|
Name |
Accession |
Description |
Interval |
E-value |
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
1-609 |
0e+00 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 1179.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 1 MTRQIRNIAIIAHVDHGKTTLVDQLLRQSGTFRDNEKIAERVMDSNDIERERGITILAKNCAVTWQGTHINIVDTPGHAD 80
Cdd:COG1217 2 MREDIRNIAIIAHVDHGKTTLVDALLKQSGTFRENQEVAERVMDSNDLERERGITILAKNTAVRYKGVKINIVDTPGHAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 81 FGGEVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVDKPGSRPDYVINAAFDLFDKLGATEDQLDF 160
Cdd:COG1217 82 FGGEVERVLSMVDGVLLLVDAFEGPMPQTRFVLKKALELGLKPIVVINKIDRPDARPDEVVDEVFDLFIELGATDEQLDF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 161 PVVYASGLNGWAALEEGAPGEawgtNMAPLFETVLKHVPPHEGDPAAPLQLQISSLDYSTFVGRIGVGRVNSGTLKPAMD 240
Cdd:COG1217 162 PVVYASARNGWASLDLDDPGE----DLTPLFDTILEHVPAPEVDPDGPLQMLVTNLDYSDYVGRIAIGRIFRGTIKKGQQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 241 VLVMeGPDGRAYKGRINQVLTFEGLNRVMADEAGPGDIVLVNGIEDLGIGVTITDPANPQPLPMLRVDEPTLTMNFCVNT 320
Cdd:COG1217 238 VALI-KRDGKVEKGKITKLFGFEGLERVEVEEAEAGDIVAIAGIEDINIGDTICDPENPEALPPIKIDEPTLSMTFSVND 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 321 SPLAGREGKYVTSRQIWDRLQKELQSNVALRVRESGEDGIFEVSGRGELHLTILLENMRREGYELAVSKPRVVFHDDGGE 400
Cdd:COG1217 317 SPFAGREGKFVTSRQIRERLEKELETNVALRVEETDSPDAFKVSGRGELHLSILIETMRREGYELQVSRPEVIFKEIDGK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 401 RQEPIELVTVDVEDQHQGGVMQALGERKGELANMEVDGRGRVRLEYRIPARGLIGFSNEFMNLTRGTGLISNIFDGYEAY 480
Cdd:COG1217 397 KLEPIEELTIDVPEEYSGAVIEKLGQRKGEMTNMEPDGGGRVRLEFLIPSRGLIGFRTEFLTDTRGTGIMNHVFDGYEPY 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 481 KGEIAGRKNGVLISMDDGEIITYALGKLDDRGRMFVKPGDPTYEGMIVGIHSRDNDLVVNATRTKQLTNFRVSGKEDAIK 560
Cdd:COG1217 477 KGEIPGRRNGSLISMETGKATAYALFNLQERGTLFIGPGTEVYEGMIVGEHSRDNDLVVNVCKEKKLTNMRASGSDEAIR 556
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1819251932 561 ITPPIDLTLEYAVEFIEDDELVEITPKSIRIRKRHLKEHDRKRASREGA 609
Cdd:COG1217 557 LTPPRKMSLEQALEFIEDDELVEVTPKSIRLRKKILDENERKRAAKKKK 605
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
5-603 |
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: 1000.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 5 IRNIAIIAHVDHGKTTLVDQLLRQSGTFRDNEKIAERVMDSNDIERERGITILAKNCAVTWQGTHINIVDTPGHADFGGE 84
Cdd:TIGR01394 1 IRNIAIIAHVDHGKTTLVDALLKQSGTFRANEAVAERVMDSNDLERERGITILAKNTAIRYNGTKINIVDTPGHADFGGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 85 VERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVDKPGSRPDYVINAAFDLFDKLGATEDQLDFPVVY 164
Cdd:TIGR01394 81 VERVLGMVDGVLLLVDASEGPMPQTRFVLKKALELGLKPIVVINKIDRPSARPDEVVDEVFDLFAELGADDEQLDFPIVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 165 ASGLNGWAALEEGAPGEawgtNMAPLFETVLKHVPPHEGDPAAPLQLQISSLDYSTFVGRIGVGRVNSGTLKPAMDVLVM 244
Cdd:TIGR01394 161 ASGRAGWASLDLDDPSD----NMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVHRGTVKKGQQVALM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 245 eGPDGRAYKGRINQVLTFEGLNRVMADEAGPGDIVLVNGIEDLGIGVTITDPANPQPLPMLRVDEPTLTMNFCVNTSPLA 324
Cdd:TIGR01394 237 -KRDGTIENGRISKLLGFEGLERVEIDEAGAGDIVAVAGLEDINIGETIADPEVPEALPTITVDEPTLSMTFSVNDSPLA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 325 GREGKYVTSRQIWDRLQKELQSNVALRVRESGEDGIFEVSGRGELHLTILLENMRREGYELAVSKPRVVFHDDGGERQEP 404
Cdd:TIGR01394 316 GKEGKKVTSRHIRDRLMRELETNVALRVEDTESADKFEVSGRGELHLSILIETMRREGFELQVGRPQVIYKEIDGKKLEP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 405 IELVTVDVEDQHQGGVMQALGERKGELANMEVDGRGRVRLEYRIPARGLIGFSNEFMNLTRGTGLISNIFDGYEAYKGEI 484
Cdd:TIGR01394 396 IEELTIDVPEEHVGAVIEKLGKRKGEMVDMEPSGNGRTRLEFKIPSRGLIGFRTEFLTDTRGTGIMNHVFDEYEPWKGEI 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 485 AGRKNGVLISMDDGEIITYALGKLDDRGRMFVKPGDPTYEGMIVGIHSRDNDLVVNATRTKQLTNFRVSGKEDAIKITPP 564
Cdd:TIGR01394 476 ETRRNGSLVSMEDGTATAYALWNLQERGVMFVSPGTEVYEGMIIGEHSRENDLDVNPCKAKKLTNVRSSGKDEAVKLTPP 555
|
570 580 590
....*....|....*....|....*....|....*....
gi 1819251932 565 IDLTLEYAVEFIEDDELVEITPKSIRIRKRHLKEHDRKR 603
Cdd:TIGR01394 556 RKLSLEQALEYIEDDELVEVTPKSIRLRKRVLDPNERKR 594
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
1-606 |
0e+00 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 738.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 1 MTRQIRNIAIIAHVDHGKTTLVDQLLRQSGTFRDNEKIAERVMDSNDIERERGITILAKNCAVTWQGTHINIVDTPGHAD 80
Cdd:PRK10218 1 MIEKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 81 FGGEVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVDKPGSRPDYVINAAFDLFDKLGATEDQLDF 160
Cdd:PRK10218 81 FGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 161 PVVYASGLNGWAALEEgapgEAWGTNMAPLFETVLKHVPPHEGDPAAPLQLQISSLDYSTFVGRIGVGRVNSGTLKPAMD 240
Cdd:PRK10218 161 PIVYASALNGIAGLDH----EDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 241 VLVMEGpDGRAYKGRINQVLTFEGLNRVMADEAGPGDIVLVNGIEDLGIGVTITDPANPQPLPMLRVDEPTLTMNFCVNT 320
Cdd:PRK10218 237 VTIIDS-EGKTRNAKVGKVLGHLGLERIETDLAEAGDIVAITGLGELNISDTVCDTQNVEALPALSVDEPTVSMFFCVNT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 321 SPLAGREGKYVTSRQIWDRLQKELQSNVALRVRESGEDGIFEVSGRGELHLTILLENMRREGYELAVSKPRVVFHDDGGE 400
Cdd:PRK10218 316 SPFCGKEGKFVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRREGFELAVSRPKVIFREIDGR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 401 RQEPIELVTVDVEDQHQGGVMQALGERKGELANMEVDGRGRVRLEYRIPARGLIGFSNEFMNLTRGTGLISNIFDGYEAY 480
Cdd:PRK10218 396 KQEPYENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 481 K-GEIAGRKNGVLISMDDGEIITYALGKLDDRGRMFVKPGDPTYEGMIVGIHSRDNDLVVNATRTKQLTNFRVSGKEDAI 559
Cdd:PRK10218 476 RpGEVGQRQNGVLISNGQGKAVAFALFGLQDRGKLFLGHGAEVYEGQIIGIHSRSNDLTVNCLTGKKLTNMRASGTDEAV 555
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1819251932 560 KITPPIDLTLEYAVEFIEDDELVEITPKSIRIRKRHLKEHDRKRASR 606
Cdd:PRK10218 556 VLVPPIRMTLEQALEFIDDDELVEVTPTSIRIRKRHLTENDRRRANR 602
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
5-200 |
3.53e-130 |
|
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: 379.63 E-value: 3.53e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 5 IRNIAIIAHVDHGKTTLVDQLLRQSGTFRDNEKIAERVMDSNDIERERGITILAKNCAVTWQGTHINIVDTPGHADFGGE 84
Cdd:cd01891 2 IRNIAIIAHVDHGKTTLVDALLKQSGTFRENEEVGERVMDSNDLERERGITILAKNTAITYKDTKINIIDTPGHADFGGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 85 VERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVDKPGSRPDYVINAAFDLFDKLGATEDQLDFPVVY 164
Cdd:cd01891 82 VERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDRPDARPEEVVDEVFDLFLELNATDEQLDFPIVY 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 1819251932 165 ASGLNGWAALEEGAPGEawgtNMAPLFETVLKHVPP 200
Cdd:cd01891 162 ASAKNGWASLNLDDPSE----DLDPLFETIIEHVPA 193
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
4-200 |
2.47e-70 |
|
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: 225.10 E-value: 2.47e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 4 QIRNIAIIAHVDHGKTTLVDQLLRQSGTFRDNEKIA---ERVMDSNDIERERGITILAKNCAVTWQGTHINIVDTPGHAD 80
Cdd:pfam00009 2 RHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKgegEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 81 FGGEVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVDKP-GSRPDYVINAAFDLFDKLgATEDQLD 159
Cdd:pfam00009 82 FVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVdGAELEEVVEEVSRELLEK-YGEDGEF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1819251932 160 FPVVYASGLNGWaaleegapgeawgtNMAPLFETVLKHVPP 200
Cdd:pfam00009 161 VPVVPGSALKGE--------------GVQTLLDALDEYLPS 187
|
|
| lepA |
TIGR01393 |
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a ... |
3-496 |
6.13e-61 |
|
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: 212.95 E-value: 6.13e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 3 RQIRNIAIIAHVDHGKTTLVDQLLRQSGTFRDNEKiAERVMDSNDIERERGITILAKNCAVTWQGTH-----INIVDTPG 77
Cdd:TIGR01393 1 KNIRNFSIIAHIDHGKSTLADRLLEYTGAISEREM-REQVLDSMDLERERGITIKAQAVRLNYKAKDgetyvLNLIDTPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 78 HADFGGEVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVDKPGSRPDYVinaAFDLFDKLGATEDQ 157
Cdd:TIGR01393 80 HVDFSYEVSRSLAACEGALLLVDAAQGIEAQTLANVYLALENDLEIIPVINKIDLPSADPERV---KKEIEEVIGLDASE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 158 ldfpVVYASGLNgwaaleegapgeawGTNMAPLFETVLKHVPPHEGDPAAPLQLQISSLDYSTFVGRIGVGRVNSGTLKP 237
Cdd:TIGR01393 157 ----AILASAKT--------------GIGIEEILEAIVKRVPPPKGDPDAPLKALIFDSHYDNYRGVVALVRVFEGTIKP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 238 AMDVLVMEgpDGRAYkgRINQVLTFEgLNRVMADEAGPGDI-VLVNGIEDLG---IGVTITDPANP--QPLPMLRVDEPt 311
Cdd:TIGR01393 219 GDKIRFMS--TGKEY--EVDEVGVFT-PKLTKTDELSAGEVgYIIAGIKDVSdvrVGDTITHVKNPakEPLPGFKEVKP- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 312 ltMNFC----VNTSplagregKYVTSRQIWDRLQ-------KELQSNVALrvresgedGI-FEVSGRGELHLTILLENMR 379
Cdd:TIGR01393 293 --MVFAglypIDTE-------DYEDLRDALEKLKlndasltYEPESSPAL--------GFgFRCGFLGLLHMEIIQERLE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 380 REgYELAV--SKPRV---VFHDDGGER-----------------QEPIELVTVDVEDQHQGGVMQALGERKGELANMEVD 437
Cdd:TIGR01393 356 RE-FNLDLitTAPSViyrVYLTNGEVIevdnpsdlpdpgkiehvEEPYVKATIITPTEYLGPIMTLCQEKRGVQTNMEYL 434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 438 GRGRVRLEYRIP-ARGLIGFSNEFMNLTRgtglisnifdGYEAYKGEIAGRKNGVLISMD 496
Cdd:TIGR01393 435 DPNRVELIYEMPlAEIVYDFFDKLKSISR----------GYASFDYELIGYRPSDLVKLD 484
