|
Name |
Accession |
Description |
Interval |
E-value |
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
9-605 |
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: 1276.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 9 RQENIRNFSIIAHIDHGKSTLADRILENTKSVETREMQSQLLDSMDLERERGITIKLNAVRLKYEAKDGKNYIFHLIDTP 88
Cdd:COG0481 2 DQKNIRNFSIIAHIDHGKSTLADRLLELTGTLSEREMKEQVLDSMDLERERGITIKAQAVRLNYKAKDGETYQLNLIDTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 89 GHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLPAADPERVKQEIEDVIGLDQDDVV 168
Cdd:COG0481 82 GHVDFSYEVSRSLAACEGALLVVDASQGVEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKQEIEDIIGIDASDAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 169 LASAKSNIGIEEILEKIVEVVPPPEGDPSEPLKALIFDSEYDAYRGVISSIRIMDGVVKAGDKIKMMATGKEFEVTEVGI 248
Cdd:COG0481 162 LVSAKTGIGIEEILEAIVERIPPPKGDPDAPLQALIFDSWYDSYRGVVVYVRVFDGTLKKGDKIKMMSTGKEYEVDEVGV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 249 NTPKQLPVEELTVGDVGYIIASIKNVDDSRVGDTITHAERPAAQPLKGYKKMNPMVFCGLFPIDNKKYNDLREALEKLQL 328
Cdd:COG0481 242 FTPKMTPVDELSAGEVGYIIAGIKDVRDARVGDTITLAKNPAAEPLPGFKEVKPMVFAGLYPVDSDDYEDLRDALEKLQL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 329 NDSSLEFEPETSQALGFGFRTGFLGMLHMEIIQERIEREFGIELIATAPSVIYECILKNGEKKIVDNPAQMPERDQIDEI 408
Cdd:COG0481 322 NDASLTYEPETSAALGFGFRCGFLGLLHMEIIQERLEREFDLDLITTAPSVVYEVTLTDGEVIEVDNPSDLPDPGKIEEI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 409 YEPYVRATMMVPNDYVGAVMELCQRKRGQFINMDYLDDIRVNIIYEIPLSEVVFDFFDQLKSNTKGYASFDYELIGYKES 488
Cdd:COG0481 402 EEPIVKATIITPSEYVGAVMELCQEKRGVQKNMEYLGENRVELTYELPLAEIVFDFFDRLKSITRGYASLDYEFIGYRES 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 489 DLVKMDILLNGEKVDALSFIVHKEFAYERGKALVERLKTLIPRQQFEVPVQAAVGHKIIARTNIKSMGKNVLAKCYGGDI 568
Cdd:COG0481 482 DLVKLDILINGEPVDALSFIVHRDKAYSRGRALVEKLKELIPRQQFEVPIQAAIGGKIIARETIKALRKDVLAKCYGGDI 561
|
570 580 590
....*....|....*....|....*....|....*..
gi 1080759641 569 SRKRKLLEKQKAGKAKMKAVGNVEIPQDAFLAVLKMD 605
Cdd:COG0481 562 SRKRKLLEKQKEGKKRMKQVGNVEIPQEAFLAVLKVD 598
|
|
| lepA |
TIGR01393 |
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a ... |
11-605 |
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: 1101.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 11 ENIRNFSIIAHIDHGKSTLADRILENTKSVETREMQSQLLDSMDLERERGITIKLNAVRLKYEAKDGKNYIFHLIDTPGH 90
Cdd:TIGR01393 1 KNIRNFSIIAHIDHGKSTLADRLLEYTGAISEREMREQVLDSMDLERERGITIKAQAVRLNYKAKDGETYVLNLIDTPGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 91 VDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLPAADPERVKQEIEDVIGLDQDDVVLA 170
Cdd:TIGR01393 81 VDFSYEVSRSLAACEGALLLVDAAQGIEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKKEIEEVIGLDASEAILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 171 SAKSNIGIEEILEKIVEVVPPPEGDPSEPLKALIFDSEYDAYRGVISSIRIMDGVVKAGDKIKMMATGKEFEVTEVGINT 250
Cdd:TIGR01393 161 SAKTGIGIEEILEAIVKRVPPPKGDPDAPLKALIFDSHYDNYRGVVALVRVFEGTIKPGDKIRFMSTGKEYEVDEVGVFT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 251 PKQLPVEELTVGDVGYIIASIKNVDDSRVGDTITHAERPAAQPLKGYKKMNPMVFCGLFPIDNKKYNDLREALEKLQLND 330
Cdd:TIGR01393 241 PKLTKTDELSAGEVGYIIAGIKDVSDVRVGDTITHVKNPAKEPLPGFKEVKPMVFAGLYPIDTEDYEDLRDALEKLKLND 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 331 SSLEFEPETSQALGFGFRTGFLGMLHMEIIQERIEREFGIELIATAPSVIYECILKNGEKKIVDNPAQMPERDQIDEIYE 410
Cdd:TIGR01393 321 ASLTYEPESSPALGFGFRCGFLGLLHMEIIQERLEREFNLDLITTAPSVIYRVYLTNGEVIEVDNPSDLPDPGKIEHVEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 411 PYVRATMMVPNDYVGAVMELCQRKRGQFINMDYLDDIRVNIIYEIPLSEVVFDFFDQLKSNTKGYASFDYELIGYKESDL 490
Cdd:TIGR01393 401 PYVKATIITPTEYLGPIMTLCQEKRGVQTNMEYLDPNRVELIYEMPLAEIVYDFFDKLKSISRGYASFDYELIGYRPSDL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 491 VKMDILLNGEKVDALSFIVHKEFAYERGKALVERLKTLIPRQQFEVPVQAAVGHKIIARTNIKSMGKNVLAKCYGGDISR 570
Cdd:TIGR01393 481 VKLDILINGEPVDALSFIVHRDKAYSRGREICEKLKELIPRQQFEIPIQAAIGGKIIARETIKALRKDVTAKCYGGDITR 560
|
570 580 590
....*....|....*....|....*....|....*
gi 1080759641 571 KRKLLEKQKAGKAKMKAVGNVEIPQDAFLAVLKMD 605
Cdd:TIGR01393 561 KRKLLEKQKEGKKRMKQIGKVEVPQEAFLAVLKVD 595
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
14-192 |
1.97e-125 |
|
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: 366.86 E-value: 1.97e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 14 RNFSIIAHIDHGKSTLADRILENTKSVETREMQSQLLDSMDLERERGITIKLNAVRLKYEAKDGKNYIFHLIDTPGHVDF 93
Cdd:cd01890 1 RNFSIIAHIDHGKSTLADRLLELTGTVSEREMKEQVLDSMDLERERGITIKAQAVRLFYKAKDGEEYLLNLIDTPGHVDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 94 TYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLPAADPERVKQEIEDVIGLDQDDVVLASAK 173
Cdd:cd01890 81 SYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVKQEIEDVLGLDASEAILVSAK 160
|
170
....*....|....*....
gi 1080759641 174 SNIGIEEILEKIVEVVPPP 192
Cdd:cd01890 161 TGLGVEDLLEAIVERIPPP 179
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
8-456 |
5.65e-72 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 242.62 E-value: 5.65e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 8 NRQENIRNFSIIAHIDHGKSTLADRILENTKSVETRE-MQSQLLDSMDLERERGITI--KLNAVRlkYeakdgKNYIFHL 84
Cdd:COG1217 1 MMREDIRNIAIIAHVDHGKTTLVDALLKQSGTFRENQeVAERVMDSNDLERERGITIlaKNTAVR--Y-----KGVKINI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 85 IDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQT---LANvylALDNDLELLPVVNKIDLPAADPERVKQEIEDV-I 160
Cdd:COG1217 74 VDTPGHADFGGEVERVLSMVDGVLLLVDAFEGPMPQTrfvLKK---ALELGLKPIVVINKIDRPDARPDEVVDEVFDLfI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 161 GLDQDD------VVLASAKSNI----------GIEEILEKIVEVVPPPEGDPSEPLKALIFDSEYDAYRGVISSIRIMDG 224
Cdd:COG1217 151 ELGATDeqldfpVVYASARNGWasldlddpgeDLTPLFDTILEHVPAPEVDPDGPLQMLVTNLDYSDYVGRIAIGRIFRG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 225 VVKAGDKIKMMATG---KEFEVTEV----GIntpKQLPVEELTVGDvgyIIAsIKNVDDSRVGDTITHAERPaaQPLKGY 297
Cdd:COG1217 231 TIKKGQQVALIKRDgkvEKGKITKLfgfeGL---ERVEVEEAEAGD---IVA-IAGIEDINIGDTICDPENP--EALPPI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 298 K------KMNPMV----FCGlfpidnK--KY---NDLREALEKLQLNDSSLEFEpETSQALGF---GfRtgflGMLHMEI 359
Cdd:COG1217 302 KideptlSMTFSVndspFAG------RegKFvtsRQIRERLEKELETNVALRVE-ETDSPDAFkvsG-R----GELHLSI 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 360 IQERIEREfGIELIATAPSVIYECIlkNGEKkivdnpaqmperdqideiYEPYVRATMMVPNDYVGAVMELCQRKRGQFI 439
Cdd:COG1217 370 LIETMRRE-GYELQVSRPEVIFKEI--DGKK------------------LEPIEELTIDVPEEYSGAVIEKLGQRKGEMT 428
|
490
....*....|....*..
gi 1080759641 440 NMDYLDDIRVNIIYEIP 456
Cdd:COG1217 429 NMEPDGGGRVRLEFLIP 445
|
|
| LepA_C |
pfam06421 |
GTP-binding protein LepA C-terminus; This family consists of the C-terminal region of several ... |
497-603 |
5.19e-70 |
|
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: 221.12 E-value: 5.19e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 497 LNGEKVDALSFIVHKEFAYERGKALVERLKTLIPRQQFEVPVQAAVGHKIIARTNIKSMGKNVLAKCYGGDISRKRKLLE 576
Cdd:pfam06421 1 INGEPVDALSFIVHRSKAYRRGRALVEKLKELIPRQQFEVPIQAAIGGKIIARETIKALRKDVTAKCYGGDISRKKKLLE 80
|
90 100
....*....|....*....|....*..
gi 1080759641 577 KQKAGKAKMKAVGNVEIPQDAFLAVLK 603
Cdd:pfam06421 81 KQKEGKKRMKQIGNVEIPQEAFLAVLK 107
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
11-191 |
6.58e-68 |
|
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.
Pssm-ID: 425418 [Multi-domain] Cd Length: 187 Bit Score: 218.93 E-value: 6.58e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 11 ENIRNFSIIAHIDHGKSTLADRILENTKSVETREMQSQ----LLDSMDLERERGITIKLNAVRLkyeakDGKNYIFHLID 86
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGegeaGLDNLPEERERGITIKSAAVSF-----ETKDYLINLID 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 87 TPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLPA-ADPERVKQEIEDVIGLDQD 165
Cdd:pfam00009 76 TPGHVDFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDgAELEEVVEEVSRELLEKYG 155
|
170 180 190
....*....|....*....|....*....|..
