|
Name |
Accession |
Description |
Interval |
E-value |
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
1-607 |
0e+00 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 1221.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 1 MSIEQLRNIAIIAHVDHGKTTLVDKLLEQSGTLETRGGNEERVMDSNDIEKERGITILAKNTAISWNDYHINIVDTPGHA 80
Cdd:COG1217 1 MMREDIRNIAIIAHVDHGKTTLVDALLKQSGTFRENQEVAERVMDSNDLERERGITILAKNTAVRYKGVKINIVDTPGHA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 81 DFGGEVERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDKPGARPDWVMDQIFDLFDNLGATDEQLD 160
Cdd:COG1217 81 DFGGEVERVLSMVDGVLLLVDAFEGPMPQTRFVLKKALELGLKPIVVINKIDRPDARPDEVVDEVFDLFIELGATDEQLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 161 FKVIYASAINGWATLDLDEPSDNMEPMFKMIVEEVSPPDADPEGDFQMQISQLDYNSYVGVVGIGRIKRGSVAPNQQVTI 240
Cdd:COG1217 161 FPVVYASARNGWASLDLDDPGEDLTPLFDTILEHVPAPEVDPDGPLQMLVTNLDYSDYVGRIAIGRIFRGTIKKGQQVAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 241 ISADGTTRNGKIGAVQSYLGLERIETDRAYAGNIVTVTGIGELKISDTVCFPGNVEALPPLSVDEPTVTMTFSVNNSPFC 320
Cdd:COG1217 241 IKRDGKVEKGKITKLFGFEGLERVEVEEAEAGDIVAIAGIEDINIGDTICDPENPEALPPIKIDEPTLSMTFSVNDSPFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 321 GKEGKFVTSRNIRERLDKELVHNVALRVEDTASPDSFRVSGRGELHLGILIENMRREGYELSVSRPEVILRTVDGVLEEP 400
Cdd:COG1217 321 GREGKFVTSRQIRERLEKELETNVALRVEETDSPDAFKVSGRGELHLSILIETMRREGYELQVSRPEVIFKEIDGKKLEP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 401 FETVTIDCQEEHQGSVMEQVGLRKGELTNMTPDGKGRMRLDFMIPSRGLIGFQTDFMTLTSGSGLMYHTFDHYGPHKgGA 480
Cdd:COG1217 401 IEELTIDVPEEYSGAVIEKLGQRKGEMTNMEPDGGGRVRLEFLIPSRGLIGFRTEFLTDTRGTGIMNHVFDGYEPYK-GE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 481 IGVRKNGVMIANATGKALTNALFNLQERGRLFIGHGVEVYEGMVIGIHNRDNDLTVNALKGKQLTNVRASGTDEAQTLSP 560
Cdd:COG1217 480 IPGRRNGSLISMETGKATAYALFNLQERGTLFIGPGTEVYEGMIVGEHSRDNDLVVNVCKEKKLTNMRASGSDEAIRLTP 559
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 489050914 561 HLNYSLEQALEFIDDDELVEVTPLNIRIRKKHLTENERKRAGRAPKS 607
Cdd:COG1217 560 PRKMSLEQALEFIEDDELVEVTPKSIRLRKKILDENERKRAAKKKKK 606
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
6-600 |
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: 1041.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 6 LRNIAIIAHVDHGKTTLVDKLLEQSGTLETRGGNEERVMDSNDIEKERGITILAKNTAISWNDYHINIVDTPGHADFGGE 85
Cdd:TIGR01394 1 IRNIAIIAHVDHGKTTLVDALLKQSGTFRANEAVAERVMDSNDLERERGITILAKNTAIRYNGTKINIVDTPGHADFGGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 86 VERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDKPGARPDWVMDQIFDLFDNLGATDEQLDFKVIY 165
Cdd:TIGR01394 81 VERVLGMVDGVLLLVDASEGPMPQTRFVLKKALELGLKPIVVINKIDRPSARPDEVVDEVFDLFAELGADDEQLDFPIVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 166 ASAINGWATLDLDEPSDNMEPMFKMIVEEVSPPDADPEGDFQMQISQLDYNSYVGVVGIGRIKRGSVAPNQQVTIISADG 245
Cdd:TIGR01394 161 ASGRAGWASLDLDDPSDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVHRGTVKKGQQVALMKRDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 246 TTRNGKIGAVQSYLGLERIETDRAYAGNIVTVTGIGELKISDTVCFPGNVEALPPLSVDEPTVTMTFSVNNSPFCGKEGK 325
Cdd:TIGR01394 241 TIENGRISKLLGFEGLERVEIDEAGAGDIVAVAGLEDINIGETIADPEVPEALPTITVDEPTLSMTFSVNDSPLAGKEGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 326 FVTSRNIRERLDKELVHNVALRVEDTASPDSFRVSGRGELHLGILIENMRREGYELSVSRPEVILRTVDGVLEEPFETVT 405
Cdd:TIGR01394 321 KVTSRHIRDRLMRELETNVALRVEDTESADKFEVSGRGELHLSILIETMRREGFELQVGRPQVIYKEIDGKKLEPIEELT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 406 IDCQEEHQGSVMEQVGLRKGELTNMTPDGKGRMRLDFMIPSRGLIGFQTDFMTLTSGSGLMYHTFDHYGPHKgGAIGVRK 485
Cdd:TIGR01394 401 IDVPEEHVGAVIEKLGKRKGEMVDMEPSGNGRTRLEFKIPSRGLIGFRTEFLTDTRGTGIMNHVFDEYEPWK-GEIETRR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 486 NGVMIANATGKALTNALFNLQERGRLFIGHGVEVYEGMVIGIHNRDNDLTVNALKGKQLTNVRASGTDEAQTLSPHLNYS 565
Cdd:TIGR01394 480 NGSLVSMEDGTATAYALWNLQERGVMFVSPGTEVYEGMIIGEHSRENDLDVNPCKAKKLTNVRSSGKDEAVKLTPPRKLS 559
|
570 580 590
....*....|....*....|....*....|....*
gi 489050914 566 LEQALEFIDDDELVEVTPLNIRIRKKHLTENERKR 600
Cdd:TIGR01394 560 LEQALEYIEDDELVEVTPKSIRLRKRVLDPNERKR 594
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
3-606 |
0e+00 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 910.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 3 IEQLRNIAIIAHVDHGKTTLVDKLLEQSGTLETRGGNEERVMDSNDIEKERGITILAKNTAISWNDYHINIVDTPGHADF 82
Cdd:PRK10218 2 IEKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 83 GGEVERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDKPGARPDWVMDQIFDLFDNLGATDEQLDFK 162
Cdd:PRK10218 82 GGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDFP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 163 VIYASAINGWATLDLDEPSDNMEPMFKMIVEEVSPPDADPEGDFQMQISQLDYNSYVGVVGIGRIKRGSVAPNQQVTIIS 242
Cdd:PRK10218 162 IVYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIID 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 243 ADGTTRNGKIGAVQSYLGLERIETDRAYAGNIVTVTGIGELKISDTVCFPGNVEALPPLSVDEPTVTMTFSVNNSPFCGK 322
Cdd:PRK10218 242 SEGKTRNAKVGKVLGHLGLERIETDLAEAGDIVAITGLGELNISDTVCDTQNVEALPALSVDEPTVSMFFCVNTSPFCGK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 323 EGKFVTSRNIRERLDKELVHNVALRVEDTASPDSFRVSGRGELHLGILIENMRREGYELSVSRPEVILRTVDGVLEEPFE 402
Cdd:PRK10218 322 EGKFVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRREGFELAVSRPKVIFREIDGRKQEPYE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 403 TVTIDCQEEHQGSVMEQVGLRKGELTNMTPDGKGRMRLDFMIPSRGLIGFQTDFMTLTSGSGLMYHTFDHYGPHKGGAIG 482
Cdd:PRK10218 402 NVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDVRPGEVG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 483 VRKNGVMIANATGKALTNALFNLQERGRLFIGHGVEVYEGMVIGIHNRDNDLTVNALKGKQLTNVRASGTDEAQTLSPHL 562
Cdd:PRK10218 482 QRQNGVLISNGQGKAVAFALFGLQDRGKLFLGHGAEVYEGQIIGIHSRSNDLTVNCLTGKKLTNMRASGTDEAVVLVPPI 561
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 489050914 563 NYSLEQALEFIDDDELVEVTPLNIRIRKKHLTENERKRAGRAPK 606
Cdd:PRK10218 562 RMTLEQALEFIDDDELVEVTPTSIRIRKRHLTENDRRRANRAPK 605
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
6-198 |
8.42e-129 |
|
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: 376.16 E-value: 8.42e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 6 LRNIAIIAHVDHGKTTLVDKLLEQSGTLETRGGNEERVMDSNDIEKERGITILAKNTAISWNDYHINIVDTPGHADFGGE 85
Cdd:cd01891 2 IRNIAIIAHVDHGKTTLVDALLKQSGTFRENEEVGERVMDSNDLERERGITILAKNTAITYKDTKINIIDTPGHADFGGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 86 VERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDKPGARPDWVMDQIFDLFDNLGATDEQLDFKVIY 165
Cdd:cd01891 82 VERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDRPDARPEEVVDEVFDLFLELNATDEQLDFPIVY 161
|
170 180 190
....*....|....*....|....*....|...
gi 489050914 166 ASAINGWATLDLDEPSDNMEPMFKMIVEEVSPP 198
Cdd:cd01891 162 ASAKNGWASLNLDDPSEDLDPLFETIIEHVPAP 194
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
4-197 |
6.34e-69 |
|
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: 221.24 E-value: 6.34e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 4 EQLRNIAIIAHVDHGKTTLVDKLLEQSGTLETRG---GNEERVMDSNDIEKERGITILAKNTAISWNDYHINIVDTPGHA 80
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGevkGEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 81 DFGGEVERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDKP-GARPDWVMDQIFDLFDNLGATDEqL 159
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVdGAELEEVVEEVSRELLEKYGEDG-E 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 489050914 160 DFKVIYASAINGWatldldepsdNMEPMFKMIVEEVSP 197
Cdd:pfam00009 160 FVPVVPGSALKGE----------GVQTLLDALDEYLPS 187
|
|
| lepA |
TIGR01393 |
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a ... |
4-510 |
2.81e-65 |
|
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: 224.51 E-value: 2.81e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 4 EQLRNIAIIAHVDHGKTTLVDKLLEQSGTLETRgGNEERVMDSNDIEKERGITILAKNTAISW-----NDYHINIVDTPG 78
Cdd:TIGR01393 1 KNIRNFSIIAHIDHGKSTLADRLLEYTGAISER-EMREQVLDSMDLERERGITIKAQAVRLNYkakdgETYVLNLIDTPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 79 HADFGGEVERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDKPGARPDWVMDQIFDLfdnLGATDEQ 158
Cdd:TIGR01393 80 HVDFSYEVSRSLAACEGALLLVDAAQGIEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKKEIEEV---IGLDASE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 159 ldfkVIYASAINGwatldldepsDNMEPMFKMIVEEVSPPDADPEGDFQMQISQLDYNSYVGVVGIGRIKRGSVAPNQQV 238
Cdd:TIGR01393 157 ----AILASAKTG----------IGIEEILEAIVKRVPPPKGDPDAPLKALIFDSHYDNYRGVVALVRVFEGTIKPGDKI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 239 TIISADGTTRNGKIGAVQsylgLERIETDRAYAGN----IVTVTGIGELKISDTVCFPGNvEALPPLSVDEPTVTMTFS- 313
Cdd:TIGR01393 223 RFMSTGKEYEVDEVGVFT----PKLTKTDELSAGEvgyiIAGIKDVSDVRVGDTITHVKN-PAKEPLPGFKEVKPMVFAg 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 314 ---VNNSPFcgkegkfvtsRNIRERLDKELVHNVALRVEDTASPD---SFRVSGRGELHLGILIENMRREgYELSV--SR 385
Cdd:TIGR01393 298 lypIDTEDY----------EDLRDALEKLKLNDASLTYEPESSPAlgfGFRCGFLGLLHMEIIQERLERE-FNLDLitTA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 386 PEVILRTV--DG------------------VLEEPFETVTIDCQEEHQGSVMEQVGLRKGELTNMTPDGKGRMRLDFMIP 445
Cdd:TIGR01393 367 PSVIYRVYltNGevievdnpsdlpdpgkieHVEEPYVKATIITPTEYLGPIMTLCQEKRGVQTNMEYLDPNRVELIYEMP 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489050914 446 -SRGLIGFQTDFMTLTSGsglmYHTFDhYGPHKGGAIGVRKNGVMIANATGKALTNALF--NLQERGR 510
Cdd:TIGR01393 447 lAEIVYDFFDKLKSISRG----YASFD-YELIGYRPSDLVKLDILINGEPVDALSFIVHrdKAYSRGR 509
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
1-445 |
3.63e-63 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 218.74 E-value: 3.63e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 1 MSIEQLRNIAIIAHVDHGKTTLVDKLLEQSGTLETRgGNEERVMDSNDIEKERGITILAKNTAISW-----NDYHINIVD 75
Cdd:COG0481 1 MDQKNIRNFSIIAHIDHGKSTLADRLLELTGTLSER-EMKEQVLDSMDLERERGITIKAQAVRLNYkakdgETYQLNLID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 76 TPGHADFGGEVERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDKPGARPDWVMDQIFDLFdNLGAT 155
Cdd:COG0481 80 TPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKQEIEDII-GIDAS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 156 DeqldfkVIYASAINGwatldldepsDNMEPMFKMIVEEVSPPDADPEGDFQMQIsqLD--YNSYVGVVGIGRIKRGSVA 233
Cdd:COG0481 159 D------AILVSAKTG----------IGIEEILEAIVERIPPPKGDPDAPLQALI--FDswYDSYRGVVVYVRVFDGTLK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 234 PNQQVTIISADGTTRNGKIGavqsYLGLERIETDRAYAGNI-VTVTGI---GELKISDTVCFPGN--VEALPPLsvdEPT 307
Cdd:COG0481 221 KGDKIKMMSTGKEYEVDEVG----VFTPKMTPVDELSAGEVgYIIAGIkdvRDARVGDTITLAKNpaAEPLPGF---KEV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 308 VTMTFS----VNNSPFcgkegkfvtsRNIRERLDKelvhnvaLRVEDTA---SPDS-------FRVSGRGELHLGILIEN 373
Cdd:COG0481 294 KPMVFAglypVDSDDY----------EDLRDALEK-------LQLNDASltyEPETsaalgfgFRCGFLGLLHMEIIQER 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 374 MRREgYELSV--SRPEVILR--TVDGV------------------LEEPFETVTIDCQEEHQGSVMEQVGLRKGELTNMT 431
Cdd:COG0481 357 LERE-FDLDLitTAPSVVYEvtLTDGEvievdnpsdlpdpgkieeIEEPIVKATIITPSEYVGAVMELCQEKRGVQKNME 435
|
490
....*....|....
