|
Name |
Accession |
Description |
Interval |
E-value |
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
1-606 |
0e+00 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 1247.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 1 MIENLRNIAIIAHVDHGKTTLVDKLLQQSGTFDARTEAQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHAD 80
Cdd:COG1217 2 MREDIRNIAIIAHVDHGKTTLVDALLKQSGTFRENQEVAERVMDSNDLERERGITILAKNTAVRYKGVKINIVDTPGHAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 81 FGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDF 160
Cdd:COG1217 82 FGGEVERVLSMVDGVLLLVDAFEGPMPQTRFVLKKALELGLKPIVVINKIDRPDARPDEVVDEVFDLFIELGATDEQLDF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 161 PIVYASALNGIAGLDHEDMAEDMTPLYQAIVDRVPAPDVDLDGPLQMQISQLDYNNYVGVIGIGRIKRGKVKPNQQITII 240
Cdd:COG1217 162 PVVYASARNGWASLDLDDPGEDLTPLFDTILEHVPAPEVDPDGPLQMLVTNLDYSDYVGRIAIGRIFRGTIKKGQQVALI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 241 DSEGKTRNGKVGKVLTHLGLERIESDVAEAGDIIAITGLGELNISDTICDPQNVEALPALSVDEPTVSMFFNVNTSPFCG 320
Cdd:COG1217 242 KRDGKVEKGKITKLFGFEGLERVEVEEAEAGDIVAIAGIEDINIGDTICDPENPEALPPIKIDEPTLSMTFSVNDSPFAG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 321 KEGKFVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRREGFEMAVSRPKVIFREIDGRKQEPF 400
Cdd:COG1217 322 REGKFVTSRQIRERLEKELETNVALRVEETDSPDAFKVSGRGELHLSILIETMRREGYELQVSRPEVIFKEIDGKKLEPI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 401 ENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDVRpGEV 480
Cdd:COG1217 402 EELTIDVPEEYSGAVIEKLGQRKGEMTNMEPDGGGRVRLEFLIPSRGLIGFRTEFLTDTRGTGIMNHVFDGYEPYK-GEI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 481 GQRNNGVLISNGQGKAVAFALFGLQDRGKLFLGHGAEVYEGQIIGIHSRSNDLTVNCLTGKKLTNMRASGTDEATVLVPP 560
Cdd:COG1217 481 PGRRNGSLISMETGKATAYALFNLQERGTLFIGPGTEVYEGMIVGEHSRDNDLVVNVCKEKKLTNMRASGSDEAIRLTPP 560
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 505181868 561 VKMTLEQALEFIDDDELVEVTPTSIRIRKRHLTENDRKRAMRGAKE 606
Cdd:COG1217 561 RKMSLEQALEFIEDDELVEVTPKSIRLRKKILDENERKRAAKKKKK 606
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
1-607 |
0e+00 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 1209.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 1 MIENLRNIAIIAHVDHGKTTLVDKLLQQSGTFDARTEAQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHAD 80
Cdd:PRK10218 1 MIEKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 81 FGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDF 160
Cdd:PRK10218 81 FGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 161 PIVYASALNGIAGLDHEDMAEDMTPLYQAIVDRVPAPDVDLDGPLQMQISQLDYNNYVGVIGIGRIKRGKVKPNQQITII 240
Cdd:PRK10218 161 PIVYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTII 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 241 DSEGKTRNGKVGKVLTHLGLERIESDVAEAGDIIAITGLGELNISDTICDPQNVEALPALSVDEPTVSMFFNVNTSPFCG 320
Cdd:PRK10218 241 DSEGKTRNAKVGKVLGHLGLERIETDLAEAGDIVAITGLGELNISDTVCDTQNVEALPALSVDEPTVSMFFCVNTSPFCG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 321 KEGKFVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRREGFEMAVSRPKVIFREIDGRKQEPF 400
Cdd:PRK10218 321 KEGKFVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRREGFELAVSRPKVIFREIDGRKQEPY 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 401 ENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDVRPGEV 480
Cdd:PRK10218 401 ENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDVRPGEV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 481 GQRNNGVLISNGQGKAVAFALFGLQDRGKLFLGHGAEVYEGQIIGIHSRSNDLTVNCLTGKKLTNMRASGTDEATVLVPP 560
Cdd:PRK10218 481 GQRQNGVLISNGQGKAVAFALFGLQDRGKLFLGHGAEVYEGQIIGIHSRSNDLTVNCLTGKKLTNMRASGTDEAVVLVPP 560
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 505181868 561 VKMTLEQALEFIDDDELVEVTPTSIRIRKRHLTENDRKRAMRGAKEE 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: 1054.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 5 LRNIAIIAHVDHGKTTLVDKLLQQSGTFDARTEAQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGE 84
Cdd:TIGR01394 1 IRNIAIIAHVDHGKTTLVDALLKQSGTFRANEAVAERVMDSNDLERERGITILAKNTAIRYNGTKINIVDTPGHADFGGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 85 VERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDFPIVY 164
Cdd:TIGR01394 81 VERVLGMVDGVLLLVDASEGPMPQTRFVLKKALELGLKPIVVINKIDRPSARPDEVVDEVFDLFAELGADDEQLDFPIVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 165 ASALNGIAGLDHEDMAEDMTPLYQAIVDRVPAPDVDLDGPLQMQISQLDYNNYVGVIGIGRIKRGKVKPNQQITIIDSEG 244
Cdd:TIGR01394 161 ASGRAGWASLDLDDPSDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVHRGTVKKGQQVALMKRDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 245 KTRNGKVGKVLTHLGLERIESDVAEAGDIIAITGLGELNISDTICDPQNVEALPALSVDEPTVSMFFNVNTSPFCGKEGK 324
Cdd:TIGR01394 241 TIENGRISKLLGFEGLERVEIDEAGAGDIVAVAGLEDINIGETIADPEVPEALPTITVDEPTLSMTFSVNDSPLAGKEGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 325 FVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRREGFEMAVSRPKVIFREIDGRKQEPFENVT 404
Cdd:TIGR01394 321 KVTSRHIRDRLMRELETNVALRVEDTESADKFEVSGRGELHLSILIETMRREGFELQVGRPQVIYKEIDGKKLEPIEELT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 405 LDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDVRpGEVGQRN 484
Cdd:TIGR01394 401 IDVPEEHVGAVIEKLGKRKGEMVDMEPSGNGRTRLEFKIPSRGLIGFRTEFLTDTRGTGIMNHVFDEYEPWK-GEIETRR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 485 NGVLISNGQGKAVAFALFGLQDRGKLFLGHGAEVYEGQIIGIHSRSNDLTVNCLTGKKLTNMRASGTDEATVLVPPVKMT 564
Cdd:TIGR01394 480 NGSLVSMEDGTATAYALWNLQERGVMFVSPGTEVYEGMIIGEHSRENDLDVNPCKAKKLTNVRSSGKDEAVKLTPPRKLS 559
|
570 580 590
....*....|....*....|....*....|....*
gi 505181868 565 LEQALEFIDDDELVEVTPTSIRIRKRHLTENDRKR 599
Cdd:TIGR01394 560 LEQALEYIEDDELVEVTPKSIRLRKRVLDPNERKR 594
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
4-197 |
5.72e-134 |
|
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: 389.26 E-value: 5.72e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 4 NLRNIAIIAHVDHGKTTLVDKLLQQSGTFDARTEAQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGG 83
Cdd:cd01891 1 KIRNIAIIAHVDHGKTTLVDALLKQSGTFRENEEVGERVMDSNDLERERGITILAKNTAITYKDTKINIIDTPGHADFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 84 EVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDFPIV 163
Cdd:cd01891 81 EVERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDRPDARPEEVVDEVFDLFLELNATDEQLDFPIV 160
|
170 180 190
....*....|....*....|....*....|....
gi 505181868 164 YASALNGIAGLDHEDMAEDMTPLYQAIVDRVPAP 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 |
3.14e-73 |
|
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: 232.80 E-value: 3.14e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 3 ENLRNIAIIAHVDHGKTTLVDKLLQQSGTFDARTE---AQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHA 79
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEvkgEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 80 DFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDRP-GARPDWVVDQVFDLFVNLDATDEqL 158
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVdGAELEEVVEEVSRELLEKYGEDG-E 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 505181868 159 DFPIVYASALNGIAgldhedmaedMTPLYQAIVDRVPA 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 |
1.57e-72 |
|
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: 243.77 E-value: 1.57e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 3 ENLRNIAIIAHVDHGKTTLVDKLLQQSGTFDARtEAQERVMDSNDLEKERGITILAKNTAIKW-----NDYRINIVDTPG 77
Cdd:TIGR01393 1 KNIRNFSIIAHIDHGKSTLADRLLEYTGAISER-EMREQVLDSMDLERERGITIKAQAVRLNYkakdgETYVLNLIDTPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 78 HADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDRPGARPDWVVDQVFDLfVNLDATDeq 157
Cdd:TIGR01393 80 HVDFSYEVSRSLAACEGALLLVDAAQGIEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKKEIEEV-IGLDASE-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 158 ldfpIVYASALNGIaGLDHedmaedmtpLYQAIVDRVPAPDVDLDGPLQMQISQLDYNNYVGVIGIGRIKRGKVKPNQQI 237
Cdd:TIGR01393 157 ----AILASAKTGI-GIEE---------ILEAIVKRVPPPKGDPDAPLKALIFDSHYDNYRGVVALVRVFEGTIKPGDKI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 238 TIIDSEGKTRNGKVGkVLTHLGLERIESDVAEAGDIIA-ITGLGELNISDTI--CDPQNVEALPALSVDEPTV-SMFFNV 313
Cdd:TIGR01393 223 RFMSTGKEYEVDEVG-VFTPKLTKTDELSAGEVGYIIAgIKDVSDVRVGDTIthVKNPAKEPLPGFKEVKPMVfAGLYPI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 314 NTSPFcgkegkfvtsRQILDRLNKELVHNVALRVE-ETEDA--DAFRVSGRGELHLSVLIENMRREgFEMAV--SRPKVI 388
Cdd:TIGR01393 302 DTEDY----------EDLRDALEKLKLNDASLTYEpESSPAlgFGFRCGFLGLLHMEIIQERLERE-FNLDLitTAPSVI 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 389 FR---------EIDG-----------RKQEPFENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIP-SRG 447
Cdd:TIGR01393 371 YRvyltngeviEVDNpsdlpdpgkieHVEEPYVKATIITPTEYLGPIMTLCQEKRGVQTNMEYLDPNRVELIYEMPlAEI 450
|
490 500 510
....*....|....*....|....*....|...
