|
Name |
Accession |
Description |
Interval |
E-value |
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
85-695 |
0e+00 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 1171.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 85 PPSQIRNFSIIAHIDHGKSTLADTLLSKTKTVAARDMEAQLLDSMDIERERGITIKLNSARMNYVANDGETYVLNLIDTP 164
Cdd:COG0481 2 DQKNIRNFSIIAHIDHGKSTLADRLLELTGTLSEREMKEQVLDSMDLERERGITIKAQAVRLNYKAKDGETYQLNLIDTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 165 GHVDFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDLEIITVLNKIDLPGAEPERVKvrsihwfpydrvgvR 244
Cdd:COG0481 82 GHVDFSYEVSRSLAACEGALLVVDASQGVEAQTLANVYLALENDLEIIPVINKIDLPSADPERVK--------------Q 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 245 EIEDVLGLDTEDAVVASAKANIGMEDILENIVKMIPPPPDTGDEPLRALIFDSYFDPYRGVVVIFRVVDGNLGVGDAVKF 324
Cdd:COG0481 148 EIEDIIGIDASDAILVSAKTGIGIEEILEAIVERIPPPKGDPDAPLQALIFDSWYDSYRGVVVYVRVFDGTLKKGDKIKM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 325 MNTGKSYTIDEIGIMRPQKVPVNRLSAGEVGYMIANIKSVADARVGDTITTTKDSSTEPLPGYSEATPMVYCGLFPTDSD 404
Cdd:COG0481 228 MSTGKEYEVDEVGVFTPKMTPVDELSAGEVGYIIAGIKDVRDARVGDTITLAKNPAAEPLPGFKEVKPMVFAGLYPVDSD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 405 QYEDLRVALGKLQINDAALRYEPEQSSAMGFGFRCGFLGLLHMEIVQERLEREYDLGLITTAPSVVYKVYTSDGACVDIA 484
Cdd:COG0481 308 DYEDLRDALEKLQLNDASLTYEPETSAALGFGFRCGFLGLLHMEIIQERLEREFDLDLITTAPSVVYEVTLTDGEVIEVD 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 485 NPADLPDASVRDRIEEPFVKLEMFAPSDYVGSLMELAQQRRGEFIDMTYLSESRTCLKYDIPLGEVVTDFFDELKSRSKG 564
Cdd:COG0481 388 NPSDLPDPGKIEEIEEPIVKATIITPSEYVGAVMELCQEKRGVQKNMEYLGENRVELTYELPLAEIVFDFFDRLKSITRG 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 565 YASMEYSFNEYRKSDLVRLDVLINYEPADPLACICHRDKSYVMGRGLVDKLKELIPRQMFRIPIQASIGTKVIASTSISA 644
Cdd:COG0481 468 YASLDYEFIGYRESDLVKLDILINGEPVDALSFIVHRDKAYSRGRALVEKLKELIPRQQFEVPIQAAIGGKIIARETIKA 547
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 317411685 645 MRKDVLAKCYGGDISRKKKLLKKQAAGKKRMKQFGKVEVPQEAFMAVLKVD 695
Cdd:COG0481 548 LRKDVLAKCYGGDISRKRKLLEKQKEGKKRMKQVGNVEIPQEAFLAVLKVD 598
|
|
| lepA |
TIGR01393 |
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a ... |
87-695 |
0e+00 |
|
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: 1025.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 87 SQIRNFSIIAHIDHGKSTLADTLLSKTKTVAARDMEAQLLDSMDIERERGITIKLNSARMNYVANDGETYVLNLIDTPGH 166
Cdd:TIGR01393 1 KNIRNFSIIAHIDHGKSTLADRLLEYTGAISEREMREQVLDSMDLERERGITIKAQAVRLNYKAKDGETYVLNLIDTPGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 167 VDFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDLEIITVLNKIDLPGAEPERVKvrsihwfpydrvgvREI 246
Cdd:TIGR01393 81 VDFSYEVSRSLAACEGALLLVDAAQGIEAQTLANVYLALENDLEIIPVINKIDLPSADPERVK--------------KEI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 247 EDVLGLDTEDAVVASAKANIGMEDILENIVKMIPPPPDTGDEPLRALIFDSYFDPYRGVVVIFRVVDGNLGVGDAVKFMN 326
Cdd:TIGR01393 147 EEVIGLDASEAILASAKTGIGIEEILEAIVKRVPPPKGDPDAPLKALIFDSHYDNYRGVVALVRVFEGTIKPGDKIRFMS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 327 TGKSYTIDEIGIMRPQKVPVNRLSAGEVGYMIANIKSVADARVGDTITTTKDSSTEPLPGYSEATPMVYCGLFPTDSDQY 406
Cdd:TIGR01393 227 TGKEYEVDEVGVFTPKLTKTDELSAGEVGYIIAGIKDVSDVRVGDTITHVKNPAKEPLPGFKEVKPMVFAGLYPIDTEDY 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 407 EDLRVALGKLQINDAALRYEPEQSSAMGFGFRCGFLGLLHMEIVQERLEREYDLGLITTAPSVVYKVYTSDGACVDIANP 486
Cdd:TIGR01393 307 EDLRDALEKLKLNDASLTYEPESSPALGFGFRCGFLGLLHMEIIQERLEREFNLDLITTAPSVIYRVYLTNGEVIEVDNP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 487 ADLPDASVRDRIEEPFVKLEMFAPSDYVGSLMELAQQRRGEFIDMTYLSESRTCLKYDIPLGEVVTDFFDELKSRSKGYA 566
Cdd:TIGR01393 387 SDLPDPGKIEHVEEPYVKATIITPTEYLGPIMTLCQEKRGVQTNMEYLDPNRVELIYEMPLAEIVYDFFDKLKSISRGYA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 567 SMEYSFNEYRKSDLVRLDVLINYEPADPLACICHRDKSYVMGRGLVDKLKELIPRQMFRIPIQASIGTKVIASTSISAMR 646
Cdd:TIGR01393 467 SFDYELIGYRPSDLVKLDILINGEPVDALSFIVHRDKAYSRGREICEKLKELIPRQQFEIPIQAAIGGKIIARETIKALR 546
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 317411685 647 KDVLAKCYGGDISRKKKLLKKQAAGKKRMKQFGKVEVPQEAFMAVLKVD 695
Cdd:TIGR01393 547 KDVTAKCYGGDITRKRKLLEKQKEGKKRMKQIGKVEVPQEAFLAVLKVD 595
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
90-282 |
2.63e-120 |
|
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: 356.84 E-value: 2.63e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 90 RNFSIIAHIDHGKSTLADTLLSKTKTVAARDMEAQLLDSMDIERERGITIKLNSARMNYVANDGETYVLNLIDTPGHVDF 169
Cdd:cd01890 1 RNFSIIAHIDHGKSTLADRLLELTGTVSEREMKEQVLDSMDLERERGITIKAQAVRLFYKAKDGEEYLLNLIDTPGHVDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 170 SYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDLEIITVLNKIDLPGAEPERVKvrsihwfpydrvgvREIEDV 249
Cdd:cd01890 81 SYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVK--------------QEIEDV 146
|
170 180 190
....*....|....*....|....*....|...
gi 317411685 250 LGLDTEDAVVASAKANIGMEDILENIVKMIPPP 282
Cdd:cd01890 147 LGLDASEAILVSAKTGLGVEDLLEAIVERIPPP 179
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
88-281 |
4.60e-64 |
|
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: 210.46 E-value: 4.60e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 88 QIRNFSIIAHIDHGKSTLADTLLSKTKTVAARDMEAQ----LLDSMDIERERGITIKLNSARMnyvanDGETYVLNLIDT 163
Cdd:pfam00009 2 RHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGegeaGLDNLPEERERGITIKSAAVSF-----ETKDYLINLIDT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 164 PGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDLEIITVLNKIDLP-GAEPERVkvrsihwfpydrvg 242
Cdd:pfam00009 77 PGHVDFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVdGAELEEV-------------- 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 317411685 243 VREIEDVL------GLDTEDAVVASAKANIGMEDILENIVKMIPP 281
Cdd:pfam00009 143 VEEVSRELlekygeDGEFVPVVPGSALKGEGVQTLLDALDEYLPS 187
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
87-576 |
9.32e-64 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 222.59 E-value: 9.32e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 87 SQIRNFSIIAHIDHGKSTLADTLLSKTKTVAAR-DMEAQLLDSMDIERERGITI--KlNSArMNYvaNDgetYVLNLIDT 163
Cdd:COG1217 4 EDIRNIAIIAHVDHGKTTLVDALLKQSGTFRENqEVAERVMDSNDLERERGITIlaK-NTA-VRY--KG---VKINIVDT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 164 PGHVDFSYEVSRSLAACEGALLVVDASQGVEAQT--VanvyL--ALENDLEIITVLNKIDLPGAEPERVkvrsihwfpyd 239
Cdd:COG1217 77 PGHADFGGEVERVLSMVDGVLLLVDAFEGPMPQTrfV----LkkALELGLKPIVVINKIDRPDARPDEV----------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 240 rvgVREIEDV-LGLDTEDA------VVASAKANI----------GMEDILENIVKMIPPPPDTGDEPLRALIFDSYFDPY 302
Cdd:COG1217 142 ---VDEVFDLfIELGATDEqldfpvVYASARNGWasldlddpgeDLTPLFDTILEHVPAPEVDPDGPLQMLVTNLDYSDY 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 303 RGVVVIFRVVDGNLGVGDAVKFMNTG---KSYTIDEI-GIMRPQKVPVNRLSAGEvgymIANIKSVADARVGDTITTTKD 378
Cdd:COG1217 219 VGRIAIGRIFRGTIKKGQQVALIKRDgkvEKGKITKLfGFEGLERVEVEEAEAGD----IVAIAGIEDINIGDTICDPEN 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 379 ssTEPLPGYS--EAT-PMVYC----------GLFPTdSDQyedLRVALGKLQINDAALRYEPEQSSAmgfgfrcGFL--- 442
Cdd:COG1217 295 --PEALPPIKidEPTlSMTFSvndspfagreGKFVT-SRQ---IRERLEKELETNVALRVEETDSPD-------AFKvsg 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 443 -GLLHMEIVQERLERE-YDLGLitTAPSVVYKvyTSDGacvdianpadlpdasvrdRIEEPFVKLEMFAPSDYVGSLMEL 520
Cdd:COG1217 362 rGELHLSILIETMRREgYELQV--SRPEVIFK--EIDG------------------KKLEPIEELTIDVPEEYSGAVIEK 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 317411685 521 AQQRRGEFIDMTYLSESRTCLKYDIP----LG---EVVTDffdelksrSKGYASMEYSFNEYR 576
Cdd:COG1217 420 LGQRKGEMTNMEPDGGGRVRLEFLIPsrglIGfrtEFLTD--------TRGTGIMNHVFDGYE 474
|
|
| LepA_C |
pfam06421 |
GTP-binding protein LepA C-terminus; This family consists of the C-terminal region of several ... |
587-693 |
3.54e-59 |
|
GTP-binding protein LepA C-terminus; This family consists of the C-terminal region of several pro- and eukaryotic GTP-binding LepA proteins.
