|
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: 1269.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 9 RRENIRNFSIIAHIDHGKSTLADRILENTKSVETREMQDQLLDSMDLERERGITIKLNAVRLKYEAKDGETYTFHLIDTP 88
Cdd:COG0481 2 DQKNIRNFSIIAHIDHGKSTLADRLLELTGTLSEREMKEQVLDSMDLERERGITIKAQAVRLNYKAKDGETYQLNLIDTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 89 GHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLPAAEPDRVKQELEDVIGIDQEDVV 168
Cdd:COG0481 82 GHVDFSYEVSRSLAACEGALLVVDASQGVEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKQEIEDIIGIDASDAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 169 LASAKSNIGIEEILEKIVDVVPAPDGDPEAPLKALIFDSEYDPYRGVISSIRIIDGVVKAGDRIKMMATGKEFEVTEVGI 248
Cdd:COG0481 162 LVSAKTGIGIEEILEAIVERIPPPKGDPDAPLQALIFDSWYDSYRGVVVYVRVFDGTLKKGDKIKMMSTGKEYEVDEVGV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 249 NTPKQLPVEELTVGDVGYIIASIKNVDDSRVGDTITLAERPADKPLQGYKKMNPMVFCGLFPIDNKDYNDLREALEKLQL 328
Cdd:COG0481 242 FTPKMTPVDELSAGEVGYIIAGIKDVRDARVGDTITLAKNPAAEPLPGFKEVKPMVFAGLYPVDSDDYEDLRDALEKLQL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 329 NDASLEFEPESSQALGFGYRTGFLGMLHMEIIQERIEREFGIELIATAPSVIYQCILKDGSEVSVDNPAQMPERDKIEHI 408
Cdd:COG0481 322 NDASLTYEPETSAALGFGFRCGFLGLLHMEIIQERLEREFDLDLITTAPSVVYEVTLTDGEVIEVDNPSDLPDPGKIEEI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 409 YEPFVKATMMVPNDYVGAVMELCQRKRGQFINMDYLDDIRVNIVYEIPLSEVVFDFFDQLKSNTKGYASFDYEFIENKES 488
Cdd:COG0481 402 EEPIVKATIITPSEYVGAVMELCQEKRGVQKNMEYLGENRVELTYELPLAEIVFDFFDRLKSITRGYASLDYEFIGYRES 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 489 NLVKMDILLNGDKVDALSFIVHRDFAYERGKALVEKLKTLIPRQQFEVPVQAAIGQKIVARTNIKSMGKNVLSKCYGGDI 568
Cdd:COG0481 482 DLVKLDILINGEPVDALSFIVHRDKAYSRGRALVEKLKELIPRQQFEVPIQAAIGGKIIARETIKALRKDVLAKCYGGDI 561
|
570 580 590
....*....|....*....|....*....|....*..
gi 487749293 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: 1096.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 11 ENIRNFSIIAHIDHGKSTLADRILENTKSVETREMQDQLLDSMDLERERGITIKLNAVRLKYEAKDGETYTFHLIDTPGH 90
Cdd:TIGR01393 1 KNIRNFSIIAHIDHGKSTLADRLLEYTGAISEREMREQVLDSMDLERERGITIKAQAVRLNYKAKDGETYVLNLIDTPGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 91 VDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLPAAEPDRVKQELEDVIGIDQEDVVLA 170
Cdd:TIGR01393 81 VDFSYEVSRSLAACEGALLLVDAAQGIEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKKEIEEVIGLDASEAILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 171 SAKSNIGIEEILEKIVDVVPAPDGDPEAPLKALIFDSEYDPYRGVISSIRIIDGVVKAGDRIKMMATGKEFEVTEVGINT 250
Cdd:TIGR01393 161 SAKTGIGIEEILEAIVKRVPPPKGDPDAPLKALIFDSHYDNYRGVVALVRVFEGTIKPGDKIRFMSTGKEYEVDEVGVFT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 251 PKQLPVEELTVGDVGYIIASIKNVDDSRVGDTITLAERPADKPLQGYKKMNPMVFCGLFPIDNKDYNDLREALEKLQLND 330
Cdd:TIGR01393 241 PKLTKTDELSAGEVGYIIAGIKDVSDVRVGDTITHVKNPAKEPLPGFKEVKPMVFAGLYPIDTEDYEDLRDALEKLKLND 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 331 ASLEFEPESSQALGFGYRTGFLGMLHMEIIQERIEREFGIELIATAPSVIYQCILKDGSEVSVDNPAQMPERDKIEHIYE 410
Cdd:TIGR01393 321 ASLTYEPESSPALGFGFRCGFLGLLHMEIIQERLEREFNLDLITTAPSVIYRVYLTNGEVIEVDNPSDLPDPGKIEHVEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 411 PFVKATMMVPNDYVGAVMELCQRKRGQFINMDYLDDIRVNIVYEIPLSEVVFDFFDQLKSNTKGYASFDYEFIENKESNL 490
Cdd:TIGR01393 401 PYVKATIITPTEYLGPIMTLCQEKRGVQTNMEYLDPNRVELIYEMPLAEIVYDFFDKLKSISRGYASFDYELIGYRPSDL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 491 VKMDILLNGDKVDALSFIVHRDFAYERGKALVEKLKTLIPRQQFEVPVQAAIGQKIVARTNIKSMGKNVLSKCYGGDISR 570
Cdd:TIGR01393 481 VKLDILINGEPVDALSFIVHRDKAYSRGREICEKLKELIPRQQFEIPIQAAIGGKIIARETIKALRKDVTAKCYGGDITR 560
|
570 580 590
....*....|....*....|....*....|....*
gi 487749293 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 |
5.65e-123 |
|
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: 360.31 E-value: 5.65e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 14 RNFSIIAHIDHGKSTLADRILENTKSVETREMQDQLLDSMDLERERGITIKLNAVRLKYEAKDGETYTFHLIDTPGHVDF 93
Cdd:cd01890 1 RNFSIIAHIDHGKSTLADRLLELTGTVSEREMKEQVLDSMDLERERGITIKAQAVRLFYKAKDGEEYLLNLIDTPGHVDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 94 TYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLPAAEPDRVKQELEDVIGIDQEDVVLASAK 173
Cdd:cd01890 81 SYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVKQEIEDVLGLDASEAILVSAK 160
|
170
....*....|....*....
gi 487749293 174 SNIGIEEILEKIVDVVPAP 192
Cdd:cd01890 161 TGLGVEDLLEAIVERIPPP 179
|
|
| LepA_C |
pfam06421 |
GTP-binding protein LepA C-terminus; This family consists of the C-terminal region of several ... |
497-603 |
2.04e-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: 222.28 E-value: 2.04e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 497 LNGDKVDALSFIVHRDFAYERGKALVEKLKTLIPRQQFEVPVQAAIGQKIVARTNIKSMGKNVLSKCYGGDISRKRKLLE 576
Cdd:pfam06421 1 INGEPVDALSFIVHRSKAYRRGRALVEKLKELIPRQQFEVPIQAAIGGKIIARETIKALRKDVTAKCYGGDISRKKKLLE 80
|
90 100
....*....|....*....|....*..
gi 487749293 577 KQKAGKAKMKAVGNVEIPQDAFLAVLK 603
Cdd:pfam06421 81 KQKEGKKRMKQIGNVEIPQEAFLAVLK 107
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
8-456 |
5.07e-70 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 237.61 E-value: 5.07e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 8 NRRENIRNFSIIAHIDHGKSTLADRILENTKSVETRE-MQDQLLDSMDLERERGITI--KLNAVRLKyeakdgeTYTFHL 84
Cdd:COG1217 1 MMREDIRNIAIIAHVDHGKTTLVDALLKQSGTFRENQeVAERVMDSNDLERERGITIlaKNTAVRYK-------GVKINI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 85 IDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQT---LANvylALDNDLELLPVVNKIDLPAAEPDRVKQELEDV-- 159
Cdd:COG1217 74 VDTPGHADFGGEVERVLSMVDGVLLLVDAFEGPMPQTrfvLKK---ALELGLKPIVVINKIDRPDARPDEVVDEVFDLfi 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 160 -IGIDQED----VVLASAKSNI----------GIEEILEKIVDVVPAPDGDPEAPLKALIFDSEYDPYRGVISSIRIIDG 224
Cdd:COG1217 151 eLGATDEQldfpVVYASARNGWasldlddpgeDLTPLFDTILEHVPAPEVDPDGPLQMLVTNLDYSDYVGRIAIGRIFRG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 225 VVKAGDRIKMMATG---KEFEVTEV----GIntpKQLPVEELTVGDvgyIIAsIKNVDDSRVGDTITLAERPadKPLQGY 297
Cdd:COG1217 231 TIKKGQQVALIKRDgkvEKGKITKLfgfeGL---ERVEVEEAEAGD---IVA-IAGIEDINIGDTICDPENP--EALPPI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 298 K------KMNPMV----FCGlfpidnKD--Y---NDLREALEKLQLNDASLEFEPESSqalgfgyRTGFL----GMLHME 358
Cdd:COG1217 302 KideptlSMTFSVndspFAG------REgkFvtsRQIRERLEKELETNVALRVEETDS-------PDAFKvsgrGELHLS 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 359 IIQERIEREfGIELIATAPSVIYQCIlkDGsevsvdnpaqmperdkieHIYEPFVKATMMVPNDYVGAVMELCQRKRGQF 438
Cdd:COG1217 369 ILIETMRRE-GYELQVSRPEVIFKEI--DG------------------KKLEPIEELTIDVPEEYSGAVIEKLGQRKGEM 427
|
490
....*....|....*...