gi 505181868 448 LIGFRSEFMTMTSGtgllYSTFS-HYDDVRPGE 479
Cdd:TIGR01393 451 VYDFFDKLKSISRG----YASFDyELIGYRPSD 479
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
3-444 |
1.76e-70 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 238.38 E-value: 1.76e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 3 ENLRNIAIIAHVDHGKTTLVDKLLQQSGTFDARtEAQERVMDSNDLEKERGITILAKNTAIKW-----NDYRINIVDTPG 77
Cdd:COG0481 4 KNIRNFSIIAHIDHGKSTLADRLLELTGTLSER-EMKEQVLDSMDLERERGITIKAQAVRLNYkakdgETYQLNLIDTPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 78 HADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDRPGARPDWVVDQVFDLFvNLDATDeq 157
Cdd:COG0481 83 HVDFSYEVSRSLAACEGALLVVDASQGVEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKQEIEDII-GIDASD-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 158 ldfpIVYASALNGIaGLDHedmaedmtpLYQAIVDRVPAPDVDLDGPLQMQIsqLD--YNNYVGVIGIGRIKRGKVKPNQ 235
Cdd:COG0481 160 ----AILVSAKTGI-GIEE---------ILEAIVERIPPPKGDPDAPLQALI--FDswYDSYRGVVVYVRVFDGTLKKGD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 236 QITIIdsegktRNGKVGKVlTHLG---LERIESDVAEAGD---IIA-ITGLGELNISDTICDPQN--VEALPALsvdEPT 306
Cdd:COG0481 224 KIKMM------STGKEYEV-DEVGvftPKMTPVDELSAGEvgyIIAgIKDVRDARVGDTITLAKNpaAEPLPGF---KEV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 307 VSM----FFNVNTSpfcgkegKFVTSRQILDRLnkELvhNVALRVEETEDADA----FRVSGRGELHLSVLIENMRREgF 378
Cdd:COG0481 294 KPMvfagLYPVDSD-------DYEDLRDALEKL--QL--NDASLTYEPETSAAlgfgFRCGFLGLLHMEIIQERLERE-F 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 379 EMAV--SRPKVIFR---------------------EIDgRKQEPFENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKG 435
Cdd:COG0481 362 DLDLitTAPSVVYEvtltdgevievdnpsdlpdpgKIE-EIEEPIVKATIITPSEYVGAVMELCQEKRGVQKNMEYLGEN 440
|
....*....
gi 505181868 436 RVRLDYVIP 444
Cdd:COG0481 441 RVELTYELP 449
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
3-439 |
4.85e-66 |
|
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: 229.40 E-value: 4.85e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 3 ENLRNIAIIAHVDHGKTTLVDKLLQQSGTFDARTEAQERVMDSNDLEKERGITILAKNTAI----KWNDYRINIVDTPGH 78
Cdd:TIGR00490 17 KFIRNIGIVAHIDHGKTTLSDNLLAGAGMISEELAGQQLYLDFDEQEQERGITINAANVSMvheyEGNEYLINLIDTPGH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 79 ADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQL 158
Cdd:TIGR00490 97 VDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKPVLFINKVDRLINELKLTPQELQERFIKIITEVNKL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 159 ------------------DFPIVYASALNGIA---------GLDHEDMAEDMT-----------PLYQAIVDRV----PA 196
Cdd:TIGR00490 177 ikamapeefrdkwkvrveDGSVAFGSAYYNWAisvpsmkktGIGFKDIYKYCKedkqkelakksPLHQVVLDMVirhlPS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 197 P-------------------------DVDLDGPLQMQISQLDYNNYVGVIGIGRIKRGKVKPNQQITIIDSEGKTRNGKV 251
Cdd:TIGR00490 257 PieaqkyripviwkgdlnsevgkamlNCDPKGPLALMITKIVVDKHAGEVAVGRLYSGTIRPGMEVYIVDRKAKARIQQV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 252 GkvlTHLGLERIESDVAEAGDIIAITGLGELNISDTICDP-QNVEALPALS-VDEPTVSMFFNV-NTSPFcgkeGKFVts 328
Cdd:TIGR00490 337 G---VYMGPERVEVDEIPAGNIVAVIGLKDAVAGETICTTvENITPFESIKhISEPVVTVAIEAkNTKDL----PKLI-- 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 329 rQILDRLNKElvhNVALRVEETEDADAFRVSGRGELHLSVLIENMRRE-GFEMAVSRPKVIFREIDGRKQEPFE------ 401
Cdd:TIGR00490 408 -EVLRQVAKE---DPTVHVEINEETGEHLISGMGELHLEIIVEKIREDyGLDVETSPPIVVYRETVTGTSPVVEgkspnk 483
|
490 500 510
....*....|....*....|....*....|....*....
gi 505181868 402 -NVTLDVEEQHQGSVMQALGErkGDLKNMNPDGKGRVRL 439
Cdd:TIGR00490 484 hNRFYIVVEPLEESVIQAFKE--GKIVDMKMKKKERRRL 520
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
2-401 |
7.01e-62 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 218.19 E-value: 7.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 2 IENLRNIAIIAHVDHGKTTLVDKLLQQSGTFDARTEAQERVMDSNDLEKERGITILAKNTAI----KWNDYRINIVDTPG 77
Cdd:PRK07560 17 PEQIRNIGIIAHIDHGKTTLSDNLLAGAGMISEELAGEQLALDFDEEEQARGITIKAANVSMvheyEGKEYLINLIDTPG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 78 HADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDR--------P---GARPDWVVDQVFD 146
Cdd:PRK07560 97 HVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKPVLFINKVDRlikelkltPqemQQRLLKIIKDVNK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 147 LFVN-----------LDATDEQLDFpivyASALNGIA---------GLDHEDM-----AEDM------TPLYQAIVDRV- 194
Cdd:PRK07560 177 LIKGmapeefkekwkVDVEDGTVAF----GSALYNWAisvpmmqktGIKFKDIidyyeKGKQkelaekAPLHEVVLDMVv 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 195 ---PAP-------------------------DVDLDGPLQMQISQLDYNNYVGVIGIGRIKRGKVKPNQQITIIDSEGKT 246
Cdd:PRK07560 253 khlPNPieaqkyripkiwkgdlnsevgkamlNCDPNGPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLVGAKKKN 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 247 RngkVGKVLTHLGLERIESDVAEAGDIIAITGLGELNISDTICDPQNVEALPALS-VDEPTVSMFF---NVNTSPfcgke 322
Cdd:PRK07560 333 R---VQQVGIYMGPEREEVEEIPAGNIAAVTGLKDARAGETVVSVEDMTPFESLKhISEPVVTVAIeakNPKDLP----- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 323 gKFVtsrQILDRLNKElvhNVALRVEETEDADAFRVSGRGELHLSVLIENMRRE-GFEMAVSRPKVIFREIDGRKQEPFE 401
Cdd:PRK07560 405 -KLI---EVLRQLAKE---DPTLVVKINEETGEHLLSGMGELHLEVITYRIKRDyGIEVVTSEPIVVYRETVRGKSQVVE 477
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
7-197 |
2.51e-61 |
|
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: 201.37 E-value: 2.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDARTEAQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVE 86
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 87 RVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDRPG-ARPDWVVDQVFDLFVNLDAT-DEQLDFPIVY 164
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGeEDFDEVLREIKELLKLIGFTfLKGKDVPIIP 160
|
170 180 190
....*....|....*....|....*....|...
gi 505181868 165 ASALNGIagldhedmaeDMTPLYQAIVDRVPAP 197
Cdd:cd00881 161 ISALTGE----------GIEELLDAIVEHLPPP 183
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
2-408 |
1.58e-57 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 205.19 E-value: 1.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 2 IENLRNIAIIAHVDHGKTTLVDKLLQQSGTFDARTEAQE--RVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHA 79
Cdd:PRK13351 5 LMQIRNIGILAHIDAGKTTLTERILFYTGKIHKMGEVEDgtTVTDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 80 DFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDRPGARPDWVVDQ---------------- 143
Cdd:PRK13351 85 DFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLFKVLEDieerfgkrplplqlpi 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 144 --------VFDLFVN----------------------------------LDA------------------TDEQLD---- 159
Cdd:PRK13351 165 gsedgfegVVDLITEpelhfsegdggstveegpipeelleeveeareklIEAlaefddellelylegeelSAEQLRaplr 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 160 --------FPIVYASALNGIAgldhedmaedMTPLYQAIVDRVPAP------------------DVDLDGPLQMQISQLD 213
Cdd:PRK13351 245 egtrsghlVPVLFGSALKNIG----------IEPLLDAVVDYLPSPlevppprgskdngkpvkvDPDPEKPLLALVFKVQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 214 YNNYVGVIGIGRIKRGKVKPNQQITIIDSEgktRNGKVGKVLTHLGLERIESDVAEAGDIIAITGLGELNISDTICDPQN 293
Cdd:PRK13351 315 YDPYAGKLTYLRVYSGTLRAGSQLYNGTGG---KREKVGRLFRLQGNKREEVDRAKAGDIVAVAGLKELETGDTLHDSAD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 294 VEALPALSVDEPTVSMFFnvntspfcgkEGKFVTSRQ-ILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIEN 372
Cdd:PRK13351 392 PVLLELLTFPEPVVSLAV----------EPERRGDEQkLAEALEKLVWEDPSLRVEEDEETGQTILSGMGELHLEVALER 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 505181868 373 MRRE-GFEMAVSRPKVIFRE---------------IDGRKQepFENVTLDVE 408
Cdd:PRK13351 462 LRREfKLEVNTGKPQVAYREtirkmaegvyrhkkqFGGKGQ--FGEVHLRVE 511
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
11-483 |
8.25e-56 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 199.97 E-value: 8.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 11 IAHVDHGKTTLVDKLLQQSGTFDA--RTEAQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVERV 88
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRigEVEDGTTTMDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVERA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 89 MSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDRPGARPDWVVDQV--------------------FDLF 148
Cdd:PRK12740 81 LRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRAGADFFRVLAQLqeklgapvvplqlpigegddFTGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 149 VNL-----------------DATDEQLD------------------------------------------------FPIV 163
Cdd:PRK12740 161 VDLlsmkayrydeggpseeiEIPAELLDraeeareellealaefddelmekylegeelseeeikaglrkatlageiVPVF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 164 YASALNGIAgldhedmaedMTPLYQAIVDRVPAPD-----------------VDLDGPLQMQISQLDYNNYVGVIGIGRI 226
Cdd:PRK12740 241 CGSALKNKG----------VQRLLDAVVDYLPSPLevppvdgedgeegaelaPDPDGPLVALVFKTMDDPFVGKLSLVRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 227 KRGKVKPNQQITIIDSEGKTRngkVGKVLTHLGLERIESDVAEAGDIIAITGLGELNISDTICDPQNVEALPALSVDEPT 306
Cdd:PRK12740 311 YSGTLKKGDTLYNSGTGKKER---VGRLYRMHGKQREEVDEAVAGDIVAVAKLKDAATGDTLCDKGDPILLEPMEFPEPV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 307 VSMffnvntspfcgkegkFVTSR---------QILDRLNKElvhNVALRVEETEDADAFRVSGRGELHLSVLIENMRRE- 376
Cdd:PRK12740 388 ISL---------------AIEPKdkgdeeklsEALGKLAEE---DPTLRVERDEETGQTILSGMGELHLDVALERLKREy 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 377 GFEMAVSRPKVIFRE-------IDGR--KQ-------------------------------------------------- 397
Cdd:PRK12740 450 GVEVETGPPQVPYREtirkkaeGHGRhkKQsgghgqfgdvwleveplprgegfefvdkvvggavprqyipavekgvreal 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 398 ----------------------------------------------------EPFENVTLDVEEQHQGSVMQALGERKGD 425
Cdd:PRK12740 530 ekgvlagypvvdvkvtltdgsyhsvdssemafkiaarlafrealpkakpvllEPIMKVEVSVPEEFVGDVIGDLSSRRGR 609
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 505181868 426 LKNMNPDGKG-RVRLDyvIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDVrPGEVGQR 483
Cdd:PRK12740 610 ILGMESRGGGdVVRAE--VPLAEMFGYATDLRSLTQGRGSFSMEFSHYEEV-PGNVAEK 665
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
2-391 |
1.26e-53 |
|
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: 194.49 E-value: 1.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 2 IENLRNIAIIAHVDHGKTTLVDKLLQQSGTFDARTEAQE--RVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHA 79
Cdd:COG0480 6 LEKIRNIGIVAHIDAGKTTLTERILFYTGAIHRIGEVHDgnTVMDWMPEEQERGITITSAATTCEWKGHKINIIDTPGHV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 80 DFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDRPGARPDWVVDQV--------------- 144
Cdd:COG0480 86 DFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQLkerlganpvplqlpi 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 145 -----FDLFVNL--------------------------------------------DA-----------TDEQLD----- 159
Cdd:COG0480 166 gaeddFKGVIDLvtmkayvyddelgakyeeeeipaelkeeaeeareelieavaetdDElmekylegeelTEEEIKaglrk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 160 -------FPIVYASALNGIaGLDhedmaedmtPLYQAIVDRVPAPD-------------------VDLDGPLQMQISQLD 213
Cdd:COG0480 246 atlagkiVPVLCGSAFKNK-GVQ---------PLLDAVVDYLPSPLdvpaikgvdpdtgeeverkPDDDEPFSALVFKTM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 214 YNNYVGVIGIGRIKRGKVKPNQQITIIDSEGKTRngkVGKVLTHLGLERIESDVAEAGDIIAITGLGELNISDTICDPQN 293
Cdd:COG0480 316 TDPFVGKLSFFRVYSGTLKSGSTVYNSTKGKKER---IGRLLRMHGNKREEVDEAGAGDIVAVVKLKDTTTGDTLCDEDH 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 294 VEALPALSVDEPTVSMFFNVNTSpfcGKEGKFVTSrqiLDRLNKElvhNVALRVEETEDADAFRVSGRGELHLSVLIENM 373
Cdd:COG0480 393 PIVLEPIEFPEPVISVAIEPKTK---ADEDKLSTA---LAKLAEE---DPTFRVETDEETGQTIISGMGELHLEIIVDRL 463
|
490
....*....|....*....