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
4-406 |
7.84e-60 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 212.42 E-value: 7.84e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 4 QIRNIAIIAHVDHGKTTLVDQLLRQSGTFrdNEKIA--ERVMDSNDIERERGITILAKNCAVT--WQGTH--INIVDTPG 77
Cdd:PRK07560 19 QIRNIGIIAHIDHGKTTLSDNLLAGAGMI--SEELAgeQLALDFDEEEQARGITIKAANVSMVheYEGKEylINLIDTPG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 78 HADFGGEVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVD------KPGS-----RPDYVINAAFD 146
Cdd:PRK07560 97 HVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKPVLFINKVDrlikelKLTPqemqqRLLKIIKDVNK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 147 LFDKLGATED----QLDF---PVVYASGLNGWA------------------ALEEGAPGEAwgTNMAPLFETVL----KH 197
Cdd:PRK07560 177 LIKGMAPEEFkekwKVDVedgTVAFGSALYNWAisvpmmqktgikfkdiidYYEKGKQKEL--AEKAPLHEVVLdmvvKH 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 198 VP----------PH---------------EGDPAAPLQLQISSLDYSTFVGRIGVGRVNSGTLKPAMDVLVMegpdGRAY 252
Cdd:PRK07560 255 LPnpieaqkyriPKiwkgdlnsevgkamlNCDPNGPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLV----GAKK 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 253 KGRINQVLTFEGLNRVMADEAGPGDIVLVNGIEDLGIGVTITDPANPQPLPMLR-VDEPTLTMNF-CVNTSPLAgregKY 330
Cdd:PRK07560 331 KNRVQQVGIYMGPEREEVEEIPAGNIAAVTGLKDARAGETVVSVEDMTPFESLKhISEPVVTVAIeAKNPKDLP----KL 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1819251932 331 V-TSRQiwdrLQKElqsNVALRVRESGEDGIFEVSGRGELHLTILLENMRRE-GYELAVSKPRVVFHDDGGERQEPIE 406
Cdd:PRK07560 407 IeVLRQ----LAKE---DPTLVVKINEETGEHLLSGMGELHLEVITYRIKRDyGIEVVTSEPIVVYRETVRGKSQVVE 477
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
5-500 |
1.06e-58 |
|
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: 208.98 E-value: 1.06e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 5 IRNIAIIAHVDHGKTTLVDQLLRQSGTFRDNEKIAERVMDSNDIERERGITILAKNCAV--TWQGTH--INIVDTPGHAD 80
Cdd:TIGR00490 19 IRNIGIVAHIDHGKTTLSDNLLAGAGMISEELAGQQLYLDFDEQEQERGITINAANVSMvhEYEGNEylINLIDTPGHVD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 81 FGGEVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVDK-----------PGSRPDYVINAAFDLFD 149
Cdd:TIGR00490 99 FGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKPVLFINKVDRlinelkltpqeLQERFIKIITEVNKLIK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 150 KLGATE-------DQLDFPVVYASGLNGWAA------------------LEEGAPGEAwgTNMAPLFETVL----KHVP- 199
Cdd:TIGR00490 179 AMAPEEfrdkwkvRVEDGSVAFGSAYYNWAIsvpsmkktgigfkdiykyCKEDKQKEL--AKKSPLHQVVLdmviRHLPs 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 200 PHEG------------------------DPAAPLQLQISSLDYSTFVGRIGVGRVNSGTLKPAMDVLVMegpdGRAYKGR 255
Cdd:TIGR00490 257 PIEAqkyripviwkgdlnsevgkamlncDPKGPLALMITKIVVDKHAGEVAVGRLYSGTIRPGMEVYIV----DRKAKAR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 256 INQVLTFEGLNRVMADEAGPGDIVLVNGIEDLGIGVTITDPA-NPQPLPMLR-VDEPTLTMNF-CVNTSPLAgregkyvt 332
Cdd:TIGR00490 333 IQQVGVYMGPERVEVDEIPAGNIVAVIGLKDAVAGETICTTVeNITPFESIKhISEPVVTVAIeAKNTKDLP-------- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 333 srQIWDRLQKELQSNVALRVRESGEDGIFEVSGRGELHLTILLENMRRE-GYELAVSKPRVVFHDDGGERQEPIE----- 406
Cdd:TIGR00490 405 --KLIEVLRQVAKEDPTVHVEINEETGEHLISGMGELHLEIIVEKIREDyGLDVETSPPIVVYRETVTGTSPVVEgkspn 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 407 ------LVTVDVEDQhqggVMQALGErkGELANMEVDGRGRVRLEYRI-----PARGLIGF--SNEFMNLTRGTGLISN- 472
Cdd:TIGR00490 483 khnrfyIVVEPLEES----VIQAFKE--GKIVDMKMKKKERRRLLIEAgmdseEAARVEEYyeGNLFINMTRGIQYLDEt 556
|
570 580 590
....*....|....*....|....*....|....
gi 1819251932 473 ---IFDGYEAY--KGEIAGRK-NGVLISMDDGEI 500
Cdd:TIGR00490 557 kelILEGFREAmrNGPIAREKcMGVKVKLMDAKL 590
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
5-449 |
5.34e-57 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 202.17 E-value: 5.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 5 IRNIAIIAHVDHGKTTLVDQLLRQSGTFRDNEKiAERVMDSNDIERERGITILAKNCAVTWQGT-----HINIVDTPGHA 79
Cdd:COG0481 6 IRNFSIIAHIDHGKSTLADRLLELTGTLSEREM-KEQVLDSMDLERERGITIKAQAVRLNYKAKdgetyQLNLIDTPGHV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 80 DFGGEVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVDKPGSRPDYVINaafDLFDKLG--ATEdq 157
Cdd:COG0481 85 DFSYEVSRSLAACEGALLVVDASQGVEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKQ---EIEDIIGidASD-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 158 ldfpVVYASGLNgwaaleegapgeawGTNMAPLFETVLKHVPPHEGDPAAPLQ-LQISSLdYSTFVGRIGVGRVNSGTLK 236
Cdd:COG0481 160 ----AILVSAKT--------------GIGIEEILEAIVERIPPPKGDPDAPLQaLIFDSW-YDSYRGVVVYVRVFDGTLK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 237 PAMDVLVMEgpDGRAYKgrINQVLTFeGLNRVMADEAGPGDI-VLVNGIEDLG---IGVTITDPANP--QPLPMLRVDEP 310
Cdd:COG0481 221 KGDKIKMMS--TGKEYE--VDEVGVF-TPKMTPVDELSAGEVgYIIAGIKDVRdarVGDTITLAKNPaaEPLPGFKEVKP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 311 tltMNFC----VNTSplagregKYVTSRqiwDRLQKeLQSNVALRVRESgedgifEVSG------R----GELHLTILLE 376
Cdd:COG0481 296 ---MVFAglypVDSD-------DYEDLR---DALEK-LQLNDASLTYEP------ETSAalgfgfRcgflGLLHMEIIQE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 377 NMRREgYELAV--SKPRVVFH---DDGGER-----------------QEPIELVTVDVEDQHQGGVMQALGERKGELANM 434
Cdd:COG0481 356 RLERE-FDLDLitTAPSVVYEvtlTDGEVIevdnpsdlpdpgkieeiEEPIVKATIITPSEYVGAVMELCQEKRGVQKNM 434
|
490
....*....|....*
gi 1819251932 435 EVDGRGRVRLEYRIP 449
Cdd:COG0481 435 EYLGENRVELTYELP 449
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
4-394 |
2.10e-53 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 193.63 E-value: 2.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 4 QIRNIAIIAHVDHGKTTLVDQLLRQSGTFRdneKIAE-----RVMDSNDIERERGITILAKNCAVTWQGTHINIVDTPGH 78
Cdd:PRK13351 7 QIRNIGILAHIDAGKTTLTERILFYTGKIH---KMGEvedgtTVTDWMPQEQERGITIESAATSCDWDNHRINLIDTPGH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 79 ADFGGEVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVDKPGS---------------RP------ 137
Cdd:PRK13351 84 IDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGAdlfkvledieerfgkRPlplqlp 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 138 -----------------------------------------------DYVINAAFDLFDKLgaTEDQLDFPVVYASGLNg 170
Cdd:PRK13351 164 igsedgfegvvdlitepelhfsegdggstveegpipeelleeveearEKLIEALAEFDDEL--LELYLEGEELSAEQLR- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 171 wAALEEGA------P---GEAW-GTNMAPLFETVLKHVP-PHEG-----------------DPAAPLQLQISSLDYSTFV 222
Cdd:PRK13351 241 -APLREGTrsghlvPvlfGSALkNIGIEPLLDAVVDYLPsPLEVppprgskdngkpvkvdpDPEKPLLALVFKVQYDPYA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 223 GRIGVGRVNSGTLKPAMDVLVMEGpdGRAYK-GRINQVltfEGLNRVMADEAGPGDIVLVNGIEDLGIGVTITDPANPQP 301
Cdd:PRK13351 320 GKLTYLRVYSGTLRAGSQLYNGTG--GKREKvGRLFRL---QGNKREEVDRAKAGDIVAVAGLKELETGDTLHDSADPVL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 302 LPMLRVDEPTLTMnfCVntsplagrEGKYVTSRQ-IWDRLQKELQSNVALRVRESGEDGIFEVSGRGELHLTILLENMRR 380
Cdd:PRK13351 395 LELLTFPEPVVSL--AV--------EPERRGDEQkLAEALEKLVWEDPSLRVEEDEETGQTILSGMGELHLEVALERLRR 464
|
490
....*....|....*
gi 1819251932 381 E-GYELAVSKPRVVF 394
Cdd:PRK13351 465 EfKLEVNTGKPQVAY 479
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
7-175 |
3.45e-52 |
|
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: 177.10 E-value: 3.45e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 7 NIAIIAHVDHGKTTLVDQLLRQSGTFRDNEKIAERVMDSNDIERERGITILAKNCAVTWQGTHINIVDTPGHADFGGEVE 86
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 87 RALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVDKPG-SRPDYVINAAFDLFDKLGATED-QLDFPVVY 164
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGeEDFDEVLREIKELLKLIGFTFLkGKDVPIIP 160
|
170
....*....|.
gi 1819251932 165 ASGLNGWAALE 175
Cdd:cd00881 161 ISALTGEGIEE 171
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
2-392 |
2.07e-50 |
|
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: 185.63 E-value: 2.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 2 TRQIRNIAIIAHVDHGKTTLVDQLLRQSGTfrdNEKIAE-----RVMDSNDIERERGITIlakNCAVT---WQGTHINIV 73
Cdd:COG0480 6 LEKIRNIGIVAHIDAGKTTLTERILFYTGA---IHRIGEvhdgnTVMDWMPEEQERGITI---TSAATtceWKGHKINII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 74 DTPGHADFGGEVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVDKPGSRPDYVINA---------- 143
Cdd:COG0480 80 DTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQlkerlganpv 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 144 ----------------------AFDLFDKLGATEDQLDFPVVYASGLNGW-------AA----------LEEGAPGEAW- 183
Cdd:COG0480 160 plqlpigaeddfkgvidlvtmkAYVYDDELGAKYEEEEIPAELKEEAEEAreelieaVAetddelmekyLEGEELTEEEi 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 184 ------GT---------------NM--APLFETVLK------HVPPHEG-------------DPAAPLQLQISSLDYSTF 221
Cdd:COG0480 240 kaglrkATlagkivpvlcgsafkNKgvQPLLDAVVDylpsplDVPAIKGvdpdtgeeverkpDDDEPFSALVFKTMTDPF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 222 VGRIGVGRVNSGTLKPAMDVLVMegpdGRAYKGRINQVLTFEGLNRVMADEAGPGDIVLVNGIEDLGIGVTITDPANPQP 301
Cdd:COG0480 320 VGKLSFFRVYSGTLKSGSTVYNS----TKGKKERIGRLLRMHGNKREEVDEAGAGDIVAVVKLKDTTTGDTLCDEDHPIV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 302 LPMLRVDEPTLTMnfcvntsplA------GREGKYVTSrqiwdrLQKELQSNVALRVRESGEDGIFEVSGRGELHLTILL 375
Cdd:COG0480 396 LEPIEFPEPVISV---------AiepktkADEDKLSTA------LAKLAEEDPTFRVETDEETGQTIISGMGELHLEIIV 460
|
490
....*....|....*...
