|
Name |
Accession |
Description |
Interval |
E-value |
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
5-610 |
0e+00 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 1219.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 5 QIDKLRNIAIIAHVDHGKTTLVDKLLQQSGTLESRGEAEERVMDSNDIEKERGITILAKNTAIDWNDYRINIVDTPGHAD 84
Cdd:COG1217 2 MREDIRNIAIIAHVDHGKTTLVDALLKQSGTFRENQEVAERVMDSNDLERERGITILAKNTAVRYKGVKINIVDTPGHAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 85 FGGEVERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDRPGARPDWVMDQVFDLFDNLGATDEQLDF 164
Cdd:COG1217 82 FGGEVERVLSMVDGVLLLVDAFEGPMPQTRFVLKKALELGLKPIVVINKIDRPDARPDEVVDEVFDLFIELGATDEQLDF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 165 TVVYASALNGWATMEEGEVGTDMEPLFQAVVDTVEAPAVDLEGPLQMQISQLDYSSYVGVIGVARVTRGSVKPNQQVTIV 244
Cdd:COG1217 162 PVVYASARNGWASLDLDDPGEDLTPLFDTILEHVPAPEVDPDGPLQMLVTNLDYSDYVGRIAIGRIFRGTIKKGQQVALI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 245 NAEGKKRNGKVGTVLGYLGLERHEVEQANAGDIIAITGLGELKISDTICDVNNVEAMEPLSVDEPTVTMTFQVNTSPFAG 324
Cdd:COG1217 242 KRDGKVEKGKITKLFGFEGLERVEVEEAEAGDIVAIAGIEDINIGDTICDPENPEALPPIKIDEPTLSMTFSVNDSPFAG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 325 KEGKFVTSRNILERLEKELVHNVALRVEETESPDRFRVSGRGELHLSILIENMRREGFELAVSRPEVIIKEEDGQKMEPF 404
Cdd:COG1217 322 REGKFVTSRQIRERLEKELETNVALRVEETDSPDAFKVSGRGELHLSILIETMRREGYELQVSRPEVIFKEIDGKKLEPI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 405 ETVTIDVVEEHQGAIMESIGLRKGELTDMAPDGKGRVRMDFMMPSRGLIGFQTEFLTMTSGSGLIYHSFDHYGPYKGGiI 484
Cdd:COG1217 402 EELTIDVPEEYSGAVIEKLGQRKGEMTNMEPDGGGRVRLEFLIPSRGLIGFRTEFLTDTRGTGIMNHVFDGYEPYKGE-I 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 485 GQRNNGVLISNATGKALTYALFFLQARGRLFTEHADEVYEGQVIGIHNRSNDLTVNCLKGKQLTNVRASGTDEAQVLSPP 564
Cdd:COG1217 481 PGRRNGSLISMETGKATAYALFNLQERGTLFIGPGTEVYEGMIVGEHSRDNDLVVNVCKEKKLTNMRASGSDEAIRLTPP 560
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1376772070 565 IKHTLEQALEFIDEDELVEVTPLNVRIRKKLLTENDRKRAARPAKA 610
Cdd:COG1217 561 RKMSLEQALEFIEDDELVEVTPKSIRLRKKILDENERKRAAKKKKK 606
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
9-603 |
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: 1047.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 9 LRNIAIIAHVDHGKTTLVDKLLQQSGTLESRGEAEERVMDSNDIEKERGITILAKNTAIDWNDYRINIVDTPGHADFGGE 88
Cdd:TIGR01394 1 IRNIAIIAHVDHGKTTLVDALLKQSGTFRANEAVAERVMDSNDLERERGITILAKNTAIRYNGTKINIVDTPGHADFGGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 89 VERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDRPGARPDWVMDQVFDLFDNLGATDEQLDFTVVY 168
Cdd:TIGR01394 81 VERVLGMVDGVLLLVDASEGPMPQTRFVLKKALELGLKPIVVINKIDRPSARPDEVVDEVFDLFAELGADDEQLDFPIVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 169 ASALNGWATMEEGEVGTDMEPLFQAVVDTVEAPAVDLEGPLQMQISQLDYSSYVGVIGVARVTRGSVKPNQQVTIVNAEG 248
Cdd:TIGR01394 161 ASGRAGWASLDLDDPSDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVHRGTVKKGQQVALMKRDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 249 KKRNGKVGTVLGYLGLERHEVEQANAGDIIAITGLGELKISDTICDVNNVEAMEPLSVDEPTVTMTFQVNTSPFAGKEGK 328
Cdd:TIGR01394 241 TIENGRISKLLGFEGLERVEIDEAGAGDIVAVAGLEDINIGETIADPEVPEALPTITVDEPTLSMTFSVNDSPLAGKEGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 329 FVTSRNILERLEKELVHNVALRVEETESPDRFRVSGRGELHLSILIENMRREGFELAVSRPEVIIKEEDGQKMEPFETVT 408
Cdd:TIGR01394 321 KVTSRHIRDRLMRELETNVALRVEDTESADKFEVSGRGELHLSILIETMRREGFELQVGRPQVIYKEIDGKKLEPIEELT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 409 IDVVEEHQGAIMESIGLRKGELTDMAPDGKGRVRMDFMMPSRGLIGFQTEFLTMTSGSGLIYHSFDHYGPYKGGiIGQRN 488
Cdd:TIGR01394 401 IDVPEEHVGAVIEKLGKRKGEMVDMEPSGNGRTRLEFKIPSRGLIGFRTEFLTDTRGTGIMNHVFDEYEPWKGE-IETRR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 489 NGVLISNATGKALTYALFFLQARGRLFTEHADEVYEGQVIGIHNRSNDLTVNCLKGKQLTNVRASGTDEAQVLSPPIKHT 568
Cdd:TIGR01394 480 NGSLVSMEDGTATAYALWNLQERGVMFVSPGTEVYEGMIIGEHSRENDLDVNPCKAKKLTNVRSSGKDEAVKLTPPRKLS 559
|
570 580 590
....*....|....*....|....*....|....*
gi 1376772070 569 LEQALEFIDEDELVEVTPLNVRIRKKLLTENDRKR 603
Cdd:TIGR01394 560 LEQALEYIEDDELVEVTPKSIRLRKRVLDPNERKR 594
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
6-609 |
0e+00 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 946.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 6 IDKLRNIAIIAHVDHGKTTLVDKLLQQSGTLESRGEAEERVMDSNDIEKERGITILAKNTAIDWNDYRINIVDTPGHADF 85
Cdd:PRK10218 2 IEKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 86 GGEVERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDRPGARPDWVMDQVFDLFDNLGATDEQLDFT 165
Cdd:PRK10218 82 GGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDFP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 166 VVYASALNGWATMEEGEVGTDMEPLFQAVVDTVEAPAVDLEGPLQMQISQLDYSSYVGVIGVARVTRGSVKPNQQVTIVN 245
Cdd:PRK10218 162 IVYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIID 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 246 AEGKKRNGKVGTVLGYLGLERHEVEQANAGDIIAITGLGELKISDTICDVNNVEAMEPLSVDEPTVTMTFQVNTSPFAGK 325
Cdd:PRK10218 242 SEGKTRNAKVGKVLGHLGLERIETDLAEAGDIVAITGLGELNISDTVCDTQNVEALPALSVDEPTVSMFFCVNTSPFCGK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 326 EGKFVTSRNILERLEKELVHNVALRVEETESPDRFRVSGRGELHLSILIENMRREGFELAVSRPEVIIKEEDGQKMEPFE 405
Cdd:PRK10218 322 EGKFVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRREGFELAVSRPKVIFREIDGRKQEPYE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 406 TVTIDVVEEHQGAIMESIGLRKGELTDMAPDGKGRVRMDFMMPSRGLIGFQTEFLTMTSGSGLIYHSFDHYGPYKGGIIG 485
Cdd:PRK10218 402 NVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDVRPGEVG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 486 QRNNGVLISNATGKALTYALFFLQARGRLFTEHADEVYEGQVIGIHNRSNDLTVNCLKGKQLTNVRASGTDEAQVLSPPI 565
Cdd:PRK10218 482 QRQNGVLISNGQGKAVAFALFGLQDRGKLFLGHGAEVYEGQIIGIHSRSNDLTVNCLTGKKLTNMRASGTDEAVVLVPPI 561
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1376772070 566 KHTLEQALEFIDEDELVEVTPLNVRIRKKLLTENDRKRAARPAK 609
Cdd:PRK10218 562 RMTLEQALEFIDDDELVEVTPTSIRIRKRHLTENDRRRANRAPK 605
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
8-201 |
1.18e-126 |
|
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: 370.77 E-value: 1.18e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 8 KLRNIAIIAHVDHGKTTLVDKLLQQSGTLESRGEAEERVMDSNDIEKERGITILAKNTAIDWNDYRINIVDTPGHADFGG 87
Cdd:cd01891 1 KIRNIAIIAHVDHGKTTLVDALLKQSGTFRENEEVGERVMDSNDLERERGITILAKNTAITYKDTKINIIDTPGHADFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 88 EVERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDRPGARPDWVMDQVFDLFDNLGATDEQLDFTVV 167
Cdd:cd01891 81 EVERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDRPDARPEEVVDEVFDLFLELNATDEQLDFPIV 160
|
170 180 190
....*....|....*....|....*....|....
gi 1376772070 168 YASALNGWATMEEGEVGTDMEPLFQAVVDTVEAP 201
Cdd:cd01891 161 YASAKNGWASLNLDDPSEDLDPLFETIIEHVPAP 194
|
|
| lepA |
TIGR01393 |
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a ... |
7-475 |
7.51e-74 |
|
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: 247.62 E-value: 7.51e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 7 DKLRNIAIIAHVDHGKTTLVDKLLQQSGTLESRgEAEERVMDSNDIEKERGITILAKNTAIDW-----NDYRINIVDTPG 81
Cdd:TIGR01393 1 KNIRNFSIIAHIDHGKSTLADRLLEYTGAISER-EMREQVLDSMDLERERGITIKAQAVRLNYkakdgETYVLNLIDTPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 82 HADFGGEVERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDRPGARPDWVMDQVFDLfdnLGATDEQ 161
Cdd:TIGR01393 80 HVDFSYEVSRSLAACEGALLLVDAAQGIEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKKEIEEV---IGLDASE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 162 ldftVVYASAlngwatmeegEVGTDMEPLFQAVVDTVEAPAVDLEGPLQMQISQLDYSSYVGVIGVARVTRGSVKPNQQV 241
Cdd:TIGR01393 157 ----AILASA----------KTGIGIEEILEAIVKRVPPPKGDPDAPLKALIFDSHYDNYRGVVALVRVFEGTIKPGDKI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 242 TIVNaegkkrNGKVGTV--LGYLGLERHEVEQANAGD----IIAITGLGELKISDTICDVNNvEAMEPLSVDEPTVTMTF 315
Cdd:TIGR01393 223 RFMS------TGKEYEVdeVGVFTPKLTKTDELSAGEvgyiIAGIKDVSDVRVGDTITHVKN-PAKEPLPGFKEVKPMVF 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 316 qvnTSPFAGKEGKFVTSRNILERLEkelVHNVALRVEETESPDR---FRVSGRGELHLSILIENMRREgFELAV--SRPE 390
Cdd:TIGR01393 296 ---AGLYPIDTEDYEDLRDALEKLK---LNDASLTYEPESSPALgfgFRCGFLGLLHMEIIQERLERE-FNLDLitTAPS 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 391 VI--IKEEDGQKM------------------EPFETVTIDVVEEHQGAIMESIGLRKGELTDMAPDGKGRVRMDFMMP-S 449
Cdd:TIGR01393 369 VIyrVYLTNGEVIevdnpsdlpdpgkiehveEPYVKATIITPTEYLGPIMTLCQEKRGVQTNMEYLDPNRVELIYEMPlA 448
|
490 500
....*....|....*....|....*.