gi 505181868 374 RRE-GFEMAVSRPKVIFRE 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 |
1.79e-51 |
|
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: 175.03 E-value: 1.79e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 6 RNIAIIAHVDHGKTTLVDKLLQQSGTFDARtEAQERVMDSNDLEKERGITILAKNTAIKW-----NDYRINIVDTPGHAD 80
Cdd:cd01890 1 RNFSIIAHIDHGKSTLADRLLELTGTVSER-EMKEQVLDSMDLERERGITIKAQAVRLFYkakdgEEYLLNLIDTPGHVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 81 FGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDRPGARPDWVVDQVFDLFvNLDATDeqldf 160
Cdd:cd01890 80 FSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVKQEIEDVL-GLDASE----- 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 505181868 161 pIVYASALNGIaGLDHedmaedmtpLYQAIVDRVPAP 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 |
2.97e-47 |
|
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: 160.17 E-value: 2.97e-47
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505181868 305 PTVSMFFNVNTSPFCGKEGKFVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRREGFEMAVS 383
Cdd:cd16263 1 PTVSMTFGVNTSPFAGREGKFVTSRKIRDRLEKELETNVALRVEETESPDSFIVSGRGELHLSILIETMRREGFELQVS 79
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
6-132 |
1.87e-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: 160.09 E-value: 1.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 6 RNIAIIAHVDHGKTTLVDKLLQQSGTFDARTEAQERVMDSNDLEKERGITIlaKNTAI-----------KWNDYRINIVD 74
Cdd:cd01885 1 RNICIIAHVDHGKTTLSDSLLASAGIISEKLAGKARYLDTREDEQERGITI--KSSAIslyfeyeeekmDGNDYLINLID 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 505181868 75 TPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDR 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 |
1.52e-42 |
|
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: 147.72 E-value: 1.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 205 LQMQISQLDYNNYVGVIGIGRIKRGKVKPNQQITIIDSEGKTRNGKVGKVLTHLGLERIESDVAEAGDIIAITGLGELNI 284
Cdd:cd03691 1 FQMLVTTLDYDDYLGRIAIGRIFSGTVKVGQQVTVVDEDGKIEKGRVTKLFGFEGLERVEVEEAEAGDIVAIAGLEDITI 80
|
90
....*....|....
gi 505181868 285 SDTICDPQNVEALP 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 |
8.10e-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: 139.95 E-value: 8.10e-40
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505181868 398 EPFENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDVR 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 |
1.46e-37 |
|
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: 140.32 E-value: 1.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDARTEAQER--VMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGE 84
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGRIHKIGEVHGGgaTMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDFTIE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 85 VERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDRPGARPDWVVDQV 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 |
1.57e-37 |
|
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: 139.29 E-value: 1.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 7 NIAIIAHVDHGKTTLVDKLLQQSGTFD--ARTEAQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGE 84
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIRelGSVDKGTTRTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIAE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 85 VERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDRPGARPDWVVDQV 144
Cdd:cd04168 81 VERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTIIFVNKIDRAGADLEKVYQEI 140
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
3-132 |
2.79e-32 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 132.86 E-value: 2.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 3 ENLRNIAIIAHVDHGKTTLVDKLLQQSGTFDARTEAQERVMDSNDLEKERGITIlaKNTAI------------KWNDYRI 70
Cdd:PTZ00416 17 DQIRNMSVIAHVDHGKSTLTDSLVCKAGIISSKNAGDARFTDTRADEQERGITI--KSTGIslyyehdledgdDKQPFLI 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505181868 71 NIVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDR 132
Cdd:PTZ00416 95 NLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKVDR 156
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
4-132 |
4.04e-30 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 126.38 E-value: 4.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 4 NLRNIAIIAHVDHGKTTLVDKLLQQSGTFDARTEAQERVMDSNDLEKERGITIlaKNTAIKW------------------ 65
Cdd:PLN00116 18 NIRNMSVIAHVDHGKSTLTDSLVAAAGIIAQEVAGDVRMTDTRADEAERGITI--KSTGISLyyemtdeslkdfkgerdg 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505181868 66 NDYRINIVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDR 132
Cdd:PLN00116 96 NEYLINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTETVLRQALGERIRPVLTVNKMDR 162
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
6-144 |
5.20e-30 |
|
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: 119.24 E-value: 5.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 6 RNIAIIAHVDHGKTTLVDKLL------QQSGTFDARTEAQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHA 79
Cdd:cd04169 3 RTFAIISHPDAGKTTLTEKLLlfggaiQEAGAVKARKSRKHATSDWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHE 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505181868 80 DFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDRPGARPDWVVDQV 144
Cdd:cd04169 83 DFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDREGRDPLELLDEI 147
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
7-274 |
1.50e-29 |
|
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: 121.19 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDART------EAQER---------VMDSNDLEKERGITILAKNTAIKWNDYRIN 71
Cdd:COG5256 9 NLVVIGHVDHGKSTLVGRLLYETGAIDEHIiekyeeEAEKKgkesfkfawVMDRLKEERERGVTIDLAHKKFETDKYYFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 72 IVDTPGHADFggeverVMSMV------DSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVV-INKVDRPG---ARPDWVV 141
Cdd:COG5256 89 IIDAPGHRDF------VKNMItgasqaDAAILVVSAKDGVMGQTREHAFLARTLGINQLIVaVNKMDAVNyseKRYEEVK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 142 DQVFDLFVNLDATDEqlDFPIVYASALNGiaglDHEDMAEDMTP------LYQAIvDRVPAPDVDLDGPLQMQIsQLDYN 215
Cdd:COG5256 163 EEVSKLLKMVGYKVD--KIPFIPVSAWKG----DNVVKKSDNMPwyngptLLEAL-DNLKEPEKPVDKPLRIPI-QDVYS 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505181868 216 -NYVGVIGIGRIKRGKVKPNQQITIIDSegktrnGKVGKVLT----HlglERIESdvAEAGDII 274
Cdd:COG5256 235 iSGIGTVPVGRVETGVLKVGDKVVFMPA------GVVGEVKSiemhH---EELEQ--AEPGDNI 287
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
6-132 |
1.53e-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: 116.21 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 6 RNIAIIAHVDHGKTTLVDKLLQQS---GTFDARTEAQERVMDSNDLEKERGITIlaKNTAI-------KWNDYRINIVDT 75
Cdd:cd04167 1 RNVCIAGHLHHGKTSLLDMLIEQThkrTPSVKLGWKPLRYTDTRKDEQERGISI--KSNPIslvledsKGKSYLINIIDT 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 505181868 76 PGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDR 132
Cdd:cd04167 79 PGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDR 135
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
7-274 |
7.87e-28 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 116.18 E-value: 7.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDART------EAQER---------VMDSNDLEKERGITILAKNTAIKWNDYRIN 71
Cdd:PRK12317 8 NLAVIGHVDHGKSTLVGRLLYETGAIDEHIieelreEAKEKgkesfkfawVMDRLKEERERGVTIDLAHKKFETDKYYFT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 72 IVDTPGHADFggeverVMSMV------DSVLLVVDAFD--GPMPQTR---FVTKKAFAHGLkpIVVINKVDRPG---ARP 137
Cdd:PRK12317 88 IVDCPGHRDF------VKNMItgasqaDAAVLVVAADDagGVMPQTRehvFLARTLGINQL--IVAINKMDAVNydeKRY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 138 DWVVDQVFDLFVNLDATDEqlDFPIVYASALNGiaglDHEDMAEDMTP------LYQAIvDRVPAPDVDLDGPLQMQISQ 211
Cdd:PRK12317 160 EEVKEEVSKLLKMVGYKPD--DIPFIPVSAFEG----DNVVKKSENMPwyngptLLEAL-DNLKPPEKPTDKPLRIPIQD 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505181868 212 LDYNNYVGVIGIGRIKRGKVKPNQQITIIDSegktrnGKVGKVLT----HlglERIESdvAEAGDII 274
Cdd:PRK12317 233 VYSISGVGTVPVGRVETGVLKVGDKVVFMPA------GVVGEVKSiemhH---EELPQ--AEPGDNI 288
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
7-148 |
2.37e-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: 111.53 E-value: 2.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDA--RTEAQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGE 84
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRlgRVEDGNTVSDYDPEEKKRKMSIETSVAPLEWNGHKINLIDTPGYADFVGE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505181868 85 VERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDRPGARPDWVVDQVFDLF 148
Cdd:cd04170 81 TLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRARADFDKTLAALREAF 144
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
7-272 |
1.65e-26 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 112.61 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 7 NIAIIAHVDHGKTTL---VDKLLQQSG-----TFDARTEAQErvmdsndlEKERGITILAKNTAIKWNDYRINIVDTPGH 78
Cdd:PLN03127 63 NVGTIGHVDHGKTTLtaaITKVLAEEGkakavAFDEIDKAPE--------EKARGITIATAHVEYETAKRHYAHVDCPGH 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 79 ADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVV-INKVDrpgarpdwVVD--QVFDLfVNLDATd 155
Cdd:PLN03127 135 ADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVfLNKVD--------VVDdeELLEL-VEMELR- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 156 EQLDF--------PIVYASALNGIAGLDHEDMAEDMTPLYQAIVDRVPAPDVDLDGPLQMQISQLDYNNYVGVIGIGRIK 227
Cdd:PLN03127 205 ELLSFykfpgdeiPIIRGSALSALQGTNDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVE 284
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 505181868 228 RGKVKPNQQITIIdseGKTRNGKVGKVLTHLGLERIESDVAEAGD 272
Cdd:PLN03127 285 QGTIKVGEEVEIV---GLRPGGPLKTTVTGVEMFKKILDQGQAGD 326
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
7-272 |
8.91e-25 |
|
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: 106.79 E-value: 8.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 7 NIAIIAHVDHGKTTL---VDKLLQQSGTFDARTEAQervMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGG 83
Cdd:TIGR00485 14 NVGTIGHVDHGKTTLtaaITTVLAKEGGAAARAYDQ---IDNAPEEKARGITINTAHVEYETETRHYAHVDCPGHADYVK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 84 EVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVV-INKVDRpgarpdwVVDQVFDLFVNLDATD--EQLDF 160
Cdd:TIGR00485 91 NMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKCDM-------VDDEELLELVEMEVREllSQYDF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 161 -----PIVYASALNGIAGldHEDMAEDMTPLYQAIVDRVPAPDVDLDGPLQMQISQLDYNNYVGVIGIGRIKRGKVKPNQ 235
Cdd:TIGR00485 164 pgddtPIIRGSALKALEG--DAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGE 241
|
250 260 270
....*....|....*....|....*....|....*..