gi 1819251932 376 ENMRRE-GYELAVSKPRV 392
Cdd:COG0480 461 DRLKREfGVEVNVGKPQV 478
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
11-478 |
1.70e-47 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 176.85 E-value: 1.70e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 11 IAHVDHGKTTLVDQLLRQSGTFRDNEKIAE--RVMDSNDIERERGITILAKNCAVTWQGTHINIVDTPGHADFGGEVERA 88
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRIGEVEDgtTTMDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVERA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 89 LSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVDKPGSRPDYVINAafdLFDKLGAT-------------- 154
Cdd:PRK12740 81 LRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRAGADFFRVLAQ---LQEKLGAPvvplqlpigegddf 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 155 --------------------------EDQLD------------------------------------------------F 160
Cdd:PRK12740 158 tgvvdllsmkayrydeggpseeieipAELLDraeeareellealaefddelmekylegeelseeeikaglrkatlageiV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 161 PVVYASGLNG------WAALEEGAPGEawgTNMAPLFETVLKHVPPHEGDPAAPLQLQISSLDYSTFVGRIGVGRVNSGT 234
Cdd:PRK12740 238 PVFCGSALKNkgvqrlLDAVVDYLPSP---LEVPPVDGEDGEEGAELAPDPDGPLVALVFKTMDDPFVGKLSLVRVYSGT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 235 LKPAMDVLVMegpdGRAYKGRINQVLTFEGLNRVMADEAGPGDIVLVNGIEDLGIGVTITDPANPQPLPMLRVDEPTLtm 314
Cdd:PRK12740 315 LKKGDTLYNS----GTGKKERVGRLYRMHGKQREEVDEAVAGDIVAVAKLKDAATGDTLCDKGDPILLEPMEFPEPVI-- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 315 nfcvntsPLA------GREGKyvtsrqIWDRLQKELQSNVALRVRESGEDGIFEVSGRGELHLTILLENMRRE-GYELAV 387
Cdd:PRK12740 389 -------SLAiepkdkGDEEK------LSEALGKLAEEDPTLRVERDEETGQTILSGMGELHLDVALERLKREyGVEVET 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 388 SKPRV------------------------------------------VFHD--DGGE--RQ------------------- 402
Cdd:PRK12740 456 GPPQVpyretirkkaeghgrhkkqsgghgqfgdvwleveplprgegfEFVDkvVGGAvpRQyipavekgvrealekgvla 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 403 ----------------------------------------------EPIELVTVDVEDQHQGGVMQALGERKGELANMEV 436
Cdd:PRK12740 536 gypvvdvkvtltdgsyhsvdssemafkiaarlafrealpkakpvllEPIMKVEVSVPEEFVGDVIGDLSSRRGRILGMES 615
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1819251932 437 DGRG-RVRLEyrIPARGLIGFSNEFMNLTRGTGLISNIFDGYE 478
Cdd:PRK12740 616 RGGGdVVRAE--VPLAEMFGYATDLRSLTQGRGSFSMEFSHYE 656
|
|
| BipA_III |
cd16263 |
Domain III of GTP-binding protein BipA (TypA); BipA (also called TypA) is a highly conserved ... |
310-388 |
1.05e-44 |
|
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: 153.24 E-value: 1.05e-44
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1819251932 310 PTLTMNFCVNTSPLAGREGKYVTSRQIWDRLQKELQSNVALRVRESGEDGIFEVSGRGELHLTILLENMRREGYELAVS 388
Cdd:cd16263 1 PTVSMTFGVNTSPFAGREGKFVTSRKIRDRLEKELETNVALRVEETESPDSFIVSGRGELHLSILIETMRREGFELQVS 79
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
6-200 |
8.49e-43 |
|
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: 153.16 E-value: 8.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 6 RNIAIIAHVDHGKTTLVDQLLRQSGTFRdnEKIA--ERVMDSNDIERERGITILAKNCAVTWQGTH---------INIVD 74
Cdd:cd01885 1 RNICIIAHVDHGKTTLSDSLLASAGIIS--EKLAgkARYLDTREDEQERGITIKSSAISLYFEYEEekmdgndylINLID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 75 TPGHADFGGEVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVD------KPGSRPDYV-------- 140
Cdd:cd01885 79 SPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDrlilelKLSPEEAYQrllrived 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1819251932 141 INAAFDLF--DKLGATEDQLDFP---VVYASGLNGWA-ALEEGApgeawgtNMAPLFETVLKHVPP 200
Cdd:cd01885 159 VNAIIETYapEEFKQEKWKFSPQkgnVAFGSALDGWGfTIIKFA-------DIYAVLEMVVKHLPS 217
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
6-200 |
1.63e-42 |
|
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: 150.76 E-value: 1.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 6 RNIAIIAHVDHGKTTLVDQLLRQSGTFRDNEKiAERVMDSNDIERERGITILAKNCAVTWQGTH-----INIVDTPGHAD 80
Cdd:cd01890 1 RNFSIIAHIDHGKSTLADRLLELTGTVSEREM-KEQVLDSMDLERERGITIKAQAVRLFYKAKDgeeylLNLIDTPGHVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 81 FGGEVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVDKPGSRPDYVinaAFDLFDKLGATEDQldf 160
Cdd:cd01890 80 FSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRV---KQEIEDVLGLDASE--- 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1819251932 161 pVVYASGLNgwaaleegapgeawGTNMAPLFETVLKHVPP 200
Cdd:cd01890 154 -AILVSAKT--------------GLGVEDLLEAIVERIPP 178
|
|
| BipA_TypA_C |
cd03710 |
BipA_TypA_C: a C-terminal portion of BipA or TypA having homology to the C terminal domains of ... |
403-481 |
1.18e-37 |
|
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: 134.17 E-value: 1.18e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1819251932 403 EPIELVTVDVEDQHQGGVMQALGERKGELANMEVDGRGRVRLEYRIPARGLIGFSNEFMNLTRGTGLISNIFDGYEAYK 481
Cdd:cd03710 1 EPIEELTIDVPEEYSGAVIEKLGKRKGEMVDMEPDGNGRTRLEFKIPSRGLIGFRSEFLTDTRGTGIMNHVFDGYEPYK 79
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
7-153 |
1.49e-36 |
|
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: 137.62 E-value: 1.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 7 NIAIIAHVDHGKTTLVDQLLRQSGTfrdNEKIAE-----RVMDSNDIERERGITILAKNCAVTWQGTHINIVDTPGHADF 81
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGR---IHKIGEvhgggATMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDF 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1819251932 82 GGEVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVDKPGSRPDYVINaafDLFDKLGA 153
Cdd:cd01886 78 TIEVERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVE---QIREKLGA 146
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
7-142 |
3.41e-36 |
|
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: 135.44 E-value: 3.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 7 NIAIIAHVDHGKTTLVDQLLRQSGTfrdnekIAE--RV------MDSNDIERERGITILAKNCAVTWQGTHINIVDTPGH 78
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGA------IRElgSVdkgttrTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGH 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1819251932 79 ADFGGEVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVDKPGSRPDYVIN 142
Cdd:cd04168 75 MDFIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTIIFVNKIDRAGADLEKVYQ 138
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
209-303 |
2.44e-35 |
|
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: 128.07 E-value: 2.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 209 LQLQISSLDYSTFVGRIGVGRVNSGTLKPAMDVLVMeGPDGRAYKGRINQVLTFEGLNRVMADEAGPGDIVLVNGIEDLG 288
Cdd:cd03691 1 FQMLVTTLDYDDYLGRIAIGRIFSGTVKVGQQVTVV-DEDGKIEKGRVTKLFGFEGLERVEVEEAEAGDIVAIAGLEDIT 79
|
90
....*....|....*
gi 1819251932 289 IGVTITDPANPQPLP 303
Cdd:cd03691 80 IGDTICDPEVPEPLP 94
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
4-132 |
6.77e-31 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 128.63 E-value: 6.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 4 QIRNIAIIAHVDHGKTTLVDQLLRQSGTFRDNEKIAERVMDSNDIERERGITI----------LAKNCAVTWQGTHINIV 73
Cdd:PTZ00416 18 QIRNMSVIAHVDHGKSTLTDSLVCKAGIISSKNAGDARFTDTRADEQERGITIkstgislyyeHDLEDGDDKQPFLINLI 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1819251932 74 DTPGHADFGGEVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVDK 132
Cdd:PTZ00416 98 DSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKVDR 156
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
6-132 |
4.15e-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: 115.06 E-value: 4.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 6 RNIAIIAHVDHGKTTLVDQLL----RQSGTFRDNEKIaERVMDSNDIERERGITILAKNCAVTWQGTH-----INIVDTP 76
Cdd:cd04167 1 RNVCIAGHLHHGKTSLLDMLIeqthKRTPSVKLGWKP-LRYTDTRKDEQERGISIKSNPISLVLEDSKgksylINIIDTP 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1819251932 77 GHADFGGEVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVDK 132
Cdd:cd04167 80 GHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDR 135
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
7-299 |
7.58e-27 |
|
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: 113.49 E-value: 7.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 7 NIAIIAHVDHGKTTLVDQLLRQSG-----TFRDNEKIAER----------VMDSNDIERERGITILAKNCAVTWQGTHIN 71
Cdd:COG5256 9 NLVVIGHVDHGKSTLVGRLLYETGaidehIIEKYEEEAEKkgkesfkfawVMDRLKEERERGVTIDLAHKKFETDKYYFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 72 IVDTPGHADFGGEVERALSMVDGVVLLIDAQEGPMPQTR---FVTKkalALGLKPIVV-VNKVDKPG---SRPDYVINAA 144
Cdd:COG5256 89 IIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTRehaFLAR---TLGINQLIVaVNKMDAVNyseKRYEEVKEEV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 145 FDLFDKLGATEDqlDFPVVYASGLNGwAALEEGAPGEAWgTNMAPLFETV--LKhVPPHEGDpaAPLQLQISSLdYS-TF 221
Cdd:COG5256 166 SKLLKMVGYKVD--KIPFIPVSAWKG-DNVVKKSDNMPW-YNGPTLLEALdnLK-EPEKPVD--KPLRIPIQDV-YSiSG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 222 VGRIGVGRVNSGTLKPAMDVLVMegPdgrayKGRINQVLTFEgLNRVMADEAGPGDIVLVN--GIE--DLGIGVTITDPA 297
Cdd:COG5256 238 IGTVPVGRVETGVLKVGDKVVFM--P-----AGVVGEVKSIE-MHHEELEQAEPGDNIGFNvrGVEknDIKRGDVAGHPD 309
|
..
