|
Name |
Accession |
Description |
Interval |
E-value |
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
5-606 |
0e+00 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 1263.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 5 TRNDIRNVAIIAHVDHGKTTLVDAMLKQSHVFRDNEKVQERVMDSNDLEKERGITILSKNTAVMYNGVKINIVDTPGHAD 84
Cdd:COG1217 2 MREDIRNIAIIAHVDHGKTTLVDALLKQSGTFRENQEVAERVMDSNDLERERGITILAKNTAVRYKGVKINIVDTPGHAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 85 FGGEVERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINKIDKPNARPQEVIDEVFDLFVELGADDEQLDF 164
Cdd:COG1217 82 FGGEVERVLSMVDGVLLLVDAFEGPMPQTRFVLKKALELGLKPIVVINKIDRPDARPDEVVDEVFDLFIELGATDEQLDF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 165 PIVYASARGGYAKKEVDEESDNMECLFDTIIKNVKAPTGYIEEPLQLLVTTIDYNEYVGRIGIGKIERGKVAKNQQVTIV 244
Cdd:COG1217 162 PVVYASARNGWASLDLDDPGEDLTPLFDTILEHVPAPEVDPDGPLQMLVTNLDYSDYVGRIAIGRIFRGTIKKGQQVALI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 245 DREGNKRNVKVSNLYVYNGLKREEVEEAQLGDIVAVSGIVDINIGETIADPSRPEAVEFIEIDEPTLSMYFMVNDSPFAG 324
Cdd:COG1217 242 KRDGKVEKGKITKLFGFEGLERVEVEEAEAGDIVAIAGIEDINIGDTICDPENPEALPPIKIDEPTLSMTFSVNDSPFAG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 325 KEGEYVTSRHLRDRLMKELETNVSLKVEETDSADSFKVSGRGELHLSILIETMRREGYEFQVSKPSVIFHEQDGKKHEPI 404
Cdd:COG1217 322 REGKFVTSRQIRERLEKELETNVALRVEETDSPDAFKVSGRGELHLSILIETMRREGYELQVSRPEVIFKEIDGKKLEPI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 405 EYLTIDVPEEFMGVVMEKLGPRKAEMINMSSAVNGYSRLEFRIPARGLIGFRNEFMTDTKGNGIMNHVFDGYEPFKGEIP 484
Cdd:COG1217 402 EELTIDVPEEYSGAVIEKLGQRKGEMTNMEPDGGGRVRLEFLIPSRGLIGFRTEFLTDTRGTGIMNHVFDGYEPYKGEIP 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 485 GRTRGSIVAFETGEAVAYGLFNAQERGKLFVTPATDVYAGMIVGECSRAEDIDVNVCKKKHLTNTRSSGSDDALKLVPVV 564
Cdd:COG1217 482 GRRNGSLISMETGKATAYALFNLQERGTLFIGPGTEVYEGMIVGEHSRDNDLVVNVCKEKKLTNMRASGSDEAIRLTPPR 561
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1486620076 565 PMSLEQSLEFIAADELVEVTPINIRMRKKILDSAARKRASRK 606
Cdd:COG1217 562 KMSLEQALEFIEDDELVEVTPKSIRLRKKILDENERKRAAKK 603
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
9-602 |
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: 1086.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 9 IRNVAIIAHVDHGKTTLVDAMLKQSHVFRDNEKVQERVMDSNDLEKERGITILSKNTAVMYNGVKINIVDTPGHADFGGE 88
Cdd:TIGR01394 1 IRNIAIIAHVDHGKTTLVDALLKQSGTFRANEAVAERVMDSNDLERERGITILAKNTAIRYNGTKINIVDTPGHADFGGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 89 VERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINKIDKPNARPQEVIDEVFDLFVELGADDEQLDFPIVY 168
Cdd:TIGR01394 81 VERVLGMVDGVLLLVDASEGPMPQTRFVLKKALELGLKPIVVINKIDRPSARPDEVVDEVFDLFAELGADDEQLDFPIVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 169 ASARGGYAKKEVDEESDNMECLFDTIIKNVKAPTGYIEEPLQLLVTTIDYNEYVGRIGIGKIERGKVAKNQQVTIVDREG 248
Cdd:TIGR01394 161 ASGRAGWASLDLDDPSDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVHRGTVKKGQQVALMKRDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 249 NKRNVKVSNLYVYNGLKREEVEEAQLGDIVAVSGIVDINIGETIADPSRPEAVEFIEIDEPTLSMYFMVNDSPFAGKEGE 328
Cdd:TIGR01394 241 TIENGRISKLLGFEGLERVEIDEAGAGDIVAVAGLEDINIGETIADPEVPEALPTITVDEPTLSMTFSVNDSPLAGKEGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 329 YVTSRHLRDRLMKELETNVSLKVEETDSADSFKVSGRGELHLSILIETMRREGYEFQVSKPSVIFHEQDGKKHEPIEYLT 408
Cdd:TIGR01394 321 KVTSRHIRDRLMRELETNVALRVEDTESADKFEVSGRGELHLSILIETMRREGFELQVGRPQVIYKEIDGKKLEPIEELT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 409 IDVPEEFMGVVMEKLGPRKAEMINMSSAVNGYSRLEFRIPARGLIGFRNEFMTDTKGNGIMNHVFDGYEPFKGEIPGRTR 488
Cdd:TIGR01394 401 IDVPEEHVGAVIEKLGKRKGEMVDMEPSGNGRTRLEFKIPSRGLIGFRTEFLTDTRGTGIMNHVFDEYEPWKGEIETRRN 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 489 GSIVAFETGEAVAYGLFNAQERGKLFVTPATDVYAGMIVGECSRAEDIDVNVCKKKHLTNTRSSGSDDALKLVPVVPMSL 568
Cdd:TIGR01394 481 GSLVSMEDGTATAYALWNLQERGVMFVSPGTEVYEGMIIGEHSRENDLDVNPCKAKKLTNVRSSGKDEAVKLTPPRKLSL 560
|
570 580 590
....*....|....*....|....*....|....
gi 1486620076 569 EQSLEFIAADELVEVTPINIRMRKKILDSAARKR 602
Cdd:TIGR01394 561 EQALEYIEDDELVEVTPKSIRLRKRVLDPNERKR 594
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
8-605 |
0e+00 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 683.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 8 DIRNVAIIAHVDHGKTTLVDAMLKQSHVFRDNEKVQERVMDSNDLEKERGITILSKNTAVMYNGVKINIVDTPGHADFGG 87
Cdd:PRK10218 4 KLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 88 EVERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINKIDKPNARPQEVIDEVFDLFVELGADDEQLDFPIV 167
Cdd:PRK10218 84 EVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDFPIV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 168 YASARGGYAKKEVDEESDNMECLFDTIIKNVKAPTGYIEEPLQLLVTTIDYNEYVGRIGIGKIERGKVAKNQQVTIVDRE 247
Cdd:PRK10218 164 YASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIIDSE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 248 GNKRNVKVSNLYVYNGLKREEVEEAQLGDIVAVSGIVDINIGETIADPSRPEAVEFIEIDEPTLSMYFMVNDSPFAGKEG 327
Cdd:PRK10218 244 GKTRNAKVGKVLGHLGLERIETDLAEAGDIVAITGLGELNISDTVCDTQNVEALPALSVDEPTVSMFFCVNTSPFCGKEG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 328 EYVTSRHLRDRLMKELETNVSLKVEETDSADSFKVSGRGELHLSILIETMRREGYEFQVSKPSVIFHEQDGKKHEPIEYL 407
Cdd:PRK10218 324 KFVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRREGFELAVSRPKVIFREIDGRKQEPYENV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 408 TIDVPEEFMGVVMEKLGPRKAEMINMSSAVNGYSRLEFRIPARGLIGFRNEFMTDTKGNGIMNHVFDGYEPFK-GEIPGR 486
Cdd:PRK10218 404 TLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDVRpGEVGQR 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 487 TRGSIVAFETGEAVAYGLFNAQERGKLFVTPATDVYAGMIVGECSRAEDIDVNVCKKKHLTNTRSSGSDDALKLVPVVPM 566
Cdd:PRK10218 484 QNGVLISNGQGKAVAFALFGLQDRGKLFLGHGAEVYEGQIIGIHSRSNDLTVNCLTGKKLTNMRASGTDEAVVLVPPIRM 563
|
570 580 590
....*....|....*....|....*....|....*....
gi 1486620076 567 SLEQSLEFIAADELVEVTPINIRMRKKILDSAARKRASR 605
Cdd:PRK10218 564 TLEQALEFIDDDELVEVTPTSIRIRKRHLTENDRRRANR 602
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
8-201 |
1.39e-139 |
|
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: 403.51 E-value: 1.39e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 8 DIRNVAIIAHVDHGKTTLVDAMLKQSHVFRDNEKVQERVMDSNDLEKERGITILSKNTAVMYNGVKINIVDTPGHADFGG 87
Cdd:cd01891 1 KIRNIAIIAHVDHGKTTLVDALLKQSGTFRENEEVGERVMDSNDLERERGITILAKNTAITYKDTKINIIDTPGHADFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 88 EVERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINKIDKPNARPQEVIDEVFDLFVELGADDEQLDFPIV 167
Cdd:cd01891 81 EVERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDRPDARPEEVVDEVFDLFLELNATDEQLDFPIV 160
|
170 180 190
....*....|....*....|....*....|....