gi 489050914 432 PDGKGRMRLDFMIP 445
Cdd:COG0481 436 YLGENRVELTYELP 449
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
8-198 |
2.67e-57 |
|
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: 190.58 E-value: 2.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 8 NIAIIAHVDHGKTTLVDKLLEQSGTLETRGGNEERVMDSNDIEKERGITILAKNTAISWNDYHINIVDTPGHADFGGEVE 87
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 88 RVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDKPG-ARPDWVMDQIFDLFDNLGAT-DEQLDFKVIY 165
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGeEDFDEVLREIKELLKLIGFTfLKGKDVPIIP 160
|
170 180 190
....*....|....*....|....*....|...
gi 489050914 166 ASAINGWAtldldepsdnMEPMFKMIVEEVSPP 198
Cdd:cd00881 161 ISALTGEG----------IEELLDAIVEHLPPP 183
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
3-402 |
3.54e-56 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 202.02 E-value: 3.54e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 3 IEQLRNIAIIAHVDHGKTTLVDKLLEQSGTLETRGGNEERVMDSNDIEKERGITILAKNtaISW------NDYHINIVDT 76
Cdd:PRK07560 17 PEQIRNIGIIAHIDHGKTTLSDNLLAGAGMISEELAGEQLALDFDEEEQARGITIKAAN--VSMvheyegKEYLINLIDT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 77 PGHADFGGEVERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDkpgaR--------PDWVMD---QI 145
Cdd:PRK07560 95 PGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKPVLFINKVD----RlikelkltPQEMQQrllKI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 146 FDLFDNL--GATDE------QLDF---KVIYASAINGWA---------------TLDLDEpSDNMEPMFK---------- 189
Cdd:PRK07560 171 IKDVNKLikGMAPEefkekwKVDVedgTVAFGSALYNWAisvpmmqktgikfkdIIDYYE-KGKQKELAEkaplhevvld 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 190 MIVEEVSPP-------------------------DADPEGDFQMQISQLDYNSYVGVVGIGRIKRGSVAPNQQVTIISAD 244
Cdd:PRK07560 250 MVVKHLPNPieaqkyripkiwkgdlnsevgkamlNCDPNGPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLVGAK 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 245 GTTRngkigaVQS---YLGLERIETDRAYAGNIVTVTGIGELKISDTVCFPGNVEALPPLS-VDEPTVTMTfsvnnspfc 320
Cdd:PRK07560 330 KKNR------VQQvgiYMGPEREEVEEIPAGNIAAVTGLKDARAGETVVSVEDMTPFESLKhISEPVVTVA--------- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 321 gkegkfVTSRNIRErLDK--ELVHNVA-----LRV---EDTAspdSFRVSGRGELHLGILIENMRRE-GYELSVSRPEVI 389
Cdd:PRK07560 395 ------IEAKNPKD-LPKliEVLRQLAkedptLVVkinEETG---EHLLSGMGELHLEVITYRIKRDyGIEVVTSEPIVV 464
|
490
....*....|....
gi 489050914 390 LR-TVDGVLeEPFE 402
Cdd:PRK07560 465 YReTVRGKS-QVVE 477
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
4-395 |
7.78e-55 |
|
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: 198.20 E-value: 7.78e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 4 EQLRNIAIIAHVDHGKTTLVDKLLEQSGTLETRGGNEERVMDSNDIEKERGITILAKNTAI----SWNDYHINIVDTPGH 79
Cdd:TIGR00490 17 KFIRNIGIVAHIDHGKTTLSDNLLAGAGMISEELAGQQLYLDFDEQEQERGITINAANVSMvheyEGNEYLINLIDTPGH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 80 ADFGGEVERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDK-----------PGARPDWVMDQIFDL 148
Cdd:TIGR00490 97 VDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKPVLFINKVDRlinelkltpqeLQERFIKIITEVNKL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 149 FDNLGA---TDEQL----DFKVIYASAINGWATL------------------------DLDEPSDNMEPMFKMIVEEV-S 196
Cdd:TIGR00490 177 IKAMAPeefRDKWKvrveDGSVAFGSAYYNWAISvpsmkktgigfkdiykyckedkqkELAKKSPLHQVVLDMVIRHLpS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 197 PPDA------------------------DPEGDFQMQISQLDYNSYVGVVGIGRIKRGSVAPNQQVTIIsadGTTRNGKI 252
Cdd:TIGR00490 257 PIEAqkyripviwkgdlnsevgkamlncDPKGPLALMITKIVVDKHAGEVAVGRLYSGTIRPGMEVYIV---DRKAKARI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 253 GAVQSYLGLERIETDRAYAGNIVTVTGIGELKISDTVCFPG-NVEALPPLS-VDEPTVTMTFSVNNSPFCGKegkfvtsr 330
Cdd:TIGR00490 334 QQVGVYMGPERVEVDEIPAGNIVAVIGLKDAVAGETICTTVeNITPFESIKhISEPVVTVAIEAKNTKDLPK-------- 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489050914 331 nIRERLDKELVHNVALRVEDTASPDSFRVSGRGELHLGILIENMRRE-GYELSVSRPEVILR-TVDG 395
Cdd:TIGR00490 406 -LIEVLRQVAKEDPTVHVEINEETGEHLISGMGELHLEIIVEKIREDyGLDVETSPPIVVYReTVTG 471
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
1-391 |
1.62e-49 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 182.84 E-value: 1.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 1 MSIEQLRNIAIIAHVDHGKTTLVDKLLEQSGTLETRG----GNEerVMDSNDIEKERGITILAKNTAISWNDYHINIVDT 76
Cdd:PRK13351 3 MPLMQIRNIGILAHIDAGKTTLTERILFYTGKIHKMGevedGTT--VTDWMPQEQERGITIESAATSCDWDNHRINLIDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 77 PGHADFGGEVERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDKPGARPDWVMDQIFD--------- 147
Cdd:PRK13351 81 PGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLFKVLEDIEErfgkrplpl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 148 -----------------------------------------LFDNLGATDEQLD-------------------------- 160
Cdd:PRK13351 161 qlpigsedgfegvvdlitepelhfsegdggstveegpipeeLLEEVEEAREKLIealaefddellelylegeelsaeqlr 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 161 ------------FKVIYASAINGWAT---LD-----LDEPSDNMEPMFKMIVEEVSPPDADPEGDFQMQISQLDYNSYVG 220
Cdd:PRK13351 241 aplregtrsghlVPVLFGSALKNIGIeplLDavvdyLPSPLEVPPPRGSKDNGKPVKVDPDPEKPLLALVFKVQYDPYAG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 221 VVGIGRIKRGSVAPNQQVTIISADGTTRNGKIGAVQsylGLERIETDRAYAGNIVTVTGIGELKISDTVCFPGNVEALPP 300
Cdd:PRK13351 321 KLTYLRVYSGTLRAGSQLYNGTGGKREKVGRLFRLQ---GNKREEVDRAKAGDIVAVAGLKELETGDTLHDSADPVLLEL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 301 LSVDEPTVTMTFSVNNSpfcGKEGKfvtsrnIRERLDKELVHNVALRVEDTASPDSFRVSGRGELHLGILIENMRRE-GY 379
Cdd:PRK13351 398 LTFPEPVVSLAVEPERR---GDEQK------LAEALEKLVWEDPSLRVEEDEETGQTILSGMGELHLEVALERLRREfKL 468
|
490
....*....|..
gi 489050914 380 ELSVSRPEVILR 391
Cdd:PRK13351 469 EVNTGKPQVAYR 480
|
|
| BipA_III |
cd16263 |
Domain III of GTP-binding protein BipA (TypA); BipA (also called TypA) is a highly conserved ... |
306-384 |
5.03e-49 |
|
Domain III of GTP-binding protein BipA (TypA); BipA (also called TypA) is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios. It is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion.
Pssm-ID: 293920 [Multi-domain] Cd Length: 79 Bit Score: 164.79 E-value: 5.03e-49
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489050914 306 PTVTMTFSVNNSPFCGKEGKFVTSRNIRERLDKELVHNVALRVEDTASPDSFRVSGRGELHLGILIENMRREGYELSVS 384
Cdd:cd16263 1 PTVSMTFGVNTSPFAGREGKFVTSRKIRDRLEKELETNVALRVEETESPDSFIVSGRGELHLSILIETMRREGFELQVS 79
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
7-198 |
1.36e-48 |
|
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.