gi 1376772070 450 RGLIGFQTEFLTMTSGsgliYHSFDH 475
Cdd:TIGR01393 449 EIVYDFFDKLKSISRG----YASFDY 470
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
7-200 |
1.72e-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: 225.48 E-value: 1.72e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 7 DKLRNIAIIAHVDHGKTTLVDKLLQQSGTLESRGE---AEERVMDSNDIEKERGITILAKNTAIDWNDYRINIVDTPGHA 83
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEvkgEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 84 DFGGEVERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDRP-GARPDWVMDQVFDLFDNLGATDEqL 162
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVdGAELEEVVEEVSRELLEKYGEDG-E 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1376772070 163 DFTVVYASALNGWAtmeegevgtdMEPLFQAVVDTVEA 200
Cdd:pfam00009 160 FVPVVPGSALKGEG----------VQTLLDALDEYLPS 187
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
7-448 |
1.48e-66 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 227.98 E-value: 1.48e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 7 DKLRNIAIIAHVDHGKTTLVDKLLQQSGTLESRgEAEERVMDSNDIEKERGITILAKN-----TAIDWNDYRINIVDTPG 81
Cdd:COG0481 4 KNIRNFSIIAHIDHGKSTLADRLLELTGTLSER-EMKEQVLDSMDLERERGITIKAQAvrlnyKAKDGETYQLNLIDTPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 82 HADFGGEVERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDRPGARPDWVMDQVFDLFdNLGATDeq 161
Cdd:COG0481 83 HVDFSYEVSRSLAACEGALLVVDASQGVEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKQEIEDII-GIDASD-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 162 ldftVVYASALNGwatmeEGevgtdMEPLFQAVVDTVEAPAVDLEGPLQMQIsqLD--YSSYVGVIGVARVTRGSVKPNQ 239
Cdd:COG0481 160 ----AILVSAKTG-----IG-----IEEILEAIVERIPPPKGDPDAPLQALI--FDswYDSYRGVVVYVRVFDGTLKKGD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 240 QVTIVNaegkkrNGKVGTV--LGYLGLERHEVEQANAGD---IIA-ITGLGELKISDTICDVNNvEAMEPLSVDEPTVTM 313
Cdd:COG0481 224 KIKMMS------TGKEYEVdeVGVFTPKMTPVDELSAGEvgyIIAgIKDVRDARVGDTITLAKN-PAAEPLPGFKEVKPM 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 314 TFQ----VNTSpfagkegKFVTSRNILERLekELvhNVALRVEETESPDR----FRVSGRGELHLSILIENMRRE-GFEL 384
Cdd:COG0481 297 VFAglypVDSD-------DYEDLRDALEKL--QL--NDASLTYEPETSAAlgfgFRCGFLGLLHMEIIQERLEREfDLDL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 385 AVSRPEVI--IKEEDGQKM------------------EPFETVTIDVVEEHQGAIMESIGLRKGELTDMAPDGKGRVRMD 444
Cdd:COG0481 366 ITTAPSVVyeVTLTDGEVIevdnpsdlpdpgkieeieEPIVKATIITPSEYVGAVMELCQEKRGVQKNMEYLGENRVELT 445
|
....
gi 1376772070 445 FMMP 448
Cdd:COG0481 446 YELP 449
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
5-465 |
2.35e-66 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 230.52 E-value: 2.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 5 QIDKLRNIAIIAHVDHGKTTLVDKLLQQSGTLESRGEAEERVMDSNDIEKERGITILAKNTAI----DWNDYRINIVDTP 80
Cdd:PRK07560 16 NPEQIRNIGIIAHIDHGKTTLSDNLLAGAGMISEELAGEQLALDFDEEEQARGITIKAANVSMvheyEGKEYLINLIDTP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 81 GHADFGGEVERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDR--------P---GARPDWVMDQVF 149
Cdd:PRK07560 96 GHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKPVLFINKVDRlikelkltPqemQQRLLKIIKDVN 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 150 DLFDNLgATDE-----QLDF---TVVYASALNGWA----TMEEGEVG----------TDME------PLFQAVVDTV--- 198
Cdd:PRK07560 176 KLIKGM-APEEfkekwKVDVedgTVAFGSALYNWAisvpMMQKTGIKfkdiidyyekGKQKelaekaPLHEVVLDMVvkh 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 199 -----EAP---------------------AVDLEGPLQMQISQLDYSSYVGVIGVARVTRGSVKPNQQVTIVNAEGKKRN 252
Cdd:PRK07560 255 lpnpiEAQkyripkiwkgdlnsevgkamlNCDPNGPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLVGAKKKNRV 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 253 GKVGTvlgYLGLERHEVEQANAGDIIAITGLGELKISDTICDVNNVEAMEPLS-VDEPTVTMTFQ-VNTSPFAgkegKFV 330
Cdd:PRK07560 335 QQVGI---YMGPEREEVEEIPAGNIAAVTGLKDARAGETVVSVEDMTPFESLKhISEPVVTVAIEaKNPKDLP----KLI 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 331 tsrNILERLEKElvhNVALRVEETESPDRFRVSGRGELHLSILIENMRRE-GFELAVSRPEVIIKEEDGQKMEPFET--- 406
Cdd:PRK07560 408 ---EVLRQLAKE---DPTLVVKINEETGEHLLSGMGELHLEVITYRIKRDyGIEVVTSEPIVVYRETVRGKSQVVEGksp 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1376772070 407 -------VTIDVVEEHqgaIMESIglRKGELTDMAPDGKGRVRMDFMMP-------SRGLIGFQTE--FLTMTSG 465
Cdd:PRK07560 482 nkhnrfyISVEPLEEE---VIEAI--KEGEISEDMDKKEAKILREKLIEagmdkdeAKRVWAIYNGnvFIDMTKG 551
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
5-442 |
1.98e-63 |
|
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: 222.08 E-value: 1.98e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 5 QIDKLRNIAIIAHVDHGKTTLVDKLLQQSGTLESRGEAEERVMDSNDIEKERGITILAKNTAI----DWNDYRINIVDTP 80
Cdd:TIGR00490 15 KPKFIRNIGIVAHIDHGKTTLSDNLLAGAGMISEELAGQQLYLDFDEQEQERGITINAANVSMvheyEGNEYLINLIDTP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 81 GHADFGGEVERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDR-----------PGARPDWVMDQVF 149
Cdd:TIGR00490 95 GHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKPVLFINKVDRlinelkltpqeLQERFIKIITEVN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 150 DLFDNLGA---TDEQL----DFTVVYASALNGWA----TMEEGEVG----------------TDMEPLFQAVVDTV---- 198
Cdd:TIGR00490 175 KLIKAMAPeefRDKWKvrveDGSVAFGSAYYNWAisvpSMKKTGIGfkdiykyckedkqkelAKKSPLHQVVLDMVirhl 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 199 ----EAPA---------------------VDLEGPLQMQISQLDYSSYVGVIGVARVTRGSVKPNQQVTIVNAEGKKRNG 253
Cdd:TIGR00490 255 pspiEAQKyripviwkgdlnsevgkamlnCDPKGPLALMITKIVVDKHAGEVAVGRLYSGTIRPGMEVYIVDRKAKARIQ 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 254 KVGTvlgYLGLERHEVEQANAGDIIAITGLGELKISDTICD-VNNVEAMEPLS-VDEPTVTMTFQV-NTSPFAgkegKFV 330
Cdd:TIGR00490 335 QVGV---YMGPERVEVDEIPAGNIVAVIGLKDAVAGETICTtVENITPFESIKhISEPVVTVAIEAkNTKDLP----KLI 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 331 tsrNILERLEKElvhNVALRVEETESPDRFRVSGRGELHLSILIENMRRE-GFELAVSRPEVIIKEEDGQKMEPFETVTI 409
Cdd:TIGR00490 408 ---EVLRQVAKE---DPTVHVEINEETGEHLISGMGELHLEIIVEKIREDyGLDVETSPPIVVYRETVTGTSPVVEGKSP 481
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1376772070 410 D-------VVEEHQGAIMESIglRKGELTDMAPDGKGRVR 442
Cdd:TIGR00490 482 NkhnrfyiVVEPLEESVIQAF--KEGKIVDMKMKKKERRR 519
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
2-395 |
1.07e-58 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 208.65 E-value: 1.07e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 2 STPQIDKLRNIAIIAHVDHGKTTLVDKLLQQSGTLESRGEAEE--RVMDSNDIEKERGITILAKNTAIDWNDYRINIVDT 79
Cdd:PRK13351 1 AEMPLMQIRNIGILAHIDAGKTTLTERILFYTGKIHKMGEVEDgtTVTDWMPQEQERGITIESAATSCDWDNHRINLIDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 80 PGHADFGGEVERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDRPGARPDWVMDQ------------ 147
Cdd:PRK13351 81 PGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLFKVLEDieerfgkrplpl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 148 ------------VFDLFDN--LGATDEQLDFTVVYAS------------------ALNGW--ATME---EGEVGTD---- 186
Cdd:PRK13351 161 qlpigsedgfegVVDLITEpeLHFSEGDGGSTVEEGPipeelleeveeareklieALAEFddELLElylEGEELSAeqlr 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 187 -------------------------MEPLFQAVVDT----VEAPAV--------------DLEGPLQMQISQLDYSSYVG 223
Cdd:PRK13351 241 aplregtrsghlvpvlfgsalknigIEPLLDAVVDYlpspLEVPPPrgskdngkpvkvdpDPEKPLLALVFKVQYDPYAG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 224 VIGVARVTRGSVKPNQQvtIVNAEGKKRnGKVGTVLGYLGLERHEVEQANAGDIIAITGLGELKISDTICDVNNVEAMEP 303
Cdd:PRK13351 321 KLTYLRVYSGTLRAGSQ--LYNGTGGKR-EKVGRLFRLQGNKREEVDRAKAGDIVAVAGLKELETGDTLHDSADPVLLEL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 304 LSVDEPtvtmTFQVNTSPF-AGKEGKFvtsRNILERLEKElvhNVALRVEETESPDRFRVSGRGELHLSILIENMRRE-G 381
Cdd:PRK13351 398 LTFPEP----VVSLAVEPErRGDEQKL---AEALEKLVWE---DPSLRVEEDEETGQTILSGMGELHLEVALERLRREfK 467
|
490
....*....|....
gi 1376772070 382 FELAVSRPEVIIKE 395
Cdd:PRK13351 468 LEVNTGKPQVAYRE 481
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
1-391 |
4.73e-57 |
|
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: 204.12 E-value: 4.73e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 1 MSTPQIDKLRNIAIIAHVDHGKTTLVDKLLQQSGTLESRGEAEE--RVMDSNDIEKERGITILAKNTAIDWNDYRINIVD 78
Cdd:COG0480 1 MAEYPLEKIRNIGIVAHIDAGKTTLTERILFYTGAIHRIGEVHDgnTVMDWMPEEQERGITITSAATTCEWKGHKINIID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 79 TPGHADFGGEVERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDRPGARPDWVMDQ----------- 147
Cdd:COG0480 81 TPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQlkerlganpvp 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 148 -------------VFDLF--------DNLGATDEQLDFTVVYASALNGW-ATM----------------EEGEVGTDM-- 187
Cdd:COG0480 161 lqlpigaeddfkgVIDLVtmkayvydDELGAKYEEEEIPAELKEEAEEArEELieavaetddelmekylEGEELTEEEik 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 188 --------------------------EPLFQAVVD----TVEAPAVDLEGPLQMQISQLDYSS---------------YV 222
Cdd:COG0480 241 aglrkatlagkivpvlcgsafknkgvQPLLDAVVDylpsPLDVPAIKGVDPDTGEEVERKPDDdepfsalvfktmtdpFV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 223 GVIGVARVTRGSVKPNQqvTIVNAeGKKRNGKVGTVLGYLGLERHEVEQANAGDIIAITGLGELKISDTICDVNNVEAME 302
Cdd:COG0480 321 GKLSFFRVYSGTLKSGS--TVYNS-TKGKKERIGRLLRMHGNKREEVDEAGAGDIVAVVKLKDTTTGDTLCDEDHPIVLE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 303 PLSVDEPTVTMTFQVNTSpfaGKEGKFVTSrniLERLEKElvhNVALRVE------ETespdrfRVSGRGELHLSILIEN 376
Cdd:COG0480 398 PIEFPEPVISVAIEPKTK---ADEDKLSTA---LAKLAEE---DPTFRVEtdeetgQT------IISGMGELHLEIIVDR 462
|
490
....*....|....*.
gi 1376772070 377 MRRE-GFELAVSRPEV 391
Cdd:COG0480 463 LKREfGVEVNVGKPQV 478
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
11-189 |
1.42e-56 |
|
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: 188.66 E-value: 1.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 11 NIAIIAHVDHGKTTLVDKLLQQSGTLESRGEAEERVMDSNDIEKERGITILAKNTAIDWNDYRINIVDTPGHADFGGEVE 90
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 91 RIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDRPG-ARPDWVMDQVFDLFDNLGAT-DEQLDFTVVY 168
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGeEDFDEVLREIKELLKLIGFTfLKGKDVPIIP 160
|
170 180
....*....|....*....|.