gi 487749293 439 INMDYLDDIRVNIVYEIP 456
Cdd:COG1217 428 TNMEPDGGGRVRLEFLIP 445
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
11-191 |
2.47e-67 |
|
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: 217.39 E-value: 2.47e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 11 ENIRNFSIIAHIDHGKSTLADRILENTKSVETREMQDQ----LLDSMDLERERGITIKLNAVRLkyeakDGETYTFHLID 86
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGegeaGLDNLPEERERGITIKSAAVSF-----ETKDYLINLID 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 87 TPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLPA-AEPDRVKQELEDVIGIDQE 165
Cdd:pfam00009 76 TPGHVDFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDgAELEEVVEEVSRELLEKYG 155
|
170 180 190
....*....|....*....|....*....|..
gi 487749293 166 D------VVLASAKSNIGIEEILEKIVDVVPA 191
Cdd:pfam00009 156 EdgefvpVVPGSALKGEGVQTLLDALDEYLPS 187
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
11-482 |
2.28e-60 |
|
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: 212.98 E-value: 2.28e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 11 ENIRNFSIIAHIDHGKSTLADRILENTK------SVE--TREMqdqllDSMDLERERGITIKLNAVRLKYeaKDgetYTF 82
Cdd:COG0480 7 EKIRNIGIVAHIDAGKTTLTERILFYTGaihrigEVHdgNTVM-----DWMPEEQERGITITSAATTCEW--KG---HKI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 83 HLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLPAAEPDRVKQELEDVIG- 161
Cdd:COG0480 77 NIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQLKERLGa 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 162 --------IDQED------------------------------------------------------------------- 166
Cdd:COG0480 157 npvplqlpIGAEDdfkgvidlvtmkayvyddelgakyeeeeipaelkeeaeeareelieavaetddelmekylegeelte 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 167 ------------------VVLASAKSNIGIEEILEKIVDVVPAPD-------------------GDPEAPLKALIFDSEY 209
Cdd:COG0480 237 eeikaglrkatlagkivpVLCGSAFKNKGVQPLLDAVVDYLPSPLdvpaikgvdpdtgeeverkPDDDEPFSALVFKTMT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 210 DPYRGVISSIRIIDGVVKAGDRIKMMATGKEFEVTevGINTP---KQLPVEELTVGDvgyIIASIKnVDDSRVGDTITLA 286
Cdd:COG0480 317 DPFVGKLSFFRVYSGTLKSGSTVYNSTKGKKERIG--RLLRMhgnKREEVDEAGAGD---IVAVVK-LKDTTTGDTLCDE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 287 ERPAdkPLQGYKKMNPMVFCGLFPIDNKDYNDLREALEKLQLNDASLEFE--PESSQALGFGyrtgfLGMLHMEIIQERI 364
Cdd:COG0480 391 DHPI--VLEPIEFPEPVISVAIEPKTKADEDKLSTALAKLAEEDPTFRVEtdEETGQTIISG-----MGELHLEIIVDRL 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 365 EREFGIELIATAPSVIY--------------------------------------------------------------- 381
Cdd:COG0480 464 KREFGVEVNVGKPQVAYretirkkaeaegkhkkqsgghgqygdvwieieplprgegfefvdkivggvipkeyipavekgi 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 382 -----------------QCILKDGSEVSVD-NP------AQMPERDKIEH----IYEPFVKATMMVPNDYVGAVMELCQR 433
Cdd:COG0480 544 reamekgvlagypvvdvKVTLYDGSYHPVDsSEmafkiaASMAFKEAAKKakpvLLEPIMKVEVTVPEEYMGDVMGDLNS 623
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 487749293 434 KRGQFINMDYLDDIRVnIVYEIPLSEvVFDFFDQLKSNTKGYASFDYEF 482
Cdd:COG0480 624 RRGRILGMESRGGAQV-IKAEVPLAE-MFGYATDLRSLTQGRGSFTMEF 670
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
19-482 |
2.19e-57 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 204.59 E-value: 2.19e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 19 IAHIDHGKSTLADRILENTKSVETR---EMQDQLLDSMDLERERGITIKLNAVRLKYeaKDgetYTFHLIDTPGHVDFTY 95
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRIgevEDGTTTMDFMPEERERGISITSAATTCEW--KG---HKINLIDTPGHVDFTG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 96 EVSRSLAACEGAILVVDAAQGIEAQTLAnvYLALDNDLEL--LPVVNKIDLPAAEPDRVKQELEDVIG---------IDQ 164
Cdd:PRK12740 76 EVERALRVLDGAVVVVCAVGGVEPQTET--VWRQAEKYGVprIIFVNKMDRAGADFFRVLAQLQEKLGapvvplqlpIGE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 165 ED------------------------------------------------------------------------------ 166
Cdd:PRK12740 154 GDdftgvvdllsmkayrydeggpseeieipaelldraeeareellealaefddelmekylegeelseeeikaglrkatla 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 167 -----VVLASAKSNIGIEEILEKIVDVVPAPD-----------------GDPEAPLKALIFDSEYDPYRGVISSIRIIDG 224
Cdd:PRK12740 234 geivpVFCGSALKNKGVQRLLDAVVDYLPSPLevppvdgedgeegaelaPDPDGPLVALVFKTMDDPFVGKLSLVRVYSG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 225 VVKAGDRIKMMATGKEFEVTevGINTP---KQLPVEELTVGDvgyIIASIKnVDDSRVGDTITLAERPAdkplqgykKMN 301
Cdd:PRK12740 314 TLKKGDTLYNSGTGKKERVG--RLYRMhgkQREEVDEAVAGD---IVAVAK-LKDAATGDTLCDKGDPI--------LLE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 302 PMVFC------GLFPIDNKDYNDLREALEKLQLNDASLEFE--PESSQALGFGyrtgfLGMLHMEIIQERIEREFGIELI 373
Cdd:PRK12740 380 PMEFPepvislAIEPKDKGDEEKLSEALGKLAEEDPTLRVErdEETGQTILSG-----MGELHLDVALERLKREYGVEVE 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 374 ATAPSVIYQ----------------------------------------------------------------------- 382
Cdd:PRK12740 455 TGPPQVPYRetirkkaeghgrhkkqsgghgqfgdvwleveplprgegfefvdkvvggavprqyipavekgvrealekgvl 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 383 ---------CILKDGSEVSVDN-------PAQMPERDKIE----HIYEPFVKATMMVPNDYVGAVMELCQRKRGQFINMD 442
Cdd:PRK12740 535 agypvvdvkVTLTDGSYHSVDSsemafkiAARLAFREALPkakpVLLEPIMKVEVSVPEEFVGDVIGDLSSRRGRILGME 614
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 487749293 443 YLDDIRVnIVYEIPLSEvVFDFFDQLKSNTKGYASFDYEF 482
Cdd:PRK12740 615 SRGGGDV-VRAEVPLAE-MFGYATDLRSLTQGRGSFSMEF 652
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
11-482 |
6.42e-57 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 203.64 E-value: 6.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 11 ENIRNFSIIAHIDHGKSTLADRILENTK------SVE--TREMqdqllDSMDLERERGITIKLNAVRLKYEakdgeTYTF 82
Cdd:PRK13351 6 MQIRNIGILAHIDAGKTTLTERILFYTGkihkmgEVEdgTTVT-----DWMPQEQERGITIESAATSCDWD-----NHRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 83 HLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLPAAEPDRVKQELEDVIG- 161
Cdd:PRK13351 76 NLIDTPGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLFKVLEDIEERFGk 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 162 ------------------------------------------IDQED--------------------------------- 166
Cdd:PRK13351 156 rplplqlpigsedgfegvvdlitepelhfsegdggstveegpIPEELleeveearekliealaefddellelylegeels 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 167 -------------------VVLASAKSNIGIEEILEKIVDVVPAP------------------DGDPEAPLKALIFDSEY 209
Cdd:PRK13351 236 aeqlraplregtrsghlvpVLFGSALKNIGIEPLLDAVVDYLPSPlevppprgskdngkpvkvDPDPEKPLLALVFKVQY 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 210 DPYRGVISSIRIIDGVVKAGDRIKMMATGKEFEVTE-VGINTPKQLPVEELTVGDvgyIIASIKnVDDSRVGDtiTLAER 288
Cdd:PRK13351 316 DPYAGKLTYLRVYSGTLRAGSQLYNGTGGKREKVGRlFRLQGNKREEVDRAKAGD---IVAVAG-LKELETGD--TLHDS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 289 PADKPLQGYKKMNPMVFCGLFPIDNKDYNDLREALEKLQLNDASLEFE--PESSQALGFGyrtgfLGMLHMEIIQERIER 366
Cdd:PRK13351 390 ADPVLLELLTFPEPVVSLAVEPERRGDEQKLAEALEKLVWEDPSLRVEedEETGQTILSG-----MGELHLEVALERLRR 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 367 EFGIELIATAPSVIYQCILKDGSE---------------------------------VSVDNPAQMPERDK--IEH---- 407
Cdd:PRK13351 465 EFKLEVNTGKPQVAYRETIRKMAEgvyrhkkqfggkgqfgevhlrveplergagfifVSKVVGGAIPEELIpaVEKgire 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 408 ----------------------------------------------------IYEPFVKATMMVPNDYVGAVMELCQRKR 435
Cdd:PRK13351 545 alasgplagypvtdlrvtvldgkyhpvdssesafkaaarkafleafrkanpvLLEPIMELEITVPTEHVGDVLGDLSQRR 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 487749293 436 GQFINMDYLDDIRVNIVYEIPLSEvVFDFFDQLKSNTKGYASFDYEF 482
Cdd:PRK13351 625 GRIEGTEPRGDGEVLVKAEAPLAE-LFGYATRLRSMTKGRGSFTMEF 670
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
11-507 |