gi 1080759641 166 D------VVLASAKSNIGIEEILEKIVEVVPP 191
Cdd:pfam00009 156 EdgefvpVVPGSALKGEGVQTLLDALDEYLPS 187
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
11-487 |
1.90e-58 |
|
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: 207.98 E-value: 1.90e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 11 ENIRNFSIIAHIDHGKSTLADRILENTK------SVE--TREMqsqllDSMDLERERGITIKLNAVRLKYeakdgKNYIF 82
Cdd:COG0480 7 EKIRNIGIVAHIDAGKTTLTERILFYTGaihrigEVHdgNTVM-----DWMPEEQERGITITSAATTCEW-----KGHKI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 83 HLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLPAADPERVKQEIED---- 158
Cdd:COG0480 77 NIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQLKErlga 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 159 -----------------VIGL-----------------------------------------DQDD-------------- 166
Cdd:COG0480 157 npvplqlpigaeddfkgVIDLvtmkayvyddelgakyeeeeipaelkeeaeeareelieavaETDDelmekylegeelte 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 167 ------------------VVLASAKSNIGIEEILEKIVEVVPPP-------------------EGDPSEPLKALIFDSEY 209
Cdd:COG0480 237 eeikaglrkatlagkivpVLCGSAFKNKGVQPLLDAVVDYLPSPldvpaikgvdpdtgeeverKPDDDEPFSALVFKTMT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 210 DAYRGVISSIRIMDGVVKAGDKIKMMATGKEFEVTevGINTP---KQLPVEELTVGDvgyIIASIKnVDDSRVGDTITHA 286
Cdd:COG0480 317 DPFVGKLSFFRVYSGTLKSGSTVYNSTKGKKERIG--RLLRMhgnKREEVDEAGAGD---IVAVVK-LKDTTTGDTLCDE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 287 ERPAaqPLKGYKKMNPMVFCGLFPidnKKYND---LREALEKLQLNDSSLEFE--PETSQALGFGfrtgfLGMLHMEIIQ 361
Cdd:COG0480 391 DHPI--VLEPIEFPEPVISVAIEP---KTKADedkLSTALAKLAEEDPTFRVEtdEETGQTIISG-----MGELHLEIIV 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 362 ERIEREFGIELIATAPSVIY-ECILKNGE-----KK-------------------------IVDN------PAQ-MP--E 401
Cdd:COG0480 461 DRLKREFGVEVNVGKPQVAYrETIRKKAEaegkhKKqsgghgqygdvwieieplprgegfeFVDKivggviPKEyIPavE 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 402 ---RDQIDE------------------------------------------------IYEPYVRATMMVPNDYVGAVMEL 430
Cdd:COG0480 541 kgiREAMEKgvlagypvvdvkvtlydgsyhpvdssemafkiaasmafkeaakkakpvLLEPIMKVEVTVPEEYMGDVMGD 620
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1080759641 431 CQRKRGQFINMDYLDDIRVnIIYEIPLSEvVFDFFDQLKSNTKGYASFDYELIGYKE 487
Cdd:COG0480 621 LNSRRGRILGMESRGGAQV-IKAEVPLAE-MFGYATDLRSLTQGRGSFTMEFSHYEE 675
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
8-487 |
6.69e-57 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 203.64 E-value: 6.69e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 8 NRQENIRNFSIIAHIDHGKSTLADRILENTK------SVE--TREMqsqllDSMDLERERGITIKLNAVRLKYeakdgKN 79
Cdd:PRK13351 3 MPLMQIRNIGILAHIDAGKTTLTERILFYTGkihkmgEVEdgTTVT-----DWMPQEQERGITIESAATSCDW-----DN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 80 YIFHLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLPAADPERVKQEIEDV 159
Cdd:PRK13351 73 HRINLIDTPGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLFKVLEDIEER 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 160 IG---------------------------------------------------------------LDQDD---------- 166
Cdd:PRK13351 153 FGkrplplqlpigsedgfegvvdlitepelhfsegdggstveegpipeelleeveearekliealAEFDDellelylege 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 167 ----------------------VVLASAKSNIGIEEILEKIVE------VVPPPEG------------DPSEPLKALIFD 206
Cdd:PRK13351 233 elsaeqlraplregtrsghlvpVLFGSALKNIGIEPLLDAVVDylpsplEVPPPRGskdngkpvkvdpDPEKPLLALVFK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 207 SEYDAYRGVISSIRIMDGVVKAGDKIKMMATGKEFEVTE-VGINTPKQLPVEELTVGDvgyIIASIKnVDDSRVGDTITH 285
Cdd:PRK13351 313 VQYDPYAGKLTYLRVYSGTLRAGSQLYNGTGGKREKVGRlFRLQGNKREEVDRAKAGD---IVAVAG-LKELETGDTLHD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 286 AERPAAqpLKGYKKMNPMVFCGLFPIDNKKYNDLREALEKLQLNDSSLEFE--PETSQALGFGfrtgfLGMLHMEIIQER 363
Cdd:PRK13351 389 SADPVL--LELLTFPEPVVSLAVEPERRGDEQKLAEALEKLVWEDPSLRVEedEETGQTILSG-----MGELHLEVALER 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 364 IEREFGIELIATAPSVIY-ECI-----------------------------LKNGEKKIVDN-------PAQMPE----- 401
Cdd:PRK13351 462 LRREFKLEVNTGKPQVAYrETIrkmaegvyrhkkqfggkgqfgevhlrvepLERGAGFIFVSkvvggaiPEELIPavekg 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 402 -RDQIDE------------------------------------------------IYEPYVRATMMVPNDYVGAVMELCQ 432
Cdd:PRK13351 542 iREALASgplagypvtdlrvtvldgkyhpvdssesafkaaarkafleafrkanpvLLEPIMELEITVPTEHVGDVLGDLS 621
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1080759641 433 RKRGQFINMDYLDDIRVNIIYEIPLSEvVFDFFDQLKSNTKGYASFDYELIGYKE 487
Cdd:PRK13351 622 QRRGRIEGTEPRGDGEVLVKAEAPLAE-LFGYATRLRSMTKGRGSFTMEFSHFDP 675
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
19-487 |
2.09e-56 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 201.89 E-value: 2.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 19 IAHIDHGKSTLADRILENTKSVETR---EMQSQLLDSMDLERERGITIKLNAVRLKYeakdgKNYIFHLIDTPGHVDFTY 95
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRIgevEDGTTTMDFMPEERERGISITSAATTCEW-----KGHKINLIDTPGHVDFTG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 96 EVSRSLAACEGAILVVDAAQGIEAQTLAnvYLALDNDLEL--LPVVNKIDLPAADPERVKQEIED--------------- 158
Cdd:PRK12740 76 EVERALRVLDGAVVVVCAVGGVEPQTET--VWRQAEKYGVprIIFVNKMDRAGADFFRVLAQLQEklgapvvplqlpige 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 159 ------VIGL---------------------------------------DQDD--------------------------- 166
Cdd:PRK12740 154 gddftgVVDLlsmkayrydeggpseeieipaelldraeeareellealaEFDDelmekylegeelseeeikaglrkatla 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 167 -----VVLASAKSNIGIEEILEKIVEVVPPP-----------------EGDPSEPLKALIFDSEYDAYRGVISSIRIMDG 224
Cdd:PRK12740 234 geivpVFCGSALKNKGVQRLLDAVVDYLPSPlevppvdgedgeegaelAPDPDGPLVALVFKTMDDPFVGKLSLVRVYSG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 225 VVKAGDKIKMMATGKEFEVTevGINTP---KQLPVEELTVGDvgyIIASIKnVDDSRVGDTITHAERPAAqplkgykkMN 301
Cdd:PRK12740 314 TLKKGDTLYNSGTGKKERVG--RLYRMhgkQREEVDEAVAGD---IVAVAK-LKDAATGDTLCDKGDPIL--------LE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 302 PMVFC------GLFPIDNKKYNDLREALEKLQLNDSSLEFE--PETSQALGFGfrtgfLGMLHMEIIQERIEREFGIELI 373
Cdd:PRK12740 380 PMEFPepvislAIEPKDKGDEEKLSEALGKLAEEDPTLRVErdEETGQTILSG-----MGELHLDVALERLKREYGVEVE 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 374 ATAPSVIY-ECILKNGE-----KK-------------------------IVDN------PAQ-MPE-----RDQIDE--- 407
Cdd:PRK12740 455 TGPPQVPYrETIRKKAEghgrhKKqsgghgqfgdvwleveplprgegfeFVDKvvggavPRQyIPAvekgvREALEKgvl 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 408 ---------------------------------------------IYEPYVRATMMVPNDYVGAVMELCQRKRGQFINMD 442
Cdd:PRK12740 535 agypvvdvkvtltdgsyhsvdssemafkiaarlafrealpkakpvLLEPIMKVEVSVPEEFVGDVIGDLSSRRGRILGME 614
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1080759641 443 YLDDIRVnIIYEIPLSEvVFDFFDQLKSNTKGYASFDYELIGYKE 487
Cdd:PRK12740 615 SRGGGDV-VRAEVPLAE-MFGYATDLRSLTQGRGSFSMEFSHYEE 657
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
15-192 |
2.08e-49 |
|
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: 169.78 E-value: 2.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 15 NFSIIAHIDHGKSTLADRILENTKSVETREM-QSQLLDSMDLERERGITIKLNAVRLKYeakdgKNYIFHLIDTPGHVDF 93
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTrKETFLDTLKEERERGITIKTGVVEFEW-----PKRRINFIDTPGHEDF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 94 TYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDL-PAADPERVKQEIEDV---IGLDQDD--- 166
Cdd:cd00881 76 SKETVRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRvGEEDFDEVLREIKELlklIGFTFLKgkd 155
|
170 180
....*....|....*....|....*...
gi 1080759641 167 --VVLASAKSNIGIEEILEKIVEVVPPP 192
Cdd:cd00881 156 vpIIPISALTGEGIEELLDAIVEHLPPP 183
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
11-480 |
7.57e-49 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 179.90 E-value: 7.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 11 ENIRNFSIIAHIDHGKSTLADRILENTKSVETR-EMQSQLLDSMDLERERGITIKLNAVRLKYeakdgKNYIFHLIDTPG 89
Cdd:PRK10218 3 EKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRaETQERVMDSNDLEKERGITILAKNTAIKW-----NDYRINIVDTPG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 90 HVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLPAADPERVKQEIEDV-IGLDQDD-- 166
Cdd:PRK10218 78 HADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLfVNLDATDeq 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 167 ----VVLASAKSNIG----------IEEILEKIVEVVPPPEGDPSEPLKALIFDSEYDAYRGVISSIRIMDGVVKAGDKI 232
Cdd:PRK10218 158 ldfpIVYASALNGIAgldhedmaedMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 233 KMMATGKEFEVTEVG-INTPKQLPVEELTVGDVGYIIAsIKNVDDSRVGDTITHAERPAAQP--------LKGYKKMNPM 303
Cdd:PRK10218 238 TIIDSEGKTRNAKVGkVLGHLGLERIETDLAEAGDIVA-ITGLGELNISDTVCDTQNVEALPalsvdeptVSMFFCVNTS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 304 VFCGlfpiDNKKYNDLREALEKLQ---LNDSSLEFEpETSQAlgFGFRTGFLGMLHMEIIQERIEREfGIELIATAPSVI 380
Cdd:PRK10218 317 PFCG----KEGKFVTSRQILDRLNkelVHNVALRVE-ETEDA--DAFRVSGRGELHLSVLIENMRRE-GFELAVSRPKVI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 381 YECIlkNGEKKivdnpaqmperdqideiyEPYVRATMMVPNDYVGAVMELCQRKRGQFINMDYLDDIRVNIIYEIPlSEV 460
Cdd:PRK10218 389 FREI--DGRKQ------------------EPYENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIP-SRG 447
|
490 500
....*....|....*....|....
gi 1080759641 461 VFDFFDQLKSNTKG----YASFDY 480
Cdd:PRK10218 448 LIGFRSEFMTMTSGtgllYSTFSH 471
|
|
| EF4_III |
cd16260 |
Domain III of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly ... |
302-377 |
1.06e-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: 161.13 E-value: 1.06e-47
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080759641 302 PMVFCGLFPIDNKKYNDLREALEKLQLNDSSLEFEPETSQALGFGFRTGFLGMLHMEIIQERIEREFGIELIATAP 377
Cdd:cd16260 1 PMVFAGLYPVDGSDYEELRDALEKLTLNDASVTFEPETSSALGFGFRCGFLGLLHMEVFQERLEREYGLDLIITAP 76
|
|
| EF4_II |
cd03699 |
Domain II of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly ... |
200-285 |
2.25e-46 |
|
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: 157.97 E-value: 2.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 200 LKALIFDSEYDAYRGVISSIRIMDGVVKAGDKIKMMATGKEFEVTEVGINTPKQLPVEELTVGDVGYIIASIKNVDDSRV 279
Cdd:cd03699 1 LRALIFDSWYDPYRGVVVLVRVFDGTLKKGDKIRFMATGKEYEVLEVGVFTPKMVPTDELSAGEVGYIIAGIKSVKDARV 80
|
....*.
gi 1080759641 280 GDTITH 285
Cdd:cd03699 81 GDTITL 86
|
|
| lepA_C |
cd03709 |
lepA_C: This family represents the C-terminal region of LepA, a GTP-binding protein localized ... |
410-489 |
9.28e-46 |
|
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: 156.11 E-value: 9.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 410 EPYVRATMMVPNDYVGAVMELCQRKRGQFINMDYLDDIRVNIIYEIPLSEVVFDFFDQLKSNTKGYASFDYELIGYKESD 489
Cdd:cd03709 1 EPFVKATIITPSEYLGAIMELCQERRGVQKDMEYLDANRVMLTYELPLAEIVYDFFDKLKSISKGYASLDYELIGYRESD 80
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
12-192 |
1.09e-44 |
|
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: 157.37 E-value: 1.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 12 NIRNFSIIAHIDHGKSTLADRILENTKS-VETREMQSQLLDSMDLERERGITIKLNAVRLKYeakdgKNYIFHLIDTPGH 90
Cdd:cd01891 1 KIRNIAIIAHVDHGKTTLVDALLKQSGTfRENEEVGERVMDSNDLERERGITILAKNTAITY-----KDTKINIIDTPGH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 91 VDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLPAADPERVKQEIEDV-IGLDQDD--- 166
Cdd:cd01891 76 ADFGGEVERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDRPDARPEEVVDEVFDLfLELNATDeql 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 1080759641 167 ---VVLASAKSNIG----------IEEILEKIVEVVPPP 192
Cdd:cd01891 156 dfpIVYASAKNGWAslnlddpsedLDPLFETIIEHVPAP 194
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
4-486 |
6.93e-44 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 167.35 E-value: 6.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 4 EERLNRQENIRNFSIIAHIDHGKSTLADRILENTKSVETREMQSQL-LDSMDLERERGITIKLNAVRLKYEAKdGKNYIF 82
Cdd:PRK07560 11 LELMKNPEQIRNIGIIAHIDHGKTTLSDNLLAGAGMISEELAGEQLaLDFDEEEQARGITIKAANVSMVHEYE-GKEYLI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 83 HLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKID-------LpaaDPERVKQE 155
Cdd:PRK07560 90 NLIDTPGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKPVLFINKVDrlikelkL---TPQEMQQR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 156 IEDVIG-------------------LDQDD--VVLASAKSNIGI----------------------------------EE 180
Cdd:PRK07560 167 LLKIIKdvnklikgmapeefkekwkVDVEDgtVAFGSALYNWAIsvpmmqktgikfkdiidyyekgkqkelaekaplhEV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 181 ILEKIVEVVPPP-------------------------EGDPSEPLKALIFDSEYDAYRGVISSIRIMDGVVKAGDKIKMM 235
Cdd:PRK07560 247 VLDMVVKHLPNPieaqkyripkiwkgdlnsevgkamlNCDPNGPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 236 ATGKEFEVTEVGINT-PKQLPVEELTVGDvgyiIASIKNVDDSRVGDTITH-AERPAAQPLKGYKKmnPMVFCGLFPIDN 313
Cdd:PRK07560 327 GAKKKNRVQQVGIYMgPEREEVEEIPAGN----IAAVTGLKDARAGETVVSvEDMTPFESLKHISE--PVVTVAIEAKNP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 314 KKYNDLREALEKLQLNDSSLEFE--PETSQALGFGfrtgfLGMLHMEIIQERIEREFGIELIATAPSVIY-ECI------ 384
Cdd:PRK07560 401 KDLPKLIEVLRQLAKEDPTLVVKinEETGEHLLSG-----MGELHLEVITYRIKRDYGIEVVTSEPIVVYrETVrgksqv 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 385 --------------------------LKNGE---------------------------KKIVD----------------- 394
Cdd:PRK07560 476 vegkspnkhnrfyisvepleeevieaIKEGEisedmdkkeakilreklieagmdkdeaKRVWAiyngnvfidmtkgiqyl 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 395 --------------------------------------------NPAQ-MPE-RDQI--------DEIYEPYVRATMMVP 420
Cdd:PRK07560 556 nevmeliiegfreamkegplaaepvrgvkvrlhdaklhedaihrGPAQvIPAvRNAIfaamltakPTLLEPIQKVDINVP 635
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080759641 421 NDYVGAVMELCQRKRGQFINMDYLDDIrVNIIYEIPLSEvVFDFFDQLKSNTKGYASFDYELIGYK 486
Cdd:PRK07560 636 QDYMGAVTREIQGRRGKILDMEQEGDM-AIIEAEAPVAE-MFGFAGEIRSATEGRALWSTEFAGFE 699
|
|
| EF-G |
TIGR00484 |
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ... |
11-487 |
1.59e-40 |
|
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: 156.89 E-value: 1.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 11 ENIRNFSIIAHIDHGKSTLADRILENT----KSVETREMQSQLlDSMDLERERGITIKLNAVRLKYeakdgKNYIFHLID 86
Cdd:TIGR00484 8 NRFRNIGISAHIDAGKTTTTERILFYTgrihKIGEVHDGAATM-DWMEQEKERGITITSAATTVFW-----KGHRINIID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 87 TPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLPAADPERVKQEIEDVIGL---- 162
Cdd:TIGR00484 82 TPGHVDFTVEVERSLRVLDGAVAVLDAVGGVQPQSETVWRQANRYEVPRIAFVNKMDKTGANFLRVVNQIKQRLGAnavp 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 163 ----------------------------------------------------------DQDD------------------ 166
Cdd:TIGR00484 162 iqlpigaednfigvidlvemkayffngdkgtkaiekeipsdlleqakelrenlveavaEFDEelmekylegeeltieeik 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 167 --------------VVLASAKSNIGIEEILEKIVEVVPPP-------------------EGDPSEPLKALIFDSEYDAYR 213
Cdd:TIGR00484 242 nairkgvlnceffpVLCGSAFKNKGVQLLLDAVVDYLPSPtdvpaikgidpdtekeierKASDDEPFSALAFKVATDPFV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 214 GVISSIRIMDGVVKAGDKIKMMATGKEFEVTE-VGINTPKQLPVEELTVGDvgyiIASIKNVDDSRVGDTITHAERPAAq 292
Cdd:TIGR00484 322 GQLTFVRVYSGVLKSGSYVKNSRKNKKERVGRlVKMHANNREEIKEVRAGD----ICAAIGLKDTTTGDTLCDPKIDVI- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 293 pLKGYKKMNPMVFCGLFPIDNKKYNDLREALEKLQLNDSSLEF--EPETSQALGFGfrtgfLGMLHMEIIQERIEREFGI 370
Cdd:TIGR00484 397 -LERMEFPEPVISLAVEPKTKADQEKMGIALGKLAEEDPTFRTftDPETGQTIIAG-----MGELHLDIIVDRMKREFKV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 371 ELIATAPSVIY-ECI----------------------------------------------------------------- 384
Cdd:TIGR00484 471 EANVGAPQVAYrETIrskvevegkhakqsggrgqyghvkirfeplepkgyefvneikggvipreyipavdkglqeamesg 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 385 -------------LKNGEKKIVDN-------PAQMPERDQIDE----IYEPYVRATMMVPNDYVGAVMELCQRKRGQFIN 440
Cdd:TIGR00484 551 plagypvvdikatLFDGSYHDVDSsemafklAASLAFKEAGKKanpvLLEPIMKVEVEVPEEYMGDVMGDLSSRRGIIEG 630
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1080759641 441 MDylDDIRVNIIY-EIPLSEvVFDFFDQLKSNTKGYASFDYELIGYKE 487
Cdd:TIGR00484 631 ME--ARGNVQKIKaEVPLSE-MFGYATDLRSFTQGRGTYSMEFLHYGE 675
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
14-192 |
2.53e-40 |
|
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.