gi 1376772070 169 ASALNGWATMEEGEVGTDMEP 189
Cdd:cd00881 161 ISALTGEGIEELLDAIVEHLP 181
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
15-478 |
4.38e-50 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 184.17 E-value: 4.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 15 IAHVDHGKTTLVDKLLQQSGTLESRGEAEE--RVMDSNDIEKERGITILAKNTAIDWNDYRINIVDTPGHADFGGEVERI 92
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRIGEVEDgtTTMDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVERA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 93 MSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDRPGARPDWVMDQ------------------------V 148
Cdd:PRK12740 81 LRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRAGADFFRVLAQlqeklgapvvplqlpigegddftgV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 149 FDL-------FDNlGATDEQLDFTVVYASALNGW-----------------ATMEEGEVGTD------------------ 186
Cdd:PRK12740 161 VDLlsmkayrYDE-GGPSEEIEIPAELLDRAEEAreellealaefddelmeKYLEGEELSEEeikaglrkatlageivpv 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 187 ----------MEPLFQAVVDtvEAP-------------------AVDLEGPLQMQISQLDYSSYVGVIGVARVTRGSVKP 237
Cdd:PRK12740 240 fcgsalknkgVQRLLDAVVD--YLPsplevppvdgedgeegaelAPDPDGPLVALVFKTMDDPFVGKLSLVRVYSGTLKK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 238 NQQVTIVNAEGKKRngkVGTVLGYLGLERHEVEQANAGDIIAITGLGELKISDTICDVNNVEAMEPLSVDEPTVTMTfqv 317
Cdd:PRK12740 318 GDTLYNSGTGKKER---VGRLYRMHGKQREEVDEAVAGDIVAVAKLKDAATGDTLCDKGDPILLEPMEFPEPVISLA--- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 318 ntspfagkegkfVTSRN---------ILERLEKElvhNVALRVEETESPDRFRVSGRGELHLSILIENMRRE-GFELAVS 387
Cdd:PRK12740 392 ------------IEPKDkgdeeklseALGKLAEE---DPTLRVERDEETGQTILSGMGELHLDVALERLKREyGVEVETG 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 388 RPEVIIKE------------------------------------------------------------------------ 395
Cdd:PRK12740 457 PPQVPYREtirkkaeghgrhkkqsgghgqfgdvwleveplprgegfefvdkvvggavprqyipavekgvrealekgvlag 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 396 ----------EDGQK-----------------------------MEPFETVTIDVVEEHQGAIMESIGLRKGELTDMAPD 436
Cdd:PRK12740 537 ypvvdvkvtlTDGSYhsvdssemafkiaarlafrealpkakpvlLEPIMKVEVSVPEEFVGDVIGDLSSRRGRILGMESR 616
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1376772070 437 GKG-RVRMdfMMPSRGLIGFQTEFLTMTSGSGLIYHSFDHYGP 478
Cdd:PRK12740 617 GGGdVVRA--EVPLAEMFGYATDLRSLTQGRGSFSMEFSHYEE 657
|
|
| BipA_III |
cd16263 |
Domain III of GTP-binding protein BipA (TypA); BipA (also called TypA) is a highly conserved ... |
309-387 |
5.63e-49 |
|
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: 164.79 E-value: 5.63e-49
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1376772070 309 PTVTMTFQVNTSPFAGKEGKFVTSRNILERLEKELVHNVALRVEETESPDRFRVSGRGELHLSILIENMRREGFELAVS 387
Cdd:cd16263 1 PTVSMTFGVNTSPFAGREGKFVTSRKIRDRLEKELETNVALRVEETESPDSFIVSGRGELHLSILIETMRREGFELQVS 79
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
10-201 |
5.57e-48 |
|
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: 165.78 E-value: 5.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 10 RNIAIIAHVDHGKTTLVDKLLQQSGTLESRgEAEERVMDSNDIEKERGITILAKN-----TAIDWNDYRINIVDTPGHAD 84
Cdd:cd01890 1 RNFSIIAHIDHGKSTLADRLLELTGTVSER-EMKEQVLDSMDLERERGITIKAQAvrlfyKAKDGEEYLLNLIDTPGHVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 85 FGGEVERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDRPGARPDWVMDQVFDLFDnLGATDeqldf 164
Cdd:cd01890 80 FSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVKQEIEDVLG-LDASE----- 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 1376772070 165 tVVYASAlngwatmeegEVGTDMEPLFQAVVDTVEAP 201
Cdd:cd01890 154 -AILVSA----------KTGLGVEDLLEAIVERIPPP 179
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
10-136 |
1.23e-47 |
|
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: 166.25 E-value: 1.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 10 RNIAIIAHVDHGKTTLVDKLLQQSGTLESRGEAEERVMDSNDIEKERGITIlaKNTAI-----------DWNDYRINIVD 78
Cdd:cd01885 1 RNICIIAHVDHGKTTLSDSLLASAGIISEKLAGKARYLDTREDEQERGITI--KSSAIslyfeyeeekmDGNDYLINLID 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1376772070 79 TPGHADFGGEVERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDR 136
Cdd:cd01885 79 SPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDR 136
|
|
| BipA_TypA_C |
cd03710 |
BipA_TypA_C: a C-terminal portion of BipA or TypA having homology to the C terminal domains of ... |
402-480 |
5.13e-42 |
|
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: 146.11 E-value: 5.13e-42
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1376772070 402 EPFETVTIDVVEEHQGAIMESIGLRKGELTDMAPDGKGRVRMDFMMPSRGLIGFQTEFLTMTSGSGLIYHSFDHYGPYK 480
Cdd:cd03710 1 EPIEELTIDVPEEYSGAVIEKLGKRKGEMVDMEPDGNGRTRLEFKIPSRGLIGFRSEFLTDTRGTGIMNHVFDGYEPYK 79
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
11-154 |
1.17e-40 |
|
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: 147.77 E-value: 1.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 11 NIAIIAHVDHGKTTLVDKLLQQSGTLESRGeaeeRV------MDSNDIEKERGITILAKNTAIDWNDYRINIVDTPGHAD 84
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIRELG----SVdkgttrTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMD 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 85 FGGEVERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDRPGARPDWVMDQVFDLFDN 154
Cdd:cd04168 77 FIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTIIFVNKIDRAGADLEKVYQEIKEKLSP 146
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
11-148 |
1.99e-38 |
|
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: 142.63 E-value: 1.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 11 NIAIIAHVDHGKTTLVDKLLQQSGTLESRGEAEER--VMDSNDIEKERGITILAKNTAIDWNDYRINIVDTPGHADFGGE 88
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGRIHKIGEVHGGgaTMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDFTIE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 89 VERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDRPGARPDWVMDQV 148
Cdd:cd01886 81 VERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQI 140
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
209-301 |
3.70e-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: 127.69 E-value: 3.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 209 LQMQISQLDYSSYVGVIGVARVTRGSVKPNQQVTIVNAEGKKRNGKVGTVLGYLGLERHEVEQANAGDIIAITGLGELKI 288
Cdd:cd03691 1 FQMLVTTLDYDDYLGRIAIGRIFSGTVKVGQQVTVVDEDGKIEKGRVTKLFGFEGLERVEVEEAEAGDIVAIAGLEDITI 80
|
90
....*....|...
gi 1376772070 289 SDTICDVNNVEAM 301
Cdd:cd03691 81 GDTICDPEVPEPL 93
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
7-136 |
2.15e-32 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 133.25 E-value: 2.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 7 DKLRNIAIIAHVDHGKTTLVDKLLQQSGTLESRGEAEERVMDSNDIEKERGITIlaKNTAI------------DWNDYRI 74
Cdd:PTZ00416 17 DQIRNMSVIAHVDHGKSTLTDSLVCKAGIISSKNAGDARFTDTRADEQERGITI--KSTGIslyyehdledgdDKQPFLI 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1376772070 75 NIVDTPGHADFGGEVERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDR 136
Cdd:PTZ00416 95 NLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKVDR 156
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
10-148 |
2.49e-32 |
|
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: 125.79 E-value: 2.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 10 RNIAIIAHVDHGKTTLVDKLL------QQSGTLESRGEAEERVMDSNDIEKERGITILAKNTAIDWNDYRINIVDTPGHA 83
Cdd:cd04169 3 RTFAIISHPDAGKTTLTEKLLlfggaiQEAGAVKARKSRKHATSDWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHE 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1376772070 84 DFGGEVERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDRPGARPDWVMDQV 148
Cdd:cd04169 83 DFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDREGRDPLELLDEI 147
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
5-136 |
2.38e-30 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 127.15 E-value: 2.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 5 QIDK---LRNIAIIAHVDHGKTTLVDKLLQQSGTLESRGEAEERVMDSNDIEKERGITIlaKNTAI-------------- 67
Cdd:PLN00116 12 IMDKkhnIRNMSVIAHVDHGKSTLTDSLVAAAGIIAQEVAGDVRMTDTRADEAERGITI--KSTGIslyyemtdeslkdf 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1376772070 68 ----DWNDYRINIVDTPGHADFGGEVERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDR 136
Cdd:PLN00116 90 kgerDGNEYLINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTETVLRQALGERIRPVLTVNKMDR 162
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
10-136 |
1.98e-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: 115.83 E-value: 1.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 10 RNIAIIAHVDHGKTTLVDKLLQQS---GTLESRGEAEERVMDSNDIEKERGITIlaKNTAI-----DWND--YRINIVDT 79
Cdd:cd04167 1 RNVCIAGHLHHGKTSLLDMLIEQThkrTPSVKLGWKPLRYTDTRKDEQERGISI--KSNPIslvleDSKGksYLINIIDT 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1376772070 80 PGHADFGGEVERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDR 136
Cdd:cd04167 79 PGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDR 135
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
11-278 |
2.49e-29 |
|
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444074 [Multi-domain] Cd Length: 423 Bit Score: 120.81 E-value: 2.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 11 NIAIIAHVDHGKTTLVDKLLQQSGTL------ESRGEAEER---------VMDSNDIEKERGITILAKNTAIDWNDYRIN 75
Cdd:COG5256 9 NLVVIGHVDHGKSTLVGRLLYETGAIdehiieKYEEEAEKKgkesfkfawVMDRLKEERERGVTIDLAHKKFETDKYYFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 76 IVDTPGHADFggeVERIM---SMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVV-INKIDRPG---ARPDWVMDQV 148
Cdd:COG5256 89 IIDAPGHRDF---VKNMItgaSQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVaVNKMDAVNyseKRYEEVKEEV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 149 FDLFDNLGATDEQLDFtvVYASALNGWATMEEGEvgtDM-----EPLFQAvVDTVEAPAVDLEGPLQMQIsQLDYS-SYV 222
Cdd:COG5256 166 SKLLKMVGYKVDKIPF--IPVSAWKGDNVVKKSD---NMpwyngPTLLEA-LDNLKEPEKPVDKPLRIPI-QDVYSiSGI 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1376772070 223 GVIGVARVTRGSVKPNQQVTIVNAegkkrnGKVGTVlgyLGLERH--EVEQANAGDII 278
Cdd:COG5256 239 GTVPVGRVETGVLKVGDKVVFMPA------GVVGEV---KSIEMHheELEQAEPGDNI 287
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
11-154 |
2.86e-28 |
|
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: 114.23 E-value: 2.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 11 NIAIIAHVDHGKTTLVDKLLQQSGTLESRGEAEE--RVMDSNDIEKERGITILAKNTAIDWNDYRINIVDTPGHADFGGE 88
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRLGRVEDgnTVSDYDPEEKKRKMSIETSVAPLEWNGHKINLIDTPGYADFVGE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1376772070 89 VERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDRPGARPDWVMDQVFDLFDN 154
Cdd:cd04170 81 TLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRARADFDKTLAALREAFGR 146
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
11-316 |
6.69e-28 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 116.56 E-value: 6.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 11 NIAIIAHVDHGKTTLVDKLLQQSGTL------ESRGEAEER---------VMDSNDIEKERGITILAKNTAIDWNDYRIN 75
Cdd:PRK12317 8 NLAVIGHVDHGKSTLVGRLLYETGAIdehiieELREEAKEKgkesfkfawVMDRLKEERERGVTIDLAHKKFETDKYYFT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 76 IVDTPGHADFggeVERIM---SMVDSVLLIVDAVD--GPMPQTRfvtQKAF-AHGL---KPIVVINKIDRPG---ARPDW 143
Cdd:PRK12317 88 IVDCPGHRDF---VKNMItgaSQADAAVLVVAADDagGVMPQTR---EHVFlARTLginQLIVAINKMDAVNydeKRYEE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 144 VMDQVFDLFDNLGATDEQLDFTVVyaSALNGWATMEEGEvgtDME----PLFQAVVDTVEAPAVDLEGPLQMQIsQLDYS 219
Cdd:PRK12317 162 VKEEVSKLLKMVGYKPDDIPFIPV--SAFEGDNVVKKSE---NMPwyngPTLLEALDNLKPPEKPTDKPLRIPI-QDVYS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 220 -SYVGVIGVARVTRGSVKPNQQVTIVNAegkkrnGKVGTVlgyLGLERH--EVEQANAGDII--AITGLG--ELKISDTI 292
Cdd:PRK12317 236 iSGVGTVPVGRVETGVLKVGDKVVFMPA------GVVGEV---KSIEMHheELPQAEPGDNIgfNVRGVGkkDIKRGDVC 306
|
330 340
....*....|....*....|....