1.20e-49 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 181.83 E-value: 1.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 11 ENIRNFSIIAHIDHGKSTLADRILENTKSVETR-EMQDQLLDSMDLERERGITIKLNAVRLKYEakdgeTYTFHLIDTPG 89
Cdd:PRK10218 3 EKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRaETQERVMDSNDLEKERGITILAKNTAIKWN-----DYRINIVDTPG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 90 HVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLPAAEPDRVKQELEDV-IGIDQED-- 166
Cdd:PRK10218 78 HADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLfVNLDATDeq 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 167 ----VVLASAKSNIG----------IEEILEKIVDVVPAPDGDPEAPLKALIFDSEYDPYRGVISSIRIIDGVVKAGDRI 232
Cdd:PRK10218 158 ldfpIVYASALNGIAgldhedmaedMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 233 KMMATGKEFEVTEVG-INTPKQLPVEELTVGDVGYIIAsIKNVDDSRVGDTI-------TLAERPADKP-LQGYKKMNPM 303
Cdd:PRK10218 238 TIIDSEGKTRNAKVGkVLGHLGLERIETDLAEAGDIVA-ITGLGELNISDTVcdtqnveALPALSVDEPtVSMFFCVNTS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 304 VFCGlfpiDNKDYNDLREALEKLQ---LNDASLEFEpESSQALGFgyRTGFLGMLHMEIIQERIEREfGIELIATAPSVI 380
Cdd:PRK10218 317 PFCG----KEGKFVTSRQILDRLNkelVHNVALRVE-ETEDADAF--RVSGRGELHLSVLIENMRRE-GFELAVSRPKVI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 381 YQCIlkDGSEvsvdnpaqmperdkiehiYEPFVKATMMVPNDYVGAVMELCQRKRGQFINMDYLDDIRVNIVYEIPlSEV 460
Cdd:PRK10218 389 FREI--DGRK------------------QEPYENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIP-SRG 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 487749293 461 VFDFFDQLKSNTKG----YASFD-YEFIENKESNLVKMDILLNGDKVDALSF 507
Cdd:PRK10218 448 LIGFRSEFMTMTSGtgllYSTFShYDDVRPGEVGQRQNGVLISNGQGKAVAF 499
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
15-192 |
1.71e-48 |
|
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: 167.09 E-value: 1.71e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 15 NFSIIAHIDHGKSTLADRILENTKSVETREM-QDQLLDSMDLERERGITIKLNAVRLKYEakdgeTYTFHLIDTPGHVDF 93
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTrKETFLDTLKEERERGITIKTGVVEFEWP-----KRRINFIDTPGHEDF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 94 TYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLPAAE-PDRVKQELEDVIGI--------DQ 164
Cdd:cd00881 76 SKETVRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGEEdFDEVLREIKELLKLigftflkgKD 155
|
170 180
....*....|....*....|....*...
gi 487749293 165 EDVVLASAKSNIGIEEILEKIVDVVPAP 192
Cdd:cd00881 156 VPIIPISALTGEGIEELLDAIVEHLPPP 183
|
|
| EF4_III |
cd16260 |
Domain III of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly ... |
302-377 |
3.67e-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: 159.59 E-value: 3.67e-47
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487749293 302 PMVFCGLFPIDNKDYNDLREALEKLQLNDASLEFEPESSQALGFGYRTGFLGMLHMEIIQERIEREFGIELIATAP 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 |
1.09e-45 |
|
Domain II of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly conserved guanosine triphosphatase found in bacteria and eukaryotic mitochondria and chloroplasts. EF4 functions as a translation factor, which promotes back-translocation of tRNAs on posttranslocational ribosome complexes and competes with elongation factor G for interaction with pretranslocational ribosomes, inhibiting the elongation phase of protein synthesis.
Pssm-ID: 293900 [Multi-domain] Cd Length: 86 Bit Score: 156.04 E-value: 1.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 200 LKALIFDSEYDPYRGVISSIRIIDGVVKAGDRIKMMATGKEFEVTEVGINTPKQLPVEELTVGDVGYIIASIKNVDDSRV 279
Cdd:cd03699 1 LRALIFDSWYDPYRGVVVLVRVFDGTLKKGDKIRFMATGKEYEVLEVGVFTPKMVPTDELSAGEVGYIIAGIKSVKDARV 80
|
....*.
gi 487749293 280 GDTITL 285
Cdd:cd03699 81 GDTITL 86
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
8-482 |
7.51e-45 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 170.04 E-value: 7.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 8 NRRENIRNFSIIAHIDHGKSTLADRILENTKSVETREMQDQL-LDSMDLERERGITIKLNAVRLKYEAKdGETYTFHLID 86
Cdd:PRK07560 15 KNPEQIRNIGIIAHIDHGKTTLSDNLLAGAGMISEELAGEQLaLDFDEEEQARGITIKAANVSMVHEYE-GKEYLINLID 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 87 TPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLPAAE----PDRVKQELEDVIG- 161
Cdd:PRK07560 94 TPGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKPVLFINKVDRLIKElkltPQEMQQRLLKIIKd 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 162 ------------------IDQED--VVLASAKSNIGI----------------------------------EEILEKIVD 187
Cdd:PRK07560 174 vnklikgmapeefkekwkVDVEDgtVAFGSALYNWAIsvpmmqktgikfkdiidyyekgkqkelaekaplhEVVLDMVVK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 188 VVPAP-------------------------DGDPEAPLKALIFDSEYDPYRGVISSIRIIDGVVKAGDRIKMMATGKEFE 242
Cdd:PRK07560 254 HLPNPieaqkyripkiwkgdlnsevgkamlNCDPNGPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLVGAKKKNR 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 243 VTEVGINT-PKQLPVEELTVGDvgyiIASIKNVDDSRVGDTI-TLAERPADKPLQGYKKmnPMVFCGLFPIDNKDYNDLR 320
Cdd:PRK07560 334 VQQVGIYMgPEREEVEEIPAGN----IAAVTGLKDARAGETVvSVEDMTPFESLKHISE--PVVTVAIEAKNPKDLPKLI 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 321 EALEKLQLNDASLEFE--PESSQALGFGyrtgfLGMLHMEIIQERIEREFGIELIATAPSVIYQCILKDGSEV------- 391
Cdd:PRK07560 408 EVLRQLAKEDPTLVVKinEETGEHLLSG-----MGELHLEVITYRIKRDYGIEVVTSEPIVVYRETVRGKSQVvegkspn 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 392 -------SV--------------DNPAQMPERD-------------------KIEHIY---------------------- 409
Cdd:PRK07560 483 khnrfyiSVepleeevieaikegEISEDMDKKEakilreklieagmdkdeakRVWAIYngnvfidmtkgiqylnevmeli 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 410 ---------------EPF-------------------------------VKATMM----------------VPNDYVGAV 427
Cdd:PRK07560 563 iegfreamkegplaaEPVrgvkvrlhdaklhedaihrgpaqvipavrnaIFAAMLtakptllepiqkvdinVPQDYMGAV 642
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 487749293 428 MELCQRKRGQFINMDYLDDIrVNIVYEIPLSEvVFDFFDQLKSNTKGYASFDYEF 482
Cdd:PRK07560 643 TREIQGRRGKILDMEQEGDM-AIIEAEAPVAE-MFGFAGEIRSATEGRALWSTEF 695
|
|
| lepA_C |
cd03709 |
lepA_C: This family represents the C-terminal region of LepA, a GTP-binding protein localized ... |
410-489 |
4.21e-44 |
|
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: 151.49 E-value: 4.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 410 EPFVKATMMVPNDYVGAVMELCQRKRGQFINMDYLDDIRVNIVYEIPLSEVVFDFFDQLKSNTKGYASFDYEFIENKESN 489
Cdd:cd03709 1 EPFVKATIITPSEYLGAIMELCQERRGVQKDMEYLDANRVMLTYELPLAEIVYDFFDKLKSISKGYASLDYELIGYRESD 80
|
|
| EF-G |
TIGR00484 |
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ... |
11-482 |
4.41e-43 |
|
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: 164.60 E-value: 4.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 11 ENIRNFSIIAHIDHGKSTLADRILENT-KSVETREMQD--QLLDSMDLERERGITIKLNAVRLKYEAkdgetYTFHLIDT 87
Cdd:TIGR00484 8 NRFRNIGISAHIDAGKTTTTERILFYTgRIHKIGEVHDgaATMDWMEQEKERGITITSAATTVFWKG-----HRINIIDT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 88 PGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLPAAEPDRVKQEL----------- 156
Cdd:TIGR00484 83 PGHVDFTVEVERSLRVLDGAVAVLDAVGGVQPQSETVWRQANRYEVPRIAFVNKMDKTGANFLRVVNQIkqrlganavpi 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 157 -------EDVIGI--------------------------------------------DQED------------------- 166
Cdd:TIGR00484 163 qlpigaeDNFIGVidlvemkayffngdkgtkaiekeipsdlleqakelrenlveavaEFDEelmekylegeeltieeikn 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 167 -------------VVLASAKSNIGIEEILEKIVDVVPAP-----------DGDPE--------APLKALIFDSEYDPYRG 214
Cdd:TIGR00484 243 airkgvlnceffpVLCGSAFKNKGVQLLLDAVVDYLPSPtdvpaikgidpDTEKEierkasddEPFSALAFKVATDPFVG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 215 VISSIRIIDGVVKAGDRIKMMATGKEFEVTE-VGINTPKQLPVEELTVGDvgyiIASIKNVDDSRVGDtiTLAERPADKP 293