gi 505181868 236 QITIIDSEgKTRNGKVgkvlTHLGLERIESDVAEAGD 272
Cdd:TIGR00485 242 EVEIVGLK-DTRKTTV----TGVEMFRKELDEGRAGD 273
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
7-276 |
4.23e-24 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 104.64 E-value: 4.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 7 NIAIIAHVDHGKTTL---VDKLLQQSGTFDARTEAQervMDSNDLEKERGITIlakNTA-IKWN-DYR-INIVDTPGHAD 80
Cdd:PRK12736 14 NIGTIGHVDHGKTTLtaaITKVLAERGLNQAKDYDS---IDAAPEEKERGITI---NTAhVEYEtEKRhYAHVDCPGHAD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 81 FggeverVMSMV------DSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVV-INKVDRPGARP--DWVVDQVFDLFVNL 151
Cdd:PRK12736 88 Y------VKNMItgaaqmDGAILVVAATDGPMPQTREHILLARQVGVPYLVVfLNKVDLVDDEEllELVEMEVRELLSEY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 152 DATDEqlDFPIVYASALngiAGLDHEDMAED-MTPLYQAIVDRVPAPDVDLDGPLQMQISQLDYNNYVGVIGIGRIKRGK 230
Cdd:PRK12736 162 DFPGD--DIPVIRGSAL---KALEGDPKWEDaIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGT 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 505181868 231 VKPNQQITI--IDSEGKTrngkvgkVLTHLGLERIESDVAEAGDIIAI 276
Cdd:PRK12736 237 VKVGDEVEIvgIKETQKT-------VVTGVEMFRKLLDEGQAGDNVGV 277
|
|
| EFG_C |
pfam00679 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
395-483 |
5.93e-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: 96.08 E-value: 5.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 395 RKQEPFENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDD 474
Cdd:pfam00679 1 VLLEPIEKVTIDVPEEYVGDVISDLNSRRGEILDMDPDDGGRVVIEAEVPLAELFGFATELRSLTKGRGSFSMEFSGYQP 80
|
....*....
gi 505181868 475 VrPGEVGQR 483
Cdd:pfam00679 81 V-PGDILDR 88
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
6-137 |
1.32e-23 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 104.83 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 6 RNIAIIAHVDHGKTTLVDKLL------QQSGTFDARTEAQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHA 79
Cdd:PRK00741 11 RTFAIISHPDAGKTTLTEKLLlfggaiQEAGTVKGRKSGRHATSDWMEMEKQRGISVTSSVMQFPYRDCLINLLDTPGHE 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505181868 80 DFGGEVERVMSMVDSVLLVVDAFDGPMPQTR--F-VTKkafAHGLkPIVV-INKVDRPGARP 137
Cdd:PRK00741 91 DFSEDTYRTLTAVDSALMVIDAAKGVEPQTRklMeVCR---LRDT-PIFTfINKLDRDGREP 148
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
7-276 |
2.74e-23 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 102.19 E-value: 2.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 7 NIAIIAHVDHGKTTL---VDKLLQQSGTFDARTEAQervMDSNDLEKERGITIlakNTAikwndyriNI----------- 72
Cdd:PRK00049 14 NVGTIGHVDHGKTTLtaaITKVLAKKGGAEAKAYDQ---IDKAPEEKARGITI---NTA--------HVeyetekrhyah 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 73 VDTPGHADFggeverVMSMV------DSVLLVVDAFDGPMPQTRfvtkkafAH-------GLKPIVV-INKVDrpgarpd 138
Cdd:PRK00049 80 VDCPGHADY------VKNMItgaaqmDGAILVVSAADGPMPQTR-------EHillarqvGVPYIVVfLNKCD------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 139 wVVD--QVFDLfVNLDATD--EQLDF-----PIVYASALNGIAGLDHEDMAEDMTPLYQAIVDRVPAPDVDLDGPLQMQI 209
Cdd:PRK00049 140 -MVDdeELLEL-VEMEVREllSKYDFpgddtPIIRGSALKALEGDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPI 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505181868 210 SQldynnyV------GVIGIGRIKRGKVKPNQQITI--IDSEGKTrngkvgkVLThlGLE--RIESDVAEAGDIIAI 276
Cdd:PRK00049 218 ED------VfsisgrGTVVTGRVERGIIKVGEEVEIvgIRDTQKT-------TVT--GVEmfRKLLDEGQAGDNVGA 279
|
|
| Elongation_Factor_C |
cd01514 |
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ... |
398-475 |
3.35e-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: 93.32 E-value: 3.35e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505181868 398 EPFENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDV 475
Cdd:cd01514 1 EPIMKVEITVPEEYLGAVIGDLSKRRGEILGMEPRGTGRVVIKAELPLAEMFGFATDLRSLTQGRASFSMEFSHYEPV 78
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
7-276 |
4.99e-23 |
|
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: 101.38 E-value: 4.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 7 NIAIIAHVDHGKTTL---VDKLLQQSGTFDARTEAQervMDSNDLEKERGITIlakNTAikWNDYRINI-----VDTPGH 78
Cdd:COG0050 14 NIGTIGHVDHGKTTLtaaITKVLAKKGGAKAKAYDQ---IDKAPEEKERGITI---NTS--HVEYETEKrhyahVDCPGH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 79 ADFggeverVMSMV------DSVLLVVDAFDGPMPQTRfvtkkafAH-------GLKPIVV-INKVDrpgarpdwVVD-- 142
Cdd:COG0050 86 ADY------VKNMItgaaqmDGAILVVSATDGPMPQTR-------EHillarqvGVPYIVVfLNKCD--------MVDde 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 143 QVFDLfVNLDATD--EQLDF-----PIVYASALNGIAGLDHEDMAEDMTPLYQAIVDRVPAPDVDLDGPLQMQISQldyn 215
Cdd:COG0050 145 ELLEL-VEMEVREllSKYGFpgddtPIIRGSALKALEGDPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVED---- 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505181868 216 nyV------GVIGIGRIKRGKVKPNQQITI--IDSEGKTrngkvgkVLThlGLE--RIESDVAEAGDIIAI 276
Cdd:COG0050 220 --VfsitgrGTVVTGRVERGIIKVGDEVEIvgIRDTQKT-------VVT--GVEmfRKLLDEGEAGDNVGL 279
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
7-276 |
2.10e-22 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 99.53 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 7 NIAIIAHVDHGKTTL---VDKLLQQSGTFDARTEAQervMDSNDLEKERGITIlakNTAikWNDYRINI-----VDTPGH 78
Cdd:PRK12735 14 NVGTIGHVDHGKTTLtaaITKVLAKKGGGEAKAYDQ---IDNAPEEKARGITI---NTS--HVEYETANrhyahVDCPGH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 79 ADFggeverVMSMV------DSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVV-INKVDrpgarpdwVVD--QVFDLfV 149
Cdd:PRK12735 86 ADY------VKNMItgaaqmDGAILVVSAADGPMPQTREHILLARQVGVPYIVVfLNKCD--------MVDdeELLEL-V 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 150 NLDATD--EQLDF-----PIVYASALNGIAGLDHEDMAEDMTPLYQAIVDRVPAPDVDLDGPLQMQISQLDYNNYVGVIG 222
Cdd:PRK12735 151 EMEVREllSKYDFpgddtPIIRGSALKALEGDDDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVV 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 505181868 223 IGRIKRGKVKPNQQITIIDSEGKTRNgkvgkVLThlGLE--RIESDVAEAGDIIAI 276
Cdd:PRK12735 231 TGRVERGIVKVGDEVEIVGIKETQKT-----TVT--GVEmfRKLLDEGQAGDNVGV 279
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
7-170 |
2.64e-22 |
|
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: 95.64 E-value: 2.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDART------EAQER---------VMDSNDLEKERGITILAKNTAIKWNDYRIN 71
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTiekyekEAKEMgkesfkyawVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 72 IVDTPGHADFggeverVMSMV------DSVLLVVDAFDG-------PMPQTRFVTKKAFAHGLKP-IVVINKVDRPG--- 134
Cdd:cd01883 81 IIDAPGHRDF------VKNMItgasqaDVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQlIVAVNKMDDVTvnw 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 505181868 135 --ARPDWVVDQVFDLFVNLDATDEQLDF-PIvyaSALNG 170
Cdd:cd01883 155 sqERYDEIKKKVSPFLKKVGYNPKDVPFiPI---SGFTG 190
|
|
| tufA |
CHL00071 |
elongation factor Tu |
7-276 |
3.99e-21 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 96.18 E-value: 3.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 7 NIAIIAHVDHGKTTL---VDKLLQQSGTFDARTEAQervMDSNDLEKERGITIlakNTAikWNDYRINI-----VDTPGH 78
Cdd:CHL00071 14 NIGTIGHVDHGKTTLtaaITMTLAAKGGAKAKKYDE---IDSAPEEKARGITI---NTA--HVEYETENrhyahVDCPGH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 79 ADFggeverVMSM------VDSVLLVVDAFDGPMPQTR---FVTKKAfahGLKPIVV-INKVDRpgarpdwVVDQVFDLF 148
Cdd:CHL00071 86 ADY------VKNMitgaaqMDGAILVVSAADGPMPQTKehiLLAKQV---GVPNIVVfLNKEDQ-------VDDEELLEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 149 VNLDATD--EQLDF-----PIVYASAL---NGIAGLDHEDMAED-----MTPLYQAIVDRVPAPDVDLDGPLQMQISQLD 213
Cdd:CHL00071 150 VELEVREllSKYDFpgddiPIVSGSALlalEALTENPKIKRGENkwvdkIYNLMDAVDSYIPTPERDTDKPFLMAIEDVF 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505181868 214 YNNYVGVIGIGRIKRGKVKPNQQITIIdSEGKTRNGKVgkvlthLGLERIES--DVAEAGDIIAI 276
Cdd:CHL00071 230 SITGRGTVATGRIERGTVKVGDTVEIV-GLRETKTTTV------TGLEMFQKtlDEGLAGDNVGI 287
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
8-175 |
4.94e-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: 90.22 E-value: 4.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 8 IAIIAHVDHGKTTLVDKLlqqSGTFDARTEAqervmdsndlekeRGIT--ILAKNTAIKWNDYRINIVDTPGHADFGGEV 85
Cdd:cd01887 3 VTVMGHVDHGKTTLLDKI---RKTNVAAGEA-------------GGITqhIGAYQVPIDVKIPGITFIDTPGHEAFTNMR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 86 ERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDRP---GARPDWVVDQVFDLfvNLDATDEQLDFPI 162
Cdd:cd01887 67 ARGASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKPygtEADPERVKNELSEL--GLVGEEWGGDVSI 144
|
170
....*....|...