Pssm-ID: 206672 [Multi-domain] Cd Length: 218 Bit Score: 146.22 E-value: 2.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 14 RNFSIIAHIDHGKSTLADRILENTKSVETREMQSQL-LDSMDLERERGITIKLNAVRLKYEAK----DGKNYIFHLIDTP 88
Cdd:cd01885 1 RNICIIAHVDHGKTTLSDSLLASAGIISEKLAGKARyLDTREDEQERGITIKSSAISLYFEYEeekmDGNDYLINLIDSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 89 GHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDL--------PAADPERVKQEIEDV- 159
Cdd:cd01885 81 GHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDRlilelklsPEEAYQRLLRIVEDVn 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1080759641 160 ----------IGLDQD-------DVVLASAKSNIG--------IEEILEKIVEVVPPP 192
Cdd:cd01885 161 aiietyapeeFKQEKWkfspqkgNVAFGSALDGWGftiikfadIYAVLEMVVKHLPSP 218
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
4-381 |
4.37e-36 |
|
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: 144.27 E-value: 4.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 4 EERLNRQENIRNFSIIAHIDHGKSTLADRILENTKSVETREMQSQL-LDSMDLERERGITIKLNAVRLKYEAkDGKNYIF 82
Cdd:TIGR00490 10 KELMWKPKFIRNIGIVAHIDHGKTTLSDNLLAGAGMISEELAGQQLyLDFDEQEQERGITINAANVSMVHEY-EGNEYLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 83 HLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKID--------LPAADPERVKQ 154
Cdd:TIGR00490 89 NLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKPVLFINKVDrlinelklTPQELQERFIK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 155 EIEDV-----------------IGLDQDDVVLASA------------KSNIGIEEI----------------------LE 183
Cdd:TIGR00490 169 IITEVnklikamapeefrdkwkVRVEDGSVAFGSAyynwaisvpsmkKTGIGFKDIykyckedkqkelakksplhqvvLD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 184 KIVEVVP-PPEG------------------------DPSEPLKALIFDSEYDAYRGVISSIRIMDGVVKAGDKIKMMATG 238
Cdd:TIGR00490 249 MVIRHLPsPIEAqkyripviwkgdlnsevgkamlncDPKGPLALMITKIVVDKHAGEVAVGRLYSGTIRPGMEVYIVDRK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 239 KEFEVTEVGINT-PKQLPVEELTVGDvgyiIASIKNVDDSRVGDTITHAERpAAQPLKGYKKMN-PMVFCGLFPIDNKKY 316
Cdd:TIGR00490 329 AKARIQQVGVYMgPERVEVDEIPAGN----IVAVIGLKDAVAGETICTTVE-NITPFESIKHISePVVTVAIEAKNTKDL 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080759641 317 NDLREALEKLQLNDSSL--EFEPETSQALGFGfrtgfLGMLHMEIIQERIEREFGIELIATAPSVIY 381
Cdd:TIGR00490 404 PKLIEVLRQVAKEDPTVhvEINEETGEHLISG-----MGELHLEIIVEKIREDYGLDVETSPPIVVY 465
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
15-208 |
1.50e-32 |
|
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling phases of protein synthesis; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains both eukaryotic and bacterial members.
Pssm-ID: 206673 [Multi-domain] Cd Length: 270 Bit Score: 126.45 E-value: 1.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 15 NFSIIAHIDHGKSTLADRILENTKSV----ETREMQSQLlDSMDLERERGITIKLNAVRLKYeakdgKNYIFHLIDTPGH 90
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGRIhkigEVHGGGATM-DWMEQERERGITIQSAATTCFW-----KDHRINIIDTPGH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 91 VDFTYEVSRSLAACEGAILVVDAAQGIEAQTL-----ANVY----LALdndlellpvVNKIDLPAADPERVKQEIEDVIG 161
Cdd:cd01886 75 VDFTIEVERSLRVLDGAVAVFDAVAGVQPQTEtvwrqADRYgvprIAF---------VNKMDRTGADFYRVVEQIREKLG 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1080759641 162 LDQDDVVLasaksNIGIEEILEKIVEVVpppegdpsePLKALIFDSE 208
Cdd:cd01886 146 ANPVPLQL-----PIGAEDDFEGVVDLI---------EMKALYWDGE 178
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
15-189 |
1.21e-30 |
|
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: 120.03 E-value: 1.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 15 NFSIIAHIDHGKSTLADRILENTKSVETR---EMQSQLLDSMDLERERGITIKLNAVRLKYEakDGKNYIfhlIDTPGHV 91
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIRELgsvDKGTTRTDSMELERQRGITIFSAVASFQWE--DTKVNI---IDTPGHM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 92 DFTYEVSRSLAACEGAILVVDAAQGIEAQT--LANVYLALDndlelLPV---VNKIDLPAADPERVKQEIEDVigLDQDD 166
Cdd:cd04168 76 DFIAEVERSLSVLDGAILVISAVEGVQAQTriLFRLLRKLN-----IPTiifVNKIDRAGADLEKVYQEIKEK--LSPDI 148
|
170 180
....*....|....*....|....*.
gi 1080759641 167 VVL---ASAKSNIGIEEILEKIVEVV 189
Cdd:cd04168 149 VPMqkvGLYPNICDTNNIDDEQIETV 174
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
14-160 |
4.24e-30 |
|
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.
Pssm-ID: 206730 [Multi-domain] Cd Length: 213 Bit Score: 117.75 E-value: 4.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 14 RNFSIIAHIDHGKSTLADRILENT--KSVETREMQSQL--LDSMDLERERGITIKLNAVRLKYEAKDGKNYIFHLIDTPG 89
Cdd:cd04167 1 RNVCIAGHLHHGKTSLLDMLIEQThkRTPSVKLGWKPLryTDTRKDEQERGISIKSNPISLVLEDSKGKSYLINIIDTPG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080759641 90 HVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKID-------LPAADPERVKQEIEDVI 160
Cdd:cd04167 81 HVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDrlilelkLPPTDAYYKLRHTIDEI 158
|
|
| EFG_C |
pfam00679 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
407-495 |
7.25e-30 |
|
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: 112.64 E-value: 7.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 407 EIYEPYVRATMMVPNDYVGAVMELCQRKRGQFINMDYLDDIRVNIIYEIPLSEvVFDFFDQLKSNTKGYASFDYELIGYK 486
Cdd:pfam00679 1 VLLEPIEKVTIDVPEEYVGDVISDLNSRRGEILDMDPDDGGRVVIEAEVPLAE-LFGFATELRSLTKGRGSFSMEFSGYQ 79
|
....*....
gi 1080759641 487 ESDLVKMDI 495
Cdd:pfam00679 80 PVPGDILDR 88
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
5-143 |
3.35e-29 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 123.23 E-value: 3.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 5 ERLNRQENIRNFSIIAHIDHGKSTLADR------ILENTKSVETREMqsqllDSMDLERERGITIKLNAVRLKYE----- 73
Cdd:PTZ00416 11 EIMDNPDQIRNMSVIAHVDHGKSTLTDSlvckagIISSKNAGDARFT-----DTRADEQERGITIKSTGISLYYEhdled 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 74 AKDGKNYIFHLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKID 143
Cdd:PTZ00416 86 GDDKQPFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKVD 155
|
|
| Elongation_Factor_C |
cd01514 |
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ... |
410-489 |
1.56e-28 |
|
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: 108.72 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 410 EPYVRATMMVPNDYVGAVMELCQRKRGQFINMDYLDDIRVNIIYEIPLSEvVFDFFDQLKSNTKGYASFDYELIGYKESD 489
Cdd:cd01514 1 EPIMKVEITVPEEYLGAVIGDLSKRRGEILGMEPRGTGRVVIKAELPLAE-MFGFATDLRSLTQGRASFSMEFSHYEPVP 79
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
14-163 |
1.88e-27 |
|
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: 111.92 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 14 RNFSIIAHIDHGKSTLADRILENTKSVET-------REMQSQLLDSMDLERERGITIKLNAVRLKYeakdgKNYIFHLID 86
Cdd:cd04169 3 RTFAIISHPDAGKTTLTEKLLLFGGAIQEagavkarKSRKHATSDWMEIEKQRGISVTSSVMQFEY-----KGCVINLLD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 87 TPGHVDF---TYevsRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLPAADPERVKQEIEDVIGLD 163
Cdd:cd04169 78 TPGHEDFsedTY---RTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDREGRDPLELLDEIENELGID 154
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
7-143 |
2.70e-26 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 114.44 E-value: 2.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 7 LNRQENIRNFSIIAHIDHGKSTLADRI--------LENTKSVetremqsQLLDSMDLERERGITIKLNAVRLKYE----- 73
Cdd:PLN00116 13 MDKKHNIRNMSVIAHVDHGKSTLTDSLvaaagiiaQEVAGDV-------RMTDTRADEAERGITIKSTGISLYYEmtdes 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080759641 74 ------AKDGKNYIFHLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKID 143
Cdd:PLN00116 86 lkdfkgERDGNEYLINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTETVLRQALGERIRPVLTVNKMD 161
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
15-289 |
3.68e-25 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 108.47 E-value: 3.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 15 NFSIIAHIDHGKSTLADRILENTKSV------ETREMQSQ----------LLDSMDLERERGITIKLNAVRLkyeakDGK 78
Cdd:PRK12317 8 NLAVIGHVDHGKSTLVGRLLYETGAIdehiieELREEAKEkgkesfkfawVMDRLKEERERGVTIDLAHKKF-----ETD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 79 NYIFHLIDTPGHVDFTYEVSRSLAACEGAILVVDA--AQGIEAQTLANVYLA--LDNDlELLPVVNKIDLPAADPER--- 151
Cdd:PRK12317 83 KYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAAddAGGVMPQTREHVFLArtLGIN-QLIVAINKMDAVNYDEKRyee 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 152 VKQEIEDV---IGLDQDDV--VLASAKSNIGIEEILEK--------IVEV---VPPPEGDPSEPLKALIfdseYDAYrgV 215
Cdd:PRK12317 162 VKEEVSKLlkmVGYKPDDIpfIPVSAFEGDNVVKKSENmpwyngptLLEAldnLKPPEKPTDKPLRIPI----QDVY--S 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 216 ISSI------RIMDGVVKAGDKIKMMATGKEFEVTEVGINtpkQLPVEELTVGD-VGYiiasikNV-----DDSRVGDTI 283
Cdd:PRK12317 236 ISGVgtvpvgRVETGVLKVGDKVVFMPAGVVGEVKSIEMH---HEELPQAEPGDnIGF------NVrgvgkKDIKRGDVC 306
|
....*.