Pssm-ID: 461905 [Multi-domain] Cd Length: 107 Bit Score: 194.55 E-value: 3.54e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 587 INYEPADPLACICHRDKSYVMGRGLVDKLKELIPRQMFRIPIQASIGTKVIASTSISAMRKDVLAKCYGGDISRKKKLLK 666
Cdd:pfam06421 1 INGEPVDALSFIVHRSKAYRRGRALVEKLKELIPRQQFEVPIQAAIGGKIIARETIKALRKDVTAKCYGGDISRKKKLLE 80
|
90 100
....*....|....*....|....*..
gi 317411685 667 KQAAGKKRMKQFGKVEVPQEAFMAVLK 693
Cdd:pfam06421 81 KQKEGKKRMKQIGNVEIPQEAFLAVLK 107
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
86-472 |
6.62e-49 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 183.53 E-value: 6.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 86 PSQIRNFSIIAHIDHGKSTLADTLLsktktvAARDM-------EAQLLDSMDIERERGITIKLNSARMnYVANDGETYVL 158
Cdd:PRK07560 17 PEQIRNIGIIAHIDHGKTTLSDNLL------AGAGMiseelagEQLALDFDEEEQARGITIKAANVSM-VHEYEGKEYLI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 159 NLIDTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDLEIITVLNKIDLPGAE----PERVKVRSih 234
Cdd:PRK07560 90 NLIDTPGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKPVLFINKVDRLIKElkltPQEMQQRL-- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 235 wfpydrvgVREIEDVLGL---------------DTEDAVVA--SAKAN------------IGMEDI-------------- 271
Cdd:PRK07560 168 --------LKIIKDVNKLikgmapeefkekwkvDVEDGTVAfgSALYNwaisvpmmqktgIKFKDIidyyekgkqkelae 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 272 --------LENIVKMIPPPPDT----------GD---------------EPLRALIFDSYFDPYRGVVVIFRVVDGNLGV 318
Cdd:PRK07560 240 kaplhevvLDMVVKHLPNPIEAqkyripkiwkGDlnsevgkamlncdpnGPLVMMVTDIIVDPHAGEVATGRVFSGTLRK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 319 GDAVKFMNTGKSYTIDEIGI-MRPQKVPVNRLSAGEvgymIANIKSVADARVGDTITTTKDSST-EPLPGYSEatPMVYC 396
Cdd:PRK07560 320 GQEVYLVGAKKKNRVQQVGIyMGPEREEVEEIPAGN----IAAVTGLKDARAGETVVSVEDMTPfESLKHISE--PVVTV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 397 GLFPTDSDQYEDLRVALGKLQINDAALRYEPEQS------SAMGFgfrcgflglLHMEIVQERLEREYDLGLITTAPSVV 470
Cdd:PRK07560 394 AIEAKNPKDLPKLIEVLRQLAKEDPTLVVKINEEtgehllSGMGE---------LHLEVITYRIKRDYGIEVVTSEPIVV 464
|
..
gi 317411685 471 YK 472
Cdd:PRK07560 465 YR 466
|
|
| EF4_III |
cd16260 |
Domain III of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly ... |
392-467 |
1.38e-47 |
|
Domain III of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly conserved guanosine triphosphatase found in bacteria and eukaryotic mitochondria and chloroplasts. EF4 functions as a translation factor, which promotes back-translocation of tRNAs on posttranslocational ribosome complexes and competes with elongation factor G for interaction with pretranslocational ribosomes, inhibiting the elongation phase of protein synthesis.
Pssm-ID: 293917 [Multi-domain] Cd Length: 76 Bit Score: 161.90 E-value: 1.38e-47
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 317411685 392 PMVYCGLFPTDSDQYEDLRVALGKLQINDAALRYEPEQSSAMGFGFRCGFLGLLHMEIVQERLEREYDLGLITTAP 467
Cdd:cd16260 1 PMVFAGLYPVDGSDYEELRDALEKLTLNDASVTFEPETSSALGFGFRCGFLGLLHMEVFQERLEREYGLDLIITAP 76
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
91-282 |
6.28e-47 |
|
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: 164.39 E-value: 6.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 91 NFSIIAHIDHGKSTLADTLLSKTKTVAARDMEAQ-LLDSMDIERERGITIKlnSARMNYVANDgetYVLNLIDTPGHVDF 169
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKEtFLDTLKEERERGITIK--TGVVEFEWPK---RRINFIDTPGHEDF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 170 SYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDLEIITVLNKIDLPGaePERvkvrsihwfpYDRVgVREIEDV 249
Cdd:cd00881 76 SKETVRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVG--EED----------FDEV-LREIKEL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 317411685 250 LGL--------DTEDAVVASAKANIGMEDILENIVKMIPPP 282
Cdd:cd00881 143 LKLigftflkgKDVPIIPISALTGEGIEELLDAIVEHLPPP 183
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
89-282 |
7.61e-46 |
|
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: 161.61 E-value: 7.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 89 IRNFSIIAHIDHGKSTLADTLLSKTKT-VAARDMEAQLLDSMDIERERGITIKLNSARMNYvaNDgetYVLNLIDTPGHV 167
Cdd:cd01891 2 IRNIAIIAHVDHGKTTLVDALLKQSGTfRENEEVGERVMDSNDLERERGITILAKNTAITY--KD---TKINIIDTPGHA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 168 DFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDLEIITVLNKIDLPGAEPERVkvrsihwfpydrvgVREIE 247
Cdd:cd01891 77 DFGGEVERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDRPDARPEEV--------------VDEVF 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 317411685 248 DV-LGLDTED------AVVASAKANIG----------MEDILENIVKMIPPP 282
Cdd:cd01891 143 DLfLELNATDeqldfpIVYASAKNGWAslnlddpsedLDPLFETIIEHVPAP 194
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
83-472 |
1.69e-45 |
|
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: 172.92 E-value: 1.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 83 QVPPSQIRNFSIIAHIDHGKSTLADTLLSKTKTVAAR----DMEAQLlDSMDIERERGITIklNSARMNYVANDgetYVL 158
Cdd:COG0480 3 EYPLEKIRNIGIVAHIDAGKTTLTERILFYTGAIHRIgevhDGNTVM-DWMPEEQERGITI--TSAATTCEWKG---HKI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 159 NLIDTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDLEIITVLNKIDLPGAEPERV---------- 228
Cdd:COG0480 77 NIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVleqlkerlga 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 229 ----------------------KVRSIHWFPYDRVGVRE------------------IEDVLGLD-------------TE 255
Cdd:COG0480 157 npvplqlpigaeddfkgvidlvTMKAYVYDDELGAKYEEeeipaelkeeaeeareelIEAVAETDdelmekylegeelTE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 256 DAVVA-----------------SAKANIGMEDILENIVKMIPPP----------PDTG---------DEPLRALIFDSYF 299
Cdd:COG0480 237 EEIKAglrkatlagkivpvlcgSAFKNKGVQPLLDAVVDYLPSPldvpaikgvdPDTGeeverkpddDEPFSALVFKTMT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 300 DPYRGVVVIFRVVDGNLGVGDAVKFMNTGKSYTIDEIGIMR-PQKVPVNRLSAGEVGyMIANIKsvaDARVGDTITTTKD 378
Cdd:COG0480 317 DPFVGKLSFFRVYSGTLKSGSTVYNSTKGKKERIGRLLRMHgNKREEVDEAGAGDIV-AVVKLK---DTTTGDTLCDEDH 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 379 SSTepLPGYSEATPMVYCGLFP-TDSDQyEDLRVALGKLQINDAALRYE--PE--QS--SAMgfgfrcgflGLLHMEIVQ 451
Cdd:COG0480 393 PIV--LEPIEFPEPVISVAIEPkTKADE-DKLSTALAKLAEEDPTFRVEtdEEtgQTiiSGM---------GELHLEIIV 460
|
490 500
....*....|....*....|.
gi 317411685 452 ERLEREYDLGLITTAPSVVYK 472
Cdd:COG0480 461 DRLKREFGVEVNVGKPQVAYR 481
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
90-219 |
2.57e-45 |
|
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.
Pssm-ID: 206672 [Multi-domain] Cd Length: 218 Bit Score: 161.25 E-value: 2.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 90 RNFSIIAHIDHGKSTLADTLLSKTKtVAARDM--EAQLLDSMDIERERGITIKLNSARMNYV----ANDGETYVLNLIDT 163
Cdd:cd01885 1 RNICIIAHVDHGKTTLSDSLLASAG-IISEKLagKARYLDTREDEQERGITIKSSAISLYFEyeeeKMDGNDYLINLIDS 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 317411685 164 PGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDLEIITVLNKID 219
Cdd:cd01885 80 PGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKID 135
|
|
| EF4_II |
cd03699 |
Domain II of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly ... |
290-375 |
3.80e-45 |
|
Domain II of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly conserved guanosine triphosphatase found in bacteria and eukaryotic mitochondria and chloroplasts. EF4 functions as a translation factor, which promotes back-translocation of tRNAs on posttranslocational ribosome complexes and competes with elongation factor G for interaction with pretranslocational ribosomes, inhibiting the elongation phase of protein synthesis.
Pssm-ID: 293900 [Multi-domain] Cd Length: 86 Bit Score: 155.65 E-value: 3.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 290 LRALIFDSYFDPYRGVVVIFRVVDGNLGVGDAVKFMNTGKSYTIDEIGIMRPQKVPVNRLSAGEVGYMIANIKSVADARV 369
Cdd:cd03699 1 LRALIFDSWYDPYRGVVVLVRVFDGTLKKGDKIRFMATGKEYEVLEVGVFTPKMVPTDELSAGEVGYIIAGIKSVKDARV 80
|
....*.
gi 317411685 370 GDTITT 375
Cdd:cd03699 81 GDTITL 86
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
85-571 |
1.13e-42 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 164.74 E-value: 1.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 85 PPSQIRNFSIIAHIDHGKSTLADTLLSKTKTVAAR---DMEAQLLDSMDIERERGITIKLNSARMNYvandgETYVLNLI 161
Cdd:PRK13351 4 PLMQIRNIGILAHIDAGKTTLTERILFYTGKIHKMgevEDGTTVTDWMPQEQERGITIESAATSCDW-----DNHRINLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 162 DTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDLEIITVLNKID---------------------- 219
Cdd:PRK13351 79 DTPGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDrvgadlfkvledieerfgkrpl 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 220 ---LP---GAEPERV----KVRSIHWFPYD------RVGVRE-------------IEDVLGLDTE--------------- 255
Cdd:PRK13351 159 plqLPigsEDGFEGVvdliTEPELHFSEGDggstveEGPIPEelleeveeareklIEALAEFDDEllelylegeelsaeq 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 256 ------DAVVA---------SAKANIGMEDILENIVKMIPPPPDT------------------GDEPLRALIFDSYFDPY 302
Cdd:PRK13351 239 lraplrEGTRSghlvpvlfgSALKNIGIEPLLDAVVDYLPSPLEVppprgskdngkpvkvdpdPEKPLLALVFKVQYDPY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 303 RGVVVIFRVVDGNLGVGDAVKFMNTGKSYTIDEIGIMRPQK-VPVNRLSAGEvgymIANIKSVADARVGDTITTTKDSST 381
Cdd:PRK13351 319 AGKLTYLRVYSGTLRAGSQLYNGTGGKREKVGRLFRLQGNKrEEVDRAKAGD----IVAVAGLKELETGDTLHDSADPVL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 382 EPLPGYSEatPMVYCGLFPTDSDQYEDLRVALGKLQINDAALRYepEQSSAMG----FGfrcgfLGLLHMEIVQERLERE 457
Cdd:PRK13351 395 LELLTFPE--PVVSLAVEPERRGDEQKLAEALEKLVWEDPSLRV--EEDEETGqtilSG-----MGELHLEVALERLRRE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 458 YDLGLITTAPSVVYK---------VYT----SDGA------------------------CVDIANPADLPDA---SVRDR 497
Cdd:PRK13351 466 FKLEVNTGKPQVAYRetirkmaegVYRhkkqFGGKgqfgevhlrveplergagfifvskVVGGAIPEELIPAvekGIREA 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 498 IE---------------------------------------------------EPFVKLEMFAPSDYVGSLMELAQQRRG 526
Cdd:PRK13351 546 LAsgplagypvtdlrvtvldgkyhpvdssesafkaaarkafleafrkanpvllEPIMELEITVPTEHVGDVLGDLSQRRG 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 317411685 527 EFIDMTYLSESRTCLKYDIPLGEvVTDFFDELKSRSKGYAS--MEYS 571
Cdd:PRK13351 626 RIEGTEPRGDGEVLVKAEAPLAE-LFGYATRLRSMTKGRGSftMEFS 671
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
89-575 |
7.21e-42 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 161.42 E-value: 7.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 89 IRNFSIIAHIDHGKSTLADTLLSKTKTVAAR-DMEAQLLDSMDIERERGITIKLNSARMNYvaNDgetYVLNLIDTPGHV 167
Cdd:PRK10218 5 LRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRaETQERVMDSNDLEKERGITILAKNTAIKW--ND---YRINIVDTPGHA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 168 DFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDLEIITVLNKIDLPGAEPERVKVRSIHWFpydrVGVREIE 247
Cdd:PRK10218 80 DFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLF----VNLDATD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 248 DVLGLDTEDAVVASAKANIGMEDILEN-------IVKMIPPPPDTGDEPLRALIFDSYFDPYRGVVVIFRVVDGNLGVGD 320
Cdd:PRK10218 156 EQLDFPIVYASALNGIAGLDHEDMAEDmtplyqaIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 321 AVKFMNTGKSYTIDEIGIMRPQkVPVNRLSA--GEVGYMIAnIKSVADARVGDTITTTKDssTEPLPGYSEATP---MVY 395
Cdd:PRK10218 236 QVTIIDSEGKTRNAKVGKVLGH-LGLERIETdlAEAGDIVA-ITGLGELNISDTVCDTQN--VEALPALSVDEPtvsMFF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 396 C---GLFPTDSDQYEDLRVALGKLQ---INDAALRYEPEQSSAmgfGFRCGFLGLLHMEIVQERLEREyDLGLITTAPSV 469
Cdd:PRK10218 312 CvntSPFCGKEGKFVTSRQILDRLNkelVHNVALRVEETEDAD---AFRVSGRGELHLSVLIENMRRE-GFELAVSRPKV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 470 VYKvytsdgacvdianpadlpdaSVRDRIEEPFVKLEMFAPSDYVGSLMELAQQRRGEFIDMTYLSESRTCLKYDIPlGE 549
Cdd:PRK10218 388 IFR--------------------EIDGRKQEPYENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIP-SR 446
|
490 500
....*....|....*....|....*.