gi 505181868 163 VYASALNGIaGLD 175
Cdd:cd01887 145 VPISAKTGE-GID 156
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
7-276 |
2.56e-18 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 88.13 E-value: 2.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDARTEAQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVE 86
Cdd:PLN03126 83 NIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMI 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 87 RVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVV-INKVDRpgarpdwVVDQVFDLFVNLDATD-------EQL 158
Cdd:PLN03126 163 TGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVfLNKQDQ-------VDDEELLELVELEVREllssyefPGD 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 159 DFPIVYASALNGIAGL--------DHEDMAEDMTPLYQAIVDRVPAPDVDLDGPLQMQISQLDYNNYVGVIGIGRIKRGK 230
Cdd:PLN03126 236 DIPIISGSALLALEALmenpnikrGDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGT 315
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 505181868 231 VKPNQQITIIdSEGKTRNGKVgkvlthLGLERIES--DVAEAGDIIAI 276
Cdd:PLN03126 316 VKVGETVDIV-GLRETRSTTV------TGVEMFQKilDEALAGDNVGL 356
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
10-194 |
3.06e-18 |
|
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: 88.43 E-value: 3.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 10 IIA---HVDHGKTTLVDKLlqqSGTfdarteaqervmDSNDL--EKERGITI--------LAkntaikwNDYRINIVDTP 76
Cdd:COG3276 2 IIGtagHIDHGKTTLVKAL---TGI------------DTDRLkeEKKRGITIdlgfaylpLP-------DGRRLGFVDVP 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 77 GHADF--------GGevervmsmVDSVLLVVDAFDGPMPQTRfvtkkafAH-------GLKP-IVVINKVDRpgARPDW- 139
Cdd:COG3276 60 GHEKFiknmlagaGG--------IDLVLLVVAADEGVMPQTR-------EHlaildllGIKRgIVVLTKADL--VDEEWl 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505181868 140 --VVDQVFDLfvnLDATDeqL-DFPIVYASALNGiAGLDH-----EDMAEDMT------PLYQAIvDRV 194
Cdd:COG3276 123 elVEEEIREL---LAGTF--LeDAPIVPVSAVTG-EGIDElraalDALAAAVPardadgPFRLPI-DRV 184
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
7-197 |
4.06e-18 |
|
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: 82.63 E-value: 4.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 7 NIAIIAHVDHGKTTL---VDKLLQQSGTFDARTEAQErvmDSNDLEKERGITIlakNTA------IKWNDYRiniVDTPG 77
Cdd:cd01884 4 NVGTIGHVDHGKTTLtaaITKVLAKKGGAKAKKYDEI---DKAPEEKARGITI---NTAhveyetANRHYAH---VDCPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 78 HADFggeverVMSMV------DSVLLVVDAFDGPMPQTRfvtkkafAH-------GLKPIVV-INKVDRpgarpdwVVDQ 143
Cdd:cd01884 75 HADY------IKNMItgaaqmDGAILVVSATDGPMPQTR-------EHlllarqvGVPYIVVfLNKADM-------VDDE 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505181868 144 VFDLFVNLDATD--EQLDF-----PIVYASALNGIAGLDHEDMAEDMTPLYQAIVDRVPAP 197
Cdd:cd01884 135 ELLELVEMEVREllSKYGFdgddtPIVRGSALKALEGDDPNKWVDKILELLDALDSYIPTP 195
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
7-238 |
3.43e-17 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 84.41 E-value: 3.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDART------EAQER---------VMDSNDLEKERGITILAKNTAIKWNDYRIN 71
Cdd:PTZ00141 9 NLVVIGHVDSGKSTTTGHLIYKCGGIDKRTiekfekEAAEMgkgsfkyawVLDKLKAERERGITIDIALWKFETPKYYFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 72 IVDTPGHADFGGEVERVMSMVDSVLLVVDA----FDGPMP---QTRFVTKKAFAHGLKPIVV-INKVDRPG-----ARPD 138
Cdd:PTZ00141 89 IIDAPGHRDFIKNMITGTSQADVAILVVAStageFEAGISkdgQTREHALLAFTLGVKQMIVcINKMDDKTvnysqERYD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 139 WVVDQVFDLFVNLDATDEQLDF-PIvyaSALNGiagldhEDMAE--DMTPLYQA-----IVDRVPAPDVDLDGPLQMQIS 210
Cdd:PTZ00141 169 EIKKEVSAYLKKVGYNPEKVPFiPI---SGWQG------DNMIEksDNMPWYKGptlleALDTLEPPKRPVDKPLRLPLQ 239
|
250 260
....*....|....*....|....*...
gi 505181868 211 QLDYNNYVGVIGIGRIKRGKVKPNQQIT 238
Cdd:PTZ00141 240 DVYKIGGIGTVPVGRVETGILKPGMVVT 267
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
6-138 |
3.57e-17 |
|
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: 78.95 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 6 RNIAIIAHVDHGKTTLVDKLLQQSGTFDARTEAQERvMDSNDLEKERGITilakntaikwndYRINIVDTPGHADF---- 81
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTR-NYVTTVIEEDGKT------------YKFNLLDTAGQEDYdair 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 82 ---GGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAhGLKPIVVINKVDRPGARPD 138
Cdd:TIGR00231 69 rlyYPQVERSLRVFDIVILVLDVEEILEKQTKEIIHHADS-GVPIILVGNKIDLKDADLK 127
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
8-272 |
3.91e-17 |
|
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: 84.82 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 8 IAIIAHVDHGKTTLVDKLLQqsgTFDARTEAQervmdsndlekerGITILAKNTAIKWND-YRINIVDTPGHADFGGEVE 86
Cdd:TIGR00487 90 VTIMGHVDHGKTSLLDSIRK---TKVAQGEAG-------------GITQHIGAYHVENEDgKMITFLDTPGHEAFTSMRA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 87 RVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDFpiVYAS 166
Cdd:TIGR00487 154 RGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVPIIVAINKIDKPEANPDRVKQELSEYGLVPEDWGGDTIF--VPVS 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 167 ALNGIaGLDH-EDM----AEDMtpLYQAIVDRVP---APDVDLD---GPLQMQISQlDYNNYVGVIGIGRIKRGKVKpnq 235
Cdd:TIGR00487 232 ALTGD-GIDElLDMillqSEVE--ELKANPNGQAsgvVIEAQLDkgrGPVATVLVQ-SGTLRVGDIVVVGAAYGRVR--- 304
|
250 260 270
....*....|....*....|....*....|....*...
gi 505181868 236 qiTIIDSEGKT-RNGKVGKVLTHLGLerieSDVAEAGD 272
Cdd:TIGR00487 305 --AMIDENGKSvKEAGPSKPVEILGL----SDVPAAGD 336
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
7-279 |
7.18e-17 |
|
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: 83.18 E-value: 7.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 7 NIAIIAHVDHGKTTLVDKLlqqSGTFdarteaqervMDSNDLEKERGITI-LAKNTAIKWNDY----------------- 68
Cdd:TIGR03680 6 NIGMVGHVDHGKTTLTKAL---TGVW----------TDTHSEELKRGISIrLGYADAEIYKCPecdgpecyttepvcpnc 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 69 --------RINIVDTPGHadfggevERVM-------SMVDSVLLVVDAFDG-PMPQTRFVTKKAFAHGLKPIVVI-NKVD 131
Cdd:TIGR03680 73 gsetellrRVSFVDAPGH-------ETLMatmlsgaALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVqNKID 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 132 ---RPGARPDWVVDQVFdlfvnLDATDEQlDFPIVYASALNGIagldhedmaeDMTPLYQAIVDRVPAPDVDLDGPLQMQ 208
Cdd:TIGR03680 146 lvsKEKALENYEEIKEF-----VKGTVAE-NAPIIPVSALHNA----------NIDALLEAIEKFIPTPERDLDKPPLMY 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 209 ISQ--------LDYNNYV-GVIGiGRIKRGKVKPNQQITI-----IDSEGKTRNGKVGKVLTHLGLERIESDVAEAGDII 274
Cdd:TIGR03680 210 VARsfdvnkpgTPPEKLKgGVIG-GSLIQGKLKVGDEIEIrpgikVEKGGKTKWEPIYTEITSLRAGGYKVEEARPGGLV 288
|
....*.
gi 505181868 275 AI-TGL 279
Cdd:TIGR03680 289 GVgTKL 294
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
8-191 |
9.97e-17 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 84.11 E-value: 9.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 8 IAIIAHVDHGKTTLVDKLLQqsgtfdarteaqervmdSNDLEKERG-IT--ILAKNTAIKWNDYRINIV--DTPGHADFG 82
Cdd:CHL00189 247 VTILGHVDHGKTTLLDKIRK-----------------TQIAQKEAGgITqkIGAYEVEFEYKDENQKIVflDTPGHEAFS 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 83 GEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDRPGARPDWVVDQVfdLFVNLDATDEQLDFPI 162
Cdd:CHL00189 310 SMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANTERIKQQL--AKYNLIPEKWGGDTPM 387
|
170 180 190
....*....|....*....|....*....|....*....
gi 505181868 163 VYASALNG--IAGL--------DHEDMAEDMTPLYQAIV 191
Cdd:CHL00189 388 IPISASQGtnIDKLletilllaEIEDLKADPTQLAQGII 426
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
13-176 |
5.21e-15 |
|
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: 73.02 E-value: 5.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 13 HVDHGKTTLVDKLLQQSGtfDARTEaqervmdsndlEKERGITI-LA-KNTAIKWNDyRINIVDTPGHADFggeverVMS 90
Cdd:cd04171 7 HIDHGKTTLIKALTGIET--DRLPE-----------EKKRGITIdLGfAYLDLPDGK-RLGFIDVPGHEKF------VKN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 91 MV------DSVLLVVDAFDGPMPQTRFVTKKAFAHGLKP-IVVINKVDRpgARPDWvVDQVFDLFVNLDATDEQLDFPIV 163
Cdd:cd04171 67 MLagaggiDAVLLVVAADEGIMPQTREHLEILELLGIKKgLVVLTKADL--VDEDR-LELVEEEILELLAGTFLADAPIF 143
|
170
....*....|...