gi 1376772070 293 CDVNNVeameplsvdePTVTMTFQ 316
Cdd:PRK12317 307 GHPDNP----------PTVAEEFT 320
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
5-148 |
1.28e-25 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 110.99 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 5 QIDKLRNIAIIAHVDHGKTTLVDKLL------QQSGTLESRGEAEERVMDSNDIEKERGITILAKNTAIDWNDYRINIVD 78
Cdd:PRK00741 6 EVAKRRTFAIISHPDAGKTTLTEKLLlfggaiQEAGTVKGRKSGRHATSDWMEMEKQRGISVTSSVMQFPYRDCLINLLD 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1376772070 79 TPGHADFGGEVERIMSMVDSVLLIVDAVDGPMPQTRfvtqKAF----AHGLkPIVV-INKIDRPGARPDWVMDQV 148
Cdd:PRK00741 86 TPGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTR----KLMevcrLRDT-PIFTfINKLDRDGREPLELLDEI 155
|
|
| EFG_C |
pfam00679 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
399-481 |
1.89e-24 |
|
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of Elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopt a ferredoxin-like fold.
Pssm-ID: 425814 [Multi-domain] Cd Length: 88 Bit Score: 97.23 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 399 QKMEPFETVTIDVVEEHQGAIMESIGLRKGELTDMAPDGKGRVRMDFMMPSRGLIGFQTEFLTMTSGSGLIYHSFDHYGP 478
Cdd:pfam00679 1 VLLEPIEKVTIDVPEEYVGDVISDLNSRRGEILDMDPDDGGRVVIEAEVPLAELFGFATELRSLTKGRGSFSMEFSGYQP 80
|
...
gi 1376772070 479 YKG 481
Cdd:pfam00679 81 VPG 83
|
|
| Elongation_Factor_C |
cd01514 |
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ... |
402-480 |
2.49e-23 |
|
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of elongation factors (EFs) bacterial EF-G, eukaryotic and archeal EF-2 and eukaryotic mitochondrial mtEFG1s and mtEFG2s. This group also includes proteins similar to the ribosomal protection proteins Tet(M) and Tet(O), BipA, LepA and, spliceosomal proteins: human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and yeast counterpart Snu114p. This domain adopts a ferredoxin-like fold consisting of an alpha-beta sandwich with anti-parallel beta-sheets, resembling the topology of domain III found in the elongation factors EF-G and eukaryotic EF-2, with which it forms the C-terminal block. The two domains however are not superimposable and domain III lacks some of the characteristics of this domain. EF-2/EF-G in complex with GTP, promotes the translocation step of translation. During translocation the peptidyl-tRNA is moved from the A site to the P site, the uncharged tRNA from the P site to the E-site and, the mRNA is shifted one codon relative to the ribosome. Tet(M) and Tet(O) mediate Tc resistance. Typical Tcs bind to the ribosome and inhibit the elongation phase of protein synthesis, by inhibiting the occupation of site A by aminoacyl-tRNA. Tet(M) and Tet(O) catalyze the release of tetracycline (Tc) from the ribosome in a GTP-dependent manner. BipA is a highly conserved protein with global regulatory properties in Escherichia coli. Yeast Snu114p is essential for cell viability and for splicing in vivo. Experiments suggest that GTP binding and probably GTP hydrolysis is important for the function of the U5-116 kD/Snu114p. The function of LepA proteins is unknown.
Pssm-ID: 238772 [Multi-domain] Cd Length: 79 Bit Score: 93.70 E-value: 2.49e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1376772070 402 EPFETVTIDVVEEHQGAIMESIGLRKGELTDMAPDGKGRVRMDFMMPSRGLIGFQTEFLTMTSGSGLIYHSFDHYGPYK 480
Cdd:cd01514 1 EPIMKVEITVPEEYLGAVIGDLSKRRGEILGMEPRGTGRVVIKAELPLAEMFGFATDLRSLTQGRASFSMEFSHYEPVP 79
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
11-276 |
4.34e-22 |
|
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: 98.70 E-value: 4.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 11 NIAIIAHVDHGKTTLVDKLlqqSGTLESRGEAEERVMDSNDI---EKERGITILAKNTAIDWNDYRINIVDTPGHADFGG 87
Cdd:TIGR00485 14 NVGTIGHVDHGKTTLTAAI---TTVLAKEGGAAARAYDQIDNapeEKARGITINTAHVEYETETRHYAHVDCPGHADYVK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 88 EVERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVV-INKIDRPGARP--DWVMDQVFDLFDNLGATDEqlDF 164
Cdd:TIGR00485 91 NMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKCDMVDDEEllELVEMEVRELLSQYDFPGD--DT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 165 TVVYASALNgwATMEEGEVGTDMEPLFQAVVDTVEAPAVDLEGPLQMQISQLDYSSYVGVIGVARVTRGSVKPNQQVTIV 244
Cdd:TIGR00485 169 PIIRGSALK--ALEGDAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIV 246
|
250 260 270
....*....|....*....|....*....|..
gi 1376772070 245 NAegkkRNGKVGTVLGyLGLERHEVEQANAGD 276
Cdd:TIGR00485 247 GL----KDTRKTTVTG-VEMFRKELDEGRAGD 273
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
11-280 |
3.07e-21 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 96.17 E-value: 3.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 11 NIAIIAHVDHGKTTL---VDKLLQQSGTLESRGEAEervMDSNDIEKERGITIlakNTA-IDWN-DYR-INIVDTPGHAD 84
Cdd:PRK12736 14 NIGTIGHVDHGKTTLtaaITKVLAERGLNQAKDYDS---IDAAPEEKERGITI---NTAhVEYEtEKRhYAHVDCPGHAD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 85 FggeverIMSMV------DSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVV-INKIDRPGARP--DWVMDQVFDLFDNL 155
Cdd:PRK12736 88 Y------VKNMItgaaqmDGAILVVAATDGPMPQTREHILLARQVGVPYLVVfLNKVDLVDDEEllELVEMEVRELLSEY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 156 GATDEqlDFTVVYASALngwATMEEGEVGTD-MEPLFQAVVDTVEAPAVDLEGPLQMQISQLDYSSYVGVIGVARVTRGS 234
Cdd:PRK12736 162 DFPGD--DIPVIRGSAL---KALEGDPKWEDaIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGT 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1376772070 235 VKPNQQVTIVNAegkkRNGKVGTVLGyLGLERHEVEQANAGDIIAI 280
Cdd:PRK12736 237 VKVGDEVEIVGI----KETQKTVVTG-VEMFRKLLDEGQAGDNVGV 277
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
11-174 |
1.79e-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: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 11 NIAIIAHVDHGKTTLVDKLLQQSGTLESR------GEAEER---------VMDSNDIEKERGITILAKNTAIDWNDYRIN 75
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRtiekyeKEAKEMgkesfkyawVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 76 IVDTPGHADFggeverIMSMV------DSVLLIVDAVDG-------PMPQTRFVTQKAFAHGLKP-IVVINKIDRPG--- 138
Cdd:cd01883 81 IIDAPGHRDF------VKNMItgasqaDVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQlIVAVNKMDDVTvnw 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 1376772070 139 --ARPDWVMDQVFDLFDNLGATDEQLDFTVVyaSALNG 174
Cdd:cd01883 155 sqERYDEIKKKVSPFLKKVGYNPKDVPFIPI--SGFTG 190
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
12-174 |
6.49e-20 |
|
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: 87.14 E-value: 6.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 12 IAIIAHVDHGKTTLVDKLlqqsgtlesRGeaeervmdSNDIEKE-RGIT--ILAKNTAIDWNDYRINIVDTPGHADFGGE 88
Cdd:cd01887 3 VTVMGHVDHGKTTLLDKI---------RK--------TNVAAGEaGGITqhIGAYQVPIDVKIPGITFIDTPGHEAFTNM 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 89 VERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDRP---GARPDWVMDQvfdlfdnLGATDEQL--- 162
Cdd:cd01887 66 RARGASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKPygtEADPERVKNE-------LSELGLVGeew 138
|
170
....*....|....
gi 1376772070 163 --DFTVVYASALNG 174
Cdd:cd01887 139 ggDVSIVPISAKTG 152
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
11-276 |
7.27e-19 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 89.50 E-value: 7.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 11 NIAIIAHVDHGKTTL---VDKLLQQSGTLESRGEAEervMDSNDIEKERGITILAKNTAIDWNDYRINIVDTPGHADFGG 87
Cdd:PLN03127 63 NVGTIGHVDHGKTTLtaaITKVLAEEGKAKAVAFDE---IDKAPEEKARGITIATAHVEYETAKRHYAHVDCPGHADYVK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 88 EVERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVV-INKIDrpgarpdwVMD--QVFDLFDNlgATDEQLDF 164
Cdd:PLN03127 140 NMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVfLNKVD--------VVDdeELLELVEM--ELRELLSF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 165 --------TVVYASALNGWATMEEgEVGTD-MEPLFQAVVDTVEAPAVDLEGPLQMQISQLDYSSYVGVIGVARVTRGSV 235
Cdd:PLN03127 210 ykfpgdeiPIIRGSALSALQGTND-EIGKNaILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTI 288
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1376772070 236 KPNQQVTIVnaeGKKRNGKVGTVLGYLGLERHEVEQANAGD 276
Cdd:PLN03127 289 KVGEEVEIV---GLRPGGPLKTTVTGVEMFKKILDQGQAGD 326
|
|
| tufA |
CHL00071 |
elongation factor Tu |
11-280 |
3.10e-18 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 87.32 E-value: 3.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 11 NIAIIAHVDHGKTTLVDKLlqqSGTLESRGEAEERVMDSNDI---EKERGITIlakNTAidWNDYRINI-----VDTPGH 82
Cdd:CHL00071 14 NIGTIGHVDHGKTTLTAAI---TMTLAAKGGAKAKKYDEIDSapeEKARGITI---NTA--HVEYETENrhyahVDCPGH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 83 ADFggeverIMSM------VDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVV-INKIDRpgarpdwVMD--------- 146
Cdd:CHL00071 86 ADY------VKNMitgaaqMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVfLNKEDQ-------VDDeellelvel 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 147 QVFDLFDNLG-ATDeqlDFTVVYASALNGW-ATMEEGEVGTDMEP-------LFQAVVDTVEAPAVDLEGPLQMQISQLD 217
Cdd:CHL00071 153 EVRELLSKYDfPGD---DIPIVSGSALLALeALTENPKIKRGENKwvdkiynLMDAVDSYIPTPERDTDKPFLMAIEDVF 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1376772070 218 YSSYVGVIGVARVTRGSVKPNQQVTIVNAegkkRNGKVGTVLGyLGLERHEVEQANAGDIIAI 280
Cdd:CHL00071 230 SITGRGTVATGRIERGTVKVGDTVEIVGL----RETKTTTVTG-LEMFQKTLDEGLAGDNVGI 287
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
11-280 |
1.72e-17 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 84.86 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 11 NIAIIAHVDHGKTTLVDKLlqqSGTLESRGEAEERVMDSNDI---EKERGITIlakNTA-----IDWNDYRinIVDTPGH 82
Cdd:PRK00049 14 NVGTIGHVDHGKTTLTAAI---TKVLAKKGGAEAKAYDQIDKapeEKARGITI---NTAhveyeTEKRHYA--HVDCPGH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 83 ADFggeverIMSMV------DSVLLIVDAVDGPMPQTRfvtqkafAH-------GLKPIVV-INKIDRpgarpdwVMD-- 146
Cdd:PRK00049 86 ADY------VKNMItgaaqmDGAILVVSAADGPMPQTR-------EHillarqvGVPYIVVfLNKCDM-------VDDee 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 147 -------QVFDLFDNLGATDEqlDFTVVYASALNGWATMEEGEVGTDMEPLFQAVVDTVEAPAVDLEGPLQMQISQLDYS 219
Cdd:PRK00049 146 llelvemEVRELLSKYDFPGD--DTPIIRGSALKALEGDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSI 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1376772070 220 SYVGVIGVARVTRGSVKPNQQVTIVnaeGKKRNGKVgTVlgyLGLE--RHEVEQANAGDIIAI 280
Cdd:PRK00049 224 SGRGTVVTGRVERGIIKVGEEVEIV---GIRDTQKT-TV---TGVEmfRKLLDEGQAGDNVGA 279
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
14-144 |
2.99e-17 |
|
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 442507 [Multi-domain] Cd Length: 630 Bit Score: 85.35 E-value: 2.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 14 IIA---HVDHGKTTLV--------DKLlqqsgtlesrgeaEErvmdsndiEKERGITI--------LAkntaidwNDYRI 74
Cdd:COG3276 2 IIGtagHIDHGKTTLVkaltgidtDRL-------------KE--------EKKRGITIdlgfaylpLP-------DGRRL 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 75 NIVDTPGHADFggeverIMSMV------DSVLLIVDAVDGPMPQTRfvtqkafAH-------GLKP-IVVINKIDRpgAR 140
Cdd:COG3276 54 GFVDVPGHEKF------IKNMLagaggiDLVLLVVAADEGVMPQTR-------EHlaildllGIKRgIVVLTKADL--VD 118
|
....