gi 1080759641 284 THAERP 289
Cdd:PRK12317 307 GHPDNP 312
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
15-289 |
3.07e-24 |
|
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444074 [Multi-domain] Cd Length: 423 Bit Score: 105.40 E-value: 3.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 15 NFSIIAHIDHGKSTLADRILENTKSVETREMQ----------------SQLLDSMDLERERGITIKLNAVRLkyeakDGK 78
Cdd:COG5256 9 NLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEkyeeeaekkgkesfkfAWVMDRLKEERERGVTIDLAHKKF-----ETD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 79 NYIFHLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPV-VNKIDLPAADPER---VKQ 154
Cdd:COG5256 84 KYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVaVNKMDAVNYSEKRyeeVKE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 155 EIED----------------VIGLDQDDVVLASAKSNIGIEEILEKIVEVVPPPEGDPSEPLKALIfdseYDAYrgVISS 218
Cdd:COG5256 164 EVSKllkmvgykvdkipfipVSAWKGDNVVKKSDNMPWYNGPTLLEALDNLKEPEKPVDKPLRIPI----QDVY--SISG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 219 I------RIMDGVVKAGDKIKMMATGKEFEVTEvgINTPKQlPVEELTVGD-VGYiiaSIKNVD--DSRVGDTITHAERP 289
Cdd:COG5256 238 IgtvpvgRVETGVLKVGDKVVFMPAGVVGEVKS--IEMHHE-ELEQAEPGDnIGF---NVRGVEknDIKRGDVAGHPDNP 311
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
18-188 |
6.33e-24 |
|
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: 98.70 E-value: 6.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 18 IIAHIDHGKSTLADRILENtkSVETREMqsqlldsmdlereRGITIKLNAVRLKYEAKDGKnyiFHLIDTPGHVDFTYEV 97
Cdd:cd01887 5 VMGHVDHGKTTLLDKIRKT--NVAAGEA-------------GGITQHIGAYQVPIDVKIPG---ITFIDTPGHEAFTNMR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 98 SRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLP---AADPERVKQEI--EDVIGLD---QDDVVL 169
Cdd:cd01887 67 ARGASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKPygtEADPERVKNELseLGLVGEEwggDVSIVP 146
|
170
....*....|....*....
gi 1080759641 170 ASAKSNIGIEEILEKIVEV 188
Cdd:cd01887 147 ISAKTGEGIDDLLEAILLL 165
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
1-290 |
2.42e-19 |
|
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: 90.92 E-value: 2.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 1 MNN--EERLNRQENIR--NFSIIAHIDHGKSTLADRILENTKSV------------ETREMQ----SQLLDSMDLERERG 60
Cdd:COG2895 1 MSTdiEAYLAQHENKDllRFITCGSVDDGKSTLIGRLLYDTKSIfedqlaalerdsKKRGTQeidlALLTDGLQAEREQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 61 ITIKlnaVRLKYEAKDGKNYIfhLIDTPGHVDFTyevsRSLA----ACEGAILVVDAAQGIEAQT-----LA------NV 125
Cdd:COG2895 81 ITID---VAYRYFSTPKRKFI--IADTPGHEQYT----RNMVtgasTADLAILLIDARKGVLEQTrrhsyIAsllgirHV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 126 YLAldndlellpvVNKIDLPAADPER---VKQEIEDV---IGLDQDDVVLASAKS--NI-----------GiEEILEkIV 186
Cdd:COG2895 152 VVA----------VNKMDLVDYSEEVfeeIVADYRAFaakLGLEDITFIPISALKgdNVversenmpwydG-PTLLE-HL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 187 EVVPPPEGDPSEPLKALI-----FDSEYDAYRGVISSirimdGVVKAGDKIKMMATGKEFEVTEvgINTPKQlPVEELTV 261
Cdd:COG2895 220 ETVEVAEDRNDAPFRFPVqyvnrPNLDFRGYAGTIAS-----GTVRVGDEVVVLPSGKTSTVKS--IVTFDG-DLEEAFA 291
|
330 340 350
....*....|....*....|....*....|
gi 1080759641 262 GD-VGYIIAsiKNVDDSRvGDTITHAERPA 290
Cdd:COG2895 292 GQsVTLTLE--DEIDISR-GDVIVAADAPP 318
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
17-232 |
2.51e-19 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 92.20 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 17 SIIAHIDHGKSTLADRIlentksvetREMQSQlldsmdlERERG-ITIKLNAVRLKYEAKD-GKNYIFhlIDTPGHVDFT 94
Cdd:CHL00189 248 TILGHVDHGKTTLLDKI---------RKTQIA-------QKEAGgITQKIGAYEVEFEYKDeNQKIVF--LDTPGHEAFS 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 95 YEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLPAADPERVKQEI--EDVIGLD---QDDVVL 169
Cdd:CHL00189 310 SMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANTERIKQQLakYNLIPEKwggDTPMIP 389
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080759641 170 ASAKSNIGIEEILEKIVEV--VPPPEGDPSEPLKALIFDSEYDAYRGVISSIRIMDGVVKAGDKI 232
Cdd:CHL00189 390 ISASQGTNIDKLLETILLLaeIEDLKADPTQLAQGIILEAHLDKTKGPVATILVQNGTLHIGDII 454
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
5-278 |
1.63e-18 |
|
translation elongation factor TU; This model models orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts, one of several GTP-binding translation factors found by the more general pfam model GTP_EFTU. The eukaryotic conterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this model. EF-Tu is one of the most abundant proteins in bacteria, as well as one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation. [Protein synthesis, Translation factors]
Pssm-ID: 129576 [Multi-domain] Cd Length: 394 Bit Score: 87.91 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 5 ERLNRQENIRNFSIIAHIDHGKSTLA---DRILENTKSVETREMQSqlLDSMDLERERGITIklNAVRLKYEAkDGKNYI 81
Cdd:TIGR00485 4 EKFERTKPHVNVGTIGHVDHGKTTLTaaiTTVLAKEGGAAARAYDQ--IDNAPEEKARGITI--NTAHVEYET-ETRHYA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 82 FhlIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPV-VNKIDLpAADPE---RVKQEIE 157
Cdd:TIGR00485 79 H--VDCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKCDM-VDDEElleLVEMEVR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 158 DVI---GLDQDD--VVLASA-KSNIGIEEILEKIVEV-------VPPPEGDPSEPLKALIFDSEYDAYRGVISSIRIMDG 224
Cdd:TIGR00485 156 ELLsqyDFPGDDtpIIRGSAlKALEGDAEWEAKILELmdavdeyIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERG 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1080759641 225 VVKAGDKIKMMATGKEFEVTEVGINTPKQLpVEELTVGD-VGYIIASIKNVDDSR 278
Cdd:TIGR00485 236 IIKVGEEVEIVGLKDTRKTTVTGVEMFRKE-LDEGRAGDnVGLLLRGIKREEIER 289
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
15-158 |
5.21e-18 |
|
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: 83.00 E-value: 5.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 15 NFSIIAHIDHGKSTLADRILENTKS--------VETREMQ---------SQLLDSMDLERERGITIKlnaVRLKYEAKDG 77
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSifedqlaaLERSKSSgtqgekldlALLVDGLQAEREQGITID---VAYRYFSTPK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 78 KNYIfhLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLAldndlELLPV------VNKIDLPAADpER 151
Cdd:cd04166 78 RKFI--IADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIA-----SLLGIrhvvvaVNKMDLVDYD-EE 149
|
....*..
gi 1080759641 152 VKQEIED 158
Cdd:cd04166 150 VFEEIKA 156
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
21-191 |
7.85e-18 |
|
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: 81.11 E-value: 7.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 21 HIDHGKSTLADRIlentKSVETremqsqllDSMDLERERGITIKLNAVRLKYEakDGKNYIFhlIDTPGHVDFtyeVSRS 100
Cdd:cd04171 7 HIDHGKTTLIKAL----TGIET--------DRLPEEKKRGITIDLGFAYLDLP--DGKRLGF--IDVPGHEKF---VKNM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 101 LAACEG---AILVVDAAQGIEAQTLAnvYLALdndLELLP------VVNKIDLpaADPERVKQEIEDVI------GLDQD 165
Cdd:cd04171 68 LAGAGGidaVLLVVAADEGIMPQTRE--HLEI---LELLGikkglvVLTKADL--VDEDRLELVEEEILellagtFLADA 140
|
170 180
....*....|....*....|....*.
gi 1080759641 166 DVVLASAKSNIGIEEILEKIVEVVPP 191
Cdd:cd04171 141 PIFPVSSVTGEGIEELKNYLDELAEP 166
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
15-306 |
8.45e-18 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 86.42 E-value: 8.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 15 NFSIIAHIDHGKSTLADRIlenTKSV-ETREMQSQLLDSMDL---ERERGITIklNAVRLKYEAKdgKNYIFHlIDTPGH 90
Cdd:PLN03127 63 NVGTIGHVDHGKTTLTAAI---TKVLaEEGKAKAVAFDEIDKapeEKARGITI--ATAHVEYETA--KRHYAH-VDCPGH 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 91 VDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPV-VNKIDLpAADPE---RVKQEIEDVIGL---- 162
Cdd:PLN03127 135 ADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVfLNKVDV-VDDEElleLVEMELRELLSFykfp 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 163 -DQDDVVLASAKS-------NIGIEEILE---KIVEVVPPPEGDPSEPLKALIFDSEYDAYRGVISSIRIMDGVVKAGDK 231
Cdd:PLN03127 214 gDEIPIIRGSALSalqgtndEIGKNAILKlmdAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEE 293
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080759641 232 IKMMA--TGKEFEVTEVGINTPKQLpVEELTVGD-VGYIIASIKNVDDSRvGDTIThaeRPAAqpLKGYKKMNPMVFC 306
Cdd:PLN03127 294 VEIVGlrPGGPLKTTVTGVEMFKKI-LDQGQAGDnVGLLLRGLKREDVQR-GQVIC---KPGS--IKTYKKFEAEIYV 364
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
15-161 |
9.38e-18 |
|
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: 83.41 E-value: 9.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 15 NFSIIAHIDHGKSTLADRILENTKSVETR---EMQSQLLDSMDLERERGITIKLNAVRLKYEAKDgknyiFHLIDTPGHV 91
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRLgrvEDGNTVSDYDPEEKKRKMSIETSVAPLEWNGHK-----INLIDTPGYA 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080759641 92 DFTYEVSRSLAACEGAILVVDAAQGIEAQTlANVYLALDnDLEL--LPVVNKIDLPAADPERVKQEIEDVIG 161
Cdd:cd04170 76 DFVGETLSALRAVDAALIVVEAQSGVEVGT-EKVWEFLD-DAKLprIIFINKMDRARADFDKTLAALREAFG 145
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
1-163 |
2.12e-17 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 85.57 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 1 MNNEERLNRQeniRNFSIIAHIDHGKSTLADRIL------ENTKSVETREMQ----SqllDSMDLERERGITIKLNAVRL 70
Cdd:PRK00741 1 SELAQEVAKR---RTFAIISHPDAGKTTLTEKLLlfggaiQEAGTVKGRKSGrhatS---DWMEMEKQRGISVTSSVMQF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 71 KYeakdgKNYIFHLIDTPGHVDF---TYevsRSLAACEGAILVVDAAQGIEAQT--LANVYLALDndlelLPV---VNKI 142
Cdd:PRK00741 75 PY-----RDCLINLLDTPGHEDFsedTY---RTLTAVDSALMVIDAAKGVEPQTrkLMEVCRLRD-----TPIftfINKL 141
|
170 180
....*....|....*....|.
gi 1080759641 143 DLPAADPERVKQEIEDVIGLD 163
Cdd:PRK00741 142 DRDGREPLELLDEIEEVLGIA 162
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
25-187 |
1.64e-16 |
|
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: 77.11 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 25 GKSTLADRILENTKSVETREMqsqlldsmdlererGITIKLNAVRLKYeakDGKNYIFHLIDTPGHVDFTYEVSRSLAA- 103
Cdd:cd00882 9 GKSSLLNALLGGEVGEVSDVP--------------GTTRDPDVYVKEL---DKGKVKLVLVDTPGLDEFGGLGREELARl 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 104 ----CEGAILVVDAAQGIEAQTLANVYLAL--DNDLELLPVVNKIDLPAADPERVKQEIEDVIGLDQDDVVLASAKSNIG 177
Cdd:cd00882 72 llrgADLILLVVDSTDRESEEDAKLLILRRlrKEGIPIILVGNKIDLLEEREVEELLRLEELAKILGVPVFEVSAKTGEG 151
|
170
....*....|
gi 1080759641 178 IEEILEKIVE 187
Cdd:cd00882 152 VDELFEKLIE 161
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
15-250 |
2.25e-16 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 81.53 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 15 NFSIIAHIDHGKSTLADRIlenTKSV-ETREMQSQLLDSMDL---ERERGITIklNAVRLKYEAkDGKNYIfHlIDTPGH 90
Cdd:PRK12736 14 NIGTIGHVDHGKTTLTAAI---TKVLaERGLNQAKDYDSIDAapeEKERGITI--NTAHVEYET-EKRHYA-H-VDCPGH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 91 VDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPV-VNKIDLpAADPER---VKQEIEDVI---GLD 163
Cdd:PRK12736 86 ADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVfLNKVDL-VDDEELlelVEMEVRELLseyDFP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 164 QDD--VVLASAKSNI--------GIEEILEKIVEVVPPPEGDPSEPLKALIFDSEYDAYRGVISSIRIMDGVVKAGDKIK 233
Cdd:PRK12736 165 GDDipVIRGSALKALegdpkwedAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGDEVE 244
|
250
....*....|....*..
