASGSDEAIRLTPP 560
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 49176434 561 IRMTLEQALEFIDDDELVEVTPTSIRIRKRHLTENDRRRANRAPK 605
Cdd:COG1217 561 RKMSLEQALEFIEDDELVEVTPKSIRLRKKILDENERKRAAKKKK 605
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
1-607 |
0e+00 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 1195.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 1 MIEKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHAD 80
Cdd:PRK10218 1 MIEKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 81 FGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDF 160
Cdd:PRK10218 81 FGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 161 PIVYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTII 240
Cdd:PRK10218 161 PIVYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTII 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 241 DSEGKTRNAKVGKVLGHLGLERIETDLAEAGDIVAITGLGELNISDTVCDTQNVEALPALSVDEPTVSMFFCVNTSPFCG 320
Cdd:PRK10218 241 DSEGKTRNAKVGKVLGHLGLERIETDLAEAGDIVAITGLGELNISDTVCDTQNVEALPALSVDEPTVSMFFCVNTSPFCG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 321 KEGKFVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRREGFELAVSRPKVIFREIDGRKQEPY 400
Cdd:PRK10218 321 KEGKFVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRREGFELAVSRPKVIFREIDGRKQEPY 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 401 ENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDVRPGEV 480
Cdd:PRK10218 401 ENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDVRPGEV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 481 GQRQNGVLISNGQGKAVAFALFGLQDRGKLFLGHGAEVYEGQIIGIHSRSNDLTVNCLTGKKLTNMRASGTDEAVVLVPP 560
Cdd:PRK10218 481 GQRQNGVLISNGQGKAVAFALFGLQDRGKLFLGHGAEVYEGQIIGIHSRSNDLTVNCLTGKKLTNMRASGTDEAVVLVPP 560
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 49176434 561 IRMTLEQALEFIDDDELVEVTPTSIRIRKRHLTENDRRRANRAPKDD 607
Cdd:PRK10218 561 IRMTLEQALEFIDDDELVEVTPTSIRIRKRHLTENDRRRANRAPKDD 607
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
5-599 |
0e+00 |
|
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, a GTP-binding protein, is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways, but the precise function is unknown. [Regulatory functions, Other, Cellular processes, Adaptations to atypical conditions, Protein synthesis, Translation factors]
Pssm-ID: 273597 [Multi-domain] Cd Length: 594 Bit Score: 1061.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 5 LRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGE 84
Cdd:TIGR01394 1 IRNIAIIAHVDHGKTTLVDALLKQSGTFRANEAVAERVMDSNDLERERGITILAKNTAIRYNGTKINIVDTPGHADFGGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 85 VERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDFPIVY 164
Cdd:TIGR01394 81 VERVLGMVDGVLLLVDASEGPMPQTRFVLKKALELGLKPIVVINKIDRPSARPDEVVDEVFDLFAELGADDEQLDFPIVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 165 ASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIIDSEG 244
Cdd:TIGR01394 161 ASGRAGWASLDLDDPSDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVHRGTVKKGQQVALMKRDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 245 KTRNAKVGKVLGHLGLERIETDLAEAGDIVAITGLGELNISDTVCDTQNVEALPALSVDEPTVSMFFCVNTSPFCGKEGK 324
Cdd:TIGR01394 241 TIENGRISKLLGFEGLERVEIDEAGAGDIVAVAGLEDINIGETIADPEVPEALPTITVDEPTLSMTFSVNDSPLAGKEGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 325 FVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRREGFELAVSRPKVIFREIDGRKQEPYENVT 404
Cdd:TIGR01394 321 KVTSRHIRDRLMRELETNVALRVEDTESADKFEVSGRGELHLSILIETMRREGFELQVGRPQVIYKEIDGKKLEPIEELT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 405 LDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDVRpGEVGQRQ 484
Cdd:TIGR01394 401 IDVPEEHVGAVIEKLGKRKGEMVDMEPSGNGRTRLEFKIPSRGLIGFRTEFLTDTRGTGIMNHVFDEYEPWK-GEIETRR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 485 NGVLISNGQGKAVAFALFGLQDRGKLFLGHGAEVYEGQIIGIHSRSNDLTVNCLTGKKLTNMRASGTDEAVVLVPPIRMT 564
Cdd:TIGR01394 480 NGSLVSMEDGTATAYALWNLQERGVMFVSPGTEVYEGMIIGEHSRENDLDVNPCKAKKLTNVRSSGKDEAVKLTPPRKLS 559
|
570 580 590
....*....|....*....|....*....|....*
gi 49176434 565 LEQALEFIDDDELVEVTPTSIRIRKRHLTENDRRR 599
Cdd:TIGR01394 560 LEQALEYIEDDELVEVTPKSIRLRKRVLDPNERKR 594
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
4-197 |
4.08e-136 |
|
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: 394.65 E-value: 4.08e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 4 KLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGG 83
Cdd:cd01891 1 KIRNIAIIAHVDHGKTTLVDALLKQSGTFRENEEVGERVMDSNDLERERGITILAKNTAITYKDTKINIIDTPGHADFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 84 EVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDFPIV 163
Cdd:cd01891 81 EVERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDRPDARPEEVVDEVFDLFLELNATDEQLDFPIV 160
|
170 180 190
....*....|....*....|....*....|....
gi 49176434 164 YASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAP 197
Cdd:cd01891 161 YASAKNGWASLNLDDPSEDLDPLFETIIEHVPAP 194
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
3-196 |
1.42e-74 |
|
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: 236.27 E-value: 1.42e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 3 EKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAE---TQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHA 79
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEvkgEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 80 DFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRP-GARPDWVVDQVFDLFVNLDATDEqL 158
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVdGAELEEVVEEVSRELLEKYGEDG-E 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 49176434 159 DFPIVYASALNGIAgldhedmaedMTPLYQAIVDHVPA 196
Cdd:pfam00009 160 FVPVVPGSALKGEG----------VQTLLDALDEYLPS 187
|
|
| lepA |
TIGR01393 |
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a ... |
3-479 |
1.22e-69 |
|
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a GTP-binding membrane protein related to EF-G and EF-Tu. Two types of phylogenetic tree, rooted by other GTP-binding proteins, suggest that eukaryotic homologs (including GUF1 of yeast) originated within the bacterial LepA family. The function is unknown. [Unknown function, General]
Pssm-ID: 130460 [Multi-domain] Cd Length: 595 Bit Score: 236.06 E-value: 1.22e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 3 EKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRaETQERVMDSNDLEKERGITILAKNTAIKW-----NDYRINIVDTPG 77
Cdd:TIGR01393 1 KNIRNFSIIAHIDHGKSTLADRLLEYTGAISER-EMREQVLDSMDLERERGITIKAQAVRLNYkakdgETYVLNLIDTPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 78 HADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLfVNLDATDeq 157
Cdd:TIGR01393 80 HVDFSYEVSRSLAACEGALLLVDAAQGIEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKKEIEEV-IGLDASE-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 158 ldfpIVYASALNGIaGLDHedmaedmtpLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQV 237
Cdd:TIGR01393 157 ----AILASAKTGI-GIEE---------ILEAIVKRVPPPKGDPDAPLKALIFDSHYDNYRGVVALVRVFEGTIKPGDKI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 238 TIIdSEGKTRNAkvgKVLGHLGLERIETDLAEAGD----IVAITGLGELNISDTVCDTQN--VEALPALSVDEPTV-SMF 310
Cdd:TIGR01393 223 RFM-STGKEYEV---DEVGVFTPKLTKTDELSAGEvgyiIAGIKDVSDVRVGDTITHVKNpaKEPLPGFKEVKPMVfAGL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 311 FCVNTSPFcgkegkfvtsRQILDRLNKELVHNVALRVE-ETEDA--DAFRVSGRGELHLSVLIENMRREgFELAV--SRP 385
Cdd:TIGR01393 299 YPIDTEDY----------EDLRDALEKLKLNDASLTYEpESSPAlgFGFRCGFLGLLHMEIIQERLERE-FNLDLitTAP 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 386 KVIFR---------EIDG-----------RKQEPYENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIP- 444
Cdd:TIGR01393 368 SVIYRvyltngeviEVDNpsdlpdpgkieHVEEPYVKATIITPTEYLGPIMTLCQEKRGVQTNMEYLDPNRVELIYEMPl 447
|
490 500 510
....*....|....*....|....*....|....*.
gi 49176434 445 SRGLIGFRSEFMTMTSGtgllYSTFS-HYDDVRPGE 479
Cdd:TIGR01393 448 AEIVYDFFDKLKSISRG----YASFDyELIGYRPSD 479
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
3-444 |
8.63e-68 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 231.45 E-value: 8.63e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 3 EKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRaETQERVMDSNDLEKERGITILAKNTAIKW-----NDYRINIVDTPG 77
Cdd:COG0481 4 KNIRNFSIIAHIDHGKSTLADRLLELTGTLSER-EMKEQVLDSMDLERERGITIKAQAVRLNYkakdgETYQLNLIDTPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 78 HADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLFvNLDATDeq 157
Cdd:COG0481 83 HVDFSYEVSRSLAACEGALLVVDASQGVEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKQEIEDII-GIDASD-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 158 ldfpIVYASALNGIaGLDHedmaedmtpLYQAIVDHVPAPDVDLDGPFQMQIsqLD--YNSYVGVIGIGRIKRGKVKPNQ 235
Cdd:COG0481 160 ----AILVSAKTGI-GIEE---------ILEAIVERIPPPKGDPDAPLQALI--FDswYDSYRGVVVYVRVFDGTLKKGD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 236 QVTIIdSEGKTrnAKVGKVlGHLGLERIETDLAEAGD---IVA-ITGLGELNISDTVCDTQN--VEALPALsvdEPTVSM 309
Cdd:COG0481 224 KIKMM-STGKE--YEVDEV-GVFTPKMTPVDELSAGEvgyIIAgIKDVRDARVGDTITLAKNpaAEPLPGF---KEVKPM 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 310 FFC----VNTSpfcgkegKFVTSRQILDRLnkELvhNVALRVEETEDADA----FRVSGRGELHLSVLIENMRRE-GFEL 380
Cdd:COG0481 297 VFAglypVDSD-------DYEDLRDALEKL--QL--NDASLTYEPETSAAlgfgFRCGFLGLLHMEIIQERLEREfDLDL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 381 AVSRPKVIFR---------------------EIDgRKQEPYENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRL 439
Cdd:COG0481 366 ITTAPSVVYEvtltdgevievdnpsdlpdpgKIE-EIEEPIVKATIITPSEYVGAVMELCQEKRGVQKNMEYLGENRVEL 444
|
....*
gi 49176434 440 DYVIP 444
Cdd:COG0481 445 TYELP 449
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
3-439 |
8.98e-67 |
|
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]
Pssm-ID: 129581 [Multi-domain] Cd Length: 720 Bit Score: 231.32 E-value: 8.98e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 3 EKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAI----KWNDYRINIVDTPGH 78
Cdd:TIGR00490 17 KFIRNIGIVAHIDHGKTTLSDNLLAGAGMISEELAGQQLYLDFDEQEQERGITINAANVSMvheyEGNEYLINLIDTPGH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 79 ADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQL 158
Cdd:TIGR00490 97 VDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKPVLFINKVDRLINELKLTPQELQERFIKIITEVNKL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 159 ------------------DFPIVYASALNGIA---------GLDHEDMAEDMT-----------PLYQAIVD----HVPA 196
Cdd:TIGR00490 177 ikamapeefrdkwkvrveDGSVAFGSAYYNWAisvpsmkktGIGFKDIYKYCKedkqkelakksPLHQVVLDmvirHLPS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 197 P-------------------------DVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIIDSEGKTRNAKV 251
Cdd:TIGR00490 257 PieaqkyripviwkgdlnsevgkamlNCDPKGPLALMITKIVVDKHAGEVAVGRLYSGTIRPGMEVYIVDRKAKARIQQV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 252 GKvlgHLGLERIETDLAEAGDIVAITGLGELNISDTVCDT-QNVEALPALS-VDEPTVSMFF-CVNTSPFcgkeGKFVts 328
Cdd:TIGR00490 337 GV---YMGPERVEVDEIPAGNIVAVIGLKDAVAGETICTTvENITPFESIKhISEPVVTVAIeAKNTKDL----PKLI-- 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 329 rQILDRLNKElvhNVALRVEETEDADAFRVSGRGELHLSVLIENMRRE-GFELAVSRPKVIFRE--------IDGRKQEP 399
Cdd:TIGR00490 408 -EVLRQVAKE---DPTVHVEINEETGEHLISGMGELHLEIIVEKIREDyGLDVETSPPIVVYREtvtgtspvVEGKSPNK 483
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 49176434 400 YENVTLDVEEQHQgSVMQALGErkGDLKNMNPDGKGRVRL 439
Cdd:TIGR00490 484 HNRFYIVVEPLEE-SVIQAFKE--GKIVDMKMKKKERRRL 520
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
7-197 |
3.91e-64 |
|
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: 208.69 E-value: 3.91e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVE 86
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 87 RVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPG-ARPDWVVDQVFDLFVNLDAT-DEQLDFPIVY 164
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGeEDFDEVLREIKELLKLIGFTfLKGKDVPIIP 160
|
170 180 190
....*....|....*....|....*....|...