gi 317411685 550 VVTDFFDELKSRSKGYASMEYSFNEY 575
Cdd:PRK10218 447 GLIGFRSEFMTMTSGTGLLYSTFSHY 472
|
|
| lepA_C |
cd03709 |
lepA_C: This family represents the C-terminal region of LepA, a GTP-binding protein localized ... |
500-579 |
1.17e-40 |
|
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: 143.02 E-value: 1.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 500 EPFVKLEMFAPSDYVGSLMELAQQRRGEFIDMTYLSESRTCLKYDIPLGEVVTDFFDELKSRSKGYASMEYSFNEYRKSD 579
Cdd:cd03709 1 EPFVKATIITPSEYLGAIMELCQERRGVQKDMEYLDANRVMLTYELPLAEIVYDFFDKLKSISKGYASLDYELIGYRESD 80
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
95-472 |
1.88e-40 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 157.98 E-value: 1.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 95 IAHIDHGKSTLADTLLSKTKTVAAR---DMEAQLLDSMDIERERGITIKLNSARMNYvanDGETyvLNLIDTPGHVDFSY 171
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRIgevEDGTTTMDFMPEERERGISITSAATTCEW---KGHK--INLIDTPGHVDFTG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 172 EVSRSLAACEGALLVVDASQGVEAQTVAnvYLALENDLEI--ITVLNKIDLPGAEPERV--------------------- 228
Cdd:PRK12740 76 EVERALRVLDGAVVVVCAVGGVEPQTET--VWRQAEKYGVprIIFVNKMDRAGADFFRVlaqlqeklgapvvplqlpige 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 229 -----------KVRSIHWFPYDRVGVREIEDVLgLD------------------------------TEDAVVA------- 260
Cdd:PRK12740 154 gddftgvvdllSMKAYRYDEGGPSEEIEIPAEL-LDraeeareellealaefddelmekylegeelSEEEIKAglrkatl 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 261 ----------SAKANIGMEDILENIVKMIPPPPDTG-----------------DEPLRALIFDSYFDPYRGVVVIFRVVD 313
Cdd:PRK12740 233 ageivpvfcgSALKNKGVQRLLDAVVDYLPSPLEVPpvdgedgeegaelapdpDGPLVALVFKTMDDPFVGKLSLVRVYS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 314 GNLGVGDAVKFMNTGKsytiDE-IG-IMRP---QKVPVNRLSAGEVGyMIANIKsvaDARVGDTITTTKD-----SSTEP 383
Cdd:PRK12740 313 GTLKKGDTLYNSGTGK----KErVGrLYRMhgkQREEVDEAVAGDIV-AVAKLK---DAATGDTLCDKGDpillePMEFP 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 384 LPGYSEAtpmvycgLFPTDSDQYEDLRVALGKLQINDAALRYEPEQS------SAMgfgfrcgflGLLHMEIVQERLERE 457
Cdd:PRK12740 385 EPVISLA-------IEPKDKGDEEKLSEALGKLAEEDPTLRVERDEEtgqtilSGM---------GELHLDVALERLKRE 448
|
490
....*....|....*
gi 317411685 458 YDLGLITTAPSVVYK 472
Cdd:PRK12740 449 YGVEVETGPPQVPYR 463
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
73-472 |
3.23e-40 |
|
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: 157.75 E-value: 3.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 73 RAK-VDPNAVLQVPPSQIRNFSIIAHIDHGKSTLADTLLSKTKTVAARDMEAQL-LDSMDIERERGITIklNSARMNYVA 150
Cdd:TIGR00490 2 RAKmIDKIKELMWKPKFIRNIGIVAHIDHGKTTLSDNLLAGAGMISEELAGQQLyLDFDEQEQERGITI--NAANVSMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 151 N-DGETYVLNLIDTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDLEIITVLNKIDLPGAE----P 225
Cdd:TIGR00490 80 EyEGNEYLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKPVLFINKVDRLINElkltP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 226 ERVKVRSIHWFP-----YDRVGVREIEDVLGLDTEDAVVA--SA------------KANIGMEDI--------------- 271
Cdd:TIGR00490 160 QELQERFIKIITevnklIKAMAPEEFRDKWKVRVEDGSVAfgSAyynwaisvpsmkKTGIGFKDIykyckedkqkelakk 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 272 -------LENIVKMIPPPPDT----------GD---------------EPLRALIFDSYFDPYRGVVVIFRVVDGNLGVG 319
Cdd:TIGR00490 240 splhqvvLDMVIRHLPSPIEAqkyripviwkGDlnsevgkamlncdpkGPLALMITKIVVDKHAGEVAVGRLYSGTIRPG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 320 DAVKFMNTGKSYTIDEIGI-MRPQKVPVNRLSAGEvgymIANIKSVADARVGDTITTTKDSST--EPLPGYSEatPMVYC 396
Cdd:TIGR00490 320 MEVYIVDRKAKARIQQVGVyMGPERVEVDEIPAGN----IVAVIGLKDAVAGETICTTVENITpfESIKHISE--PVVTV 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 317411685 397 GLFPTDSDQYEDLRVALGKLQINDAALRYEPEQSSamGFGFRCGfLGLLHMEIVQERLEREYDLGLITTAPSVVYK 472
Cdd:TIGR00490 394 AIEAKNTKDLPKLIEVLRQVAKEDPTVHVEINEET--GEHLISG-MGELHLEIIVEKIREDYGLDVETSPPIVVYR 466
|
|
| EF-G |
TIGR00484 |
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ... |
84-472 |
2.98e-34 |
|
translation elongation factor EF-G; After peptide bond formation, this elongation factor of bacteria and organelles catalyzes the translocation of the tRNA-mRNA complex, with its attached nascent polypeptide chain, from the A-site to the P-site of the ribosome. Every completed bacterial genome has at least one copy, but some species have additional EF-G-like proteins. The closest homolog to canonical (e.g. E. coli) EF-G in the spirochetes clusters as if it is derived from mitochondrial forms, while a more distant second copy is also present. Synechocystis PCC6803 has a few proteins more closely related to EF-G than to any other characterized protein. Two of these resemble E. coli EF-G more closely than does the best match from the spirochetes; it may be that both function as authentic EF-G. [Protein synthesis, Translation factors]
Pssm-ID: 129575 [Multi-domain] Cd Length: 689 Bit Score: 139.17 E-value: 2.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 84 VPPSQIRNFSIIAHIDHGKSTLADTLLSKT----KTVAARDMEAQLlDSMDIERERGITIklNSARMNYVANDgetYVLN 159
Cdd:TIGR00484 5 TDLNRFRNIGISAHIDAGKTTTTERILFYTgrihKIGEVHDGAATM-DWMEQEKERGITI--TSAATTVFWKG---HRIN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 160 LIDTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDLEIITVLNKIDLPGAEPER------------ 227
Cdd:TIGR00484 79 IIDTPGHVDFTVEVERSLRVLDGAVAVLDAVGGVQPQSETVWRQANRYEVPRIAFVNKMDKTGANFLRvvnqikqrlgan 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 228 --------------------VKVRSIHW------------FPYDRVGVRE------IEDVLGLD-------------TED 256
Cdd:TIGR00484 159 avpiqlpigaednfigvidlVEMKAYFFngdkgtkaiekeIPSDLLEQAKelrenlVEAVAEFDeelmekylegeelTIE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 257 AV-----------------VASAKANIGMEDILENIVKMIPPP----------PDTG---------DEPLRALIFDSYFD 300
Cdd:TIGR00484 239 EIknairkgvlnceffpvlCGSAFKNKGVQLLLDAVVDYLPSPtdvpaikgidPDTEkeierkasdDEPFSALAFKVATD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 301 PYRGVVVIFRVVDGNLGVGDAVKFMNTGKSYTIDEIGIMRPQKV-PVNRLSAGEvgymIANIKSVADARVGDTITTTKDS 379
Cdd:TIGR00484 319 PFVGQLTFVRVYSGVLKSGSYVKNSRKNKKERVGRLVKMHANNReEIKEVRAGD----ICAAIGLKDTTTGDTLCDPKID 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 380 STepLPGYSEATPMVYCGLFPTDSDQYEDLRVALGKLQINDAALRY--EPEQSSAMGFGfrcgfLGLLHMEIVQERLERE 457
Cdd:TIGR00484 395 VI--LERMEFPEPVISLAVEPKTKADQEKMGIALGKLAEEDPTFRTftDPETGQTIIAG-----MGELHLDIIVDRMKRE 467
|
490
....*....|....*
gi 317411685 458 YDLGLITTAPSVVYK 472
Cdd:TIGR00484 468 FKVEANVGAPQVAYR 482
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
86-219 |
2.83e-33 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 137.10 E-value: 2.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 86 PSQIRNFSIIAHIDHGKSTLADTLLSKTKTVAARDM-EAQLLDSMDIERERGITIKLNSARMNY-----VANDGETYVLN 159
Cdd:PTZ00416 16 PDQIRNMSVIAHVDHGKSTLTDSLVCKAGIISSKNAgDARFTDTRADEQERGITIKSTGISLYYehdleDGDDKQPFLIN 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 160 LIDTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDLEIITVLNKID 219
Cdd:PTZ00416 96 LIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKVD 155
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
91-294 |
4.93e-32 |
|
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: 124.27 E-value: 4.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 91 NFSIIAHIDHGKSTLADTLLSKTKTVAAR---DMEAQLLDSMDIERERGITIKLNSARMNYvaNDGEtyvLNLIDTPGHV 167
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIRELgsvDKGTTRTDSMELERQRGITIFSAVASFQW--EDTK---VNIIDTPGHM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 168 DFSYEVSRSLAACEGALLVVDASQGVEAQTvaNVYLALENDLEIITVL--NKIDLPGAEPERVkVRSI------HWFPYD 239
Cdd:cd04168 76 DFIAEVERSLSVLDGAILVISAVEGVQAQT--RILFRLLRKLNIPTIIfvNKIDRAGADLEKV-YQEIkeklspDIVPMQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 317411685 240 RVGVREIEDVLGLDTEDAVVASAKANigmEDILENIVKMIPPPPDTGDEPLRALI 294
Cdd:cd04168 153 KVGLYPNICDTNNIDDEQIETVAEGN---DELLEKYLSGGPLEELELDNELSARI 204
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
90-219 |
7.77e-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: 117.37 E-value: 7.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 90 RNFSIIAHIDHGKSTLADTLLSKT--KTVAARDMEAQL--LDSMDIERERGITIKLNSarMNYVANDGE--TYVLNLIDT 163
Cdd:cd04167 1 RNVCIAGHLHHGKTSLLDMLIEQThkRTPSVKLGWKPLryTDTRKDEQERGISIKSNP--ISLVLEDSKgkSYLINIIDT 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 317411685 164 PGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDLEIITVLNKID 219
Cdd:cd04167 79 PGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKID 134
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
91-234 |
1.73e-28 |
|
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: 115.28 E-value: 1.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 91 NFSIIAHIDHGKSTLADTLL---SKTKTVAARDMEAQLLDSMDIERERGITIklNSARMNYVANDgetYVLNLIDTPGHV 167
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILyytGRIHKIGEVHGGGATMDWMEQERERGITI--QSAATTCFWKD---HRINIIDTPGHV 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 317411685 168 DFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDLEIITVLNKIDLPGAEPERVkVRSIH 234
Cdd:cd01886 76 DFTIEVERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRV-VEQIR 141
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
90-300 |
3.67e-28 |
|
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.