gi 1486620076 168 YASARGGYAKKEVDEESDNMECLFDTIIKNVKAP 201
Cdd:cd01891 161 YASAKNGWASLNLDDPSEDLDPLFETIIEHVPAP 194
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
7-198 |
3.10e-68 |
|
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: 219.70 E-value: 3.10e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 7 NDIRNVAIIAHVDHGKTTLVDAMLKQSHVFRDNEKVQ---ERVMDSNDLEKERGITILSKNTAVMYNGVKINIVDTPGHA 83
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKgegEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 84 DFGGEVERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINKIDKPN-ARPQEVIDEVFDLFVELGADDEqL 162
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDgAELEEVVEEVSRELLEKYGEDG-E 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 1486620076 163 DFPIVYASARGGyakkevdeesDNMECLFDTIIKNV 198
Cdd:pfam00009 160 FVPVVPGSALKG----------EGVQTLLDALDEYL 185
|
|
| lepA |
TIGR01393 |
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a ... |
9-478 |
7.84e-61 |
|
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a GTP-binding membrane protein related to EF-G and EF-Tu. Two types of phylogenetic tree, rooted by other GTP-binding proteins, suggest that eukaryotic homologs (including GUF1 of yeast) originated within the bacterial LepA family. The function is unknown. [Unknown function, General]
Pssm-ID: 130460 [Multi-domain] Cd Length: 595 Bit Score: 212.57 E-value: 7.84e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 9 IRNVAIIAHVDHGKTTLVDAMLKQSHVFRDNEKvQERVMDSNDLEKERGITILSKNTAVMY-----NGVKINIVDTPGHA 83
Cdd:TIGR01393 3 IRNFSIIAHIDHGKSTLADRLLEYTGAISEREM-REQVLDSMDLERERGITIKAQAVRLNYkakdgETYVLNLIDTPGHV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 84 DFGGEVERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINKIDKPNARPQEVIDEVFDLfveLGADDEQld 163
Cdd:TIGR01393 82 DFSYEVSRSLAACEGALLLVDAAQGIEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKKEIEEV---IGLDASE-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 164 fpIVYASARGGyakkevdeesDNMECLFDTIIKNVKAPTGYIEEPLQLLVTTIDYNEYVGRIGIGKIERGKVAKNQQVTI 243
Cdd:TIGR01393 157 --AILASAKTG----------IGIEEILEAIVKRVPPPKGDPDAPLKALIFDSHYDNYRGVVALVRVFEGTIKPGDKIRF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 244 VdreGNKRNVKVSNLYVY--NGLKREEVEEAQLGDIVA-VSGIVDINIGETIADPSRPeAVEFIEIDEPTLSMYFMvndS 320
Cdd:TIGR01393 225 M---STGKEYEVDEVGVFtpKLTKTDELSAGEVGYIIAgIKDVSDVRVGDTITHVKNP-AKEPLPGFKEVKPMVFA---G 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 321 PFAGKEGEYvtsRHLRDRLMKeLETNVSLKVEETDSADS----FKVSGRGELHLSILIETMRREgYEFQV--SKPSVIF- 393
Cdd:TIGR01393 298 LYPIDTEDY---EDLRDALEK-LKLNDASLTYEPESSPAlgfgFRCGFLGLLHMEIIQERLERE-FNLDLitTAPSVIYr 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 394 -HEQDGKK------------------HEPIEYLTIDVPEEFMGVVMEKLGPRKAEMINMSSAVNGYSRLEFRIP-ARGLI 453
Cdd:TIGR01393 373 vYLTNGEVievdnpsdlpdpgkiehvEEPYVKATIITPTEYLGPIMTLCQEKRGVQTNMEYLDPNRVELIYEMPlAEIVY 452
|
490 500
....*....|....*....|....*
gi 1486620076 454 GFRNEFMTDTKGNGIMNHVFDGYEP 478
Cdd:TIGR01393 453 DFFDKLKSISRGYASFDYELIGYRP 477
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
9-478 |
9.35e-59 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 206.79 E-value: 9.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 9 IRNVAIIAHVDHGKTTLVDAMLKQSHVFRDNEKvQERVMDSNDLEKERGITILSKNTAVMY---NGVK--INIVDTPGHA 83
Cdd:COG0481 6 IRNFSIIAHIDHGKSTLADRLLELTGTLSEREM-KEQVLDSMDLERERGITIKAQAVRLNYkakDGETyqLNLIDTPGHV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 84 DFGGEVERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINKIDKPNARPQEVIDEVFDLFvELGADDeqld 163
Cdd:COG0481 85 DFSYEVSRSLAACEGALLVVDASQGVEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKQEIEDII-GIDASD---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 164 fpIVYASARGGYAkkeVDEesdnmecLFDTIIKNVKAPTGYIEEPLQLLVttID--YNEYVGRIGIGKIERGKVAKNQQV 241
Cdd:COG0481 160 --AILVSAKTGIG---IEE-------ILEAIVERIPPPKGDPDAPLQALI--FDswYDSYRGVVVYVRVFDGTLKKGDKI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 242 TIVdreGNKRNVKVSNLYVYNgLKREEVEEAQLGD---IVA-VSGIVDINIGETIADPSRPeAVEFIEIDEPTLSmyfMV 317
Cdd:COG0481 226 KMM---STGKEYEVDEVGVFT-PKMTPVDELSAGEvgyIIAgIKDVRDARVGDTITLAKNP-AAEPLPGFKEVKP---MV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 318 ndspFAG---KEGEYVTsrHLRDRLMKeLETN-VSLKVE-ETDSADSFkvsG-R----GELHLSILIETMRRegyEFQVS 387
Cdd:COG0481 298 ----FAGlypVDSDDYE--DLRDALEK-LQLNdASLTYEpETSAALGF---GfRcgflGLLHMEIIQERLER---EFDLD 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 388 ----KPSVIFH--EQDGKK------------------HEPIEYLTIDVPEEFMGVVMEKLGPRKAEMINMSSAVNGYSRL 443
Cdd:COG0481 365 littAPSVVYEvtLTDGEVievdnpsdlpdpgkieeiEEPIVKATIITPSEYVGAVMELCQEKRGVQKNMEYLGENRVEL 444
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1486620076 444 EFRIPArgligfrNEFMTD--------TKGNGIMNHVFDGYEP 478
Cdd:COG0481 445 TYELPL-------AEIVFDffdrlksiTRGYASLDYEFIGYRE 480
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
9-477 |
8.50e-55 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 198.16 E-value: 8.50e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 9 IRNVAIIAHVDHGKTTLVDAMLKQSHVFRDNEKVQERVMDSNDLEKERGITILSKNtAVMYNGVK-----INIVDTPGHA 83
Cdd:PRK07560 20 IRNIGIIAHIDHGKTTLSDNLLAGAGMISEELAGEQLALDFDEEEQARGITIKAAN-VSMVHEYEgkeylINLIDTPGHV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 84 DFGGEVERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINKIDK--------PN---ARPQEVIDEVFDLf 152
Cdd:PRK07560 99 DFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKPVLFINKVDRlikelkltPQemqQRLLKIIKDVNKL- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 153 VELGADDE-----QLDF---PIVYASARGGYA-------KKEVD-------EESDNM----------ECLFDTIIKNVKA 200
Cdd:PRK07560 178 IKGMAPEEfkekwKVDVedgTVAFGSALYNWAisvpmmqKTGIKfkdiidyYEKGKQkelaekaplhEVVLDMVVKHLPN 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 201 PT------------GYIEE-------------PLQLLVTTIDYNEYVGRIGIGKIERGKVAKNQQVTIVdreGNKRNVKV 255
Cdd:PRK07560 258 PIeaqkyripkiwkGDLNSevgkamlncdpngPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLV---GAKKKNRV 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 256 SNLYVYNGLKREEVEEAQLGDIVAVSGIVDINIGETIADPSRPEAVEFIE-IDEPTLSMyfmvndspfagkegeYVTSRH 334
Cdd:PRK07560 335 QQVGIYMGPEREEVEEIPAGNIAAVTGLKDARAGETVVSVEDMTPFESLKhISEPVVTV---------------AIEAKN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 335 LRDrLMKELET-------NVSLKV---EETdsaDSFKVSGRGELHLSILIETMRRE-GYEFQVSKPSVIFHEQDGKKHEP 403
Cdd:PRK07560 400 PKD-LPKLIEVlrqlakeDPTLVVkinEET---GEHLLSGMGELHLEVITYRIKRDyGIEVVTSEPIVVYRETVRGKSQV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 404 IE----------YLTID-VPEEFM-----GVVMEKLGPRKAEMINMSSAVNGYSRLEfripARGLIGFRNE--FMTDTKG 465
Cdd:PRK07560 476 VEgkspnkhnrfYISVEpLEEEVIeaikeGEISEDMDKKEAKILREKLIEAGMDKDE----AKRVWAIYNGnvFIDMTKG 551
|
570
....*....|....*.
gi 1486620076 466 ----NGIMNHVFDGYE 477
Cdd:PRK07560 552 iqylNEVMELIIEGFR 567
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
1-391 |
2.68e-53 |
|
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440248 [Multi-domain] Cd Length: 693 Bit Score: 193.34 E-value: 2.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 1 MNLFTRNDIRNVAIIAHVDHGKTTLVDAMLKQSHVfrdNEKVQE-----RVMDSNDLEKERGITILSKNTAVMYNGVKIN 75
Cdd:COG0480 1 MAEYPLEKIRNIGIVAHIDAGKTTLTERILFYTGA---IHRIGEvhdgnTVMDWMPEEQERGITITSAATTCEWKGHKIN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 76 IVDTPGHADFGGEVERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINKIDKPNARPQEVIDEVFDLF--- 152
Cdd:COG0480 78 IIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQLKERLgan 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 153 ---VEL--GADDeqlDF----------PIVYASARGG-YAKKEVDEE-------------------SDN-MECLF----- 191
Cdd:COG0480 158 pvpLQLpiGAED---DFkgvidlvtmkAYVYDDELGAkYEEEEIPAElkeeaeeareelieavaetDDElMEKYLegeel 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 192 --DTII---------------------KN-------------------VKAPTGYI-------------EEPLQLLV--T 214
Cdd:COG0480 235 teEEIKaglrkatlagkivpvlcgsafKNkgvqplldavvdylpspldVPAIKGVDpdtgeeverkpddDEPFSALVfkT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 215 TIDynEYVGRIGIGKIERGKVAKNQQVTIVdREGNKrnVKVSNLYVYNGLKREEVEEAQLGDIVAVSGIVDINIGETIAD 294
Cdd:COG0480 315 MTD--PFVGKLSFFRVYSGTLKSGSTVYNS-TKGKK--ERIGRLLRMHGNKREEVDEAGAGDIVAVVKLKDTTTGDTLCD 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 295 PSRPEAVEFIEIDEPTLSMyfmvndspfA----GKEGEyvtsrhlrDRLMKEL----ETNVSLKVeETDsADS--FKVSG 364
Cdd:COG0480 390 EDHPIVLEPIEFPEPVISV---------AiepkTKADE--------DKLSTALaklaEEDPTFRV-ETD-EETgqTIISG 450
|
490 500
....*....|....*....|....*...
gi 1486620076 365 RGELHLSILIETMRRE-GYEFQVSKPSV 391
Cdd:COG0480 451 MGELHLEIIVDRLKREfGVEVNVGKPQV 478
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
11-179 |
3.47e-51 |
|
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: 174.41 E-value: 3.47e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 11 NVAIIAHVDHGKTTLVDAMLKQSHVFRDNEKVQERVMDSNDLEKERGITILSKNTAVMYNGVKINIVDTPGHADFGGEVE 90
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 91 RVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINKIDK-PNARPQEVIDEVFDLFVELGAD-DEQLDFPIVY 168
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRvGEEDFDEVLREIKELLKLIGFTfLKGKDVPIIP 160
|
170
....*....|.
gi 1486620076 169 ASARGGYAKKE 179
Cdd:cd00881 161 ISALTGEGIEE 171
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
9-405 |
9.68e-51 |
|
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: 186.64 E-value: 9.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 9 IRNVAIIAHVDHGKTTLVDAMLKQSHVFRDNEKVQERVMDSNDLEKERGITILSKNTAVMY----NGVKINIVDTPGHAD 84
Cdd:TIGR00490 19 IRNIGIVAHIDHGKTTLSDNLLAGAGMISEELAGQQLYLDFDEQEQERGITINAANVSMVHeyegNEYLINLIDTPGHVD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 85 FGGEVERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINKIDK----PNARPQE-------VIDEVFDLFV 153
Cdd:TIGR00490 99 FGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKPVLFINKVDRlineLKLTPQElqerfikIITEVNKLIK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 154 ELGAD---DEQL----DFPIVYASARGGYA------------------------KKEVDEESDNMECLFDTIIKNVKAP- 201
Cdd:TIGR00490 179 AMAPEefrDKWKvrveDGSVAFGSAYYNWAisvpsmkktgigfkdiykyckedkQKELAKKSPLHQVVLDMVIRHLPSPi 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 202 -----------TGYIEE-------------PLQLLVTTIDYNEYVGRIGIGKIERGKVAKNQQVTIVDREGNKRNVKVSn 257
Cdd:TIGR00490 259 eaqkyripviwKGDLNSevgkamlncdpkgPLALMITKIVVDKHAGEVAVGRLYSGTIRPGMEVYIVDRKAKARIQQVG- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 258 lyVYNGLKREEVEEAQLGDIVAVSGIVDINIGETIADPSRP-EAVEFIE-IDEPTLSMYFMVNDSPFAGKegeyvtsrhL 335
Cdd:TIGR00490 338 --VYMGPERVEVDEIPAGNIVAVIGLKDAVAGETICTTVENiTPFESIKhISEPVVTVAIEAKNTKDLPK---------L 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1486620076 336 RDRLMKELETNVSLKVEETDSADSFKVSGRGELHLSILIETMRRE-GYEFQVSKPSVIFHEQDGKKHEPIE 405
Cdd:TIGR00490 407 IEVLRQVAKEDPTVHVEINEETGEHLISGMGELHLEIIVEKIREDyGLDVETSPPIVVYRETVTGTSPVVE 477
|
|
| BipA_III |
cd16263 |
Domain III of GTP-binding protein BipA (TypA); BipA (also called TypA) is a highly conserved ... |
309-387 |
1.58e-50 |
|
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: 169.03 E-value: 1.58e-50
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1486620076 309 PTLSMYFMVNDSPFAGKEGEYVTSRHLRDRLMKELETNVSLKVEETDSADSFKVSGRGELHLSILIETMRREGYEFQVS 387
Cdd:cd16263 1 PTVSMTFGVNTSPFAGREGKFVTSRKIRDRLEKELETNVALRVEETESPDSFIVSGRGELHLSILIETMRREGFELQVS 79
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
4-395 |
4.59e-48 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 178.61 E-value: 4.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 4 FTRNDIRNVAIIAHVDHGKTTLVDAMLKQSHVFRDNEKVQE--RVMDSNDLEKERGITILSKNTAVMYNGVKINIVDTPG 81
Cdd:PRK13351 3 MPLMQIRNIGILAHIDAGKTTLTERILFYTGKIHKMGEVEDgtTVTDWMPQEQERGITIESAATSCDWDNHRINLIDTPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 82 HADFGGEVERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINKIDKPNARPQEVIDE-------------- 147
Cdd:PRK13351 83 HIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLFKVLEDieerfgkrplplql 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 148 ----------VFDLFV--ELGADDEQLDFPIVYASARGGY------AKKEVDEE----SDN-MEC--------------- 189
Cdd:PRK13351 163 pigsedgfegVVDLITepELHFSEGDGGSTVEEGPIPEELleeveeAREKLIEAlaefDDElLELylegeelsaeqlrap 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 190 --------------------------LFDTIIK------NVKAPTGYI------------EEPLQLLVTTIDYNEYVGRI 225
Cdd:PRK13351 243 lregtrsghlvpvlfgsalknigiepLLDAVVDylpsplEVPPPRGSKdngkpvkvdpdpEKPLLALVFKVQYDPYAGKL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 226 GIGKIERGKVAKNQQVTIVDRegnKRNVKVSNLYVYNGLKREEVEEAQLGDIVAVSGIVDINIGETIADPSRPEAVEFIE 305
Cdd:PRK13351 323 TYLRVYSGTLRAGSQLYNGTG---GKREKVGRLFRLQGNKREEVDRAKAGDIVAVAGLKELETGDTLHDSADPVLLELLT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 306 IDEPTLSMYFmvndspfagkEGEYVTSrhlRDRLMKELETNV----SLKVEETDSADSFKVSGRGELHLSILIETMRRE- 380
Cdd:PRK13351 400 FPEPVVSLAV----------EPERRGD---EQKLAEALEKLVwedpSLRVEEDEETGQTILSGMGELHLEVALERLRREf 466
|
490
....*....|....*
gi 1486620076 381 GYEFQVSKPSVIFHE 395
Cdd:PRK13351 467 KLEVNTGKPQVAYRE 481
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
15-395 |
1.34e-47 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 177.24 E-value: 1.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 15 IAHVDHGKTTLVDAMLKQSHVFRDNEKVQE--RVMDSNDLEKERGITILSKNTAVMYNGVKINIVDTPGHADFGGEVERV 92
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRIGEVEDgtTTMDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVERA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 93 LKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINKIDKPNARPQEVIDE------------------------V 148
Cdd:PRK12740 81 LRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRAGADFFRVLAQlqeklgapvvplqlpigegddftgV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 149 FDLF---------------VELGAD-----------------------------DEQLD-----------------FPIV 167
Cdd:PRK12740 161 VDLLsmkayrydeggpseeIEIPAElldraeeareellealaefddelmekyleGEELSeeeikaglrkatlageiVPVF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 168 YASARGGYAKKE-----VDE-----ESDNMECLfDTIIKNVKAPTGyiEEPLQLLV--TTIDynEYVGRIGIGKIERGKV 235
Cdd:PRK12740 241 CGSALKNKGVQRlldavVDYlpsplEVPPVDGE-DGEEGAELAPDP--DGPLVALVfkTMDD--PFVGKLSLVRVYSGTL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 236 AKNQQVTIVDREgnkRNVKVSNLYVYNGLKREEVEEAQLGDIVAVSGIVDINIGETIADPSRPEAVEFIEIDEPTLSMyf 315
Cdd:PRK12740 316 KKGDTLYNSGTG---KKERVGRLYRMHGKQREEVDEAVAGDIVAVAKLKDAATGDTLCDKGDPILLEPMEFPEPVISL-- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 316 mvndspfAgkegeyVTSRHLRD---------RLMKEletNVSLKVE-ETDSADSFkVSGRGELHLSILIETMRRE-GYEF 384
Cdd:PRK12740 391 -------A------IEPKDKGDeeklsealgKLAEE---DPTLRVErDEETGQTI-LSGMGELHLDVALERLKREyGVEV 453
|
490
....*....|.