gi 49176434 165 ASALNGIagldhedmaeDMTPLYQAIVDHVPAP 197
Cdd:cd00881 161 ISALTGE----------GIEELLDAIVEHLPPP 183
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
2-401 |
1.54e-61 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 217.04 E-value: 1.54e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 2 IEKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAI----KWNDYRINIVDTPG 77
Cdd:PRK07560 17 PEQIRNIGIIAHIDHGKTTLSDNLLAGAGMISEELAGEQLALDFDEEEQARGITIKAANVSMvheyEGKEYLINLIDTPG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 78 HADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDR--------P---GARPDWVVDQVFD 146
Cdd:PRK07560 97 HVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKPVLFINKVDRlikelkltPqemQQRLLKIIKDVNK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 147 LFVN-----------LDATDEQLDFpivyASALNGIA---------GLDHEDM-----AEDM------TPLYQAIVD--- 192
Cdd:PRK07560 177 LIKGmapeefkekwkVDVEDGTVAF----GSALYNWAisvpmmqktGIKFKDIidyyeKGKQkelaekAPLHEVVLDmvv 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 193 -HVPAP-------------------------DVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIIDSEGKT 246
Cdd:PRK07560 253 kHLPNPieaqkyripkiwkgdlnsevgkamlNCDPNGPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLVGAKKKN 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 247 RNAKVGKvlgHLGLERIETDLAEAGDIVAITGLGELNISDTVCDTQNVEALPALS-VDEPTVSMffCV---NTS--Pfcg 320
Cdd:PRK07560 333 RVQQVGI---YMGPEREEVEEIPAGNIAAVTGLKDARAGETVVSVEDMTPFESLKhISEPVVTV--AIeakNPKdlP--- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 321 kegKFVtsrQILDRLNKElvhNVALRVEETEDADAFRVSGRGELHLSVLIENMRRE-GFELAVSRPKVIFREIDGRKQEP 399
Cdd:PRK07560 405 ---KLI---EVLRQLAKE---DPTLVVKINEETGEHLLSGMGELHLEVITYRIKRDyGIEVVTSEPIVVYRETVRGKSQV 475
|
..
gi 49176434 400 YE 401
Cdd:PRK07560 476 VE 477
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
2-391 |
4.76e-59 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 209.42 E-value: 4.76e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 2 IEKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQE--RVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHA 79
Cdd:PRK13351 5 LMQIRNIGILAHIDAGKTTLTERILFYTGKIHKMGEVEDgtTVTDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 80 DFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQ---------------- 143
Cdd:PRK13351 85 DFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLFKVLEDieerfgkrplplqlpi 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 144 --------VFDLFVN----------------------------------LDA------------------TDEQLD---- 159
Cdd:PRK13351 165 gsedgfegVVDLITEpelhfsegdggstveegpipeelleeveeareklIEAlaefddellelylegeelSAEQLRaplr 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 160 --------FPIVYASALNGIAgldhedmaedMTPLYQAIVDHVPAP------------------DVDLDGPFQMQISQLD 213
Cdd:PRK13351 245 egtrsghlVPVLFGSALKNIG----------IEPLLDAVVDYLPSPlevppprgskdngkpvkvDPDPEKPLLALVFKVQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 214 YNSYVGVIGIGRIKRGKVKPNQQVTIIDSEGKTRNAKVGKVLGHlglERIETDLAEAGDIVAITGLGELNISDTVCDTQN 293
Cdd:PRK13351 315 YDPYAGKLTYLRVYSGTLRAGSQLYNGTGGKREKVGRLFRLQGN---KREEVDRAKAGDIVAVAGLKELETGDTLHDSAD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 294 VEALPALSVDEPTVSMffCVntspfcgkEGKFVTSRQ-ILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIEN 372
Cdd:PRK13351 392 PVLLELLTFPEPVVSL--AV--------EPERRGDEQkLAEALEKLVWEDPSLRVEEDEETGQTILSGMGELHLEVALER 461
|
490 500
....*....|....*....|
gi 49176434 373 MRRE-GFELAVSRPKVIFRE 391
Cdd:PRK13351 462 LRREfKLEVNTGKPQVAYRE 481
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
11-483 |
2.22e-55 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 198.81 E-value: 2.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 11 IAHVDHGKTTLVDKLLQQSGTFDSRAETQE--RVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVERV 88
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRIGEVEDgtTTMDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVERA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 89 MSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQV--------------------FDLF 148
Cdd:PRK12740 81 LRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRAGADFFRVLAQLqeklgapvvplqlpigegddFTGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 149 VNL-----------------DATDEQLD------------------------------------------------FPIV 163
Cdd:PRK12740 161 VDLlsmkayrydeggpseeiEIPAELLDraeeareellealaefddelmekylegeelseeeikaglrkatlageiVPVF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 164 YASALNGIAgldhedmaedMTPLYQAIVDHVPAPD-----------------VDLDGPFQMQISQLDYNSYVGVIGIGRI 226
Cdd:PRK12740 241 CGSALKNKG----------VQRLLDAVVDYLPSPLevppvdgedgeegaelaPDPDGPLVALVFKTMDDPFVGKLSLVRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 227 KRGKVKPNQQVTIIDSEGKTRnakVGKVLGHLGLERIETDLAEAGDIVAITGLGELNISDTVCDTQNVEALPALSVDEPT 306
Cdd:PRK12740 311 YSGTLKKGDTLYNSGTGKKER---VGRLYRMHGKQREEVDEAVAGDIVAVAKLKDAATGDTLCDKGDPILLEPMEFPEPV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 307 VSM-FFCVNTspfcGKEGKFVtsrQILDRLNKElvhNVALRVEETEDADAFRVSGRGELHLSVLIENMRRE-GFELAVSR 384
Cdd:PRK12740 388 ISLaIEPKDK----GDEEKLS---EALGKLAEE---DPTLRVERDEETGQTILSGMGELHLDVALERLKREyGVEVETGP 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 385 PKVIFRE-------IDGR--KQ---------------------------------------------------------- 397
Cdd:PRK12740 458 PQVPYREtirkkaeGHGRhkKQsgghgqfgdvwleveplprgegfefvdkvvggavprqyipavekgvrealekgvlagy 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 398 --------------------------------------------EPYENVTLDVEEQHQGSVMQALGERKGDLKNMNPDG 433
Cdd:PRK12740 538 pvvdvkvtltdgsyhsvdssemafkiaarlafrealpkakpvllEPIMKVEVSVPEEFVGDVIGDLSSRRGRILGMESRG 617
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 49176434 434 KG-RVRLDyvIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDVrPGEVGQR 483
Cdd:PRK12740 618 GGdVVRAE--VPLAEMFGYATDLRSLTQGRGSFSMEFSHYEEV-PGNVAEK 665
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
2-391 |
1.90e-54 |
|
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: 196.81 E-value: 1.90e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 2 IEKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQE--RVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHA 79
Cdd:COG0480 6 LEKIRNIGIVAHIDAGKTTLTERILFYTGAIHRIGEVHDgnTVMDWMPEEQERGITITSAATTCEWKGHKINIIDTPGHV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 80 DFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQV--------------- 144
Cdd:COG0480 86 DFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQLkerlganpvplqlpi 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 145 -----FDLFVNL--------------------------------------------DA-----------TDEQLD----- 159
Cdd:COG0480 166 gaeddFKGVIDLvtmkayvyddelgakyeeeeipaelkeeaeeareelieavaetdDElmekylegeelTEEEIKaglrk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 160 -------FPIVYASALNGIaGLDhedmaedmtPLYQAIVDHVPAPD-------------------VDLDGPFQMQISQLD 213
Cdd:COG0480 246 atlagkiVPVLCGSAFKNK-GVQ---------PLLDAVVDYLPSPLdvpaikgvdpdtgeeverkPDDDEPFSALVFKTM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 214 YNSYVGVIGIGRIKRGKVKPNQQVTIIDSEGKTRnakVGKVLGHLGLERIETDLAEAGDIVAITGLGELNISDTVCDTQN 293
Cdd:COG0480 316 TDPFVGKLSFFRVYSGTLKSGSTVYNSTKGKKER---IGRLLRMHGNKREEVDEAGAGDIVAVVKLKDTTTGDTLCDEDH 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 294 VEALPALSVDEPTVSMFFCVNTSpfcGKEGKFVTSrqiLDRLNKElvhNVALRVEETEDADAFRVSGRGELHLSVLIENM 373
Cdd:COG0480 393 PIVLEPIEFPEPVISVAIEPKTK---ADEDKLSTA---LAKLAEE---DPTFRVETDEETGQTIISGMGELHLEIIVDRL 463
|
490
....*....|....*....
gi 49176434 374 RRE-GFELAVSRPKVIFRE 391
Cdd:COG0480 464 KREfGVEVNVGKPQVAYRE 482
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
6-197 |
7.00e-50 |
|
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.
Pssm-ID: 206677 [Multi-domain] Cd Length: 179 Bit Score: 170.79 E-value: 7.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 6 RNIAIIAHVDHGKTTLVDKLLQQSGTFDSRaETQERVMDSNDLEKERGITILAKNTAIKW-----NDYRINIVDTPGHAD 80
Cdd:cd01890 1 RNFSIIAHIDHGKSTLADRLLELTGTVSER-EMKEQVLDSMDLERERGITIKAQAVRLFYkakdgEEYLLNLIDTPGHVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 81 FGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLFvNLDATDeqldf 160
Cdd:cd01890 80 FSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVKQEIEDVL-GLDASE----- 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 49176434 161 pIVYASALNGIaGLDHedmaedmtpLYQAIVDHVPAP 197
Cdd:cd01890 154 -AILVSAKTGL-GVED---------LLEAIVERIPPP 179
|
|
| BipA_III |
cd16263 |
Domain III of GTP-binding protein BipA (TypA); BipA (also called TypA) is a highly conserved ... |
305-383 |
7.93e-48 |
|
Domain III of GTP-binding protein BipA (TypA); BipA (also called TypA) is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios. It is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion.