gi 1819251932 298 NP 299
Cdd:COG5256 310 NP 311
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
7-143 |
3.48e-26 |
|
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: 108.06 E-value: 3.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 7 NIAIIAHVDHGKTTLVDQLLRQSGTFRDNEKIAE--RVMDSNDIERERGITILAKNCAVTWQGTHINIVDTPGHADFGGE 84
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRLGRVEDgnTVSDYDPEEKKRKMSIETSVAPLEWNGHKINLIDTPGYADFVGE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1819251932 85 VERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVDKPGSRPDYVINA 143
Cdd:cd04170 81 TLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRARADFDKTLAA 139
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
5-132 |
1.90e-25 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 111.74 E-value: 1.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 5 IRNIAIIAHVDHGKTTLVDQLLRQSGTFRDNEKIAERVMDSNDIERERGITILAKNCAVTWQGTH--------------- 69
Cdd:PLN00116 19 IRNMSVIAHVDHGKSTLTDSLVAAAGIIAQEVAGDVRMTDTRADEAERGITIKSTGISLYYEMTDeslkdfkgerdgney 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1819251932 70 -INIVDTPGHADFGGEVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVDK 132
Cdd:PLN00116 99 lINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTETVLRQALGERIRPVLTVNKMDR 162
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
7-285 |
4.31e-25 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 108.09 E-value: 4.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 7 NIAIIAHVDHGKTTLVDQLLRQSG-----TFRDNEKIAER----------VMDSNDIERERGITILAKNCAVTWQGTHIN 71
Cdd:PRK12317 8 NLAVIGHVDHGKSTLVGRLLYETGaidehIIEELREEAKEkgkesfkfawVMDRLKEERERGVTIDLAHKKFETDKYYFT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 72 IVDTPGHADFGGEVERALSMVDGVVLLIDAQE--GPMPQTR---FVTKkalALGLKP-IVVVNKVDKPG---SRPDYVIN 142
Cdd:PRK12317 88 IVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTRehvFLAR---TLGINQlIVAINKMDAVNydeKRYEEVKE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 143 AAFDLFDKLGATEDQLDF-PVVYASGLNgwaaLEEGAPGEAWGTnmAPLFETVLKHVPPHEGDPAAPLQLQISSLdYS-T 220
Cdd:PRK12317 165 EVSKLLKMVGYKPDDIPFiPVSAFEGDN----VVKKSENMPWYN--GPTLLEALDNLKPPEKPTDKPLRIPIQDV-YSiS 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1819251932 221 FVGRIGVGRVNSGTLKPAMDVLVMEGpdgraykGRINQVLTFEgLNRVMADEAGPGDIVLVN--GIE 285
Cdd:PRK12317 238 GVGTVPVGRVETGVLKVGDKVVFMPA-------GVVGEVKSIE-MHHEELPQAEPGDNIGFNvrGVG 296
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
6-151 |
6.01e-25 |
|
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: 104.60 E-value: 6.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 6 RNIAIIAHVDHGKTTLVDQLL------RQSGTFRDNeKIAERVM-DSNDIERERGITILAKNCAVTWQGTHINIVDTPGH 78
Cdd:cd04169 3 RTFAIISHPDAGKTTLTEKLLlfggaiQEAGAVKAR-KSRKHATsDWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGH 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1819251932 79 ADFGGEVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVDKPGSRPdyvinaaFDLFDKL 151
Cdd:cd04169 82 EDFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDREGRDP-------LELLDEI 147
|
|
| EFG_C |
pfam00679 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
403-487 |
1.42e-22 |
|
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: 91.84 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 403 EPIELVTVDVEDQHQGGVMQALGERKGELANMEVDGRGRVRLEYRIPARGLIGFSNEFMNLTRGTGLISNIFDGYEAYKG 482
Cdd:pfam00679 4 EPIEKVTIDVPEEYVGDVISDLNSRRGEILDMDPDDGGRVVIEAEVPLAELFGFATELRSLTKGRGSFSMEFSGYQPVPG 83
|
....*
gi 1819251932 483 EIAGR 487
Cdd:pfam00679 84 DILDR 88
|
|
| Elongation_Factor_C |
cd01514 |
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ... |
403-481 |
2.17e-22 |
|
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: 91.00 E-value: 2.17e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1819251932 403 EPIELVTVDVEDQHQGGVMQALGERKGELANMEVDGRGRVRLEYRIPARGLIGFSNEFMNLTRGTGLISNIFDGYEAYK 481
Cdd:cd01514 1 EPIMKVEITVPEEYLGAVIGDLSKRRGEILGMEPRGTGRVVIKAELPLAEMFGFATDLRSLTQGRASFSMEFSHYEPVP 79
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
7-170 |
1.69e-20 |
|
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: 90.24 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 7 NIAIIAHVDHGKTTLVDQLLRQSG-----TFRDNEKIAER----------VMDSNDIERERGITIlakNCAVTWQGT--- 68
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGgvdkrTIEKYEKEAKEmgkesfkyawVLDKLKEERERGVTI---DVGLAKFETeky 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 69 HINIVDTPGHADF-----GGEveralSMVDGVVLLIDAQEG-------PMPQTR---FVTKkalALGLKP-IVVVNKVDK 132
Cdd:cd01883 78 RFTIIDAPGHRDFvknmiTGA-----SQADVAVLVVSARKGefeagfeKGGQTRehaLLAR---TLGVKQlIVAVNKMDD 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1819251932 133 PG-----SRPDYVINAAFDLFDKLGATEDQLDF-PVvyaSGLNG 170
Cdd:cd01883 150 VTvnwsqERYDEIKKKVSPFLKKVGYNPKDVPFiPI---SGFTG 190
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
7-301 |
1.29e-19 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 91.99 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 7 NIAIIAHVDHGKTTLVDQLLRQSGTFRDNEKIAERVMDSNDIERERGITILAKNCAVTWQGTHINIVDTPGHADFGGEVE 86
Cdd:PLN03126 83 NIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMI 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 87 RALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVV-VNKVDKPGSRpDYVINAAFDLFDKLGATE-DQLDFPVVY 164
Cdd:PLN03126 163 TGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVfLNKQDQVDDE-ELLELVELEVRELLSSYEfPGDDIPIIS 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 165 ASGLNGWAALEEGAP---GE-AWGTNMAPLFETVLKHVPPHEGDPAAPLQLQISSLDYSTFVGRIGVGRVNSGTLKPAMD 240
Cdd:PLN03126 242 GSALLALEALMENPNikrGDnKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGET 321
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1819251932 241 VLVMEGPDGRAYkgrinQVLTFEGLNRVMaDEAGPGDIV--LVNGIE--DLGIGVTITDPANPQP 301
Cdd:PLN03126 322 VDIVGLRETRST-----TVTGVEMFQKIL-DEALAGDNVglLLRGIQkaDIQRGMVLAKPGSITP 380
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
7-236 |
2.83e-19 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 90.39 E-value: 2.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 7 NIAIIAHVDHGKTTL---VDQLL--RQSGTFRDNEKIaervmDSNDIERERGITILAKNCAVTWQGTHINIVDTPGHADF 81
Cdd:PRK12736 14 NIGTIGHVDHGKTTLtaaITKVLaeRGLNQAKDYDSI-----DAAPEEKERGITINTAHVEYETEKRHYAHVDCPGHADY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 82 GGEVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVV-VNKVDKPGSRP--DYVINAAFDLFDKLGATEDql 158
Cdd:PRK12736 89 VKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVfLNKVDLVDDEEllELVEMEVRELLSEYDFPGD-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 159 DFPVVYASGLngwAALEEGAPgeaWGTNMAPLFETVLKHVPPHEGDPAAPLQLQISslDYSTFVGRIGV--GRVNSGTLK 236
Cdd:PRK12736 167 DIPVIRGSAL---KALEGDPK---WEDAIMELMDAVDEYIPTPERDTDKPFLMPVE--DVFTITGRGTVvtGRVERGTVK 238
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
5-153 |
4.11e-19 |
|
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: 84.73 E-value: 4.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 5 IRNIAIIAHVDHGKTTLVDQLLR--------QSGTFRDNEKiaervmdsnDIERERGITILakncavtwqgthINIVDTP 76
Cdd:TIGR00231 1 DIKIVIVGHPNVGKSTLLNSLLGnkgsiteyYPGTTRNYVT---------TVIEEDGKTYK------------FNLLDTA 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 77 GHADF-------GGEVERALSMVDGVVLLIDAQEGPMPQTRFVtKKALALGLKPIVVVNKVDKPGSRPDYVINaafDLFD 149
Cdd:TIGR00231 60 GQEDYdairrlyYPQVERSLRVFDIVILVLDVEEILEKQTKEI-IHHADSGVPIILVGNKIDLKDADLKTHVA---SEFA 135
|
....
gi 1819251932 150 KLGA 153
Cdd:TIGR00231 136 KLNG 139
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
7-301 |
1.38e-18 |
|
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: 88.30 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 7 NIAIIAHVDHGKTTLVDQLLR-----QSGTFRDNEKIaervmDSNDIERERGITILAKNCAVTWQGTHINIVDTPGHADF 81
Cdd:TIGR00485 14 NVGTIGHVDHGKTTLTAAITTvlakeGGAAARAYDQI-----DNAPEEKARGITINTAHVEYETETRHYAHVDCPGHADY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 82 GGEVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVV-VNKVDKPGSRP--DYVINAAFDLFDKLGATEDql 158
Cdd:TIGR00485 89 VKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKCDMVDDEEllELVEMEVRELLSQYDFPGD-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 159 DFPVVYASGLNgwaALEEGApgeAWGTNMAPLFETVLKHVPPHEGDPAAPLQLQISSLDYSTFVGRIGVGRVNSGTLKPA 238
Cdd:TIGR00485 167 DTPIIRGSALK---ALEGDA---EWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVG 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1819251932 239 MDVLVMEGPDGRayKGRINQVLTFeglnRVMADEAGPGDIV--LVNGI--EDLGIGVTITDPANPQP 301
Cdd:TIGR00485 241 EEVEIVGLKDTR--KTTVTGVEMF----RKELDEGRAGDNVglLLRGIkrEEIERGMVLAKPGSIKP 301
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
7-298 |
1.75e-18 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 88.27 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 7 NIAIIAHVDHGKTTLVDQLLRQSG-----TFRDNEKIAER----------VMDSNDIERERGITIlakNCAvTWQ----G 67
Cdd:PTZ00141 9 NLVVIGHVDSGKSTTTGHLIYKCGgidkrTIEKFEKEAAEmgkgsfkyawVLDKLKAERERGITI---DIA-LWKfetpK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 68 THINIVDTPGHADFGGEVERALSMVDGVVLLIDAQEGPMP-------QTRFVTKKALALGLKPIVV-VNKVDKPG----- 134
Cdd:PTZ00141 85 YYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVcINKMDDKTvnysq 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 135 SRPDYVINAAFDLFDKLGATEDQLDFpvVYASGLNGWAALEEGapgeawgTNMA-----PLFETVLKHVPPHEgdPA-AP 208
Cdd:PTZ00141 165 ERYDEIKKEVSAYLKKVGYNPEKVPF--IPISGWQGDNMIEKS-------DNMPwykgpTLLEALDTLEPPKR--PVdKP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 209 LQLQISSLDYSTFVGRIGVGRVNSGTLKPAMDVLVmegpdgrAYKGRINQVLTFEGLNRVMAdEAGPGDIVLVN----GI 284
Cdd:PTZ00141 234 LRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTF-------APSGVTTEVKSVEMHHEQLA-EAVPGDNVGFNvknvSV 305
|
330
....*....|....
gi 1819251932 285 EDLGIGVTITDPAN 298
Cdd:PTZ00141 306 KDIKRGYVASDSKN 319
|
|
| tufA |
CHL00071 |
elongation factor Tu |
7-236 |
2.59e-17 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 84.24 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 7 NIAIIAHVDHGKTTLVDQL-----LRQSGTFRDNEKIaervmDSNDIERERGITILAKNCAVTWQGTHINIVDTPGHADF 81
Cdd:CHL00071 14 NIGTIGHVDHGKTTLTAAItmtlaAKGGAKAKKYDEI-----DSAPEEKARGITINTAHVEYETENRHYAHVDCPGHADY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 82 GGEVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVV-VNKVDKpgsrpdyVINAAF---------DLFDKL 151
Cdd:CHL00071 89 VKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVfLNKEDQ-------VDDEELlelvelevrELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 152 GATEDqlDFPVVYASGLNGWAALEEG---APGE-AWGTNMAPLFETVLKHVPPHEGDPAAPLQLQISSLDYSTFVGRIGV 227
Cdd:CHL00071 162 DFPGD--DIPIVSGSALLALEALTENpkiKRGEnKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVAT 239
|
....*....