Pssm-ID: 206677 [Multi-domain] Cd Length: 179 Bit Score: 167.33 E-value: 1.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 7 RNIAIIAHVDHGKTTLVDKLLEQSGTLETRGGNEErVMDSNDIEKERGITILAKNTAISW-----NDYHINIVDTPGHAD 81
Cdd:cd01890 1 RNFSIIAHIDHGKSTLADRLLELTGTVSEREMKEQ-VLDSMDLERERGITIKAQAVRLFYkakdgEEYLLNLIDTPGHVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 82 FGGEVERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDKPGARPDWVMDQIFDLFDnlgaTDEQldf 161
Cdd:cd01890 80 FSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVKQEIEDVLG----LDAS--- 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 489050914 162 KVIYASAINGwatldldepsDNMEPMFKMIVEEVSPP 198
Cdd:cd01890 153 EAILVSAKTG----------LGVEDLLEAIVERIPPP 179
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
7-198 |
1.07e-46 |
|
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: 163.56 E-value: 1.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 7 RNIAIIAHVDHGKTTLVDKLLEQSGTLETRGGNEERVMDSNDIEKERGITIlaKNTAISW-----------NDYHINIVD 75
Cdd:cd01885 1 RNICIIAHVDHGKTTLSDSLLASAGIISEKLAGKARYLDTREDEQERGITI--KSSAISLyfeyeeekmdgNDYLINLID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 76 TPGHADFGGEVERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDK-------PGARPDWVMDQIFDL 148
Cdd:cd01885 79 SPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDRlilelklSPEEAYQRLLRIVED 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489050914 149 FDNLGATDEQLDFK------------VIYASAINGWAtLDLDEPSDnMEPMFKMIVEEVSPP 198
Cdd:cd01885 159 VNAIIETYAPEEFKqekwkfspqkgnVAFGSALDGWG-FTIIKFAD-IYAVLEMVVKHLPSP 218
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
2-388 |
3.07e-46 |
|
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: 173.69 E-value: 3.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 2 SIEQLRNIAIIAHVDHGKTTLVDKLLEQSGTL----ETRGGNeeRVMDSNDIEKERGITILAKNTAISWNDYHINIVDTP 77
Cdd:COG0480 5 PLEKIRNIGIVAHIDAGKTTLTERILFYTGAIhrigEVHDGN--TVMDWMPEEQERGITITSAATTCEWKGHKINIIDTP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 78 GHADFGGEVERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDKPGARPDWVMDQI------------ 145
Cdd:COG0480 83 GHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQLkerlganpvplq 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 146 --------F----DLF--------DNLGAT--------------------------------------DEQLDFKVIYA- 166
Cdd:COG0480 163 lpigaeddFkgviDLVtmkayvydDELGAKyeeeeipaelkeeaeeareelieavaetddelmekyleGEELTEEEIKAg 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 167 ----------------SAINGWAT---LD-----LDEPSDnMEPM--FKMIVEEVSPPDADPEGDFQMQISQLDYNSYVG 220
Cdd:COG0480 243 lrkatlagkivpvlcgSAFKNKGVqplLDavvdyLPSPLD-VPAIkgVDPDTGEEVERKPDDDEPFSALVFKTMTDPFVG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 221 VVGIGRIKRGSVAPNQQVTIISADGTTRngkIGAVQSYLGLERIETDRAYAGNIVTVTGIGELKISDTVCFPGNVEALPP 300
Cdd:COG0480 322 KLSFFRVYSGTLKSGSTVYNSTKGKKER---IGRLLRMHGNKREEVDEAGAGDIVAVVKLKDTTTGDTLCDEDHPIVLEP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 301 LSVDEPTVTMtfSVnnspfcgkEGKfvtSRNIRERLDKELVHnvaLRVEDtasPdSFRV-----------SGRGELHLGI 369
Cdd:COG0480 399 IEFPEPVISV--AI--------EPK---TKADEDKLSTALAK---LAEED---P-TFRVetdeetgqtiiSGMGELHLEI 458
|
490 500
....*....|....*....|
gi 489050914 370 LIENMRRE-GYELSVSRPEV 388
Cdd:COG0480 459 IVDRLKREfGVEVNVGKPQV 478
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
12-475 |
7.45e-44 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 166.45 E-value: 7.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 12 IAHVDHGKTTLVDKLLEQSGTLETRGGNEE--RVMDSNDIEKERGITILAKNTAISWNDYHINIVDTPGHADFGGEVERV 89
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRIGEVEDgtTTMDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVERA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 90 LSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDKPGARPDWVMDQI------------------------ 145
Cdd:PRK12740 81 LRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRAGADFFRVLAQLqeklgapvvplqlpigegddftgv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 146 ----------------------------------FDLFDNLGATDEQL-----------------DFK----------VI 164
Cdd:PRK12740 161 vdllsmkayrydeggpseeieipaelldraeearEELLEALAEFDDELmekylegeelseeeikaGLRkatlageivpVF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 165 YASAINGWAT---LD-----LDEPSDnMEPMFKMIVEEVSPPDADPEGDFQMQISQLDYNSYVGVVGIGRIKRGSVAPNQ 236
Cdd:PRK12740 241 CGSALKNKGVqrlLDavvdyLPSPLE-VPPVDGEDGEEGAELAPDPDGPLVALVFKTMDDPFVGKLSLVRVYSGTLKKGD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 237 QVTIISADGTTRngkIGAVQSYLGLERIETDRAYAGNIVTVTGIGELKISDTVCFPGNVEALPPLSVDEPtvtmTFSVNN 316
Cdd:PRK12740 320 TLYNSGTGKKER---VGRLYRMHGKQREEVDEAVAGDIVAVAKLKDAATGDTLCDKGDPILLEPMEFPEP----VISLAI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 317 SPfcgkegkfvTSRNIRERLDKELVHnvaLRVEDtasPdSFRV-----------SGRGELHLGILIENMRRE-GYELSVS 384
Cdd:PRK12740 393 EP---------KDKGDEEKLSEALGK---LAEED---P-TLRVerdeetgqtilSGMGELHLDVALERLKREyGVEVETG 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 385 RPEVILR------------------------------------------------------------------------- 391
Cdd:PRK12740 457 PPQVPYRetirkkaeghgrhkkqsgghgqfgdvwleveplprgegfefvdkvvggavprqyipavekgvrealekgvlag 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 392 ----------------TVDG----------------------VLEEPFETVTIDCQEEHQGSVMEQVGLRKGELTNMTPD 433
Cdd:PRK12740 537 ypvvdvkvtltdgsyhSVDSsemafkiaarlafrealpkakpVLLEPIMKVEVSVPEEFVGDVIGDLSSRRGRILGMESR 616
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 489050914 434 GKGrMRLDFMIPSRGLIGFQTDFMTLTSGSGLMYHTFDHYGP 475
Cdd:PRK12740 617 GGG-DVVRAEVPLAEMFGYATDLRSLTQGRGSFSMEFSHYEE 657
|
|
| BipA_TypA_C |
cd03710 |
BipA_TypA_C: a C-terminal portion of BipA or TypA having homology to the C terminal domains of ... |
399-477 |
3.18e-42 |
|
BipA_TypA_C: a C-terminal portion of BipA or TypA having homology to the C terminal domains of the elongation factors EF-G and EF-2. A member of the ribosome binding GTPase superfamily, BipA is widely distributed in bacteria and plants. BipA is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios and, is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion.
Pssm-ID: 239681 [Multi-domain] Cd Length: 79 Bit Score: 146.50 E-value: 3.18e-42
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489050914 399 EPFETVTIDCQEEHQGSVMEQVGLRKGELTNMTPDGKGRMRLDFMIPSRGLIGFQTDFMTLTSGSGLMYHTFDHYGPHK 477
Cdd:cd03710 1 EPIEELTIDVPEEYSGAVIEKLGKRKGEMVDMEPDGNGRTRLEFKIPSRGLIGFRSEFLTDTRGTGIMNHVFDGYEPYK 79
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
8-151 |
1.16e-38 |
|
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.
Pssm-ID: 206731 [Multi-domain] Cd Length: 237 Bit Score: 142.38 E-value: 1.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 8 NIAIIAHVDHGKTTLVDKLLEQSGTLETRGgneeRV------MDSNDIEKERGITILAKNTAISWNDYHINIVDTPGHAD 81
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIRELG----SVdkgttrTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMD 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 82 FGGEVERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDKPGARPDWVMDQIFDLFDN 151
Cdd:cd04168 77 FIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTIIFVNKIDRAGADLEKVYQEIKEKLSP 146
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
8-145 |
1.01e-35 |
|
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: 135.31 E-value: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 8 NIAIIAHVDHGKTTLVDKLLEQSGTL----ETRGGNEerVMDSNDIEKERGITILAKNTAISWNDYHINIVDTPGHADFG 83
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGRIhkigEVHGGGA--TMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDFT 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489050914 84 GEVERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDKPGARPDWVMDQI 145
Cdd:cd01886 79 IEVERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQI 140
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
206-299 |
1.31e-35 |
|
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios and is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion. The domain II of BipA shows similarity to the domain II of the elongation factors (EFs) EF-G and EF-Tu.
Pssm-ID: 293892 [Multi-domain] Cd Length: 94 Bit Score: 128.84 E-value: 1.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 206 FQMQISQLDYNSYVGVVGIGRIKRGSVAPNQQVTIISADGTTRNGKIGAVQSYLGLERIETDRAYAGNIVTVTGIGELKI 285
Cdd:cd03691 1 FQMLVTTLDYDDYLGRIAIGRIFSGTVKVGQQVTVVDEDGKIEKGRVTKLFGFEGLERVEVEEAEAGDIVAIAGLEDITI 80
|
90
....*....|....
gi 489050914 286 SDTVCFPGNVEALP 299
Cdd:cd03691 81 GDTICDPEVPEPLP 94
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
4-133 |
4.62e-32 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 132.09 E-value: 4.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 4 EQLRNIAIIAHVDHGKTTLVDKLLEQSGTLETRGGNEERVMDSNDIEKERGITIlaKNTAISW------------NDYHI 71
Cdd:PTZ00416 17 DQIRNMSVIAHVDHGKSTLTDSLVCKAGIISSKNAGDARFTDTRADEQERGITI--KSTGISLyyehdledgddkQPFLI 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489050914 72 NIVDTPGHADFGGEVERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDK 133
Cdd:PTZ00416 95 NLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKVDR 156
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
7-145 |
1.81e-30 |
|
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.
Pssm-ID: 206732 [Multi-domain] Cd Length: 268 Bit Score: 120.39 E-value: 1.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 7 RNIAIIAHVDHGKTTLVDKLL------EQSGTLETRGGNEERVMDSNDIEKERGITILAKNTAISWNDYHINIVDTPGHA 80
Cdd:cd04169 3 RTFAIISHPDAGKTTLTEKLLlfggaiQEAGAVKARKSRKHATSDWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHE 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489050914 81 DFGGEVERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDKPGARPDWVMDQI 145
Cdd:cd04169 83 DFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDREGRDPLELLDEI 147
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
7-133 |
3.92e-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: 117.75 E-value: 3.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 7 RNIAIIAHVDHGKTTLVDKLLEQSGTLET---RGGNEERVMDSNDIEKERGITIlaKNTAISW-------NDYHINIVDT 76
Cdd:cd04167 1 RNVCIAGHLHHGKTSLLDMLIEQTHKRTPsvkLGWKPLRYTDTRKDEQERGISI--KSNPISLvledskgKSYLINIIDT 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 489050914 77 PGHADFGGEVERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDK 133
Cdd:cd04167 79 PGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDR 135
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
6-133 |
3.58e-29 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 123.30 E-value: 3.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 6 LRNIAIIAHVDHGKTTLVDKLLEQSGTLETRGGNEERVMDSNDIEKERGITIlaKNTAISW------------------N 67
Cdd:PLN00116 19 IRNMSVIAHVDHGKSTLTDSLVAAAGIIAQEVAGDVRMTDTRADEAERGITI--KSTGISLyyemtdeslkdfkgerdgN 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489050914 68 DYHINIVDTPGHADFGGEVERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDK 133
Cdd:PLN00116 97 EYLINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTETVLRQALGERIRPVLTVNKMDR 162
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
8-151 |
2.49e-28 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 114.23 E-value: 2.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 8 NIAIIAHVDHGKTTLVDKLLEQSGTLETRGGNEE--RVMDSNDIEKERGITILAKNTAISWNDYHINIVDTPGHADFGGE 85
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRLGRVEDgnTVSDYDPEEKKRKMSIETSVAPLEWNGHKINLIDTPGYADFVGE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489050914 86 VERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDKPGARPDWVMDQIFDLFDN 151
Cdd:cd04170 81 TLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRARADFDKTLAALREAFGR 146
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
8-305 |
1.04e-26 |
|
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444074 [Multi-domain] Cd Length: 423 Bit Score: 113.10 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 8 NIAIIAHVDHGKTTLVDKLLEQSGTL------ETRGGNEER---------VMDSNDIEKERGITILAKNTAISWNDYHIN 72
Cdd:COG5256 9 NLVVIGHVDHGKSTLVGRLLYETGAIdehiieKYEEEAEKKgkesfkfawVMDRLKEERERGVTIDLAHKKFETDKYYFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 73 IVDTPGHADFggeVERVL---SMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVV-INKIDKPG---ARPDWVMDQI 145
Cdd:COG5256 89 IIDAPGHRDF---VKNMItgaSQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVaVNKMDAVNyseKRYEEVKEEV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 146 FDLFDNLGATDEQLDFkvIYASAINGwatLDLDEPSDNMePMFK--MIVE---EVSPPDADPEGDFQMQIsQLDYN-SYV 219
Cdd:COG5256 166 SKLLKMVGYKVDKIPF--IPVSAWKG---DNVVKKSDNM-PWYNgpTLLEaldNLKEPEKPVDKPLRIPI-QDVYSiSGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 220 GVVGIGRIKRGSVAPNQQVTIISAdgttrnGKIGAVQSylglerIET-----DRAYAG-NI-VTVTGIGE--LKISDTVC 290
Cdd:COG5256 239 GTVPVGRVETGVLKVGDKVVFMPA------GVVGEVKS------IEMhheelEQAEPGdNIgFNVRGVEKndIKRGDVAG 306
|
330
....*....|....*
gi 489050914 291 FPGNvealPPLSVDE 305
Cdd:COG5256 307 HPDN----PPTVAEE 317
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
8-312 |
2.36e-25 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 108.86 E-value: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 8 NIAIIAHVDHGKTTLVDKLLEQSGTL------ETRGGNEER---------VMDSNDIEKERGITILAKNTAISWNDYHIN 72
Cdd:PRK12317 8 NLAVIGHVDHGKSTLVGRLLYETGAIdehiieELREEAKEKgkesfkfawVMDRLKEERERGVTIDLAHKKFETDKYYFT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 73 IVDTPGHADFggeVERVL---SMADSVLLLVDAQE--GPMPQTRfvtQKAF-AQGL---KPIVVINKIDKPG---ARPDW 140
Cdd:PRK12317 88 IVDCPGHRDF---VKNMItgaSQADAAVLVVAADDagGVMPQTR---EHVFlARTLginQLIVAINKMDAVNydeKRYEE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 141 VMDQIFDLFDNLGATDEQLDFkvIYASAINGwatLDLDEPSDNMePMFK--MIVE---EVSPPDADPEGDFQMQISQLDY 215
Cdd:PRK12317 162 VKEEVSKLLKMVGYKPDDIPF--IPVSAFEG---DNVVKKSENM-PWYNgpTLLEaldNLKPPEKPTDKPLRIPIQDVYS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 216 NSYVGVVGIGRIKRGSVAPNQQVTIISAdgttrnGKIGAVQSylglerIET-----DRAYAG-NI-VTVTGIG--ELKIS 286
Cdd:PRK12317 236 ISGVGTVPVGRVETGVLKVGDKVVFMPA------GVVGEVKS------IEMhheelPQAEPGdNIgFNVRGVGkkDIKRG 303
|
330 340
....*....|....*....|....*.
gi 489050914 287 DtVCFPGNvealpplsvDEPTVTMTF 312
Cdd:PRK12317 304 D-VCGHPD---------NPPTVAEEF 319
|
|
| EFG_C |
pfam00679 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
396-475 |
3.37e-24 |
|
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of Elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopt a ferredoxin-like fold.