Pssm-ID: 293920 [Multi-domain] Cd Length: 79 Bit Score: 161.71 E-value: 7.93e-48
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 49176434 305 PTVSMFFCVNTSPFCGKEGKFVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRREGFELAVS 383
Cdd:cd16263 1 PTVSMTFGVNTSPFAGREGKFVTSRKIRDRLEKELETNVALRVEETESPDSFIVSGRGELHLSILIETMRREGFELQVS 79
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
6-132 |
1.32e-45 |
|
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: 160.47 E-value: 1.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 6 RNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITIlaKNTAI-----------KWNDYRINIVD 74
Cdd:cd01885 1 RNICIIAHVDHGKTTLSDSLLASAGIISEKLAGKARYLDTREDEQERGITI--KSSAIslyfeyeeekmDGNDYLINLID 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 49176434 75 TPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDR 132
Cdd:cd01885 79 SPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDR 136
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
205-298 |
9.29e-43 |
|
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios and is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion. The domain II of BipA shows similarity to the domain II of the elongation factors (EFs) EF-G and EF-Tu.
Pssm-ID: 293892 [Multi-domain] Cd Length: 94 Bit Score: 148.49 E-value: 9.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 205 FQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIIDSEGKTRNAKVGKVLGHLGLERIETDLAEAGDIVAITGLGELNI 284
Cdd:cd03691 1 FQMLVTTLDYDDYLGRIAIGRIFSGTVKVGQQVTVVDEDGKIEKGRVTKLFGFEGLERVEVEEAEAGDIVAIAGLEDITI 80
|
90
....*....|....
gi 49176434 285 SDTVCDTQNVEALP 298
Cdd:cd03691 81 GDTICDPEVPEPLP 94
|
|
| BipA_TypA_C |
cd03710 |
BipA_TypA_C: a C-terminal portion of BipA or TypA having homology to the C terminal domains of ... |
398-476 |
2.50e-40 |
|
BipA_TypA_C: a C-terminal portion of BipA or TypA having homology to the C terminal domains of the elongation factors EF-G and EF-2. A member of the ribosome binding GTPase superfamily, BipA is widely distributed in bacteria and plants. BipA is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios and, is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion.
Pssm-ID: 239681 [Multi-domain] Cd Length: 79 Bit Score: 141.49 E-value: 2.50e-40
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 49176434 398 EPYENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDVR 476
Cdd:cd03710 1 EPIEELTIDVPEEYSGAVIEKLGKRKGEMVDMEPDGNGRTRLEFKIPSRGLIGFRSEFLTDTRGTGIMNHVFDGYEPYK 79
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
7-144 |
4.01e-39 |
|
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling phases of protein synthesis; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains both eukaryotic and bacterial members.
Pssm-ID: 206673 [Multi-domain] Cd Length: 270 Bit Score: 144.56 E-value: 4.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQER--VMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGE 84
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGRIHKIGEVHGGgaTMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDFTIE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 85 VERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQV 144
Cdd:cd01886 81 VERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQI 140
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
7-144 |
4.36e-38 |
|
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.
Pssm-ID: 206731 [Multi-domain] Cd Length: 237 Bit Score: 140.83 E-value: 4.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRAetqeRV------MDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHAD 80
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIRELG----SVdkgttrTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMD 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49176434 81 FGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQV 144
Cdd:cd04168 77 FIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTIIFVNKIDRAGADLEKVYQEI 140
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
3-132 |
1.81e-31 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 130.55 E-value: 1.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 3 EKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITIlaKNTAI------------KWNDYRI 70
Cdd:PTZ00416 17 DQIRNMSVIAHVDHGKSTLTDSLVCKAGIISSKNAGDARFTDTRADEQERGITI--KSTGIslyyehdledgdDKQPFLI 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49176434 71 NIVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDR 132
Cdd:PTZ00416 95 NLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKVDR 156
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
6-132 |
4.36e-29 |
|
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: 114.67 E-value: 4.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 6 RNIAIIAHVDHGKTTLVDKLLQQS---GTFDSRAETQERVMDSNDLEKERGITIlaKNTAI-------KWNDYRINIVDT 75
Cdd:cd04167 1 RNVCIAGHLHHGKTSLLDMLIEQThkrTPSVKLGWKPLRYTDTRKDEQERGISI--KSNPIslvledsKGKSYLINIIDT 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 49176434 76 PGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDR 132
Cdd:cd04167 79 PGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDR 135
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
6-144 |
4.83e-29 |
|
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: 116.16 E-value: 4.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 6 RNIAIIAHVDHGKTTLVDKLL------QQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHA 79
Cdd:cd04169 3 RTFAIISHPDAGKTTLTEKLLlfggaiQEAGAVKARKSRKHATSDWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHE 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 49176434 80 DFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQV 144
Cdd:cd04169 83 DFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDREGRDPLELLDEI 147
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
5-132 |
4.89e-29 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 122.91 E-value: 4.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 5 LRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITIlaKNTAIKW------------------N 66
Cdd:PLN00116 19 IRNMSVIAHVDHGKSTLTDSLVAAAGIIAQEVAGDVRMTDTRADEAERGITI--KSTGISLyyemtdeslkdfkgerdgN 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 49176434 67 DYRINIVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDR 132
Cdd:PLN00116 97 EYLINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTETVLRQALGERIRPVLTVNKMDR 162
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
7-240 |
3.68e-28 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 117.62 E-value: 3.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 7 NIAIIAHVDHGKTTL---VDKLLQQSGTFDSRAETQervMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGG 83
Cdd:PLN03127 63 NVGTIGHVDHGKTTLtaaITKVLAEEGKAKAVAFDE---IDKAPEEKARGITIATAHVEYETAKRHYAHVDCPGHADYVK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 84 EVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDrpgarpdwVVD--QVFDLfVNLDATdEQLDF 160
Cdd:PLN03127 140 NMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVfLNKVD--------VVDdeELLEL-VEMELR-ELLSF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 161 --------PIVYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVK 232
Cdd:PLN03127 210 ykfpgdeiPIIRGSALSALQGTNDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIK 289
|
....*...
gi 49176434 233 PNQQVTII 240
Cdd:PLN03127 290 VGEEVEIV 297
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
7-276 |
9.82e-28 |
|
translation elongation factor TU; This model models orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts, one of several GTP-binding translation factors found by the more general pfam model GTP_EFTU. The eukaryotic conterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this model. EF-Tu is one of the most abundant proteins in bacteria, as well as one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation. [Protein synthesis, Translation factors]
Pssm-ID: 129576 [Multi-domain] Cd Length: 394 Bit Score: 115.64 E-value: 9.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 7 NIAIIAHVDHGKTTL---VDKLLQQSGTFDSRAETQervMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGG 83
Cdd:TIGR00485 14 NVGTIGHVDHGKTTLtaaITTVLAKEGGAAARAYDQ---IDNAPEEKARGITINTAHVEYETETRHYAHVDCPGHADYVK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 84 EVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRpgarpdwVVDQVFDLFVNLDATD--EQLDF 160
Cdd:TIGR00485 91 NMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKCDM-------VDDEELLELVEMEVREllSQYDF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 161 -----PIVYASALNGIAGldHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQ 235
Cdd:TIGR00485 164 pgddtPIIRGSALKALEG--DAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGE 241
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 49176434 236 QVTIIDSEgKTRNAKVgkvlghLGLE--RIETDLAEAGDIVAI 276
Cdd:TIGR00485 242 EVEIVGLK-DTRKTTV------TGVEmfRKELDEGRAGDNVGL 277
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
7-272 |
9.92e-28 |
|
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444074 [Multi-domain] Cd Length: 423 Bit Score: 115.80 E-value: 9.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRA------ETQER---------VMDSNDLEKERGITILAKNTAIKWNDYRIN 71
Cdd:COG5256 9 NLVVIGHVDHGKSTLVGRLLYETGAIDEHIiekyeeEAEKKgkesfkfawVMDRLKEERERGVTIDLAHKKFETDKYYFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 72 IVDTPGHADFggeverVMSMV------DSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRPG---ARPDWVV 141
Cdd:COG5256 89 IIDAPGHRDF------VKNMItgasqaDAAILVVSAKDGVMGQTREHAFLARTLGINQLIVaVNKMDAVNyseKRYEEVK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 142 DQVFDLFVNLDATDEqlDFPIVYASALNGiaglDHEDMAEDMTP------LYQAIvDHVPAPDVDLDGPFQMQIsQLDYN 215
Cdd:COG5256 163 EEVSKLLKMVGYKVD--KIPFIPVSAWKG----DNVVKKSDNMPwyngptLLEAL-DNLKEPEKPVDKPLRIPI-QDVYS 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 49176434 216 -SYVGVIGIGRIKRGKVKPNQQVTIIDSegktrnAKVGKVlghlglERIET-----DLAEAGD 272
Cdd:COG5256 235 iSGIGTVPVGRVETGVLKVGDKVVFMPA------GVVGEV------KSIEMhheelEQAEPGD 285
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
7-148 |
2.90e-27 |
|
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: 111.15 E-value: 2.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDsRAETQER---VMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGG 83
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAID-RLGRVEDgntVSDYDPEEKKRKMSIETSVAPLEWNGHKINLIDTPGYADFVG 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 49176434 84 EVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLF 148
Cdd:cd04170 80 ETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRARADFDKTLAALREAF 144
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
7-276 |
7.38e-27 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 112.73 E-value: 7.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 7 NIAIIAHVDHGKTTL---VDKLLQQSGTFDSRAETQervMDSNDLEKERGITIlakNTA-IKWN-DYR-INIVDTPGHAD 80
Cdd:PRK12736 14 NIGTIGHVDHGKTTLtaaITKVLAERGLNQAKDYDS---IDAAPEEKERGITI---NTAhVEYEtEKRhYAHVDCPGHAD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 81 FggeverVMSMV------DSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRPGARP--DWVVDQVFDLFVNL 151
Cdd:PRK12736 88 Y------VKNMItgaaqmDGAILVVAATDGPMPQTREHILLARQVGVPYLVVfLNKVDLVDDEEllELVEMEVRELLSEY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 152 DATDEqlDFPIVYASALngiAGLDHEDMAED-MTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGK 230
Cdd:PRK12736 162 DFPGD--DIPVIRGSAL---KALEGDPKWEDaIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGT 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 49176434 231 VKPNQQVTIIdSEGKTRNAKVgkvlghLGLE--RIETDLAEAGDIVAI 276
Cdd:PRK12736 237 VKVGDEVEIV-GIKETQKTVV------TGVEmfRKLLDEGQAGDNVGV 277
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
7-272 |
8.57e-26 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 110.40 E-value: 8.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDS------RAETQER---------VMDSNDLEKERGITILAKNTAIKWNDYRIN 71
Cdd:PRK12317 8 NLAVIGHVDHGKSTLVGRLLYETGAIDEhiieelREEAKEKgkesfkfawVMDRLKEERERGVTIDLAHKKFETDKYYFT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 72 IVDTPGHADFggeverVMSMV------DSVLLVVDAFD--GPMPQTR---FVTKkafAYGLKP-IVVINKVDRPG---AR 136
Cdd:PRK12317 88 IVDCPGHRDF------VKNMItgasqaDAAVLVVAADDagGVMPQTRehvFLAR---TLGINQlIVAINKMDAVNydeKR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 137 PDWVVDQVFDLFVNLDATDEqlDFPIVYASALNGiaglDHEDMAEDMTP------LYQAIvDHVPAPDVDLDGPFQMQIS 210
Cdd:PRK12317 159 YEEVKEEVSKLLKMVGYKPD--DIPFIPVSAFEG----DNVVKKSENMPwyngptLLEAL-DNLKPPEKPTDKPLRIPIQ 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 49176434 211 QLDYNSYVGVIGIGRIKRGKVKPNQQVTIIDSegktrnAKVGKVlghlglERIET-----DLAEAGD 272
Cdd:PRK12317 232 DVYSISGVGTVPVGRVETGVLKVGDKVVFMPA------GVVGEV------KSIEMhheelPQAEPGD 286
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
7-240 |
1.14e-25 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 109.51 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 7 NIAIIAHVDHGKTTL---VDKLLQQSGTFDSRAETQervMDSNDLEKERGITIlakNTAikwndyriNI----------- 72
Cdd:PRK00049 14 NVGTIGHVDHGKTTLtaaITKVLAKKGGAEAKAYDQ---IDKAPEEKARGITI---NTA--------HVeyetekrhyah 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 73 VDTPGHADFggeverVMSMV------DSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDrpgarpdwVVD--Q 143
Cdd:PRK00049 80 VDCPGHADY------VKNMItgaaqmDGAILVVSAADGPMPQTREHILLARQVGVPYIVVfLNKCD--------MVDdeE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 144 VFDLfVNLDATD--EQLDF-----PIVYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNS 216
Cdd:PRK00049 146 LLEL-VEMEVREllSKYDFpgddtPIIRGSALKALEGDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSIS 224
|
250 260
....*....|....*....|....