Cdd:TIGR00484 323 QLTFVRVYSGVLKSGSYVKNSRKNKKERVGRlVKMHANNREEIKEVRAGD----ICAAIGLKDTTTGD--TLCDPKIDVI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 294 LQGYKKMNPMVFCGLFPIDNKDYNDLREALEKLQLNDASLEF--EPESSQALGFGyrtgfLGMLHMEIIQERIEREFGIE 371
Cdd:TIGR00484 397 LERMEFPEPVISLAVEPKTKADQEKMGIALGKLAEEDPTFRTftDPETGQTIIAG-----MGELHLDIIVDRMKREFKVE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 372 LIATAPSVIYQCILKDGSEVSVDNPAQMPERDKIEHIY------------------------------------------ 409
Cdd:TIGR00484 472 ANVGAPQVAYRETIRSKVEVEGKHAKQSGGRGQYGHVKirfeplepkgyefvneikggvipreyipavdkglqeamesgp 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 410 ------------------------------------------------EPFVKATMMVPNDYVGAVMELCQRKRGQFINM 441
Cdd:TIGR00484 552 lagypvvdikatlfdgsyhdvdssemafklaaslafkeagkkanpvllEPIMKVEVEVPEEYMGDVMGDLSSRRGIIEGM 631
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 487749293 442 DylDDIRVNIVY-EIPLSEvVFDFFDQLKSNTKGYASFDYEF 482
Cdd:TIGR00484 632 E--ARGNVQKIKaEVPLSE-MFGYATDLRSFTQGRGTYSMEF 670
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
12-192 |
2.71e-42 |
|
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: 150.82 E-value: 2.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 12 NIRNFSIIAHIDHGKSTLADRILENTKS-VETREMQDQLLDSMDLERERGITIKLNAVRLKYeaKDgetYTFHLIDTPGH 90
Cdd:cd01891 1 KIRNIAIIAHVDHGKTTLVDALLKQSGTfRENEEVGERVMDSNDLERERGITILAKNTAITY--KD---TKINIIDTPGH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 91 VDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLPAAEPDRVKQELEDV-IGIDQED--- 166
Cdd:cd01891 76 ADFGGEVERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDRPDARPEEVVDEVFDLfLELNATDeql 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 487749293 167 ---VVLASAKSNIG----------IEEILEKIVDVVPAP 192
Cdd:cd01891 156 dfpIVYASAKNGWAslnlddpsedLDPLFETIIEHVPAP 194
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
14-192 |
4.98e-38 |
|
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: 140.06 E-value: 4.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 14 RNFSIIAHIDHGKSTLADRILENTKSVETREMQDQL-LDSMDLERERGITIKLNAVRLKYEAK----DGETYTFHLIDTP 88
Cdd:cd01885 1 RNICIIAHVDHGKTTLSDSLLASAGIISEKLAGKARyLDTREDEQERGITIKSSAISLYFEYEeekmDGNDYLINLIDSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 89 GHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKID-------LPAAE------------- 148
Cdd:cd01885 81 GHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDrlilelkLSPEEayqrllrivedvn 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 487749293 149 -------PDRVKQElEDVIGIDQEDVVLASAKSNIG--------IEEILEKIVDVVPAP 192
Cdd:cd01885 161 aiietyaPEEFKQE-KWKFSPQKGNVAFGSALDGWGftiikfadIYAVLEMVVKHLPSP 218
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
11-382 |
8.17e-38 |
|
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: 149.28 E-value: 8.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 11 ENIRNFSIIAHIDHGKSTLADRILENTKSVETREMQDQL-LDSMDLERERGITIKLNAVRLKYEAkDGETYTFHLIDTPG 89
Cdd:TIGR00490 17 KFIRNIGIVAHIDHGKTTLSDNLLAGAGMISEELAGQQLyLDFDEQEQERGITINAANVSMVHEY-EGNEYLINLIDTPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 90 HVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLPAAE----PDRVKQELEDVIG---- 161
Cdd:TIGR00490 96 HVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKPVLFINKVDRLINElkltPQELQERFIKIITevnk 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 162 ---------------IDQED--VVLASA------------KSNIGIEEI----------------------LEKIVDVVP 190
Cdd:TIGR00490 176 likamapeefrdkwkVRVEDgsVAFGSAyynwaisvpsmkKTGIGFKDIykyckedkqkelakksplhqvvLDMVIRHLP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 191 AP-------------------------DGDPEAPLKALIFDSEYDPYRGVISSIRIIDGVVKAGDRIKMMATGKEFEVTE 245
Cdd:TIGR00490 256 SPieaqkyripviwkgdlnsevgkamlNCDPKGPLALMITKIVVDKHAGEVAVGRLYSGTIRPGMEVYIVDRKAKARIQQ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 246 VGINT-PKQLPVEELTVGDvgyiIASIKNVDDSRVGDTITLAERPAdKPLQGYKKMN-PMVFCGLFPIDNKDYNDLREAL 323
Cdd:TIGR00490 336 VGVYMgPERVEVDEIPAGN----IVAVIGLKDAVAGETICTTVENI-TPFESIKHISePVVTVAIEAKNTKDLPKLIEVL 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487749293 324 EKLQLNDASL--EFEPESSQALGFGyrtgfLGMLHMEIIQERIEREFGIELIATAPSVIYQ 382
Cdd:TIGR00490 411 RQVAKEDPTVhvEINEETGEHLISG-----MGELHLEIIVEKIREDYGLDVETSPPIVVYR 466
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
15-208 |
4.28e-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: 124.91 E-value: 4.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 15 NFSIIAHIDHGKSTLADRILENTKSV----ETREmQDQLLDSMDLERERGITIKLNAVRLKYeaKDgetYTFHLIDTPGH 90
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGRIhkigEVHG-GGATMDWMEQERERGITIQSAATTCFW--KD---HRINIIDTPGH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 91 VDFTYEVSRSLAACEGAILVVDAAQGIEAQTL-----ANVY----LALdndlellpvVNKIDLPAAEPDRVKQELEDVIG 161
Cdd:cd01886 75 VDFTIEVERSLRVLDGAVAVFDAVAGVQPQTEtvwrqADRYgvprIAF---------VNKMDRTGADFYRVVEQIREKLG 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 487749293 162 IDQEDVVLasaksNIGIEEILEKIVDVVpapdgdpeaPLKALIFDSE 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 |
1.07e-28 |
|
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: 114.26 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 15 NFSIIAHIDHGKSTLADRILENTKSVETR---EMQDQLLDSMDLERERGITIKLNAVRLKYEakdGETYTfhLIDTPGHV 91
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIRELgsvDKGTTRTDSMELERQRGITIFSAVASFQWE---DTKVN--IIDTPGHM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 92 DFTYEVSRSLAACEGAILVVDAAQGIEAQT--LANVYLALDndlelLPV---VNKIDLPAAEPDRVKQE----LEDVIGI 162
Cdd:cd04168 76 DFIAEVERSLSVLDGAILVISAVEGVQAQTriLFRLLRKLN-----IPTiifVNKIDRAGADLEKVYQEikekLSPDIVP 150
|
170 180
....*....|....*....|....*..
gi 487749293 163 DQEDVvlaSAKSNIGIEEILEKIVDVV 189
Cdd:cd04168 151 MQKVG---LYPNICDTNNIDDEQIETV 174
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
14-143 |
1.31e-28 |
|
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: 113.52 E-value: 1.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 14 RNFSIIAHIDHGKSTLADRILENT--KSVETREMQDQL--LDSMDLERERGITIKLNAVRLKYEAKDGETYTFHLIDTPG 89
Cdd:cd04167 1 RNVCIAGHLHHGKTSLLDMLIEQThkRTPSVKLGWKPLryTDTRKDEQERGISIKSNPISLVLEDSKGKSYLINIIDTPG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 487749293 90 HVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKID 143
Cdd:cd04167 81 HVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKID 134
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
8-167 |
2.90e-28 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 120.54 E-value: 2.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 8 NRRENIRNFSIIAHIDHGKSTLADR------ILENTKSVETREMqdqllDSMDLERERGITIKLNAVRLKYE-----AKD 76
Cdd:PTZ00416 14 DNPDQIRNMSVIAHVDHGKSTLTDSlvckagIISSKNAGDARFT-----DTRADEQERGITIKSTGISLYYEhdledGDD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 77 GETYTFHLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIdlpaaepDRVKQEL 156
Cdd:PTZ00416 89 KQPFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKV-------DRAILEL 161
|
170
....*....|.
gi 487749293 157 EDvigiDQEDV 167
Cdd:PTZ00416 162 QL----DPEEI 168
|
|
| Elongation_Factor_C |
cd01514 |
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ... |
410-484 |
3.76e-27 |
|
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: 104.49 E-value: 3.76e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487749293 410 EPFVKATMMVPNDYVGAVMELCQRKRGQFINMDYLDDIRVNIVYEIPLSEvVFDFFDQLKSNTKGYASFDYEFIE 484
Cdd:cd01514 1 EPIMKVEITVPEEYLGAVIGDLSKRRGEILGMEPRGTGRVVIKAELPLAE-MFGFATDLRSLTQGRASFSMEFSH 74
|
|
| EFG_C |
pfam00679 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
408-495 |
4.17e-27 |
|
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of Elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopt a ferredoxin-like fold.