Pssm-ID: 425814 [Multi-domain] Cd Length: 88 Bit Score: 96.46 E-value: 3.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 396 VLEEPFETVTIDCQEEHQGSVMEQVGLRKGELTNMTPDGKGRMRLDFMIPSRGLIGFQTDFMTLTSGSGLMYHTFDHYGP 475
Cdd:pfam00679 1 VLLEPIEKVTIDVPEEYVGDVISDLNSRRGEILDMDPDDGGRVVIEAEVPLAELFGFATELRSLTKGRGSFSMEFSGYQP 80
|
|
| Elongation_Factor_C |
cd01514 |
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ... |
399-477 |
4.27e-23 |
|
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of elongation factors (EFs) bacterial EF-G, eukaryotic and archeal EF-2 and eukaryotic mitochondrial mtEFG1s and mtEFG2s. This group also includes proteins similar to the ribosomal protection proteins Tet(M) and Tet(O), BipA, LepA and, spliceosomal proteins: human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and yeast counterpart Snu114p. This domain adopts a ferredoxin-like fold consisting of an alpha-beta sandwich with anti-parallel beta-sheets, resembling the topology of domain III found in the elongation factors EF-G and eukaryotic EF-2, with which it forms the C-terminal block. The two domains however are not superimposable and domain III lacks some of the characteristics of this domain. EF-2/EF-G in complex with GTP, promotes the translocation step of translation. During translocation the peptidyl-tRNA is moved from the A site to the P site, the uncharged tRNA from the P site to the E-site and, the mRNA is shifted one codon relative to the ribosome. Tet(M) and Tet(O) mediate Tc resistance. Typical Tcs bind to the ribosome and inhibit the elongation phase of protein synthesis, by inhibiting the occupation of site A by aminoacyl-tRNA. Tet(M) and Tet(O) catalyze the release of tetracycline (Tc) from the ribosome in a GTP-dependent manner. BipA is a highly conserved protein with global regulatory properties in Escherichia coli. Yeast Snu114p is essential for cell viability and for splicing in vivo. Experiments suggest that GTP binding and probably GTP hydrolysis is important for the function of the U5-116 kD/Snu114p. The function of LepA proteins is unknown.
Pssm-ID: 238772 [Multi-domain] Cd Length: 79 Bit Score: 93.32 E-value: 4.27e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489050914 399 EPFETVTIDCQEEHQGSVMEQVGLRKGELTNMTPDGKGRMRLDFMIPSRGLIGFQTDFMTLTSGSGLMYHTFDHYGPHK 477
Cdd:cd01514 1 EPIMKVEITVPEEYLGAVIGDLSKRRGEILGMEPRGTGRVVIKAELPLAEMFGFATDLRSLTQGRASFSMEFSHYEPVP 79
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
3-145 |
3.74e-21 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 97.13 E-value: 3.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 3 IEQLRNIAIIAHVDHGKTTLVDKLL------EQSGTLETRGGNEERVMDSNDIEKERGITILAKNTAISWNDYHINIVDT 76
Cdd:PRK00741 7 VAKRRTFAIISHPDAGKTTLTEKLLlfggaiQEAGTVKGRKSGRHATSDWMEMEKQRGISVTSSVMQFPYRDCLINLLDT 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489050914 77 PGHADFGGEVERVLSMADSVLLLVDAQEGPMPQTRfvtqKAF----AQGLkPIVV-INKIDKPGARPDWVMDQI 145
Cdd:PRK00741 87 PGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTR----KLMevcrLRDT-PIFTfINKLDRDGREPLELLDEI 155
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
8-184 |
1.81e-20 |
|
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 206670 [Multi-domain] Cd Length: 219 Bit Score: 90.24 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 8 NIAIIAHVDHGKTTLVDKLLEQSG-----TLETRGGNEER----------VMDSNDIEKERGITILAKNTAISWNDYHIN 72
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGgvdkrTIEKYEKEAKEmgkesfkyawVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 73 IVDTPGHADFggeverVLSM------ADSVLLLVDAQEG-------PMPQTRFVTQKAFAQGLKP-IVVINKIDKPG--- 135
Cdd:cd01883 81 IIDAPGHRDF------VKNMitgasqADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQlIVAVNKMDDVTvnw 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489050914 136 --ARPDWVMDQIFDLFDNLGATDEQLDFkviyaSAINGWATLDLDEPSDNM 184
Cdd:cd01883 155 sqERYDEIKKKVSPFLKKVGYNPKDVPF-----IPISGFTGDNLIEKSENM 200
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
9-171 |
7.90e-20 |
|
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.
Pssm-ID: 206674 [Multi-domain] Cd Length: 169 Bit Score: 86.76 E-value: 7.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 9 IAIIAHVDHGKTTLVDKLleqsgtletRGgneervmdSNDIEKE-RGIT--ILAKNTAISWNDYHINIVDTPGHADFGGE 85
Cdd:cd01887 3 VTVMGHVDHGKTTLLDKI---------RK--------TNVAAGEaGGITqhIGAYQVPIDVKIPGITFIDTPGHEAFTNM 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 86 VERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDKP---GARPDWVMDQIFDLfdNLGATDEQLDFK 162
Cdd:cd01887 66 RARGASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKPygtEADPERVKNELSEL--GLVGEEWGGDVS 143
|
....*....
gi 489050914 163 VIYASAING 171
Cdd:cd01887 144 IVPISAKTG 152
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
8-248 |
2.73e-18 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 87.31 E-value: 2.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 8 NIAIIAHVDHGKTTLVDKLleqSGTLETRGGNEERVMDSNDI---EKERGITIlakNTA-ISWN--DYHINIVDTPGHAD 81
Cdd:PRK12736 14 NIGTIGHVDHGKTTLTAAI---TKVLAERGLNQAKDYDSIDAapeEKERGITI---NTAhVEYEteKRHYAHVDCPGHAD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 82 FggeVERVLSMA---DSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVV-INKIDKPGARP--DWVMDQIFDLFDNLGAT 155
Cdd:PRK12736 88 Y---VKNMITGAaqmDGAILVVAATDGPMPQTREHILLARQVGVPYLVVfLNKVDLVDDEEllELVEMEVRELLSEYDFP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 156 DEqlDFKVIYASAIngwATLDLDEP-SDNMEPMFKMIVEEVSPPDADPEGDFQMQISQLDYNSYVGVVGIGRIKRGSVAP 234
Cdd:PRK12736 165 GD--DIPVIRGSAL---KALEGDPKwEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKV 239
|
250
....*....|....
gi 489050914 235 NQQVTIISADGTTR 248
Cdd:PRK12736 240 GDEVEIVGIKETQK 253
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
8-295 |
3.05e-18 |
|
translation elongation factor TU; This model models orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts, one of several GTP-binding translation factors found by the more general pfam model GTP_EFTU. The eukaryotic conterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this model. EF-Tu is one of the most abundant proteins in bacteria, as well as one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation. [Protein synthesis, Translation factors]
Pssm-ID: 129576 [Multi-domain] Cd Length: 394 Bit Score: 87.14 E-value: 3.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 8 NIAIIAHVDHGKTTLVDKLleqSGTLETRGGNEERVMDSNDI---EKERGITILAKNTAISWNDYHINIVDTPGHADFgg 84
Cdd:TIGR00485 14 NVGTIGHVDHGKTTLTAAI---TTVLAKEGGAAARAYDQIDNapeEKARGITINTAHVEYETETRHYAHVDCPGHADY-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 85 eVERVLSMA---DSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVV-INKIDKPGARP--DWVMDQIFDLFdnlgatdEQ 158
Cdd:TIGR00485 89 -VKNMITGAaqmDGAILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKCDMVDDEEllELVEMEVRELL-------SQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 159 LDFKVIYASAINGWATLDLDEPSDNMEPMFKMI--VEEVSP-PDADPEGDFQMQISQLDYNSYVGVVGIGRIKRGSVAPN 235
Cdd:TIGR00485 161 YDFPGDDTPIIRGSALKALEGDAEWEAKILELMdaVDEYIPtPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVG 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489050914 236 QQVTIISADgTTRNGKIGAVQSYlgleRIETDRAYAGNIVTV--TGIG--ELKISDTVCFPGNV 295
Cdd:TIGR00485 241 EEVEIVGLK-DTRKTTVTGVEMF----RKELDEGRAGDNVGLllRGIKreEIERGMVLAKPGSI 299
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
8-247 |
8.25e-18 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 86.34 E-value: 8.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 8 NIAIIAHVDHGKTTLVDKLLEQSGTLETRGGN--EER-------------VMDSNDIEKERGITIlakntAIS-W----N 67
Cdd:PTZ00141 9 NLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEkfEKEaaemgkgsfkyawVLDKLKAERERGITI-----DIAlWkfetP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 68 DYHINIVDTPGHADFGGEVERVLSMADSVLLLVDAQEGPMP-------QTRFVTQKAFAQGLKPIVV-INKIDKPG---- 135
Cdd:PTZ00141 84 KYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVcINKMDDKTvnys 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 136 -ARPDWVMDQIFDLFDNLGATDEQLDFkviyaSAINGWATLDLDEPSDNME----PMFKMIVEEVSPPDADPEGDFQMQI 210
Cdd:PTZ00141 164 qERYDEIKKEVSAYLKKVGYNPEKVPF-----IPISGWQGDNMIEKSDNMPwykgPTLLEALDTLEPPKRPVDKPLRLPL 238
|
250 260 270
....*....|....*....|....*....|....*..
gi 489050914 211 SQLDYNSYVGVVGIGRIKRGSVAPNQQVTIISADGTT 247
Cdd:PTZ00141 239 QDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTT 275
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
7-139 |
1.02e-17 |
|
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]
Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 80.49 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 7 RNIAIIAHVDHGKTTLVDKLLEQSGTLETRGGNEERvMDSNDIEKERGITILakntaiswndyhINIVDTPGHADF---- 82
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTR-NYVTTVIEEDGKTYK------------FNLLDTAGQEDYdair 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 83 ---GGEVERVLSMADSVLLLVDAQEGPMPQTRFVTQKAfAQGLKPIVVINKIDKPGARPD 139
Cdd:TIGR00231 69 rlyYPQVERSLRVFDIVILVLDVEEILEKQTKEIIHHA-DSGVPIILVGNKIDLKDADLK 127
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
9-252 |
1.32e-16 |
|
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]
Pssm-ID: 273102 [Multi-domain] Cd Length: 587 Bit Score: 83.28 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 9 IAIIAHVDHGKTTLVDKLlEQSGTLETRGGNEERVMDSNDIEKErgitilakntaiswNDYHINIVDTPGHADFGGEVER 88
Cdd:TIGR00487 90 VTIMGHVDHGKTSLLDSI-RKTKVAQGEAGGITQHIGAYHVENE--------------DGKMITFLDTPGHEAFTSMRAR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 89 VLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDKPGARPDWVMDQIfdlfDNLGATDEQLDFKVIYA-- 166
Cdd:TIGR00487 155 GAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVPIIVAINKIDKPEANPDRVKQEL----SEYGLVPEDWGGDTIFVpv 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 167 SAINGwatLDLDEPSDNMepmfkMIVEEVSPPDADPEGdfqmqisqldynSYVGVVGIGRIK--RGSVApnqqvTIISAD 244
Cdd:TIGR00487 231 SALTG---DGIDELLDMI-----LLQSEVEELKANPNG------------QASGVVIEAQLDkgRGPVA-----TVLVQS 285
|
....*...