gi 49176434 217 YVGVIGIGRIKRGKVKPNQQVTII 240
Cdd:PRK00049 225 GRGTVVTGRVERGIIKVGEEVEIV 248
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
7-276 |
1.45e-25 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 109.16 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 7 NIAIIAHVDHGKTTL---VDKLLQQSGTFDSRAETQervMDSNDLEKERGITIlakNTAikWNDYRINI-----VDTPGH 78
Cdd:PRK12735 14 NVGTIGHVDHGKTTLtaaITKVLAKKGGGEAKAYDQ---IDNAPEEKARGITI---NTS--HVEYETANrhyahVDCPGH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 79 ADFggeverVMSMV------DSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDrpgarpdwVVD--QVFDLfV 149
Cdd:PRK12735 86 ADY------VKNMItgaaqmDGAILVVSAADGPMPQTREHILLARQVGVPYIVVfLNKCD--------MVDdeELLEL-V 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 150 NLDATD--EQLDF-----PIVYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIG 222
Cdd:PRK12735 151 EMEVREllSKYDFpgddtPIIRGSALKALEGDDDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVV 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 49176434 223 IGRIKRGKVKPNQQVTIIdSEGKTRNAKVgkvlghLGLE--RIETDLAEAGDIVAI 276
Cdd:PRK12735 231 TGRVERGIVKVGDEVEIV-GIKETQKTTV------TGVEmfRKLLDEGQAGDNVGV 279
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
7-276 |
2.94e-25 |
|
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-Tu, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 439820 [Multi-domain] Cd Length: 396 Bit Score: 108.31 E-value: 2.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 7 NIAIIAHVDHGKTTLV--------DKLLQQSGTFDSRAETQErvmdsndlEKERGITIlakNTAikWNDYRINI-----V 73
Cdd:COG0050 14 NIGTIGHVDHGKTTLTaaitkvlaKKGGAKAKAYDQIDKAPE--------EKERGITI---NTS--HVEYETEKrhyahV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 74 DTPGHADFggeverVMSMV------DSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDrpgarpdwVVD--QV 144
Cdd:COG0050 81 DCPGHADY------VKNMItgaaqmDGAILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKCD--------MVDdeEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 145 FDLfVNLDATD--EQLDF-----PIVYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSY 217
Cdd:COG0050 147 LEL-VEMEVREllSKYGFpgddtPIIRGSALKALEGDPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITG 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 49176434 218 VGVIGIGRIKRGKVKPNQQVTIIdSEGKTRNAKVgkvlghLGLE--RIETDLAEAGDIVAI 276
Cdd:COG0050 226 RGTVVTGRVERGIIKVGDEVEIV-GIRDTQKTVV------TGVEmfRKLLDEGEAGDNVGL 279
|
|
| EFG_C |
pfam00679 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
395-483 |
1.62e-24 |
|
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: 97.62 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 395 RKQEPYENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDD 474
Cdd:pfam00679 1 VLLEPIEKVTIDVPEEYVGDVISDLNSRRGEILDMDPDDGGRVVIEAEVPLAELFGFATELRSLTKGRGSFSMEFSGYQP 80
|
....*....
gi 49176434 475 VrPGEVGQR 483
Cdd:pfam00679 81 V-PGDILDR 88
|
|
| tufA |
CHL00071 |
elongation factor Tu |
7-276 |
5.77e-24 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 104.65 E-value: 5.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 7 NIAIIAHVDHGKTTL---VDKLLQQSGTfdSRAETQERVmDSNDLEKERGITIlakNTAikWNDYRINI-----VDTPGH 78
Cdd:CHL00071 14 NIGTIGHVDHGKTTLtaaITMTLAAKGG--AKAKKYDEI-DSAPEEKARGITI---NTA--HVEYETENrhyahVDCPGH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 79 ADFggeverVMSMV------DSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRpgarpdwVVDQVFDLFVNL 151
Cdd:CHL00071 86 ADY------VKNMItgaaqmDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVfLNKEDQ-------VDDEELLELVEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 152 DATD--EQLDF-----PIVYASAL---NGIAGLDHEDMAED-----MTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNS 216
Cdd:CHL00071 153 EVREllSKYDFpgddiPIVSGSALlalEALTENPKIKRGENkwvdkIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSIT 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49176434 217 YVGVIGIGRIKRGKVKPNQQVTIIdSEGKTRNAKVgkvlghLGLERIETDL--AEAGDIVAI 276
Cdd:CHL00071 233 GRGTVATGRIERGTVKVGDTVEIV-GLRETKTTTV------TGLEMFQKTLdeGLAGDNVGI 287
|
|
| Elongation_Factor_C |
cd01514 |
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ... |
398-475 |
1.83e-23 |
|
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: 94.09 E-value: 1.83e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 49176434 398 EPYENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDV 475
Cdd:cd01514 1 EPIMKVEITVPEEYLGAVIGDLSKRRGEILGMEPRGTGRVVIKAELPLAEMFGFATDLRSLTQGRASFSMEFSHYEPV 78
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
2-137 |
2.77e-23 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 103.67 E-value: 2.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 2 IEKLRNIAIIAHVDHGKTTLVDKLL------QQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDT 75
Cdd:PRK00741 7 VAKRRTFAIISHPDAGKTTLTEKLLlfggaiQEAGTVKGRKSGRHATSDWMEMEKQRGISVTSSVMQFPYRDCLINLLDT 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 49176434 76 PGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTR--F-VTKkafaygLK--PIVV-INKVDRPGARP 137
Cdd:PRK00741 87 PGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTRklMeVCR------LRdtPIFTfINKLDRDGREP 148
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
7-276 |
9.92e-22 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 98.53 E-value: 9.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVE 86
Cdd:PLN03126 83 NIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMI 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 87 RVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRpgarpdwVVDQVFDLFVNLDATD-------EQL 158
Cdd:PLN03126 163 TGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVfLNKQDQ-------VDDEELLELVELEVREllssyefPGD 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 159 DFPIVYASALNGIAGL--------DHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGK 230
Cdd:PLN03126 236 DIPIISGSALLALEALmenpnikrGDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGT 315
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 49176434 231 VKPNQQVTIIdSEGKTRNAKVgkvlghLGLERIETDLAE--AGDIVAI 276
Cdd:PLN03126 316 VKVGETVDIV-GLRETRSTTV------TGVEMFQKILDEalAGDNVGL 356
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
8-175 |
2.07e-21 |
|
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: 91.38 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 8 IAIIAHVDHGKTTLVDKLLQqsgtfdsraetqervmdSNDLEKE-RGIT--ILAKNTAIKWNDYRINIVDTPGHADFGGE 84
Cdd:cd01887 3 VTVMGHVDHGKTTLLDKIRK-----------------TNVAAGEaGGITqhIGAYQVPIDVKIPGITFIDTPGHEAFTNM 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 85 VERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRP---GARPDWVVDQVFDLfvNLDATDEQLDFP 161
Cdd:cd01887 66 RARGASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKPygtEADPERVKNELSEL--GLVGEEWGGDVS 143
|
170
....*....|....
gi 49176434 162 IVYASALNGIaGLD 175
Cdd:cd01887 144 IVPISAKTGE-GID 156
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
7-170 |
7.38e-21 |
|
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 206670 [Multi-domain] Cd Length: 219 Bit Score: 91.40 E-value: 7.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSR------AETQER---------VMDSNDLEKERGITILAKNTAIKWNDYRIN 71
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRtiekyeKEAKEMgkesfkyawVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 72 IVDTPGHADFggeverVMSMV------DSVLLVVDAFDG-------PMPQTRFVTKKAFAYGLKP-IVVINKVDRPG--- 134
Cdd:cd01883 81 IIDAPGHRDF------VKNMItgasqaDVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQlIVAVNKMDDVTvnw 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 49176434 135 --ARPDWVVDQVFDLFVNLDATDEQLDF-PIvyaSALNG 170
Cdd:cd01883 155 sqERYDEIKKKVSPFLKKVGYNPKDVPFiPI---SGFTG 190
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
7-197 |
2.17e-19 |
|
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.
Pssm-ID: 206671 [Multi-domain] Cd Length: 195 Bit Score: 86.48 E-value: 2.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 7 NIAIIAHVDHGKTTL---VDKLLQQSGTFDSRAETQErvmDSNDLEKERGITIlakNTA------IKWNDYRiniVDTPG 77
Cdd:cd01884 4 NVGTIGHVDHGKTTLtaaITKVLAKKGGAKAKKYDEI---DKAPEEKARGITI---NTAhveyetANRHYAH---VDCPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 78 HADFggeverVMSMV------DSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRpgarpdwVVDQVFDLFVN 150
Cdd:cd01884 75 HADY------IKNMItgaaqmDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVfLNKADM-------VDDEELLELVE 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 49176434 151 LDATD--EQLDF-----PIVYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAP 197
Cdd:cd01884 142 MEVREllSKYGFdgddtPIVRGSALKALEGDDPNKWVDKILELLDALDSYIPTP 195
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
6-138 |
1.21e-18 |
|
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: 83.19 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 6 RNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERvMDSNDLEKERGITilakntaikwndYRINIVDTPGHADF---- 81
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTR-NYVTTVIEEDGKT------------YKFNLLDTAGQEDYdair 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 82 ---GGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAfAYGLKPIVVINKVDRPGARPD 138
Cdd:TIGR00231 69 rlyYPQVERSLRVFDIVILVLDVEEILEKQTKEIIHHA-DSGVPIILVGNKIDLKDADLK 127
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
10-175 |
1.94e-17 |
|
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 442507 [Multi-domain] Cd Length: 630 Bit Score: 86.12 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 10 IIA---HVDHGKTTLVdkllqqsgtfdsRAETQervMDSNDL--EKERGITI--------LAkntaikwNDYRINIVDTP 76
Cdd:COG3276 2 IIGtagHIDHGKTTLV------------KALTG---IDTDRLkeEKKRGITIdlgfaylpLP-------DGRRLGFVDVP 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 77 GHADF--------GGevervmsmVDSVLLVVDAFDGPMPQTR-------FVtkkafayGLKP-IVVINKVDRpgARPDW- 139
Cdd:COG3276 60 GHEKFiknmlagaGG--------IDLVLLVVAADEGVMPQTRehlaildLL-------GIKRgIVVLTKADL--VDEEWl 122
|
170 180 190
....*....|....*....|....*....|....*....
gi 49176434 140 --VVDQVFDLfvnLDATDeqL-DFPIVYASALNGiAGLD 175
Cdd:COG3276 123 elVEEEIREL---LAGTF--LeDAPIVPVSAVTG-EGID 155
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
8-191 |
5.33e-17 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 84.88 E-value: 5.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 8 IAIIAHVDHGKTTLVDKLLQqsgtfdsraetqervmdSNDLEKERG-IT--ILAKNTAIKWNDYRINIV--DTPGHADFG 82
Cdd:CHL00189 247 VTILGHVDHGKTTLLDKIRK-----------------TQIAQKEAGgITqkIGAYEVEFEYKDENQKIVflDTPGHEAFS 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 83 GEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVfdLFVNLDATDEQLDFPI 162
Cdd:CHL00189 310 SMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANTERIKQQL--AKYNLIPEKWGGDTPM 387
|
170 180 190
....*....|....*....|....*....|....*....
gi 49176434 163 VYASALNG--IAGL--------DHEDMAEDMTPLYQAIV 191
Cdd:CHL00189 388 IPISASQGtnIDKLletilllaEIEDLKADPTQLAQGII 426
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
7-279 |
1.18e-16 |
|
translation initiation factor 2 subunit gamma; This model represents the archaeal translation initiation factor 2 subunit gamma and is found in all known archaea. eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.