gi 1486620076 385 QVSKPSVIFHE 395
Cdd:PRK12740 454 ETGPPQVPYRE 464
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
10-201 |
3.23e-45 |
|
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: 158.08 E-value: 3.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 10 RNVAIIAHVDHGKTTLVDAMLKQSHVFRDNEKvQERVMDSNDLEKERGITILSKNTAVMYNGVK-----INIVDTPGHAD 84
Cdd:cd01890 1 RNFSIIAHIDHGKSTLADRLLELTGTVSEREM-KEQVLDSMDLERERGITIKAQAVRLFYKAKDgeeylLNLIDTPGHVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 85 FGGEVERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINKIDKPNARPQEVIDEVFDLfveLGADDEQldf 164
Cdd:cd01890 80 FSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVKQEIEDV---LGLDASE--- 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 1486620076 165 pIVYASARGGYakkevdeesdNMECLFDTIIKNVKAP 201
Cdd:cd01890 154 -AILVSAKTGL----------GVEDLLEAIVERIPPP 179
|
|
| 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 |
4.71e-45 |
|
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: 154.20 E-value: 4.71e-45
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1486620076 402 EPIEYLTIDVPEEFMGVVMEKLGPRKAEMINMSSAVNGYSRLEFRIPARGLIGFRNEFMTDTKGNGIMNHVFDGYEPFK 480
Cdd:cd03710 1 EPIEELTIDVPEEYSGAVIEKLGKRKGEMVDMEPDGNGRTRLEFKIPSRGLIGFRSEFLTDTRGTGIMNHVFDGYEPYK 79
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
10-136 |
4.29e-40 |
|
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: 145.45 E-value: 4.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 10 RNVAIIAHVDHGKTTLVDAMLKQSHVFRDNEKVQERVMDSNDLEKERGITIlsKNTAV-MY----------NGVKINIVD 78
Cdd:cd01885 1 RNICIIAHVDHGKTTLSDSLLASAGIISEKLAGKARYLDTREDEQERGITI--KSSAIsLYfeyeeekmdgNDYLINLID 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1486620076 79 TPGHADFGGEVERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINKIDK 136
Cdd:cd01885 79 SPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDR 136
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
209-300 |
1.41e-38 |
|
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: 136.93 E-value: 1.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 209 LQLLVTTIDYNEYVGRIGIGKIERGKVAKNQQVTIVDREGNKRNVKVSNLYVYNGLKREEVEEAQLGDIVAVSGIVDINI 288
Cdd:cd03691 1 FQMLVTTLDYDDYLGRIAIGRIFSGTVKVGQQVTVVDEDGKIEKGRVTKLFGFEGLERVEVEEAEAGDIVAIAGLEDITI 80
|
90
....*....|..
gi 1486620076 289 GETIADPSRPEA 300
Cdd:cd03691 81 GDTICDPEVPEP 92
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
11-148 |
4.79e-37 |
|
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.
Pssm-ID: 206731 [Multi-domain] Cd Length: 237 Bit Score: 137.75 E-value: 4.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 11 NVAIIAHVDHGKTTLVDAMLKQSHVFRDNEKVQE--RVMDSNDLEKERGITILSKNTAVMYNGVKINIVDTPGHADFGGE 88
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIRELGSVDKgtTRTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIAE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1486620076 89 VERVLKMVDSVVLVVDAYEGPMPQTKfVLKKALELHLRP-IVVINKIDKPNARPQEVIDEV 148
Cdd:cd04168 81 VERSLSVLDGAILVISAVEGVQAQTR-ILFRLLRKLNIPtIIFVNKIDRAGADLEKVYQEI 140
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
11-148 |
1.81e-32 |
|
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: 126.07 E-value: 1.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 11 NVAIIAHVDHGKTTLVDAMLKQSHVFRDNEKVQER--VMDSNDLEKERGITILSKNTAVMYNGVKINIVDTPGHADFGGE 88
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGRIHKIGEVHGGgaTMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDFTIE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 89 VERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINKIDKPNARPQEVIDEV 148
Cdd:cd01886 81 VERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQI 140
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
6-136 |
1.14e-31 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 130.94 E-value: 1.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 6 RNDIRNVAIIAHVDHGKTTLVDAMLKQSHVFRDNEKVQERVMDSNDLEKERGITIlsKNTAV-------MYNGVK----- 73
Cdd:PTZ00416 16 PDQIRNMSVIAHVDHGKSTLTDSLVCKAGIISSKNAGDARFTDTRADEQERGITI--KSTGIslyyehdLEDGDDkqpfl 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1486620076 74 INIVDTPGHADFGGEVERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINKIDK 136
Cdd:PTZ00416 94 INLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKVDR 156
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
10-201 |
1.13e-30 |
|
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: 119.30 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 10 RNVAIIAHVDHGKTTLVDAMLKQSH----VFRDNEKvQERVMDSNDLEKERGITILSKNTAVMYNGVK-----INIVDTP 80
Cdd:cd04167 1 RNVCIAGHLHHGKTSLLDMLIEQTHkrtpSVKLGWK-PLRYTDTRKDEQERGISIKSNPISLVLEDSKgksylINIIDTP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 81 GHADFGGEVERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINKIDK--------PN---ARPQEVIDEVF 149
Cdd:cd04167 80 GHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDRlilelklpPTdayYKLRHTIDEIN 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1486620076 150 DLFVELGADDEQLDFP----IVYASARGGYakKEVDEESDNMECLFDTIIKNVKAP 201
Cdd:cd04167 160 NYIASFSTTEGFLVSPelgnVLFASSKFGF--CFTLESFAKKYGLVDSILSHIPSP 213
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
10-148 |
6.91e-28 |
|
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: 113.07 E-value: 6.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 10 RNVAIIAHVDHGKTTLVDAMLKQSHVFRDNEKVQER------VMDSNDLEKERGITIlskNTAVM---YNGVKINIVDTP 80
Cdd:cd04169 3 RTFAIISHPDAGKTTLTEKLLLFGGAIQEAGAVKARksrkhaTSDWMEIEKQRGISV---TSSVMqfeYKGCVINLLDTP 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1486620076 81 GHADFGGEVERVLKMVDSVVLVVDAYEGPMPQTkfvlKKALE---LHLRPIV-VINKIDKPNARPQEVIDEV 148
Cdd:cd04169 80 GHEDFSEDTYRTLTAVDSAVMVIDAAKGVEPQT----RKLFEvcrLRGIPIItFINKLDREGRDPLELLDEI 147
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
11-152 |
8.00e-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: 112.69 E-value: 8.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 11 NVAIIAHVDHGKTTLVDAMLKQSHVFRDNEKVQE--RVMDSNDLEKERGITILSKNTAVMYNGVKINIVDTPGHADFGGE 88
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRLGRVEDgnTVSDYDPEEKKRKMSIETSVAPLEWNGHKINLIDTPGYADFVGE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1486620076 89 VERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINKIDKPNARPQEVIDEVFDLF 152
Cdd:cd04170 81 TLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRARADFDKTLAALREAF 144
|
|
| EFG_C |
pfam00679 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
399-486 |
1.53e-27 |
|
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: 106.09 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 399 KKHEPIEYLTIDVPEEFMGVVMEKLGPRKAEMINMSSAVNGYSRLEFRIPARGLIGFRNEFMTDTKGNGIMNHVFDGYEP 478
Cdd:pfam00679 1 VLLEPIEKVTIDVPEEYVGDVISDLNSRRGEILDMDPDDGGRVVIEAEVPLAELFGFATELRSLTKGRGSFSMEFSGYQP 80
|
....*...
gi 1486620076 479 FKGEIPGR 486
Cdd:pfam00679 81 VPGDILDR 88
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
6-136 |
9.15e-27 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 115.98 E-value: 9.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 6 RNDIRNVAIIAHVDHGKTTLVDAMLKQSHVFRDNEKVQERVMDSNDLEKERGITILSKNTAVMY---------------- 69
Cdd:PLN00116 16 KHNIRNMSVIAHVDHGKSTLTDSLVAAAGIIAQEVAGDVRMTDTRADEAERGITIKSTGISLYYemtdeslkdfkgerdg 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1486620076 70 NGVKINIVDTPGHADFGGEVERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINKIDK 136
Cdd:PLN00116 96 NEYLINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTETVLRQALGERIRPVLTVNKMDR 162
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
11-304 |
3.78e-24 |
|
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: 105.40 E-value: 3.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 11 NVAIIAHVDHGKTTLVDAMLKQS-----HVFRDNEKVQER----------VMDSNDLEKERGITI-LSK---NTAVMYng 71
Cdd:COG5256 9 NLVVIGHVDHGKSTLVGRLLYETgaideHIIEKYEEEAEKkgkesfkfawVMDRLKEERERGVTIdLAHkkfETDKYY-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 72 vkINIVDTPGHADFggeverVLKMV------DSVVLVVDAYEGPMPQTK--FVLKKALELHlRPIVVINKIDKPN---AR 140
Cdd:COG5256 87 --FTIIDAPGHRDF------VKNMItgasqaDAAILVVSAKDGVMGQTRehAFLARTLGIN-QLIVAVNKMDAVNyseKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 141 PQEVIDEVFDLFVELGADDEqlDFPIVYASArggYAKKEVDEESDNM-----ECLFDTiIKNVKAPTGYIEEPLQLLVTT 215
Cdd:COG5256 158 YEEVKEEVSKLLKMVGYKVD--KIPFIPVSA---WKGDNVVKKSDNMpwyngPTLLEA-LDNLKEPEKPVDKPLRIPIQD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 216 IdYN-EYVGRIGIGKIERGKVAKNQQVtIVDREGNKRNVKVSNLYvynglkREEVEEAQLGDIV--AVSGIV--DINIGE 290
Cdd:COG5256 232 V-YSiSGIGTVPVGRVETGVLKVGDKV-VFMPAGVVGEVKSIEMH------HEELEQAEPGDNIgfNVRGVEknDIKRGD 303
|
330
....*....|....*.