Pssm-ID: 206732 [Multi-domain] Cd Length: 268 Bit Score: 114.23 E-value: 3.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 90 RNFSIIAHIDHGKSTLADTLL------SKTKTVAAR-DMEAQLLDSMDIERERGITIklNSARMNYVANDgetYVLNLID 162
Cdd:cd04169 3 RTFAIISHPDAGKTTLTEKLLlfggaiQEAGAVKARkSRKHATSDWMEIEKQRGISV--TSSVMQFEYKG---CVINLLD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 163 TPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDLEIITVLNKIDLPGAEPERVkvrsihwfpydrvg 242
Cdd:cd04169 78 TPGHEDFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDREGRDPLEL-------------- 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 317411685 243 VREIEDVLGLDTEDAV--VASAKANIGMEDILENIV---------KMIPPPPDTG--DEPLRALIFDSYFD 300
Cdd:cd04169 144 LDEIENELGIDCAPMTwpIGMGKDFKGVYDRYDKEIylyergaggAIKAPEETKGldDPKLDELLGEDLAE 214
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
89-233 |
5.12e-28 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 120.60 E-value: 5.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 89 IRNFSIIAHIDHGKSTLADTLLSKTKTVAARDM-EAQLLDSMDIERERGITIK---------LNSARMNYVAN--DGETY 156
Cdd:PLN00116 19 IRNMSVIAHVDHGKSTLTDSLVAAAGIIAQEVAgDVRMTDTRADEAERGITIKstgislyyeMTDESLKDFKGerDGNEY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 157 VLNLIDTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDLEIITVLNKID-------LPGAEPERVK 229
Cdd:PLN00116 99 LINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTETVLRQALGERIRPVLTVNKMDrcflelqVDGEEAYQTF 178
|
....
gi 317411685 230 VRSI 233
Cdd:PLN00116 179 SRVI 182
|
|
| EFG_C |
pfam00679 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
497-585 |
1.67e-26 |
|
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: 103.39 E-value: 1.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 497 RIEEPFVKLEMFAPSDYVGSLMELAQQRRGEFIDMTYLSESRTCLKYDIPLGEVVtDFFDELKSRSKGYASMEYSFNEYR 576
Cdd:pfam00679 1 VLLEPIEKVTIDVPEEYVGDVISDLNSRRGEILDMDPDDGGRVVIEAEVPLAELF-GFATELRSLTKGRGSFSMEFSGYQ 79
|
....*....
gi 317411685 577 KSDLVRLDV 585
Cdd:pfam00679 80 PVPGDILDR 88
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
91-330 |
7.75e-25 |
|
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: 107.71 E-value: 7.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 91 NFSIIAHIDHGKSTLADTLLSKTKTVAARDME----------------AQLLDSMDIERERGITIKLnsARMNYvanDGE 154
Cdd:COG5256 9 NLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEkyeeeaekkgkesfkfAWVMDRLKEERERGVTIDL--AHKKF---ETD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 155 TYVLNLIDTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLA--LENDlEIITVLNKIDLPGAEPERvkvrs 232
Cdd:COG5256 84 KYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLArtLGIN-QLIVAVNKMDAVNYSEKR----- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 233 ihwfpYDRVgVREIEDVL---GLDTEDAVVASAKANIGmedilENIVK------------------MIPPPPDTGDEPLR 291
Cdd:COG5256 158 -----YEEV-KEEVSKLLkmvGYKVDKIPFIPVSAWKG-----DNVVKksdnmpwyngptllealdNLKEPEKPVDKPLR 226
|
250 260 270
....*....|....*....|....*....|....*....
gi 317411685 292 ALIFDSYFDPYRGVVVIFRVVDGNLGVGDAVKFMNTGKS 330
Cdd:COG5256 227 IPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVV 265
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
91-330 |
1.24e-24 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 107.32 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 91 NFSIIAHIDHGKSTLADTLLSKTKTVAARDME----------------AQLLDSMDIERERGITIKLNSARMnyvanDGE 154
Cdd:PRK12317 8 NLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEelreeakekgkesfkfAWVMDRLKEERERGVTIDLAHKKF-----ETD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 155 TYVLNLIDTPGHVDFSYEVSRSLAACEGALLVVDA--SQGVEAQTVANVYLA--LENDlEIITVLNKIDLPGAEPERvkv 230
Cdd:PRK12317 83 KYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAAddAGGVMPQTREHVFLArtLGIN-QLIVAINKMDAVNYDEKR--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 231 rsihwfpYDRVgVREIEDVL---GLDTEDAVVASAKANIGmedilENIVK------------------MIPPPPDTGDEP 289
Cdd:PRK12317 159 -------YEEV-KEEVSKLLkmvGYKPDDIPFIPVSAFEG-----DNVVKksenmpwyngptllealdNLKPPEKPTDKP 225
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 317411685 290 LRALIFDSYFDPYRGVVVIFRVVDGNLGVGDAVKFMNTGKS 330
Cdd:PRK12317 226 LRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMPAGVV 266
|
|
| Elongation_Factor_C |
cd01514 |
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ... |
500-579 |
1.19e-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: 94.86 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 500 EPFVKLEMFAPSDYVGSLMELAQQRRGEFIDMTYLSESRTCLKYDIPLGEVVtDFFDELKSRSKGYASMEYSFNEYRKSD 579
Cdd:cd01514 1 EPIMKVEITVPEEYLGAVIGDLSKRRGEILGMEPRGTGRVVIKAELPLAEMF-GFATDLRSLTQGRASFSMEFSHYEPVP 79
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
90-254 |
3.19e-22 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 100.98 E-value: 3.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 90 RNFSIIAHIDHGKSTLADTLL------SKTKTVAARdmEAQLL---DSMDIERERGITIklNSARMNYVANDgetYVLNL 160
Cdd:PRK00741 11 RTFAIISHPDAGKTTLTEKLLlfggaiQEAGTVKGR--KSGRHatsDWMEMEKQRGISV--TSSVMQFPYRD---CLINL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 161 IDTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTvanvyLALEN-----DLEIITVLNKIDLPGAEPERVkvrsihw 235
Cdd:PRK00741 84 LDTPGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQT-----RKLMEvcrlrDTPIFTFINKLDRDGREPLEL------- 151
|
170
....*....|....*....
gi 317411685 236 fpydrvgVREIEDVLGLDT 254
Cdd:PRK00741 152 -------LDEIEEVLGIAC 163
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
94-278 |
2.97e-19 |
|
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: 85.60 E-value: 2.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 94 IIAHIDHGKSTLADTLlSKTKtVAArdMEAqlldsmdiereRGITIKLnsarmnyvandGETYV--------LNLIDTPG 165
Cdd:cd01887 5 VMGHVDHGKTTLLDKI-RKTN-VAA--GEA-----------GGITQHI-----------GAYQVpidvkipgITFIDTPG 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 166 HVDFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDLEIITVLNKIDLP---GAEPERVKvrsihwfpydrvg 242
Cdd:cd01887 59 HEAFTNMRARGASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKPygtEADPERVK------------- 125
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 317411685 243 vrEIEDVLGLDTED------AVVASAKANIGMEDILENIVKM 278
Cdd:cd01887 126 --NELSELGLVGEEwggdvsIVPISAKTGEGIDDLLEAILLL 165
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
91-353 |
1.20e-18 |
|
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: 89.93 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 91 NFSIIAHIDHGKSTLADTLlskTKTVAARDMEaqlldsmdiERERGITIKLNSARMnyvanDGETYVLNLIDTPGHVDFS 170
Cdd:TIGR00475 2 IIATAGHVDHGKTTLLKAL---TGIAADRLPE---------EKKRGMTIDLGFAYF-----PLPDYRLGFIDVPGHEKFI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 171 YEVSRSLAACEGALLVVDASQGVEAQTVANV-YLALENDLEIITVLNKIDLpgAEPERVKVRSIHwfpydrvgVREI-ED 248
Cdd:TIGR00475 65 SNAIAGGGGIDAALLVVDADEGVMTQTGEHLaVLDLLGIPHTIVVITKADR--VNEEEIKRTEMF--------MKQIlNS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 249 VLGLDTEDAVVASAKANIGMEDiLENIVKMIPPPPDTGD--EPLRALIfDSYFD-PYRGVVVIFRVVDGNLGVGDAVKFM 325
Cdd:TIGR00475 135 YIFLKNAKIFKTSAKTGQGIGE-LKKELKNLLESLDIKRiqKPLRMAI-DRAFKvKGAGTVVTGTAFSGEVKVGDNLRLL 212
|
250 260
....*....|....*....|....*...
gi 317411685 326 NTGKsytIDEIGIMRPQKVPVNRLSAGE 353
Cdd:TIGR00475 213 PINH---EVRVKAIQAQNQDVEIAYAGQ 237
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
91-223 |
1.04e-17 |
|
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: 83.80 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 91 NFSIIAHIDHGKSTLADTLLSKTKTVAAR---DMEAQLLDSMDIERERGITIKLNSARMNYvandgETYVLNLIDTPGHV 167
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRLgrvEDGNTVSDYDPEEKKRKMSIETSVAPLEW-----NGHKINLIDTPGYA 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 317411685 168 DFSYEVSRSLAACEGALLVVDASQGVEAQTvANVYLALEnDLEI--ITVLNKIDLPGA 223
Cdd:cd04170 76 DFVGETLSALRAVDAALIVVEAQSGVEVGT-EKVWEFLD-DAKLprIIFINKMDRARA 131
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
93-331 |
3.53e-17 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 85.65 E-value: 3.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 93 SIIAHIDHGKSTLADTLlskTKTVAARDmEAQlldsmdiererGITIKLNSARMNYVANDgETYVLNLIDTPGHVDFSYE 172
Cdd:CHL00189 248 TILGHVDHGKTTLLDKI---RKTQIAQK-EAG-----------GITQKIGAYEVEFEYKD-ENQKIVFLDTPGHEAFSSM 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 173 VSRSLAACEGALLVVDASQGVEAQTVANVYLALENDLEIITVLNKIDLPGAEPERVKvrsihwfpYDRVGVREIEDVLGL 252
Cdd:CHL00189 312 RSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANTERIK--------QQLAKYNLIPEKWGG 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 253 DTEdAVVASAKANIGMEDILENIV---KMIPPPPDTgDEPLRALIFDSYFDPYRGVVVIFRVVDGNLGVGDAvkfMNTGK 329
Cdd:CHL00189 384 DTP-MIPISASQGTNIDKLLETILllaEIEDLKADP-TQLAQGIILEAHLDKTKGPVATILVQNGTLHIGDI---IVIGT 458
|
..