gi 1376772070 141 PDWV 144
Cdd:COG3276 119 EEWL 122
|
|
| EFG_III-like |
cd16257 |
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G ... |
309-387 |
3.74e-17 |
|
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: 76.23 E-value: 3.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 309 PTVTMTFQVNTspfagkegkFVTSRNILERLEKELVHNVALRVEETESPDRFRVSGRGELHLSILIENMRRE-GFELAVS 387
Cdd:cd16257 1 PVVFVTVEVKN---------PLDQEKLLEGLERLSEEDPALQVYREESTGEFILSGLGELHLEIIVARLEREyGVELVVS 71
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
10-157 |
4.79e-17 |
|
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]
Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 78.57 E-value: 4.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 10 RNIAIIAHVDHGKTTLVDKLLQQSGTLESRGEAEERvMDSNDIEKERGITilakntaidwndYRINIVDTPGHADF---- 85
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTR-NYVTTVIEEDGKT------------YKFNLLDTAGQEDYdair 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1376772070 86 ---GGEVERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAhGLKPIVVINKIDRPGARPDwvmDQVFDLFDNLGA 157
Cdd:TIGR00231 69 rlyYPQVERSLRVFDIVILVLDVEEILEKQTKEIIHHADS-GVPIILVGNKIDLKDADLK---THVASEFAKLNG 139
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
11-280 |
5.96e-17 |
|
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: 83.28 E-value: 5.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 11 NIAIIAHVDHGKTTLVDKLLQqsgTLESRGEAEERVMDSNDI---EKERGITIlakNTAidWNDYRINI-----VDTPGH 82
Cdd:COG0050 14 NIGTIGHVDHGKTTLTAAITK---VLAKKGGAKAKAYDQIDKapeEKERGITI---NTS--HVEYETEKrhyahVDCPGH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 83 ADFggeverIMSMV------DSVLLIVDAVDGPMPQTRfvtqkafAH-------GLKPIVV-INKIDRpGARP---DWVM 145
Cdd:COG0050 86 ADY------VKNMItgaaqmDGAILVVSATDGPMPQTR-------EHillarqvGVPYIVVfLNKCDM-VDDEellELVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 146 DQVFDLFDNLGATDEqlDFTVVYAS---ALNGwatmEEGEVGTD-MEPLFQAVVDTVEAPAVDLEGPLQMQISqlDYSSY 221
Cdd:COG0050 152 MEVRELLSKYGFPGD--DTPIIRGSalkALEG----DPDPEWEKkILELMDAVDSYIPEPERDTDKPFLMPVE--DVFSI 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1376772070 222 VGVIGVA--RVTRGSVKPNQQVTIVNAEGKKRngkvgTVLgyLGLE--RHEVEQANAGDIIAI 280
Cdd:COG0050 224 TGRGTVVtgRVERGIIKVGDEVEIVGIRDTQK-----TVV--TGVEmfRKLLDEGEAGDNVGL 279
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
11-280 |
1.82e-16 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 81.81 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 11 NIAIIAHVDHGKTTLVDKLlqqSGTLESRGEAEERVMDSNDI---EKERGITIlakNTAidWNDYRINI-----VDTPGH 82
Cdd:PRK12735 14 NVGTIGHVDHGKTTLTAAI---TKVLAKKGGGEAKAYDQIDNapeEKARGITI---NTS--HVEYETANrhyahVDCPGH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 83 ADFggeverIMSMV------DSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVV-INKIDRpgarpdwVMD--------- 146
Cdd:PRK12735 86 ADY------VKNMItgaaqmDGAILVVSAADGPMPQTREHILLARQVGVPYIVVfLNKCDM-------VDDeellelvem 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 147 QVFDLFDNLGATDEqlDFTVVYASALNGWATMEEGEVGTDMEPLFQAVVDTVEAPAVDLEGPLQMQISQLDYSSYVGVIG 226
Cdd:PRK12735 153 EVRELLSKYDFPGD--DTPIIRGSALKALEGDDDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVV 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1376772070 227 VARVTRGSVKPNQQVTIVnaeGKKRNGKVgTVlgyLGLE--RHEVEQANAGDIIAI 280
Cdd:PRK12735 231 TGRVERGIVKVGDEVEIV---GIKETQKT-TV---TGVEmfRKLLDEGQAGDNVGV 279
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
11-242 |
1.86e-16 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 82.10 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 11 NIAIIAHVDHGKTTLVDKLLQQSGTLESR------GEAEER---------VMDSNDIEKERGITILAKNTAIDWNDYRIN 75
Cdd:PTZ00141 9 NLVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfeKEAAEMgkgsfkyawVLDKLKAERERGITIDIALWKFETPKYYFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 76 IVDTPGHADFGGEVERIMSMVDSVLLIVDAVDGPMP-------QTRFVTQKAFAHGLKPIVV-INKIDRPG-----ARPD 142
Cdd:PTZ00141 89 IIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVcINKMDDKTvnysqERYD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 143 WVMDQVFDLFDNLGATDEQLDFTvvyasALNGWATMEEGEVGTDME----PLFQAVVDTVEAPAVDLEGPLQMQISQLDY 218
Cdd:PTZ00141 169 EIKKEVSAYLKKVGYNPEKVPFI-----PISGWQGDNMIEKSDNMPwykgPTLLEALDTLEPPKRPVDKPLRLPLQDVYK 243
|
250 260
....*....|....*....|....
gi 1376772070 219 SSYVGVIGVARVTRGSVKPNQQVT 242
Cdd:PTZ00141 244 IGGIGTVPVGRVETGILKPGMVVT 267
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
12-174 |
2.84e-16 |
|
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]
Pssm-ID: 273102 [Multi-domain] Cd Length: 587 Bit Score: 82.12 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 12 IAIIAHVDHGKTTLVDKLLQqsgTLESRGEAEervmdsndiekerGIT--ILAKNTAIDWNDYrINIVDTPGHADFGGEV 89
Cdd:TIGR00487 90 VTIMGHVDHGKTSLLDSIRK---TKVAQGEAG-------------GITqhIGAYHVENEDGKM-ITFLDTPGHEAFTSMR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 90 ERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDRPGARPDWVMDQVFDLfdNLGATDEQLDFTVVYA 169
Cdd:TIGR00487 153 ARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVPIIVAINKIDKPEANPDRVKQELSEY--GLVPEDWGGDTIFVPV 230
|
....*
gi 1376772070 170 SALNG 174
Cdd:TIGR00487 231 SALTG 235
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
11-135 |
5.77e-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: 76.47 E-value: 5.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 11 NIAIIAHVDHGKTTLVDKLlqqSGTLESRGEAEERVMDSNDI---EKERGITIlakNTAidwndyriNI----------- 76
Cdd:cd01884 4 NVGTIGHVDHGKTTLTAAI---TKVLAKKGGAKAKKYDEIDKapeEKARGITI---NTA--------HVeyetanrhyah 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1376772070 77 VDTPGHADFggeverIMSMV------DSVLLIVDAVDGPMPQTRfvtqkafAH-------GLKPIVV-INKID 135
Cdd:cd01884 70 VDCPGHADY------IKNMItgaaqmDGAILVVSATDGPMPQTR-------EHlllarqvGVPYIVVfLNKAD 129
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
12-147 |
9.66e-16 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 80.65 E-value: 9.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 12 IAIIAHVDHGKTTLVDKLLQqsgtlesrgeaeervmdSNDIEKERG-IT--ILAKNTAIDWNDYRINIV--DTPGHADFG 86
Cdd:CHL00189 247 VTILGHVDHGKTTLLDKIRK-----------------TQIAQKEAGgITqkIGAYEVEFEYKDENQKIVflDTPGHEAFS 309
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1376772070 87 GEVERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDRPGARPDWVMDQ 147
Cdd:CHL00189 310 SMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANTERIKQQ 370
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
11-136 |
1.60e-15 |
|
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]
Pssm-ID: 129567 [Multi-domain] Cd Length: 581 Bit Score: 79.92 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 11 NIAIIAHVDHGKTTLVDKLlqqsgtlesRGEAEERVMDsndiEKERGITILAKNTAIDWNDYRINIVDTPGHADFGGEVE 90
Cdd:TIGR00475 2 IIATAGHVDHGKTTLLKAL---------TGIAADRLPE----EKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNAI 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1376772070 91 RIMSMVDSVLLIVDAVDGPMPQTR----FVTQKAFAHGlkpIVVINKIDR 136
Cdd:TIGR00475 69 AGGGGIDAALLVVDADEGVMTQTGehlaVLDLLGIPHT---IVVITKADR 115
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
12-147 |
1.92e-15 |
|
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: 79.29 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 12 IAIIAHVDHGKTTLVDKLLQqsgtlesrgeaeervmdSNDIEKE-RGIT--ILAknTAIDWNDYRINIVDTPGHADF--- 85
Cdd:COG0532 7 VTVMGHVDHGKTSLLDAIRK-----------------TNVAAGEaGGITqhIGA--YQVETNGGKITFLDTPGHEAFtam 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1376772070 86 ---GGEVerimsmVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLkPIVV-INKIDRPGARPDWVMDQ 147
Cdd:COG0532 68 rarGAQV------TDIVILVVAADDGVMPQTIEAINHAKAAGV-PIIVaINKIDKPGANPDRVKQE 126
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
11-280 |
3.06e-15 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 78.50 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 11 NIAIIAHVDHGKTTLVDKLlqqSGTLESRGEAEERVMDSNDI---EKERGITILAKNTAIDWNDYRINIVDTPGHADFGG 87
Cdd:PLN03126 83 NIGTIGHVDHGKTTLTAAL---TMALASMGGSAPKKYDEIDAapeERARGITINTATVEYETENRHYAHVDCPGHADYVK 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 88 EVERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVV-INKIDRPGARP--DWVMDQVFDLFDNLGATDEqlDF 164
Cdd:PLN03126 160 NMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVfLNKQDQVDDEEllELVELEVRELLSSYEFPGD--DI 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 165 TVVYASALNGW-ATMEEGEV--GTD-----MEPLFQAVVDTVEAPAVDLEGPLQMQISQLDYSSYVGVIGVARVTRGSVK 236
Cdd:PLN03126 238 PIISGSALLALeALMENPNIkrGDNkwvdkIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVK 317
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1376772070 237 PNQQVTIVNAegkkRNGKVGTVLGyLGLERHEVEQANAGDIIAI 280
Cdd:PLN03126 318 VGETVDIVGL----RETRSTTVTG-VEMFQKILDEALAGDNVGL 356
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
11-242 |
1.29e-14 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 76.28 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 11 NIAIIAHVDHGKTTLVDKLLQQSGTLESR---------GEAEER------VMDSNDIEKERGITILAKNTAIDWNDYRIN 75
Cdd:PLN00043 9 NIVVIGHVDSGKSTTTGHLIYKLGGIDKRvierfekeaAEMNKRsfkyawVLDKLKAERERGITIDIALWKFETTKYYCT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 76 IVDTPGHADFGGEVERIMSMVDSVLLIVDAVDGPMP-------QTRFVTQKAFAHGLKPIV-VINKIDR-----PGARPD 142
Cdd:PLN00043 89 VIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMIcCCNKMDAttpkySKARYD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 143 WVMDQVFDLFDNLGATDEQLDFTVVyaSALNGWATMEEgevGTDME----PLFQAVVDTVEAPAVDLEGPLQMQISQLDY 218
Cdd:PLN00043 169 EIVKEVSSYLKKVGYNPDKIPFVPI--SGFEGDNMIER---STNLDwykgPTLLEALDQINEPKRPSDKPLRLPLQDVYK 243
|
250 260
....*....|....*....|....
gi 1376772070 219 SSYVGVIGVARVTRGSVKPNQQVT 242
Cdd:PLN00043 244 IGGIGTVPVGRVETGVIKPGMVVT 267
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
17-174 |
1.52e-14 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.