gi 489050914 245 GTTRNGKI 252
Cdd:TIGR00487 286 GTLRVGDI 293
|
|
| tufA |
CHL00071 |
elongation factor Tu |
8-246 |
2.40e-16 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 81.54 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 8 NIAIIAHVDHGKTTLVDKLleqSGTLETRGGNEERVMDSNDI---EKERGITIlakNTA---ISWNDYHINIVDTPGHAD 81
Cdd:CHL00071 14 NIGTIGHVDHGKTTLTAAI---TMTLAAKGGAKAKKYDEIDSapeEKARGITI---NTAhveYETENRHYAHVDCPGHAD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 82 FggeVERVLSMA---DSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVV-INKIDKpgarpdwVMD---------QIFDL 148
Cdd:CHL00071 88 Y---VKNMITGAaqmDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVfLNKEDQ-------VDDeellelvelEVREL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 149 FDNLGATDEQLDFkviyasaINGWATLDLDEPSDN----------MEPMFKMI--VEEVSP-PDADPEGDFQMQISQLDY 215
Cdd:CHL00071 158 LSKYDFPGDDIPI-------VSGSALLALEALTENpkikrgenkwVDKIYNLMdaVDSYIPtPERDTDKPFLMAIEDVFS 230
|
250 260 270
....*....|....*....|....*....|.
gi 489050914 216 NSYVGVVGIGRIKRGSVAPNQQVTIISADGT 246
Cdd:CHL00071 231 ITGRGTVATGRIERGTVKVGDTVEIVGLRET 261
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
8-241 |
3.47e-16 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 81.41 E-value: 3.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 8 NIAIIAHVDHGKTTL---VDKLLEQSGTLETRGGNEervMDSNDIEKERGITILAKNTAISWNDYHINIVDTPGHADFgg 84
Cdd:PLN03127 63 NVGTIGHVDHGKTTLtaaITKVLAEEGKAKAVAFDE---IDKAPEEKARGITIATAHVEYETAKRHYAHVDCPGHADY-- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 85 eVERVLSMA---DSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVV-INKIDkpgarpdwVMD--QIFDLFDNlgATDEQ 158
Cdd:PLN03127 138 -VKNMITGAaqmDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVfLNKVD--------VVDdeELLELVEM--ELREL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 159 LDF--------KVIYASAINGWATLDLDEPSDNMEPMFKMIVEEVSPPDADPEGDFQMQISQLDYNSYVGVVGIGRIKRG 230
Cdd:PLN03127 207 LSFykfpgdeiPIIRGSALSALQGTNDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQG 286
|
250
....*....|.
gi 489050914 231 SVAPNQQVTII 241
Cdd:PLN03127 287 TIKVGEEVEIV 297
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
8-241 |
3.78e-16 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 80.62 E-value: 3.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 8 NIAIIAHVDHGKTTLVDKLleqSGTLETRGGNEERVMDSNDI---EKERGITIlakNTAiswndyHINI---------VD 75
Cdd:PRK00049 14 NVGTIGHVDHGKTTLTAAI---TKVLAKKGGAEAKAYDQIDKapeEKARGITI---NTA------HVEYetekrhyahVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 76 TPGHADFggeVERVLSMA---DSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVV-INKIDKpgarpdwVMD-------- 143
Cdd:PRK00049 82 CPGHADY---VKNMITGAaqmDGAILVVSAADGPMPQTREHILLARQVGVPYIVVfLNKCDM-------VDDeellelve 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 144 -QIFDLFDNLGATDEqlDFKVIYASAIngwATLDLDEPSDNMEPMFKMI--VEEVSP-PDADPEGDFQMQISQLDYNSYV 219
Cdd:PRK00049 152 mEVRELLSKYDFPGD--DTPIIRGSAL---KALEGDDDEEWEKKILELMdaVDSYIPtPERAIDKPFLMPIEDVFSISGR 226
|
250 260
....*....|....*....|..
gi 489050914 220 GVVGIGRIKRGSVAPNQQVTII 241
Cdd:PRK00049 227 GTVVTGRVERGIIKVGEEVEIV 248
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
11-141 |
7.91e-16 |
|
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: 80.73 E-value: 7.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 11 IIA---HVDHGKTTLV--------DKLLEqsgtletrggneervmdsndiEKERGITI--------LAkntaiswNDYHI 71
Cdd:COG3276 2 IIGtagHIDHGKTTLVkaltgidtDRLKE---------------------EKKRGITIdlgfaylpLP-------DGRRL 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 72 NIVDTPGHADF--------GGevervlsmADSVLLLVDAQEGPMPQTR-------FVtqkafaqGLKP-IVVINKIDKpg 135
Cdd:COG3276 54 GFVDVPGHEKFiknmlagaGG--------IDLVLLVVAADEGVMPQTRehlaildLL-------GIKRgIVVLTKADL-- 116
|
....*.
gi 489050914 136 ARPDWV 141
Cdd:COG3276 117 VDEEWL 122
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
9-144 |
8.80e-16 |
|
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: 80.44 E-value: 8.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 9 IAIIAHVDHGKTTLVDKLLEqsgtletrggneervmdSNDIEKE-RGIT--ILAkntaiswndYHINI-------VDTPG 78
Cdd:COG0532 7 VTVMGHVDHGKTSLLDAIRK-----------------TNVAAGEaGGITqhIGA---------YQVETnggkitfLDTPG 60
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489050914 79 HADF------GGEVervlsmADSVLLLVDAQEGPMPQTRFVTQKAFAQGLkPIVV-INKIDKPGARPDWVMDQ 144
Cdd:COG0532 61 HEAFtamrarGAQV------TDIVILVVAADDGVMPQTIEAINHAKAAGV-PIIVaINKIDKPGANPDRVKQE 126
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
8-132 |
9.85e-16 |
|
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: 79.42 E-value: 9.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 8 NIAIIAHVDHGKTTLVDKLleqSGTLETRGGNEERVMDSNDI---EKERGITIlakntAISWNDY-----HINIVDTPGH 79
Cdd:COG0050 14 NIGTIGHVDHGKTTLTAAI---TKVLAKKGGAKAKAYDQIDKapeEKERGITI-----NTSHVEYetekrHYAHVDCPGH 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 80 ADFggeverVLSM------ADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVV-INKID 132
Cdd:COG0050 86 ADY------VKNMitgaaqMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKCD 139
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
9-145 |
1.25e-15 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 80.26 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 9 IAIIAHVDHGKTTLVDKlleqsgtletrggneerVMDSNDIEKER-GIT--ILAKNTAISWNDYHINIV--DTPGHADFG 83
Cdd:CHL00189 247 VTILGHVDHGKTTLLDK-----------------IRKTQIAQKEAgGITqkIGAYEVEFEYKDENQKIVflDTPGHEAFS 309
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489050914 84 GEVERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDKPGARPDWVMDQI 145
Cdd:CHL00189 310 SMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANTERIKQQL 371
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
8-132 |
2.05e-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: 74.71 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 8 NIAIIAHVDHGKTTLVDKLLEQSGTletrggneeRVMDSNDIEKERGITI--------------LAKNTAISWNDYHINI 73
Cdd:cd01889 2 NVGLLGHVDSGKTSLAKALSEIAST---------AAFDKNPQSQERGITLdlgfssfevdkpkhLEDNENPQIENYQITL 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489050914 74 VDTPGHADFggeVERVLSMA---DSVLLLVDAQEGPMPQTRF------VTQKafaqglKPIVVINKID 132
Cdd:cd01889 73 VDCPGHASL---IRTIIGGAqiiDLMLLVVDAKKGIQTQTAEclvigeLLCK------PLIVVLNKID 131
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
8-132 |
2.11e-15 |
|
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: 74.93 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 8 NIAIIAHVDHGKTTLVDKLleqSGTLETRGGNEERVMDSNDI---EKERGITIlakNTA------ISWNDYHiniVDTPG 78
Cdd:cd01884 4 NVGTIGHVDHGKTTLTAAI---TKVLAKKGGAKAKKYDEIDKapeEKARGITI---NTAhveyetANRHYAH---VDCPG 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 489050914 79 HADFggeVERVLSMA---DSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVV-INKID 132
Cdd:cd01884 75 HADY---IKNMITGAaqmDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVfLNKAD 129
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
8-132 |
2.13e-15 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 78.34 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 8 NIAIIAHVDHGKTTLVDKLleqSGTLETRGGNEERVMDSNDI---EKERGITIlakntAISWNDY-----HINIVDTPGH 79
Cdd:PRK12735 14 NVGTIGHVDHGKTTLTAAI---TKVLAKKGGGEAKAYDQIDNapeEKARGITI-----NTSHVEYetanrHYAHVDCPGH 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 489050914 80 ADFggeVERVLSMA---DSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVV-INKID 132
Cdd:PRK12735 86 ADY---VKNMITGAaqmDGAILVVSAADGPMPQTREHILLARQVGVPYIVVfLNKCD 139
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
8-275 |
9.32e-15 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 76.96 E-value: 9.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 8 NIAIIAHVDHGKTTLVDKLleqSGTLETRGGNEERVMDSNDI---EKERGITILAKNTAISWNDYHINIVDTPGHADFGG 84
Cdd:PLN03126 83 NIGTIGHVDHGKTTLTAAL---TMALASMGGSAPKKYDEIDAapeERARGITINTATVEYETENRHYAHVDCPGHADYVK 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 85 EVERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVV-INKIDKPGARP--DWVMDQIFDLFDNLGATDEqlDF 161
Cdd:PLN03126 160 NMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVfLNKQDQVDDEEllELVELEVRELLSSYEFPGD--DI 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 162 KVIYASAINGWATLdLDEPS----DN--MEPMFKMI--VEEVSP-PDADPEGDFQMQISQLDYNSYVGVVGIGRIKRGSV 232
Cdd:PLN03126 238 PIISGSALLALEAL-MENPNikrgDNkwVDKIYELMdaVDSYIPiPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTV 316
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 489050914 233 APNQQVTIISAdGTTRNGKIGAVQSYlgleRIETDRAYAGNIV 275
Cdd:PLN03126 317 KVGETVDIVGL-RETRSTTVTGVEMF----QKILDEALAGDNV 354
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
8-133 |
1.89e-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: 76.45 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 8 NIAIIAHVDHGKTTLVDKLLEQSGtletrggneervmDSNDIEKERGITILAKNTAISWNDYHINIVDTPGHADFGGEVE 87
Cdd:TIGR00475 2 IIATAGHVDHGKTTLLKALTGIAA-------------DRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNAI 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 489050914 88 RVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKP-IVVINKIDK 133
Cdd:TIGR00475 69 AGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHtIVVITKADR 115
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
14-171 |
2.42e-14 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.