gi 1486620076 291 TIADPSRPEAV--EFI 304
Cdd:COG5256 304 VAGHPDNPPTVaeEFT 319
|
|
| Elongation_Factor_C |
cd01514 |
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ... |
402-478 |
4.61e-24 |
|
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: 96.01 E-value: 4.61e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1486620076 402 EPIEYLTIDVPEEFMGVVMEKLGPRKAEMINMSSAVNGYSRLEFRIPARGLIGFRNEFMTDTKGNGIMNHVFDGYEP 478
Cdd:cd01514 1 EPIMKVEITVPEEYLGAVIGDLSKRRGEILGMEPRGTGRVVIKAELPLAEMFGFATDLRSLTQGRASFSMEFSHYEP 77
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
11-280 |
6.33e-23 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 101.17 E-value: 6.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 11 NVAIIAHVDHGKTTLVDAMLKQSHVFRDNEKVQERVMDSNDLEKERGITIlskNTA-VMYNGVKINI--VDTPGHADFgg 87
Cdd:PRK12736 14 NIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITI---NTAhVEYETEKRHYahVDCPGHADY-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 88 everVLKMV------DSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVV-INKIDKPNArpQEVID----EVFDLFVELG 156
Cdd:PRK12736 89 ----VKNMItgaaqmDGAILVVAATDGPMPQTREHILLARQVGVPYLVVfLNKVDLVDD--EELLElvemEVRELLSEYD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 157 ADDEqlDFPIVYASARGgyAKKEVDEESDNMECLFDTIIKNVKAPTGYIEEPLqLL----VTTIdyneyVGR--IGIGKI 230
Cdd:PRK12736 163 FPGD--DIPVIRGSALK--ALEGDPKWEDAIMELMDAVDEYIPTPERDTDKPF-LMpvedVFTI-----TGRgtVVTGRV 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1486620076 231 ERGKVAKNQQVTIVdreGNKRNVKVsnlyVYNGLK--REEVEEAQLGDIVAV 280
Cdd:PRK12736 233 ERGTVKVGDEVEIV---GIKETQKT----VVTGVEmfRKLLDEGQAGDNVGV 277
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
11-303 |
5.04e-22 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 98.84 E-value: 5.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 11 NVAIIAHVDHGKTTLVDAMLKQS-----HVFRDNEKVQER----------VMDSNDLEKERGITILSKNTAVMYNGVKIN 75
Cdd:PRK12317 8 NLAVIGHVDHGKSTLVGRLLYETgaideHIIEELREEAKEkgkesfkfawVMDRLKEERERGVTIDLAHKKFETDKYYFT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 76 IVDTPGHADFggeverVLKMV------DSVVLVVDAYE--GPMPQTK--FVLKKAL---ELhlrpIVVINKIDKPN---A 139
Cdd:PRK12317 88 IVDCPGHRDF------VKNMItgasqaDAAVLVVAADDagGVMPQTRehVFLARTLginQL----IVAINKMDAVNydeK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 140 RPQEVIDEVFDLFVELGADDEqlDFPIVYASARGGyakKEVDEESDNM-----ECLFDTiIKNVKAPTGYIEEPLQLL-- 212
Cdd:PRK12317 158 RYEEVKEEVSKLLKMVGYKPD--DIPFIPVSAFEG---DNVVKKSENMpwyngPTLLEA-LDNLKPPEKPTDKPLRIPiq 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 213 -VTTIDyneYVGRIGIGKIERGKVAKNQQVTIV--DREGNKRNVKvsnlyvyngLKREEVEEAQLGDIV--AVSGIV--D 285
Cdd:PRK12317 232 dVYSIS---GVGTVPVGRVETGVLKVGDKVVFMpaGVVGEVKSIE---------MHHEELPQAEPGDNIgfNVRGVGkkD 299
|
330 340
....*....|....*....|
gi 1486620076 286 INIGETIADPSRPEAV--EF 303
Cdd:PRK12317 300 IKRGDVCGHPDNPPTVaeEF 319
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
12-174 |
9.62e-22 |
|
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: 92.54 E-value: 9.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 12 VAIIAHVDHGKTTLVDAMLKqshvfrdnekvqervmdSNDLEKE-RGITILSKNTAVMYNGV--KINIVDTPGHADFGGE 88
Cdd:cd01887 3 VTVMGHVDHGKTTLLDKIRK-----------------TNVAAGEaGGITQHIGAYQVPIDVKipGITFIDTPGHEAFTNM 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 89 VERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINKIDKPNARpQEVIDEVFDLFVELGADDEQL--DFPI 166
Cdd:cd01887 66 RARGASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKPYGT-EADPERVKNELSELGLVGEEWggDVSI 144
|
....*...
gi 1486620076 167 VYASARGG 174
Cdd:cd01887 145 VPISAKTG 152
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
11-280 |
2.03e-21 |
|
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: 96.76 E-value: 2.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 11 NVAIIAHVDHGKTTLVDAMLKQSHVFRDNEKVQERVMDSNDLEKERGITIlskNTA-VMYNGVKINI--VDTPGHADFgg 87
Cdd:COG0050 14 NIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITI---NTShVEYETEKRHYahVDCPGHADY-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 88 everVLKMV------DSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVV-INKIDKpnARPQEVID----EVFDLFVELG 156
Cdd:COG0050 89 ----VKNMItgaaqmDGAILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKCDM--VDDEELLElvemEVRELLSKYG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 157 ADDEqlDFPIVYASARGGYAKKEVDEESDNMECLFDTIIKNVKAPTGYIEEPLqLL----VTTIDyneyvGR--IGIGKI 230
Cdd:COG0050 163 FPGD--DTPIIRGSALKALEGDPDPEWEKKILELMDAVDSYIPEPERDTDKPF-LMpvedVFSIT-----GRgtVVTGRV 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1486620076 231 ERGKVAKNQQVTIVdreGNKRNVKVsnlyVYNGLK--REEVEEAQLGDIVAV 280
Cdd:COG0050 235 ERGIIKVGDEVEIV---GIRDTQKT----VVTGVEmfRKLLDEGEAGDNVGL 279
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
10-148 |
3.32e-21 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 97.51 E-value: 3.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 10 RNVAIIAHVDHGKTTLVDAMLKQSHVFRDNEKVQER------VMDSNDLEKERGITILSkntAVM---YNGVKINIVDTP 80
Cdd:PRK00741 11 RTFAIISHPDAGKTTLTEKLLLFGGAIQEAGTVKGRksgrhaTSDWMEMEKQRGISVTS---SVMqfpYRDCLINLLDTP 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1486620076 81 GHADFGGEVERVLKMVDSVVLVVDAYEGPMPQTkfvlKKALEL-HLR--PIVV-INKIDKPNARPQEVIDEV 148
Cdd:PRK00741 88 GHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQT----RKLMEVcRLRdtPIFTfINKLDRDGREPLELLDEI 155
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
4-295 |
3.98e-20 |
|
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: 92.92 E-value: 3.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 4 FTRNDIR-NVAIIAHVDHGKTTLVDAMlkqSHVFRDNEKVQERVMDSNDL---EKERGITIlskNTA-VMYNGVKINI-- 76
Cdd:TIGR00485 6 FERTKPHvNVGTIGHVDHGKTTLTAAI---TTVLAKEGGAAARAYDQIDNapeEKARGITI---NTAhVEYETETRHYah 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 77 VDTPGHADFGGEVERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVV-INKIDKpnARPQEVID----EVFDL 151
Cdd:TIGR00485 80 VDCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKCDM--VDDEELLElvemEVREL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 152 FVELGADDEqlDFPIVYASARGgyAKKEVDEESDNMECLFDTIIKNVKAPTGYIEEPLQLLVTTIDYNEYVGRIGIGKIE 231
Cdd:TIGR00485 158 LSQYDFPGD--DTPIIRGSALK--ALEGDAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVE 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1486620076 232 RGKVAKNQQVTIVDREGNKRNVkVSNLYVYnglkREEVEEAQLGDIVAV--SGI--VDINIGETIADP 295
Cdd:TIGR00485 234 RGIIKVGEEVEIVGLKDTRKTT-VTGVEMF----RKELDEGRAGDNVGLllRGIkrEEIERGMVLAKP 296
|
|
| tufA |
CHL00071 |
elongation factor Tu |
11-295 |
1.10e-19 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 91.56 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 11 NVAIIAHVDHGKTTLVDAMLKQSHVFRDNEKVQERVMDSNDLEKERGITIlskNTA-VMYNGVKINI--VDTPGHADFgg 87
Cdd:CHL00071 14 NIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITI---NTAhVEYETENRHYahVDCPGHADY-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 88 everVLKM------VDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVV-INKIDKpnarpqeVIDEVFDLFVELGADD- 159
Cdd:CHL00071 89 ----VKNMitgaaqMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVfLNKEDQ-------VDDEELLELVELEVREl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 160 -EQLDF-----PIVYASA--------RGGYAKKEVDEESDNMECLFDTIIKNVKAPTGYIEEPLQLLVTTIDYNEYVGRI 225
Cdd:CHL00071 158 lSKYDFpgddiPIVSGSAllalealtENPKIKRGENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTV 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1486620076 226 GIGKIERGKVAKNQQVTIVDReGNKRNVKVSNLYVYNglkrEEVEEAQLGDIVAVS--GI--VDINIGETIADP 295
Cdd:CHL00071 238 ATGRIERGTVKVGDTVEIVGL-RETKTTTVTGLEMFQ----KTLDEGLAGDNVGILlrGIqkEDIERGMVLAKP 306
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
11-244 |
1.96e-19 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 90.63 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 11 NVAIIAHVDHGKTTLVDAMLKQSHVFRDNEKVQERVMDSNDLEKERGITIlskNTA-VMYNGVKINI--VDTPGHADFgg 87
Cdd:PRK00049 14 NVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITI---NTAhVEYETEKRHYahVDCPGHADY-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 88 everVLKMV------DSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVV-INKIDKpnARPQEVID----EVFDLFVELG 156
Cdd:PRK00049 89 ----VKNMItgaaqmDGAILVVSAADGPMPQTREHILLARQVGVPYIVVfLNKCDM--VDDEELLElvemEVRELLSKYD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 157 ADDEqlDFPIVYASarggyAKKEVDEESDNMEClfDTIIKNVKAPTGYIEEPLQ------LL----VTTIDyneyvGR-- 224
Cdd:PRK00049 163 FPGD--DTPIIRGS-----ALKALEGDDDEEWE--KKILELMDAVDSYIPTPERaidkpfLMpiedVFSIS-----GRgt 228
|
250 260
....*....|....*....|
gi 1486620076 225 IGIGKIERGKVAKNQQVTIV 244
Cdd:PRK00049 229 VVTGRVERGIIKVGEEVEIV 248
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
1-274 |
3.46e-19 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 90.65 E-value: 3.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 1 MNLFTRNDIR-NVAIIAHVDHGKTTLVDAMLKqshVFRDNEKVQERVMDSNDL---EKERGITIlskNTA-VMYNGVKIN 75
Cdd:PLN03127 52 MATFTRTKPHvNVGTIGHVDHGKTTLTAAITK---VLAEEGKAKAVAFDEIDKapeEKARGITI---ATAhVEYETAKRH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 76 I--VDTPGHADFGGEVERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVV-INKIDKpnarpqeVIDEVFDLF 152
Cdd:PLN03127 126 YahVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVfLNKVDV-------VDDEELLEL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 153 VELGAdDEQLDF--------PIVYASARGgyAKKEVDEE--SDNMECLFDTIIKNVKAPTGYIEEPLQLLVTTIDYNEYV 222
Cdd:PLN03127 199 VEMEL-RELLSFykfpgdeiPIIRGSALS--ALQGTNDEigKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGR 275
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 223 GRIGIGKIERGKVAKNQQVTIVD-REGNKRNVKVSNLYVYN-----------------GLKREEVEEAQL 274
Cdd:PLN03127 276 GTVATGRVEQGTIKVGEEVEIVGlRPGGPLKTTVTGVEMFKkildqgqagdnvglllrGLKREDVQRGQV 345
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
11-295 |
3.65e-18 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 87.75 E-value: 3.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 11 NVAIIAHVDHGKTTLVDAMLKQSHVFRDNEKVQERVMDSNDLEKERGITIlskNTA-VMYNGVKINI--VDTPGHADFGG 87
Cdd:PLN03126 83 NIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITI---NTAtVEYETENRHYahVDCPGHADYVK 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 88 EVERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVV-INKIDkpnarpqEVIDEVFDLFVELGADD------- 159
Cdd:PLN03126 160 NMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVfLNKQD-------QVDDEELLELVELEVREllssyef 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 160 EQLDFPIVYASARGGYA--------KKEVDEESDNMECLFDTIIKNVKAPTGYIEEPLQLLVTTIDYNEYVGRIGIGKIE 231
Cdd:PLN03126 233 PGDDIPIISGSALLALEalmenpniKRGDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVE 312
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1486620076 232 RGKVAKNQQVTIVDReGNKRNVKVSNLYVYnglkREEVEEAQLGDIVAV--SGI--VDINIGETIADP 295
Cdd:PLN03126 313 RGTVKVGETVDIVGL-RETRSTTVTGVEMF----QKILDEALAGDNVGLllRGIqkADIQRGMVLAKP 375
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
11-171 |
7.62e-18 |
|
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.