Pssm-ID: 206734 [Multi-domain] Cd Length: 170 Bit Score: 71.87 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 17 HVDHGKTTLVDKLLQQSGtlesrgeaeervmDSNDIEKERGITI--------LAKNTaidwndyRINIVDTPGHADFgge 88
Cdd:cd04171 7 HIDHGKTTLIKALTGIET-------------DRLPEEKKRGITIdlgfayldLPDGK-------RLGFIDVPGHEKF--- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 89 verIMSMV------DSVLLIVDAVDGPMPQTRFVTQKAFAHGLKP-IVVINKIDRpgARPDWVMDQVFDLFDNLGATDEQ 161
Cdd:cd04171 64 ---VKNMLagaggiDAVLLVVAADEGIMPQTREHLEILELLGIKKgLVVLTKADL--VDEDRLELVEEEILELLAGTFLA 138
|
170
....*....|...
gi 1376772070 162 lDFTVVYASALNG 174
Cdd:cd04171 139 -DAPIFPVSSVTG 150
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
11-135 |
1.64e-14 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.
Pssm-ID: 206676 [Multi-domain] Cd Length: 192 Bit Score: 72.40 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 11 NIAIIAHVDHGKTTLVDKLLQQSGTlesrgeaeeRVMDSNDIEKERGITI--------------LAKNTAIDWNDYRINI 76
Cdd:cd01889 2 NVGLLGHVDSGKTSLAKALSEIAST---------AAFDKNPQSQERGITLdlgfssfevdkpkhLEDNENPQIENYQITL 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1376772070 77 VDTPGHADF------GGEVerimsmVDSVLLIVDAVDGPMPQTRF------VTQKafahglKPIVVINKID 135
Cdd:cd01889 73 VDCPGHASLirtiigGAQI------IDLMLLVVDAKKGIQTQTAEclvigeLLCK------PLIVVLNKID 131
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
13-175 |
2.52e-13 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 67.87 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 13 AIIAHVDHGKTTLVDKLLQQSGTLESRGEAEERVMDSNDIEkergitilakntaIDWNDYRINIVDTPGHADFGG----- 87
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPDVYVKE-------------LDKGKVKLVLVDTPGLDEFGGlgree 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 88 EVERIMSMVDSVLLIVDAVDGPMP--QTRFVTQKAFAHGLKPIVVINKIDRPGARPDWVMDQVFDLFdnlgatdEQLDFT 165
Cdd:cd00882 68 LARLLLRGADLILLVVDSTDRESEedAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELA-------KILGVP 140
|
170
....*....|
gi 1376772070 166 VVYASALNGW 175
Cdd:cd00882 141 VFEVSAKTGE 150
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
9-318 |
2.82e-12 |
|
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: 68.96 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 9 LRnIAIIAHVDHGKTTLVDKLLQQSGTL----------ESRGEAEERV-----MDSNDIEKERGITIlakNTAidwndYR 73
Cdd:COG2895 18 LR-FITCGSVDDGKSTLIGRLLYDTKSIfedqlaalerDSKKRGTQEIdlallTDGLQAEREQGITI---DVA-----YR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 74 ---------InIVDTPGHADFggevERIM----SMVDSVLLIVDAVDGPMPQTR---FVtqkafAH--GLKPIVV-INKI 134
Cdd:COG2895 89 yfstpkrkfI-IADTPGHEQY----TRNMvtgaSTADLAILLIDARKGVLEQTRrhsYI-----ASllGIRHVVVaVNKM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 135 DRPG---ARPDWVMDQVFDLFDNLGATdeqlDFTVVYASALNGW------ATME--EGEvgTDMEPLfqavvDTVEAPAV 203
Cdd:COG2895 159 DLVDyseEVFEEIVADYRAFAAKLGLE----DITFIPISALKGDnvversENMPwyDGP--TLLEHL-----ETVEVAED 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 204 DLEGPLQMQI-----SQLDYSSYVGvigvaRVTRGSVKPNQQVTIVnAEGKKrnGKVGTVLGYLGlerhEVEQANAGDII 278
Cdd:COG2895 228 RNDAPFRFPVqyvnrPNLDFRGYAG-----TIASGTVRVGDEVVVL-PSGKT--STVKSIVTFDG----DLEEAFAGQSV 295
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1376772070 279 AITGLGELKIS--DTICDVNNVeameplsvdePTVTMTFQVN 318
Cdd:COG2895 296 TLTLEDEIDISrgDVIVAADAP----------PEVADQFEAT 327
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
18-289 |
5.40e-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: 67.78 E-value: 5.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 18 VDHGKTTLVDKLLQQSGTL----------ESRGEAEE-------RVMDSNDIEKERGITILAKNTAIDWNDYRINIVDTP 80
Cdd:TIGR02034 9 VDDGKSTLIGRLLHDTKQIyedqlaalerDSKKHGTQggeidlaLLVDGLQAEREQGITIDVAYRYFSTDKRKFIVADTP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 81 GHADFGGEVERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVV-INKIDRPGARPDwVMDQVFDLFDNLGATD 159
Cdd:TIGR02034 89 GHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLaVNKMDLVDYDEE-VFENIKKDYLAFAEQL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 160 EQLDFTVVYASALNGwatmEEGEVGTDMEPLFQA-----VVDTVEAPAVDLEGPLQMQIS-----QLDYSSYVGVIgvar 229
Cdd:TIGR02034 168 GFRDVTFIPLSALKG----DNVVSRSESMPWYSGptlleILETVEVERDAQDLPLRFPVQyvnrpNLDFRGYAGTI---- 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 230 vTRGSVKPNQQVTIVnAEGkkRNGKVGTVLGYLGlerhEVEQANAGDIIAITGLGELKIS 289
Cdd:TIGR02034 240 -ASGSVHVGDEVVVL-PSG--RSSRVARIVTFDG----DLEQARAGQAVTLTLDDEIDIS 291
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
11-174 |
8.19e-11 |
|
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: 61.82 E-value: 8.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 11 NIAIIAHVDHGKTTLVDKLLQQSGTL-----------ESRGEAEERV-----MDSNDIEKERGITIlakNTAidwndYR- 73
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSIfedqlaalersKSSGTQGEKLdlallVDGLQAEREQGITI---DVA-----YRy 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 74 --------InIVDTPGHADFggevERIM----SMVDSVLLIVDAVDGPMPQTRfvtQKAF-AH--GLKPIVV-INKIDRP 137
Cdd:cd04166 73 fstpkrkfI-IADTPGHEQY----TRNMvtgaSTADLAILLVDARKGVLEQTR---RHSYiASllGIRHVVVaVNKMDLV 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 1376772070 138 GARPDwVMDQVFDLFDNLGATDEQLDFTVVYASALNG 174
Cdd:cd04166 145 DYDEE-VFEEIKADYLAFAASLGIEDITFIPISALEG 180
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
11-283 |
3.07e-10 |
|
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: 62.38 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 11 NIAIIAHVDHGKTTLVDKLlqqSGTLESRGEAEERvmdsndiekeRGITI--------LAKNTAIDWNDY---------- 72
Cdd:TIGR03680 6 NIGMVGHVDHGKTTLTKAL---TGVWTDTHSEELK----------RGISIrlgyadaeIYKCPECDGPECyttepvcpnc 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 73 --------RINIVDTPGHadfggevERIM-------SMVDSVLLIVDAVDG-PMPQTRFVTQKAFAHGLKPIVVI-NKID 135
Cdd:TIGR03680 73 gsetellrRVSFVDAPGH-------ETLMatmlsgaALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVqNKID 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 136 ---RPGARPDWvmDQVFDLFDnlGATDEqlDFTVVYASALNgwatmeegevGTDMEPLFQAVVDTVEAPAVDLEGPLQMQ 212
Cdd:TIGR03680 146 lvsKEKALENY--EEIKEFVK--GTVAE--NAPIIPVSALH----------NANIDALLEAIEKFIPTPERDLDKPPLMY 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 213 ISQ--------LDYSSYV-GVIGvARVTRGSVKPNQQVTI-----VNAEGKKRNGKVGTVLGYLGLERHEVEQANAGDII 278
Cdd:TIGR03680 210 VARsfdvnkpgTPPEKLKgGVIG-GSLIQGKLKVGDEIEIrpgikVEKGGKTKWEPIYTEITSLRAGGYKVEEARPGGLV 288
|
....*.
gi 1376772070 279 AI-TGL 283
Cdd:TIGR03680 289 GVgTKL 294
|
|
| EFG_mtEFG_II |
cd04088 |
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation ... |
221-294 |
5.41e-10 |
|
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation factors G1 and G2; This family represents the domain II of bacterial Elongation factor G (EF-G)and mitochondrial Elongation factors G1 (mtEFG1) and G2 (mtEFG2). During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. In bacteria this translocation step is catalyzed by EF-G_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. mtEFG1 and mtEFG2 show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. No clear phenotype has been found for mutants in the yeast homolog of mtEFG2, MEF2.
Pssm-ID: 293905 [Multi-domain] Cd Length: 83 Bit Score: 55.99 E-value: 5.41e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1376772070 221 YVGVIGVARVTRGSVKPNQQVTIVNaEGKKRngKVGTVLGYLGLERHEVEQANAGDIIAITGLGELKISDTICD 294
Cdd:cd04088 13 FVGKLTFFRVYSGTLKSGSTVYNST-KGKKE--RVGRLLRMHGKKREEVEELGAGDIGAVVGLKDTRTGDTLCD 83
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
223-293 |
6.32e-10 |
|
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.
Pssm-ID: 427163 [Multi-domain] Cd Length: 73 Bit Score: 55.73 E-value: 6.32e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1376772070 223 GVIGVARVTRGSVKPNQQVTIVNAE--GKKRNGKVGTVLGYLGLERHEVEQANAGDIIAITGLGELKISDTIC 293
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGtgKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
12-194 |
1.06e-09 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 58.07 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 12 IAIIAHVDHGKTTLVDKLLQqsgtlesrgeaeervmDSNDIEKE---RGITILAKNTAIDWNDYRINIVDTPGHADFGGE 88
Cdd:COG1100 6 IVVVGTGGVGKTSLVNRLVG----------------DIFSLEKYlstNGVTIDKKELKLDGLDVDLVIWDTPGQDEFRET 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 89 VERIMSMVD--SVLLIVdaVDGPMPQTRFVT----QKAFAHGLKP--IVVINKIDRpgaRPDWVMDQVFDLFDNLGatdE 160
Cdd:COG1100 70 RQFYARQLTgaSLYLFV--VDGTREETLQSLyellESLRRLGKKSpiILVLNKIDL---YDEEEIEDEERLKEALS---E 141
|
170 180 190
....*....|....*....|....*....|....
gi 1376772070 161 QLDFTVVYASALNGWatmeegevgtDMEPLFQAV 194
Cdd:COG1100 142 DNIVEVVATSAKTGE----------GVEELFAAL 165
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
209-293 |
2.27e-09 |
|
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: 54.19 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 209 LQMQISQLDYSSYVGVIGVARVTRGSVKPNQQVTIVnaeGKKRNGKVGtvlgylGLERH--EVEQANAGDIIAITGLG-- 284
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRIL---PKGITGRVT------SIERFheEVDEAKAGDIVGIGILGvk 71
|
....*....
gi 1376772070 285 ELKISDTIC 293
Cdd:cd01342 72 DILTGDTLT 80
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
11-135 |
1.87e-08 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 56.78 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 11 NIAIIAHVDHGKTTLVDKLlqqSGTLESRGEAEERvmdsndiekeRGITI--------LAKNTAIDWNDY---------- 72
Cdd:PRK04000 11 NIGMVGHVDHGKTTLVQAL---TGVWTDRHSEELK----------RGITIrlgyadatIRKCPDCEEPEAyttepkcpnc 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 73 --------RINIVDTPGHadfggevERIM-------SMVDSVLLIVDAVDG-PMPQTRfvtqkafAH-------GLKPIV 129
Cdd:PRK04000 78 gsetellrRVSFVDAPGH-------ETLMatmlsgaALMDGAILVIAANEPcPQPQTK-------EHlmaldiiGIKNIV 143
|
....*..