gi 1080759641 234 MMATGKEFEVTEVGINT 250
Cdd:PRK12736 245 IVGIKETQKTVVTGVEM 261
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
5-278 |
4.63e-16 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 81.20 E-value: 4.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 5 ERLNRQENIRNFSIIAHIDHGKSTLADRILENTKSV-ETREMQSQLLDSMDLERERGITIklNAVRLKYEAKDgKNYIFh 83
Cdd:PLN03126 73 GKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMgGSAPKKYDEIDAAPEERARGITI--NTATVEYETEN-RHYAH- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 84 lIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPV-VNKIDLpaADPER----VKQEIED 158
Cdd:PLN03126 149 -VDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVfLNKQDQ--VDDEEllelVELEVRE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 159 VIG---LDQDDVVLASAKSNIGIEEILE-------------KIVEV-------VPPPEGDPSEPLKALIFDSEYDAYRGV 215
Cdd:PLN03126 226 LLSsyeFPGDDIPIISGSALLALEALMEnpnikrgdnkwvdKIYELmdavdsyIPIPQRQTDLPFLLAVEDVFSITGRGT 305
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080759641 216 ISSIRIMDGVVKAGDKIKMMATGKEFEVTEVGINTPKQLPVEELTVGDVGYIIASIKNVDDSR 278
Cdd:PLN03126 306 VATGRVERGTVKVGETVDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQR 368
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
18-189 |
1.06e-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: 80.34 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 18 IIA---HIDHGKSTL--------ADRILEntksvetremqsqlldsmdlERERGITIKLNAVRLKYEakDGKNYIFhlID 86
Cdd:COG3276 2 IIGtagHIDHGKTTLvkaltgidTDRLKE--------------------EKKRGITIDLGFAYLPLP--DGRRLGF--VD 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 87 TPGHVDFtyeVSRSLAACEG---AILVVDAAQGIEAQTLAnvYLALdndLELLP------VVNKIDLpaADPER---VKQ 154
Cdd:COG3276 58 VPGHEKF---IKNMLAGAGGidlVLLVVAADEGVMPQTRE--HLAI---LDLLGikrgivVLTKADL--VDEEWlelVEE 127
|
170 180 190
....*....|....*....|....*....|....*...
gi 1080759641 155 EIEDVI---GLDQDDVVLASAKSNIGIEEILEKIVEVV 189
Cdd:COG3276 128 EIRELLagtFLEDAPIVPVSAVTGEGIDELRAALDALA 165
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
21-232 |
3.65e-15 |
|
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440298 [Multi-domain] Cd Length: 502 Bit Score: 78.52 E-value: 3.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 21 HIDHGKSTLADRILeNTKSVEtremqsqlldsmdleRE-RGITIKLNAvrlkYEAK-DGKNYIFhlIDTPGHVDFTYEVS 98
Cdd:COG0532 12 HVDHGKTSLLDAIR-KTNVAA---------------GEaGGITQHIGA----YQVEtNGGKITF--LDTPGHEAFTAMRA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 99 RslaaceGA------ILVVDAAQGIEAQTL--------ANVylaldndlellPVV---NKIDLPAADPERVKQE------ 155
Cdd:COG0532 70 R------GAqvtdivILVVAADDGVMPQTIeainhakaAGV-----------PIIvaiNKIDKPGANPDRVKQElaehgl 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 156 -IE----DVIgldqddVVLASAKSNIGIEEILEKIV---EVVpppE--GDPSEPLKALIFDSEYDAYRGVISSIRIMDGV 225
Cdd:COG0532 133 vPEewggDTI------FVPVSAKTGEGIDELLEMILlqaEVL---ElkANPDRPARGTVIEAKLDKGRGPVATVLVQNGT 203
|
....*..
gi 1080759641 226 VKAGDKI 232
Cdd:COG0532 204 LKVGDIV 210
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
15-243 |
1.85e-14 |
|
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]
Pssm-ID: 129567 [Multi-domain] Cd Length: 581 Bit Score: 76.45 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 15 NFSIIAHIDHGKSTLADRILEntksvetremqsqlLDSMDL--ERERGITIKLNavrlkYEAKDGKNYIFHLIDTPGHVD 92
Cdd:TIGR00475 2 IIATAGHVDHGKTTLLKALTG--------------IAADRLpeEKKRGMTIDLG-----FAYFPLPDYRLGFIDVPGHEK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 93 FTYEVSRSLAACEGAILVVDAAQGIEAQTLANV-YLALDNDLELLPVVNKIDLpaADPER-------VKQEIEDVIGLDQ 164
Cdd:TIGR00475 63 FISNAIAGGGGIDAALLVVDADEGVMTQTGEHLaVLDLLGIPHTIVVITKADR--VNEEEikrtemfMKQILNSYIFLKN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 165 DDVVLASAKSNIGIEEILEKIVEVVPPPE-GDPSEPLKALIfDSEYdAYRGVISSIR--IMDGVVKAGDKIKMMATGKEF 241
Cdd:TIGR00475 141 AKIFKTSAKTGQGIGELKKELKNLLESLDiKRIQKPLRMAI-DRAF-KVKGAGTVVTgtAFSGEVKVGDNLRLLPINHEV 218
|
..
gi 1080759641 242 EV 243
Cdd:TIGR00475 219 RV 220
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
18-186 |
2.10e-14 |
|
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: 71.25 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 18 IIAHIDHGKSTLADRILENTKSVETREMQSQLLDSMDLERERGITIKLNavrlkyeakdgknyifhLIDTPGHVDF---- 93
Cdd:TIGR00231 6 IVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNYVTTVIEEDGKTYKFN-----------------LLDTAGQEDYdair 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 94 ---TYEVSRSLAACEGAILVVDAAQGIEAQT--LANVylaLDNDLELLPVVNKIDLPAADPErvKQEIEDVIGLDQDDVV 168
Cdd:TIGR00231 69 rlyYPQVERSLRVFDIVILVLDVEEILEKQTkeIIHH---ADSGVPIILVGNKIDLKDADLK--THVASEFAKLNGEPII 143
|
170
....*....|....*...
gi 1080759641 169 LASAKSNIGIEEILEKIV 186
Cdd:TIGR00231 144 PLSAETGKNIDSAFKIVE 161
|
|
| EFG_III-like |
cd16257 |
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G ... |
302-375 |
2.44e-14 |
|
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G (EF-G) and related proteins play a role in translation and share a similar domain architecture. Elongation factor EFG participates in the elongation phase during protein biosynthesis on the ribosome by stimulating translocation. Its functional cycles depend on GTP binding and its hydrolysis. Domain III is involved in the activation of GTP hydrolysis. This domain III, which is different from domain III in EF-TU and related elongation factors, is found in several translation factors, like bacterial release factors RF3, elongation factor 4, elongation factor 2, GTP-binding protein BipA and tetracycline resistance protein Tet.
Pssm-ID: 293914 [Multi-domain] Cd Length: 71 Bit Score: 68.14 E-value: 2.44e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080759641 302 PMVFCGLFPIDNKKYNDLREALEKLQLNDSSLEFEPETSQalgFGFRTGFLGMLHMEIIQERIEREFGIELIAT 375
Cdd:cd16257 1 PVVFVTVEVKNPLDQEKLLEGLERLSEEDPALQVYREEST---GEFILSGLGELHLEIIVARLEREYGVELVVS 71
|
|
| tufA |
CHL00071 |
elongation factor Tu |
15-278 |
4.38e-14 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 74.61 E-value: 4.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 15 NFSIIAHIDHGKSTLADRI-----LENTKSVETREmqsqLLDSMDLERERGITIklNAVRLKYEAKdgKNYIFHlIDTPG 89
Cdd:CHL00071 14 NIGTIGHVDHGKTTLTAAItmtlaAKGGAKAKKYD----EIDSAPEEKARGITI--NTAHVEYETE--NRHYAH-VDCPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 90 HVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPV-VNKIDLpAADPE---RVKQEIEDVI---GL 162
Cdd:CHL00071 85 HADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVfLNKEDQ-VDDEElleLVELEVRELLskyDF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 163 DQDDV--VLASA---------KSNIG---------IEEILEKIVEVVPPPEGDPSEPLKALIFDSEYDAYRGVISSIRIM 222
Cdd:CHL00071 164 PGDDIpiVSGSAllalealteNPKIKrgenkwvdkIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIE 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1080759641 223 DGVVKAGDKIKMMATGKEFEVTEVGINTPKQLPVEELTVGDVGYIIASIKNVDDSR 278
Cdd:CHL00071 244 RGTVKVGDTVEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIER 299
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
15-168 |
7.70e-14 |
|
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: 70.98 E-value: 7.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 15 NFSIIAHIDHGKSTLADRILENTKSVETREMQ----------------SQLLDSMDLERERGITIklNAVRLKYEAkdgK 78
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEkyekeakemgkesfkyAWVLDKLKEERERGVTI--DVGLAKFET---E 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 79 NYIFHLIDTPGHVDFTYE--VSRSLAACegAILVVDAAQG-------IEAQTLANVYLAldNDL---ELLPVVNKIDLPA 146
Cdd:cd01883 76 KYRFTIIDAPGHRDFVKNmiTGASQADV--AVLVVSARKGefeagfeKGGQTREHALLA--RTLgvkQLIVAVNKMDDVT 151
|
170 180 190
....*....|....*....|....*....|
gi 1080759641 147 A--DPER---VKQEIEDV---IGLDQDDVV 168
Cdd:cd01883 152 VnwSQERydeIKKKVSPFlkkVGYNPKDVP 181
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
19-192 |
1.20e-13 |
|
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: 69.92 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 19 IAHIDHGKSTLADRI---LENTKSVETREMQSqlLDSMDLERERGITIklNAVRLKYEAkDGKNYiFHlIDTPGHVDFTY 95
Cdd:cd01884 8 IGHVDHGKTTLTAAItkvLAKKGGAKAKKYDE--IDKAPEEKARGITI--NTAHVEYET-ANRHY-AH-VDCPGHADYIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 96 EVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPV-VNKIDLpAADPER---VKQEIEDVI---GLDQDD-- 166
Cdd:cd01884 81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVfLNKADM-VDDEELlelVEMEVRELLskyGFDGDDtp 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 1080759641 167 VVLASA-------KSNIG---IEEILEKIVEVVPPP 192
Cdd:cd01884 160 IVRGSAlkalegdDPNKWvdkILELLDALDSYIPTP 195
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
214-284 |
2.31e-13 |
|
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: 65.36 E-value: 2.31e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080759641 214 GVISSIRIMDGVVKAGDKIKMM--ATGKEFEVTEVGINTPKQLPVEELTVGDVGYIIASIKNVDDSRVGDTIT 284
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILpnGTGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
22-289 |
3.65e-13 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 72.27 E-value: 3.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 22 IDHGKSTLADRILENTKSV----------ETREMQSQ--------LLDSMDLERERGITIKlnaVRLKYEAKDGKNYIfh 83
Cdd:PRK05506 33 VDDGKSTLIGRLLYDSKMIfedqlaalerDSKKVGTQgdeidlalLVDGLAAEREQGITID---VAYRYFATPKRKFI-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 84 LIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLAldndlELLPV------VNKIDLPAADPER------ 151
Cdd:PRK05506 108 VADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIA-----SLLGIrhvvlaVNKMDLVDYDQEVfdeiva 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 152 ------VKQEIEDVI-----GLDQDDVVLASAKS----NIGIEEILEKiVEVVPPP-EGDPSEPLKALIF-DSEYDAYRG 214
Cdd:PRK05506 183 dyrafaAKLGLHDVTfipisALKGDNVVTRSARMpwyeGPSLLEHLET-VEIASDRnLKDFRFPVQYVNRpNLDFRGFAG 261
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080759641 215 VISSirimdGVVKAGDKIKMMATGKEFEVTEvgINTPKQlPVEELTVGD-VGYIIASikNVDDSRvGDTITHAERP 289
Cdd:PRK05506 262 TVAS-----GVVRPGDEVVVLPSGKTSRVKR--IVTPDG-DLDEAFAGQaVTLTLAD--EIDISR-GDMLARADNR 326
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
22-246 |
4.58e-13 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 71.48 E-value: 4.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 22 IDHGKSTLADRILENTKSV----------ETREMQSQ--------LLDSMDLERERGITIKlnaVRLKYEAKDGKNYIfh 83
Cdd:PRK05124 36 VDDGKSTLIGRLLHDTKQIyedqlaslhnDSKRHGTQgekldlalLVDGLQAEREQGITID---VAYRYFSTEKRKFI-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 84 LIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLAldndlELLPV------VNKIDLPAADPER---VKQ 154
Cdd:PRK05124 111 IADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIA-----TLLGIkhlvvaVNKMDLVDYSEEVferIRE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 155 EIEDVIG---------------LDQDDVVLASAK----SNIGIEEILEKiVEVVPPPEGDP--------SEPlkalifDS 207
Cdd:PRK05124 186 DYLTFAEqlpgnldirfvplsaLEGDNVVSQSESmpwySGPTLLEVLET-VDIQRVVDAQPfrfpvqyvNRP------NL 258
|
250 260 270
....*....|....*....|....*....|....*....
gi 1080759641 208 EYDAYRGVISSirimdGVVKAGDKIKMMATGKEFEVTEV 246
Cdd:PRK05124 259 DFRGYAGTLAS-----GVVKVGDRVKVLPSGKESNVARI 292
|
|
| EFG_C |
smart00838 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
408-487 |
5.53e-13 |
|
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: 64.45 E-value: 5.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 408 IYEPYVRATMMVPNDYVGAVMELCQRKRGQFINMDYLDDIRVnIIYEIPLSEvVFDFFDQLKSNTKGYASFDYELIGYKE 487
Cdd:smart00838 1 LLEPIMKVEVTVPEEYMGDVIGDLNSRRGKIEGMEQRGGAQV-IKAKVPLSE-MFGYATDLRSATQGRATWSMEFSHYEE 78
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
25-188 |
1.30e-12 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 66.54 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 25 GKSTLADRILENTksVETREMQSqlldsmdlerERGITIKLNAVRLkyeakDGKNYIFHLIDTPGHVDftYEVSRSLAAC 104
Cdd:COG1100 15 GKTSLVNRLVGDI--FSLEKYLS----------TNGVTIDKKELKL-----DGLDVDLVIWDTPGQDE--FRETRQFYAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 105 E-----GAILVVDAAQgieAQTLANVYLALDN------DLELLPVVNKIDLPAADPERVKQEIEDVIGLDQ-DDVVLASA 172
Cdd:COG1100 76 QltgasLYLFVVDGTR---EETLQSLYELLESlrrlgkKSPIILVLNKIDLYDEEEIEDEERLKEALSEDNiVEVVATSA 152
|
170
....*....|....*.