gi 317411685 330 SY 331
Cdd:CHL00189 459 SY 460
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
91-364 |
1.11e-16 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 83.51 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 91 NFSIIAHIDHGKSTLADTL---LSKTKTVAARDMEAqlLDSMDIERERGITIklNSARMNYvanDGETYVLNLIDTPGHV 167
Cdd:PLN03126 83 NIGTIGHVDHGKTTLTAALtmaLASMGGSAPKKYDE--IDAAPEERARGITI--NTATVEY---ETENRHYAHVDCPGHA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 168 DFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDL-EIITVLNKID-------LPGAEPERVKVRSIHWFPYD 239
Cdd:PLN03126 156 DYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVpNMVVFLNKQDqvddeelLELVELEVRELLSSYEFPGD 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 240 RVGVREIEDVLGLdteDAVVASAKANIG-------MEDILENIVKMIPPPPDTGDEPLRALIFDSYFDPYRGVVVIFRVV 312
Cdd:PLN03126 236 DIPIISGSALLAL---EALMENPNIKRGdnkwvdkIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVE 312
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 317411685 313 DGNLGVGDAVKFMNTGKSYTIDEIGIMRPQKVPVNRLSAGEVGYMIANIKSV 364
Cdd:PLN03126 313 RGTVKVGETVDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKA 364
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
91-322 |
5.72e-16 |
|
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: 80.59 E-value: 5.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 91 NFSIIAHIDHGKSTLA---DTLLSKTKTVAARDMEAqlLDSMDIERERGITIklNSARMNYvanDGETYVLNLIDTPGHV 167
Cdd:TIGR00485 14 NVGTIGHVDHGKTTLTaaiTTVLAKEGGAAARAYDQ--IDNAPEEKARGITI--NTAHVEY---ETETRHYAHVDCPGHA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 168 DFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDL-EIITVLNKIDLPgAEPERVKVRSIHwfpydrvgVREI 246
Cdd:TIGR00485 87 DYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVpYIVVFLNKCDMV-DDEELLELVEME--------VREL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 247 EDVLGLDTEDAVVASAKA-------NIGMEDILE---NIVKMIPPPPDTGDEPLRALIFDSYFDPYRGVVVIFRVVDGNL 316
Cdd:TIGR00485 158 LSQYDFPGDDTPIIRGSAlkalegdAEWEAKILElmdAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGII 237
|
....*.
gi 317411685 317 GVGDAV 322
Cdd:TIGR00485 238 KVGEEV 243
|
|
| EFG_III-like |
cd16257 |
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G ... |
392-463 |
8.37e-16 |
|
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: 72.38 E-value: 8.37e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 317411685 392 PMVYCGLFPTDSDQYEDLRVALGKLQINDAALRYEPEQSSamgFGFRCGFLGLLHMEIVQERLEREYDLGLI 463
Cdd:cd16257 1 PVVFVTVEVKNPLDQEKLLEGLERLSEEDPALQVYREEST---GEFILSGLGELHLEIIVARLEREYGVELV 69
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
91-220 |
2.07e-15 |
|
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: 75.68 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 91 NFSIIAHIDHGKSTL------------ADTL--LSKTKTVAARDME---AQLLDSMDIERERGITIklNSARMnYVANDG 153
Cdd:cd04166 1 RFITCGSVDDGKSTLigrllydsksifEDQLaaLERSKSSGTQGEKldlALLVDGLQAEREQGITI--DVAYR-YFSTPK 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 317411685 154 ETYVlnLIDTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLA-LENDLEIITVLNKIDL 220
Cdd:cd04166 78 RKFI--IADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIAsLLGIRHVVVAVNKMDL 143
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
91-322 |
2.29e-15 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 78.45 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 91 NFSIIAHIDHGKSTLA---DTLLSKTKTVAARDMEAqlLDSMDIERERGITIklNSARMNYvanDGETYVLNLIDTPGHV 167
Cdd:PRK12736 14 NIGTIGHVDHGKTTLTaaiTKVLAERGLNQAKDYDS--IDAAPEEKERGITI--NTAHVEY---ETEKRHYAHVDCPGHA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 168 DFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDLEIITV-LNKIDLPGaEPE-----RVKVR---SIHWFPY 238
Cdd:PRK12736 87 DYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVfLNKVDLVD-DEEllelvEMEVRellSEYDFPG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 239 DRVGVREIEDVLGLDTEDAVVASakanigMEDILENIVKMIPPPPDTGDEPLRALIFDSYFDPYRGVVVIFRVVDGNLGV 318
Cdd:PRK12736 166 DDIPVIRGSALKALEGDPKWEDA------IMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKV 239
|
....
gi 317411685 319 GDAV 322
Cdd:PRK12736 240 GDEV 243
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
91-221 |
5.14e-15 |
|
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: 74.45 E-value: 5.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 91 NFSIIAHIDHGKSTLADTLLSKTKTVAARDME----------------AQLLDSMDIERERGITIKLNSARMNYvandgE 154
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEkyekeakemgkesfkyAWVLDKLKEERERGVTIDVGLAKFET-----E 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 155 TYVLNLIDTPGHVDFsyeVSR-----SLAACegALLVVDASQG-------VEAQTVANVYLAleNDL---EIITVLNKID 219
Cdd:cd01883 76 KYRFTIIDAPGHRDF---VKNmitgaSQADV--AVLVVSARKGefeagfeKGGQTREHALLA--RTLgvkQLIVAVNKMD 148
|
..
gi 317411685 220 LP 221
Cdd:cd01883 149 DV 150
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
94-394 |
8.96e-15 |
|
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: 78.03 E-value: 8.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 94 IIA---HIDHGKSTLA------DTllsktktvaardmeaqllDSMDIERERGITIKLNSARMNYvaNDGetYVLNLIDTP 164
Cdd:COG3276 2 IIGtagHIDHGKTTLVkaltgiDT------------------DRLKEEKKRGITIDLGFAYLPL--PDG--RRLGFVDVP 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 165 GHVDFsyeVSRSLAACEG---ALLVVDASQGVEAQTVAnvYLALENDLEI---ITVLNKIDLpgAEPERVK-VRSihwfp 237
Cdd:COG3276 60 GHEKF---IKNMLAGAGGidlVLLVVAADEGVMPQTRE--HLAILDLLGIkrgIVVLTKADL--VDEEWLElVEE----- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 238 ydrvgvrEIEDVL-GLDTEDA--VVASAKANIGME---DILENIVKMIPPPPDTGdeplralifdsyfdPYR-------- 303
Cdd:COG3276 128 -------EIRELLaGTFLEDApiVPVSAVTGEGIDelrAALDALAAAVPARDADG--------------PFRlpidrvfs 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 304 ----GVVVIFRVVDGNLGVGDAVKFMNTGKSYTIDEIgimRPQKVPVNRLSAGE-VGYMIANIkSVADARVGDTITTtkd 378
Cdd:COG3276 187 ikgfGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGI---QVHGQPVEEAYAGQrVALNLAGV-EKEEIERGDVLAA--- 259
|
330
....*....|....*.
gi 317411685 379 ssteplPGYSEATPMV 394
Cdd:COG3276 260 ------PGALRPTDRI 269
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
97-228 |
3.17e-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: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 97 HIDHGKSTLADTLLSktktvaardMEAqllDSMDIERERGITIKLNSARMNYVANDgetyVLNLIDTPGHVDFsyeVSRS 176
Cdd:cd04171 7 HIDHGKTTLIKALTG---------IET---DRLPEEKKRGITIDLGFAYLDLPDGK----RLGFIDVPGHEKF---VKNM 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 317411685 177 LAACEG---ALLVVDASQGVEAQTVAnvYLALENDLEI---ITVLNKIDLpgAEPERV 228
Cdd:cd04171 68 LAGAGGidaVLLVVAADEGIMPQTRE--HLEILELLGIkkgLVVLTKADL--VDEDRL 121
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
94-277 |
1.03e-13 |
|
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: 69.32 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 94 IIAHIDHGKSTLADtllsktktvaardmeaQLLDSMDIERERGITIKLNsARMNYVANDGETYVLNLIDTPGHVDFSY-- 171
Cdd:TIGR00231 6 IVGHPNVGKSTLLN----------------SLLGNKGSITEYYPGTTRN-YVTTVIEEDGKTYKFNLLDTAGQEDYDAir 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 172 -----EVSRSLAACEGALLVVDASQGVEAQTVAnVYLALENDLEIITVLNKIDLPGAEPERVkvrsihwfpydrvgvrEI 246
Cdd:TIGR00231 69 rlyypQVERSLRVFDIVILVLDVEEILEKQTKE-IIHHADSGVPIILVGNKIDLKDADLKTH----------------VA 131
|
170 180 190
....*....|....*....|....*....|.
gi 317411685 247 EDVLGLDTEDAVVASAKANIGMEDILENIVK 277
Cdd:TIGR00231 132 SEFAKLNGEPIIPLSAETGKNIDSAFKIVEA 162
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
91-336 |
1.42e-13 |
|
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and metabolism]; Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 442140 [Multi-domain] Cd Length: 430 Bit Score: 73.20 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 91 NFSIIAHIDHGKSTL------------ADTLLSKTKTVAARDME----AQLLDSMDIERERGITIklNSARMnYVANDGE 154
Cdd:COG2895 19 RFITCGSVDDGKSTLigrllydtksifEDQLAALERDSKKRGTQeidlALLTDGLQAEREQGITI--DVAYR-YFSTPKR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 155 TYVlnLIDTPGHVDFsyevSRSLA----ACEGALLVVDASQGVEAQT-----------VANVYLAlendleiitvLNKID 219
Cdd:COG2895 96 KFI--IADTPGHEQY----TRNMVtgasTADLAILLIDARKGVLEQTrrhsyiasllgIRHVVVA----------VNKMD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 220 LPGAEPERvkvrsihwfpYDRVgVREIEDV---LGLDTEDAVVASAKA--NI-----------G---MEdILENivkmIP 280
Cdd:COG2895 160 LVDYSEEV----------FEEI-VADYRAFaakLGLEDITFIPISALKgdNVversenmpwydGptlLE-HLET----VE 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 317411685 281 PPPDTGDEPLRalifdsyF---------DPYRGvvviF--RVVDGNLGVGDAVKFMNTGKSYTIDEI 336
Cdd:COG2895 224 VAEDRNDAPFR-------FpvqyvnrpnLDFRG----YagTIASGTVRVGDEVVVLPSGKTSTVKSI 279
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
91-333 |
2.62e-13 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 72.55 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 91 NFSIIAHIDHGKSTLADTLlskTKTVA----ARDMEAQLLDSMDIERERGITIklNSARMNY-VANDGETYVlnliDTPG 165
Cdd:PLN03127 63 NVGTIGHVDHGKTTLTAAI---TKVLAeegkAKAVAFDEIDKAPEEKARGITI--ATAHVEYeTAKRHYAHV----DCPG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 166 HVDFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDL-EIITVLNKID-------LPGAEPERVKVRSIHWFP 237
Cdd:PLN03127 134 HADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVpSLVVFLNKVDvvddeelLELVEMELRELLSFYKFP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 238 YDrvgvrEIEDVLGldteDAVVASAKAN--IGMEDILE---NIVKMIPPPPDTGDEPLRALIFDSYFDPYRGVVVIFRVV 312
Cdd:PLN03127 214 GD-----EIPIIRG----SALSALQGTNdeIGKNAILKlmdAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVE 284
|
250 260
....*....|....*....|.
gi 317411685 313 DGNLGVGDAVKFMNTGKSYTI 333
Cdd:PLN03127 285 QGTIKVGEEVEIVGLRPGGPL 305
|
|
| tufA |
CHL00071 |
elongation factor Tu |
91-343 |
2.80e-13 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 72.30 E-value: 2.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 91 NFSIIAHIDHGKSTL--ADTL-LSKTKTVAARDMEAqlLDSMDIERERGITIklNSARMNYvandgETYVLNL--IDTPG 165
Cdd:CHL00071 14 NIGTIGHVDHGKTTLtaAITMtLAAKGGAKAKKYDE--IDSAPEEKARGITI--NTAHVEY-----ETENRHYahVDCPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 166 HVDFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDLEIITV-LNKID-------LPGAEPERVKVRSIHWFP 237
Cdd:CHL00071 85 HADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVfLNKEDqvddeelLELVELEVRELLSKYDFP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 238 YDRVGVREIEDVLGLdteDAVVASAKANIG-------MEDILENIVKMIPPPPDTGDEPLRALIFDSYFDPYRGVVVIFR 310
Cdd:CHL00071 165 GDDIPIVSGSALLAL---EALTENPKIKRGenkwvdkIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGR 241
|
250 260 270
....*....|....*....|....*....|...
gi 317411685 311 VVDGNLGVGDAVKFMNTGKSYTIDEIGIMRPQK 343
Cdd:CHL00071 242 IERGTVKVGDTVEIVGLRETKTTTVTGLEMFQK 274
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
91-227 |
4.57e-13 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.