Pssm-ID: 425814 [Multi-domain] Cd Length: 88 Bit Score: 104.94 E-value: 4.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 408 IYEPFVKATMMVPNDYVGAVMELCQRKRGQFINMDYLDDIRVNIVYEIPLSEvVFDFFDQLKSNTKGYASFDYEFIENKE 487
Cdd:pfam00679 2 LLEPIEKVTIDVPEEYVGDVISDLNSRRGEILDMDPDDGGRVVIEAEVPLAE-LFGFATELRSLTKGRGSFSMEFSGYQP 80
|
....*...
gi 487749293 488 SNLVKMDI 495
Cdd:pfam00679 81 VPGDILDR 88
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
8-143 |
2.36e-25 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 111.35 E-value: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 8 NRRENIRNFSIIAHIDHGKSTLADRILENTKSVETREMQDQ-LLDSMDLERERGITIKLNAVRLKYE-----------AK 75
Cdd:PLN00116 14 DKKHNIRNMSVIAHVDHGKSTLTDSLVAAAGIIAQEVAGDVrMTDTRADEAERGITIKSTGISLYYEmtdeslkdfkgER 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487749293 76 DGETYTFHLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKID 143
Cdd:PLN00116 94 DGNEYLINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTETVLRQALGERIRPVLTVNKMD 161
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
9-163 |
1.10e-24 |
|
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: 103.83 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 9 RReniRNFSIIAHIDHGKSTLADRILENTK------SVETREMQDQLL-DSMDLERERGITIKLNAVRLKYEAkdgetYT 81
Cdd:cd04169 1 RR---RTFAIISHPDAGKTTLTEKLLLFGGaiqeagAVKARKSRKHATsDWMEIEKQRGISVTSSVMQFEYKG-----CV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 82 FHLIDTPGHVDF---TYevsRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLPAAEPDRVKQELED 158
Cdd:cd04169 73 INLLDTPGHEDFsedTY---RTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDREGRDPLELLDEIEN 149
|
....*
gi 487749293 159 VIGID 163
Cdd:cd04169 150 ELGID 154
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
18-186 |
9.23e-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: 98.31 E-value: 9.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 18 IIAHIDHGKSTLADRIlentksvetREMQDQlldsmdlERE-RGITIKLNAVRLKYEAKdGETYTFhlIDTPGHVDFTYE 96
Cdd:cd01887 5 VMGHVDHGKTTLLDKI---------RKTNVA-------AGEaGGITQHIGAYQVPIDVK-IPGITF--IDTPGHEAFTNM 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 97 VSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLP---AAEPDRVKQELEDvIGIDQED------V 167
Cdd:cd01887 66 RARGASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKPygtEADPERVKNELSE-LGLVGEEwggdvsI 144
|
170
....*....|....*....
gi 487749293 168 VLASAKSNIGIEEILEKIV 186
Cdd:cd01887 145 VPISAKTGEGIDDLLEAIL 163
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
15-243 |
6.56e-21 |
|
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: 95.39 E-value: 6.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 15 NFSIIAHIDHGKSTLADRILENTKSVETREMQDQ----------------LLDSMDLERERGITIKLNAVrlKYEAKdge 78
Cdd:COG5256 9 NLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYeeeaekkgkesfkfawVMDRLKEERERGVTIDLAHK--KFETD--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 79 TYTFHLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPV-VNKIDLPAAEPDR---VKQ 154
Cdd:COG5256 84 KYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVaVNKMDAVNYSEKRyeeVKE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 155 ELEDV---IGIDQEDV--VLASAKSNIGIEE-----------ILEKIVDVVPAPDGDPEAPLKALIFDSEYDPYRGVISS 218
Cdd:COG5256 164 EVSKLlkmVGYKVDKIpfIPVSAWKGDNVVKksdnmpwyngpTLLEALDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPV 243
|
250 260
....*....|....*....|....*
gi 487749293 219 IRIIDGVVKAGDRIKMMATGKEFEV 243
Cdd:COG5256 244 GRVETGVLKVGDKVVFMPAGVVGEV 268
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
15-243 |
6.77e-21 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 95.38 E-value: 6.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 15 NFSIIAHIDHGKSTLADRILENTKSV------ETREMQDQ----------LLDSMDLERERGITIKLNAVRLkyeakDGE 78
Cdd:PRK12317 8 NLAVIGHVDHGKSTLVGRLLYETGAIdehiieELREEAKEkgkesfkfawVMDRLKEERERGVTIDLAHKKF-----ETD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 79 TYTFHLIDTPGHVDFTYEVSRSLAACEGAILVVDA--AQGIEAQTLANVYLA--LDNDlELLPVVNKIDLPAAEPDR--- 151
Cdd:PRK12317 83 KYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAAddAGGVMPQTREHVFLArtLGIN-QLIVAINKMDAVNYDEKRyee 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 152 VKQELEDV---IGIDQEDV--VLASAKSNIGIEE-----------ILEKIVDVVPAPDGDPEAPLKALIfdseYDPYrgV 215
Cdd:PRK12317 162 VKEEVSKLlkmVGYKPDDIpfIPVSAFEGDNVVKksenmpwyngpTLLEALDNLKPPEKPTDKPLRIPI----QDVY--S 235
|
250 260 270
....*....|....*....|....*....|....
gi 487749293 216 ISSI------RIIDGVVKAGDRIKMMATGKEFEV 243
Cdd:PRK12317 236 ISGVgtvpvgRVETGVLKVGDKVVFMPAGVVGEV 269
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
17-232 |
3.29e-19 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 91.82 E-value: 3.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 17 SIIAHIDHGKSTLADRIlENTKSVEtREMQdqlldsmdlererGITIKLNAVRLKYEAKDgETYTFHLIDTPGHVDFTYE 96
Cdd:CHL00189 248 TILGHVDHGKTTLLDKI-RKTQIAQ-KEAG-------------GITQKIGAYEVEFEYKD-ENQKIVFLDTPGHEAFSSM 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 97 VSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLPAAEPDRVKQEL--EDVIGID---QEDVVLAS 171
Cdd:CHL00189 312 RSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANTERIKQQLakYNLIPEKwggDTPMIPIS 391
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487749293 172 AKSNIGIEEILEKIVDVVPAPD--GDPEAPLKALIFDSEYDPYRGVISSIRIIDGVVKAGDRI 232
Cdd:CHL00189 392 ASQGTNIDKLLETILLLAEIEDlkADPTQLAQGIILEAHLDKTKGPVATILVQNGTLHIGDII 454
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
15-162 |
3.71e-17 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 81.87 E-value: 3.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 15 NFSIIAHIDHGKSTLADRILENTKSVETR---EMQDQLLDSMDLERERGITIKLNAVRLKYEAKDgetytFHLIDTPGHV 91
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRLgrvEDGNTVSDYDPEEKKRKMSIETSVAPLEWNGHK-----INLIDTPGYA 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487749293 92 DFTYEVSRSLAACEGAILVVDAAQGIEAQTlANVYLALDnDLEL--LPVVNKIDLPAAEPDRVKQELEDVIGI 162
Cdd:cd04170 76 DFVGETLSALRAVDAALIVVEAQSGVEVGT-EKVWEFLD-DAKLprIIFINKMDRARADFDKTLAALREAFGR 146
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
4-278 |
4.38e-17 |
|
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: 83.67 E-value: 4.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 4 QERYNRRENIRNFSIIAHIDHGKSTLA---DRILENTKSVETREMQDqlLDSMDLERERGITIklNAVRLKYEAkdgETY 80
Cdd:TIGR00485 3 KEKFERTKPHVNVGTIGHVDHGKTTLTaaiTTVLAKEGGAAARAYDQ--IDNAPEEKARGITI--NTAHVEYET---ETR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 81 TFHLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPV-VNKIDLPAAEP--DRVKQELE 157
Cdd:TIGR00485 76 HYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKCDMVDDEEllELVEMEVR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 158 DVI---GIDQED--VVLASA-KSNIGIEEILEKIVDV-------VPAPDGDPEAPLKALIFDSEYDPYRGVISSIRIIDG 224
Cdd:TIGR00485 156 ELLsqyDFPGDDtpIIRGSAlKALEGDAEWEAKILELmdavdeyIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERG 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 487749293 225 VVKAGDRIKMMATGKEFEVTEVGINTPKQLpVEELTVGD-VGYIIASIKNVDDSR 278
Cdd:TIGR00485 236 IIKVGEEVEIVGLKDTRKTTVTGVEMFRKE-LDEGRAGDnVGLLLRGIKREEIER 289
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
21-230 |
9.47e-17 |
|
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440298 [Multi-domain] Cd Length: 502 Bit Score: 83.14 E-value: 9.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 21 HIDHGKSTLADRILeNTKSVEtremqdqlldsmdleRE-RGITIKLNAvrlkYEAK-DGETYTFhlIDTPGHVDFTYEVS 98
Cdd:COG0532 12 HVDHGKTSLLDAIR-KTNVAA---------------GEaGGITQHIGA----YQVEtNGGKITF--LDTPGHEAFTAMRA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 99 RslaaceGA------ILVVDAAQGIEAQTL--------ANVylaldndlellPVV---NKIDLPAAEPDRVKQELEDvIG 161
Cdd:COG0532 70 R------GAqvtdivILVVAADDGVMPQTIeainhakaAGV-----------PIIvaiNKIDKPGANPDRVKQELAE-HG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487749293 162 IDQED------VVLASAKSNIGIEEILEKIVDVVPAPD--GDPEAPLKALIFDSEYDPYRGVISSIRIIDGVVKAGD 230
Cdd:COG0532 132 LVPEEwggdtiFVPVSAKTGEGIDELLEMILLQAEVLElkANPDRPARGTVIEAKLDKGRGPVATVLVQNGTLKVGD 208
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
15-144 |
1.38e-16 |
|
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: 78.77 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 15 NFSIIAHIDHGKSTLADRILENTKSVetreMQDQ---------------------LLDSMDLERERGITIKlnaVRLKYE 73
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSI----FEDQlaalerskssgtqgekldlalLVDGLQAEREQGITID---VAYRYF 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487749293 74 AKDgeTYTFHLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLAldndlELLPV------VNKIDL 144
Cdd:cd04166 74 STP--KRKFIIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIA-----SLLGIrhvvvaVNKMDL 143
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
1-163 |
1.81e-16 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 82.49 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 1 MDKQERYNRReniRNFSIIAHIDHGKSTLADRIL------ENTKSVETREMQDQLL-DSMDLERERGITIKlNAVrLKYE 73
Cdd:PRK00741 1 SELAQEVAKR---RTFAIISHPDAGKTTLTEKLLlfggaiQEAGTVKGRKSGRHATsDWMEMEKQRGISVT-SSV-MQFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 74 AKDgetYTFHLIDTPGHVDF---TYevsRSLAACEGAILVVDAAQGIEAQT--LANVYLALDndlelLPV---VNKIDLP 145
Cdd:PRK00741 76 YRD---CLINLLDTPGHEDFsedTY---RTLTAVDSALMVIDAAKGVEPQTrkLMEVCRLRD-----TPIftfINKLDRD 144
|
170
....*....|....*...