Pssm-ID: 274720 [Multi-domain] Cd Length: 406 Bit Score: 82.41 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 7 NIAIIAHVDHGKTTLVDKLlqqSGTF-DSRAEtqervmdsndlEKERGITI-LAKNTAIKWNDY---------------- 68
Cdd:TIGR03680 6 NIGMVGHVDHGKTTLTKAL---TGVWtDTHSE-----------ELKRGISIrLGYADAEIYKCPecdgpecyttepvcpn 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 69 ---------RINIVDTPGHadfggevERVM-------SMVDSVLLVVDAFDG-PMPQTRFVTKKAFAYGLKPIVVI-NKV 130
Cdd:TIGR03680 72 cgsetellrRVSFVDAPGH-------ETLMatmlsgaALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVqNKI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 131 D---RPGARPDWVVDQVFdlfvnLDATDEQlDFPIVYASALNGIagldhedmaeDMTPLYQAIVDHVPAPDVDLDGPFQM 207
Cdd:TIGR03680 145 DlvsKEKALENYEEIKEF-----VKGTVAE-NAPIIPVSALHNA----------NIDALLEAIEKFIPTPERDLDKPPLM 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 208 QISQ-LDYNS--------YVGVIGiGRIKRGKVKPNQQVTI-----IDSEGKTRNAKVGKVLGHLGLERIETDLAEAGDI 273
Cdd:TIGR03680 209 YVARsFDVNKpgtppeklKGGVIG-GSLIQGKLKVGDEIEIrpgikVEKGGKTKWEPIYTEITSLRAGGYKVEEARPGGL 287
|
....*..
gi 49176434 274 VAI-TGL 279
Cdd:TIGR03680 288 VGVgTKL 294
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
13-176 |
2.05e-16 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.
Pssm-ID: 206734 [Multi-domain] Cd Length: 170 Bit Score: 77.26 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 13 HVDHGKTTLVDKLLQQSGtfDSRAEtqervmdsndlEKERGITI-LA-KNTAIKWNDyRINIVDTPGHADFggeverVMS 90
Cdd:cd04171 7 HIDHGKTTLIKALTGIET--DRLPE-----------EKKRGITIdLGfAYLDLPDGK-RLGFIDVPGHEKF------VKN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 91 MV------DSVLLVVDAFDGPMPQTRFVTKKAFAYGLKP-IVVINKVDRpgARPDWvVDQVFDLFVNLDATDEQLDFPIV 163
Cdd:cd04171 67 MLagaggiDAVLLVVAADEGIMPQTREHLEILELLGIKKgLVVLTKADL--VDEDR-LELVEEEILELLAGTFLADAPIF 143
|
170
....*....|...
gi 49176434 164 YASALNGiAGLDH 176
Cdd:cd04171 144 PVSSVTG-EGIEE 155
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
8-175 |
4.47e-16 |
|
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]
Pssm-ID: 273102 [Multi-domain] Cd Length: 587 Bit Score: 81.74 E-value: 4.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 8 IAIIAHVDHGKTTLVDKLlqqsgtfdsraetqervMDSNDLEKERG-ITILAKNTAIKWND-YRINIVDTPGHADFGGEV 85
Cdd:TIGR00487 90 VTIMGHVDHGKTSLLDSI-----------------RKTKVAQGEAGgITQHIGAYHVENEDgKMITFLDTPGHEAFTSMR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 86 ERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDFpiVYA 165
Cdd:TIGR00487 153 ARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVPIIVAINKIDKPEANPDRVKQELSEYGLVPEDWGGDTIF--VPV 230
|
170
....*....|
gi 49176434 166 SALNGIaGLD 175
Cdd:TIGR00487 231 SALTGD-GID 239
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
7-238 |
6.68e-16 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 80.18 E-value: 6.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRA-ETQER--------------VMDSNDLEKERGITILAKNTAIKWNDYRIN 71
Cdd:PTZ00141 9 NLVVIGHVDSGKSTTTGHLIYKCGGIDKRTiEKFEKeaaemgkgsfkyawVLDKLKAERERGITIDIALWKFETPKYYFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 72 IVDTPGHADFGGEVERVMSMVDSVLLVVDA----FDGPMP---QTRFVTKKAFAYGLKPIVV-INKVDRPG-----ARPD 138
Cdd:PTZ00141 89 IIDAPGHRDFIKNMITGTSQADVAILVVAStageFEAGISkdgQTREHALLAFTLGVKQMIVcINKMDDKTvnysqERYD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 139 WVVDQVFDLFVNLDATDEQLDF-PIvyaSALNGiagldhEDMAE--DMTPLYQA-----IVDHVPAPDVDLDGPFQMQIS 210
Cdd:PTZ00141 169 EIKKEVSAYLKKVGYNPEKVPFiPI---SGWQG------DNMIEksDNMPWYKGptlleALDTLEPPKRPVDKPLRLPLQ 239
|
250 260
....*....|....*....|....*...
gi 49176434 211 QLDYNSYVGVIGIGRIKRGKVKPNQQVT 238
Cdd:PTZ00141 240 DVYKIGGIGTVPVGRVETGILKPGMVVT 267
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
7-132 |
3.00e-15 |
|
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]
Pssm-ID: 129567 [Multi-domain] Cd Length: 581 Bit Score: 78.76 E-value: 3.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 7 NIAIIAHVDHGKTTLVDKLlqqSGTfdsraetqervmDSNDL--EKERGITILAKNTAIKWNDYRINIVDTPGHADFGGE 84
Cdd:TIGR00475 2 IIATAGHVDHGKTTLLKAL---TGI------------AADRLpeEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISN 66
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 49176434 85 VERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKP-IVVINKVDR 132
Cdd:TIGR00475 67 AIAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHtIVVITKADR 115
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
7-238 |
4.65e-15 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 77.82 E-value: 4.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSR---------AETQER------VMDSNDLEKERGITILAKNTAIKWNDYRIN 71
Cdd:PLN00043 9 NIVVIGHVDSGKSTTTGHLIYKLGGIDKRvierfekeaAEMNKRsfkyawVLDKLKAERERGITIDIALWKFETTKYYCT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 72 IVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMP-------QTRFVTKKAFAYGLKPIV-VINKVDR-----PGARPD 138
Cdd:PLN00043 89 VIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMIcCCNKMDAttpkySKARYD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 139 WVVDQVFDLFVNLDATDEQLDFPivyasalnGIAGLDHEDMAEDMT-------PLYQAIVDHVPAPDVDLDGPFQMQISQ 211
Cdd:PLN00043 169 EIVKEVSSYLKKVGYNPDKIPFV--------PISGFEGDNMIERSTnldwykgPTLLEALDQINEPKRPSDKPLRLPLQD 240
|
250 260
....*....|....*....|....*..
gi 49176434 212 LDYNSYVGVIGIGRIKRGKVKPNQQVT 238
Cdd:PLN00043 241 VYKIGGIGTVPVGRVETGVIKPGMVVT 267
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
7-131 |
1.51e-14 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.
Pssm-ID: 206676 [Multi-domain] Cd Length: 192 Bit Score: 72.40 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 7 NIAIIAHVDHGKTTLVDKLLQQSGT--FDSRAETQervmdsndlekERGITI--------------LAKNTAIKWNDYRI 70
Cdd:cd01889 2 NVGLLGHVDSGKTSLAKALSEIASTaaFDKNPQSQ-----------ERGITLdlgfssfevdkpkhLEDNENPQIENYQI 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49176434 71 NIVDTPGHADF------GGEVervmsmVDSVLLVVDAFDGPMPQT-------RFVTKKAfayglkpIVVINKVD 131
Cdd:cd01889 71 TLVDCPGHASLirtiigGAQI------IDLMLLVVDAKKGIQTQTaeclvigELLCKPL-------IVVLNKID 131
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
8-138 |
1.83e-14 |
|
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440298 [Multi-domain] Cd Length: 502 Bit Score: 76.21 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 8 IAIIAHVDHGKTTLVDKLlqqsgtfdsRaetQERVMdsndlEKE-RGIT--ILAknTAIKWNDYRINIVDTPGHADF--- 81
Cdd:COG0532 7 VTVMGHVDHGKTSLLDAI---------R---KTNVA-----AGEaGGITqhIGA--YQVETNGGKITFLDTPGHEAFtam 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 49176434 82 ---GGEVervmsmVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLkPIVV-INKVDRPGARPD 138
Cdd:COG0532 68 rarGAQV------TDIVILVVAADDGVMPQTIEAINHAKAAGV-PIIVaINKIDKPGANPD 121
|
|
| EFG_III-like |
cd16257 |
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G ... |
324-383 |
4.82e-14 |
|
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: 67.37 E-value: 4.82e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 49176434 324 KFVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRRE-GFELAVS 383
Cdd:cd16257 11 NPLDQEKLLEGLERLSEEDPALQVYREESTGEFILSGLGELHLEIIVARLEREyGVELVVS 71
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
9-171 |
1.53e-13 |
|
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: 68.64 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 9 AIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEkergitilakntaIKWNDYRINIVDTPGHADFGG----- 83
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPDVYVKE-------------LDKGKVKLVLVDTPGLDEFGGlgree 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 84 EVERVMSMVDSVLLVVDAFDGPMP--QTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLFvnldatdEQLDFP 161
Cdd:cd00882 68 LARLLLRGADLILLVVDSTDRESEedAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELA-------KILGVP 140
|
170
....*....|
gi 49176434 162 IVYASALNGI 171
Cdd:cd00882 141 VFEVSAKTGE 150
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
7-247 |
1.74e-13 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 72.58 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 7 NIAIIAHVDHGKTTLVDKLlqqSGTFDSR-AEtqervmdsndlEKERGITI--------LAKNTAIKWNDY--------- 68
Cdd:PRK04000 11 NIGMVGHVDHGKTTLVQAL---TGVWTDRhSE-----------ELKRGITIrlgyadatIRKCPDCEEPEAyttepkcpn 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 69 ---------RINIVDTPGHadfggevERVM-------SMVDSVLLVVDAFDG-PMPQTRFVTKKAFAYGLKPIVVI-NKV 130
Cdd:PRK04000 77 cgsetellrRVSFVDAPGH-------ETLMatmlsgaALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVqNKI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 131 DrpgarpdwVVD---------QVFDlFVnlDAT-DEqlDFPIVYASALNGIagldhedmaeDMTPLYQAIVDHVPAPDVD 200
Cdd:PRK04000 150 D--------LVSkeralenyeQIKE-FV--KGTvAE--NAPIIPVSALHKV----------NIDALIEAIEEEIPTPERD 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 49176434 201 LDGPFQMQISQ-LDYNS--------YVGVIGiGRIKRGKVKPNQQVTI-----IDSEGKTR 247
Cdd:PRK04000 207 LDKPPRMYVARsFDVNKpgtppeklKGGVIG-GSLIQGVLKVGDEIEIrpgikVEEGGKTK 266
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
5-293 |
5.01e-13 |
|
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and metabolism]; Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 442140 [Multi-domain] Cd Length: 430 Bit Score: 71.27 E-value: 5.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 5 LRnIAIIAHVDHGKTTLVDKLLqqsgtFDS-----------RAETQERVMDSNDL---------EKERGITIlakNTAik 64
Cdd:COG2895 18 LR-FITCGSVDDGKSTLIGRLL-----YDTksifedqlaalERDSKKRGTQEIDLalltdglqaEREQGITI---DVA-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 65 wndYR---------InIVDTPGHADFggevERVM----SMVDSVLLVVDAFDGPMPQTRfvtkkAFAY-----GLKPIVV 126
Cdd:COG2895 87 ---YRyfstpkrkfI-IADTPGHEQY----TRNMvtgaSTADLAILLIDARKGVLEQTR-----RHSYiasllGIRHVVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 127 -INKVDRpgarpdwvVD---QVFDLFVNlDATD--EQLDFPIVYA---SALNGiagldhEDMAE--DMTPLYQ-----AI 190
Cdd:COG2895 154 aVNKMDL--------VDyseEVFEEIVA-DYRAfaAKLGLEDITFipiSALKG------DNVVErsENMPWYDgptllEH 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 191 VDHVPAPDVDLDGPFQMQI-----SQLDYNSYVgvigiGRIKRGKVKPNQQVTIIDSeGKTrnAKVGKVLGHLGleriET 265
Cdd:COG2895 219 LETVEVAEDRNDAPFRFPVqyvnrPNLDFRGYA-----GTIASGTVRVGDEVVVLPS-GKT--STVKSIVTFDG----DL 286
|
330 340 350
....*....|....*....|....*....|
gi 49176434 266 DLAEAGDIVAITGLGELNIS--DTVCDTQN 293
Cdd:COG2895 287 EEAFAGQSVTLTLEDEIDISrgDVIVAADA 316
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
205-289 |
3.33e-11 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 59.59 E-value: 3.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 205 FQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIIDSEGKTRnakvgkvLGHLGLERIETDLAEAGDIVAITGLG--EL 282
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGR-------VTSIERFHEEVDEAKAGDIVGIGILGvkDI 73
|
....*..