gi 1819251932 228 GRVNSGTLK 236
Cdd:CHL00071 240 GRIERGTVK 248
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
8-136 |
3.32e-17 |
|
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: 79.44 E-value: 3.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 8 IAIIAHVDHGKTTLVDQlLRQsgtfrdnekiaervmdSNDIERE-RGIT--ILAKNCAVTWQGTHINIVDTPGHADFGGE 84
Cdd:cd01887 3 VTVMGHVDHGKTTLLDK-IRK----------------TNVAAGEaGGITqhIGAYQVPIDVKIPGITFIDTPGHEAFTNM 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1819251932 85 VERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVDKPGSR 136
Cdd:cd01887 66 RARGASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKPYGT 117
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
7-296 |
4.08e-17 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 84.11 E-value: 4.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 7 NIAIIAHVDHGKTTL---VDQLLRQSGTfrdNEKIAERVMDSNDIERERGITILAKNCAVTWQGTHINIVDTPGHADFGG 83
Cdd:PLN03127 63 NVGTIGHVDHGKTTLtaaITKVLAEEGK---AKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVDCPGHADYVK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 84 EVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVV-VNKVDKPgSRPDYVINAAFDLFDKLGATE-DQLDFP 161
Cdd:PLN03127 140 NMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVfLNKVDVV-DDEELLELVEMELRELLSFYKfPGDEIP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 162 VVYASGLngwAALeEGAPGEAWGTNMAPLFETVLKHVPPHEGDPAAPLQLQISslDYSTFVGR--IGVGRVNSGTLKPAM 239
Cdd:PLN03127 219 IIRGSAL---SAL-QGTNDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIE--DVFSIQGRgtVATGRVEQGTIKVGE 292
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1819251932 240 DVLVMEGPDGRAYKGRINQVLTFEGLnrvmADEAGPGDIV--LVNGI--EDLGIGVTITDP 296
Cdd:PLN03127 293 EVEIVGLRPGGPLKTTVTGVEMFKKI----LDQGQAGDNVglLLRGLkrEDVQRGQVICKP 349
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
7-200 |
1.26e-16 |
|
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: 78.39 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 7 NIAIIAHVDHGKTTLVDQL-----LRQSGTFRDNEKIaervmDSNDIERERGITILAKNCAVTWQGTHINIVDTPGHADF 81
Cdd:cd01884 4 NVGTIGHVDHGKTTLTAAItkvlaKKGGAKAKKYDEI-----DKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 82 GGEVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVV-VNKVDKPGSRP--DYVINAAFDLFDKLGATEDql 158
Cdd:cd01884 79 IKNMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVfLNKADMVDDEEllELVEMEVRELLSKYGFDGD-- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1819251932 159 DFPVVYASGLNgwaALEEGAPGEaWGTNMAPLFETVLKHVPP 200
Cdd:cd01884 157 DTPIVRGSALK---ALEGDDPNK-WVDKILELLDALDSYIPT 194
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
6-137 |
5.83e-16 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 80.95 E-value: 5.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 6 RNIAIIAHVDHGKTTLVDQLL------RQSGTFRdnEKIAERVMDSN--DIERERGITILAKNCAVTWQGTHINIVDTPG 77
Cdd:PRK00741 11 RTFAIISHPDAGKTTLTEKLLlfggaiQEAGTVK--GRKSGRHATSDwmEMEKQRGISVTSSVMQFPYRDCLINLLDTPG 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1819251932 78 HADFGGEVERALSMVDGVVLLIDAQEGPMPQTR--F-VTKkalaLGLKPIVV-VNKVDKPGSRP 137
Cdd:PRK00741 89 HEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTRklMeVCR----LRDTPIFTfINKLDRDGREP 148
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
7-298 |
1.68e-15 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 78.98 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 7 NIAIIAHVDHGKTTLVDQLLRQSGTFrdNEKIAER-----------------VMDSNDIERERGITILAKNCAVTWQGTH 69
Cdd:PLN00043 9 NIVVIGHVDSGKSTTTGHLIYKLGGI--DKRVIERfekeaaemnkrsfkyawVLDKLKAERERGITIDIALWKFETTKYY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 70 INIVDTPGHADFGGEVERALSMVDGVVLLIDAQEGPMP-------QTRFVTKKALALGLKPIV-VVNKVDK-----PGSR 136
Cdd:PLN00043 87 CTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMIcCCNKMDAttpkySKAR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 137 PDYVINAAFDLFDKLGATEDQLdfPVVYASGLNGWAALEEGAPGEAWgtnMAPLFETVLKHVPPHEGDPAAPLQLQISSL 216
Cdd:PLN00043 167 YDEIVKEVSSYLKKVGYNPDKI--PFVPISGFEGDNMIERSTNLDWY---KGPTLLEALDQINEPKRPSDKPLRLPLQDV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 217 DYSTFVGRIGVGRVNSGTLKPAMdvLVMEGPDGRAykgriNQVLTFEGLNRVMAdEAGPGDIVLVN----GIEDLGIGVT 292
Cdd:PLN00043 242 YKIGGIGTVPVGRVETGVIKPGM--VVTFGPTGLT-----TEVKSVEMHHESLQ-EALPGDNVGFNvknvAVKDLKRGYV 313
|
....*.
gi 1819251932 293 ITDPAN 298
Cdd:PLN00043 314 ASNSKD 319
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
8-142 |
2.01e-15 |
|
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: 79.43 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 8 IAIIAHVDHGKTTLVDQLlrqsgtfrDNEKIAERvmDSNDIERERGITILAKNcavtwQGTHINIVDTPGHADFGGEVER 87
Cdd:TIGR00487 90 VTIMGHVDHGKTSLLDSI--------RKTKVAQG--EAGGITQHIGAYHVENE-----DGKMITFLDTPGHEAFTSMRAR 154
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1819251932 88 ALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVDKPGSRPDYVIN 142
Cdd:TIGR00487 155 GAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVPIIVAINKIDKPEANPDRVKQ 209
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
7-236 |
2.60e-15 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 78.31 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 7 NIAIIAHVDHGKTTLVDQLL-----RQSGTFRDNEKIaervmDSNDIERERGITIlakNCA-VTWQ--GTHINIVDTPGH 78
Cdd:PRK00049 14 NVGTIGHVDHGKTTLTAAITkvlakKGGAEAKAYDQI-----DKAPEEKARGITI---NTAhVEYEteKRHYAHVDCPGH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 79 ADF------GgeverALSMvDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVV-VNKVDKpgsrpdyVINAAF------ 145
Cdd:PRK00049 86 ADYvknmitG-----AAQM-DGAILVVSAADGPMPQTREHILLARQVGVPYIVVfLNKCDM-------VDDEELlelvem 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 146 ---DLFDKLGATEDqlDFPVVYASGLngwAALeEGAPGEAWGTNMAPLFETVLKHVPPHEGDPAAPLQLQISslDYSTFV 222
Cdd:PRK00049 153 evrELLSKYDFPGD--DTPIIRGSAL---KAL-EGDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIE--DVFSIS 224
|
250
....*....|....*.
gi 1819251932 223 GRIGV--GRVNSGTLK 236
Cdd:PRK00049 225 GRGTVvtGRVERGIIK 240
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
7-237 |
5.59e-15 |
|
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: 77.11 E-value: 5.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 7 NIAIIAHVDHGKTTLVDQL-----LRQSGTFRDNEKIaervmDSNDIERERGITIlakNCA-VTWQ--GTHINIVDTPGH 78
Cdd:COG0050 14 NIGTIGHVDHGKTTLTAAItkvlaKKGGAKAKAYDQI-----DKAPEEKERGITI---NTShVEYEteKRHYAHVDCPGH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 79 ADF------GgeverALSMvDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVV-VNKVDKpGSRP---DYVINAAFDLF 148
Cdd:COG0050 86 ADYvknmitG-----AAQM-DGAILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKCDM-VDDEellELVEMEVRELL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 149 DKLGATEDqlDFPVVYASGLngwAALeEGAPGEAWGTNMAPLFETVLKHVPPHEGDPAAPLQLQISslDYSTFVGRIGV- 227
Cdd:COG0050 159 SKYGFPGD--DTPIIRGSAL---KAL-EGDPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVE--DVFSITGRGTVv 230
|
250
....*....|.
gi 1819251932 228 -GRVNSGTLKP 237
Cdd:COG0050 231 tGRVERGIIKV 241
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
10-131 |
1.61e-14 |
|
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: 76.88 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 10 IIA---HVDHGKTTLVDQLlrqsgTFRDNEKIAErvmdsndiERERGITI--------LAkncavtwQGTHINIVDTPGH 78
Cdd:COG3276 2 IIGtagHIDHGKTTLVKAL-----TGIDTDRLKE--------EKKRGITIdlgfaylpLP-------DGRRLGFVDVPGH 61
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1819251932 79 ADF--------GGeveralsmVDGVVLLIDAQEGPMPQTRfvtkKALA----LGLKP-IVVVNKVD 131
Cdd:COG3276 62 EKFiknmlagaGG--------IDLVLLVVAADEGVMPQTR----EHLAildlLGIKRgIVVLTKAD 115
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
8-284 |
2.39e-14 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 76.41 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 8 IAIIAHVDHGKTTLVDQLlRQSGTfrdNEKIAErvmdsndiererGIT--ILAKNCAVTWQGTHINIV--DTPGHADFGG 83
Cdd:CHL00189 247 VTILGHVDHGKTTLLDKI-RKTQI---AQKEAG------------GITqkIGAYEVEFEYKDENQKIVflDTPGHEAFSS 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 84 EVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVDKPGSRPDYVIN--AAFDLF-DKLGAtedqlDF 160
Cdd:CHL00189 311 MRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANTERIKQqlAKYNLIpEKWGG-----DT 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 161 PVVYASGLNgwaaleegapgeawGTNMAPLFETV--LKHVPPHEGDPAAPLQLQISSLDYSTFVGRIGVGRVNSGTLKPA 238
Cdd:CHL00189 386 PMIPISASQ--------------GTNIDKLLETIllLAEIEDLKADPTQLAQGIILEAHLDKTKGPVATILVQNGTLHIG 451
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1819251932 239 mDVLVMegpdGRAYkGRINQVLTFEGlNRVmaDEAGPGDIVLVNGI 284
Cdd:CHL00189 452 -DIIVI----GTSY-AKIRGMINSLG-NKI--NLATPSSVVEIWGL 488
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
7-236 |
2.71e-14 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 74.87 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 7 NIAIIAHVDHGKTTLVDQL-----LRQSGTFRDNEKIaervmDSNDIERERGITIlakNCA-VTWQGT--HINIVDTPGH 78
Cdd:PRK12735 14 NVGTIGHVDHGKTTLTAAItkvlaKKGGGEAKAYDQI-----DNAPEEKARGITI---NTShVEYETAnrHYAHVDCPGH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 79 ADF-GGEVERALSMvDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVV-VNKVDKPGSRP--DYVINAAFDLFDKLGAT 154
Cdd:PRK12735 86 ADYvKNMITGAAQM-DGAILVVSAADGPMPQTREHILLARQVGVPYIVVfLNKCDMVDDEEllELVEMEVRELLSKYDFP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 155 EDqlDFPVVYASGLngwAALeEGAPGEAWGTNMAPLFETVLKHVPPHEGDPAAPLQLQISslDYSTFVGRIGV--GRVNS 232
Cdd:PRK12735 165 GD--DTPIIRGSAL---KAL-EGDDDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIE--DVFSISGRGTVvtGRVER 236
|
....