gi 505181868 164 YASALNGiAGLDH 176
Cdd:cd04171 144 PVSSVTG-EGIEE 155
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
7-131 |
8.45e-15 |
|
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: 73.17 E-value: 8.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 7 NIAIIAHVDHGKTTLVDKLlqqsgTFDARTEAqervMDSNDLEKERGITI--------------LAKNTAIKWNDYRINI 72
Cdd:cd01889 2 NVGLLGHVDSGKTSLAKAL-----SEIASTAA----FDKNPQSQERGITLdlgfssfevdkpkhLEDNENPQIENYQITL 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505181868 73 VDTPGHADF------GGEVervmsmVDSVLLVVDAFDGPMPQT-------RFVTKKAfahglkpIVVINKVD 131
Cdd:cd01889 73 VDCPGHASLirtiigGAQI------IDLMLLVVDAKKGIQTQTaeclvigELLCKPL-------IVVLNKID 131
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
7-132 |
8.78e-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: 77.61 E-value: 8.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 7 NIAIIAHVDHGKTTLVDKLlqqsgtfdarTEaqervMDSNDL--EKERGITILAKNTAIKWNDYRINIVDTPGHADFGGE 84
Cdd:TIGR00475 2 IIATAGHVDHGKTTLLKAL----------TG-----IAADRLpeEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISN 66
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 505181868 85 VERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKP-IVVINKVDR 132
Cdd:TIGR00475 67 AIAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHtIVVITKADR 115
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
8-138 |
1.48e-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: 76.59 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 8 IAIIAHVDHGKTTLVDKLlqqsgtfdaRteaQERVMdsndlEKE-RGIT--ILAknTAIKWNDYRINIVDTPGHADF--- 81
Cdd:COG0532 7 VTVMGHVDHGKTSLLDAI---------R---KTNVA-----AGEaGGITqhIGA--YQVETNGGKITFLDTPGHEAFtam 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505181868 82 ---GGEVervmsmVDSVLLVVDAFDGPMPQtrfvTKKAFAHgLK----PIVV-INKVDRPGARPD 138
Cdd:COG0532 68 rarGAQV------TDIVILVVAADDGVMPQ----TIEAINH-AKaagvPIIVaINKIDKPGANPD 121
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
7-238 |
1.69e-14 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 75.90 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDART------EAQER---------VMDSNDLEKERGITILAKNTAIKWNDYRIN 71
Cdd:PLN00043 9 NIVVIGHVDSGKSTTTGHLIYKLGGIDKRVierfekEAAEMnkrsfkyawVLDKLKAERERGITIDIALWKFETTKYYCT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 72 IVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMP-------QTRFVTKKAFAHGLKPIV-VINKVDR-----PGARPD 138
Cdd:PLN00043 89 VIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMIcCCNKMDAttpkySKARYD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 139 WVVDQVFDLFVNLDATDEQLDFPivyasalnGIAGLDHEDMAEDMT-------PLYQAIVDRVPAPDVDLDGPLQMQISQ 211
Cdd:PLN00043 169 EIVKEVSSYLKKVGYNPDKIPFV--------PISGFEGDNMIERSTnldwykgPTLLEALDQINEPKRPSDKPLRLPLQD 240
|
250 260
....*....|....*....|....*..
gi 505181868 212 LDYNNYVGVIGIGRIKRGKVKPNQQIT 238
Cdd:PLN00043 241 VYKIGGIGTVPVGRVETGVIKPGMVVT 267
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
7-247 |
3.71e-14 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 74.50 E-value: 3.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 7 NIAIIAHVDHGKTTLVDKLlqqSGTFDAR-TEaqervmdsndlEKERGITI--------LAKNTAIKWNDY--------- 68
Cdd:PRK04000 11 NIGMVGHVDHGKTTLVQAL---TGVWTDRhSE-----------ELKRGITIrlgyadatIRKCPDCEEPEAyttepkcpn 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 69 ---------RINIVDTPGHadfggevERVM-------SMVDSVLLVVDAFDG-PMPQTRfvtkkafAH-------GLKPI 124
Cdd:PRK04000 77 cgsetellrRVSFVDAPGH-------ETLMatmlsgaALMDGAILVIAANEPcPQPQTK-------EHlmaldiiGIKNI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 125 VVI-NKVDrpgarpdwVVD---------QVFDlFVnlDAT-DEqlDFPIVYASALNGIagldhedmaeDMTPLYQAIVDR 193
Cdd:PRK04000 143 VIVqNKID--------LVSkeralenyeQIKE-FV--KGTvAE--NAPIIPVSALHKV----------NIDALIEAIEEE 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505181868 194 VPAPDVDLDGPLQMQISQ-LDYN-------NYV-GVIGiGRIKRGKVKPNQQITI-----IDSEGKTR 247
Cdd:PRK04000 200 IPTPERDLDKPPRMYVARsFDVNkpgtppeKLKgGVIG-GSLIQGVLKVGDEIEIrpgikVEEGGKTK 266
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
3-293 |
1.26e-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: 73.20 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 3 ENLRnIAIIAHVDHGKTTLVDKLLQQSGT-FDARTEAQERV-----MDSNDL---------EKERGITIlakNTAikwnd 67
Cdd:COG2895 16 DLLR-FITCGSVDDGKSTLIGRLLYDTKSiFEDQLAALERDskkrgTQEIDLalltdglqaEREQGITI---DVA----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 68 YR---------InIVDTPGHADFggevERVM----SMVDSVLLVVDAFDGPMPQTR---FVtkkafAH--GLKPIVV-IN 128
Cdd:COG2895 87 YRyfstpkrkfI-IADTPGHEQY----TRNMvtgaSTADLAILLIDARKGVLEQTRrhsYI-----ASllGIRHVVVaVN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 129 KVDRpgarpdwvVD---QVFDLFVNlDATD--EQLDFPIVYA---SALNGiagldhEDMAE--DMTPLYQ-----AIVDR 193
Cdd:COG2895 157 KMDL--------VDyseEVFEEIVA-DYRAfaAKLGLEDITFipiSALKG------DNVVErsENMPWYDgptllEHLET 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 194 VPAPDVDLDGPLQMQI-----SQLDYNNYVgvigiGRIKRGKVKPNQQITIIDSeGKTrnGKVGKVLTHLGleriESDVA 268
Cdd:COG2895 222 VEVAEDRNDAPFRFPVqyvnrPNLDFRGYA-----GTIASGTVRVGDEVVVLPS-GKT--STVKSIVTFDG----DLEEA 289
|
330 340
....*....|....*....|....*..
gi 505181868 269 EAGDIIAITGLGELNIS--DTICDPQN 293
Cdd:COG2895 290 FAGQSVTLTLEDEIDISrgDVIVAADA 316
|
|
| EFG_III-like |
cd16257 |
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G ... |
324-383 |
1.40e-13 |
|
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: 65.83 E-value: 1.40e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505181868 324 KFVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRRE-GFEMAVS 383
Cdd:cd16257 11 NPLDQEKLLEGLERLSEEDPALQVYREESTGEFILSGLGELHLEIIVARLEREyGVELVVS 71
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
9-171 |
3.19e-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: 67.87 E-value: 3.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 9 AIIAHVDHGKTTLVDKLLQQsgtfdarteaqERVMDSNDLEKERGITILAKNtaIKWNDYRINIVDTPGHADFGG----- 83
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGG-----------EVGEVSDVPGTTRDPDVYVKE--LDKGKVKLVLVDTPGLDEFGGlgree 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 84 EVERVMSMVDSVLLVVDAFDGPMPQ--TRFVTKKAFAHGLKPIVVINKVDRPGARPDWVVDQVFDLFvnldatdEQLDFP 161
Cdd:cd00882 68 LARLLLRGADLILLVVDSTDRESEEdaKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELA-------KILGVP 140
|
170
....*....|
gi 505181868 162 IVYASALNGI 171
Cdd:cd00882 141 VFEVSAKTGE 150
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
219-289 |
1.12e-11 |
|
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: 60.36 E-value: 1.12e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505181868 219 GVIGIGRIKRGKVKPNQQITII--DSEGKTRNGKVGKVLTHLGLERIESDVAEAGDIIAITGLGELNISDTIC 289
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILpnGTGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
205-289 |
2.32e-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: 59.97 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 205 LQMQISQLDYNNYVGVIGIGRIKRGKVKPNQQITIIdseGKTRNGKVGKVLTHlgleRIESDVAEAGDIIAITGLG--EL 282
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRIL---PKGITGRVTSIERF----HEEVDEAKAGDIVGIGILGvkDI 73
|
....*..
gi 505181868 283 NISDTIC 289
Cdd:cd01342 74 LTGDTLT 80
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
14-285 |
4.35e-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: 65.09 E-value: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 14 VDHGKTTLVDKLLQQSGT-FDARTEAQER----------------VMDSNDLEKERGITIlakNTAIKW--NDYRINIV- 73
Cdd:TIGR02034 9 VDDGKSTLIGRLLHDTKQiYEDQLAALERdskkhgtqggeidlalLVDGLQAEREQGITI---DVAYRYfsTDKRKFIVa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 74 DTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVV-INKVDrpgarpdwVVDQVFDLFVNLD 152
Cdd:TIGR02034 86 DTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLaVNKMD--------LVDYDEEVFENIK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 153 AT----DEQLDFPIVYASALNGIAGldhEDMAE--DMTPLYQA-----IVDRVPAPDVDLDGPLQMQIS-----QLDYNN 216
Cdd:TIGR02034 158 KDylafAEQLGFRDVTFIPLSALKG---DNVVSrsESMPWYSGptlleILETVEVERDAQDLPLRFPVQyvnrpNLDFRG 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505181868 217 YVGVIGIGRikrgkVKPNQQITIIDSegkTRNGKVGKVLTHLGleriESDVAEAGDIIAITGLGELNIS 285
Cdd:TIGR02034 235 YAGTIASGS-----VHVGDEVVVLPS---GRSSRVARIVTFDG----DLEQARAGQAVTLTLDDEIDIS 291
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
7-247 |
4.53e-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: 64.86 E-value: 4.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 7 NIAIIAHVDHGKTTLVDKLlqqSGTFDAR-TEaqervmdsndlEKERGITI------------------LAKNTAIKWND 67
Cdd:COG5257 7 NIGVVGHVDHGKTTLVQAL---TGVWTDRhSE-----------ELKRGITIrlgyadatfykcpnceppEAYTTEPKCPN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 68 Y--------RINIVDTPGHadfggevERVM-------SMVDSVLLVVDAFDG-PMPQTRfvtkkafAH-------GLKPI 124
Cdd:COG5257 73 CgsetellrRVSFVDAPGH-------ETLMatmlsgaALMDGAILVIAANEPcPQPQTK-------EHlmaldiiGIKNI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 125 VVI-NKVDrpgarpdwVVDQVfdlfvnlDATD--EQL----------DFPIVYASALNGIagldhedmaeDMTPLYQAIV 191
Cdd:COG5257 139 VIVqNKID--------LVSKE-------RALEnyEQIkefvkgtvaeNAPIIPVSAQHKV----------NIDALIEAIE 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 192 DRVPAPDVDLDGPLQMQISQ-LDYN-------NYVG-VIGiGRIKRGKVKPNQQITI-----IDSEGKTR 247
Cdd:COG5257 194 EEIPTPERDLSKPPRMLVARsFDVNkpgtppkDLKGgVIG-GSLIQGVLKVGDEIEIrpgikVEKGGKTK 262
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
7-170 |
6.93e-10 |
|
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: 59.12 E-value: 6.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 7 NIAIIAHVDHGKTTLVDKLLQQSGT-FDARTEAQER---------------VMDSNDLEKERGITIlakNTAikwndYR- 69
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSiFEDQLAALERskssgtqgekldlalLVDGLQAEREQGITI---DVA-----YRy 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 70 --------InIVDTPGHADFggevERVM----SMVDSVLLVVDAFDGPMPQTRfvtKKAF-AH--GLKPIVV-INKVDrp 133
Cdd:cd04166 73 fstpkrkfI-IADTPGHEQY----TRNMvtgaSTADLAILLVDARKGVLEQTR---RHSYiASllGIRHVVVaVNKMD-- 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505181868 134 garpdwVVD---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 |
1.08e-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: 55.22 E-value: 1.08e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505181868 217 YVGVIGIGRIKRGKVKPNQQITIIdSEGKTRngKVGKVLTHLGLERIESDVAEAGDIIAITGLGELNISDTICD 290
Cdd:cd04088 13 FVGKLTFFRVYSGTLKSGSTVYNS-TKGKKE--RVGRLLRMHGKKREEVEELGAGDIGAVVGLKDTRTGDTLCD 83
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
8-190 |
2.62e-09 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 56.91 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 8 IAIIAHVDHGKTTLVDKLLQqsgtfdarteaqervmDSNDLEKE---RGITILAKNTAIKWNDYRINIVDTPGHADFGGE 84
Cdd:COG1100 6 IVVVGTGGVGKTSLVNRLVG----------------DIFSLEKYlstNGVTIDKKELKLDGLDVDLVIWDTPGQDEFRET 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 85 VERVMSMVDSVLLVVDAFDGPMPQTRFVT----KKAFAHGLKP--IVVINKVDRpgaRPDWVVDQVFDLfvnLDATDEQL 158
Cdd:COG1100 70 RQFYARQLTGASLYLFVVDGTREETLQSLyellESLRRLGKKSpiILVLNKIDL---YDEEEIEDEERL---KEALSEDN 143
|
170 180 190
....*....|....*....|....*....|..