gi 1080759641 173 KSNIGIEEILEKIVEV 188
Cdd:COG1100 153 KTGEGVEELFAALAEI 168
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
15-232 |
2.73e-12 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 68.71 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 15 NFSIIAHIDHGKSTLADRI---LENTKSVETREMQSqlLDSMDLERERGITIklNAVRLKYEAkDGKNYIfHlIDTPGHV 91
Cdd:PRK12735 14 NVGTIGHVDHGKTTLTAAItkvLAKKGGGEAKAYDQ--IDNAPEEKARGITI--NTSHVEYET-ANRHYA-H-VDCPGHA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 92 DFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPV-VNKIDLpAADPER---VKQEIEDVI---GLDQ 164
Cdd:PRK12735 87 DYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVfLNKCDM-VDDEELlelVEMEVRELLskyDFPG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 165 DD--VVLASA-------KSNIG---IEEILEKIVEVVPPPEGDPSEPLKALIFDSEYDAYRGVISSIRIMDGVVKAGDKI 232
Cdd:PRK12735 166 DDtpIIRGSAlkalegdDDEEWeakILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGDEV 245
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
71-189 |
4.67e-12 |
|
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: 64.19 E-value: 4.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 71 KYEAKDGKNYIFHLIDTPGHVD-------FTYEVSRSLAACEGAILVVDAAQGIEAQTlANVYLALDNDLELLPVVNKID 143
Cdd:cd00880 37 RKEWELLPLGPVVLIDTPGLDEegglgreRVEEARQVADRADLVLLVVDSDLTPVEEE-AKLGLLRERGKPVLLVLNKID 115
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1080759641 144 LPAADPERVKQEIEDVIGLDQDDVVLASAKSNIGIEEILEKIVEVV 189
Cdd:cd00880 116 LVPESEEEELLRERKLELLPDLPVIAVSALPGEGIDELRKKIAELL 161
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
25-188 |
1.16e-11 |
|
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206682 [Multi-domain] Cd Length: 174 Bit Score: 63.61 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 25 GKSTLADRILEntksvETREMQSQlldsmdlerERGITIklNAVRLKYEaKDGKNYIFhlIDTPG---------HVDFtY 95
Cdd:cd01895 14 GKSSLLNALLG-----EERVIVSD---------IAGTTR--DSIDVPFE-YDGQKYTL--IDTAGirkkgkvteGIEK-Y 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 96 EVSRSLAACEGA---ILVVDAAQGIEAQ--TLANvyLALDNDLELLPVVNKIDLPAADPER---VKQEIEDVIG-LDQDD 166
Cdd:cd01895 74 SVLRTLKAIERAdvvLLVLDASEGITEQdlRIAG--LILEEGKALIIVVNKWDLVEKDEKTmkeFEKELRRKLPfLDYAP 151
|
170 180
....*....|....*....|..
gi 1080759641 167 VVLASAKSNIGIEEILEKIVEV 188
Cdd:cd01895 152 IVFISALTGQGVDKLFDAIKEV 173
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
15-232 |
1.45e-11 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 66.37 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 15 NFSIIAHIDHGKSTLADRIlenTKSVETREM-QSQLLDSMDL---ERERGITIklNAVRLKYEAkDGKNYIfHlIDTPGH 90
Cdd:PRK00049 14 NVGTIGHVDHGKTTLTAAI---TKVLAKKGGaEAKAYDQIDKapeEKARGITI--NTAHVEYET-EKRHYA-H-VDCPGH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 91 VDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPV-VNKIDLpAADPER---VKQEIEDVI---GLD 163
Cdd:PRK00049 86 ADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVfLNKCDM-VDDEELlelVEMEVRELLskyDFP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 164 QDD--VVLASA-------KSNIG---IEEILEKIVEVVPPPEGDPSEPLKALIFDSEYDAYRGVISSIRIMDGVVKAGDK 231
Cdd:PRK00049 165 GDDtpIIRGSAlkalegdDDEEWekkILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEE 244
|
.
gi 1080759641 232 I 232
Cdd:PRK00049 245 V 245
|
|
| EFG_mtEFG_C |
cd03713 |
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational ... |
410-487 |
2.15e-11 |
|
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: 59.85 E-value: 2.15e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080759641 410 EPYVRATMMVPNDYVGAVMELCQRKRGQFINMDYLDDIRVnIIYEIPLSEvVFDFFDQLKSNTKGYASFDYELIGYKE 487
Cdd:cd03713 1 EPIMKVEVTVPEEYMGDVIGDLSSRRGQILGTESRGGWKV-IKAEVPLAE-MFGYSTDLRSLTQGRGSFTMEFSHYEE 76
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
25-188 |
4.99e-11 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 65.07 E-value: 4.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 25 GKSTLADRIL-EntksvetremqsqlldsmdlER-----ERGITIklNAVRLKYEaKDGKNYIfhLIDTPG-----HVDF 93
Cdd:PRK00093 185 GKSSLINALLgE--------------------ERvivsdIAGTTR--DSIDTPFE-RDGQKYT--LIDTAGirrkgKVTE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 94 T---YEVSRSLAACEGA---ILVVDAAQGIEAQ--TLANvyLALDNDLELLPVVNKIDL-PAADPERVKQEIEDVIG-LD 163
Cdd:PRK00093 240 GvekYSVIRTLKAIERAdvvLLVIDATEGITEQdlRIAG--LALEAGRALVIVVNKWDLvDEKTMEEFKKELRRRLPfLD 317
|
170 180
....*....|....*....|....*
gi 1080759641 164 QDDVVLASAKSNIGIEEILEKIVEV 188
Cdd:PRK00093 318 YAPIVFISALTGQGVDKLLEAIDEA 342
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
15-274 |
5.55e-11 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 65.15 E-value: 5.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 15 NFSIIAHIDHGKSTLADRILE-----NTKSVETREMQSQ-----------LLDSMDLERERGITIKLNAvrLKYEAKdgk 78
Cdd:PTZ00141 9 NLVVIGHVDSGKSTTTGHLIYkcggiDKRTIEKFEKEAAemgkgsfkyawVLDKLKAERERGITIDIAL--WKFETP--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 79 NYIFHLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGI-------EAQTLANVYLALDNDLELLPV-VNKIDLPAAD-- 148
Cdd:PTZ00141 84 KYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEfeagiskDGQTREHALLAFTLGVKQMIVcINKMDDKTVNys 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 149 PER---VKQEIEDVI----------------GLDQDDVVLASAKSNIGIEEILEKIVEVVPPPEGDPSEPLKALIfdseY 209
Cdd:PTZ00141 164 QERydeIKKEVSAYLkkvgynpekvpfipisGWQGDNMIEKSDNMPWYKGPTLLEALDTLEPPKRPVDKPLRLPL----Q 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 210 DAYR----GVISSIRIMDGVVKAGDKIKMMATGKEFEVTEVGINTpKQLPveELTVGD-VGYiiaSIKNV 274
Cdd:PTZ00141 240 DVYKiggiGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHH-EQLA--EAVPGDnVGF---NVKNV 303
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
15-157 |
1.29e-10 |
|
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: 60.84 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 15 NFSIIAHIDHGKSTLAdRILENTKSVETremqsqlLDSMDLERERGITIKL---------NAVRLKYEAKDGKNYIFHLI 85
Cdd:cd01889 2 NVGLLGHVDSGKTSLA-KALSEIASTAA-------FDKNPQSQERGITLDLgfssfevdkPKHLEDNENPQIENYQITLV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080759641 86 DTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLpaADPERVKQEIE 157
Cdd:cd01889 74 DCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDL--IPEEERKRKIE 143
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
25-188 |
1.90e-10 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 63.12 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 25 GKSTLADRILEntksvetremqsqlldsmdleRER-------GITIklNAVRLKYEaKDGKNYIfhLIDTPG-----HVD 92
Cdd:COG1160 187 GKSSLINALLG---------------------EERvivsdiaGTTR--DSIDTPFE-RDGKKYT--LIDTAGirrkgKVD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 93 FT---YEVSRSLAA---CEGAILVVDAAQGIEAQ--TLANvyLALDNDLELLPVVNKIDLPAADP---ERVKQEIEDVIG 161
Cdd:COG1160 241 EGiekYSVLRTLRAierADVVLLVIDATEGITEQdlKIAG--LALEAGKALVIVVNKWDLVEKDRktrEELEKEIRRRLP 318
|
170 180
....*....|....*....|....*...
gi 1080759641 162 -LDQDDVVLASAKSNIGIEEILEKIVEV 188
Cdd:COG1160 319 fLDYAPIVFISALTGQGVDKLLEAVDEV 346
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
19-232 |
2.47e-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: 62.86 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 19 IAHIDHGKSTL--------ADRILENTKSVETremqsqlLDSMDLERERGITIklNAVRLKYEAkDGKNYIfHlIDTPGH 90
Cdd:COG0050 18 IGHVDHGKTTLtaaitkvlAKKGGAKAKAYDQ-------IDKAPEEKERGITI--NTSHVEYET-EKRHYA-H-VDCPGH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 91 VDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPV-VNKIDLpAADPER---VKQEIEDVI---GLD 163
Cdd:COG0050 86 ADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKCDM-VDDEELlelVEMEVRELLskyGFP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 164 QDD--VVLASA-------KSNIG---IEEILEKIVEVVPPPEGDPSEPLKALIFDSEYDAYRGVISSIRIMDGVVKAGDK 231
Cdd:COG0050 165 GDDtpIIRGSAlkalegdPDPEWekkILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDE 244
|
.
gi 1080759641 232 I 232
Cdd:COG0050 245 V 245
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
200-284 |
9.95e-10 |
|
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: 55.35 E-value: 9.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 200 LKALIFDSEYDAYRGVISSIRIMDGVVKAGDKIKMMATGKEFEVTEVGINTpkqLPVEELTVGDVGYIiaSIKNVDDSRV 279
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFH---EEVDEAKAGDIVGI--GILGVKDILT 75
|
....*
gi 1080759641 280 GDTIT 284
Cdd:cd01342 76 GDTLT 80
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
78-189 |
2.47e-09 |
|
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: 56.35 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 78 KNYIFHLIDTPGHVDFTYEV-----SRSLAACEGA---ILVVDAAQGIEAQTLANvyLALDNDLELLPVVNKIDLPAADP 149
Cdd:cd04164 49 GGIPVRLIDTAGLRETEDEIekigiERAREAIEEAdlvLLVVDASEGLDEEDLEI--LELPAKKPVIVVLNKSDLLSDAE 126
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1080759641 150 ERVKQEIEDVIGLdqddvvlaSAKSNIGIEEILEKIVEVV 189
Cdd:cd04164 127 GISELNGKPIIAI--------SAKTGEGIDELKEALLELA 158
|
|
| BipA_TypA_C |
cd03710 |
BipA_TypA_C: a C-terminal portion of BipA or TypA having homology to the C terminal domains of ... |
410-485 |
3.67e-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: 53.66 E-value: 3.67e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080759641 410 EPYVRATMMVPNDYVGAVMELCQRKRGQFINMDYLDDIRVNIIYEIPlSEVVFDFFDQLKSNTKGYASFDYELIGY 485
Cdd:cd03710 1 EPIEELTIDVPEEYSGAVIEKLGKRKGEMVDMEPDGNGRTRLEFKIP-SRGLIGFRSEFLTDTRGTGIMNHVFDGY 75
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
15-233 |
4.32e-09 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 58.71 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 15 NFSIIAHIDHGKSTLadrilentksveTREMQSQLLDSMDLERERGITIKLN----AVRLKYEAKDGKNYI--------- 81
Cdd:PRK04000 11 NIGMVGHVDHGKTTL------------VQALTGVWTDRHSEELKRGITIRLGyadaTIRKCPDCEEPEAYTtepkcpncg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 82 --------FHLIDTPGHvdftyEV------SRSlAACEGAILVVDAAQGI-EAQTLANvYLALD-----NdleLLPVVNK 141
Cdd:PRK04000 79 setellrrVSFVDAPGH-----ETlmatmlSGA-ALMDGAILVIAANEPCpQPQTKEH-LMALDiigikN---IVIVQNK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 142 IDLpaADPERVK---QEIEDVI-GLDQDD--VVLASAKSNIGIEEILEKIVEVVPPPEGDPSEPLKALI---FD-----S 207
Cdd:PRK04000 149 IDL--VSKERALenyEQIKEFVkGTVAENapIIPVSALHKVNIDALIEAIEEEIPTPERDLDKPPRMYVarsFDvnkpgT 226
|
250 260
....*....|....*....|....*..
gi 1080759641 208 EYDAYR-GVISSiRIMDGVVKAGDKIK 233
Cdd:PRK04000 227 PPEKLKgGVIGG-SLIQGVLKVGDEIE 252
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
15-274 |
1.03e-08 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 57.79 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 15 NFSIIAHIDHGKSTLADRILENTKSVETR----------EMQSQ------LLDSMDLERERGITIKLnaVRLKYEAkdgK 78
Cdd:PLN00043 9 NIVVIGHVDSGKSTTTGHLIYKLGGIDKRvierfekeaaEMNKRsfkyawVLDKLKAERERGITIDI--ALWKFET---T 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 79 NYIFHLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQG-------IEAQTLANVYLALDNDL-ELLPVVNKIDlpAADPE 150
Cdd:PLN00043 84 KYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGgfeagisKDGQTREHALLAFTLGVkQMICCCNKMD--ATTPK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 151 RVKQEIEDVI-----------------------GLDQDDVVLASAKSNIGIEEILEKIVEVVPPPEGDPSEPLKALIFDS 207
Cdd:PLN00043 162 YSKARYDEIVkevssylkkvgynpdkipfvpisGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQDV 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080759641 208 EYDAYRGVISSIRIMDGVVKAGDKIKMMATGKEFEVTEVGINTPKQLpvEELTVGDVGYiiaSIKNV 274
Cdd:PLN00043 242 YKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQ--EALPGDNVGF---NVKNV 303
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
18-181 |
1.21e-08 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 57.75 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 18 IIA---HIDHGKSTLadriLENTKSVETremqsqllDSMDLERERGITIKLNAVRLKYEakDGKnyIFHLIDTPGHVDFt 94
Cdd:PRK10512 2 IIAtagHVDHGKTTL----LQAITGVNA--------DRLPEEKKRGMTIDLGYAYWPQP--DGR--VLGFIDVPGHEKF- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 95 yeVSRSLAACEG---AILVVDAAQGIEAQTLANV-YLALDNDLELLPVVNKIDLpaADPER---VKQEIEDVI---GLDQ 164
Cdd:PRK10512 65 --LSNMLAGVGGidhALLVVACDDGVMAQTREHLaILQLTGNPMLTVALTKADR--VDEARiaeVRRQVKAVLreyGFAE 140
|
170
....*....|....*..