Pssm-ID: 206734 [Multi-domain] Cd Length: 170 Bit Score: 71.10 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 14 HVDHGKTTLVDKLleqSGTlETrggneervmDSNDIEKERGITIlakNTAISWNDY----HINIVDTPGHADFggeVERV 89
Cdd:cd04171 7 HIDHGKTTLIKAL---TGI-ET---------DRLPEEKKRGITI---DLGFAYLDLpdgkRLGFIDVPGHEKF---VKNM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 90 LSMA---DSVLLLVDAQEGPMPQTRFVTQKAFAQGLKP-IVVINKIDKpgARPDWVMDQIFDLFDNLGATDEQlDFKVIY 165
Cdd:cd04171 68 LAGAggiDAVLLVVAADEGIMPQTREHLEILELLGIKKgLVVLTKADL--VDEDRLELVEEEILELLAGTFLA-DAPIFP 144
|
....*.
gi 489050914 166 ASAING 171
Cdd:cd04171 145 VSSVTG 150
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
10-193 |
4.18e-14 |
|
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: 70.18 E-value: 4.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 10 AIIAHVDHGKTTLVDKLLeqsgtletrggNEERVMDSNDIEKERGITILAKNtaISWNDYHINIVDTPGHADFGG----- 84
Cdd:cd00882 1 VVVGRGGVGKSSLLNALL-----------GGEVGEVSDVPGTTRDPDVYVKE--LDKGKVKLVLVDTPGLDEFGGlgree 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 85 EVERVLSMADSVLLLVDAQEGPMPQ--TRFVTQKAFAQGLKPIVVINKIDKPGARPDWVMDQIFDLFdnlgatdEQLDFK 162
Cdd:cd00882 68 LARLLLRGADLILLVVDSTDRESEEdaKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELA-------KILGVP 140
|
170 180 190
....*....|....*....|....*....|.
gi 489050914 163 VIYASAINGWatldldepsdNMEPMFKMIVE 193
Cdd:cd00882 141 VFEVSAKTGE----------GVDELFEKLIE 161
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
8-247 |
5.30e-14 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 74.36 E-value: 5.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 8 NIAIIAHVDHGKTT---------------LVDKLLEQSGTLETRGGNEERVMDSNDIEKERGITILAKNTAISWNDYHIN 72
Cdd:PLN00043 9 NIVVIGHVDSGKSTttghliyklggidkrVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYYCT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 73 IVDTPGHADFGGEVERVLSMADSVLLLVDAQEGPMP-------QTRFVTQKAFAQGLKPIV-VINKIDK-----PGARPD 139
Cdd:PLN00043 89 VIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMIcCCNKMDAttpkySKARYD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 140 WVMDQIFDLFDNLGATDEQLDFkviyaSAINGWATLDLDEPSDNME----PMFKMIVEEVSPPDADPEGDFQMQISQLDY 215
Cdd:PLN00043 169 EIVKEVSSYLKKVGYNPDKIPF-----VPISGFEGDNMIERSTNLDwykgPTLLEALDQINEPKRPSDKPLRLPLQDVYK 243
|
250 260 270
....*....|....*....|....*....|..
gi 489050914 216 NSYVGVVGIGRIKRGSVAPNQQVTIISADGTT 247
Cdd:PLN00043 244 IGGIGTVPVGRVETGVIKPGMVVTFGPTGLTT 275
|
|
| EFG_III-like |
cd16257 |
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G ... |
306-384 |
8.33e-14 |
|
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G (EF-G) and related proteins play a role in translation and share a similar domain architecture. Elongation factor EFG participates in the elongation phase during protein biosynthesis on the ribosome by stimulating translocation. Its functional cycles depend on GTP binding and its hydrolysis. Domain III is involved in the activation of GTP hydrolysis. This domain III, which is different from domain III in EF-TU and related elongation factors, is found in several translation factors, like bacterial release factors RF3, elongation factor 4, elongation factor 2, GTP-binding protein BipA and tetracycline resistance protein Tet.
Pssm-ID: 293914 [Multi-domain] Cd Length: 71 Bit Score: 66.60 E-value: 8.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 306 PTVTMTFSVNNspfcgkegkFVTSRNIRERLDKELVHNVALRVEDTASPDSFRVSGRGELHLGILIENMRRE-GYELSVS 384
Cdd:cd16257 1 PVVFVTVEVKN---------PLDQEKLLEGLERLSEEDPALQVYREESTGEFILSGLGELHLEIIVARLEREyGVELVVS 71
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
4-278 |
8.94e-14 |
|
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and metabolism]; Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 442140 [Multi-domain] Cd Length: 430 Bit Score: 73.58 E-value: 8.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 4 EQLRnIAIIAHVDHGKTTLVDKLLEQS-----GTLET------RGGNEE----RVMDSNDIEKERGITI--------LAK 60
Cdd:COG2895 16 DLLR-FITCGSVDDGKSTLIGRLLYDTksifeDQLAAlerdskKRGTQEidlaLLTDGLQAEREQGITIdvayryfsTPK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 61 NTAIswndyhinIVDTPGHADF------GGevervlSMADSVLLLVDAQEGPMPQTR---FVtqkafAQ--GLKPIVV-I 128
Cdd:COG2895 95 RKFI--------IADTPGHEQYtrnmvtGA------STADLAILLIDARKGVLEQTRrhsYI-----ASllGIRHVVVaV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 129 NKIDkpgaRPDW---VMDQIFDLFDNLGAtdeQLDFKVIYA---SAINGwatldlD---EPSDNMePMFK----M-IVEE 194
Cdd:COG2895 156 NKMD----LVDYseeVFEEIVADYRAFAA---KLGLEDITFipiSALKG------DnvvERSENM-PWYDgptlLeHLET 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 195 VSPPDADPEGDFQMQI-----SQLDYNSYVgvvgiGRIKRGSVAPNQQVTIISADGTTRngkigavqsylgLERIET--- 266
Cdd:COG2895 222 VEVAEDRNDAPFRFPVqyvnrPNLDFRGYA-----GTIASGTVRVGDEVVVLPSGKTST------------VKSIVTfdg 284
|
330
....*....|....
gi 489050914 267 --DRAYAGNIVTVT 278
Cdd:COG2895 285 dlEEAFAGQSVTLT 298
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
15-305 |
3.52e-13 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 72.27 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 15 VDHGKTTLVDKLL--------EQSGTLE----TRGGNEERV-----MDSNDIEKERGITI--------LAKNTAIswndy 69
Cdd:PRK05506 33 VDDGKSTLIGRLLydskmifeDQLAALErdskKVGTQGDEIdlallVDGLAAEREQGITIdvayryfaTPKRKFI----- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 70 hinIVDTPGHADFGGEVERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVV-INKIDKPGARPDwVMDQIFDL 148
Cdd:PRK05506 108 ---VADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLaVNKMDLVDYDQE-VFDEIVAD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 149 FDNLGATDEQLDFKVIYASAINGwatlD-LDEPSDNME----PMFKMIVEEVSPPDADPEGDFQMQI-----SQLDYNSY 218
Cdd:PRK05506 184 YRAFAAKLGLHDVTFIPISALKG----DnVVTRSARMPwyegPSLLEHLETVEIASDRNLKDFRFPVqyvnrPNLDFRGF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 219 VGVVGIGRIKRG---SVAPNQQVT----IISADGttrngkigavqsylgleriETDRAYAGNIVTVTGIGELKIS--DTV 289
Cdd:PRK05506 260 AGTVASGVVRPGdevVVLPSGKTSrvkrIVTPDG-------------------DLDEAFAGQAVTLTLADEIDISrgDML 320
|
330
....*....|....*.
gi 489050914 290 CFPGNvealPPLSVDE 305
Cdd:PRK05506 321 ARADN----RPEVADQ 332
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
15-286 |
8.04e-13 |
|
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules. With members of the Rhizobiaceae family, nodQ often appears as a fusion of cysN (large subunit of ATP sulfurase) and cysC (APS kinase). [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 213679 [Multi-domain] Cd Length: 406 Bit Score: 70.48 E-value: 8.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 15 VDHGKTTLVDKLL--------EQSGTLET---RGGNEER------VMDSNDIEKERGITILAKNTAISWNDYHINIVDTP 77
Cdd:TIGR02034 9 VDDGKSTLIGRLLhdtkqiyeDQLAALERdskKHGTQGGeidlalLVDGLQAEREQGITIDVAYRYFSTDKRKFIVADTP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 78 GHADFGGEVERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVV-INKIDKPGARPDwVMDQIFDLFDNLGatd 156
Cdd:TIGR02034 89 GHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLaVNKMDLVDYDEE-VFENIKKDYLAFA--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 157 EQLDFKVIYASAINGWATLDLDEPSDNME----PMFKMIVEEVSPPDADPEGDFQMQIS-----QLDYNSYVGVvgigrI 227
Cdd:TIGR02034 165 EQLGFRDVTFIPLSALKGDNVVSRSESMPwysgPTLLEILETVEVERDAQDLPLRFPVQyvnrpNLDFRGYAGT-----I 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 489050914 228 KRGSVAPNQQVTIISADGTTRNGKIgavQSYLGleriETDRAYAGNIVTVTGIGELKIS 286
Cdd:TIGR02034 240 ASGSVHVGDEVVVLPSGRSSRVARI---VTFDG----DLEQARAGQAVTLTLDDEIDIS 291
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
8-171 |
2.15e-12 |
|
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN.
Pssm-ID: 206729 [Multi-domain] Cd Length: 209 Bit Score: 66.44 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 8 NIAIIAHVDHGKTTLVDKLLEQSGTL-----------ETRGGNEERV-----MDSNDIEKERGITI--------LAKNTA 63
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSIfedqlaalersKSSGTQGEKLdlallVDGLQAEREQGITIdvayryfsTPKRKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 64 IswndyhinIVDTPGHADFGGEVERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVV-INKIDKPGARPDwVM 142
Cdd:cd04166 81 I--------IADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVaVNKMDLVDYDEE-VF 151
|
170 180
....*....|....*....|....*....
gi 489050914 143 DQIFDLFDNLGATDEQLDFKVIYASAING 171
Cdd:cd04166 152 EEIKADYLAFAASLGIEDITFIPISALEG 180
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
8-277 |
2.36e-12 |
|
translation initiation factor 2 subunit gamma; This model represents the archaeal translation initiation factor 2 subunit gamma and is found in all known archaea. eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.
Pssm-ID: 274720 [Multi-domain] Cd Length: 406 Bit Score: 68.93 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 8 NIAIIAHVDHGKTTLVDKLleqSGTLetrggneervMDSNDIEKERGITI-LAKNTAISWNDYH---------------- 70
Cdd:TIGR03680 6 NIGMVGHVDHGKTTLTKAL---TGVW----------TDTHSEELKRGISIrLGYADAEIYKCPEcdgpecyttepvcpnc 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 71 ---------INIVDTPGHADFggeVERVLSMA---DSVLLLVDAQEG-PMPQTRFVTQKAFAQGLKPIVVI-NKID---K 133
Cdd:TIGR03680 73 gsetellrrVSFVDAPGHETL---MATMLSGAalmDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVqNKIDlvsK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 134 PGARPDWvmDQIFDLFDnlGATDEqlDFKVIYASAINGwatldldepsDNMEPMFKMIVEEVSPPDADPEGDFQMQISQ- 212
Cdd:TIGR03680 150 EKALENY--EEIKEFVK--GTVAE--NAPIIPVSALHN----------ANIDALLEAIEKFIPTPERDLDKPPLMYVARs 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489050914 213 LDYNS--------YVGVVGiGRIKRGSVAPNQQVTIISADGTTRNGKIGAVQSY-----LGLERIETDRAYAGNIVTV 277
Cdd:TIGR03680 214 FDVNKpgtppeklKGGVIG-GSLIQGKLKVGDEIEIRPGIKVEKGGKTKWEPIYteitsLRAGGYKVEEARPGGLVGV 290
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
9-172 |
2.57e-10 |
|
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: 59.75 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 9 IAIIAHVDHGKTTLVDKLLeqsgtletrggNEERVMDSNdiekERGITILAKNTAISWNDYHINIVDTPG-----HADFG 83
Cdd:cd01895 5 IAIIGRPNVGKSSLLNALL-----------GEERVIVSD----IAGTTRDSIDVPFEYDGQKYTLIDTAGirkkgKVTEG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 84 GE------VERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINK---IDKPGARPDWVMDQIFDLFDnlga 154
Cdd:cd01895 70 IEkysvlrTLKAIERADVVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKwdlVEKDEKTMKEFEKELRRKLP---- 145
|
170
....*....|....*....
gi 489050914 155 tdeQLDF-KVIYASAINGW 172
Cdd:cd01895 146 ---FLDYaPIVFISALTGQ 161
|
|
| EngA1 |
cd01894 |
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
64-177 |
4.27e-10 |
|
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: 58.60 E-value: 4.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 64 ISWNDYHINIVDTPGHADFGGE--------VERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDkpG 135
Cdd:cd01894 40 AEWGGREFILIDTGGIEPDDEGiskeireqAEIAIEEADVILFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKID--N 117
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 489050914 136 ARPDWVMDQifdlFDNLGATDeqldfkVIYASAINGWATLDL 177
Cdd:cd01894 118 IKEEEEAAE----FYSLGFGE------PIPISAEHGRGIGDL 149
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
206-290 |
4.18e-09 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 53.42 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 206 FQMQISQLDYNSYVGVVGIGRIKRGSVAPNQQVTIIsadGTTRNGKIGAVQSylglERIETDRAYAGNIVTVT--GIGEL 283
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRIL---PKGITGRVTSIER----FHEEVDEAKAGDIVGIGilGVKDI 73
|
....*..
gi 489050914 284 KISDTVC 290
Cdd:cd01342 74 LTGDTLT 80
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
9-138 |
1.53e-08 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 57.50 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 9 IAIIAHVDHGKTTLVDKLleqsgtletRGgneervmdSNDIEKERG-IT--ILAknTAISWN-----------DYHINI- 73
Cdd:PRK04004 9 VVVLGHVDHGKTTLLDKI---------RG--------TAVAAKEAGgITqhIGA--TEVPIDviekiagplkkPLPIKLk 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 74 ------VDTPGHADF------GGevervlSMADSVLLLVDAQEGPMPQT--------RFVTqkafaqglkP-IVVINKID 132
Cdd:PRK04004 70 ipgllfIDTPGHEAFtnlrkrGG------ALADIAILVVDINEGFQPQTieainilkRRKT---------PfVVAANKID 134
|
....*..
gi 489050914 133 K-PGARP 138
Cdd:PRK04004 135 RiPGWKS 141
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
9-194 |
3.55e-08 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 53.45 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 9 IAIIAHVDHGKTTLVDKLLEQSGTLETRGGneervmdsndiekERGITILAKNTAISWNDYHINIVDTPGHADF---GGE 85
Cdd:COG1100 6 IVVVGTGGVGKTSLVNRLVGDIFSLEKYLS-------------TNGVTIDKKELKLDGLDVDLVIWDTPGQDEFretRQF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 86 VERVLSMADSVLLLVDAQegpMPQTRFVT----QKAFAQGLKP--IVVINKIDKpgaRPDWVMDQIFDLFDNLGatdEQL 159
Cdd:COG1100 73 YARQLTGASLYLFVVDGT---REETLQSLyellESLRRLGKKSpiILVLNKIDL---YDEEEIEDEERLKEALS---EDN 143
|
170 180 190
....*....|....*....|....*....|....*
gi 489050914 160 DFKVIYASAINGwatldldepsDNMEPMFKMIVEE 194
Cdd:COG1100 144 IVEVVATSAKTG----------EGVEELFAALAEI 168
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
220-290 |
3.98e-08 |
|
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.