gi 49176434 283 NISDTVC 289
Cdd:cd01342 74 LTGDTLT 80
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
14-285 |
3.77e-11 |
|
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules. With members of the Rhizobiaceae family, nodQ often appears as a fusion of cysN (large subunit of ATP sulfurase) and cysC (APS kinase). [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 213679 [Multi-domain] Cd Length: 406 Bit Score: 65.47 E-value: 3.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 14 VDHGKTTLVDKLLQQSGT-FDSRAETQER----------------VMDSNDLEKERGITIlakNTAIKW--NDYRINIV- 73
Cdd:TIGR02034 9 VDDGKSTLIGRLLHDTKQiYEDQLAALERdskkhgtqggeidlalLVDGLQAEREQGITI---DVAYRYfsTDKRKFIVa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 74 DTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRPGARPDwVVDQVFDLFVNLD 152
Cdd:TIGR02034 86 DTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLaVNKMDLVDYDEE-VFENIKKDYLAFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 153 ATDEQLDFPIVYASALNGiagldhEDMAE--DMTPLYQA-----IVDHVPAPDVDLDGPFQMQIS-----QLDYNSYVGV 220
Cdd:TIGR02034 165 EQLGFRDVTFIPLSALKG------DNVVSrsESMPWYSGptlleILETVEVERDAQDLPLRFPVQyvnrpNLDFRGYAGT 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 49176434 221 IGIGRikrgkVKPNQQVTIIDSegkTRNAKVGKVLGHLGleriETDLAEAGDIVAITGLGELNIS 285
Cdd:TIGR02034 239 IASGS-----VHVGDEVVVLPS---GRSSRVARIVTFDG----DLEQARAGQAVTLTLDDEIDIS 291
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
7-247 |
7.58e-11 |
|
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal structure and biogenesis]; Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444075 [Multi-domain] Cd Length: 408 Bit Score: 64.47 E-value: 7.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 7 NIAIIAHVDHGKTTLVDKLlqqSGTFDSR-AEtqervmdsndlEKERGITI------------------LAKNTAIKWND 67
Cdd:COG5257 7 NIGVVGHVDHGKTTLVQAL---TGVWTDRhSE-----------ELKRGITIrlgyadatfykcpnceppEAYTTEPKCPN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 68 Y--------RINIVDTPGHadfggevERVM-------SMVDSVLLVVDAFDG-PMPQTR--FVTKKAFayGLKPIVVI-N 128
Cdd:COG5257 73 CgsetellrRVSFVDAPGH-------ETLMatmlsgaALMDGAILVIAANEPcPQPQTKehLMALDII--GIKNIVIVqN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 129 KVDrpgarpdwVVDQVfdlfvnlDATD--EQL----------DFPIVYASALNGIagldhedmaeDMTPLYQAIVDHVPA 196
Cdd:COG5257 144 KID--------LVSKE-------RALEnyEQIkefvkgtvaeNAPIIPVSAQHKV----------NIDALIEAIEEEIPT 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 49176434 197 PDVDLDGPFQMQISQ-LDYN----SYV----GVIGiGRIKRGKVKPNQQVTI-----IDSEGKTR 247
Cdd:COG5257 199 PERDLSKPPRMLVARsFDVNkpgtPPKdlkgGVIG-GSLIQGVLKVGDEIEIrpgikVEKGGKTK 262
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
219-289 |
1.14e-10 |
|
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.
Pssm-ID: 427163 [Multi-domain] Cd Length: 73 Bit Score: 57.66 E-value: 1.14e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 49176434 219 GVIGIGRIKRGKVKPNQQVTII--DSEGKTRNAKVGKVLGHLGLERIETDLAEAGDIVAITGLGELNISDTVC 289
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILpnGTGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
1-193 |
1.10e-09 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 58.07 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 1 MIEKlrNIAIIAHVDHGKTTLVDKLLQqsgtfdsraetqervmDSNDLEKE---RGITILAKNTAIKWNDYRINIVDTPG 77
Cdd:COG1100 1 MGEK--KIVVVGTGGVGKTSLVNRLVG----------------DIFSLEKYlstNGVTIDKKELKLDGLDVDLVIWDTPG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 78 HADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVT----KKAFAYGLKP--IVVINKVDRpgaRPDWVVDQVFDLfvnL 151
Cdd:COG1100 63 QDEFRETRQFYARQLTGASLYLFVVDGTREETLQSLyellESLRRLGKKSpiILVLNKIDL---YDEEEIEDEERL---K 136
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 49176434 152 DATDEQLDFPIVYASALNGiagldhedmaEDMTPLYQAIVDH 193
Cdd:COG1100 137 EALSEDNIVEVVATSAKTG----------EGVEELFAALAEI 168
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
7-170 |
2.71e-09 |
|
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN.
Pssm-ID: 206729 [Multi-domain] Cd Length: 209 Bit Score: 57.58 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 7 NIAIIAHVDHGKTTLVDKLLQQSGT-FDSRAETQER---------------VMDSNDLEKERGITIlakNTAikwndYR- 69
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSiFEDQLAALERskssgtqgekldlalLVDGLQAEREQGITI---DVA-----YRy 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 70 --------InIVDTPGHADFggevERVM----SMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDrpgar 136
Cdd:cd04166 73 fstpkrkfI-IADTPGHEQY----TRNMvtgaSTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVaVNKMD----- 142
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 49176434 137 pdwVVD---QVFDLFVN-LDATDEQLDFPIVYA---SALNG 170
Cdd:cd04166 143 ---LVDydeEVFEEIKAdYLAFAASLGIEDITFipiSALEG 180
|
|
| EFG_mtEFG_II |
cd04088 |
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation ... |
217-290 |
3.38e-09 |
|
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation factors G1 and G2; This family represents the domain II of bacterial Elongation factor G (EF-G)and mitochondrial Elongation factors G1 (mtEFG1) and G2 (mtEFG2). During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. In bacteria this translocation step is catalyzed by EF-G_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. mtEFG1 and mtEFG2 show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. No clear phenotype has been found for mutants in the yeast homolog of mtEFG2, MEF2.
Pssm-ID: 293905 [Multi-domain] Cd Length: 83 Bit Score: 53.68 E-value: 3.38e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49176434 217 YVGVIGIGRIKRGKVKPNQQVTIIdSEGKTRnaKVGKVLGHLGLERIETDLAEAGDIVAITGLGELNISDTVCD 290
Cdd:cd04088 13 FVGKLTFFRVYSGTLKSGSTVYNS-TKGKKE--RVGRLLRMHGKKREEVEELGAGDIGAVVGLKDTRTGDTLCD 83
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
8-170 |
4.38e-08 |
|
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. 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. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206682 [Multi-domain] Cd Length: 174 Bit Score: 53.21 E-value: 4.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 8 IAIIAHVDHGKTTLVDKLLQQsgtfdsraetqERVMDSNdlekERGITILAKNTAIKWNDYRINIVDTPG-----HADFG 82
Cdd:cd01895 5 IAIIGRPNVGKSSLLNALLGE-----------ERVIVSD----IAGTTRDSIDVPFEYDGQKYTLIDTAGirkkgKVTEG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 83 GE------VERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINK---VDRPGARPDWVVDQVFDLFVnlda 153
Cdd:cd01895 70 IEkysvlrTLKAIERADVVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKwdlVEKDEKTMKEFEKELRRKLP---- 145
|
170
....*....|....*...
gi 49176434 154 tdeQLDF-PIVYASALNG 170
Cdd:cd01895 146 ---FLDYaPIVFISALTG 160
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
14-285 |
7.01e-08 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 55.32 E-value: 7.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 14 VDHGKTTLVDKLLQQSGT-FDSRAETQER----------------VMDSNDLEKERGITIlakNTAIKW--NDYRINIV- 73
Cdd:PRK05506 33 VDDGKSTLIGRLLYDSKMiFEDQLAALERdskkvgtqgdeidlalLVDGLAAEREQGITI---DVAYRYfaTPKRKFIVa 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 74 DTPGHADFggevERVM----SMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDrpgarpdwVVD---QVF 145
Cdd:PRK05506 110 DTPGHEQY----TRNMvtgaSTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLaVNKMD--------LVDydqEVF 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 146 DLFV-NLDATDEQLDFPIVYA---SALNGiaglDHEDMAEDMTPLYQ-----AIVDHVPAPDVDLDGPFQMQI-----SQ 211
Cdd:PRK05506 178 DEIVaDYRAFAAKLGLHDVTFipiSALKG----DNVVTRSARMPWYEgpsllEHLETVEIASDRNLKDFRFPVqyvnrPN 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49176434 212 LDYNSYVGVIGIGRIKRGkvkpnQQVTIIDSeGKTrnAKVGKVLGHLGleriETDLAEAGDIVAITGLGELNIS 285
Cdd:PRK05506 254 LDFRGFAGTVASGVVRPG-----DEVVVLPS-GKT--SRVKRIVTPDG----DLDEAFAGQAVTLTLADEIDIS 315
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
8-176 |
8.73e-08 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 55.06 E-value: 8.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 8 IAIIAHVDHGKTTLVdkllqqsgtfdsRAETQervMDSNDL--EKERGITILAKNTAIKWNDYR-INIVDTPGHADF--- 81
Cdd:PRK10512 3 IATAGHVDHGKTTLL------------QAITG---VNADRLpeEKKRGMTIDLGYAYWPQPDGRvLGFIDVPGHEKFlsn 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 82 -----GGevervmsmVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPI-VVINKVDR-PGARPDWVVDQVFDLFVNLDAT 154
Cdd:PRK10512 68 mlagvGG--------IDHALLVVACDDGVMAQTREHLAILQLTGNPMLtVALTKADRvDEARIAEVRRQVKAVLREYGFA 139
|
170 180
....*....|....*....|...