gi 1080759641 165 DDVVLASAKSNIGIEEI 181
Cdd:PRK10512 141 AKLFVTAATEGRGIDAL 157
|
|
| MnmE_helical |
pfam12631 |
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ... |
78-200 |
1.61e-08 |
|
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: 56.72 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 78 KNYIFHLIDTPG------HVdftyE---VSRSLAACEGA---ILVVDAAQGIEAQTLAnVYLALDNDLELLPVVNKIDLP 145
Cdd:pfam12631 140 GGIPLRLIDTAGiretddEV----EkigIERAREAIEEAdlvLLVLDASRPLDEEDLE-ILELLKDKKPIIVVLNKSDLL 214
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1080759641 146 AADPERVKQEIEDVIGLdqddvvlaSAKSNIGIEEILEKIVEVVPPPEGDPSEPL 200
Cdd:pfam12631 215 GEIDELEELKGKPVLAI--------SAKTGEGLDELEEAIKELFLAGEIASDGPI 261
|
|
| MnmE |
COG0486 |
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
82-189 |
2.34e-08 |
|
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: 56.61 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 82 FHLIDTPG------HVdftyE---VSRSLAACEGA---ILVVDAAQGIEAQTLAnvYLALDNDLELLPVVNKIDLPAADP 149
Cdd:COG0486 263 VRLIDTAGlretedEV----EkigIERAREAIEEAdlvLLLLDASEPLTEEDEE--ILEKLKDKPVIVVLNKIDLPSEAD 336
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1080759641 150 ERVKQeiedvigLDQDDVVLASAKSNIGIEEILEKIVEVV 189
Cdd:COG0486 337 GELKS-------LPGEPVIAISAKTGEGIDELKEAILELV 369
|
|
| EFG_mtEFG_II |
cd04088 |
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation ... |
202-285 |
8.49e-08 |
|
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation factors G1 and G2; This family represents the domain II of bacterial Elongation factor G (EF-G)and mitochondrial Elongation factors G1 (mtEFG1) and G2 (mtEFG2). During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. In bacteria this translocation step is catalyzed by EF-G_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. mtEFG1 and mtEFG2 show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. No clear phenotype has been found for mutants in the yeast homolog of mtEFG2, MEF2.
Pssm-ID: 293905 [Multi-domain] Cd Length: 83 Bit Score: 49.83 E-value: 8.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 202 ALIFDSEYDAYRGVISSIRIMDGVVKAGDKIKMMATGKEFEVTE-VGINTPKQLPVEELTVGDvgyIIASIKnVDDSRVG 280
Cdd:cd04088 3 ALVFKTMADPFVGKLTFFRVYSGTLKSGSTVYNSTKGKKERVGRlLRMHGKKREEVEELGAGD---IGAVVG-LKDTRTG 78
|
....*
gi 1080759641 281 DTITH 285
Cdd:cd04088 79 DTLCD 83
|
|
| trmE |
PRK05291 |
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; |
78-189 |
1.51e-07 |
|
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
Pssm-ID: 235392 [Multi-domain] Cd Length: 449 Bit Score: 53.96 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 78 KNYIFHLIDTPG------HVdftyE---VSRSLAACEGA---ILVVDAAQGIEAQTLANvyLALDNDLELLPVVNKIDLP 145
Cdd:PRK05291 261 DGIPLRLIDTAGiretddEV----EkigIERSREAIEEAdlvLLVLDASEPLTEEDDEI--LEELKDKPVIVVLNKADLT 334
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1080759641 146 AADpervkqeieDVIGLDQDDVVLASAKSNIGIEEILEKIVEVV 189
Cdd:PRK05291 335 GEI---------DLEEENGKPVIRISAKTGEGIDELREAIKELA 369
|
|
| EFG_III |
pfam14492 |
Elongation Factor G, domain III; This domain is found in Elongation Factor G. It shares a ... |
302-373 |
2.02e-07 |
|
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: 48.63 E-value: 2.02e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080759641 302 PMVFCGLFPIDNKKYNDLREALEKLQLNDSSL--EFEPETSQALGFGfrtgfLGMLHMEIIQERIEREFGIELI 373
Cdd:pfam14492 4 PVISVAIEPKTKGDEDKLSKALNRLLEEDPTLrvERDEETGETILSG-----MGELHLEIVVDRLKRKYGVEVE 72
|
|
| EFG_III |
cd16262 |
Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial ... |
302-371 |
2.20e-07 |
|
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: 48.61 E-value: 2.20e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080759641 302 PMVFCGLFPIDNKKYNDLREALEKLQLNDSSL--EFEPETSQALGFGfrtgfLGMLHMEIIQERIEREFGIE 371
Cdd:cd16262 3 PVISLAIEPKTKADEDKLSKALARLAEEDPTLrvSRDEETGQTILSG-----MGELHLEIIVERLKREYGVE 69
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
200-293 |
4.50e-07 |
|
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: 47.95 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 200 LKALIFDSEYDAYRGVISSIRIMDGVVKAGDKIKMMATGKE---FEVTEV----GIntpKQLPVEELTVGDvgyIIAsIK 272
Cdd:cd03691 1 FQMLVTTLDYDDYLGRIAIGRIFSGTVKVGQQVTVVDEDGKiekGRVTKLfgfeGL---ERVEVEEAEAGD---IVA-IA 73
|
90 100
....*....|....*....|.
gi 1080759641 273 NVDDSRVGDTITHAERPAAQP 293
Cdd:cd03691 74 GLEDITIGDTICDPEVPEPLP 94
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
84-196 |
3.43e-06 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 49.22 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 84 LIDTPG-H----------VDFtyeVSRSLAACEGAILVVDAAQGIEAQtlanvylalDND-LELLP--------VVNKID 143
Cdd:COG1159 55 FVDTPGiHkpkrklgrrmNKA---AWSALEDVDVILFVVDATEKIGEG---------DEFiLELLKklktpvilVINKID 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1080759641 144 LpaADPERVKQEIEDVIGL-DQDDVVLASAKSNIGIEEILEKIVEVVppPEGDP 196
Cdd:COG1159 123 L--VKKEELLPLLAEYSELlDFAEIVPISALKGDNVDELLDEIAKLL--PEGPP 172
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
15-193 |
3.79e-06 |
|
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.
Pssm-ID: 206675 [Multi-domain] Cd Length: 197 Bit Score: 48.03 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 15 NFSIIAHIDHGKSTLAdRILENTKSVETREmqsqlldsmdlERERGITIKL---NA-VRLKYEAKDGKNYI--------- 81
Cdd:cd01888 2 NIGTIGHVAHGKTTLV-KALSGVWTVRHKE-----------ELKRNITIKLgyaNAkIYKCPNCGCPRPYDtpececpgc 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 82 ---------FHLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGI-EAQTLANVyLALDN-DLELLPVV-NKIDLpaADP 149
Cdd:cd01888 70 ggetklvrhVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPCpQPQTSEHL-AALEImGLKHIIILqNKIDL--VKE 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1080759641 150 ER-------VKQEIEDVIGLDQdDVVLASAKSNIGIEEILEKIVEVVPPPE 193
Cdd:cd01888 147 EQalenyeqIKEFVKGTIAENA-PIIPISAQLKYNIDVLCEYIVKKIPTPP 196
|
|
| YqeH |
cd01855 |
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ... |
138-185 |
6.82e-06 |
|
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases.
Pssm-ID: 206748 [Multi-domain] Cd Length: 191 Bit Score: 46.87 E-value: 6.82e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1080759641 138 VVNKIDL--PAADPERVKQEIEDVI---GLDQDDVVLASAKSNIGIEEILEKI 185
Cdd:cd01855 66 VGNKIDLlpKDVKPNRLKQWVKKRLkigGLKIKDVILVSAKKGWGVEELIEEI 118
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
84-196 |
8.15e-06 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 48.12 E-value: 8.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 84 LIDTPG-H----------VDFtyeVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLpAADPERV 152
Cdd:PRK00089 57 FVDTPGiHkpkralnramNKA---AWSSLKDVDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDL-VKDKEEL 132
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1080759641 153 KQEIEDVIGL-DQDDVVLASAKSNIGIEEILEKIVEVVppPEGDP 196
Cdd:PRK00089 133 LPLLEELSELmDFAEIVPISALKGDNVDELLDVIAKYL--PEGPP 175
|
|
| HflX |
cd01878 |
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
108-189 |
1.13e-05 |
|
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: 46.68 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 108 ILVVDAAQGIEAQTLANVyLALDNDLEL-----LPVVNKIDLpaADPERVKQEIEDviglDQDDVVLASAKSNIGIEEIL 182
Cdd:cd01878 125 LHVVDASDPDREEQIETV-EEVLKELGAddipiILVLNKIDL--LDDEELEERLRA----GRPDAVFISAKTGEGLDLLK 197
|
....*..
gi 1080759641 183 EKIVEVV 189
Cdd:cd01878 198 EAIEELL 204
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
69-204 |
1.22e-05 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 48.10 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 69 RLKYEAK-DGKNyiFHLIDTPGHVD-----FTYEVSR-SLAACEGA---ILVVDAAQGIeaqtlanvyLALDNDL-ELL- 136
Cdd:COG1160 40 RIYGEAEwGGRE--FTLIDTGGIEPddddgLEAEIREqAELAIEEAdviLFVVDGRAGL---------TPLDEEIaKLLr 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080759641 137 ----PV---VNKIDLPAADpervkQEIEDVIGLDQDDVVLASAKSNIGIEEILEKIVEVVPPP--EGDPSEPLK-ALI 204
Cdd:COG1160 109 rsgkPVilvVNKVDGPKRE-----ADAAEFYSLGLGEPIPISAEHGRGVGDLLDAVLELLPEEeeEEEEDDPIKiAIV 181
|
|
| Srp102 |
COG2229 |
Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, ... |
77-189 |
1.42e-05 |
|
Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 441830 [Multi-domain] Cd Length: 189 Bit Score: 45.97 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 77 GKNYIFHLIDTPGHV--DFTYE--VSRSLaaceGAILVVDaAQGIEAQTLANVYLALDNDLELLPVV---NKIDLPAADP 149
Cdd:COG2229 67 GDGLRLHLFGTPGQVrfDFMWDilLRGAD----GVVFLAD-SRRLEDSFNAESLDFFEERLEKLPFVvavNKRDLPDALS 141
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1080759641 150 ErvkQEIEDVIGLDQD-DVVLASAKSNIGIEEILEKIVEVV 189
Cdd:COG2229 142 L---EELREALDLGPDvPVVEADARDGESVKETLIALLELV 179
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
17-182 |
2.22e-05 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 47.48 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 17 SIIAHIDHGKSTLADRIlENTkSVETREmqsqlldsmdlerERGIT-------IKLNAVrlKYEAKDGKNYI-------- 81
Cdd:PRK04004 10 VVLGHVDHGKTTLLDKI-RGT-AVAAKE-------------AGGITqhigateVPIDVI--EKIAGPLKKPLpiklkipg 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 82 FHLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANvylaldndLELL-----PVV---NKID-LP------- 145
Cdd:PRK04004 73 LLFIDTPGHEAFTNLRKRGGALADIAILVVDINEGFQPQTIEA--------INILkrrktPFVvaaNKIDrIPgwksted 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080759641 146 -------AADPERVKQEIEDVI----------GLDQD------------DVVLASAKSNIGIEEIL 182
Cdd:PRK04004 145 apflesiEKQSQRVQQELEEKLyeligqlselGFSADrfdrvkdftktvAIVPVSAKTGEGIPDLL 210
|
|
| YihA_EngB |
cd01876 |
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
82-187 |
3.17e-05 |
|
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.
Pssm-ID: 206665 [Multi-domain] Cd Length: 170 Bit Score: 44.81 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 82 FHLIDTPG----------HVDFTYEVSRSLAACE---GAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKID-LPAA 147
Cdd:cd01876 47 FRLVDLPGygyakvskevREKWGKLIEEYLENREnlkGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADkLKKS 126
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1080759641 148 DPERVKQEIEDVIGLDQDD--VVLASAKSNIGIEEILEKIVE 187
Cdd:cd01876 127 ELAKVLKKIKEELNLFNILppVILFSSKKGTGIDELRALIAE 168
|
|
| Tet_C |
cd03711 |
Tet_C: C-terminus of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology ... |
410-487 |
4.91e-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: 41.84 E-value: 4.91e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080759641 410 EPYVRATMMVPNDYVGAVMELCQRKRGQFINMdYLDDIRVNIIYEIPLSEVVfDFFDQLKSNTKGYASFDYELIGYKE 487
Cdd:cd03711 1 EPYLRFELEVPQDALGRAMSDLAKMGATFEDP-QIKGDEVTLEGTIPVATSQ-DYQSELPSYTHGEGVLETEFKGYRP 76
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
5-232 |
5.44e-05 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 46.15 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 5 ERLNRQENIrNFSIIAHIDHGKSTLAdRILENTKSVETREmqsqlldsmdlERERGITIKL---NAVRLK---------- 71
Cdd:PTZ00327 27 EVISRQATI-NIGTIGHVAHGKSTVV-KALSGVKTVRFKR-----------EKVRNITIKLgyaNAKIYKcpkcprptcy 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 72 --YEAKDGKNYI-------------FHLIDTPGHvDFTYEVSRSLAAC-EGAILVVDAAQGI-EAQTL----ANVYLALD 130
Cdd:PTZ00327 94 qsYGSSKPDNPPcpgcghkmtlkrhVSFVDCPGH-DILMATMLNGAAVmDAALLLIAANESCpQPQTSehlaAVEIMKLK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 131 NdleLLPVVNKIDL-PAADPERVKQEIEDVI-GLDQDD--VVLASAKSNIGIEEILEKIVEVVPPPEGDPSEPLKALI-- 204
Cdd:PTZ00327 173 H---IIILQNKIDLvKEAQAQDQYEEIRNFVkGTIADNapIIPISAQLKYNIDVVLEYICTQIPIPKRDLTSPPRMIVir 249
|
250 260 270
....*....|....*....|....*....|....
gi 1080759641 205 -FD-----SEYDAYRGVISSIRIMDGVVKAGDKI 232
Cdd:PTZ00327 250 sFDvnkpgEDIENLKGGVAGGSILQGVLKVGDEI 283
|
|
| Rab |
cd00154 |
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ... |
76-187 |
2.71e-04 |
|
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases form the largest family within the Ras superfamily. There are at least 60 Rab genes in the human genome, and a number of Rab GTPases are conserved from yeast to humans. Rab GTPases are small, monomeric proteins that function as molecular switches to regulate vesicle trafficking pathways. The different Rab GTPases are localized to the cytosolic face of specific intracellular membranes, where they regulate distinct steps in membrane traffic pathways. In the GTP-bound form, Rab GTPases recruit specific sets of effector proteins onto membranes. Through their effectors, Rab GTPases regulate vesicle formation, actin- and tubulin-dependent vesicle movement, and membrane fusion. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which mask C-terminal lipid binding and promote cytosolic localization. While most unicellular organisms possess 5-20 Rab members, several have been found to possess 60 or more Rabs; for many of these Rab isoforms, homologous proteins are not found in other organisms. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Since crystal structures often lack C-terminal residues, the lipid modification site is not available for annotation in many of the CDs in the hierarchy, but is included where possible.