gi 1819251932 233 GTLK 236
Cdd:PRK12735 237 GIVK 240
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
8-142 |
4.44e-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: 75.05 E-value: 4.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 8 IAIIAHVDHGKTTLVDqLLRQSgtfrdnekiaeRVmdsndIERE-RGIT--ILAKNcaVTWQGTHINIVDTPGHADF--- 81
Cdd:COG0532 7 VTVMGHVDHGKTSLLD-AIRKT-----------NV-----AAGEaGGITqhIGAYQ--VETNGGKITFLDTPGHEAFtam 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1819251932 82 ---GGEVeralsmVDGVVLLIDAQEGPMPQTRFVTKKALALGLkPIVV-VNKVDKPGSRPDYVIN 142
Cdd:COG0532 68 rarGAQV------TDIVILVVAADDGVMPQTIEAINHAKAAGV-PIIVaINKIDKPGANPDRVKQ 125
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
7-132 |
9.75e-14 |
|
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: 74.14 E-value: 9.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 7 NIAIIAHVDHGKTTLVDQLlrqsgTFRDNEKIAErvmdsndiERERGITILAKNCAVTWQGTHINIVDTPGHADFGGEVE 86
Cdd:TIGR00475 2 IIATAGHVDHGKTTLLKAL-----TGIAADRLPE--------EKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNAI 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1819251932 87 RALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKP-IVVVNKVDK 132
Cdd:TIGR00475 69 AGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHtIVVITKADR 115
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
7-131 |
3.83e-13 |
|
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: 68.16 E-value: 3.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 7 NIAIIAHVDHGKTTLVDQLlrqsgtfrdNEKIAERVMDSNDIERERGITI--------------LAKNCAVTWQGTHINI 72
Cdd:cd01889 2 NVGLLGHVDSGKTSLAKAL---------SEIASTAAFDKNPQSQERGITLdlgfssfevdkpkhLEDNENPQIENYQITL 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1819251932 73 VDTPGHADFGGEVERALSMVDGVVLLIDAQEGPMPQtrfvTKKALALG----LKPIVVVNKVD 131
Cdd:cd01889 73 VDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQ----TAECLVIGellcKPLIVVLNKID 131
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
13-132 |
4.02e-13 |
|
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: 67.63 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 13 HVDHGKTTLVDQLlrqsgTFRDNEKIAErvmdsndiERERGITIlakNCAVTW----QGTHINIVDTPGHADFGGEVERA 88
Cdd:cd04171 7 HIDHGKTTLIKAL-----TGIETDRLPE--------EKKRGITI---DLGFAYldlpDGKRLGFIDVPGHEKFVKNMLAG 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1819251932 89 LSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKP-IVVVNKVDK 132
Cdd:cd04171 71 AGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKgLVVLTKADL 115
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
7-131 |
2.66e-12 |
|
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: 66.05 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 7 NIAIIAHVDHGKTTLVDQLLRQSG--------TFRDNEKIAER--------VMDSNDIERERGITI-LAKNCAVTWQGTH 69
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKsifedqlaALERSKSSGTQgekldlalLVDGLQAEREQGITIdVAYRYFSTPKRKF 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1819251932 70 InIVDTPGHADFGGEVERALSMVDGVVLLIDAQEGPMPQTR---FVTkkALaLGLKPIVV-VNKVD 131
Cdd:cd04166 81 I-IADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRrhsYIA--SL-LGIRHVVVaVNKMD 142
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
14-301 |
3.94e-12 |
|
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: 68.55 E-value: 3.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 14 VDHGKTTLVDQLLRQSGTF---------RDNEKIAER--------VMDSNDIERERGITI-LAKNCAVTWQGTHInIVDT 75
Cdd:TIGR02034 9 VDDGKSTLIGRLLHDTKQIyedqlaaleRDSKKHGTQggeidlalLVDGLQAEREQGITIdVAYRYFSTDKRKFI-VADT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 76 PGHADFGGEVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVV-VNKVDKPGSRPDYVINAAFDlFDKLGAT 154
Cdd:TIGR02034 88 PGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLaVNKMDLVDYDEEVFENIKKD-YLAFAEQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 155 EDQLDFPVVYASGLNGwAALEEGAPGEAW--GTNMAPLFETVLKHVPPHEGDPAAPLQLQI-SSLDYSTFVGRIgvgrvN 231
Cdd:TIGR02034 167 LGFRDVTFIPLSALKG-DNVVSRSESMPWysGPTLLEILETVEVERDAQDLPLRFPVQYVNrPNLDFRGYAGTI-----A 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1819251932 232 SGTLKPAMDVLVMegPDGRayKGRINQVLTFEGlnrvMADEAGPGD---IVLVNGIeDLGIGVTITDPANPQP 301
Cdd:TIGR02034 241 SGSVHVGDEVVVL--PSGR--SSRVARIVTFDG----DLEQARAGQavtLTLDDEI-DISRGDLLAAADSAPE 304
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
9-171 |
4.63e-12 |
|
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: 64.40 E-value: 4.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 9 AIIAHVDHGKTTLVDQLLRQsgtfrdnekiaervmDSNDIERERGITILAKNCAVTWQ--GTHINIVDTPGHADFGG--- 83
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGG---------------EVGEVSDVPGTTRDPDVYVKELDkgKVKLVLVDTPGLDEFGGlgr 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 84 --EVERALSMVDGVVLLIDAQEGPMPQT-RFVTKKALALGLKPIVVV-NKVDKPGSRPDYVINAAFDLFDKlgatedqLD 159
Cdd:cd00882 66 eeLARLLLRGADLILLVVDSTDRESEEDaKLLILRRLRKEGIPIILVgNKIDLLEEREVEELLRLEELAKI-------LG 138
|
170
....*....|..
gi 1819251932 160 FPVVYASGLNGW 171
Cdd:cd00882 139 VPVFEVSAKTGE 150
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
7-217 |
2.21e-11 |
|
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: 65.84 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 7 NIAIIAHVDHGKTTLVDQLlrqSGTFRDNEKiaErvmdsndiERERGITI--------------LAKNCAVTWQGT---- 68
Cdd:TIGR03680 6 NIGMVGHVDHGKTTLTKAL---TGVWTDTHS--E--------ELKRGISIrlgyadaeiykcpeCDGPECYTTEPVcpnc 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 69 --------HINIVDTPGHADFGGEVERALSMVDGVVLLIDAQEG-PMPQTRFVTKKALALGLKPIVVV-NKVD---KPGS 135
Cdd:TIGR03680 73 gsetellrRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVqNKIDlvsKEKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 136 RPDYvinAAFDLFDKLGATEDQldfPVVYASGLNgwaaleegapgeawGTNMAPLFETVLKHVPPHEGDPAAPLQLQIS- 214
Cdd:TIGR03680 153 LENY---EEIKEFVKGTVAENA---PIIPVSALH--------------NANIDALLEAIEKFIPTPERDLDKPPLMYVAr 212
|
...
gi 1819251932 215 SLD 217
Cdd:TIGR03680 213 SFD 215
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
7-131 |
3.53e-11 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 65.26 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 7 NIAIIAHVDHGKTTLVDQLlrqSGTFRDneKIAErvmdsndiERERGITI----------LAKNC----AVTWQGT---- 68
Cdd:PRK04000 11 NIGMVGHVDHGKTTLVQAL---TGVWTD--RHSE--------ELKRGITIrlgyadatirKCPDCeepeAYTTEPKcpnc 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 69 --------HINIVDTPGHadfggEVERA--LS---MVDGVVLLIDAQEG-PMPQTR--FVtkkAL-ALGLKPIVVV-NKV 130
Cdd:PRK04000 78 gsetellrRVSFVDAPGH-----ETLMAtmLSgaaLMDGAILVIAANEPcPQPQTKehLM---ALdIIGIKNIVIVqNKI 149
|
.
gi 1819251932 131 D 131
Cdd:PRK04000 150 D 150
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
7-131 |
6.65e-11 |
|
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: 61.90 E-value: 6.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 7 NIAIIAHVDHGKTTLVDQLlrqSG--TFRDNEkiaervmdsndiERERGITIL-----AK----------NCAVTWQGT- 68
Cdd:cd01888 2 NIGTIGHVAHGKTTLVKAL---SGvwTVRHKE------------ELKRNITIKlgyanAKiykcpncgcpRPYDTPECEc 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 69 -----------HINIVDTPGHadfggEVERA-----LSMVDGVVLLIDAQEG-PMPQTRfvtkKALA----LGLKPIVVV 127
Cdd:cd01888 67 pgcggetklvrHVSFVDCPGH-----EILMAtmlsgAAVMDGALLLIAANEPcPQPQTS----EHLAaleiMGLKHIIIL 137
|
....*
gi 1819251932 128 -NKVD 131
Cdd:cd01888 138 qNKID 142
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
7-279 |
1.02e-10 |
|
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: 63.95 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 7 NIAIIAHVDHGKTTLV------------DQL--LRQSGTFRDNEKI--AeRVMDSNDIERERGITIlakncAVTW----- 65
Cdd:COG2895 19 RFITCGSVDDGKSTLIgrllydtksifeDQLaaLERDSKKRGTQEIdlA-LLTDGLQAEREQGITI-----DVAYryfst 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 66 QGTHINIVDTPGHADFggevERalSMVDG------VVLLIDAQEGPMPQTR---FVTkkALaLGLKPIVV-VNKVDkpgs 135
Cdd:COG2895 93 PKRKFIIADTPGHEQY----TR--NMVTGastadlAILLIDARKGVLEQTRrhsYIA--SL-LGIRHVVVaVNKMD---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 136 RPDY------VINAAFDLFDKlgatedQLDFPVVYA---SGLNGWAALEEGApgeawgtNMA-----PLFETvLKHVPPH 201
Cdd:COG2895 160 LVDYseevfeEIVADYRAFAA------KLGLEDITFipiSALKGDNVVERSE-------NMPwydgpTLLEH-LETVEVA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 202 EGDPAAPLQLQI-----SSLDYstfvgRIGVGRVNSGTLKPAMDVLVMegPDGRayKGRINQVLTFEGlnrvMADEAGPG 276
Cdd:COG2895 226 EDRNDAPFRFPVqyvnrPNLDF-----RGYAGTIASGTVRVGDEVVVL--PSGK--TSTVKSIVTFDG----DLEEAFAG 292
|
...
gi 1819251932 277 DIV 279
Cdd:COG2895 293 QSV 295
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
14-279 |
8.30e-10 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 61.48 E-value: 8.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 14 VDHGKTTLVDQLL------------------RQSGTFRDNEKIAeRVMDSNDIERERGITI-LAKNCAVTWQGTHInIVD 74
Cdd:PRK05506 33 VDDGKSTLIGRLLydskmifedqlaalerdsKKVGTQGDEIDLA-LLVDGLAAEREQGITIdVAYRYFATPKRKFI-VAD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 75 TPGHADFGGEVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVV-VNKVDKPGSRPD--YVINAAFDLF-DK 150
Cdd:PRK05506 111 TPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLaVNKMDLVDYDQEvfDEIVADYRAFaAK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 151 LGATedqlDFPVVYASGLNG--WAALEEGAPgeaW--GTNMAPLFETVLKHVPPHEGDPAAPLQLQI-SSLDYSTFVGRI 225
Cdd:PRK05506 191 LGLH----DVTFIPISALKGdnVVTRSARMP---WyeGPSLLEHLETVEIASDRNLKDFRFPVQYVNrPNLDFRGFAGTV 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1819251932 226 GvgrvnSGTLKPAMDVLVMegPDGRayKGRINQVLTFEGlnrvMADEAGPGDIV 279
Cdd:PRK05506 264 A-----SGVVRPGDEVVVL--PSGK--TSRVKRIVTPDG----DLDEAFAGQAV 304
|
|
| EFG_mtEFG_II |
cd04088 |
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation ... |
221-295 |
1.09e-08 |
|
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: 52.52 E-value: 1.09e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1819251932 221 FVGRIGVGRVNSGTLKPAMDVLVmegpDGRAYKGRINQVLTFEGLNRVMADEAGPGDIVLVNGIEDLGIGVTITD 295
Cdd:cd04088 13 FVGKLTFFRVYSGTLKSGSTVYN----STKGKKERVGRLLRMHGKKREEVEELGAGDIGAVVGLKDTRTGDTLCD 83
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
7-131 |
1.32e-08 |
|
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: 57.15 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 7 NIAIIAHVDHGKTTLVDQLlrqSGTFRDneKIAErvmdsndiERERGITI----------LAKNC----AVTWQGT---- 68
Cdd:COG5257 7 NIGVVGHVDHGKTTLVQAL---TGVWTD--RHSE--------ELKRGITIrlgyadatfyKCPNCeppeAYTTEPKcpnc 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 69 --------HINIVDTPGHadfggEVERA--LS---MVDGVVLLIDAQEG-PMPQTR--FVtkkAL-ALGLKPIVVV-NKV 130
Cdd:COG5257 74 gsetellrRVSFVDAPGH-----ETLMAtmLSgaaLMDGAILVIAANEPcPQPQTKehLM---ALdIIGIKNIVIVqNKI 145
|
.