Pssm-ID: 206671 [Multi-domain] Cd Length: 195 Bit Score: 81.86 E-value: 7.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 11 NVAIIAHVDHGKTTLVDAMLKQSHVFRDNEKVQERVMDSNDLEKERGITIlskNTA-VMYNGVKINI--VDTPGHADFgg 87
Cdd:cd01884 4 NVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITI---NTAhVEYETANRHYahVDCPGHADY-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 88 everVLKMV------DSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVV-INKIDKpnARPQEVID----EVFDLFVELG 156
Cdd:cd01884 79 ----IKNMItgaaqmDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVfLNKADM--VDDEELLElvemEVRELLSKYG 152
|
170
....*....|....*
gi 1486620076 157 ADDEqlDFPIVYASA 171
Cdd:cd01884 153 FDGD--DTPIVRGSA 165
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
11-280 |
9.54e-18 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 85.66 E-value: 9.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 11 NVAIIAHVDHGKTTLVDAMLKqshVFRDNEKVQERVMDSNDL---EKERGITIlskNTA-VMYNGVKINI--VDTPGHAD 84
Cdd:PRK12735 14 NVGTIGHVDHGKTTLTAAITK---VLAKKGGGEAKAYDQIDNapeEKARGITI---NTShVEYETANRHYahVDCPGHAD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 85 FggeverVLKMV------DSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVV-INKIDKpnARPQEVID----EVFDLFV 153
Cdd:PRK12735 88 Y------VKNMItgaaqmDGAILVVSAADGPMPQTREHILLARQVGVPYIVVfLNKCDM--VDDEELLElvemEVRELLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 154 ELGADDEqlDFPIVYASARGGYAKKEVDEESDNMECLFDTIIKNVKAPTGYIEEPLQLLVttidynEYV------GRIGI 227
Cdd:PRK12735 160 KYDFPGD--DTPIIRGSALKALEGDDDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPI------EDVfsisgrGTVVT 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1486620076 228 GKIERGKVAKNQQVTIVdreGNKRNVKVsnlyVYNGLK--REEVEEAQLGDIVAV 280
Cdd:PRK12735 232 GRVERGIVKVGDEVEIV---GIKETQKT----TVTGVEmfRKLLDEGQAGDNVGV 279
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
14-306 |
1.29e-17 |
|
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 442507 [Multi-domain] Cd Length: 630 Bit Score: 86.51 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 14 IIA---HVDHGKTTLVDAM-------LKQshvfrdnekvqervmdsndlEKERGITI--------LSkntavmyNGVKIN 75
Cdd:COG3276 2 IIGtagHIDHGKTTLVKALtgidtdrLKE--------------------EKKRGITIdlgfaylpLP-------DGRRLG 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 76 IVDTPGHADF--------GGevervlkmVDSVVLVVDAYEGPMPQTKfvlkkalElHL---------RPIVVINKIDK-P 137
Cdd:COG3276 55 FVDVPGHEKFiknmlagaGG--------IDLVLLVVAADEGVMPQTR-------E-HLaildllgikRGIVVLTKADLvD 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 138 NARPQEVIDEVFDLFVELGADdeqlDFPIVYASARGGYAKKEVDEEsdnmeclFDTIIKNVKAPTgyIEEPLQL------ 211
Cdd:COG3276 119 EEWLELVEEEIRELLAGTFLE----DAPIVPVSAVTGEGIDELRAA-------LDALAAAVPARD--ADGPFRLpidrvf 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 212 ------LVTTidyneyvgrigiGKIERGKVAKNQQVTIVdrEGNKRnVKVSNLYVYNglkrEEVEEAQLGDIVAV--SGI 283
Cdd:COG3276 186 sikgfgTVVT------------GTLLSGTVRVGDELELL--PSGKP-VRVRGIQVHG----QPVEEAYAGQRVALnlAGV 246
|
330 340
....*....|....*....|....*
gi 1486620076 284 --VDINIGETIADPSRPEAVEFIEI 306
Cdd:COG3276 247 ekEEIERGDVLAAPGALRPTDRIDV 271
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
12-147 |
2.54e-17 |
|
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: 85.07 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 12 VAIIAHVDHGKTTLVDAmLKQSHVfrdnekvqervmdsndLEKE-RGIT--IlsknTA--VMYNGVKINIVDTPGHADF- 85
Cdd:COG0532 7 VTVMGHVDHGKTSLLDA-IRKTNV----------------AAGEaGGITqhI----GAyqVETNGGKITFLDTPGHEAFt 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1486620076 86 -----GGEVervlkmVDSVVLVVDAYEGPMPQTKfvlkKALElHLR----PIVV-INKIDKPNARPQEVIDE 147
Cdd:COG0532 66 amrarGAQV------TDIVILVVAADDGVMPQTI----EAIN-HAKaagvPIIVaINKIDKPGANPDRVKQE 126
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
12-147 |
9.37e-17 |
|
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]
Pssm-ID: 273102 [Multi-domain] Cd Length: 587 Bit Score: 83.66 E-value: 9.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 12 VAIIAHVDHGKTTLVDAMLKqshvfrdnekvqervmdSNDLEKERG-ITI-LSKNTAVMYNGVKINIVDTPGHADFGGEV 89
Cdd:TIGR00487 90 VTIMGHVDHGKTSLLDSIRK-----------------TKVAQGEAGgITQhIGAYHVENEDGKMITFLDTPGHEAFTSMR 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1486620076 90 ERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINKIDKPNARPQEVIDE 147
Cdd:TIGR00487 153 ARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVPIIVAINKIDKPEANPDRVKQE 210
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
17-189 |
1.79e-16 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.
Pssm-ID: 206734 [Multi-domain] Cd Length: 170 Bit Score: 77.26 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 17 HVDHGKTTLVDAMLKQshvfrDNEKVQErvmdsndlEKERGITI-LSKNTAVMYNGVKINIVDTPGHADFggeverVLKM 95
Cdd:cd04171 7 HIDHGKTTLIKALTGI-----ETDRLPE--------EKKRGITIdLGFAYLDLPDGKRLGFIDVPGHEKF------VKNM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 96 V------DSVVLVVDAYEGPMPQTKFVLK--KALELHlRPIVVINKIDK-PNARPQEVIDEVFDLFVELGADDEqldfPI 166
Cdd:cd04171 68 LagaggiDAVLLVVAADEGIMPQTREHLEilELLGIK-KGLVVLTKADLvDEDRLELVEEEILELLAGTFLADA----PI 142
|
170 180
....*....|....*....|...
gi 1486620076 167 VYASARGGYAKKEVDEESDNMEC 189
Cdd:cd04171 143 FPVSSVTGEGIEELKNYLDELAE 165
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
2-202 |
5.65e-16 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 81.42 E-value: 5.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 2 NLFTRNDIRN---VAIIAHVDHGKTTLVDAMLKqshvfrdnekvqervmdSNDLEKER-GIT--ILSKNTAVMYNGVKIN 75
Cdd:CHL00189 234 SAFTENSINRppiVTILGHVDHGKTTLLDKIRK-----------------TQIAQKEAgGITqkIGAYEVEFEYKDENQK 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 76 IV--DTPGHADFGGEVERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINKIDKPNARPQEVIDEV--FDL 151
Cdd:CHL00189 297 IVflDTPGHEAFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANTERIKQQLakYNL 376
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1486620076 152 FVE-LGAddeqlDFPIVYASARGGYakkevdeesdNMECLFDTI-----IKNVKA-PT 202
Cdd:CHL00189 377 IPEkWGG-----DTPMIPISASQGT----------NIDKLLETIlllaeIEDLKAdPT 419
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
11-187 |
6.99e-16 |
|
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: 76.76 E-value: 6.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 11 NVAIIAHVDHGKTTLVDAML--------KQSHVFRDNEKVQER-------VMDSNDLEKERGITIlskNTAVMY---NGV 72
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLyklggvdkRTIEKYEKEAKEMGKesfkyawVLDKLKEERERGVTI---DVGLAKfetEKY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 73 KINIVDTPGHADFggeverVLKMV------DSVVLVVDAYEG-------PMPQTK--FVLKKALEL-HLrpIVVINKIDK 136
Cdd:cd01883 78 RFTIIDAPGHRDF------VKNMItgasqaDVAVLVVSARKGefeagfeKGGQTRehALLARTLGVkQL--IVAVNKMDD 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1486620076 137 PN-----ARPQEVIDEVFDLFVELGADDEQLDF-PIvyasarGGYAKKEVDEESDNM 187
Cdd:cd01883 150 VTvnwsqERYDEIKKKVSPFLKKVGYNPKDVPFiPI------SGFTGDNLIEKSENM 200
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
9-140 |
1.08e-15 |
|
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: 74.72 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 9 IRNVAIIAHVDHGKTTLVDAmLKQSHVFRDNEKVQERVMDSNDLEKERGITIlskntavmyngvKINIVDTPGHADF--- 85
Cdd:TIGR00231 1 DIKIVIVGHPNVGKSTLLNS-LLGNKGSITEYYPGTTRNYVTTVIEEDGKTY------------KFNLLDTAGQEDYdai 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1486620076 86 ----GGEVERVLKMVDSVVLVVDAYEGPMPQTKfVLKKALELHLRPIVVINKIDKPNAR 140
Cdd:TIGR00231 68 rrlyYPQVERSLRVFDIVILVLDVEEILEKQTK-EIIHHADSGVPIILVGNKIDLKDAD 125
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
11-185 |
4.24e-15 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.
Pssm-ID: 206676 [Multi-domain] Cd Length: 192 Bit Score: 73.94 E-value: 4.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 11 NVAIIAHVDHGKTTLVDAMlkqshvfrdNEKVQERVMDSNDLEKERGITI--------------LSKNTAVMYNGVKINI 76
Cdd:cd01889 2 NVGLLGHVDSGKTSLAKAL---------SEIASTAAFDKNPQSQERGITLdlgfssfevdkpkhLEDNENPQIENYQITL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 77 VDTPGHADF-----GGEvervlKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINKIDK-PNARPQEVIDEVFD 150
Cdd:cd01889 73 VDCPGHASLirtiiGGA-----QIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDLiPEEERKRKIEKMKK 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 1486620076 151 LFVELGADDEQLDFPIVYASAR-GGYAKKEVDEESD 185
Cdd:cd01889 148 RLQKTLEKTRLKDSPIIPVSAKpGEGEAELGGELKN 183
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
13-196 |
5.91e-15 |
|
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: 72.87 E-value: 5.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 13 AIIAHVDHGKTTLVDAMLKQSHVFRDNEKVQERVMDSNDLEKErgitilskntavmYNGVKINIVDTPGHADFGG----- 87
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPDVYVKELD-------------KGKVKLVLVDTPGLDEFGGlgree 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 88 EVERVLKMVDSVVLVVDA--YEGPMPQTKFVLKKALELHLRPIVVINKIDKPNARPQEVIDEVFDLFvelgaddEQLDFP 165
Cdd:cd00882 68 LARLLLRGADLILLVVDStdRESEEDAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELA-------KILGVP 140
|
170 180 190
....*....|....*....|....*....|.