gi 487749293 146 AAEPDRVKQELEDVIGID 163
Cdd:PRK00741 145 GREPLELLDEIEEVLGIA 162
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
25-187 |
2.35e-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: 76.73 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 25 GKSTLADRILENTKSVETREMqdqlldsmdlererGITIKLNAVRLKYEAKdgeTYTFHLIDTPGHVDFTYEVSRSLAA- 103
Cdd:cd00882 9 GKSSLLNALLGGEVGEVSDVP--------------GTTRDPDVYVKELDKG---KVKLVLVDTPGLDEFGGLGREELARl 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 104 ----CEGAILVVDAAQGIEAQTLANVYLAL--DNDLELLPVVNKIDLPAAEPDRVKQELEDVIGIDQEDVVLASAKSNIG 177
Cdd:cd00882 72 llrgADLILLVVDSTDRESEEDAKLLILRRlrKEGIPIILVGNKIDLLEEREVEELLRLEELAKILGVPVFEVSAKTGEG 151
|
170
....*....|
gi 487749293 178 IEEILEKIVD 187
Cdd:cd00882 152 VDELFEKLIE 161
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
4-278 |
2.62e-16 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 81.97 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 4 QERYNRRENIRNFSIIAHIDHGKSTLADRILENTKSV--ETREMQDQLlDSMDLERERGITIklNAVRLKYEAkdgETYT 81
Cdd:PLN03126 72 RGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMggSAPKKYDEI-DAAPEERARGITI--NTATVEYET---ENRH 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 82 FHLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPV-VNKIDLPAAEP--DRVKQELED 158
Cdd:PLN03126 146 YAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVfLNKQDQVDDEEllELVELEVRE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 159 VIG---IDQEDVVLASAKSNIGIE--------------------EILEKIVDVVPAPDGDPEAPLKALIFDSEYDPYRGV 215
Cdd:PLN03126 226 LLSsyeFPGDDIPIISGSALLALEalmenpnikrgdnkwvdkiyELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGT 305
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487749293 216 ISSIRIIDGVVKAGDRIKMMATGKEFEVTEVGINTPKQLPVEELTVGDVGYIIASIKNVDDSR 278
Cdd:PLN03126 306 VATGRVERGTVKVGETVDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQR 368
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
21-185 |
9.77e-16 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.
Pssm-ID: 206734 [Multi-domain] Cd Length: 170 Bit Score: 75.33 E-value: 9.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 21 HIDHGKSTLADRIlentKSVETremqdqllDSMDLERERGITIKLNAVRLKYEakDGETYTFhlIDTPGHVDFtyeVSRS 100
Cdd:cd04171 7 HIDHGKTTLIKAL----TGIET--------DRLPEEKKRGITIDLGFAYLDLP--DGKRLGF--IDVPGHEKF---VKNM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 101 LAACEG---AILVVDAAQGIEAQTLAnvYLALdndLELLP------VVNKIDLpaAEPDRVKQELEDVI----GIDQED- 166
Cdd:cd04171 68 LAGAGGidaVLLVVAADEGIMPQTRE--HLEI---LELLGikkglvVLTKADL--VDEDRLELVEEEILellaGTFLADa 140
|
170 180
....*....|....*....|
gi 487749293 167 -VVLASAKSNIGIEEILEKI 185
Cdd:cd04171 141 pIFPVSSVTGEGIEELKNYL 160
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
15-290 |
2.31e-15 |
|
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: 78.59 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 15 NFSIIAHIDHGKSTLADRILENTKSVetreMQDQL-----------LDSMDL---------ERERGITIKlnaVRLKYEA 74
Cdd:COG2895 19 RFITCGSVDDGKSTLIGRLLYDTKSI----FEDQLaalerdskkrgTQEIDLalltdglqaEREQGITID---VAYRYFS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 75 KDgeTYTFHLIDTPGHVDFTyevsRSLA----ACEGAILVVDAAQGIEAQT-----LA------NVYLAldndlellpvV 139
Cdd:COG2895 92 TP--KRKFIIADTPGHEQYT----RNMVtgasTADLAILLIDARKGVLEQTrrhsyIAsllgirHVVVA----------V 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 140 NKIDL---PAAEPDRVKQELEDV---IGIDQEDVVLASAKS--NIgIE--------------EILEKivdvVPAPDGDPE 197
Cdd:COG2895 156 NKMDLvdySEEVFEEIVADYRAFaakLGLEDITFIPISALKgdNV-VErsenmpwydgptllEHLET----VEVAEDRND 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 198 APLKaliFDSEY-----DPYRGVisSIRIIDGVVKAGDRIKMMATGKEFEVTEvgINTPKQlPVEELTVGD-VGYIIAsi 271
Cdd:COG2895 231 APFR---FPVQYvnrpnLDFRGY--AGTIASGTVRVGDEVVVLPSGKTSTVKS--IVTFDG-DLEEAFAGQsVTLTLE-- 300
|
330
....*....|....*....
gi 487749293 272 KNVDDSRvGDTITLAERPA 290
Cdd:COG2895 301 DEIDISR-GDVIVAADAPP 318
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
15-278 |
3.16e-15 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 78.33 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 15 NFSIIAHIDHGKSTLADRIlenTKSV----ETREMQDQLLDSMDLERERGITIklNAVRLKYEAkdgETYTFHLIDTPGH 90
Cdd:PLN03127 63 NVGTIGHVDHGKTTLTAAI---TKVLaeegKAKAVAFDEIDKAPEEKARGITI--ATAHVEYET---AKRHYAHVDCPGH 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 91 VDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPV-VNKIDLPAAEP--DRVKQELEDVIGI----- 162
Cdd:PLN03127 135 ADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVfLNKVDVVDDEEllELVEMELRELLSFykfpg 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 163 DQEDVVLASAKS-------NIGIEEILE--KIVD-VVPAPDGDPEAPLKALIFDSEYDPYRGVISSIRIIDGVVKAGDRI 232
Cdd:PLN03127 215 DEIPIIRGSALSalqgtndEIGKNAILKlmDAVDeYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEEV 294
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 487749293 233 KMMA--TGKEFEVTEVGINTPKQLpVEELTVGD-VGYIIASIKNVDDSR 278
Cdd:PLN03127 295 EIVGlrPGGPLKTTVTGVEMFKKI-LDQGQAGDnVGLLLRGLKREDVQR 342
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-250 |
3.76e-15 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 77.68 E-value: 3.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 1 MDKqERYNRRENIRNFSIIAHIDHGKSTLADRILENTKSVETREMQDqlLDSMDL---ERERGITIklNAVRLKYEAkdg 77
Cdd:PRK12736 1 MAK-EKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKD--YDSIDAapeEKERGITI--NTAHVEYET--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 78 ETYTFHLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPV-VNKIDLPAAEP--DRVKQ 154
Cdd:PRK12736 73 EKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVfLNKVDLVDDEEllELVEM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 155 ELEDVI---GIDQED--VVLASAKSNI--------GIEEILEKIVDVVPAPDGDPEAPLKALIFDSEYDPYRGVISSIRI 221
Cdd:PRK12736 153 EVRELLseyDFPGDDipVIRGSALKALegdpkwedAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRV 232
|
250 260
....*....|....*....|....*....