gi 1819251932 131 D 131
Cdd:COG5257 146 D 146
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
63-233 |
1.47e-08 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 57.37 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 63 VTWQGTHINIVDTPG----HADFGGEV----ERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVDKPG 134
Cdd:PRK00093 44 AEWLGREFILIDTGGiepdDDGFEKQIreqaELAIEEADVILFVVDGRAGLTPADEEIAKILRKSNKPVILVVNKVDGPD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 135 SRPDyvinaAFDlFDKLGATEdqldfpVVYASGLNgwaaleegapgeawGTNMAPLFETVLKHVPPHEGDPAAPLQLQIS 214
Cdd:PRK00093 124 EEAD-----AYE-FYSLGLGE------PYPISAEH--------------GRGIGDLLDAILEELPEEEEEDEEDEPIKIA 177
|
170
....*....|....*....
gi 1819251932 215 sldystfvgrIgVGRVNSG 233
Cdd:PRK00093 178 ----------I-IGRPNVG 185
|
|
| EngA1 |
cd01894 |
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
63-138 |
5.54e-08 |
|
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: 52.44 E-value: 5.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 63 VTWQGTHINIVDTPGHADFGGE--------VERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVDKPG 134
Cdd:cd01894 40 AEWGGREFILIDTGGIEPDDEGiskeireqAEIAIEEADVILFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKIDNIK 119
|
....
gi 1819251932 135 SRPD 138
Cdd:cd01894 120 EEEE 123
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
223-294 |
5.57e-08 |
|
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: 49.96 E-value: 5.57e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1819251932 223 GRIGVGRVNSGTLKPAMDVLVMEGPDGRAY-KGRINQVLTFEGLNRVMADEAGPGDIVLVNGIEDLGIGVTIT 294
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTGKKKiVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| EFG_III-like |
cd16257 |
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G ... |
310-388 |
7.16e-08 |
|
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: 49.65 E-value: 7.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 310 PTLTMNFCVNTSplagregkyVTSRQIWDRLQKELQSNVALRVRESGEDGIFEVSGRGELHLTILLENMRRE-GYELAVS 388
Cdd:cd16257 1 PVVFVTVEVKNP---------LDQEKLLEGLERLSEEDPALQVYREESTGEFILSGLGELHLEIIVARLEREyGVELVVS 71
|
|
| EFG_mtEFG_C |
cd03713 |
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational ... |
403-478 |
7.17e-08 |
|
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: 49.83 E-value: 7.17e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1819251932 403 EPIELVTVDVEDQHQGGVMQALGERKGELANMEVDGRGRVrLEYRIPARGLIGFSNEFMNLTRGTGLISNIFDGYE 478
Cdd:cd03713 1 EPIMKVEVTVPEEYMGDVIGDLSSRRGQILGTESRGGWKV-IKAEVPLAEMFGYSTDLRSLTQGRGSFTMEFSHYE 75
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
63-228 |
7.90e-08 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 55.03 E-value: 7.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 63 VTWQGTHINIVDTPG-----HADFGGE----VERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGlKP-IVVVNKVDK 132
Cdd:COG1160 45 AEWGGREFTLIDTGGiepddDDGLEAEireqAELAIEEADVILFVVDGRAGLTPLDEEIAKLLRRSG-KPvILVVNKVDG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 133 PGSRPDyvinaAFDLFdKLGATEdqldfpVVYASGLNgwaaleegapgeawGTNMAPLFETVLKHVPPHEGDPAAPLQLQ 212
Cdd:COG1160 124 PKREAD-----AAEFY-SLGLGE------PIPISAEH--------------GRGVGDLLDAVLELLPEEEEEEEEDDPIK 177
|
170
....*....|....*.
gi 1819251932 213 ISsldystFVGRIGVG 228
Cdd:COG1160 178 IA------IVGRPNVG 187
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
7-129 |
8.27e-08 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 50.70 E-value: 8.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 7 NIAIIAHVDHGKTTLVDQLLRQsgtfrdnEKIAERVMdsndiererGITILAKNCAVTWQGTHINIVDTPG-----HADF 81
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGA-------KAIVSDYP---------GTTRDPNEGRLELKGKQIILVDTPGliegaSEGE 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1819251932 82 G-GEVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNK 129
Cdd:pfam01926 65 GlGRAFLAIIEADLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
8-171 |
1.39e-07 |
|
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: 51.66 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 8 IAIIAHVDHGKTTLVDQLLRQsgtfrdnekiaERVMDSNdierERGITILAKNCAVTWQGTHINIVDTPG-----HADFG 82
Cdd:cd01895 5 IAIIGRPNVGKSSLLNALLGE-----------ERVIVSD----IAGTTRDSIDVPFEYDGQKYTLIDTAGirkkgKVTEG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 83 GE------VERALSMVDGVVLLIDAQEGPMPQ----TRFVTKKALALglkpIVVVNKVDKPGSRPDYVINAAFDLFDKLG 152
Cdd:cd01895 70 IEkysvlrTLKAIERADVVLLVLDASEGITEQdlriAGLILEEGKAL----IIVVNKWDLVEKDEKTMKEFEKELRRKLP 145
|
170 180
....*....|....*....|
gi 1819251932 153 atedQLDF-PVVYASGLNGW 171
Cdd:cd01895 146 ----FLDYaPIVFISALTGQ 161
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
14-131 |
8.43e-07 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 51.84 E-value: 8.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 14 VDHGKTTLVDQLL---RQ------SGTFRDNEKIA---ERV-----MDSNDIERERGITI-LAKNCAVTWQGTHInIVDT 75
Cdd:PRK05124 36 VDDGKSTLIGRLLhdtKQiyedqlASLHNDSKRHGtqgEKLdlallVDGLQAEREQGITIdVAYRYFSTEKRKFI-IADT 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1819251932 76 PGHADFGGEVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVV-VNKVD 131
Cdd:PRK05124 115 PGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVaVNKMD 171
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
8-134 |
1.21e-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: 51.35 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 8 IAIIAHVDHGKTTLVDQLLRQSGTFRDNEKIAERVMDSndierERGITILAKNCAVTWQGTHINI-------VDTPGHAD 80
Cdd:TIGR00491 7 VVVLGHVDHGKTTLLDKIRGTAVVKKEAGGITQHIGAS-----EVPTDVIEKICGDLLKSFKIKLkipgllfIDTPGHEA 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1819251932 81 FGGEVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVDK-PG 134
Cdd:TIGR00491 82 FTNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTPFVVAANKIDRiPG 136
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
8-197 |
1.21e-06 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 48.82 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 8 IAIIAHVDHGKTTLVDQLLRqsgtfrdnEKIAERVMDSndierERGITILAKNCAVTWQGTHINIVDTPGHADF---GGE 84
Cdd:COG1100 6 IVVVGTGGVGKTSLVNRLVG--------DIFSLEKYLS-----TNGVTIDKKELKLDGLDVDLVIWDTPGQDEFretRQF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 85 VERALSMVDGVVLLIDAQegpMPQTRFVTKKALA----LGLKP--IVVVNKVDKpgsRPDYVINAAFDLFDKLGateDQL 158
Cdd:COG1100 73 YARQLTGASLYLFVVDGT---REETLQSLYELLEslrrLGKKSpiILVLNKIDL---YDEEEIEDEERLKEALS---EDN 143
|
170 180 190
....*....|....*....|....*....|....*....
gi 1819251932 159 DFPVVYASGLNGWaaleegapgeawgtNMAPLFETVLKH 197
Cdd:COG1100 144 IVEVVATSAKTGE--------------GVEELFAALAEI 168
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
73-202 |
1.21e-06 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 50.37 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 73 VDTPG-----HAdFG----GEVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVDKpgSRPDyvina 143
Cdd:COG1159 56 VDTPGihkpkRK-LGrrmnKAAWSALEDVDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDL--VKKE----- 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 144 afDLFDKLGATEDQLDF-PVVYASGLNgwaaleegapgeawGTNMAPLFETVLKHVPPHE 202
Cdd:COG1159 128 --ELLPLLAEYSELLDFaEIVPISALK--------------GDNVDELLDEIAKLLPEGP 171
|
|
| lepA_C |
cd03709 |
lepA_C: This family represents the C-terminal region of LepA, a GTP-binding protein localized ... |
403-478 |
2.81e-06 |
|
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: 45.56 E-value: 2.81e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1819251932 403 EPIELVTVDVEDQHQGGVMQALGERKGELANMEVDGRGRVRLEYRIPARGLI-GFSNEFMNLTRGTGLISNIFDGYE 478
Cdd:cd03709 1 EPFVKATIITPSEYLGAIMELCQERRGVQKDMEYLDANRVMLTYELPLAEIVyDFFDKLKSISKGYASLDYELIGYR 77
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
17-202 |
3.00e-06 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 49.28 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 17 GKTTLVDQLLrqsgtfrdNEKIAervMDS-------NDIereRGItilakncaVTWQGTHINIVDTPG----HADFG--- 82
Cdd:PRK00089 17 GKSTLLNALV--------GQKIS---IVSpkpqttrHRI---RGI--------VTEDDAQIIFVDTPGihkpKRALNram 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 83 -GEVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVDKPGSRPdyvinaafDLFDKLGATEDQLDF- 160
Cdd:PRK00089 75 nKAAWSSLKDVDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLVKDKE--------ELLPLLEELSELMDFa 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1819251932 161 PVVYASGLNgwaaleegapgeawGTNMAPLFETVLKHVPPHE 202
Cdd:PRK00089 147 EIVPISALK--------------GDNVDELLDVIAKYLPEGP 174
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
17-170 |
5.04e-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: 47.07 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 17 GKTTLVDQLLrqsgtfrdNEKIA--------ERvmdsNDIereRGItilakncaVTWQGTHINIVDTPG-HADFGG---- 83
Cdd:cd04163 15 GKSTLLNALV--------GQKISivspkpqtTR----NRI---RGI--------YTDDDAQIIFVDTPGiHKPKKKlger 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 84 ---EVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVDKpgsrpdyvINAAFDLFDKLGATEDQLDF 160
Cdd:cd04163 72 mvkAAWSALKDVDLVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDL--------VKDKEDLLPLLEKLKELHPF 143
|
170
....*....|.
gi 1819251932 161 -PVVYASGLNG 170
Cdd:cd04163 144 aEIFPISALKG 154
|
|
| PRK09518 |
PRK09518 |
bifunctional cytidylate kinase/GTPase Der; Reviewed |
8-138 |
7.54e-06 |
|
bifunctional cytidylate kinase/GTPase Der; Reviewed
Pssm-ID: 236546 [Multi-domain] Cd Length: 712 Bit Score: 49.02 E-value: 7.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 8 IAIIAHVDHGKTTLVDQLLRQSgtfrdnekiAERVMDSNDIERERgITILAKncavtWQGTHINIVDTPG--------HA 79
Cdd:PRK09518 278 VAIVGRPNVGKSTLVNRILGRR---------EAVVEDTPGVTRDR-VSYDAE-----WAGTDFKLVDTGGweadvegiDS 342
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1819251932 80 DFGGEVERALSMVDGVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKVDKPGSRPD 138
Cdd:PRK09518 343 AIASQAQIAVSLADAVVFVVDGQVGLTSTDERIVRMLRRAGKPVVLAVNKIDDQASEYD 401
|
|
| mtEFG1_C |
cd04097 |
mtEFG1_C: C-terminus of mitochondrial Elongation factor G1 (mtEFG1)-like proteins found in ... |
403-468 |
1.10e-05 |
|
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: 43.85 E-value: 1.10e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1819251932 403 EPIELVTVDVEDQHQGGVMQALGERKGELANMEVDGrGRVRLEYRIPARGLIGFSNEFMNLTRGTG 468
Cdd:cd04097 1 EPIMKVEVTAPTEFQGNVIGLLNKRKGTIVDTDTGE-DEFTLEAEVPLNDMFGYSTELRSMTQGKG 65
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
8-137 |
1.18e-05 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 48.25 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 8 IAIIAHVDHGKTTLVDqllrqsgtfrdnekiaeRVMDSNDIERERG-IT-----------ILAKNCAVTWQGTHINI--- 72
Cdd:PRK04004 9 VVVLGHVDHGKTTLLD-----------------KIRGTAVAAKEAGgITqhigatevpidVIEKIAGPLKKPLPIKLkip 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1819251932 73 ----VDTPGHADFGGEVERALSMVDGVVLLIDAQEGPMPQtrfvTKKALALgLK----P-IVVVNKVDK-PGSRP 137
Cdd:PRK04004 72 gllfIDTPGHEAFTNLRKRGGALADIAILVVDINEGFQPQ----TIEAINI-LKrrktPfVVAANKIDRiPGWKS 141
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
8-110 |
1.34e-05 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 48.12 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 8 IAIIAHVDHGKTTLVdqllrQSGTFRDNEKIAErvmdsndiERERGITI-LAkncAVTW---QGTHINIVDTPGHADFGG 83
Cdd:PRK10512 3 IATAGHVDHGKTTLL-----QAITGVNADRLPE--------EKKRGMTIdLG---YAYWpqpDGRVLGFIDVPGHEKFLS 66
|
90 100
....*....|....*....|....*..