gi 1486620076 166 IVYASARGGYakkEVDEesdnmecLFDTIIK 196
Cdd:cd00882 141 VFEVSAKTGE---GVDE-------LFEKLIE 161
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
11-281 |
2.35e-14 |
|
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]
Pssm-ID: 129567 [Multi-domain] Cd Length: 581 Bit Score: 76.07 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 11 NVAIIAHVDHGKTTLVDAMLKqshvfrdnekvqervMDSNDL--EKERGITILSKNTAVMYNGVKINIVDTPGHADFGGE 88
Cdd:TIGR00475 2 IIATAGHVDHGKTTLLKALTG---------------IAADRLpeEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 89 VERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRP-IVVINKIDKPNarpQEVIDEVFDLFVELGADDEQL-DFPI 166
Cdd:TIGR00475 67 AIAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHtIVVITKADRVN---EEEIKRTEMFMKQILNSYIFLkNAKI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 167 VYASARGGYAKKEVDEESDNMECLFDTIIKNvkaptgyieEPLQLLVTTIDYNEYVGRIGIGKIERGKVAKNQQVTIvdr 246
Cdd:TIGR00475 144 FKTSAKTGQGIGELKKELKNLLESLDIKRIQ---------KPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRL--- 211
|
250 260 270
....*....|....*....|....*....|....*
gi 1486620076 247 EGNKRNVKVSNLYVYNglkrEEVEEAQLGDIVAVS 281
Cdd:TIGR00475 212 LPINHEVRVKAIQAQN----QDVEIAYAGQRIALN 242
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
11-187 |
2.08e-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: 63.74 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 11 NVAIIAHVDHGKTTLVDAMLKQS-HVFRDN-EKVQER--------------VMDSNDLEKERGITIlskNTAVMY---NG 71
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSkSIFEDQlAALERSkssgtqgekldlalLVDGLQAEREQGITI---DVAYRYfstPK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 72 VKINIVDTPGHADFggevervLK-MV------DSVVLVVDAYEGPMPQTK---FVLkkALeLHLRPIVV-INKIDKPNAR 140
Cdd:cd04166 78 RKFIIADTPGHEQY-------TRnMVtgastaDLAILLVDARKGVLEQTRrhsYIA--SL-LGIRHVVVaVNKMDLVDYD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1486620076 141 pQEVIDEVFDLFVELGAddeQLDFPIVYA---SARGGyakKEVDEESDNM 187
Cdd:cd04166 148 -EEVFEEIKADYLAFAA---SLGIEDITFipiSALEG---DNVVSRSENM 190
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
8-196 |
3.55e-11 |
|
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: 62.06 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 8 DIRNVAIIAHVDHGKTTLVDAMLKQshvfrdnekvqERVMDSNdlekERGITILSKNTAVMYNGVKINIVDTPG-----H 82
Cdd:cd01895 1 DPIKIAIIGRPNVGKSSLLNALLGE-----------ERVIVSD----IAGTTRDSIDVPFEYDGQKYTLIDTAGirkkgK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 83 ADFGGE------VERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINK---IDKPNARPQEVIDEVFDLFV 153
Cdd:cd01895 66 VTEGIEkysvlrTLKAIERADVVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKwdlVEKDEKTMKEFEKELRRKLP 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1486620076 154 elgaddeQLDF-PIVYASARGGYakkevdeesdNMECLFDTIIK 196
Cdd:cd01895 146 -------FLDYaPIVFISALTGQ----------GVDKLFDAIKE 172
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
11-278 |
2.44e-10 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 62.84 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 11 NVAIIAHVDHGKTTLVdamlkqSHVF--------RDNEKVQER-------------VMDSNDLEKERGITI---LSKNTA 66
Cdd:PTZ00141 9 NLVVIGHVDSGKSTTT------GHLIykcggidkRTIEKFEKEaaemgkgsfkyawVLDKLKAERERGITIdiaLWKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 67 VMYNgvkINIVDTPGHADFGGEVERVLKMVDSVVLVVDA----YEGPMP---QTKFVLKKALELHLRPIVV-INKIDKPN 138
Cdd:PTZ00141 83 PKYY---FTIIDAPGHRDFIKNMITGTSQADVAILVVAStageFEAGISkdgQTREHALLAFTLGVKQMIVcINKMDDKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 139 -----ARPQEVIDEVFDLFVELGADDEQLDF-PIvyasarGGYAKKEVDEESDNME-----CLFDTiIKNVKAPTGYIEE 207
Cdd:PTZ00141 160 vnysqERYDEIKKEVSAYLKKVGYNPEKVPFiPI------SGWQGDNMIEKSDNMPwykgpTLLEA-LDTLEPPKRPVDK 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1486620076 208 PLQLLVTTIDYNEYVGRIGIGKIERGKVAKNQQVTIVDrEGNKRNVKVSNLYvynglkREEVEEAQLGDIV 278
Cdd:PTZ00141 233 PLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAP-SGVTTEVKSVEMH------HEQLAEAVPGDNV 296
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
14-173 |
4.54e-10 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 62.38 E-value: 4.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 14 IIA---HVDHGKTTLVDAMlkqSHVfrDNEKVQErvmdsndlEKERGITIlskNTAVMY----NGVKINIVDTPGHADF- 85
Cdd:PRK10512 2 IIAtagHVDHGKTTLLQAI---TGV--NADRLPE--------EKKRGMTI---DLGYAYwpqpDGRVLGFIDVPGHEKFl 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 86 -------GGevervlkmVDSVVLVVDAYEGPMPQTKFVLkKALELHLRP--IVVINKIDK-PNARPQEVIDEVFDLFVEL 155
Cdd:PRK10512 66 snmlagvGG--------IDHALLVVACDDGVMAQTREHL-AILQLTGNPmlTVALTKADRvDEARIAEVRRQVKAVLREY 136
|
170
....*....|....*...
gi 1486620076 156 GADDEQLdFPIVYASARG 173
Cdd:PRK10512 137 GFAEAKL-FVTAATEGRG 153
|
|
| EFG_mtEFG_II |
cd04088 |
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation ... |
212-294 |
5.48e-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: 5.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 212 LVTTIDYNEYVGRIGIGKIERGKVAKNQQVTIVDREgnkRNVKVSNLYVYNGLKREEVEEAQLGDIVAVSGIVDINIGET 291
Cdd:cd04088 4 LVFKTMADPFVGKLTFFRVYSGTLKSGSTVYNSTKG---KKERVGRLLRMHGKKREEVEELGAGDIGAVVGLKDTRTGDT 80
|
...
gi 1486620076 292 IAD 294
Cdd:cd04088 81 LCD 83
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
11-172 |
6.76e-10 |
|
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.
Pssm-ID: 206739 [Multi-domain] Cd Length: 180 Bit Score: 58.71 E-value: 6.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 11 NVAIIAHVDHGKTTLVDAMLkqshvfrdnekvQERVMDSndlekerGITILSKNTAVMYNGVK--INIVDTPG------- 81
Cdd:cd09912 2 LLAVVGEFSAGKSTLLNALL------------GEEVLPT-------GVTPTTAVITVLRYGLLkgVVLVDTPGlnstieh 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 82 HADfggEVERVLKMVDSVVLVVDAyEGPMPQT--KFVLKKALELHLRPIVVINKIDKpnARPQEVIDEVFDLFVELGADD 159
Cdd:cd09912 63 HTE---ITESFLPRADAVIFVLSA-DQPLTESerEFLKEILKWSGKKIFFVLNKIDL--LSEEELEEVLEYSREELGVLE 136
|
170
....*....|....
gi 1486620076 160 EQLDFPIVYA-SAR 172
Cdd:cd09912 137 LGGGEPRIFPvSAK 150
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
12-196 |
8.41e-10 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 58.07 E-value: 8.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 12 VAIIAHVDHGKTTLVdAMLKQSHVFRDNEKVqervmdsndlekERGITILSKNTAVMYNGVKINIVDTPGHADF---GGE 88
Cdd:COG1100 6 IVVVGTGGVGKTSLV-NRLVGDIFSLEKYLS------------TNGVTIDKKELKLDGLDVDLVIWDTPGQDEFretRQF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 89 VERVLKMVDSVVLVVDayeGPMPQTKFVLKKALE------LHLRPIVVINKIDKPNARPQEVIDEVFDLFVELGAddeql 162
Cdd:COG1100 73 YARQLTGASLYLFVVD---GTREETLQSLYELLEslrrlgKKSPIILVLNKIDLYDEEEIEDEERLKEALSEDNI----- 144
|
170 180 190
....*....|....*....|....*....|....
gi 1486620076 163 dFPIVYASARGGyakkevdeesDNMECLFDTIIK 196
Cdd:COG1100 145 -VEVVATSAKTG----------EGVEELFAALAE 167
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
223-293 |
1.46e-09 |
|
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: 54.58 E-value: 1.46e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1486620076 223 GRIGIGKIERGKVAKNQQVTIV--DREGNKRNVKVSNLYVYNGLKREEVEEAQLGDIVAVSGIVDINIGETIA 293
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILpnGTGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
14-305 |
3.58e-09 |
|
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: 59.33 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 14 IIA-HVDHGKTTLVDAMLKQSH-VFRDN-EKVQE----RVMDSNDL---------EKERGITIlskNTAVMY---NGVKI 74
Cdd:COG2895 21 ITCgSVDDGKSTLIGRLLYDTKsIFEDQlAALERdskkRGTQEIDLalltdglqaEREQGITI---DVAYRYfstPKRKF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 75 NIVDTPGHADFggevervLK-MV------DSVVLVVDAYEGPMPQTK---FVLkkALeLHLRPIVV-INKIDKPNARpQE 143
Cdd:COG2895 98 IIADTPGHEQY-------TRnMVtgastaDLAILLIDARKGVLEQTRrhsYIA--SL-LGIRHVVVaVNKMDLVDYS-EE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 144 VIDEVFDLFVELGAddeQLDFPIVYA---SARGGyakkevD---EESDNM-----ECLFDtIIKNVKAPTGYIEEPLQLL 212
Cdd:COG2895 167 VFEEIVADYRAFAA---KLGLEDITFipiSALKG------DnvvERSENMpwydgPTLLE-HLETVEVAEDRNDAPFRFP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 213 VTTI-----DYNEYVGRigigkIERGKVAKNQQVTIVdreGNKRNVKVSNLYVYNGlkreEVEEAQLGDIVAVSGIVDIN 287
Cdd:COG2895 237 VQYVnrpnlDFRGYAGT-----IASGTVRVGDEVVVL---PSGKTSTVKSIVTFDG----DLEEAFAGQSVTLTLEDEID 304
|
330 340
....*....|....*....|.
gi 1486620076 288 I--GETIADP-SRPEAVEFIE 305
Cdd:COG2895 305 IsrGDVIVAAdAPPEVADQFE 325
|
|
| EFG_III-like |
cd16257 |
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G ... |
330-380 |
2.73e-08 |
|
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G (EF-G) and related proteins play a role in translation and share a similar domain architecture. Elongation factor EFG participates in the elongation phase during protein biosynthesis on the ribosome by stimulating translocation. Its functional cycles depend on GTP binding and its hydrolysis. Domain III is involved in the activation of GTP hydrolysis. This domain III, which is different from domain III in EF-TU and related elongation factors, is found in several translation factors, like bacterial release factors RF3, elongation factor 4, elongation factor 2, GTP-binding protein BipA and tetracycline resistance protein Tet.
Pssm-ID: 293914 [Multi-domain] Cd Length: 71 Bit Score: 50.81 E-value: 2.73e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1486620076 330 VTSRHLRDRLMKELETNVSLKVEETDSADSFKVSGRGELHLSILIETMRRE 380
Cdd:cd16257 13 LDQEKLLEGLERLSEEDPALQVYREESTGEFILSGLGELHLEIIVARLERE 63
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
11-133 |
9.33e-08 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 50.70 E-value: 9.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 11 NVAIIAHVDHGKTTLVDAMLKqshvfrdnekvqERVMDSNDLekerGITILSKNTAVMYNGVKINIVDTPG-----HADF 85
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTG------------AKAIVSDYP----GTTRDPNEGRLELKGKQIILVDTPGliegaSEGE 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1486620076 86 G-GEVERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINK 133
Cdd:pfam01926 65 GlGRAFLAIIEADLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
12-143 |
9.54e-08 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 54.80 E-value: 9.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 12 VAIIAHVDHGKTTLVDamlkqshvfrdnekvqeRVMDSNDLEKERG-IT-----------ILSKNTAVMYNGVKINI--- 76
Cdd:PRK04004 9 VVVLGHVDHGKTTLLD-----------------KIRGTAVAAKEAGgITqhigatevpidVIEKIAGPLKKPLPIKLkip 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 77 ----VDTPGHADF------GGEVervlkmVDSVVLVVDAYEGPMPQTkfvlKKALELhLR----P-IVVINKIDK-PNAR 140
Cdd:PRK04004 72 gllfIDTPGHEAFtnlrkrGGAL------ADIAILVVDINEGFQPQT----IEAINI-LKrrktPfVVAANKIDRiPGWK 140
|
...
gi 1486620076 141 PQE 143
Cdd:PRK04004 141 STE 143
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
11-242 |
1.09e-07 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 54.71 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 11 NVAIIAHVDHGKTTLVDAMLKQ-----SHVFRDNEK----VQER------VMDSNDLEKERGITI---LSKNTAVMYngv 72
Cdd:PLN00043 9 NIVVIGHVDSGKSTTTGHLIYKlggidKRVIERFEKeaaeMNKRsfkyawVLDKLKAERERGITIdiaLWKFETTKY--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 73 KINIVDTPGHADFGGEVERVLKMVDSVVLVVDAYEGPMP-------QTKFVLKKALELHLRPIV-VINKIDK-----PNA 139
Cdd:PLN00043 86 YCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMIcCCNKMDAttpkySKA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 140 RPQEVIDEVFDLFVELGADDEQLDF-PIvyasarGGYAKKEVDEESDNME-----CLFDTiIKNVKAPTGYIEEPLQLLV 213
Cdd:PLN00043 166 RYDEIVKEVSSYLKKVGYNPDKIPFvPI------SGFEGDNMIERSTNLDwykgpTLLEA-LDQINEPKRPSDKPLRLPL 238
|
250 260
....*....|....*....|....*....
gi 1486620076 214 TTIDYNEYVGRIGIGKIERGKVAKNQQVT 242
Cdd:PLN00043 239 QDVYKIGGIGTVPVGRVETGVIKPGMVVT 267
|
|
| EFG_mtEFG_C |
cd03713 |
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational ... |
402-478 |
1.33e-07 |
|
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational elongation factor (EF) EF-G. Included in this group is the C-terminus of mitochondrial Elongation factor G1 (mtEFG1) and G2 (mtEFG2) proteins. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. In bacteria this translocation step is catalyzed by EF-G_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. No clear phenotype has been found for mutants in the yeast homologue of mtEFG2, MEF2.