gi 487749293 222 IDGVVKAGDRIKMMATGKEFEVTEVGINT 250
Cdd:PRK12736 233 ERGTVKVGDEVEIVGIKETQKTVVTGVEM 261
|
|
| EFG_III-like |
cd16257 |
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G ... |
302-375 |
3.89e-15 |
|
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: 70.46 E-value: 3.89e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487749293 302 PMVFCGLFPIDNKDYNDLREALEKLQLNDASLEFEPESSQalgFGYRTGFLGMLHMEIIQERIEREFGIELIAT 375
Cdd:cd16257 1 PVVFVTVEVKNPLDQEKLLEGLERLSEEDPALQVYREEST---GEFILSGLGELHLEIIVARLEREYGVELVVS 71
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
15-243 |
1.48e-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: 76.84 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 15 NFSIIAHIDHGKSTLADRILEntksvetremqdqlLDSMDL--ERERGITIKLNavrlkYEAKDGETYTFHLIDTPGHVD 92
Cdd:TIGR00475 2 IIATAGHVDHGKTTLLKALTG--------------IAADRLpeEKKRGMTIDLG-----FAYFPLPDYRLGFIDVPGHEK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 93 FTYEVSRSLAACEGAILVVDAAQGIEAQTLANV-YLALDNDLELLPVVNKID-LPAAEPDR----VKQELEDVIGIDQED 166
Cdd:TIGR00475 63 FISNAIAGGGGIDAALLVVDADEGVMTQTGEHLaVLDLLGIPHTIVVITKADrVNEEEIKRtemfMKQILNSYIFLKNAK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 167 VVLASAKSNIGIEEILEKIVDVVPAPD-GDPEAPLKALIfDSEYDpYRGVISSIR--IIDGVVKAGDRIKMMATGKEFEV 243
Cdd:TIGR00475 143 IFKTSAKTGQGIGELKKELKNLLESLDiKRIQKPLRMAI-DRAFK-VKGAGTVVTgtAFSGEVKVGDNLRLLPINHEVRV 220
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
18-195 |
2.73e-14 |
|
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: 76.11 E-value: 2.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 18 IIA---HIDHGKSTL--------ADRILEntksvetremqdqlldsmdlERERGITIKLNAVRLKYEakDGETYTFhlID 86
Cdd:COG3276 2 IIGtagHIDHGKTTLvkaltgidTDRLKE--------------------EKKRGITIDLGFAYLPLP--DGRRLGF--VD 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 87 TPGHVDFtyeVSRSLAACEG---AILVVDAAQGIEAQTLAnvYLALdndLELLP------VVNKIDLpaAEPDR---VKQ 154
Cdd:COG3276 58 VPGHEKF---IKNMLAGAGGidlVLLVVAADEGVMPQTRE--HLAI---LDLLGikrgivVLTKADL--VDEEWlelVEE 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 487749293 155 ELEDVI---GIDQEDVVLASAKSNIGIEEI---LEKIVDVVPAPDGD 195
Cdd:COG3276 128 EIRELLagtFLEDAPIVPVSAVTGEGIDELraaLDALAAAVPARDAD 174
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
18-186 |
3.00e-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: 70.86 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 18 IIAHIDHGKSTLADRILENTKSVEtremqdqlldsmdlERERGITIKLNAVRLKYeakDGETYTFHLIDTPGHVDF---- 93
Cdd:TIGR00231 6 IVGHPNVGKSTLLNSLLGNKGSIT--------------EYYPGTTRNYVTTVIEE---DGKTYKFNLLDTAGQEDYdair 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 94 ---TYEVSRSLAACEGAILVVDAAQGIEAQT--LANVylaLDNDLELLPVVNKIDLPAAEPDRVKQELEDVIGidQEDVV 168
Cdd:TIGR00231 69 rlyYPQVERSLRVFDIVILVLDVEEILEKQTkeIIHH---ADSGVPIILVGNKIDLKDADLKTHVASEFAKLN--GEPII 143
|
170
....*....|....*...
gi 487749293 169 LASAKSNIGIEEILEKIV 186
Cdd:TIGR00231 144 PLSAETGKNIDSAFKIVE 161
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
15-148 |
1.77e-13 |
|
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: 69.83 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 15 NFSIIAHIDHGKSTLADRILENTKSVETREMQDQ----------------LLDSMDLERERGITIklNAVRLKYEAkdgE 78
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYekeakemgkesfkyawVLDKLKEERERGVTI--DVGLAKFET---E 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 79 TYTFHLIDTPGHVDFTYE--VSRSLAACegAILVVDAAQG-------IEAQTLANVYLAldNDL---ELLPVVNKIDLPA 146
Cdd:cd01883 76 KYRFTIIDAPGHRDFVKNmiTGASQADV--AVLVVSARKGefeagfeKGGQTREHALLA--RTLgvkQLIVAVNKMDDVT 151
|
..
gi 487749293 147 AE 148
Cdd:cd01883 152 VN 153
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
25-188 |
2.67e-13 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 68.47 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 25 GKSTLADRILENTKSvetremQDQLLDSMdlererGITIKLNAVRLkyeakDGETYTFHLIDTPGHVDftYEVSRSLAAC 104
Cdd:COG1100 15 GKTSLVNRLVGDIFS------LEKYLSTN------GVTIDKKELKL-----DGLDVDLVIWDTPGQDE--FRETRQFYAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 105 E-----GAILVVDAAQgieAQTLANVYLALDN------DLELLPVVNKIDLPAAEPDRVKQELEDVIGIDQ-EDVVLASA 172
Cdd:COG1100 76 QltgasLYLFVVDGTR---EETLQSLYELLESlrrlgkKSPIILVLNKIDLYDEEEIEDEERLKEALSEDNiVEVVATSA 152
|
170
....*....|....*.
gi 487749293 173 KSNIGIEEILEKIVDV 188
Cdd:COG1100 153 KTGEGVEELFAALAEI 168
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
214-284 |
5.78e-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: 64.21 E-value: 5.78e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487749293 214 GVISSIRIIDGVVKAGDRIKMM--ATGKEFEVTEVGINTPKQLPVEELTVGDVGYIIASIKNVDDSRVGDTIT 284
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILpnGTGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| EFG_C |
smart00838 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
408-482 |
1.22e-12 |
|
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: 63.68 E-value: 1.22e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487749293 408 IYEPFVKATMMVPNDYVGAVMELCQRKRGQFINMDYLDDIRVnIVYEIPLSEvVFDFFDQLKSNTKGYASFDYEF 482
Cdd:smart00838 1 LLEPIMKVEVTVPEEYMGDVIGDLNSRRGKIEGMEQRGGAQV-IKAKVPLSE-MFGYATDLRSATQGRATWSMEF 73
|
|
| tufA |
CHL00071 |
elongation factor Tu |
15-278 |
1.51e-12 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 69.60 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 15 NFSIIAHIDHGKSTLADRI---LENTKSVETREMQDqlLDSMDLERERGITIklNAVRLKYeakdgETYTFHL--IDTPG 89
Cdd:CHL00071 14 NIGTIGHVDHGKTTLTAAItmtLAAKGGAKAKKYDE--IDSAPEEKARGITI--NTAHVEY-----ETENRHYahVDCPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 90 HVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLA-----------------LDnDLELLPVVNKidlpaaepdRV 152
Cdd:CHL00071 85 HADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAkqvgvpnivvflnkedqVD-DEELLELVEL---------EV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 153 KQELE------DVIGIDQEDVVLA----SAKSNIG---------IEEILEKIVDVVPAPDGDPEAPLKALIFDSEYDPYR 213
Cdd:CHL00071 155 RELLSkydfpgDDIPIVSGSALLAlealTENPKIKrgenkwvdkIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGR 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487749293 214 GVISSIRIIDGVVKAGDRIKMMATGKEFEVTEVGINTPKQLPVEELTVGDVGYIIASIKNVDDSR 278
Cdd:CHL00071 235 GTVATGRIERGTVKVGDTVEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIER 299
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
71-186 |
2.13e-11 |
|
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: 62.26 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 71 KYEAKDGETYTFHLIDTPGHVD-------FTYEVSRSLAACEGAILVVDAAQGIEAQTlANVYLALDNDLELLPVVNKID 143
Cdd:cd00880 37 RKEWELLPLGPVVLIDTPGLDEegglgreRVEEARQVADRADLVLLVVDSDLTPVEEE-AKLGLLRERGKPVLLVLNKID 115
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 487749293 144 LPAAEPDRVKQELEDVIGIDQEDVVLASAKSNIGIEEILEKIV 186
Cdd:cd00880 116 LVPESEEEELLRERKLELLPDLPVIAVSALPGEGIDELRKKIA 158
|
|
| EFG_mtEFG_C |
cd03713 |
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational ... |
410-482 |
2.26e-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: 2.26e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487749293 410 EPFVKATMMVPNDYVGAVMELCQRKRGQFINMDYLDDIRVnIVYEIPLSEvVFDFFDQLKSNTKGYASFDYEF 482
Cdd:cd03713 1 EPIMKVEVTVPEEYMGDVIGDLSSRRGQILGTESRGGWKV-IKAEVPLAE-MFGYSTDLRSLTQGRGSFTMEF 71
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
19-192 |
2.85e-11 |
|
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: 62.99 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 19 IAHIDHGKSTLADRI---LENTKSVETREMQDqlLDSMDLERERGITIklNAVRLKYEakdgeTYTFHL--IDTPGHVDF 93
Cdd:cd01884 8 IGHVDHGKTTLTAAItkvLAKKGGAKAKKYDE--IDKAPEEKARGITI--NTAHVEYE-----TANRHYahVDCPGHADY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 94 TYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPV-VNKIDLPAAEP--DRVKQELEDVI---GIDQED- 166
Cdd:cd01884 79 IKNMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVfLNKADMVDDEEllELVEMEVRELLskyGFDGDDt 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 487749293 167 -VVLASA-------KSNIG---IEEILEKIVDVVPAP 192
Cdd:cd01884 159 pIVRGSAlkalegdDPNKWvdkILELLDALDSYIPTP 195
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
25-188 |
1.70e-10 |
|
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206682 [Multi-domain] Cd Length: 174 Bit Score: 60.14 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 25 GKSTLADRILENTKSV------ETRemqdqllDSMDLERERgitiklnavrlkyeakDGETYTFhlIDTPG--------- 89
Cdd:cd01895 14 GKSSLLNALLGEERVIvsdiagTTR-------DSIDVPFEY----------------DGQKYTL--IDTAGirkkgkvte 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 90 HVDFtYEVSRSLAACEGA---ILVVDAAQGIEAQ--TLANvyLALDNDLELLPVVNKIDL---PAAEPDRVKQELEDVIG 161
Cdd:cd01895 69 GIEK-YSVLRTLKAIERAdvvLLVLDASEGITEQdlRIAG--LILEEGKALIIVVNKWDLvekDEKTMKEFEKELRRKLP 145
|
170 180
....*....|....*....|....*...