gi 1376772070 130 VI-NKID 135
Cdd:PRK04000 144 IVqNKID 150
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
6-141 |
2.05e-08 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 57.11 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 6 IDKLRN--IAIIAHVDHGKTTLVDKLlqqsgtlesRGeaeervmdSNDIEKERG-IT--ILAknTAIDWN---------- 70
Cdd:PRK04004 1 EKKLRQpiVVVLGHVDHGKTTLLDKI---------RG--------TAVAAKEAGgITqhIGA--TEVPIDviekiagplk 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 71 -DYRINI-------VDTPGHADF------GGeverimSMVDSVLLIVDAVDGPMPQT--------RFVTqkafahglkP- 127
Cdd:PRK04004 62 kPLPIKLkipgllfIDTPGHEAFtnlrkrGG------ALADIAILVVDINEGFQPQTieainilkRRKT---------Pf 126
|
170
....*....|....*
gi 1376772070 128 IVVINKIDR-PGARP 141
Cdd:PRK04004 127 VVAANKIDRiPGWKS 141
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
12-162 |
3.74e-08 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 56.21 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 12 IAIIAHVDHGKTTLVdkllqQSGTlesrGEAEERVMDsndiEKERGITILAKNTAIDWNDYR-INIVDTPGHADF----- 85
Cdd:PRK10512 3 IATAGHVDHGKTTLL-----QAIT----GVNADRLPE----EKKRGMTIDLGYAYWPQPDGRvLGFIDVPGHEKFlsnml 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 86 ---GGeverimsmVDSVLLIVDAVDGPMPQTR---FVTQKAFAHGLKpiVVINKIDR-PGARPDWVMDQVFDLFDNLGAT 158
Cdd:PRK10512 70 agvGG--------IDHALLVVACDDGVMAQTRehlAILQLTGNPMLT--VALTKADRvDEARIAEVRRQVKAVLREYGFA 139
|
....
gi 1376772070 159 DEQL 162
Cdd:PRK10512 140 EAKL 143
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
18-298 |
1.09e-07 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 54.94 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 18 VDHGKTTLVDKLLQQSGTL-ESRGEAEER----------------VMDSNDIEKERGITI--------LAKNTAIdwndy 72
Cdd:PRK05506 33 VDDGKSTLIGRLLYDSKMIfEDQLAALERdskkvgtqgdeidlalLVDGLAAEREQGITIdvayryfaTPKRKFI----- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 73 rinIVDTPGHADFggevERIM----SMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVV-INKIDRPGARPDwVMDQ 147
Cdd:PRK05506 108 ---VADTPGHEQY----TRNMvtgaSTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLaVNKMDLVDYDQE-VFDE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 148 VFDLFDNLGATDEQLDFTVVYASALNG------WATMEEGEVGTDMEPLFQAVVDTVEApAVDLEGPLQMQI-SQLDYSS 220
Cdd:PRK05506 180 IVADYRAFAAKLGLHDVTFIPISALKGdnvvtrSARMPWYEGPSLLEHLETVEIASDRN-LKDFRFPVQYVNrPNLDFRG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 221 YVGVIgvarvTRGSVKPNQQVTIVNAegkKRNGKVGTVLGYLGlerhEVEQANAGDIIAITGLGELKIS--DTICDVNNV 298
Cdd:PRK05506 259 FAGTV-----ASGVVRPGDEVVVLPS---GKTSRVKRIVTPDG----DLDEAFAGQAVTLTLADEIDISrgDMLARADNR 326
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
12-175 |
1.26e-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: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 12 IAIIAHVDHGKTTLVDKLLQqsgtlesrgeaEERVMDSNdiekERGITILAKNTAIDWNDYRINIVDTPG-----HADFG 86
Cdd:cd01895 5 IAIIGRPNVGKSSLLNALLG-----------EERVIVSD----IAGTTRDSIDVPFEYDGQKYTLIDTAGirkkgKVTEG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 87 GE------VERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINK---IDRPGARPDWVMDQVFDLFDnlga 157
Cdd:cd01895 70 IEkysvlrTLKAIERADVVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKwdlVEKDEKTMKEFEKELRRKLP---- 145
|
170
....*....|....*....
gi 1376772070 158 tdeQLDFT-VVYASALNGW 175
Cdd:cd01895 146 ---FLDYApIVFISALTGQ 161
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
12-140 |
3.37e-07 |
|
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: 53.28 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 12 IAIIAHVDHGKTTLVDKLL------QQSGTLESRGEAEERVMDSndIEKERGItiLAKNTAIDWNDYRINIVDTPGHADF 85
Cdd:TIGR00491 7 VVVLGHVDHGKTTLLDKIRgtavvkKEAGGITQHIGASEVPTDV--IEKICGD--LLKSFKIKLKIPGLLFIDTPGHEAF 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1376772070 86 GGEVERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDR-PGAR 140
Cdd:TIGR00491 83 TNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTPFVVAANKIDRiPGWK 138
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
57-133 |
5.40e-07 |
|
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: 48.38 E-value: 5.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 57 GITILAKNTAIDWNDYRINIVDTPG-----HADFG-GEVERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVV 130
Cdd:pfam01926 31 GTTRDPNEGRLELKGKQIILVDTPGliegaSEGEGlGRAFLAIIEADLILFVVDSEEGITPLDEELLELLRENKKPIILV 110
|
...
gi 1376772070 131 INK 133
Cdd:pfam01926 111 LNK 113
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
18-318 |
9.80e-07 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 51.45 E-value: 9.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 18 VDHGKTTLVDKLLQ--------QSGTLES----RGEAEERV-----MDSNDIEKERGITIlakNTAidwndYR------- 73
Cdd:PRK05124 36 VDDGKSTLIGRLLHdtkqiyedQLASLHNdskrHGTQGEKLdlallVDGLQAEREQGITI---DVA-----YRyfstekr 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 74 --InIVDTPGHADFggevERIM----SMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVV-INKIDRPG---ARPDW 143
Cdd:PRK05124 108 kfI-IADTPGHEQY----TRNMatgaSTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVaVNKMDLVDyseEVFER 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 144 VMDQVFDLFDNLGAtdeQLDFTVVYASALNG------WATMEEGEVGTDMEPLFQAVVDTvEAPAVDLEGPLQ-MQISQL 216
Cdd:PRK05124 183 IREDYLTFAEQLPG---NLDIRFVPLSALEGdnvvsqSESMPWYSGPTLLEVLETVDIQR-VVDAQPFRFPVQyVNRPNL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 217 DYSSYVGVigvarVTRGSVKPNQQVTIVNAeGKKrnGKVGTVLGYLGlerhEVEQANAGDIIAITGLGELKIS--DTICD 294
Cdd:PRK05124 259 DFRGYAGT-----LASGVVKVGDRVKVLPS-GKE--SNVARIVTFDG----DLEEAFAGEAITLVLEDEIDISrgDLLVA 326
|
330 340
....*....|....*....|....
gi 1376772070 295 VNNveameplsvdEPTVTMTFQVN 318
Cdd:PRK05124 327 ADE----------ALQAVQHASAD 340
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
11-135 |
1.24e-06 |
|
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.
Pssm-ID: 206675 [Multi-domain] Cd Length: 197 Bit Score: 49.19 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 11 NIAIIAHVDHGKTTLVDKLlqqSGTLESRgeaeervmdsNDIEKERGITI--------------LAKNTAIDWNDY---- 72
Cdd:cd01888 2 NIGTIGHVAHGKTTLVKAL---SGVWTVR----------HKEELKRNITIklgyanakiykcpnCGCPRPYDTPECecpg 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 73 ---------RINIVDTPGHadfggevERIM-------SMVDSVLLIVDAVDG-PMPQTRfvtqkafAH-------GLKPI 128
Cdd:cd01888 69 cggetklvrHVSFVDCPGH-------EILMatmlsgaAVMDGALLLIAANEPcPQPQTS-------EHlaaleimGLKHI 134
|
....*...
gi 1376772070 129 VVI-NKID 135
Cdd:cd01888 135 IILqNKID 142
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
71-174 |
2.46e-06 |
|
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.
Pssm-ID: 206726 [Multi-domain] Cd Length: 168 Bit Score: 47.84 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 71 DYRINIVDTPG-HADFGG-------EVERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDRPGARPD 142
Cdd:cd04163 50 DAQIIFVDTPGiHKPKKKlgermvkAAWSALKDVDLVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDLVKDKED 129
|
90 100 110
....*....|....*....|....*....|...
gi 1376772070 143 WVMDQVFdlfdnlgaTDEQLDFT-VVYASALNG 174
Cdd:cd04163 130 LLPLLEK--------LKELHPFAeIFPISALKG 154
|
|
| EFG_mtEFG_C |
cd03713 |
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational ... |
402-478 |
2.85e-06 |
|
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational elongation factor (EF) EF-G. Included in this group is the C-terminus of mitochondrial Elongation factor G1 (mtEFG1) and G2 (mtEFG2) proteins. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. In bacteria this translocation step is catalyzed by EF-G_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. No clear phenotype has been found for mutants in the yeast homologue of mtEFG2, MEF2.
Pssm-ID: 239683 [Multi-domain] Cd Length: 78 Bit Score: 45.21 E-value: 2.85e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1376772070 402 EPFETVTIDVVEEHQGAIMESIGLRKGELTDMAPDGkGRVRMDFMMPSRGLIGFQTEFLTMTSGSGLIYHSFDHYGP 478
Cdd:cd03713 1 EPIMKVEVTVPEEYMGDVIGDLSSRRGQILGTESRG-GWKVIKAEVPLAEMFGYSTDLRSLTQGRGSFTMEFSHYEE 76
|
|
| EngA1 |
cd01894 |
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
67-174 |
7.31e-06 |
|
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: 46.27 E-value: 7.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 67 IDWNDYRINIVDTPGHADFGGE--------VERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDrpG 138
Cdd:cd01894 40 AEWGGREFILIDTGGIEPDDEGiskeireqAEIAIEEADVILFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKID--N 117
|
90 100 110
....*....|....*....|....*....|....*.
gi 1376772070 139 ARPDWVMDQvfdlFDNLGATDeqldftVVYASALNG 174
Cdd:cd01894 118 IKEEEEAAE----FYSLGFGE------PIPISAEHG 143
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
71-174 |
2.18e-05 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 46.52 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 71 DYRINIVDTPG-----HAdFG----GEVERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDRpgARP 141
Cdd:COG1159 50 DAQIVFVDTPGihkpkRK-LGrrmnKAAWSALEDVDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDL--VKK 126
|
90 100 110
....*....|....*....|....*....|....
gi 1376772070 142 DwvmdqvfDLFDNLGATDEQLDFT-VVYASALNG 174
Cdd:COG1159 127 E-------ELLPLLAEYSELLDFAeIVPISALKG 153
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
12-174 |
2.81e-05 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 46.97 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 12 IAIIAHVDHGKTTLVDKLLQqsgtlesrgeaEERVMDSNdiekERGITILAKNTAIDWNDYRINIVDTPG-------HAD 84
Cdd:PRK00093 176 IAIIGRPNVGKSSLINALLG-----------EERVIVSD----IAGTTRDSIDTPFERDGQKYTLIDTAGirrkgkvTEG 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 85 fggeVE--------RIMSMVDSVLLIVDAVDGpmpqtrFVTQKA----FAH--GLKPIVVINKIDrpgARPDWVMDQVFD 150
Cdd:PRK00093 241 ----VEkysvirtlKAIERADVVLLVIDATEG------ITEQDLriagLALeaGRALVIVVNKWD---LVDEKTMEEFKK 307
|
170 180
....*....|....*....|....*.
gi 1376772070 151 LFDN-LGatdeQLDFT-VVYASALNG 174
Cdd:PRK00093 308 ELRRrLP----FLDYApIVFISALTG 329
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
70-174 |
3.34e-05 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 46.19 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 70 NDYRINIVDTPG-HADfGGEVERIM------SM--VDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDRPGAR 140
Cdd:PRK00089 51 DDAQIIFVDTPGiHKP-KRALNRAMnkaawsSLkdVDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLVKDK 129
|
90 100 110
....*....|....*....|....*....|....*
gi 1376772070 141 pdwvmDQVFDLFDNLgatDEQLDFT-VVYASALNG 174
Cdd:PRK00089 130 -----EELLPLLEEL---SELMDFAeIVPISALKG 156
|
|
| lepA_C |
cd03709 |
lepA_C: This family represents the C-terminal region of LepA, a GTP-binding protein localized ... |
402-474 |
6.32e-05 |
|
lepA_C: This family represents the C-terminal region of LepA, a GTP-binding protein localized in the cytoplasmic membrane. LepA is ubiquitous in Bacteria and Eukaryota (e.g. Saccharomyces cerevisiae GUF1p), but is missing from Archaea. LepA exhibits significant homology to elongation factors (EFs) Tu and G. The function(s) of the proteins in this family are unknown. The N-terminal domain of LepA is homologous to a domain of similar size found in initiation factor 2 (IF2), and in EF-Tu and EF-G (factors required for translation in Escherichia coli). Two types of phylogenetic tree, rooted by other GTP-binding proteins, suggest that eukaryotic homologs (including S. cerevisiae GUF1) originated within the bacterial LepA family. LepA has never been observed in archaea, and eukaryl LepA is organellar. LepA is therefore a true bacterial GTPase, found only in the bacterial lineage.