Pssm-ID: 239683 [Multi-domain] Cd Length: 78 Bit Score: 49.06 E-value: 1.33e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1486620076 402 EPIEYLTIDVPEEFMGVVMEKLGPRKAEMINMSSAvNGYSRLEFRIPARGLIGFRNEFMTDTKGNGIMNHVFDGYEP 478
Cdd:cd03713 1 EPIMKVEVTVPEEYMGDVIGDLSSRRGQILGTESR-GGWKVIKAEVPLAEMFGYSTDLRSLTQGRGSFTMEFSHYEE 76
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
21-196 |
1.39e-07 |
|
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: 51.48 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 21 GKTTLVDAMLKQsHVFrdneKVqERVMdsndlekerGITILSKNTAV-MYNGVKINIVDTPGHADFGG-------EVERV 92
Cdd:cd00880 9 GKSSLLNALLGQ-NVG----IV-SPIP---------GTTRDPVRKEWeLLPLGPVVLIDTPGLDEEGGlgrerveEARQV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 93 LKMVDSVVLVVDAYEGPMPQtKFVLKKALELHLRPIVVINKIDKPNARPQEVIDEVFDLfvelgadDEQLDFPIVYASAR 172
Cdd:cd00880 74 ADRADLVLLVVDSDLTPVEE-EAKLGLLRERGKPVLLVLNKIDLVPESEEEELLRERKL-------ELLPDLPVIAVSAL 145
|
170 180
....*....|....*....|....
gi 1486620076 173 GGyakKEVDEesdnmecLFDTIIK 196
Cdd:cd00880 146 PG---EGIDE-------LRKKIAE 159
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
209-293 |
1.42e-07 |
|
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: 49.19 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 209 LQLLVTTIDYNEYVGRIGIGKIERGKVAKNQQVTIVDREgnkRNVKVSNLYVynglKREEVEEAQLGDIVAVS--GIVDI 286
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKG---ITGRVTSIER----FHEEVDEAKAGDIVGIGilGVKDI 73
|
....*..
gi 1486620076 287 NIGETIA 293
Cdd:cd01342 74 LTGDTLT 80
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
9-203 |
1.74e-07 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 53.90 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 9 IRnVAIIAHVDHGKTTLVDAMLKQshvfrdnekvqERVMDSNdlekERGITILSKNTAVMYNGVKINIVDTPG------- 81
Cdd:PRK00093 174 IK-IAIIGRPNVGKSSLINALLGE-----------ERVIVSD----IAGTTRDSIDTPFERDGQKYTLIDTAGirrkgkv 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 82 HADfggeVE--------RVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINKIDK-PNARPQEVIDEVFDLF 152
Cdd:PRK00093 238 TEG----VEkysvirtlKAIERADVVLLVIDATEGITEQDLRIAGLALEAGRALVIVVNKWDLvDEKTMEEFKKELRRRL 313
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1486620076 153 velgaddEQLDF-PIVYASARGGYakkevdeesdNMECLFDTIIK-----NVKAPTG 203
Cdd:PRK00093 314 -------PFLDYaPIVFISALTGQ----------GVDKLLEAIDEayenaNRRISTS 353
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
77-197 |
4.90e-07 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 51.53 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 77 VDTPG-----HAdFG----GEVERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINKIDKPnarPQEVIDE 147
Cdd:COG1159 56 VDTPGihkpkRK-LGrrmnKAAWSALEDVDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDLV---KKEELLP 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1486620076 148 VFDLFVELGADDEqldfpIVYASARGGyakkevdeesDNMECLFDTIIKN 197
Cdd:COG1159 132 LLAEYSELLDFAE-----IVPISALKG----------DNVDELLDEIAKL 166
|
|
| EFG_C |
smart00838 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
402-478 |
5.78e-07 |
|
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: 47.50 E-value: 5.78e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1486620076 402 EPIEYLTIDVPEEFMGVVMEKLGPRKAEMINMSSAVNGySRLEFRIPARGLIGFRNEFMTDTKGNGIMNHVFDGYEP 478
Cdd:smart00838 3 EPIMKVEVTVPEEYMGDVIGDLNSRRGKIEGMEQRGGA-QVIKAKVPLSEMFGYATDLRSATQGRATWSMEFSHYEE 78
|
|
| Tet_C |
cd03711 |
Tet_C: C-terminus of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology ... |
402-478 |
5.86e-07 |
|
Tet_C: C-terminus of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology to the C terminal domains of the elongation factors EF-G and EF-2. Tet(M) and Tet(O) catalyze the release of tetracycline (Tc) from the ribosome in a GTP-dependent manner thereby mediating Tc resistance. Tcs are broad-spectrum antibiotics. Typical Tcs bind to the ribosome and inhibit the elongation phase of protein synthesis, by inhibiting the occupation of site A by aminoacyl-tRNA.
Pssm-ID: 239682 [Multi-domain] Cd Length: 78 Bit Score: 47.23 E-value: 5.86e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1486620076 402 EPIEYLTIDVPEEFMGVVMEKLGPRKAEmINMSSAVNGYSRLEFRIPARGLIGFRNEFMTDTKGNGIMNHVFDGYEP 478
Cdd:cd03711 1 EPYLRFELEVPQDALGRAMSDLAKMGAT-FEDPQIKGDEVTLEGTIPVATSQDYQSELPSYTHGEGVLETEFKGYRP 76
|
|
| EngA1 |
cd01894 |
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
69-174 |
6.13e-07 |
|
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206681 [Multi-domain] Cd Length: 157 Bit Score: 49.36 E-value: 6.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 69 YNGVKINIVDTPGHADFGGE--------VERVLKMVDSVVLVVDAYEGPMPQTKFVLKkalelHLRP-----IVVINKID 135
Cdd:cd01894 42 WGGREFILIDTGGIEPDDEGiskeireqAEIAIEEADVILFVVDGREGLTPADEEIAK-----YLRKskkpvILVVNKID 116
|
90 100 110
....*....|....*....|....*....|....*....
gi 1486620076 136 kpNARPQEVIDEvfdlFVELGADDeqldfpIVYASARGG 174
Cdd:cd01894 117 --NIKEEEEAAE----FYSLGFGE------PIPISAEHG 143
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
11-135 |
7.37e-07 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 51.78 E-value: 7.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 11 NVAIIAHVDHGKTTLVDAmLKQSHVFRDNEkvqervmdsndlEKERGITI--------------------LSKNTAVMYN 70
Cdd:PRK04000 11 NIGMVGHVDHGKTTLVQA-LTGVWTDRHSE------------ELKRGITIrlgyadatirkcpdceepeaYTTEPKCPNC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 71 GV------KINIVDTPGHadfggeveRVLKM--------VDSVVLVVDAYEG-PMPQTKFVLkKALEL----HLrpIVVI 131
Cdd:PRK04000 78 GSetellrRVSFVDAPGH--------ETLMAtmlsgaalMDGAILVIAANEPcPQPQTKEHL-MALDIigikNI--VIVQ 146
|
....
gi 1486620076 132 NKID 135
Cdd:PRK04000 147 NKID 150
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
12-136 |
1.26e-06 |
|
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic orthologs of bacterial IF-2. Like IF-2, it helps convey the initiator tRNA to the ribosome, although the initiator is N-formyl-Met in bacteria and Met here. This protein is not closely related to the subunits of eIF-2 of eukaryotes, which is also involved in the initiation of translation. The aIF-2 of Methanococcus jannaschii contains a large intein interrupting a region of very strongly conserved sequence very near the amino end; the alignment generated by this model does not correctly align the sequences from Methanococcus jannaschii and Pyrococcus horikoshii in this region. [Protein synthesis, Translation factors]
Pssm-ID: 273104 [Multi-domain] Cd Length: 591 Bit Score: 51.35 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 12 VAIIAHVDHGKTTLVDAMLKQSHVFRDNEKVQERVMDSndlekERGITILSKNTAVMYNGVKINI-------VDTPGHAD 84
Cdd:TIGR00491 7 VVVLGHVDHGKTTLLDKIRGTAVVKKEAGGITQHIGAS-----EVPTDVIEKICGDLLKSFKIKLkipgllfIDTPGHEA 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1486620076 85 FGGEVERVLKMVDSVVLVVDAYEGPMPQTKFVLkKALELHLRPIVV-INKIDK 136
Cdd:TIGR00491 82 FTNLRKRGGALADIAILVVDINEGFKPQTLEAL-NILRSRKTPFVVaANKIDR 133
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
77-196 |
3.27e-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: 47.46 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 77 VDTPG-HADFGG-------EVERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINKIDKpnARPQEVIDEV 148
Cdd:cd04163 56 VDTPGiHKPKKKlgermvkAAWSALKDVDLVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDL--VKDKEDLLPL 133
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1486620076 149 FDLFVELGADDEqldfpIVYASARGGyakkevdeesDNMECLFDTIIK 196
Cdd:cd04163 134 LEKLKELHPFAE-----IFPISALKG----------ENVDELLEYIVE 166
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
11-135 |
5.54e-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: 47.26 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 11 NVAIIAHVDHGKTTLVDAmLKQSHVFRDNEkvqervmdsndlEKERGITI---------------------LSKNTAVMY 69
Cdd:cd01888 2 NIGTIGHVAHGKTTLVKA-LSGVWTVRHKE------------ELKRNITIklgyanakiykcpncgcprpyDTPECECPG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 70 NGVK------INIVDTPGHadfggeveRVLKM--------VDSVVLVVDAYEG-PMPQTKFVLkKALEL----HLrpIVV 130
Cdd:cd01888 69 CGGEtklvrhVSFVDCPGH--------EILMAtmlsgaavMDGALLLIAANEPcPQPQTSEHL-AALEImglkHI--IIL 137
|
....*
gi 1486620076 131 INKID 135
Cdd:cd01888 138 QNKID 142
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
21-197 |
1.26e-05 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 47.35 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 21 GKTTLVDAMLKQ-----SHvfrdneKVQ---ERVmdsndlekeRGItilskntaVMYNGVKINIVDTPG----HADFG-- 86
Cdd:PRK00089 17 GKSTLLNALVGQkisivSP------KPQttrHRI---------RGI--------VTEDDAQIIFVDTPGihkpKRALNra 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 87 --GEVERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINKIDKpnARPQEVIDEVFDLFVELGADDEqldf 164
Cdd:PRK00089 74 mnKAAWSSLKDVDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDL--VKDKEELLPLLEELSELMDFAE---- 147
|
170 180 190
....*....|....*....|....*....|...
gi 1486620076 165 pIVYASArggyakkevdEESDNMECLFDTIIKN 197
Cdd:PRK00089 148 -IVPISA----------LKGDNVDELLDVIAKY 169
|
|
| Arf_Arl |
cd00878 |
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ... |
21-174 |
3.18e-05 |
|
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl (Arf-like) small GTPases. Arf proteins are activators of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. Arfs are N-terminally myristoylated. Members of the Arf family are regulators of vesicle formation in intracellular traffic that interact reversibly with membranes of the secretory and endocytic compartments in a GTP-dependent manner. They depart from other small GTP-binding proteins by a unique structural device, interswitch toggle, that implements front-back communication from N-terminus to the nucleotide binding site. Arf-like (Arl) proteins are close relatives of the Arf, but only Arl1 has been shown to function in membrane traffic like the Arf proteins. Arl2 has an unrelated function in the folding of native tubulin, and Arl4 may function in the nucleus. Most other Arf family proteins are so far relatively poorly characterized. Thus, despite their significant sequence homologies, Arf family proteins may regulate unrelated functions.