gi 1819251932 84 EVERALSMVDGVVLLIDAQEGPMPQTR 110
Cdd:PRK10512 67 NMLAGVGGIDHALLVVACDDGVMAQTR 93
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
7-190 |
1.87e-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: 45.62 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 7 NIAIIAHVDHGKTTLVDQLLRqsgtfrdnekiaERVMDSndiererGITIL-AKNCAVTWQ-GTHINIVDTPG------- 77
Cdd:cd09912 2 LLAVVGEFSAGKSTLLNALLG------------EEVLPT-------GVTPTtAVITVLRYGlLKGVVLVDTPGlnstieh 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 78 HADfggEVERALSMVDGVVLLIDAQEgpmPQTR----FVTKKALALGLKPIVVVNKVDKpgSRPDYVINAAFDLFDKLGA 153
Cdd:cd09912 63 HTE---ITESFLPRADAVIFVLSADQ---PLTEsereFLKEILKWSGKKIFFVLNKIDL--LSEEELEEVLEYSREELGV 134
|
170 180 190
....*....|....*....|....*....|....*...
gi 1819251932 154 TEDQLDFPVVYA-SGLNGWAALEEGAPGEAWGTNMAPL 190
Cdd:cd09912 135 LELGGGEPRIFPvSAKEALEARLQGDEELLEQSGFEEL 172
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
209-294 |
3.40e-05 |
|
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: 42.25 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 209 LQLQISSLDYSTFVGRIGVGRVNSGTLKPAMDVLVMegpdGRAYKGRINQVLTFeglnRVMADEAGPGDIVLVN--GIED 286
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRIL----PKGITGRVTSIERF----HEEVDEAKAGDIVGIGilGVKD 72
|
....*...
gi 1819251932 287 LGIGVTIT 294
Cdd:cd01342 73 ILTGDTLT 80
|
|
| EF2_II |
cd16268 |
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 ... |
225-286 |
5.11e-05 |
|
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: 42.20 E-value: 5.11e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1819251932 225 IGVGRVNSGTLKPAMDVLVME-----GPDGRAYKGRINQVLTFEGLNRVMADEAGPGDIVLVNGIED 286
Cdd:cd16268 19 VAFGRVFSGTVRRGQEVYILGpkyvpGKKDDLKKKRIQQTYLMMGREREPVDEVPAGNIVGLVGLDD 85
|
|
| EFG_C |
smart00838 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
403-478 |
5.17e-05 |
|
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of Elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopt a ferredoxin-like fold.
Pssm-ID: 197906 [Multi-domain] Cd Length: 85 Bit Score: 42.11 E-value: 5.17e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1819251932 403 EPIELVTVDVEDQHQGGVMQALGERKGELANMEvDGRGRVRLEYRIPARGLIGFSNEFMNLTRGTGLISNIFDGYE 478
Cdd:smart00838 3 EPIMKVEVTVPEEYMGDVIGDLNSRRGKIEGME-QRGGAQVIKAKVPLSEMFGYATDLRSATQGRATWSMEFSHYE 77
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
17-171 |
5.55e-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: 43.77 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 17 GKTTLVDQLLRQsgtfrdNEKIAERVMDSN-DIERERGITILAKNcavtwqgthINIVDTPGHADFGGE----VERALSM 91
Cdd:cd00880 9 GKSSLLNALLGQ------NVGIVSPIPGTTrDPVRKEWELLPLGP---------VVLIDTPGLDEEGGLgrerVEEARQV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 92 ---VDGVVLLIDAQEGPMPQTRFVTKKaLALGLKPIVVVNKVDKPGSRPdyviNAAFDLFDKLGATedqLDFPVVYASGL 168
Cdd:cd00880 74 adrADLVLLVVDSDLTPVEEEAKLGLL-RERGKPVLLVLNKIDLVPESE----EEELLRERKLELL---PDLPVIAVSAL 145
|
...
gi 1819251932 169 NGW 171
Cdd:cd00880 146 PGE 148
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
5-170 |
6.51e-05 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 45.81 E-value: 6.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 5 IRnIAIIAHVDHGKTTLVDQLLRQsgtfrdnekiaERVMDSNdierERGITILAKNCAVTWQGTHINIVDTPG------- 77
Cdd:PRK00093 174 IK-IAIIGRPNVGKSSLINALLGE-----------ERVIVSD----IAGTTRDSIDTPFERDGQKYTLIDTAGirrkgkv 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 78 HADfggeVE--------RALSMVDGVVLLIDAQEGPMPQ----TRFVTKKALALglkpIVVVNKVDKpgsrpdyVINAAF 145
Cdd:PRK00093 238 TEG----VEkysvirtlKAIERADVVLLVIDATEGITEQdlriAGLALEAGRAL----VIVVNKWDL-------VDEKTM 302
|
170 180 190
....*....|....*....|....*....|.
gi 1819251932 146 DLF-----DKLGatedQLDF-PVVYASGLNG 170
Cdd:PRK00093 303 EEFkkelrRRLP----FLDYaPIVFISALTG 329
|
|
| EFG_III |
cd16262 |
Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial ... |
338-391 |
1.79e-04 |
|
Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial Elongation factor G (EF-G), and mitochondrial Elongation factor G1 (mtEFG1) and G2 (mtEFG2), which play an important role during peptide synthesis and tRNA site changes. In bacteria, this translocation step is catalyzed by EF-G_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. mtEFG1 and mtEFG2 show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects, and a tendency to lose mitochondrial DNA. No clear phenotype has been found for mutants of the yeast homolog of mtEFG2, MEF2.
Pssm-ID: 293919 [Multi-domain] Cd Length: 76 Bit Score: 40.13 E-value: 1.79e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1819251932 338 DRLQKELQSnvaLRVRESGEDGIFEVSGRGELHLTILLENMRRE-GYELAVSKPR 391
Cdd:cd16262 25 ARLAEEDPT---LRVSRDEETGQTILSGMGELHLEIIVERLKREyGVEVEVGKPQ 76
|
|
| Tet_C |
cd03711 |
Tet_C: C-terminus of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology ... |
403-481 |
3.27e-04 |
|
Tet_C: C-terminus of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology to the C terminal domains of the elongation factors EF-G and EF-2. Tet(M) and Tet(O) catalyze the release of tetracycline (Tc) from the ribosome in a GTP-dependent manner thereby mediating Tc resistance. Tcs are broad-spectrum antibiotics. Typical Tcs bind to the ribosome and inhibit the elongation phase of protein synthesis, by inhibiting the occupation of site A by aminoacyl-tRNA.
Pssm-ID: 239682 [Multi-domain] Cd Length: 78 Bit Score: 39.53 E-value: 3.27e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1819251932 403 EPIELVTVDVEDQHQGGVMQALGERKGELANMEVDGrGRVRLEYRIPARGLIGFSNEFMNLTRGTGLISNIFDGYEAYK 481
Cdd:cd03711 1 EPYLRFELEVPQDALGRAMSDLAKMGATFEDPQIKG-DEVTLEGTIPVATSQDYQSELPSYTHGEGVLETEFKGYRPCH 78
|
|
| YihA_EngB |
cd01876 |
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
67-132 |
1.02e-03 |
|
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.
Pssm-ID: 206665 [Multi-domain] Cd Length: 170 Bit Score: 40.19 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 67 GTHINIVDTPGhadFGG------EVERALSMVD----------GVVLLIDAQEGPMPQTRFVTKKALALGLKPIVVVNKV 130
Cdd:cd01876 44 GDKFRLVDLPG---YGYakvskeVREKWGKLIEeylenrenlkGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKA 120
|
..
gi 1819251932 131 DK 132
Cdd:cd01876 121 DK 122
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
17-171 |
1.08e-03 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 41.93 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 17 GKTTLVDQLLRQsgtfrdnekiaERVM---------DSNDIErergitilakncaVTWQGTHINIVDTPG-----HADFG 82
Cdd:COG1160 187 GKSSLINALLGE-----------ERVIvsdiagttrDSIDTP-------------FERDGKKYTLIDTAGirrkgKVDEG 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819251932 83 GE---VERALSMV---DGVVLLIDAQEGpmpqtrfVTK--KALAlGL-----KPIV-VVNK---VDKPGSRPDYVINaaf 145
Cdd:COG1160 243 IEkysVLRTLRAIeraDVVLLVIDATEG-------ITEqdLKIA-GLaleagKALViVVNKwdlVEKDRKTREELEK--- 311
|
170 180
....*....|....*....|....*..
gi 1819251932 146 DLFDKLGatedQLDF-PVVYASGLNGW 171
Cdd:COG1160 312 EIRRRLP----FLDYaPIVFISALTGQ 334
|
|
| RF3_II |
cd03689 |
Domain II of bacterial Release Factor 3; This subfamily represents domain II of bacterial ... |
224-294 |
1.16e-03 |
|
Domain II of bacterial Release Factor 3; This subfamily represents domain II of bacterial Release Factor 3 (RF3). Termination of protein synthesis by the ribosome requires two release factor (RF) classes. The class II RF3 is a GTPase that removes class I RFs (RF1 or RF2) from the ribosome after release of the nascent polypeptide. RF3 in the GDP state binds to the ribosomal class I RF complex, followed by an exchange of GDP for GTP and release of the class I RF. Sequence comparison of class II release factors with elongation factors shows that prokaryotic RF3 is more similar to EF-G whereas eukaryotic eRF3 is more similar to eEF1A, implying that their precise function may differ.
Pssm-ID: 293890 [Multi-domain] Cd Length: 87 Bit Score: 38.41 E-value: 1.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1819251932 224 RIGVGRVNSGTLKPAMDVLVMEGpdGRayKGRINQVLTFEGLNRVMADEAGPGDIVLVNGIEDLGIGVTIT 294
Cdd:cd03689 19 RIAFLRVCSGKFERGMKVKHVRT--GK--EVRLSNATTFMAQDRETVEEAYPGDIIGLPNHGTFQIGDTFT 85
|
|
| EFG_III |
pfam14492 |
Elongation Factor G, domain III; This domain is found in Elongation Factor G. It shares a ... |
340-381 |
2.74e-03 |
|
Elongation Factor G, domain III; This domain is found in Elongation Factor G. It shares a similar structure with domain V (pfam00679). Structural studies in drosophila indicate this is domain 3.
Pssm-ID: 464188 [Multi-domain] Cd Length: 75 Bit Score: 36.69 E-value: 2.74e-03
10 20 30 40
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gi 1819251932 340 LQKELQSNVALRVRESGEDGIFEVSGRGELHLTILLENMRRE 381
Cdd:pfam14492 25 LNRLLEEDPTLRVERDEETGETILSGMGELHLEIVVDRLKRK 66
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