Pssm-ID: 239680 [Multi-domain] Cd Length: 80 Bit Score: 41.71 E-value: 6.32e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1376772070 402 EPFETVTIDVVEEHQGAIMESIGLRKGELTDMAPDGKGRVRMDFMMPSRGLI-GFQTEFLTMTSGsgliYHSFD 474
Cdd:cd03709 1 EPFVKATIITPSEYLGAIMELCQERRGVQKDMEYLDANRVMLTYELPLAEIVyDFFDKLKSISKG----YASLD 70
|
|
| mtEFG1_C |
cd04097 |
mtEFG1_C: C-terminus of mitochondrial Elongation factor G1 (mtEFG1)-like proteins found in ... |
402-478 |
6.51e-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: 41.54 E-value: 6.51e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1376772070 402 EPFETVTIDVVEEHQGAIMESIGLRKGELTDMAPDGkGRVRMDFMMPSRGLIGFQTEFLTMTSGSGLIYHSFDHYGP 478
Cdd:cd04097 1 EPIMKVEVTAPTEFQGNVIGLLNKRKGTIVDTDTGE-DEFTLEAEVPLNDMFGYSTELRSMTQGKGEFSMEFSRYAP 76
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
11-135 |
1.87e-04 |
|
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: 44.06 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 11 NIAIIAHVDHGKTTLVDKLlqqSGTLESRGEAEERvmdsndiekeRGITI------------------LAKNTAIDWNDY 72
Cdd:COG5257 7 NIGVVGHVDHGKTTLVQAL---TGVWTDRHSEELK----------RGITIrlgyadatfykcpnceppEAYTTEPKCPNC 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 73 --------RINIVDTPGHadfggevERIM-------SMVDSVLLIVDAVDG-PMPQTRfvtqkafAH-------GLKPIV 129
Cdd:COG5257 74 gsetellrRVSFVDAPGH-------ETLMatmlsgaALMDGAILVIAANEPcPQPQTK-------EHlmaldiiGIKNIV 139
|
....*..
gi 1376772070 130 VI-NKID 135
Cdd:COG5257 140 IVqNKID 146
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
67-142 |
1.99e-04 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 44.24 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 67 IDWNDYRINIVDTPG-----HADFGGE----VERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGlKP-IVVINKIDR 136
Cdd:COG1160 45 AEWGGREFTLIDTGGiepddDDGLEAEireqAELAIEEADVILFVVDGRAGLTPLDEEIAKLLRRSG-KPvILVVNKVDG 123
|
....*.
gi 1376772070 137 PGARPD 142
Cdd:COG1160 124 PKREAD 129
|
|
| EF2_II |
cd16268 |
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 ... |
223-294 |
2.97e-04 |
|
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: 40.28 E-value: 2.97e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1376772070 223 GVIGVARVTRGSVKPNQQVTIV------NAEGKKRNGKVGTVLGYLGLERHEVEQANAGDIIAITGL-GELKISDTICD 294
Cdd:cd16268 17 GFVAFGRVFSGTVRRGQEVYILgpkyvpGKKDDLKKKRIQQTYLMMGREREPVDEVPAGNIVGLVGLdDFLAKSGTTTS 95
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
96-174 |
3.88e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 42.00 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 96 VDsVLLIVDAVDGPMPQT----RFVTQkAFAHGLKPIVVINKIDRPgarPDWVMDQVFDLFdnlgatdEQLDFTVVYASA 171
Cdd:cd01854 3 VD-QVLIVFSLKEPFFNLrlldRYLVA-AEASGIEPVIVLNKADLV---DDEELEELLEIY-------EKLGYPVLAVSA 70
|
...
gi 1376772070 172 LNG 174
Cdd:cd01854 71 KTG 73
|
|
| EF4_II |
cd03699 |
Domain II of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly ... |
218-294 |
4.40e-04 |
|
Domain II of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly conserved guanosine triphosphatase found in bacteria and eukaryotic mitochondria and chloroplasts. EF4 functions as a translation factor, which promotes back-translocation of tRNAs on posttranslocational ribosome complexes and competes with elongation factor G for interaction with pretranslocational ribosomes, inhibiting the elongation phase of protein synthesis.
Pssm-ID: 293900 [Multi-domain] Cd Length: 86 Bit Score: 39.32 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 218 YSSYVGVIGVARVTRGSVKPNQQVTIVNaegkkrNGKVGTV--LGYLGLERHEVEQANAGD---IIA-ITGLGELKISDT 291
Cdd:cd03699 10 YDPYRGVVVLVRVFDGTLKKGDKIRFMA------TGKEYEVleVGVFTPKMVPTDELSAGEvgyIIAgIKSVKDARVGDT 83
|
...
gi 1376772070 292 ICD 294
Cdd:cd03699 84 ITL 86
|
|
| MnmE |
COG0486 |
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
67-209 |
4.68e-04 |
|
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440253 [Multi-domain] Cd Length: 448 Bit Score: 43.13 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 67 IDWNDYRINIVDTPGHADFGGEVERI--------MSMVDSVLLIVDAVDGPMPQTRFVTQKAFahGLKPIVVINKIDRPG 138
Cdd:COG0486 256 INIGGIPVRLIDTAGLRETEDEVEKIgierareaIEEADLVLLLLDASEPLTEEDEEILEKLK--DKPVIVVLNKIDLPS 333
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1376772070 139 ARPDWVmdqvfdlfdnlgatDEQLDFTVVYASALNGwatmeEGevgtdMEPLFQAVVDTVEAPAVDLEGPL 209
Cdd:COG0486 334 EADGEL--------------KSLPGEPVIAISAKTG-----EG-----IDELKEAILELVGEGALEGEGVL 380
|
|
| PRK09518 |
PRK09518 |
bifunctional cytidylate kinase/GTPase Der; Reviewed |
12-137 |
5.29e-04 |
|
bifunctional cytidylate kinase/GTPase Der; Reviewed
Pssm-ID: 236546 [Multi-domain] Cd Length: 712 Bit Score: 43.24 E-value: 5.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 12 IAIIAHVDHGKTTLVDKLLqqsgtlesrGEAEERVMDSNDIEKERgITILAkntaiDWNDYRINIVDTPG--------HA 83
Cdd:PRK09518 278 VAIVGRPNVGKSTLVNRIL---------GRREAVVEDTPGVTRDR-VSYDA-----EWAGTDFKLVDTGGweadvegiDS 342
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1376772070 84 DFGGEVERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDRP 137
Cdd:PRK09518 343 AIASQAQIAVSLADAVVFVVDGQVGLTSTDERIVRMLRRAGKPVVLAVNKIDDQ 396
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
67-142 |
5.38e-04 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 42.73 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 67 IDWNDYRINIVDTPG----HADFGGEV----ERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDRPG 138
Cdd:PRK00093 44 AEWLGREFILIDTGGiepdDDGFEKQIreqaELAIEEADVILFVVDGRAGLTPADEEIAKILRKSNKPVILVVNKVDGPD 123
|
....
gi 1376772070 139 ARPD 142
Cdd:PRK00093 124 EEAD 127
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
21-141 |
1.10e-03 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 39.92 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 21 GKTTLVDKLLQQsgtlesrgeaeervmDSNDIEKERGITILAKNTAIDWNDYR-INIVDTPGHADFGGE----VERIMSM 95
Cdd:cd00880 9 GKSSLLNALLGQ---------------NVGIVSPIPGTTRDPVRKEWELLPLGpVVLIDTPGLDEEGGLgrerVEEARQV 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1376772070 96 VDSVLLIVDAVDGPMPQTRFVTQKAFAHGL-KP-IVVINKIDRPGARP 141
Cdd:cd00880 74 ADRADLVLLVVDSDLTPVEEEAKLGLLRERgKPvLLVLNKIDLVPESE 121
|
|
| Tet_II |
cd03690 |
Domain II of ribosomal protection proteins Tet(M) and Tet(O); This subfamily represents domain ... |
229-292 |
2.47e-03 |
|
Domain II of ribosomal protection proteins Tet(M) and Tet(O); This subfamily represents domain II of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology to domain II of the elongation factors EF-G and EF-2. Tet(M) and Tet(O) catalyze the release of tetracycline (Tc) from the ribosome in a GTP-dependent manner thereby mediating Tc resistance. Tcs are broad-spectrum antibiotics. Typical Tcs bind to the ribosome and inhibit the elongation phase of protein synthesis, by inhibiting the occupation of site A by aminoacyl-tRNA.
Pssm-ID: 293891 [Multi-domain] Cd Length: 86 Bit Score: 37.22 E-value: 2.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1376772070 229 RVTRGSVKPNQQVTIVnaeGKKRNGKVGTVLGYLGLERHEVEQANAGDIIAITGLGELKISDTI 292
Cdd:cd03690 24 RLYSGTLRLRDSVRVS---GEEEKIKITELRTFENGELVKVDRVYAGDIAILVGLKSLRVGDVL 84
|
|
| PRK03003 |
PRK03003 |
GTP-binding protein Der; Reviewed |
12-142 |
5.13e-03 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 179525 [Multi-domain] Cd Length: 472 Bit Score: 39.57 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 12 IAIIAHVDHGKTTLVDKLLqqsgtlesrGEAEERVMDSNDIEKERgITILAkntaiDWNDYRINIVDTPG--------HA 83
Cdd:PRK03003 41 VAVVGRPNVGKSTLVNRIL---------GRREAVVEDVPGVTRDR-VSYDA-----EWNGRRFTVVDTGGwepdakglQA 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1376772070 84 DFGGEVERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDRPGARPD 142
Cdd:PRK03003 106 SVAEQAEVAMRTADAVLFVVDATVGATATDEAVARVLRRSGKPVILAANKVDDERGEAD 164
|
|
| EFG_C |
smart00838 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
401-478 |
6.66e-03 |
|
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of Elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopt a ferredoxin-like fold.
Pssm-ID: 197906 [Multi-domain] Cd Length: 85 Bit Score: 35.94 E-value: 6.66e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1376772070 401 MEPFETVTIDVVEEHQGAIMESIGLRKGELTDMAPDGkGRVRMDFMMPSRGLIGFQTEFLTMTSGSGLIYHSFDHYGP 478
Cdd:smart00838 2 LEPIMKVEVTVPEEYMGDVIGDLNSRRGKIEGMEQRG-GAQVIKAKVPLSEMFGYATDLRSATQGRATWSMEFSHYEE 78
|
|
| MJ1464 |
cd01859 |
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ... |
89-171 |
9.21e-03 |
|
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents archaeal GTPase typified by the protein MJ1464 from Methanococcus jannaschii. The members of this family show a circular permutation of the GTPase signature motifs so that C-terminal strands 5, 6, and 7 (strands 6 contain the NKxD motif) are relocated to the N terminus.
Pssm-ID: 206752 [Multi-domain] Cd Length: 157 Bit Score: 37.30 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376772070 89 VERIMSMVDSVLLIVDAVDGPMPQTRFVTQKAFAHGLKPIVVINKIDrpgARPDWVMDQVFDLFdnlgatdEQLDFTVVY 168
Cdd:cd01859 5 VRRIIKEADVVLEVVDARDPELTRSRKLERMALELGKKLIIVLNKAD---LVPREVLEKWKEVF-------ESEGLPVVY 74
|
...
gi 1376772070 169 ASA 171
Cdd:cd01859 75 VSA 77
|
|
| |