gi 505181868 159 DFPIVYASALNGiagldhedmaEDMTPLYQAI 190
Cdd:COG1100 144 IVEVVATSAKTG----------EGVEELFAAL 165
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
8-170 |
2.36e-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: 53.98 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 8 IAIIAHVDHGKTTLVDKLLQQsgtfdarteaqERVMDSNdlekERGITILAKNTAIKWNDYRINIVDTPG-----HADFG 82
Cdd:cd01895 5 IAIIGRPNVGKSSLLNALLGE-----------ERVIVSD----IAGTTRDSIDVPFEYDGQKYTLIDTAGirkkgKVTEG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 83 GE------VERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINK---VDRPGARPDWVVDQVFDLFVnlda 153
Cdd:cd01895 70 IEkysvlrTLKAIERADVVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKwdlVEKDEKTMKEFEKELRRKLP---- 145
|
170
....*....|....*...
gi 505181868 154 tdeQLDF-PIVYASALNG 170
Cdd:cd01895 146 ---FLDYaPIVFISALTG 160
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
14-294 |
4.47e-08 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 56.09 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 14 VDHGKTTLVDKLLQQSGT-FDARTEAQER----------------VMDSNDLEKERGITIlakNTAIKW--NDYRINIV- 73
Cdd:PRK05506 33 VDDGKSTLIGRLLYDSKMiFEDQLAALERdskkvgtqgdeidlalLVDGLAAEREQGITI---DVAYRYfaTPKRKFIVa 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 74 DTPGHADFggevERVM----SMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVV-INKVDrpgarpdwVVD---QVF 145
Cdd:PRK05506 110 DTPGHEQY----TRNMvtgaSTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLaVNKMD--------LVDydqEVF 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 146 DLFV-NLDATDEQLDFPIVYA---SALNGiaglDHEDMAEDMTPLYQ-----AIVDRVP-APDVDLDG---PLQMQI-SQ 211
Cdd:PRK05506 178 DEIVaDYRAFAAKLGLHDVTFipiSALKG----DNVVTRSARMPWYEgpsllEHLETVEiASDRNLKDfrfPVQYVNrPN 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 212 LDYNNYVGVIGIGRIKRGkvkpnQQITIIDSeGKTrnGKVGKVLTHLGleriESDVAEAGDIIAITGLGELNIS--DTIC 289
Cdd:PRK05506 254 LDFRGFAGTVASGVVRPG-----DEVVVLPS-GKT--SRVKRIVTPDG----DLDEAFAGQAVTLTLADEIDISrgDMLA 321
|
....*
gi 505181868 290 DPQNV 294
Cdd:PRK05506 322 RADNR 326
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
7-129 |
5.07e-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: 51.47 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 7 NIAIIAHVDHGKTTLVDKLLQQsgtfDARTEAQErvmdsndlekerGITILAKNTAIKWNDYRINIVDTPG-----HADF 81
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGA----KAIVSDYP------------GTTRDPNEGRLELKGKQIILVDTPGliegaSEGE 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 505181868 82 G-GEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINK 129
Cdd:pfam01926 65 GlGRAFLAIIEADLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
8-176 |
7.54e-08 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 55.44 E-value: 7.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 8 IAIIAHVDHGKTTlvdkLLQQSGTFDArteaqervmDSNDLEKERGITILAKNTAIKWNDYR-INIVDTPGHADF----- 81
Cdd:PRK10512 3 IATAGHVDHGKTT----LLQAITGVNA---------DRLPEEKKRGMTIDLGYAYWPQPDGRvLGFIDVPGHEKFlsnml 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 82 ---GGevervmsmVDSVLLVVDAFDGPMPQTR---FVTKKAFAHGLKpiVVINKVDR-PGARPDWVVDQVFDLFVNLDAT 154
Cdd:PRK10512 70 agvGG--------IDHALLVVACDDGVMAQTRehlAILQLTGNPMLT--VALTKADRvDEARIAEVRRQVKAVLREYGFA 139
|
170 180
....*....|....*....|...
gi 505181868 155 DEQLdFPIVYASALnGIAGL-DH 176
Cdd:PRK10512 140 EAKL-FVTAATEGR-GIDALrEH 160
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
2-137 |
5.25e-07 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 52.49 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 2 IENLRN--IAIIAHVDHGKTTLVDKLlqqSGTFDARTEAQervmdsndlekerGIT--ILAknTAIKWN----------- 66
Cdd:PRK04004 1 EKKLRQpiVVVLGHVDHGKTTLLDKI---RGTAVAAKEAG-------------GITqhIGA--TEVPIDviekiagplkk 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 67 DYRINI-------VDTPGHADF------GGevervmSMVDSVLLVVDAFDGPMPQT--------RFvtKKAFahglkpIV 125
Cdd:PRK04004 63 PLPIKLkipgllfIDTPGHEAFtnlrkrGG------ALADIAILVVDINEGFQPQTieainilkRR--KTPF------VV 128
|
170
....*....|...
gi 505181868 126 VINKVDR-PGARP 137
Cdd:PRK04004 129 AANKIDRiPGWKS 141
|
|
| EngA1 |
cd01894 |
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
63-131 |
5.48e-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: 5.48e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505181868 63 IKWNDYRINIVDTPGHADFGGE--------VERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVD 131
Cdd:cd01894 40 AEWGGREFILIDTGGIEPDDEGiskeireqAEIAIEEADVILFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKID 116
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
67-195 |
5.77e-07 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 51.53 E-value: 5.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 67 DYRINIVDTPG-----HAdFG----GEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDRpgARP 137
Cdd:COG1159 50 DAQIVFVDTPGihkpkRK-LGrrmnKAAWSALEDVDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDL--VKK 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 505181868 138 DwvvdqvfDLFVNLDATDEQLDF-PIVYASALNGIaGLDHedmaedmtpLYQAIVDRVP 195
Cdd:COG1159 127 E-------ELLPLLAEYSELLDFaEIVPISALKGD-NVDE---------LLDEIAKLLP 168
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
7-131 |
6.69e-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: 49.96 E-value: 6.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 7 NIAIIAHVDHGKTTLVDKLlqqSGTFdarteaqervMDSNDLEKERGITIlaK----NTAI-------KWNDY------- 68
Cdd:cd01888 2 NIGTIGHVAHGKTTLVKAL---SGVW----------TVRHKEELKRNITI--KlgyaNAKIykcpncgCPRPYdtpecec 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 69 -----------RINIVDTPGHadfggevERVM-------SMVDSVLLVVDAFDG-PMPQTRfvtkkafAH-------GLK 122
Cdd:cd01888 67 pgcggetklvrHVSFVDCPGH-------EILMatmlsgaAVMDGALLLIAANEPcPQPQTS-------EHlaaleimGLK 132
|
170
....*....|
gi 505181868 123 PIVVI-NKVD 131
Cdd:cd01888 133 HIIILqNKID 142
|
|
| EFG_mtEFG_C |
cd03713 |
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational ... |
398-476 |
1.07e-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: 1.07e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505181868 398 EPFENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGkGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDVR 476
Cdd:cd03713 1 EPIMKVEVTVPEEYMGDVIGDLSSRRGQILGTESRG-GWKVIKAEVPLAEMFGYSTDLRSLTQGRGSFTMEFSHYEEVP 78
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
4-136 |
2.20e-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: 50.58 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 4 NLRN--IAIIAHVDHGKTTLVDKLlqqSGTFDARTEAQErvMDSNDLEKERGITILAKNTAIKWNDYRINI-------VD 74
Cdd:TIGR00491 1 RLRQpiVVVLGHVDHGKTTLLDKI---RGTAVVKKEAGG--ITQHIGASEVPTDVIEKICGDLLKSFKIKLkipgllfID 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505181868 75 TPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDR-PGAR 136
Cdd:TIGR00491 76 TPGHEAFTNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTPFVVAANKIDRiPGWK 138
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
67-175 |
2.28e-06 |
|
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: 47.84 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 67 DYRINIVDTPG-HADFGG-------EVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDRpgarpd 138
Cdd:cd04163 50 DAQIIFVDTPGiHKPKKKlgermvkAAWSALKDVDLVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDL------ 123
|
90 100 110
....*....|....*....|....*....|....*...
gi 505181868 139 wvVDQVFDLFVNLDATDEQLDF-PIVYASALNGIaGLD 175
Cdd:cd04163 124 --VKDKEDLLPLLEKLKELHPFaEIFPISALKGE-NVD 158
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
66-175 |
3.45e-06 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 49.28 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 66 NDYRINIVDTPG-HADfGGEVERVM------SM--VDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDRPGAR 136
Cdd:PRK00089 51 DDAQIIFVDTPGiHKP-KRALNRAMnkaawsSLkdVDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLVKDK 129
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 505181868 137 pdwvvDQVFDLfvnLDATDEQLDF-PIVYASALNGIaGLD 175
Cdd:PRK00089 130 -----EELLPL---LEELSELMDFaEIVPISALKGD-NVD 160
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
8-176 |
2.11e-05 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 47.35 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 8 IAIIAHVDHGKTTLVDKLLQQsgtfdarteaqERVMDSNdlekERGITILAKNTAIKWNDYRINIVDTPG-------HAD 80
Cdd:PRK00093 176 IAIIGRPNVGKSSLINALLGE-----------ERVIVSD----IAGTTRDSIDTPFERDGQKYTLIDTAGirrkgkvTEG 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 81 fggeVE--------RVMSMVDSVLLVVDAFDGPmpqTRFVTKKA-FAH--GLKPIVVINKVDrpgarpdwVVDQ-VFDLF 148
Cdd:PRK00093 241 ----VEkysvirtlKAIERADVVLLVIDATEGI---TEQDLRIAgLALeaGRALVIVVNKWD--------LVDEkTMEEF 305
|
170 180 190
....*....|....*....|....*....|
gi 505181868 149 VN-LDATDEQLDF-PIVYASALNGIaGLDH 176
Cdd:PRK00093 306 KKeLRRRLPFLDYaPIVFISALTGQ-GVDK 334
|
|
| lepA_C |
cd03709 |
lepA_C: This family represents the C-terminal region of LepA, a GTP-binding protein localized ... |
398-474 |
2.74e-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: 2.74e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505181868 398 EPFENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLI-GFRSEFMTMTSGtgllYSTFShYDD 474
Cdd:cd03709 1 EPFVKATIITPSEYLGAIMELCQERRGVQKDMEYLDANRVMLTYELPLAEIVyDFFDKLKSISKG----YASLD-YEL 73
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
7-178 |
2.97e-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: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 7 NIAIIAHVDHGKTTLVDKLLqqsgtfdarteaQERVMDSndlekerGITIL-AKNTAIKWN-DYRINIVDTPG------- 77
Cdd:cd09912 2 LLAVVGEFSAGKSTLLNALL------------GEEVLPT-------GVTPTtAVITVLRYGlLKGVVLVDTPGlnstieh 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 78 HADfggEVERVMSMVDSVLLVVDAfDGPMPQT--RFVTKKAFAHGLKPIVVINKVDRpgARPDWVVDQVFDLFVNLDATD 155
Cdd:cd09912 63 HTE---ITESFLPRADAVIFVLSA-DQPLTESerEFLKEILKWSGKKIFFVLNKIDL--LSEEELEEVLEYSREELGVLE 136
|
170 180
....*....|....*....|....