Pssm-ID: 206676 [Multi-domain] Cd Length: 192 Bit Score: 68.16 E-value: 4.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 91 NFSIIAHIDHGKSTLADTLLSKTKTVAardmeaqlLDSMDIERERGITIKL----------NSARMNYVANDgETYVLNL 160
Cdd:cd01889 2 NVGLLGHVDSGKTSLAKALSEIASTAA--------FDKNPQSQERGITLDLgfssfevdkpKHLEDNENPQI-ENYQITL 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 317411685 161 IDTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDLEIITVLNKIDL-PGAEPER 227
Cdd:cd01889 73 VDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDLiPEEERKR 140
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
101-277 |
4.72e-13 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 67.48 E-value: 4.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 101 GKSTLADTLLSKTKTVaardmeaqlldsmdIERERGITIKLNSARMNYvanDGETYVLNLIDTPGHVDFSYEVSRSLAA- 179
Cdd:cd00882 9 GKSSLLNALLGGEVGE--------------VSDVPGTTRDPDVYVKEL---DKGKVKLVLVDTPGLDEFGGLGREELARl 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 180 ----CEGALLVVDASQGVEAQTVANVYLAL--ENDLEIITVLNKIDLPGAEPERVKVRSIHWFPYDRVGVREIedvlgld 253
Cdd:cd00882 72 llrgADLILLVVDSTDRESEEDAKLLILRRlrKEGIPIILVGNKIDLLEEREVEELLRLEELAKILGVPVFEV------- 144
|
170 180
....*....|....*....|....
gi 317411685 254 tedavvaSAKANIGMEDILENIVK 277
Cdd:cd00882 145 -------SAKTGEGVDELFEKLIE 161
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
91-383 |
8.45e-13 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 70.93 E-value: 8.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 91 NFSIIAHIDHGKSTLADTLLSKTKTVAARDME----------------AQLLDSMDIERERGITIKLNSARMnyvandgE 154
Cdd:PTZ00141 9 NLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEkfekeaaemgkgsfkyAWVLDKLKAERERGITIDIALWKF-------E 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 155 T--YVLNLIDTPGHVDFSYEVSRSLAACEGALLVVDASQGV-------EAQTVANVYLALENDL-EIITVLNKIDLPGAE 224
Cdd:PTZ00141 82 TpkYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEfeagiskDGQTREHALLAFTLGVkQMIVCINKMDDKTVN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 225 --PERvkvrsihwfpYDRVgVREIEDVL---GLDTEDAVVASAKANIGmEDILENIVKM--------------IPPPPDT 285
Cdd:PTZ00141 162 ysQER----------YDEI-KKEVSAYLkkvGYNPEKVPFIPISGWQG-DNMIEKSDNMpwykgptllealdtLEPPKRP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 286 GDEPLRALIFDSYFDPYRGVVVIFRVVDGNLGVGDAVKFMNTGKSYTIDEIGiMRPQKVPVNRlSAGEVGYMIANIkSVA 365
Cdd:PTZ00141 230 VDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVE-MHHEQLAEAV-PGDNVGFNVKNV-SVK 306
|
330
....*....|....*...
gi 317411685 366 DARVGDTITttkDSSTEP 383
Cdd:PTZ00141 307 DIKRGYVAS---DSKNDP 321
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
97-322 |
5.46e-12 |
|
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: 68.50 E-value: 5.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 97 HIDHGKSTLADTLLsKTKtVAARdmEAqlldsmdiereRGIT-------IKLNSARMnyvandgeTYvlnlIDTPGHVDF 169
Cdd:COG0532 12 HVDHGKTSLLDAIR-KTN-VAAG--EA-----------GGITqhigayqVETNGGKI--------TF----LDTPGHEAF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 170 SYEVSRslaaceGA------LLVVDASQGVEAQTV--------ANVylalendlEIITVLNKIDLPGAEPERVKvrsihw 235
Cdd:COG0532 65 TAMRAR------GAqvtdivILVVAADDGVMPQTIeainhakaAGV--------PIIVAINKIDKPGANPDRVK------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 236 fpydrvgvRE-------IEDvLGLDTEDAVVaSAKANIGMEDILENIV--------KMIPpppdtgDEPLRALIFDSYFD 300
Cdd:COG0532 125 --------QElaehglvPEE-WGGDTIFVPV-SAKTGEGIDELLEMILlqaevlelKANP------DRPARGTVIEAKLD 188
|
250 260
....*....|....*....|..
gi 317411685 301 PYRGVVVIFRVVDGNLGVGDAV 322
Cdd:COG0532 189 KGRGPVATVLVQNGTLKVGDIV 210
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
91-283 |
8.28e-12 |
|
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: 64.60 E-value: 8.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 91 NFSIIAHIDHGKSTLADTLlSKTKTVAARDmeaqlldsmdiERERGITIKLNSARMN-------YVANDGETY------- 156
Cdd:cd01888 2 NIGTIGHVAHGKTTLVKAL-SGVWTVRHKE-----------ELKRNITIKLGYANAKiykcpncGCPRPYDTPececpgc 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 157 --------VLNLIDTPGHvdfsyEVsrsLAAC--------EGALLVVDASQGV-EAQTVANVyLALEN-DLE-IITVLNK 217
Cdd:cd01888 70 ggetklvrHVSFVDCPGH-----EI---LMATmlsgaavmDGALLLIAANEPCpQPQTSEHL-AALEImGLKhIIILQNK 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 317411685 218 IDLPGAEPERVKVRSIHWFpydrvgvreiedVLGLDTEDAVVA--SAKANIGMEDILENIVKMIPPPP 283
Cdd:cd01888 141 IDLVKEEQALENYEQIKEF------------VKGTIAENAPIIpiSAQLKYNIDVLCEYIVKKIPTPP 196
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
95-282 |
9.03e-12 |
|
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: 64.53 E-value: 9.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 95 IAHIDHGKSTLAD---TLLSKTKTVAARDMEAqlLDSMDIERERGITIklNSARMNYvanDGETYVLNLIDTPGHVDFSY 171
Cdd:cd01884 8 IGHVDHGKTTLTAaitKVLAKKGGAKAKKYDE--IDKAPEEKARGITI--NTAHVEY---ETANRHYAHVDCPGHADYIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 172 EVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDLEIITV-LNKIDLPgAEPERVKVRSIHwfpydrvgVREIEDVL 250
Cdd:cd01884 81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVfLNKADMV-DDEELLELVEME--------VRELLSKY 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 317411685 251 GLDTEDA--VVASA-KA------NIGMEDILENIVKM---IPPP 282
Cdd:cd01884 152 GFDGDDTpiVRGSAlKAlegddpNKWVDKILELLDALdsyIPTP 195
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
91-394 |
1.88e-11 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 66.65 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 91 NFSIIAHIDHGKSTLADTLLSKTKTVAARDME----------------AQLLDSMDIERERGITIKLNSARMNYVandge 154
Cdd:PLN00043 9 NIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIErfekeaaemnkrsfkyAWVLDKLKAERERGITIDIALWKFETT----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 155 TYVLNLIDTPGHVDFSYEVSRSLAACEGALLVVDASQG-------VEAQTVANVYLALENDL-EIITVLNKIDlpGAEPE 226
Cdd:PLN00043 84 KYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGgfeagisKDGQTREHALLAFTLGVkQMICCCNKMD--ATTPK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 227 RVKVRsihwfpYDRVgVREIEDVL----------------GLDTEDAVVASAKANIGMEDILENIVKMIPPPPDTGDEPL 290
Cdd:PLN00043 162 YSKAR------YDEI-VKEVSSYLkkvgynpdkipfvpisGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 291 RALIFDSYFDPYRGVVVIFRVVDGNLGVGDAVKFMNTGKSYTIDEIGIMrpQKVPVNRLSAGEVGYMIANIkSVADARVG 370
Cdd:PLN00043 235 RLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMH--HESLQEALPGDNVGFNVKNV-AVKDLKRG 311
|
330 340
....*....|....*....|....
gi 317411685 371 DTITTTKDsstEPLPGYSEATPMV 394
Cdd:PLN00043 312 YVASNSKD---DPAKEAANFTSQV 332
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
91-322 |
3.46e-11 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 65.63 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 91 NFSIIAHIDHGKSTLADTLlskTKTVAARDM-EAQLLDSMDI---ERERGITIklNSARMNYvandgET----YVlnLID 162
Cdd:PRK12735 14 NVGTIGHVDHGKTTLTAAI---TKVLAKKGGgEAKAYDQIDNapeEKARGITI--NTSHVEY-----ETanrhYA--HVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 163 TPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDLEIITV-LNKIDLPGaEPE-----RVKVR---SI 233
Cdd:PRK12735 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVfLNKCDMVD-DEEllelvEMEVRellSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 234 HWFPYDRVGVREIEDVLGLDTEDAVVASAKanigMEDILENIVKMIPPPPDTGDEPLRALIFDSYFDPYRGVVVIFRVVD 313
Cdd:PRK12735 161 YDFPGDDTPIIRGSALKALEGDDDEEWEAK----ILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVER 236
|
....*....
gi 317411685 314 GNLGVGDAV 322
Cdd:PRK12735 237 GIVKVGDEV 245
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
91-322 |
1.40e-10 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 63.67 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 91 NFSIIAHIDHGKSTLADTLlskTKTVAARDM-EAQLLDSMDI---ERERGITIklNSARMNYvandgET----YVlnLID 162
Cdd:PRK00049 14 NVGTIGHVDHGKTTLTAAI---TKVLAKKGGaEAKAYDQIDKapeEKARGITI--NTAHVEY-----ETekrhYA--HVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 163 TPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDLEIITV-LNKIDLPGAEP--ERVKVRsihwfpyd 239
Cdd:PRK00049 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVfLNKCDMVDDEEllELVEME-------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 240 rvgVREIEDVLGLDTEDA--VVASA-KA------NIGMEDILE---NIVKMIPPPPDTGDEPLRALIFDSYFDPYRGVVV 307
Cdd:PRK00049 154 ---VRELLSKYDFPGDDTpiIRGSAlKAlegdddEEWEKKILElmdAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVV 230
|
250
....*....|....*
gi 317411685 308 IFRVVDGNLGVGDAV 322
Cdd:PRK00049 231 TGRVERGIIKVGEEV 245
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
95-220 |
2.32e-10 |
|
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: 63.25 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 95 IAHIDHGKSTLADTLlskTKTVAARDM-EAQLLDSMDI---ERERGITIklNSARMNYvandgET----YVlnLIDTPGH 166
Cdd:COG0050 18 IGHVDHGKTTLTAAI---TKVLAKKGGaKAKAYDQIDKapeEKERGITI--NTSHVEY-----ETekrhYA--HVDCPGH 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 317411685 167 VDFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDLEIITV-LNKIDL 220
Cdd:COG0050 86 ADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKCDM 140
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
158-278 |
1.14e-09 |
|
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: 57.64 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 158 LNLIDTPGHVD-------FSYEVSRSLAACEGALLVVDASQGVEAQtVANVYLALENDLEIITVLNKIDLPGAEPERVKV 230
Cdd:cd00880 48 VVLIDTPGLDEegglgreRVEEARQVADRADLVLLVVDSDLTPVEE-EAKLGLLRERGKPVLLVLNKIDLVPESEEEELL 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 317411685 231 RSIhwfpydrvgvreieDVLGLDTEDAVVASAKANIGMEDILENIVKM 278
Cdd:cd00880 127 RER--------------KLELLPDLPVIAVSALPGEGIDELRKKIAEL 160
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
304-374 |
4.21e-09 |
|
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.