Pssm-ID: 206640 [Multi-domain] Cd Length: 159 Bit Score: 41.67 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 76 DGKNYIFHLIDTPGHvdftyEVSRSLAA-----CEGAILVVDaaqGIEAQTLANVY----LALDNDLELLPVV---NKID 143
Cdd:cd00154 45 DGKKVKLQIWDTAGQ-----ERFRSITSsyyrgAHGAILVYD---VTNRESFENLDkwlnELKEYAPPNIPIIlvgNKSD 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1080759641 144 LPAadpERV--KQEIEDVIGLDQDDVVLASAKSNIGIEEILEKIVE 187
Cdd:cd00154 117 LED---ERQvsTEEAQQFAKENGLLFFETSAKTGENVDEAFESLAR 159
|
|
| mtEFG2_II_like |
cd04092 |
Domain II of mitochondrial elongation factor G2-like proteins found in eukaryotes; Eukaryotic ... |
202-283 |
3.51e-04 |
|
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: 39.61 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 202 ALIFDSEYDAYRGVISSIRIMDGVVKAGDKIKMMATGKEFEVTE-VGINTPKQLPVEELTVGDVGyIIASIKNVddsRVG 280
Cdd:cd04092 3 ALAFKVIHDPQRGPLVFVRVYSGTLKAGSNVYNTTTGKKERISRlLKMHADQTEEVDSLSAGNIG-VITGLKVT---STG 78
|
...
gi 1080759641 281 DTI 283
Cdd:cd04092 79 DTL 81
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
84-187 |
3.77e-04 |
|
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.
Pssm-ID: 206726 [Multi-domain] Cd Length: 168 Bit Score: 41.68 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 84 LIDTPG-HVDFT-------YEVSRSLAACEGAILVVDAAQGIEAQTlANVYLAL-DNDLELLPVVNKIDLpAADPERVKQ 154
Cdd:cd04163 55 FVDTPGiHKPKKklgermvKAAWSALKDVDLVLFVVDASEWIGEGD-EFILELLkKSKTPVILVLNKIDL-VKDKEDLLP 132
|
90 100 110
....*....|....*....|....*....|....
gi 1080759641 155 EIEDVIGLDQ-DDVVLASAKSNIGIEEILEKIVE 187
Cdd:cd04163 133 LLEKLKELHPfAEIFPISALKGENVDELLEYIVE 166
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
126-185 |
4.27e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 42.00 E-value: 4.27e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080759641 126 YLAL--DNDLELLPVVNKIDLpaADPERVKQEIEDV--IGLDqddVVLASAKSNIGIEEILEKI 185
Cdd:cd01854 25 YLVAaeASGIEPVIVLNKADL--VDDEELEELLEIYekLGYP---VLAVSAKTGEGLDELRELL 83
|
|
| Arf_Arl |
cd00878 |
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ... |
25-187 |
4.45e-04 |
|
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl (Arf-like) small GTPases. Arf proteins are activators of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. Arfs are N-terminally myristoylated. Members of the Arf family are regulators of vesicle formation in intracellular traffic that interact reversibly with membranes of the secretory and endocytic compartments in a GTP-dependent manner. They depart from other small GTP-binding proteins by a unique structural device, interswitch toggle, that implements front-back communication from N-terminus to the nucleotide binding site. Arf-like (Arl) proteins are close relatives of the Arf, but only Arl1 has been shown to function in membrane traffic like the Arf proteins. Arl2 has an unrelated function in the folding of native tubulin, and Arl4 may function in the nucleus. Most other Arf family proteins are so far relatively poorly characterized. Thus, despite their significant sequence homologies, Arf family proteins may regulate unrelated functions.
Pssm-ID: 206644 [Multi-domain] Cd Length: 158 Bit Score: 41.02 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 25 GKSTLADRILENtKSVETRemqsqlldsmdlerergITIKLNAVRLKYeakdgKNYIFHLIDTPGHVDFtyevsRSL--- 101
Cdd:cd00878 11 GKTTILYKLKLG-EVVTTI-----------------PTIGFNVETVEY-----KNVKFTVWDVGGQDKI-----RPLwkh 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 102 --AACEGAILVVDAA---QGIEAQT-LANVYLALDN-DLELLPVVNKIDLPAADPErvkQEIEDVIGLDQDD-----VVL 169
Cdd:cd00878 63 yyENTDGLIFVVDSSdreRIEEAKNeLHKLLNEEELkGAPLLILANKQDLPGALTE---SELIELLGLESIKgrrwhIQP 139
|
170
....*....|....*...
gi 1080759641 170 ASAKSNIGIEEILEKIVE 187
Cdd:cd00878 140 CSAVTGDGLDEGLDWLIE 157
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
82-204 |
4.86e-04 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 42.73 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 82 FHLIDTPGHV----DFTYEVSR-SLAACEGA---ILVVDAAQGIEAQ--TLAN--------VYLaldndlellpVVNKID 143
Cdd:PRK00093 51 FILIDTGGIEpdddGFEKQIREqAELAIEEAdviLFVVDGRAGLTPAdeEIAKilrksnkpVIL----------VVNKVD 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080759641 144 LPAADpervkQEIEDVIGLDQDDVVLASAKSNIGIEEILEKIVEVVPPPEGDPSE--PLK-ALI 204
Cdd:PRK00093 121 GPDEE-----ADAYEFYSLGLGEPYPISAEHGRGIGDLLDAILEELPEEEEEDEEdePIKiAII 179
|
|
| mtEFG1_C |
cd04097 |
mtEFG1_C: C-terminus of mitochondrial Elongation factor G1 (mtEFG1)-like proteins found in ... |
410-485 |
5.33e-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: 5.33e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080759641 410 EPYVRATMMVPNDYVGAVMELCQRKRGQFINMDYLDDiRVNIIYEIPLSEvVFDFFDQLKSNTKGYASFDYELIGY 485
Cdd:cd04097 1 EPIMKVEVTAPTEFQGNVIGLLNKRKGTIVDTDTGED-EFTLEAEVPLND-MFGYSTELRSMTQGKGEFSMEFSRY 74
|
|
| SR_beta |
cd04105 |
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ... |
75-190 |
2.97e-03 |
|
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms the heterodimeric signal recognition particle (SRP); Signal recognition particle receptor, beta subunit (SR-beta). SR-beta and SR-alpha form the heterodimeric signal recognition particle (SRP or SR) receptor that binds SRP to regulate protein translocation across the ER membrane. Nascent polypeptide chains are synthesized with an N-terminal hydrophobic signal sequence that binds SRP54, a component of the SRP. SRP directs targeting of the ribosome-nascent chain complex (RNC) to the ER membrane via interaction with the SR, which is localized to the ER membrane. The RNC is then transferred to the protein-conducting channel, or translocon, which facilitates polypeptide translation across the ER membrane or integration into the ER membrane. SR-beta is found only in eukaryotes; it is believed to control the release of the signal sequence from SRP54 upon binding of the ribosome to the translocon. High expression of SR-beta has been observed in human colon cancer, suggesting it may play a role in the development of this type of cancer.
Pssm-ID: 206691 [Multi-domain] Cd Length: 202 Bit Score: 39.23 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 75 KDGKNYIFHLIDTPGHVDFTYEVSRSL-AACEGAILVVDAA---QGIE--AQTLANVYLALDNDLELLPVV---NKIDLP 145
Cdd:cd04105 42 NSSKGKKLTLVDVPGHEKLRDKLLEYLkASLKAIVFVVDSAtfqKNIRdvAEFLYDILTDLEKIKNKIPILiacNKQDLF 121
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080759641 146 AA-DPERVKQEIE------------DVIGLDQDDVVLASAKSNIGI---EEILEKIVEVVP 190
Cdd:cd04105 122 TAkPAKKIKELLEkeintlresrskSLESLDGDDGSKDTLGDKGGKdfeFDQLEGEVDFVE 182
|
|
| Obg |
cd01898 |
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ... |
138-189 |
3.57e-03 |
|
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress response, chromosome partitioning, replication initiation, mycelium development, and sporulation. Obg proteins are among a large group of GTP binding proteins conserved from bacteria to humans. The E. coli homolog, ObgE is believed to function in ribosomal biogenesis. Members of the subfamily contain two equally and highly conserved domains, a C-terminal GTP binding domain and an N-terminal glycine-rich domain.
Pssm-ID: 206685 [Multi-domain] Cd Length: 170 Bit Score: 38.56 E-value: 3.57e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1080759641 138 VVNKIDLPAADP--ERVKQEIEdviGLDQDDVVLASAKSNIGIEEILEKIVEVV 189
Cdd:cd01898 120 VLNKIDLLDAEErfEKLKELLK---ELKGKKVFPISALTGEGLDELLKKLAKLL 170
|
|
| Tet_II |
cd03690 |
Domain II of ribosomal protection proteins Tet(M) and Tet(O); This subfamily represents domain ... |
197-283 |
3.82e-03 |
|
Domain II of ribosomal protection proteins Tet(M) and Tet(O); This subfamily represents domain II of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology to domain II of the elongation factors EF-G and EF-2. Tet(M) and Tet(O) catalyze the release of tetracycline (Tc) from the ribosome in a GTP-dependent manner thereby mediating Tc resistance. Tcs are broad-spectrum antibiotics. Typical Tcs bind to the ribosome and inhibit the elongation phase of protein synthesis, by inhibiting the occupation of site A by aminoacyl-tRNA.
Pssm-ID: 293891 [Multi-domain] Cd Length: 86 Bit Score: 36.83 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 197 SEPLKALIFDSEYDAYRGVISSIRIMDGVVKAGDKIKMMATGKEFEVTEV-GINTPKQLPVEELTVGDvgyiIASIKNVD 275
Cdd:cd03690 1 ESELSGTVFKIEYDPKGERLAYLRLYSGTLRLRDSVRVSGEEEKIKITELrTFENGELVKVDRVYAGD----IAILVGLK 76
|
....*...
gi 1080759641 276 DSRVGDTI 283
Cdd:cd03690 77 SLRVGDVL 84
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
25-141 |
4.63e-03 |
|
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: 37.21 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 25 GKSTLADRILeNTKSVETREMqsqlldsmdlererGITIKLNAVRLKYeakdgKNYIFHLIDTPGHVD---FTYEVSRSL 101
Cdd:pfam01926 11 GKSTLINALT-GAKAIVSDYP--------------GTTRDPNEGRLEL-----KGKQIILVDTPGLIEgasEGEGLGRAF 70
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1080759641 102 AA---CEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNK 141
Cdd:pfam01926 71 LAiieADLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
|
|
| eEF2_snRNP_like_C |
cd04096 |
eEF2_snRNP_like_C: this family represents a C-terminal domain of eukaryotic elongation factor ... |
410-480 |
4.77e-03 |
|
eEF2_snRNP_like_C: this family represents a C-terminal domain of eukaryotic elongation factor 2 (eEF-2) and a homologous domain of the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and, its yeast counterpart Snu114p. Yeast Snu114p is essential for cell viability and for splicing in vivo. U5-116 kD binds GTP. Experiments suggest that GTP binding and probably GTP hydrolysis is important for the function of the U5-116 kD/Snu114p. In complex with GTP, EF-2 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.
Pssm-ID: 239763 [Multi-domain] Cd Length: 80 Bit Score: 36.36 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 410 EPYVRATMMVPNDYVGAVMELCQRKRGQFINmdylDDIRV-NIIYEI----PLSEvVFDFFDQLKSNTKGYAS----FDY 480
Cdd:cd04096 1 EPIYLVEIQCPEDALGKVYSVLSKRRGHVLS----EEPKEgTPLFEIkaylPVIE-SFGFETDLRSATSGQAFpqlvFSH 75
|
|
| obgE |
PRK12299 |
GTPase CgtA; Reviewed |
108-189 |
4.83e-03 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237048 [Multi-domain] Cd Length: 335 Bit Score: 39.28 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 108 ILVVDAAQGI---EAQTLANVYLALDNDLELLP---VVNKIDLPAADPERvKQEIEDVIGLDQDDVVLASAKSNIGIEEI 181
Cdd:PRK12299 241 LHLVDIEAVDpveDYKTIRNELEKYSPELADKPrilVLNKIDLLDEEEER-EKRAALELAALGGPVFLISAVTGEGLDEL 319
|
....*...
gi 1080759641 182 LEKIVEVV 189
Cdd:PRK12299 320 LRALWELL 327
|
|
| EngA1 |
cd01894 |
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
82-187 |
7.85e-03 |
|
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206681 [Multi-domain] Cd Length: 157 Bit Score: 37.41 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080759641 82 FHLIDTPGHVDFTYEVSR-----SLAACEGA---ILVVDAAQGIeaqTLANVYLAldndlELL-----P---VVNKIDLP 145
Cdd:cd01894 47 FILIDTGGIEPDDEGISKeireqAEIAIEEAdviLFVVDGREGL---TPADEEIA-----KYLrkskkPvilVVNKIDNI 118
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1080759641 146 AADpervkQEIEDVIGLDQDDVVLASAKSNIGIEEILEKIVE 187
Cdd:cd01894 119 KEE-----EEAAEFYSLGFGEPIPISAEHGRGIGDLLDAILE 155
|
|
| |