Pssm-ID: 206644 [Multi-domain] Cd Length: 158 Bit Score: 44.49 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 21 GKTTLVDaMLKQSHVfrdnEKVQervmdsndlekergITILSKNTAVMYNGVKINIVDTPGHADFggeveRVL-----KM 95
Cdd:cd00878 11 GKTTILY-KLKLGEV----VTTI--------------PTIGFNVETVEYKNVKFTVWDVGGQDKI-----RPLwkhyyEN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 96 VDSVVLVVDAY-EGPMPQTKFVLKKAL---ELHLRPI-VVINKIDKPNARPQEVIDEVFDLFVELGaddeqLDFPIVYAS 170
Cdd:cd00878 67 TDGLIFVVDSSdRERIEEAKNELHKLLneeELKGAPLlILANKQDLPGALTESELIELLGLESIKG-----RRWHIQPCS 141
|
....
gi 1486620076 171 ARGG 174
Cdd:cd00878 142 AVTG 145
|
|
| MJ1464 |
cd01859 |
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ... |
89-172 |
3.37e-05 |
|
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: 44.23 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 89 VERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINKIDkpnARPQEVIDEVFDLFvelgaddEQLDFPIVY 168
Cdd:cd01859 5 VRRIIKEADVVLEVVDARDPELTRSRKLERMALELGKKLIIVLNKAD---LVPREVLEKWKEVF-------ESEGLPVVY 74
|
....
gi 1486620076 169 ASAR 172
Cdd:cd01859 75 VSAR 78
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
7-171 |
4.24e-05 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 46.17 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 7 NDIRNVAIIAHVDHGKTTLVDAMLKQshvfrdnekvqERVMDSNdlekERGITILSKNTAVMYNGVKINIVDTPG----- 81
Cdd:COG1160 173 DDPIKIAIVGRPNVGKSSLINALLGE-----------ERVIVSD----IAGTTRDSIDTPFERDGKKYTLIDTAGirrkg 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 82 HADFGGE---VERVLKMVDS---VVLVVDAYEGPMPQTKFVLKKALELHlRPIV-VINK---IDKPNARPQEVIDEVFDL 151
Cdd:COG1160 238 KVDEGIEkysVLRTLRAIERadvVLLVIDATEGITEQDLKIAGLALEAG-KALViVVNKwdlVEKDRKTREELEKEIRRR 316
|
170 180
....*....|....*....|.
gi 1486620076 152 FVelgaddeQLDF-PIVYASA 171
Cdd:COG1160 317 LP-------FLDYaPIVFISA 330
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
69-208 |
2.96e-04 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 43.50 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 69 YNGVKINIVDTPG----HADFGGEV----ERVLKMVDSVVLVVDAYEGPMPQTKFVLKkalelHLRP-----IVVINKID 135
Cdd:PRK00093 46 WLGREFILIDTGGiepdDDGFEKQIreqaELAIEEADVILFVVDGRAGLTPADEEIAK-----ILRKsnkpvILVVNKVD 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1486620076 136 KPNARpqEVIDEvfdlFVELGADDEqldFPIvyaSARGGyakkevdeesDNMECLFDTIIKNVKAPTGYIEEP 208
Cdd:PRK00093 121 GPDEE--ADAYE----FYSLGLGEP---YPI---SAEHG----------RGIGDLLDAILEELPEEEEEDEED 171
|
|
| mtEFG1_II_like |
cd04091 |
Domain II of mitochondrial elongation factor G1-like proteins found in eukaryotes; Eukaryotic ... |
224-294 |
4.19e-04 |
|
Domain II of mitochondrial elongation factor G1-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: 293908 [Multi-domain] Cd Length: 81 Bit Score: 39.19 E-value: 4.19e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1486620076 224 RIGIGKIERGKVAKNQqvtivdREGNKrnVKVSNLYVYNGLKREEVEEAQLGDIVAVSGIvDINIGETIAD 294
Cdd:cd04091 20 RVYQGVLRKGDTIYNV------RTGKK--VRVPRLVRMHSDEMEDIEEVYAGDICALFGI-DCASGDTFTD 81
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
69-159 |
8.41e-04 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 41.93 E-value: 8.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 69 YNGVKINIVDTPG-----HADFGGE----VERVLKMVDSVVLVVDAYEGPMPQTKFVLKkalelHLRP-----IVVINKI 134
Cdd:COG1160 47 WGGREFTLIDTGGiepddDDGLEAEireqAELAIEEADVILFVVDGRAGLTPLDEEIAK-----LLRRsgkpvILVVNKV 121
|
90 100
....*....|....*....|....*
gi 1486620076 135 DKPNARpqeviDEVFDLFvELGADD 159
Cdd:COG1160 122 DGPKRE-----ADAAEFY-SLGLGE 140
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
18-307 |
1.04e-03 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 41.82 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 18 VDHGKTTLVDAML---KQ------SHVFRDNEKVQ---ERV-----MDSNDLEKERGITIlskNTAVMY---NGVKINIV 77
Cdd:PRK05124 36 VDDGKSTLIGRLLhdtKQiyedqlASLHNDSKRHGtqgEKLdlallVDGLQAEREQGITI---DVAYRYfstEKRKFIIA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 78 DTPGHADFggevERvlKMV------DSVVLVVDAYEGPMPQTK---FVlkkALELHLRPIVV-INKIDKPNARpQEVIDE 147
Cdd:PRK05124 113 DTPGHEQY----TR--NMAtgastcDLAILLIDARKGVLDQTRrhsFI---ATLLGIKHLVVaVNKMDLVDYS-EEVFER 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 148 VFDLFVELGAD-DEQLDFPIVYASARGGyakKEVDEESDNM-----ECLFDtIIKNVKAPTGYIEEPLQLLVttidynEY 221
Cdd:PRK05124 183 IREDYLTFAEQlPGNLDIRFVPLSALEG---DNVVSQSESMpwysgPTLLE-VLETVDIQRVVDAQPFRFPV------QY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 222 VGRIGI------GKIERGKVAKNQQVTIVdrEGNKRNvKVSNLYVYNGlkreEVEEAQLGDIVAV--SGIVDINIGETIA 293
Cdd:PRK05124 253 VNRPNLdfrgyaGTLASGVVKVGDRVKVL--PSGKES-NVARIVTFDG----DLEEAFAGEAITLvlEDEIDISRGDLLV 325
|
330
....*....|....*
gi 1486620076 294 DP-SRPEAVEFIEID 307
Cdd:PRK05124 326 AAdEALQAVQHASAD 340
|
|
| YihA_EngB |
cd01876 |
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
73-180 |
1.10e-03 |
|
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.
Pssm-ID: 206665 [Multi-domain] Cd Length: 170 Bit Score: 40.19 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 73 KINIVDTPGhadFGG------EVERVLKMVDS----------VVLVVDAYEGPMPQTKFVLKKALELHLRPIVVINKIDK 136
Cdd:cd01876 46 KFRLVDLPG---YGYakvskeVREKWGKLIEEylenrenlkgVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADK 122
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1486620076 137 PNarPQEVIDEVFDLFVELGADDEqlDFPIVYASARGGYAKKEV 180
Cdd:cd01876 123 LK--KSELAKVLKKIKEELNLFNI--LPPVILFSSKKGTGIDEL 162
|
|
| MnmE |
COG0486 |
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
70-155 |
1.56e-03 |
|
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440253 [Multi-domain] Cd Length: 448 Bit Score: 41.20 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 70 NGVKINIVDTPGHADFGGEVER--------VLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLrpIVVINKIDKPNARP 141
Cdd:COG0486 259 GGIPVRLIDTAGLRETEDEVEKigierareAIEEADLVLLLLDASEPLTEEDEEILEKLKDKPV--IVVLNKIDLPSEAD 336
|
90
....*....|....
gi 1486620076 142 QEVIDEVFDLFVEL 155
Cdd:COG0486 337 GELKSLPGEPVIAI 350
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
76-133 |
2.21e-03 |
|
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.
Pssm-ID: 349751 [Multi-domain] Cd Length: 107 Bit Score: 38.18 E-value: 2.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1486620076 76 IVDTPGHADFGGEVERV-----LKMVDSVVLVVDAYEGPMPQTKFVLKKALELH--LRP-IVVINK 133
Cdd:cd01983 42 LIDGGGGLETGLLLGTIvallaLKKADEVIVVVDPELGSLLEAVKLLLALLLLGigIRPdGIVLNK 107
|
|
| mtEFG1_C |
cd04097 |
mtEFG1_C: C-terminus of mitochondrial Elongation factor G1 (mtEFG1)-like proteins found in ... |
402-478 |
2.46e-03 |
|
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: 36.91 E-value: 2.46e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1486620076 402 EPIEYLTIDVPEEFMGVVMEKLGPRKAeMINMSSAVNGYSRLEFRIPARGLIGFRNEFMTDTKGNGIMNHVFDGYEP 478
Cdd:cd04097 1 EPIMKVEVTAPTEFQGNVIGLLNKRKG-TIVDTDTGEDEFTLEAEVPLNDMFGYSTELRSMTQGKGEFSMEFSRYAP 76
|
|
| Srp102 |
COG2229 |
Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, ... |
70-172 |
3.32e-03 |
|
Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 441830 [Multi-domain] Cd Length: 189 Bit Score: 39.04 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 70 NGVKINIVDTPGHADFGGEVERVLKMVDSVVLVVDAYEGPMPQTKFVLKKALELHLR-PIVV-INKIDKPNARPQEVIDE 147
Cdd:COG2229 68 DGLRLHLFGTPGQVRFDFMWDILLRGADGVVFLADSRRLEDSFNAESLDFFEERLEKlPFVVaVNKRDLPDALSLEELRE 147
|
90 100
....*....|....*....|....*
gi 1486620076 148 VFDLfvelgaddeQLDFPIVYASAR 172
Cdd:COG2229 148 ALDL---------GPDVPVVEADAR 163
|
|
| lepA_C |
cd03709 |
lepA_C: This family represents the C-terminal region of LepA, a GTP-binding protein localized ... |
402-478 |
3.74e-03 |
|
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: 36.70 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 402 EPIEYLTIDVPEEFMGVVMEKLGPRKAEMINMSSAVNGYSRLEFRIPArgligfrNEFMTD--------TKGNGIMNHVF 473
Cdd:cd03709 1 EPFVKATIITPSEYLGAIMELCQERRGVQKDMEYLDANRVMLTYELPL-------AEIVYDffdklksiSKGYASLDYEL 73
|
....*
gi 1486620076 474 DGYEP 478
Cdd:cd03709 74 IGYRE 78
|
|
| EF2_II |
cd16268 |
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 ... |
225-294 |
4.88e-03 |
|
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 (EF-2) found in eukaryotes and archaea. During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. This translocation step is catalyzed by EF-2_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site.
Pssm-ID: 293913 [Multi-domain] Cd Length: 96 Bit Score: 36.81 E-value: 4.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1486620076 225 IGIGKIERGKVAKNQQVTIV------DREGNKRNVKVSNLYVYNGLKREEVEEAQLGDIVAVSGIVD--INIGETIAD 294
Cdd:cd16268 19 VAFGRVFSGTVRRGQEVYILgpkyvpGKKDDLKKKRIQQTYLMMGREREPVDEVPAGNIVGLVGLDDflAKSGTTTSS 96
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| RF3_II |
cd03689 |
Domain II of bacterial Release Factor 3; This subfamily represents domain II of bacterial ... |
224-293 |
5.32e-03 |
|
Domain II of bacterial Release Factor 3; This subfamily represents domain II of bacterial Release Factor 3 (RF3). Termination of protein synthesis by the ribosome requires two release factor (RF) classes. The class II RF3 is a GTPase that removes class I RFs (RF1 or RF2) from the ribosome after release of the nascent polypeptide. RF3 in the GDP state binds to the ribosomal class I RF complex, followed by an exchange of GDP for GTP and release of the class I RF. Sequence comparison of class II release factors with elongation factors shows that prokaryotic RF3 is more similar to EF-G whereas eukaryotic eRF3 is more similar to eEF1A, implying that their precise function may differ.
Pssm-ID: 293890 [Multi-domain] Cd Length: 87 Bit Score: 36.48 E-value: 5.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486620076 224 RIGIGKIERGKVAKNQQVtivdregnKRNVKVSNLYVYNGLKREEVEEAQLGDIVAVSGIVDINIGETIA 293
Cdd:cd03689 24 RVCSGKFERGMKVKHVRT--------GKEVRLSNATTFMAQDRETVEEAYPGDIIGLPNHGTFQIGDTFT 85
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