Pssm-ID: 427163 [Multi-domain] Cd Length: 73 Bit Score: 53.42 E-value: 4.21e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 317411685 304 GVVVIFRVVDGNLGVGDAVKFM--NTGKSYTIDEIGIMRPQKVPVNRLSAGEVGYMIANIKSVADARVGDTIT 374
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILpnGTGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| BipA_TypA_C |
cd03710 |
BipA_TypA_C: a C-terminal portion of BipA or TypA having homology to the C terminal domains of ... |
500-577 |
5.30e-09 |
|
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: 53.28 E-value: 5.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 500 EPFVKLEMFAPSDYVGSLMELAQQRRGEFIDMTYLSESRTCLKYDIP----LGevvtdFFDELKSRSKGYASMEYSFNEY 575
Cdd:cd03710 1 EPIEELTIDVPEEYSGAVIEKLGKRKGEMVDMEPDGNGRTRLEFKIPsrglIG-----FRSEFLTDTRGTGIMNHVFDGY 75
|
..
gi 317411685 576 RK 577
Cdd:cd03710 76 EP 77
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
290-374 |
5.87e-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: 5.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 290 LRALIFDSYFDPYRGVVVIFRVVDGNLGVGDAVKFMNTGKSYTIDEIGIMRpqkVPVNRLSAGEVGYMiaNIKSVADARV 369
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFH---EEVDEAKAGDIVGI--GILGVKDILT 75
|
....*
gi 317411685 370 GDTIT 374
Cdd:cd01342 76 GDTLT 80
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
158-279 |
9.13e-09 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 55.37 E-value: 9.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 158 LNLIDTPGHVDfsYEVSRSLAACE-----GALLVVDASQgveAQTVANVYLALEN------DLEIITVLNKIDLPGAEpe 226
Cdd:COG1100 55 LVIWDTPGQDE--FRETRQFYARQltgasLYLFVVDGTR---EETLQSLYELLESlrrlgkKSPIILVLNKIDLYDEE-- 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 317411685 227 rvkvrsihwfpyDRVGVREIEDVLGLDTEDAVVA-SAKANIGMEDILENIVKMI 279
Cdd:COG1100 128 ------------EIEDEERLKEALSEDNIVEVVAtSAKTGEGVEELFAALAEIL 169
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
91-320 |
9.32e-09 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 57.94 E-value: 9.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 91 NFSIIAHIDHGKSTLADTLlskTKTVAARDMEaqlldsmdiERERGITIKLNSA----RMNYVANDGETYVLN------- 159
Cdd:PRK04000 11 NIGMVGHVDHGKTTLVQAL---TGVWTDRHSE---------ELKRGITIRLGYAdatiRKCPDCEEPEAYTTEpkcpncg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 160 ----------LIDTPGHvdfsyEV------SRSlAACEGALLVVDASQGV-EAQTVANvYLALE-----NdleIITVLNK 217
Cdd:PRK04000 79 setellrrvsFVDAPGH-----ETlmatmlSGA-ALMDGAILVIAANEPCpQPQTKEH-LMALDiigikN---IVIVQNK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 218 IDLpgAEPERVKVRsihwfpYdrvgvREIED-VLGLDTEDA----VVASAKANIGMedILENIVKMIPPPPDTGDEPLRA 292
Cdd:PRK04000 149 IDL--VSKERALEN------Y-----EQIKEfVKGTVAENApiipVSALHKVNIDA--LIEAIEEEIPTPERDLDKPPRM 213
|
250 260 270
....*....|....*....|....*....|....*..
gi 317411685 293 LIFDSyFD------PY---RGVVVIFRVVDGNLGVGD 320
Cdd:PRK04000 214 YVARS-FDvnkpgtPPeklKGGVIGGSLIQGVLKVGD 249
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
94-320 |
1.87e-08 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 57.75 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 94 IIA---HIDHGKSTLadtLLSKTKTVAARDMEaqlldsmdiERERGITIKLNSArmnYVAN-DGEtyVLNLIDTPGHVDF 169
Cdd:PRK10512 2 IIAtagHVDHGKTTL---LQAITGVNADRLPE---------EKKRGMTIDLGYA---YWPQpDGR--VLGFIDVPGHEKF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 170 syeVSRSLAACEG---ALLVVDASQGVEAQTVANV-YLALENDLEIITVLNKIDLPgAEPERVKVRsihwfpydrvgvRE 245
Cdd:PRK10512 65 ---LSNMLAGVGGidhALLVVACDDGVMAQTREHLaILQLTGNPMLTVALTKADRV-DEARIAEVR------------RQ 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 317411685 246 IEDVL---GLDTEDAVVASAKANIGMEDILENIVKMiPPPPDTGDEPLRaLIFDSYFD-PYRGVVVIFRVVDGNLGVGD 320
Cdd:PRK10512 129 VKAVLreyGFAEAKLFVTAATEGRGIDALREHLLQL-PEREHAAQHRFR-LAIDRAFTvKGAGLVVTGTALSGEVKVGD 205
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
101-277 |
5.10e-08 |
|
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206682 [Multi-domain] Cd Length: 174 Bit Score: 53.21 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 101 GKSTLADTLLSKTKTVAArDMEAQLLDSMDIERERgitiklnsarmnyvanDGETYVLnlIDTPG---------HVDFsY 171
Cdd:cd01895 14 GKSSLLNALLGEERVIVS-DIAGTTRDSIDVPFEY----------------DGQKYTL--IDTAGirkkgkvteGIEK-Y 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 172 EVSRSLAACEGA---LLVVDASQGVEAQ--TVANvyLALENDLEIITVLNKIDLPGAEPERvkvrsihwfpYDRVgVREI 246
Cdd:cd01895 74 SVLRTLKAIERAdvvLLVLDASEGITEQdlRIAG--LILEEGKALIIVVNKWDLVEKDEKT----------MKEF-EKEL 140
|
170 180 190
....*....|....*....|....*....|..
gi 317411685 247 EDVLG-LDTEDAVVASAKANIGMEDILENIVK 277
Cdd:cd01895 141 RRKLPfLDYAPIVFISALTGQGVDKLFDAIKE 172
|
|
| MnmE_helical |
pfam12631 |
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ... |
156-290 |
5.66e-07 |
|
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An N-terminal domain, a helical domain and a GTPase domain which is nested within the helical domain. This family represents the helical domain.
Pssm-ID: 463649 [Multi-domain] Cd Length: 326 Bit Score: 52.10 E-value: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 156 YVLNLIDTPG------HVdfsyE---VSRSLAACEGA---LLVVDASQGVEAQTvANVYLALENDLEIITVLNKIDLPGA 223
Cdd:pfam12631 142 IPLRLIDTAGiretddEV----EkigIERAREAIEEAdlvLLVLDASRPLDEED-LEILELLKDKKPIIVVLNKSDLLGE 216
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 317411685 224 EPERVKvrsihwfpydrvgvreiedvlgLDTEDAVVASAKANIGMEDILENIVKMIPPPPDTGDEPL 290
Cdd:pfam12631 217 IDELEE----------------------LKGKPVLAISAKTGEGLDELEEAIKELFLAGEIASDGPI 261
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
101-277 |
1.22e-06 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 51.59 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 101 GKSTLADTLLSKTKTVAArDMEAQLLDSMDIERERgitiklnsarmnyvanDGETYVLnlIDTPG-----HVDFS---YE 172
Cdd:PRK00093 185 GKSSLINALLGEERVIVS-DIAGTTRDSIDTPFER----------------DGQKYTL--IDTAGirrkgKVTEGvekYS 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 173 VSRSLAACEGA---LLVVDASQGVEAQ--TVANvyLALENDLEIITVLNKIDL-PGAEPERVKvrsihwfpydrvgvREI 246
Cdd:PRK00093 246 VIRTLKAIERAdvvLLVIDATEGITEQdlRIAG--LALEAGRALVIVVNKWDLvDEKTMEEFK--------------KEL 309
|
170 180 190
....*....|....*....|....*....|..
gi 317411685 247 EDVLG-LDTEDAVVASAKANIGMEDILENIVK 277
Cdd:PRK00093 310 RRRLPfLDYAPIVFISALTGQGVDKLLEAIDE 341
|
|
| EFG_mtEFG_C |
cd03713 |
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational ... |
500-577 |
1.31e-06 |
|
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational elongation factor (EF) EF-G. Included in this group is the C-terminus of mitochondrial Elongation factor G1 (mtEFG1) and G2 (mtEFG2) proteins. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. In bacteria this translocation step is catalyzed by EF-G_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. No clear phenotype has been found for mutants in the yeast homologue of mtEFG2, MEF2.
Pssm-ID: 239683 [Multi-domain] Cd Length: 78 Bit Score: 46.37 E-value: 1.31e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 317411685 500 EPFVKLEMFAPSDYVGSLMELAQQRRGEFIDMTyLSESRTCLKYDIPLGEVVtDFFDELKSRSKGYASMEYSFNEYRK 577
Cdd:cd03713 1 EPIMKVEVTVPEEYMGDVIGDLSSRRGQILGTE-SRGGWKVIKAEVPLAEMF-GYSTDLRSLTQGRGSFTMEFSHYEE 76
|
|
| EFG_mtEFG_II |
cd04088 |
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation ... |
290-374 |
3.68e-06 |
|
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: 45.21 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 290 LRALIFDSYFDPYRGVVVIFRVVDGNLGVGDAVKFMNTGKSYTIDEIGIMRPQK-VPVNRLSAGEVGyMIANIKsvaDAR 368
Cdd:cd04088 1 FSALVFKTMADPFVGKLTFFRVYSGTLKSGSTVYNSTKGKKERVGRLLRMHGKKrEEVEELGAGDIG-AVVGLK---DTR 76
|
....*.
gi 317411685 369 VGDTIT 374
Cdd:cd04088 77 TGDTLC 82
|
|
| HflX |
COG2262 |
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ... |
184-298 |
5.36e-06 |
|
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441863 [Multi-domain] Cd Length: 419 Bit Score: 49.31 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 184 LLVVDAS-QGVEAQ--TVANVylaLE----NDLEIITVLNKIDLpgAEPERVkvrsihwfpydrvgvreieDVLGLDTED 256
Cdd:COG2262 283 LHVVDASdPDFEEQieTVNEV---LEelgaDDKPIILVFNKIDL--LDDEEL-------------------ERLRAGYPD 338
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 317411685 257 AVVASAKANIGMEDILENIVKMIPP---------PPDTGDepLRALIFDSY 298
Cdd:COG2262 339 AVFISAKTGEGIDELLEAIEERLPEdrvevelllPYSDGD--LVAWLHEHG 387
|
|
| MnmE |
COG0486 |
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
158-279 |
6.56e-06 |
|
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: 49.29 E-value: 6.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 158 LNLIDTPG------HVdfsyE---VSRSLAACEGA---LLVVDASQGVEAQTVAnvYLALENDLEIITVLNKIDLPGAEP 225
Cdd:COG0486 263 VRLIDTAGlretedEV----EkigIERAREAIEEAdlvLLLLDASEPLTEEDEE--ILEKLKDKPVIVVLNKIDLPSEAD 336
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 317411685 226 ERVKvrsiHWFPYDRVGVreiedvlgldtedavvaSAKANIGMEDILENIVKMI 279
Cdd:COG0486 337 GELK----SLPGEPVIAI-----------------SAKTGEGIDELKEAILELV 369
|
|
| mtEFG2_II_like |
cd04092 |
Domain II of mitochondrial elongation factor G2-like proteins found in eukaryotes; Eukaryotic ... |
292-375 |
8.24e-06 |
|
Domain II of mitochondrial elongation factor G2-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. No clear phenotype has been found for mutants in the yeast homolog of mtEFG2, MEF2. There are two forms of mtEFG present in mammals (designated mtEFG1s and mtEFG2s); mtEFG1s are not present in this group.