gi 49176434 155 DEQLdFPIVYASALnGIAGL-DH 176
Cdd:PRK10512 140 EAKL-FVTAATEGR-GIDALrEH 160
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
7-129 |
9.72e-08 |
|
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: 50.70 E-value: 9.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 7 NIAIIAHVDHGKTTLVDKLLQQsgtfdsRAETqervmdSNDLekerGITILAKNTAIKWNDYRINIVDTPG-----HADF 81
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGA------KAIV------SDYP----GTTRDPNEGRLELKGKQIILVDTPGliegaSEGE 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 49176434 82 G-GEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINK 129
Cdd:pfam01926 65 GlGRAFLAIIEADLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
67-195 |
2.22e-07 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 52.68 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 67 DYRINIVDTPG-----HAdFG----GEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRpgARP 137
Cdd:COG1159 50 DAQIVFVDTPGihkpkRK-LGrrmnKAAWSALEDVDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDL--VKK 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 49176434 138 DwvvdqvfDLFVNLDATDEQLDF-PIVYASALNGIaGLDHedmaedmtpLYQAIVDHVP 195
Cdd:COG1159 127 E-------ELLPLLAEYSELLDFaEIVPISALKGD-NVDE---------LLDEIAKLLP 168
|
|
| EngA1 |
cd01894 |
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
63-131 |
4.19e-07 |
|
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. 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. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206681 [Multi-domain] Cd Length: 157 Bit Score: 49.74 E-value: 4.19e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 49176434 63 IKWNDYRINIVDTPGHADFGGE--------VERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVD 131
Cdd:cd01894 40 AEWGGREFILIDTGGIEPDDEGiskeireqAEIAIEEADVILFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKID 116
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
7-131 |
5.39e-07 |
|
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.
Pssm-ID: 206675 [Multi-domain] Cd Length: 197 Bit Score: 50.34 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 7 NIAIIAHVDHGKTTLVDKLlqqSGTFDSRaetqervmdsNDLEKERGITIlaK----NTAI-------KWNDY------- 68
Cdd:cd01888 2 NIGTIGHVAHGKTTLVKAL---SGVWTVR----------HKEELKRNITI--KlgyaNAKIykcpncgCPRPYdtpecec 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 69 -----------RINIVDTPGHadfggevERVM-------SMVDSVLLVVDAFDG-PMPQTR--FVTKKAFayGLKPIVVI 127
Cdd:cd01888 67 pgcggetklvrHVSFVDCPGH-------EILMatmlsgaAVMDGALLLIAANEPcPQPQTSehLAALEIM--GLKHIIIL 137
|
....*
gi 49176434 128 -NKVD 131
Cdd:cd01888 138 qNKID 142
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
67-175 |
9.09e-07 |
|
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.
Pssm-ID: 206726 [Multi-domain] Cd Length: 168 Bit Score: 49.00 E-value: 9.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 67 DYRINIVDTPG-HADFGG-------EVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRpgarpd 138
Cdd:cd04163 50 DAQIIFVDTPGiHKPKKKlgermvkAAWSALKDVDLVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDL------ 123
|
90 100 110
....*....|....*....|....*....|....*...
gi 49176434 139 wvVDQVFDLFVNLDATDEQLDF-PIVYASALNGIaGLD 175
Cdd:cd04163 124 --VKDKEDLLPLLEKLKELHPFaEIFPISALKGE-NVD 158
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
2-137 |
1.09e-06 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 51.72 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 2 IEKLRN--IAIIAHVDHGKTTLVDKLlqqSGTfdsraetqeRVMdsndlEKERG-IT--ILAknTAIKWN---------- 66
Cdd:PRK04004 1 EKKLRQpiVVVLGHVDHGKTTLLDKI---RGT---------AVA-----AKEAGgITqhIGA--TEVPIDviekiagplk 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 67 -DYRINI-------VDTPGHADF------GGevervmSMVDSVLLVVDAFDGPMPQT--------RFvtKKAFayglkpI 124
Cdd:PRK04004 62 kPLPIKLkipgllfIDTPGHEAFtnlrkrGG------ALADIAILVVDINEGFQPQTieainilkRR--KTPF------V 127
|
170
....*....|....
gi 49176434 125 VVINKVDR-PGARP 137
Cdd:PRK04004 128 VAANKIDRiPGWKS 141
|
|
| EFG_mtEFG_C |
cd03713 |
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational ... |
398-476 |
1.10e-06 |
|
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: 46.37 E-value: 1.10e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 49176434 398 EPYENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGkGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDVR 476
Cdd:cd03713 1 EPIMKVEVTVPEEYMGDVIGDLSSRRGQILGTESRG-GWKVIKAEVPLAEMFGYSTDLRSLTQGRGSFTMEFSHYEEVP 78
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
17-194 |
1.41e-06 |
|
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: 48.40 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 17 GKTTLVDKLLQQSgtfdsRAETqERVMdsndlekerGITILAKNTAIKWNDYR-INIVDTPGHADFGG-------EVERV 88
Cdd:cd00880 9 GKSSLLNALLGQN-----VGIV-SPIP---------GTTRDPVRKEWELLPLGpVVLIDTPGLDEEGGlgrerveEARQV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 89 MSMVDSVLLVVDAfDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDwvvDQVFDLFVNLdatdEQLDFPIVYASAL 168
Cdd:cd00880 74 ADRADLVLLVVDS-DLTPVEEEAKLGLLRERGKPVLLVLNKIDLVPESEE---EELLRERKLE----LLPDLPVIAVSAL 145
|
170 180
....*....|....*....|....*.
gi 49176434 169 NGiagldhedmaEDMTPLYQAIVDHV 194
Cdd:cd00880 146 PG----------EGIDELRKKIAELL 161
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
66-195 |
1.64e-06 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 50.05 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 66 NDYRINIVDTPG-HADfGGEVERVM------SM--VDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGAR 136
Cdd:PRK00089 51 DDAQIIFVDTPGiHKP-KRALNRAMnkaawsSLkdVDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLVKDK 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 137 pdwvvDQVFDLfvnLDATDEQLDF-PIVYASALNGIaGLDHedmaedmtpLYQAIVDHVP 195
Cdd:PRK00089 130 -----EELLPL---LEELSELMDFaEIVPISALKGD-NVDE---------LLDVIAKYLP 171
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
8-136 |
5.30e-06 |
|
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic orthologs of bacterial IF-2. Like IF-2, it helps convey the initiator tRNA to the ribosome, although the initiator is N-formyl-Met in bacteria and Met here. This protein is not closely related to the subunits of eIF-2 of eukaryotes, which is also involved in the initiation of translation. The aIF-2 of Methanococcus jannaschii contains a large intein interrupting a region of very strongly conserved sequence very near the amino end; the alignment generated by this model does not correctly align the sequences from Methanococcus jannaschii and Pyrococcus horikoshii in this region. [Protein synthesis, Translation factors]
Pssm-ID: 273104 [Multi-domain] Cd Length: 591 Bit Score: 49.43 E-value: 5.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 8 IAIIAHVDHGKTTLVDKLlqqSGTFDSRAE----TQERVMDSNDLEKERGIT-ILAKNTAIKWNDYRINIVDTPGHADFG 82
Cdd:TIGR00491 7 VVVLGHVDHGKTTLLDKI---RGTAVVKKEaggiTQHIGASEVPTDVIEKICgDLLKSFKIKLKIPGLLFIDTPGHEAFT 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 49176434 83 GEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDR-PGAR 136
Cdd:TIGR00491 84 NLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTPFVVAANKIDRiPGWK 138
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
63-200 |
1.71e-05 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 47.35 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 63 IKWNDYRINIVDTPG----HADFGGEV----ERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPG 134
Cdd:PRK00093 44 AEWLGREFILIDTGGiepdDDGFEKQIreqaELAIEEADVILFVVDGRAGLTPADEEIAKILRKSNKPVILVVNKVDGPD 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 49176434 135 ARpdwvvDQVFDlFVNLDATDEqldFPIvyaSALNGIaGLDHedmaedmtpLYQAIVDHVPAPDVD 200
Cdd:PRK00093 124 EE-----ADAYE-FYSLGLGEP---YPI---SAEHGR-GIGD---------LLDAILEELPEEEEE 167
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
63-200 |
2.25e-05 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 47.33 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 63 IKWNDYRINIVDTPG-----HADFGGE----VERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGlKP-IVVINKVDR 132
Cdd:COG1160 45 AEWGGREFTLIDTGGiepddDDGLEAEireqAELAIEEADVILFVVDGRAGLTPLDEEIAKLLRRSG-KPvILVVNKVDG 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 49176434 133 PGARPDwvvdqVFDLFvnldatdeQLDF-PIVYASALNGIaGLDheDmaedmtpLYQAIVDHVPAPDVD 200
Cdd:COG1160 124 PKREAD-----AAEFY--------SLGLgEPIPISAEHGR-GVG--D-------LLDAVLELLPEEEEE 169
|
|
| lepA_C |
cd03709 |
lepA_C: This family represents the C-terminal region of LepA, a GTP-binding protein localized ... |
398-474 |
2.71e-05 |
|
lepA_C: This family represents the C-terminal region of LepA, a GTP-binding protein localized in the cytoplasmic membrane. LepA is ubiquitous in Bacteria and Eukaryota (e.g. Saccharomyces cerevisiae GUF1p), but is missing from Archaea. LepA exhibits significant homology to elongation factors (EFs) Tu and G. The function(s) of the proteins in this family are unknown. The N-terminal domain of LepA is homologous to a domain of similar size found in initiation factor 2 (IF2), and in EF-Tu and EF-G (factors required for translation in Escherichia coli). Two types of phylogenetic tree, rooted by other GTP-binding proteins, suggest that eukaryotic homologs (including S. cerevisiae GUF1) originated within the bacterial LepA family. LepA has never been observed in archaea, and eukaryl LepA is organellar. LepA is therefore a true bacterial GTPase, found only in the bacterial lineage.
Pssm-ID: 239680 [Multi-domain] Cd Length: 80 Bit Score: 42.48 E-value: 2.71e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 49176434 398 EPYENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLI-GFRSEFMTMTSGtgllYSTFShYDD 474
Cdd:cd03709 1 EPFVKATIITPSEYLGAIMELCQERRGVQKDMEYLDANRVMLTYELPLAEIVyDFFDKLKSISKG----YASLD-YEL 73
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
7-193 |
2.89e-05 |
|
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.