Pssm-ID: 427163 [Multi-domain] Cd Length: 73 Bit Score: 50.34 E-value: 3.98e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489050914 220 GVVGIGRIKRGSVAPNQQVTIISAD--GTTRNGKIGAVQSYLGLERIETDRAYAGNIVTVTGIGELKISDTVC 290
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGtgKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
15-286 |
5.96e-08 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 55.30 E-value: 5.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 15 VDHGKTTLVDKLL--------EQSGTLE---TRGGNE-ERV-----MDSNDIEKERGITILAKNTAISWNDYHINIVDTP 77
Cdd:PRK05124 36 VDDGKSTLIGRLLhdtkqiyeDQLASLHndsKRHGTQgEKLdlallVDGLQAEREQGITIDVAYRYFSTEKRKFIIADTP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 78 GHADF------GGevervlSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVV-INKIDKPGARPDwVMDQIFDLFD 150
Cdd:PRK05124 116 GHEQYtrnmatGA------STCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVaVNKMDLVDYSEE-VFERIREDYL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 151 NLGAT-DEQLDFKVIYASAINGwatldlD---EPSDNME----PMFKMIVEEVSPPDADPEGDFQMQIS-----QLDYNS 217
Cdd:PRK05124 189 TFAEQlPGNLDIRFVPLSALEG------DnvvSQSESMPwysgPTLLEVLETVDIQRVVDAQPFRFPVQyvnrpNLDFRG 262
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489050914 218 YVGVVGIGRIKRGsvapnQQVTIISAdgttrnGKIGAVqsylglERIET-----DRAYAGNIVTVTGIGELKIS 286
Cdd:PRK05124 263 YAGTLASGVVKVG-----DRVKVLPS------GKESNV------ARIVTfdgdlEEAFAGEAITLVLEDEIDIS 319
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
8-132 |
6.10e-08 |
|
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: 53.04 E-value: 6.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 8 NIAIIAHVDHGKTTLVDKLleqSGTLETRGGNeervmdsndiEKERGITIlaK----NTAI-------SWNDY------- 69
Cdd:cd01888 2 NIGTIGHVAHGKTTLVKAL---SGVWTVRHKE----------ELKRNITI--KlgyaNAKIykcpncgCPRPYdtpecec 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 70 -----------HINIVDTPGHadfggEV--ERVLSMA---DSVLLLVDAQEG-PMPQTRfvtQKAFA---QGLKPIVVI- 128
Cdd:cd01888 67 pgcggetklvrHVSFVDCPGH-----EIlmATMLSGAavmDGALLLIAANEPcPQPQTS---EHLAAleiMGLKHIIILq 138
|
....
gi 489050914 129 NKID 132
Cdd:cd01888 139 NKID 142
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
64-211 |
8.30e-08 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 55.06 E-value: 8.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 64 ISWNDYHINIVDTPG----HADFGGEV----ERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDKPG 135
Cdd:PRK00093 44 AEWLGREFILIDTGGiepdDDGFEKQIreqaELAIEEADVILFVVDGRAGLTPADEEIAKILRKSNKPVILVVNKVDGPD 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489050914 136 ARpdwvmDQIFDlFDNLGATDeqldfkVIYASAINGwatldldepsDNMEPMFKMIVEEVSPPDADPEGDFQMQIS 211
Cdd:PRK00093 124 EE-----ADAYE-FYSLGLGE------PYPISAEHG----------RGIGDLLDAILEELPEEEEEDEEDEPIKIA 177
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
66-203 |
1.14e-07 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 54.26 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 66 WNDYHINIVDTPG-----HADFGGE----VERVLSMADSVLLLVDAQEGPMPqtrfvTQKAFAQGL----KP-IVVINKI 131
Cdd:COG1160 47 WGGREFTLIDTGGiepddDDGLEAEireqAELAIEEADVILFVVDGRAGLTP-----LDEEIAKLLrrsgKPvILVVNKV 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489050914 132 DKPGARPDwvmdqIFDLFdNLGATDeqldfkVIYASAINGWATLDLdepsdnMEPMFKMIVEEVSPPDADPE 203
Cdd:COG1160 122 DGPKREAD-----AAEFY-SLGLGE------PIPISAEHGRGVGDL------LDAVLELLPEEEEEEEEDDP 175
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
9-193 |
1.16e-07 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 54.29 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 9 IAIIAHVDHGKTTLVDKLLeqsgtletrggNEERVMDSNdiekERGITILAKNTAISWNDYHINIVDTPG-------HAD 81
Cdd:PRK00093 176 IAIIGRPNVGKSSLINALL-----------GEERVIVSD----IAGTTRDSIDTPFERDGQKYTLIDTAGirrkgkvTEG 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 82 fggeVE--------RVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDkpgARPDWVMDQIFDLFDN-L 152
Cdd:PRK00093 241 ----VEkysvirtlKAIERADVVLLVIDATEGITEQDLRIAGLALEAGRALVIVVNKWD---LVDEKTMEEFKKELRRrL 313
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489050914 153 GatdeQLDF-KVIYASAINGWatldldepsdNMEPMFKMIVE 193
Cdd:PRK00093 314 P----FLDYaPIVFISALTGQ----------GVDKLLEAIDE 341
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
54-130 |
1.41e-07 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 50.31 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 54 GITILAKNTAISWNDYHINIVDTPG-----HADFG-GEVERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVV 127
Cdd:pfam01926 31 GTTRDPNEGRLELKGKQIILVDTPGliegaSEGEGlGRAFLAIIEADLILFVVDSEEGITPLDEELLELLRENKKPIILV 110
|
...
gi 489050914 128 INK 130
Cdd:pfam01926 111 LNK 113
|
|
| EFG_mtEFG_C |
cd03713 |
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational ... |
399-475 |
1.63e-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: 1.63e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489050914 399 EPFETVTIDCQEEHQGSVMEQVGLRKGELTNMTPDGkGRMRLDFMIPSRGLIGFQTDFMTLTSGSGLMYHTFDHYGP 475
Cdd:cd03713 1 EPIMKVEVTVPEEYMGDVIGDLSSRRGQILGTESRG-GWKVIKAEVPLAEMFGYSTDLRSLTQGRGSFTMEFSHYEE 76
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
9-137 |
3.91e-07 |
|
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic orthologs of bacterial IF-2. Like IF-2, it helps convey the initiator tRNA to the ribosome, although the initiator is N-formyl-Met in bacteria and Met here. This protein is not closely related to the subunits of eIF-2 of eukaryotes, which is also involved in the initiation of translation. The aIF-2 of Methanococcus jannaschii contains a large intein interrupting a region of very strongly conserved sequence very near the amino end; the alignment generated by this model does not correctly align the sequences from Methanococcus jannaschii and Pyrococcus horikoshii in this region. [Protein synthesis, Translation factors]
Pssm-ID: 273104 [Multi-domain] Cd Length: 591 Bit Score: 52.90 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 9 IAIIAHVDHGKTTLVDKLLEQSGTLETRGGNEERVMDSndiekERGITILAKNTAISWNDYHINI-------VDTPGHAD 81
Cdd:TIGR00491 7 VVVLGHVDHGKTTLLDKIRGTAVVKKEAGGITQHIGAS-----EVPTDVIEKICGDLLKSFKIKLkipgllfIDTPGHEA 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 489050914 82 FGGEVERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDK-PGAR 137
Cdd:TIGR00491 82 FTNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTPFVVAANKIDRiPGWK 138
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
8-210 |
6.48e-07 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 52.16 E-value: 6.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 8 NIAIIAHVDHGKTTLVDKLleqSGTLETRGGNEERvmdsndiekeRGITI--------LAKNTAISWNDYH--------- 70
Cdd:PRK04000 11 NIGMVGHVDHGKTTLVQAL---TGVWTDRHSEELK----------RGITIrlgyadatIRKCPDCEEPEAYttepkcpnc 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 71 ---------INIVDTPGHadfggEV--ERVLSMA---DSVLLLVDAQEG-PMPQTR--FVTQKAFaqGLKPIVVI-NKID 132
Cdd:PRK04000 78 gsetellrrVSFVDAPGH-----ETlmATMLSGAalmDGAILVIAANEPcPQPQTKehLMALDII--GIKNIVIVqNKID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 133 ---KPGARPDWvmDQIFDLFDnlGATDEqlDFKVIYASAINGwatldldepsDNMEPMFKMIVEEVSPPDADPEGDFQMQ 209
Cdd:PRK04000 151 lvsKERALENY--EQIKEFVK--GTVAE--NAPIIPVSALHK----------VNIDALIEAIEEEIPTPERDLDKPPRMY 214
|
.
gi 489050914 210 I 210
Cdd:PRK04000 215 V 215
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
18-172 |
1.01e-06 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 48.78 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 18 GKTTLVDKLLEQ--------SGTleTRGGNEERVmdsndiekergiTILAKNTaiswndyhINIVDTPGHADFGG----- 84
Cdd:cd00880 9 GKSSLLNALLGQnvgivspiPGT--TRDPVRKEW------------ELLPLGP--------VVLIDTPGLDEEGGlgrer 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 85 --EVERVLSMADSVLLLVDAQEGPMPQTRFVtQKAFAQGLKPIVVINKIDKPGARPDwvmDQIFDLFDNLgatdEQLDFK 162
Cdd:cd00880 67 veEARQVADRADLVLLVVDSDLTPVEEEAKL-GLLRERGKPVLLVLNKIDLVPESEE---EELLRERKLE----LLPDLP 138
|
170
....*....|
gi 489050914 163 VIYASAINGW 172
Cdd:cd00880 139 VIAVSALPGE 148
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
68-171 |
1.60e-06 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 49.99 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 68 DYHINIVDTPG-----HAdFG----GEVERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDKpgARP 138
Cdd:COG1159 50 DAQIVFVDTPGihkpkRK-LGrrmnKAAWSALEDVDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDL--VKK 126
|
90 100 110
....*....|....*....|....*....|....
gi 489050914 139 DwvmdqifDLFDNLGATDEQLDFK-VIYASAING 171
Cdd:COG1159 127 E-------ELLPLLAEYSELLDFAeIVPISALKG 153
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
68-171 |
1.98e-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: 48.23 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 68 DYHINIVDTPG-HADFGG-------EVERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDKpgarpd 139
Cdd:cd04163 50 DAQIIFVDTPGiHKPKKKlgermvkAAWSALKDVDLVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDL------ 123
|
90 100 110
....*....|....*....|....*....|...
gi 489050914 140 wVMDQIfDLFDNLGATDEQLDFK-VIYASAING 171
Cdd:cd04163 124 -VKDKE-DLLPLLEKLKELHPFAeIFPISALKG 154
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
67-171 |
7.19e-06 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 48.12 E-value: 7.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 67 NDYHINIVDTPG----HADFG----GEVERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDKPGARp 138
Cdd:PRK00089 51 DDAQIIFVDTPGihkpKRALNramnKAAWSSLKDVDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLVKDK- 129
|
90 100 110
....*....|....*....|....*....|....
gi 489050914 139 dwvmDQIFDLFDNLgatDEQLDFK-VIYASAING 171
Cdd:PRK00089 130 ----EELLPLLEEL---SELMDFAeIVPISALKG 156
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
8-168 |
3.62e-05 |
|
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.