Pssm-ID: 293909 [Multi-domain] Cd Length: 83 Bit Score: 44.23 E-value: 8.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 292 ALIFDSYFDPYRGVVVIFRVVDGNLGVGDAVKFMNTGKSYTIDEIGIMRP-QKVPVNRLSAGEVGyMIANIKSVadaRVG 370
Cdd:cd04092 3 ALAFKVIHDPQRGPLVFVRVYSGTLKAGSNVYNTTTGKKERISRLLKMHAdQTEEVDSLSAGNIG-VITGLKVT---STG 78
|
....*
gi 317411685 371 DTITT 375
Cdd:cd04092 79 DTLVS 83
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
98-220 |
9.90e-06 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 48.76 E-value: 9.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 98 IDHGKSTLADTLLSKTKTV-----AA--RDME-----------AQLLDSMDIERERGITIKLnSARmnYVANDGETYVln 159
Cdd:PRK05124 36 VDDGKSTLIGRLLHDTKQIyedqlASlhNDSKrhgtqgekldlALLVDGLQAEREQGITIDV-AYR--YFSTEKRKFI-- 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 317411685 160 LIDTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLAleNDLEI---ITVLNKIDL 220
Cdd:PRK05124 111 IADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIA--TLLGIkhlVVAVNKMDL 172
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
98-227 |
9.92e-06 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 48.77 E-value: 9.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 98 IDHGKSTLADTLLSKTKTVAARDME------------------AQLLDSMDIERERGITIKLnSARmnYVANDGETYVln 159
Cdd:PRK05506 33 VDDGKSTLIGRLLYDSKMIFEDQLAalerdskkvgtqgdeidlALLVDGLAAEREQGITIDV-AYR--YFATPKRKFI-- 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 317411685 160 LIDTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLA-LENDLEIITVLNKIDLPGAEPER 227
Cdd:PRK05506 108 VADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIAsLLGIRHVVLAVNKMDLVDYDQEV 176
|
|
| trmE |
PRK05291 |
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; |
158-279 |
1.71e-05 |
|
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
Pssm-ID: 235392 [Multi-domain] Cd Length: 449 Bit Score: 47.80 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 158 LNLIDTPG------HVdfsyE---VSRSLAACEGA---LLVVDASQGVEAQTVANvyLALENDLEIITVLNKIDLPGAEP 225
Cdd:PRK05291 265 LRLIDTAGiretddEV----EkigIERSREAIEEAdlvLLVLDASEPLTEEDDEI--LEELKDKPVIVVLNKADLTGEID 338
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 317411685 226 ErvkvrsIHWFPYDRVGVreiedvlgldtedavvaSAKANIGMEDILENIVKMI 279
Cdd:PRK05291 339 L------EEENGKPVIRI-----------------SAKTGEGIDELREAIKELA 369
|
|
| Tet_C |
cd03711 |
Tet_C: C-terminus of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology ... |
500-576 |
2.15e-05 |
|
Tet_C: C-terminus of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology to the C terminal domains of the elongation factors EF-G and EF-2. Tet(M) and Tet(O) catalyze the release of tetracycline (Tc) from the ribosome in a GTP-dependent manner thereby mediating Tc resistance. Tcs are broad-spectrum antibiotics. Typical Tcs bind to the ribosome and inhibit the elongation phase of protein synthesis, by inhibiting the occupation of site A by aminoacyl-tRNA.
Pssm-ID: 239682 [Multi-domain] Cd Length: 78 Bit Score: 43.00 E-value: 2.15e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 317411685 500 EPFVKLEMFAPSDYVGSLMELAQQRRGEFIDmTYLSESRTCLKYDIPLGEvVTDFFDELKSRSKGYASMEYSFNEYR 576
Cdd:cd03711 1 EPYLRFELEVPQDALGRAMSDLAKMGATFED-PQIKGDEVTLEGTIPVAT-SQDYQSELPSYTHGEGVLETEFKGYR 75
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
101-217 |
2.24e-05 |
|
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: 44.15 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 101 GKSTLADTLLSKTKTVAardmeaqlldsmDIErerGITIKLNSARMNYvanDGETYVLnlIDTPGHVDFSYE---VSRSL 177
Cdd:pfam01926 11 GKSTLINALTGAKAIVS------------DYP---GTTRDPNEGRLEL---KGKQIIL--VDTPGLIEGASEgegLGRAF 70
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 317411685 178 AA---CEGALLVVDASQGVEAQTVANVYLALENDLEIITVLNK 217
Cdd:pfam01926 71 LAiieADLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
160-294 |
8.36e-05 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 44.98 E-value: 8.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 160 LIDTPG-H----------VDFsyeVSRSLAACEGALLVVDASQGV--EAQTVANVyLAlENDLEIITVLNKIDLpgAEPE 226
Cdd:COG1159 55 FVDTPGiHkpkrklgrrmNKA---AWSALEDVDVILFVVDATEKIgeGDEFILEL-LK-KLKTPVILVINKIDL--VKKE 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 317411685 227 RVKVRsihwfpydrvgvreIEDVLGLDTEDAVVA-SAKANIGMEDILENIVKMIPP-----PPD--TgDEPLRALI 294
Cdd:COG1159 128 ELLPL--------------LAEYSELLDFAEIVPiSALKGDNVDELLDEIAKLLPEgppyyPEDqiT-DRPERFLA 188
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
290-385 |
8.90e-05 |
|
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: 41.79 E-value: 8.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 290 LRALIFDSYFDPYRGVVVIFRVVDGNLGVGDAVKFMNTGKSYTIDEI----GIMRPQKVPVNrlsAGEVGYMIAnIKSVA 365
Cdd:cd03691 1 FQMLVTTLDYDDYLGRIAIGRIFSGTVKVGQQVTVVDEDGKIEKGRVtklfGFEGLERVEVE---EAEAGDIVA-IAGLE 76
|
90 100
....*....|....*....|
gi 317411685 366 DARVGDTITTTKDssTEPLP 385
Cdd:cd03691 77 DITIGDTICDPEV--PEPLP 94
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
173-279 |
1.06e-04 |
|
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.
Pssm-ID: 206727 [Multi-domain] Cd Length: 159 Bit Score: 43.25 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 173 VSRSLAACEGA---LLVVDASQGVEAQTVANvyLALENDLEIITVLNKIDLPGAEPERVKVrsihwfpydrvgvrEIEDV 249
Cdd:cd04164 73 IERAREAIEEAdlvLLVVDASEGLDEEDLEI--LELPAKKPVIVVLNKSDLLSDAEGISEL--------------NGKPI 136
|
90 100 110
....*....|....*....|....*....|
gi 317411685 250 LGLdtedavvaSAKANIGMEDILENIVKMI 279
Cdd:cd04164 137 IAI--------SAKTGEGIDELKEALLELA 158
|
|
| EFG_C |
smart00838 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
500-571 |
1.08e-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: 41.34 E-value: 1.08e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 317411685 500 EPFVKLEMFAPSDYVGSLMELAQQRRGEFIDMTYLSESRTcLKYDIPLGEVVtDFFDELKSRSKGYA--SMEYS 571
Cdd:smart00838 3 EPIMKVEVTVPEEYMGDVIGDLNSRRGKIEGMEQRGGAQV-IKAKVPLSEMF-GYATDLRSATQGRAtwSMEFS 74
|
|
| HflX |
cd01878 |
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
184-279 |
3.49e-04 |
|
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment N-terminal of the GTPase domain characterizes the HflX subfamily. The E. coli HflX has been implicated in the control of the lambda cII repressor proteolysis, but the actual biological functions of these GTPases remain unclear. HflX is widespread, but not universally represented in all three superkingdoms.
Pssm-ID: 206666 [Multi-domain] Cd Length: 204 Bit Score: 42.45 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 184 LLVVDASQGVEAQTVANVYLALE----NDLEIITVLNKIDLpgAEPERVKVRSIHWFPydrvgvreiedvlgldteDAVV 259
Cdd:cd01878 125 LHVVDASDPDREEQIETVEEVLKelgaDDIPIILVLNKIDL--LDDEELEERLRAGRP------------------DAVF 184
|
90 100
....*....|....*....|
gi 317411685 260 ASAKANIGMEDILENIVKMI 279
Cdd:cd01878 185 ISAKTGEGLDLLKEAIEELL 204
|
|
| EFG_III |
pfam14492 |
Elongation Factor G, domain III; This domain is found in Elongation Factor G. It shares a ... |
392-464 |
4.00e-04 |
|
Elongation Factor G, domain III; This domain is found in Elongation Factor G. It shares a similar structure with domain V (pfam00679). Structural studies in drosophila indicate this is domain 3.
Pssm-ID: 464188 [Multi-domain] Cd Length: 75 Bit Score: 39.39 E-value: 4.00e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 317411685 392 PMVYCGLFPTDSDQYEDLRVALGKLQINDAALRYE--PE--QS--SAMGfgfrcgflgLLHMEIVQERLEREYDLGLIT 464
Cdd:pfam14492 4 PVISVAIEPKTKGDEDKLSKALNRLLEEDPTLRVErdEEtgETilSGMG---------ELHLEIVVDRLKRKYGVEVEL 73
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
93-225 |
6.63e-04 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 42.86 E-value: 6.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 93 SIIAHIDHGKSTLADTLlsKTKTVAARD-------MEAQLLDSMDIERERGITIKLNSARMNYVAndgetyvLNLIDTPG 165
Cdd:PRK04004 10 VVLGHVDHGKTTLLDKI--RGTAVAAKEaggitqhIGATEVPIDVIEKIAGPLKKPLPIKLKIPG-------LLFIDTPG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 317411685 166 HVDFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDLEIITVLNKID-LPGAEP 225
Cdd:PRK04004 81 HEAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVAANKIDrIPGWKS 141
|
|
| mtEFG1_C |
cd04097 |
mtEFG1_C: C-terminus of mitochondrial Elongation factor G1 (mtEFG1)-like proteins found in ... |
500-571 |
7.78e-04 |
|
mtEFG1_C: C-terminus of mitochondrial Elongation factor G1 (mtEFG1)-like proteins found in eukaryotes. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. Eukaryotic EF-2 operates in the cytosolic protein synthesis machinery of eukaryotes, EF-Gs in protein synthesis in bacteria. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. There are two forms of mtEFG present in mammals (designated mtEFG1s and mtEFG2s) mtEFG2s are not present in this group.
Pssm-ID: 239764 [Multi-domain] Cd Length: 78 Bit Score: 38.84 E-value: 7.78e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 317411685 500 EPFVKLEMFAPSDYVGSLMELAQQRRGEFIDmTYLSESRTCLKYDIPLGEVVTdFFDELKS--RSKGYASMEYS 571
Cdd:cd04097 1 EPIMKVEVTAPTEFQGNVIGLLNKRKGTIVD-TDTGEDEFTLEAEVPLNDMFG-YSTELRSmtQGKGEFSMEFS 72
|
|
| EFG_III |
cd16262 |
Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial ... |
392-467 |
8.72e-04 |
|
Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial Elongation factor G (EF-G), and mitochondrial Elongation factor G1 (mtEFG1) and G2 (mtEFG2), which play an important role during peptide synthesis and tRNA site changes. In bacteria, this translocation step is catalyzed by EF-G_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. mtEFG1 and mtEFG2 show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects, and a tendency to lose mitochondrial DNA. No clear phenotype has been found for mutants of the yeast homolog of mtEFG2, MEF2.
Pssm-ID: 293919 [Multi-domain] Cd Length: 76 Bit Score: 38.59 E-value: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 392 PMVYCGLFPTDSDQYEDLRVALGKLQINDAALRYE--PEQS----SAMGfgfrcgflgLLHMEIVQERLEREYDLGLITT 465
Cdd:cd16262 3 PVISLAIEPKTKADEDKLSKALARLAEEDPTLRVSrdEETGqtilSGMG---------ELHLEIIVERLKREYGVEVEVG 73
|
..
gi 317411685 466 AP 467
Cdd:cd16262 74 KP 75
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
160-294 |
1.63e-03 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 41.19 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317411685 160 LIDTPG-H----------VDFsyeVSRSLAACEGALLVVDASQGV--EAQTVANvyLALENDLEIITVLNKIDLPGAEPE 226
Cdd:PRK00089 57 FVDTPGiHkpkralnramNKA---AWSSLKDVDLVLFVVDADEKIgpGDEFILE--KLKKVKTPVILVLNKIDLVKDKEE 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 317411685 227 RVKVrsihwfpydrvgvreIEDVLGLDTEDAVVA-SAKANIGMEDILENIVKMIPP-----PPDT-GDEPLRALI 294
Cdd:PRK00089 132 LLPL---------------LEELSELMDFAEIVPiSALKGDNVDELLDVIAKYLPEgppyyPEDQiTDRPERFLA 191
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
158-222 |
3.08e-03 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 41.02 E-value: 3.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 317411685 158 LNLIDTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDLEIITVLNKIDL-PG 222
Cdd:PRK14845 528 LLFIDTPGHEAFTSLRKRGGSLADLAVLVVDINEGFKPQTIEAINILRQYKTPFVVAANKIDLiPG 593
|
|
| |