gi 505181868 156 EQLDFPIVYA-SALNGIAGLDHED 178
Cdd:cd09912 137 LGGGEPRIFPvSAKEALEARLQGD 160
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
63-138 |
4.68e-05 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 46.17 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 63 IKWNDYRINIVDTPG-----HADFGGE----VERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGlKP-IVVINKVDR 132
Cdd:COG1160 45 AEWGGREFTLIDTGGiepddDDGLEAEireqAELAIEEADVILFVVDGRAGLTPLDEEIAKLLRRSG-KPvILVVNKVDG 123
|
....*.
gi 505181868 133 PGARPD 138
Cdd:COG1160 124 PKREAD 129
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
17-191 |
4.80e-05 |
|
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: 44.16 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 17 GKTTLVDKLLQQsgtfdarteaqervmDSNDLEKERGITILAKNTAIKWNDYR-INIVDTPGHADFGG-------EVERV 88
Cdd:cd00880 9 GKSSLLNALLGQ---------------NVGIVSPIPGTTRDPVRKEWELLPLGpVVLIDTPGLDEEGGlgrerveEARQV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 89 MSMVDSVLLVVDAfDGPMPQTRFVTKKAFAHGLKPIVVINKVDRPGARPDwvvDQVFDLFVNLdatdEQLDFPIVYASAL 168
Cdd:cd00880 74 ADRADLVLLVVDS-DLTPVEEEAKLGLLRERGKPVLLVLNKIDLVPESEE---EELLRERKLE----LLPDLPVIAVSAL 145
|
170 180
....*....|....*....|...
gi 505181868 169 NGiagldhedmaEDMTPLYQAIV 191
Cdd:cd00880 146 PG----------EGIDELRKKIA 158
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
92-175 |
7.15e-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: 44.31 E-value: 7.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 92 VDSVLLVVdAFDGPMPQTRFVTK---KAFAHGLKPIVVINKVDRPgarPDWVVDQVFDLFvnldatdEQLDFPIVYASAL 168
Cdd:cd01854 3 VDQVLIVF-SLKEPFFNLRLLDRylvAAEASGIEPVIVLNKADLV---DDEELEELLEIY-------EKLGYPVLAVSAK 71
|
....*..
gi 505181868 169 NGIaGLD 175
Cdd:cd01854 72 TGE-GLD 77
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
63-210 |
7.71e-05 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 45.43 E-value: 7.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 63 IKWNDYRINIVDTPG----HADFGGEV----ERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDRPG 134
Cdd:PRK00093 44 AEWLGREFILIDTGGiepdDDGFEKQIreqaELAIEEADVILFVVDGRAGLTPADEEIAKILRKSNKPVILVVNKVDGPD 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505181868 135 ARpdwvvDQVFDlFVNLDATDEqldFPIvyaSALNGIaGLDHedmaedmtpLYQAIVDRVPAPDVDLDGPLQMQIS 210
Cdd:PRK00093 124 EE-----ADAYE-FYSLGLGEP---YPI---SAEHGR-GIGD---------LLDAILEELPEEEEEDEEDEPIKIA 177
|
|
| MJ1464 |
cd01859 |
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ... |
85-167 |
3.39e-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: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 85 VERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDrpgARPDWVVDQVFDLFvnldatdEQLDFPIVY 164
Cdd:cd01859 5 VRRIIKEADVVLEVVDARDPELTRSRKLERMALELGKKLIIVLNKAD---LVPREVLEKWKEVF-------ESEGLPVVY 74
|
...
gi 505181868 165 ASA 167
Cdd:cd01859 75 VSA 77
|
|
| PRK09518 |
PRK09518 |
bifunctional cytidylate kinase/GTPase Der; Reviewed |
8-133 |
4.74e-04 |
|
bifunctional cytidylate kinase/GTPase Der; Reviewed
Pssm-ID: 236546 [Multi-domain] Cd Length: 712 Bit Score: 43.24 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 8 IAIIAHVDHGKTTLVDKLLqqsgtfdARTEAQerVMDSNDLEKERgITILAKntaikWNDYRINIVDTPG--------HA 79
Cdd:PRK09518 278 VAIVGRPNVGKSTLVNRIL-------GRREAV--VEDTPGVTRDR-VSYDAE-----WAGTDFKLVDTGGweadvegiDS 342
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 505181868 80 DFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDRP 133
Cdd:PRK09518 343 AIASQAQIAVSLADAVVFVVDGQVGLTSTDERIVRMLRRAGKPVVLAVNKIDDQ 396
|
|
| mtEFG1_C |
cd04097 |
mtEFG1_C: C-terminus of mitochondrial Elongation factor G1 (mtEFG1)-like proteins found in ... |
398-472 |
6.55e-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: 38.84 E-value: 6.55e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505181868 398 EPFENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGkGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHY 472
Cdd:cd04097 1 EPIMKVEVTAPTEFQGNVIGLLNKRKGTIVDTDTGE-DEFTLEAEVPLNDMFGYSTELRSMTQGKGEFSMEFSRY 74
|
|
| EFG_C |
smart00838 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
398-475 |
1.28e-03 |
|
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: 37.87 E-value: 1.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505181868 398 EPFENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGkGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDV 475
Cdd:smart00838 3 EPIMKVEVTVPEEYMGDVIGDLNSRRGKIEGMEQRG-GAQVIKAKVPLSEMFGYATDLRSATQGRATWSMEFSHYEEV 79
|
|
| EFG_III |
cd16262 |
Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial ... |
330-386 |
1.35e-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: 37.82 E-value: 1.35e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 505181868 330 QILDRLNKElvhNVALRVEETEDADAFRVSGRGELHLSVLIENMRRE-GFEMAVSRPK 386
Cdd:cd16262 22 KALARLAEE---DPTLRVSRDEETGQTILSGMGELHLEIIVERLKREyGVEVEVGKPQ 76
|
|
| MnmE |
COG0486 |
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
63-205 |
2.35e-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: 40.81 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 63 IKWNDYRINIVDTPGHADFGGEVER--------VMSMVDSVLLVVDAFDGPMPQTRFVTKKAFahGLKPIVVINKVDRPG 134
Cdd:COG0486 256 INIGGIPVRLIDTAGLRETEDEVEKigierareAIEEADLVLLLLDASEPLTEEDEEILEKLK--DKPVIVVLNKIDLPS 333
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505181868 135 ARPDWVvdqvfdlfvnldatDEQLDFPIVYASALNGiAGLDHedmaedmtpLYQAIVDRVPAPDVDLDGPL 205
Cdd:COG0486 334 EADGEL--------------KSLPGEPVIAISAKTG-EGIDE---------LKEAILELVGEGALEGEGVL 380
|
|
| EF4_II |
cd03699 |
Domain II of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly ... |
214-290 |
2.81e-03 |
|
Domain II of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly conserved guanosine triphosphatase found in bacteria and eukaryotic mitochondria and chloroplasts. EF4 functions as a translation factor, which promotes back-translocation of tRNAs on posttranslocational ribosome complexes and competes with elongation factor G for interaction with pretranslocational ribosomes, inhibiting the elongation phase of protein synthesis.
Pssm-ID: 293900 [Multi-domain] Cd Length: 86 Bit Score: 37.01 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 214 YNNYVGVIGIGRIKRGKVKPNQQITIIDSEGKTRNGKVGkVLThlgLERIESDVAEAGD---IIA-ITGLGELNISDTIC 289
Cdd:cd03699 10 YDPYRGVVVLVRVFDGTLKKGDKIRFMATGKEYEVLEVG-VFT---PKMVPTDELSAGEvgyIIAgIKSVKDARVGDTIT 85
|
.
gi 505181868 290 D 290
Cdd:cd03699 86 L 86
|
|
| PRK03003 |
PRK03003 |
GTP-binding protein Der; Reviewed |
8-138 |
3.17e-03 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 179525 [Multi-domain] Cd Length: 472 Bit Score: 40.34 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 8 IAIIAHVDHGKTTLVDKLLqqsgtfdARTEAQerVMDSNDLEKERgITILAKntaikWNDYRINIVDTPG--------HA 79
Cdd:PRK03003 41 VAVVGRPNVGKSTLVNRIL-------GRREAV--VEDVPGVTRDR-VSYDAE-----WNGRRFTVVDTGGwepdakglQA 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 505181868 80 DFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDRPGARPD 138
Cdd:PRK03003 106 SVAEQAEVAMRTADAVLFVVDATVGATATDEAVARVLRRSGKPVILAANKVDDERGEAD 164
|
|
| Tet_II |
cd03690 |
Domain II of ribosomal protection proteins Tet(M) and Tet(O); This subfamily represents domain ... |
225-288 |
4.34e-03 |
|
Domain II of ribosomal protection proteins Tet(M) and Tet(O); This subfamily represents domain II of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology to domain II 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: 293891 [Multi-domain] Cd Length: 86 Bit Score: 36.45 E-value: 4.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505181868 225 RIKRGKVKPNQQITIIDSEGKtrnGKVGKVLTHLGLERIESDVAEAGDIIAITGLGELNISDTI 288
Cdd:cd03690 24 RLYSGTLRLRDSVRVSGEEEK---IKITELRTFENGELVKVDRVYAGDIAILVGLKSLRVGDVL 84
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
3-170 |
5.93e-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: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 3 ENLRNIAIIAHVDHGKTTLVDKLLQQsgtfdarteaqERVMDSNdlekERGITILAKNTAIKWNDYRINIVDTPG----- 77
Cdd:COG1160 173 DDPIKIAIVGRPNVGKSSLINALLGE-----------ERVIVSD----IAGTTRDSIDTPFERDGKKYTLIDTAGirrkg 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 78 --HADfggeVERvMSMVDS---------VLLVVDAFDGpmpqtrfVT---KK--AFAH----GLkpIVVINK---VDRPG 134
Cdd:COG1160 238 kvDEG----IEK-YSVLRTlraieradvVLLVIDATEG-------ITeqdLKiaGLALeagkAL--VIVVNKwdlVEKDR 303
|
170 180 190
....*....|....*....|....*....|....*.
gi 505181868 135 ARPDWVVDQVFDLFVNLDatdeqlDFPIVYASALNG 170
Cdd:COG1160 304 KTREELEKEIRRRLPFLD------YAPIVFISALTG 333
|
|
| EF2_II |
cd16268 |
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 ... |
219-291 |
8.05e-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: 36.04 E-value: 8.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505181868 219 GVIGIGRIKRGKVKPNQQITIIDSE---GKTRNGKVGKVlTHLGL----ERIESDVAEAGDIIAITGL-GELNISDTICD 290
Cdd:cd16268 17 GFVAFGRVFSGTVRRGQEVYILGPKyvpGKKDDLKKKRI-QQTYLmmgrEREPVDEVPAGNIVGLVGLdDFLAKSGTTTS 95
|
.
gi 505181868 291 P 291
Cdd:cd16268 96 S 96
|
|
| |