Pssm-ID: 206739 [Multi-domain] Cd Length: 180 Bit Score: 44.84 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 8 NIAIIAHVDHGKTTLVDKLLeqsgtletrggnEERVMDSndiekerGITIL-AKNTAISWN-DYHINIVDTPG------- 78
Cdd:cd09912 2 LLAVVGEFSAGKSTLLNALL------------GEEVLPT-------GVTPTtAVITVLRYGlLKGVVLVDTPGlnstieh 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 79 HADfggEVERVLSMADSVLLLVDAQEgpmPQTR----FVTQKAFAQGLKPIVVINKIDKpgARPDWVMDQIFDLFDNLGA 154
Cdd:cd09912 63 HTE---ITESFLPRADAVIFVLSADQ---PLTEsereFLKEILKWSGKKIFFVLNKIDL--LSEEELEEVLEYSREELGV 134
|
170
....*....|....*
gi 489050914 155 TDEQLDFKVIYA-SA 168
Cdd:cd09912 135 LELGGGEPRIFPvSA 149
|
|
| PRK09518 |
PRK09518 |
bifunctional cytidylate kinase/GTPase Der; Reviewed |
4-134 |
7.18e-05 |
|
bifunctional cytidylate kinase/GTPase Der; Reviewed
Pssm-ID: 236546 [Multi-domain] Cd Length: 712 Bit Score: 45.94 E-value: 7.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 4 EQLRNIAIIAHVDHGKTTLVDKLLeqsgtletrGGNEERVMDSNDIEKERgITILAKntaisWNDYHINIVDTPG----- 78
Cdd:PRK09518 273 KAVGVVAIVGRPNVGKSTLVNRIL---------GRREAVVEDTPGVTRDR-VSYDAE-----WAGTDFKLVDTGGweadv 337
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 489050914 79 ---HADFGGEVERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDKP 134
Cdd:PRK09518 338 egiDSAIASQAQIAVSLADAVVFVVDGQVGLTSTDERIVRMLRRAGKPVVLAVNKIDDQ 396
|
|
| EFG_mtEFG_II |
cd04088 |
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation ... |
218-290 |
1.04e-04 |
|
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: 40.97 E-value: 1.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489050914 218 YVGVVGIGRIKRGSVAPNQQVTIISADGTTRNGKIGAVQsylGLERIETDRAYAGNIVTVTGIGELKISDTVC 290
Cdd:cd04088 13 FVGKLTFFRVYSGTLKSGSTVYNSTKGKKERVGRLLRMH---GKKREEVEELGAGDIGAVVGLKDTRTGDTLC 82
|
|
| Tet_II |
cd03690 |
Domain II of ribosomal protection proteins Tet(M) and Tet(O); This subfamily represents domain ... |
226-289 |
1.56e-04 |
|
Domain II of ribosomal protection proteins Tet(M) and Tet(O); This subfamily represents domain II of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology to domain II of the elongation factors EF-G and EF-2. Tet(M) and Tet(O) catalyze the release of tetracycline (Tc) from the ribosome in a GTP-dependent manner thereby mediating Tc resistance. Tcs are broad-spectrum antibiotics. Typical Tcs bind to the ribosome and inhibit the elongation phase of protein synthesis, by inhibiting the occupation of site A by aminoacyl-tRNA.
Pssm-ID: 293891 [Multi-domain] Cd Length: 86 Bit Score: 40.68 E-value: 1.56e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489050914 226 RIKRGSVAPNQQVTIIsadGTTRNGKIGAVQSYLGLERIETDRAYAGNIVTVTGIGELKISDTV 289
Cdd:cd03690 24 RLYSGTLRLRDSVRVS---GEEEKIKITELRTFENGELVKVDRVYAGDIAILVGLKSLRVGDVL 84
|
|
| lepA_C |
cd03709 |
lepA_C: This family represents the C-terminal region of LepA, a GTP-binding protein localized ... |
399-471 |
1.60e-04 |
|
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: 40.55 E-value: 1.60e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489050914 399 EPFETVTIDCQEEHQGSVMEQVGLRKGELTNMTPDGKGRMRLDFMIPSRGLIgfqTDFM----TLTSGsglmYHTFD 471
Cdd:cd03709 1 EPFVKATIITPSEYLGAIMELCQERRGVQKDMEYLDANRVMLTYELPLAEIV---YDFFdklkSISKG----YASLD 70
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
18-172 |
1.69e-04 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 44.24 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 18 GKTTLVDKLLeqsgtletrggNEERVMDSNdiekERGITILAKNTAISWNDYHINIVDTPG-------HADfggeVE--- 87
Cdd:COG1160 187 GKSSLINALL-----------GEERVIVSD----IAGTTRDSIDTPFERDGKKYTLIDTAGirrkgkvDEG----IEkys 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 88 -----RVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINK---IDKPGARPDWVMDQIFDLFDnlgatdeQL 159
Cdd:COG1160 248 vlrtlRAIERADVVLLVIDATEGITEQDLKIAGLALEAGKALVIVVNKwdlVEKDRKTREELEKEIRRRLP-------FL 320
|
170
....*....|....
gi 489050914 160 DF-KVIYASAINGW 172
Cdd:COG1160 321 DYaPIVFISALTGQ 334
|
|
| mtEFG1_C |
cd04097 |
mtEFG1_C: C-terminus of mitochondrial Elongation factor G1 (mtEFG1)-like proteins found in ... |
399-475 |
1.76e-04 |
|
mtEFG1_C: C-terminus of mitochondrial Elongation factor G1 (mtEFG1)-like proteins found in eukaryotes. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. Eukaryotic EF-2 operates in the cytosolic protein synthesis machinery of eukaryotes, EF-Gs in protein synthesis in bacteria. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. There are two forms of mtEFG present in mammals (designated mtEFG1s and mtEFG2s) mtEFG2s are not present in this group.
Pssm-ID: 239764 [Multi-domain] Cd Length: 78 Bit Score: 40.38 E-value: 1.76e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489050914 399 EPFETVTIDCQEEHQGSVMEQVGLRKGELTNMTPDGkGRMRLDFMIPSRGLIGFQTDFMTLTSGSGLMYHTFDHYGP 475
Cdd:cd04097 1 EPIMKVEVTAPTEFQGNVIGLLNKRKGTIVDTDTGE-DEFTLEAEVPLNDMFGYSTELRSMTQGKGEFSMEFSRYAP 76
|
|
| EFG_C |
smart00838 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
399-475 |
4.31e-04 |
|
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of Elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopt a ferredoxin-like fold.
Pssm-ID: 197906 [Multi-domain] Cd Length: 85 Bit Score: 39.41 E-value: 4.31e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489050914 399 EPFETVTIDCQEEHQGSVMEQVGLRKGELTNMTPDGkGRMRLDFMIPSRGLIGFQTDFMTLTSGSGLMYHTFDHYGP 475
Cdd:smart00838 3 EPIMKVEVTVPEEYMGDVIGDLNSRRGKIEGMEQRG-GAQVIKAKVPLSEMFGYATDLRSATQGRATWSMEFSHYEE 78
|
|
| MnmE |
COG0486 |
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
64-206 |
5.54e-04 |
|
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440253 [Multi-domain] Cd Length: 448 Bit Score: 42.74 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 64 ISWNDYHINIVDTPGHADFGGEVER--------VLSMADSVLLLVDAQEGPMPQTRFVTQKAfaQGLKPIVVINKIDKPG 135
Cdd:COG0486 256 INIGGIPVRLIDTAGLRETEDEVEKigierareAIEEADLVLLLLDASEPLTEEDEEILEKL--KDKPVIVVLNKIDLPS 333
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489050914 136 ARPDWVmdqifdlfdnlgatDEQLDFKVIYASAINGwatldldepsDNMEPMFKMIVEEVSPPDADPEGDF 206
Cdd:COG0486 334 EADGEL--------------KSLPGEPVIAISAKTG----------EGIDELKEAILELVGEGALEGEGVL 380
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
8-132 |
6.63e-04 |
|
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal structure and biogenesis]; Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444075 [Multi-domain] Cd Length: 408 Bit Score: 42.52 E-value: 6.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 8 NIAIIAHVDHGKTTLVDKLleqSGTLETRGGNEERvmdsndiekeRGITI------------------LAKNTAISWNDY 69
Cdd:COG5257 7 NIGVVGHVDHGKTTLVQAL---TGVWTDRHSEELK----------RGITIrlgyadatfykcpnceppEAYTTEPKCPNC 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 70 --------HINIVDTPGHadfggEV--ERVLSMA---DSVLLLVDAQEG-PMPQTR--FVTQKAFaqGLKPIVVI-NKID 132
Cdd:COG5257 74 gsetellrRVSFVDAPGH-----ETlmATMLSGAalmDGAILVIAANEPcPQPQTKehLMALDII--GIKNIVIVqNKID 146
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
73-144 |
1.99e-03 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 41.41 E-value: 1.99e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489050914 73 IVDTPGHADFGGEVERVLSMADSVLLLVDAQEGPMPQTrFVTQKAFAQGLKPIVVI-NKIDKPgarPDWVMDQ 144
Cdd:PRK14845 530 FIDTPGHEAFTSLRKRGGSLADLAVLVVDINEGFKPQT-IEAINILRQYKTPFVVAaNKIDLI---PGWNISE 598
|
|
| YihA_EngB |
cd01876 |
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
65-171 |
3.24e-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: 38.65 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 65 SWNDyHINIVDTPG----------HADFGGEVERVLSMADS---VLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKI 131
Cdd:cd01876 42 NVGD-KFRLVDLPGygyakvskevREKWGKLIEEYLENRENlkgVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKA 120
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 489050914 132 DK--PGARpDWVMDQIFDLFDNLGATDEqldfkVIYASAING 171
Cdd:cd01876 121 DKlkKSEL-AKVLKKIKEELNLFNILPP-----VILFSSKKG 156
|
|
| EF2_II |
cd16268 |
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 ... |
220-282 |
3.28e-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: 37.20 E-value: 3.28e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489050914 220 GVVGIGRIKRGSVAPNQQVTIIS---ADGTTRNGKIGAVQS---YLGLERIETDRAYAGNIVTVTGIGE 282
Cdd:cd16268 17 GFVAFGRVFSGTVRRGQEVYILGpkyVPGKKDDLKKKRIQQtylMMGREREPVDEVPAGNIVGLVGLDD 85
|
|
| MJ1464 |
cd01859 |
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ... |
86-168 |
3.88e-03 |
|
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents archaeal GTPase typified by the protein MJ1464 from Methanococcus jannaschii. The members of this family show a circular permutation of the GTPase signature motifs so that C-terminal strands 5, 6, and 7 (strands 6 contain the NKxD motif) are relocated to the N terminus.
Pssm-ID: 206752 [Multi-domain] Cd Length: 157 Bit Score: 38.45 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 86 VERVLSMADSVLLLVDAQEGPMPQTRFVTQKAFAQGLKPIVVINKIDkpgARPDWVMDQIFDLFdnlgatdEQLDFKVIY 165
Cdd:cd01859 5 VRRIIKEADVVLEVVDARDPELTRSRKLERMALELGKKLIIVLNKAD---LVPREVLEKWKEVF-------ESEGLPVVY 74
|
...
gi 489050914 166 ASA 168
Cdd:cd01859 75 VSA 77
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
111-179 |
4.20e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 38.68 E-value: 4.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489050914 111 RFVTQkAFAQGLKPIVVINKIDKpgarpdwVMDQifDLFDNLGATDEQLDFKVIYASAINGWATLDLDE 179
Cdd:pfam03193 44 RFLVL-AEASGIEPVIVLNKIDL-------LDEE--EELEELLKIYRAIGYPVLFVSAKTGEGIEALKE 102
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| trmE |
PRK05291 |
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; |
64-136 |
6.89e-03 |
|
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
Pssm-ID: 235392 [Multi-domain] Cd Length: 449 Bit Score: 39.32 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050914 64 ISWNDYHINIVDTPGHADFGGEVER--------VLSMADSVLLLVDAQEGPMPQTRFVTQKAfaQGLKPIVVINKIDKPG 135
Cdd:PRK05291 258 INLDGIPLRLIDTAGIRETDDEVEKigiersreAIEEADLVLLVLDASEPLTEEDDEILEEL--KDKPVIVVLNKADLTG 335
|
.
gi 489050914 136 A 136
Cdd:PRK05291 336 E 336
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| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
111-171 |
9.77e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 37.76 E-value: 9.77e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489050914 111 RFVTQkAFAQGLKPIVVINKIDKPgarPDWVMDQIFDLFdnlgatdEQLDFKVIYASAING 171
Cdd:cd01854 24 RYLVA-AEASGIEPVIVLNKADLV---DDEELEELLEIY-------EKLGYPVLAVSAKTG 73
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