Pssm-ID: 206739 [Multi-domain] Cd Length: 180 Bit Score: 44.84 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 7 NIAIIAHVDHGKTTLVDKLLqqsgtfdsraetQERVMDSndlekerGITIL-AKNTAIKWN-DYRINIVDTPG------- 77
Cdd:cd09912 2 LLAVVGEFSAGKSTLLNALL------------GEEVLPT-------GVTPTtAVITVLRYGlLKGVVLVDTPGlnstieh 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 78 HADfggEVERVMSMVDSVLLVVDAfDGPMPQT--RFVTKKAFAYGLKPIVVINKVDRpgARPDWVVDQVFDLFVNLDATD 155
Cdd:cd09912 63 HTE---ITESFLPRADAVIFVLSA-DQPLTESerEFLKEILKWSGKKIFFVLNKIDL--LSEEELEEVLEYSREELGVLE 136
|
170 180 190
....*....|....*....|....*....|....*....
gi 49176434 156 EQLDFPIVYA-SALNGIAGLDHEDMAEDMTPLYQAIVDH 193
Cdd:cd09912 137 LGGGEPRIFPvSAKEALEARLQGDEELLEQSGFEELEEH 175
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
8-176 |
3.65e-05 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 46.58 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 8 IAIIAHVDHGKTTLVDKLLQQsgtfdsraetqERVMDSNdlekERGITILAKNTAIKWNDYRINIVDTPG-------HAD 80
Cdd:PRK00093 176 IAIIGRPNVGKSSLINALLGE-----------ERVIVSD----IAGTTRDSIDTPFERDGQKYTLIDTAGirrkgkvTEG 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 81 fggeVE--------RVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDrpgarpdwVVDQ-VFDLFVN- 150
Cdd:PRK00093 241 ----VEkysvirtlKAIERADVVLLVIDATEGITEQDLRIAGLALEAGRALVIVVNKWD--------LVDEkTMEEFKKe 308
|
170 180
....*....|....*....|....*..
gi 49176434 151 LDATDEQLDF-PIVYASALNGIaGLDH 176
Cdd:PRK00093 309 LRRRLPFLDYaPIVFISALTGQ-GVDK 334
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
92-175 |
4.98e-05 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 44.70 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 92 VDSVLLVVdAFDGPMPQTRFVTK---KAFAYGLKPIVVINKVDRPgarPDWVVDQVFDLFvnldatdEQLDFPIVYASAL 168
Cdd:cd01854 3 VDQVLIVF-SLKEPFFNLRLLDRylvAAEASGIEPVIVLNKADLV---DDEELEELLEIY-------EKLGYPVLAVSAK 71
|
....*..
gi 49176434 169 NGIaGLD 175
Cdd:cd01854 72 TGE-GLD 77
|
|
| MJ1464 |
cd01859 |
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ... |
85-167 |
2.86e-04 |
|
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents archaeal GTPase typified by the protein MJ1464 from Methanococcus jannaschii. The members of this family show a circular permutation of the GTPase signature motifs so that C-terminal strands 5, 6, and 7 (strands 6 contain the NKxD motif) are relocated to the N terminus.
Pssm-ID: 206752 [Multi-domain] Cd Length: 157 Bit Score: 41.53 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 85 VERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDrpgARPDWVVDQVFDLFvnldatdEQLDFPIVY 164
Cdd:cd01859 5 VRRIIKEADVVLEVVDARDPELTRSRKLERMALELGKKLIIVLNKAD---LVPREVLEKWKEVF-------ESEGLPVVY 74
|
...
gi 49176434 165 ASA 167
Cdd:cd01859 75 VSA 77
|
|
| EFG_C |
smart00838 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
398-475 |
3.72e-04 |
|
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: 39.41 E-value: 3.72e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 49176434 398 EPYENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGkGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDV 475
Cdd:smart00838 3 EPIMKVEVTVPEEYMGDVIGDLNSRRGKIEGMEQRG-GAQVIKAKVPLSEMFGYATDLRSATQGRATWSMEFSHYEEV 79
|
|
| mtEFG1_C |
cd04097 |
mtEFG1_C: C-terminus of mitochondrial Elongation factor G1 (mtEFG1)-like proteins found in ... |
398-472 |
8.12e-04 |
|
mtEFG1_C: C-terminus of mitochondrial Elongation factor G1 (mtEFG1)-like proteins found in eukaryotes. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. Eukaryotic EF-2 operates in the cytosolic protein synthesis machinery of eukaryotes, EF-Gs in protein synthesis in bacteria. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. There are two forms of mtEFG present in mammals (designated mtEFG1s and mtEFG2s) mtEFG2s are not present in this group.
Pssm-ID: 239764 [Multi-domain] Cd Length: 78 Bit Score: 38.46 E-value: 8.12e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 49176434 398 EPYENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGkGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHY 472
Cdd:cd04097 1 EPIMKVEVTAPTEFQGNVIGLLNKRKGTIVDTDTGE-DEFTLEAEVPLNDMFGYSTELRSMTQGKGEFSMEFSRY 74
|
|
| PRK09518 |
PRK09518 |
bifunctional cytidylate kinase/GTPase Der; Reviewed |
3-133 |
2.34e-03 |
|
bifunctional cytidylate kinase/GTPase Der; Reviewed
Pssm-ID: 236546 [Multi-domain] Cd Length: 712 Bit Score: 40.93 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 3 EKLRNIAIIAHVDHGKTTLVDKLL--QQSGTFDSRAETQERVmdSNDLEkergitilakntaikWNDYRINIVDTPG--- 77
Cdd:PRK09518 273 KAVGVVAIVGRPNVGKSTLVNRILgrREAVVEDTPGVTRDRV--SYDAE---------------WAGTDFKLVDTGGwea 335
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 49176434 78 -----HADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRP 133
Cdd:PRK09518 336 dvegiDSAIASQAQIAVSLADAVVFVVDGQVGLTSTDERIVRMLRRAGKPVVLAVNKIDDQ 396
|
|
| EFG_III |
cd16262 |
Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial ... |
330-386 |
2.74e-03 |
|
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: 36.66 E-value: 2.74e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 49176434 330 QILDRLNKElvhNVALRVEETEDADAFRVSGRGELHLSVLIENMRRE-GFELAVSRPK 386
Cdd:cd16262 22 KALARLAEE---DPTLRVSRDEETGQTILSGMGELHLEIIVERLKREyGVEVEVGKPQ 76
|
|
| MnmE |
COG0486 |
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
63-205 |
2.82e-03 |
|
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440253 [Multi-domain] Cd Length: 448 Bit Score: 40.43 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 63 IKWNDYRINIVDTPGHADFGGEVER--------VMSMVDSVLLVVDAFDGPMPQTRFVTKKAFayGLKPIVVINKVDRPG 134
Cdd:COG0486 256 INIGGIPVRLIDTAGLRETEDEVEKigierareAIEEADLVLLLLDASEPLTEEDEEILEKLK--DKPVIVVLNKIDLPS 333
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 49176434 135 ARPDWVvdqvfdlfvnldatDEQLDFPIVYASALNGiAGLDHedmaedmtpLYQAIVDHVPAPDVDLDGPF 205
Cdd:COG0486 334 EADGEL--------------KSLPGEPVIAISAKTG-EGIDE---------LKEAILELVGEGALEGEGVL 380
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
204-276 |
3.39e-03 |
|
Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 293899 [Multi-domain] Cd Length: 84 Bit Score: 36.71 E-value: 3.39e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 49176434 204 PFQMQISQLdYNSYVGVIGIGRIKRGKVKPNQQVTIIDSEgktRNAKVGKVLGHlglERIETDLAEAGDIVAI 276
Cdd:cd03698 1 PFRLSIDDK-YKSPRGTTVTGKLEAGSIQKNQVLYDMPSQ---QDAEVKNIIRN---SDEETDWAIAGDTVTL 66
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|
| EF2_II |
cd16268 |
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 ... |
219-281 |
3.99e-03 |
|
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: 36.81 E-value: 3.99e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 219 GVIGIGRIKRGKVKPNQQVTIIDSE---GKTRNAKVGKVLgHLGL----ERIETDLAEAGDIVAITGLGE 281
Cdd:cd16268 17 GFVAFGRVFSGTVRRGQEVYILGPKyvpGKKDDLKKKRIQ-QTYLmmgrEREPVDEVPAGNIVGLVGLDD 85
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
92-175 |
6.33e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 37.91 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 92 VDSVLLVVdAFDGPMPQTRFVTK---KAFAYGLKPIVVINKVDrpgarpdwVVDQVfDLFVNLDATDEQLDFPIVYASAL 168
Cdd:pfam03193 23 VDQAVIVF-SLKEPDFNLNLLDRflvLAEASGIEPVIVLNKID--------LLDEE-EELEELLKIYRAIGYPVLFVSAK 92
|
....*..
gi 49176434 169 NGiAGLD 175
Cdd:pfam03193 93 TG-EGIE 98
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
3-170 |
6.75e-03 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 39.24 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 3 EKLRNIAIIAHVDHGKTTLVDKLLQQsgtfdsraetqERVMDSNdlekERGITILAKNTAIKWNDYRINIVDTPG----- 77
Cdd:COG1160 173 DDPIKIAIVGRPNVGKSSLINALLGE-----------ERVIVSD----IAGTTRDSIDTPFERDGKKYTLIDTAGirrkg 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 78 --HADfggeVERvMSMVDS---------VLLVVDAFDGpmpqtrfVT---KKAFAYGL---KPIV-VINK---VDRPGAR 136
Cdd:COG1160 238 kvDEG----IEK-YSVLRTlraieradvVLLVIDATEG-------ITeqdLKIAGLALeagKALViVVNKwdlVEKDRKT 305
|
170 180 190
....*....|....*....|....*....|....
gi 49176434 137 PDWVVDQVFDLFVNLDatdeqlDFPIVYASALNG 170
Cdd:COG1160 306 REELEKEIRRRLPFLD------YAPIVFISALTG 333
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|
| Tet_C |
cd03711 |
Tet_C: C-terminus of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology ... |
398-473 |
6.96e-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: 35.68 E-value: 6.96e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 49176434 398 EPYENVTLDVEEQHQGSVMQALGERKGDLKNmnPDGKG-RVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYD 473
Cdd:cd03711 1 EPYLRFELEVPQDALGRAMSDLAKMGATFED--PQIKGdEVTLEGTIPVATSQDYQSELPSYTHGEGVLETEFKGYR 75
|
|
| PRK03003 |
PRK03003 |
GTP-binding protein Der; Reviewed |
8-138 |
7.01e-03 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 179525 [Multi-domain] Cd Length: 472 Bit Score: 39.18 E-value: 7.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176434 8 IAIIAHVDHGKTTLVDKLL--QQSGTFDSRAETQERVmdSNDLEkergitilakntaikWNDYRINIVDTPG-------- 77
Cdd:PRK03003 41 VAVVGRPNVGKSTLVNRILgrREAVVEDVPGVTRDRV--SYDAE---------------WNGRRFTVVDTGGwepdakgl 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 49176434 78 HADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPD 138
Cdd:PRK03003 104 QASVAEQAEVAMRTADAVLFVVDATVGATATDEAVARVLRRSGKPVILAANKVDDERGEAD 164
|
|
| EFG_III |
pfam14492 |
Elongation Factor G, domain III; This domain is found in Elongation Factor G. It shares a ... |
335-376 |
9.05e-03 |
|
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: 35.53 E-value: 9.05e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 49176434 335 LNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRRE 376
Cdd:pfam14492 25 LNRLLEEDPTLRVERDEETGETILSGMGELHLEIVVDRLKRK 66
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