gi 487749293 162 -IDQEDVVLASAKSNIGIEEILEKIVDV 188
Cdd:cd01895 146 fLDYAPIVFISALTGQGVDKLFDAIKEV 173
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
15-144 |
2.08e-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: 60.46 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 15 NFSIIAHIDHGKSTLAdRILENTKSVETremqdqlLDSMDLERERGITIKL---------NAVRLKYEAKDGETYTFHLI 85
Cdd:cd01889 2 NVGLLGHVDSGKTSLA-KALSEIASTAA-------FDKNPQSQERGITLDLgfssfevdkPKHLEDNENPQIENYQITLV 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 487749293 86 DTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDL 144
Cdd:cd01889 74 DCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDL 132
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
22-246 |
2.16e-10 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 63.01 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 22 IDHGKSTLADRILENTKSV----------ETREMQDQ--------LLDSMDLERERGITIKlnaVRLKYEAKDGEtyTFH 83
Cdd:PRK05124 36 VDDGKSTLIGRLLHDTKQIyedqlaslhnDSKRHGTQgekldlalLVDGLQAEREQGITID---VAYRYFSTEKR--KFI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 84 LIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLAldndlELLPV------VNKIDL---PAAEPDRVKQ 154
Cdd:PRK05124 111 IADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIA-----TLLGIkhlvvaVNKMDLvdySEEVFERIRE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 155 E-------LEDVIGI--------DQEDVVLASAK----SNIGIEEILEKiVDVVPAPDGDPeaplkaLIFDSEY--DP-- 211
Cdd:PRK05124 186 DyltfaeqLPGNLDIrfvplsalEGDNVVSQSESmpwySGPTLLEVLET-VDIQRVVDAQP------FRFPVQYvnRPnl 258
|
250 260 270
....*....|....*....|....*....|....*....
gi 487749293 212 ----YRGVISSiriidGVVKAGDRIKMMATGKEFEVTEV 246
Cdd:PRK05124 259 dfrgYAGTLAS-----GVVKVGDRVKVLPSGKESNVARI 292
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
200-284 |
2.66e-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: 56.89 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 200 LKALIFDSEYDPYRGVISSIRIIDGVVKAGDRIKMMATGKEFEVTEVGINTpkqLPVEELTVGDVGYIiaSIKNVDDSRV 279
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFH---EEVDEAKAGDIVGI--GILGVKDILT 75
|
....*
gi 487749293 280 GDTIT 284
Cdd:cd01342 76 GDTLT 80
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
25-188 |
4.88e-10 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 61.99 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 25 GKSTLADRIL-EntksvetremqdqlldsmdlER-----ERGITIklNAVRLKYEaKDGETYTfhLIDTPG-----HVDF 93
Cdd:PRK00093 185 GKSSLINALLgE--------------------ERvivsdIAGTTR--DSIDTPFE-RDGQKYT--LIDTAGirrkgKVTE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 94 T---YEVSRSLAACEGA---ILVVDAAQGIEAQ--TLANvyLALDNDLELLPVVNKIDL-PAAEPDRVKQELEDVIG-ID 163
Cdd:PRK00093 240 GvekYSVIRTLKAIERAdvvLLVIDATEGITEQdlRIAG--LALEAGRALVIVVNKWDLvDEKTMEEFKKELRRRLPfLD 317
|
170 180
....*....|....*....|....*
gi 487749293 164 QEDVVLASAKSNIGIEEILEKIVDV 188
Cdd:PRK00093 318 YAPIVFISALTGQGVDKLLEAIDEA 342
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
80-189 |
1.47e-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: 57.12 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 80 YTFHLIDTPGHVDFTYEV-----SRSLAACEGA---ILVVDAAQGIEAQTLANvyLALDNDLELLPVVNKIDLPAAEPDR 151
Cdd:cd04164 51 IPVRLIDTAGLRETEDEIekigiERAREAIEEAdlvLLVVDASEGLDEEDLEI--LELPAKKPVIVVLNKSDLLSDAEGI 128
|
90 100 110
....*....|....*....|....*....|....*...
gi 487749293 152 VKQELEDVIGIdqedvvlaSAKSNIGIEEILEKIVDVV 189
Cdd:cd04164 129 SELNGKPIIAI--------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 ... |
410-482 |
3.63e-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: 3.63e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487749293 410 EPFVKATMMVPNDYVGAVMELCQRKRGQFINMDYLDDIRVNIVYEIPlSEVVFDFFDQLKSNTKGYASFDYEF 482
Cdd:cd03710 1 EPIEELTIDVPEEYSGAVIEKLGKRKGEMVDMEPDGNGRTRLEFKIP-SRGLIGFRSEFLTDTRGTGIMNHVF 72
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
22-144 |
3.85e-09 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 59.56 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 22 IDHGKSTLADRILENTKSVetreMQDQL----------------------LDSMDLERERGITIKlnaVRLKYEAKDgeT 79
Cdd:PRK05506 33 VDDGKSTLIGRLLYDSKMI----FEDQLaalerdskkvgtqgdeidlallVDGLAAEREQGITID---VAYRYFATP--K 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487749293 80 YTFHLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLAldndlELLPV------VNKIDL 144
Cdd:PRK05506 104 RKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIA-----SLLGIrhvvlaVNKMDL 169
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
15-274 |
4.09e-09 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 58.99 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 15 NFSIIAHIDHGKSTLA-----------DRILENTKSvETREMQDQ------LLDSMDLERERGITIKLNAvrLKYEAKDg 77
Cdd:PTZ00141 9 NLVVIGHVDSGKSTTTghliykcggidKRTIEKFEK-EAAEMGKGsfkyawVLDKLKAERERGITIDIAL--WKFETPK- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 78 etYTFHLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGI-------EAQTLANVYLALDNDLELLPV-VNKIDLPAAE- 148
Cdd:PTZ00141 85 --YYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEfeagiskDGQTREHALLAFTLGVKQMIVcINKMDDKTVNy 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 149 ----PDRVKQELEDV---IGIDQEDVVLAsAKSNIGIEEILEKI--------------VDVVPAPDGDPEAPLKALIfds 207
Cdd:PTZ00141 163 sqerYDEIKKEVSAYlkkVGYNPEKVPFI-PISGWQGDNMIEKSdnmpwykgptlleaLDTLEPPKRPVDKPLRLPL--- 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487749293 208 eYDPYR----GVISSIRIIDGVVKAGDRIKMMATGKEFEVTEVGINTpKQLPveELTVGD-VGYiiaSIKNV 274
Cdd:PTZ00141 239 -QDVYKiggiGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHH-EQLA--EAVPGDnVGF---NVKNV 303
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
25-188 |
4.15e-09 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 58.88 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 25 GKSTLADRILEntksvetremqdqlldsmdleRER-------GITIklNAVRLKYEaKDGETYTfhLIDTPG-----HVD 92
Cdd:COG1160 187 GKSSLINALLG---------------------EERvivsdiaGTTR--DSIDTPFE-RDGKKYT--LIDTAGirrkgKVD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 93 FT---YEVSRSLAA---CEGAILVVDAAQGIEAQ--TLANvyLALDNDLELLPVVNKIDLpaAEPDR-----VKQELEDV 159
Cdd:COG1160 241 EGiekYSVLRTLRAierADVVLLVIDATEGITEQdlKIAG--LALEAGKALVIVVNKWDL--VEKDRktreeLEKEIRRR 316
|
170 180 190
....*....|....*....|....*....|
gi 487749293 160 IG-IDQEDVVLASAKSNIGIEEILEKIVDV 188
Cdd:COG1160 317 LPfLDYAPIVFISALTGQGVDKLLEAVDEV 346
|
|
| MnmE |
COG0486 |
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
80-200 |
4.33e-09 |
|
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: 58.92 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 80 YTFHLIDTPG------HVdftyE---VSRSLAACEGA---ILVVDAAQGIEAQTLAnvYLALDNDLELLPVVNKIDLPAA 147
Cdd:COG0486 261 IPVRLIDTAGlretedEV----EkigIERAREAIEEAdlvLLLLDASEPLTEEDEE--ILEKLKDKPVIVVLNKIDLPSE 334
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 487749293 148 EPDRVKQeledvigIDQEDVVLASAKSNIGIEEILEKIVDVVPAPDGDPEAPL 200
Cdd:COG0486 335 ADGELKS-------LPGEPVIAISAKTGEGIDELKEAILELVGEGALEGEGVL 380
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-232 |
4.34e-09 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 58.70 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 1 MDKqERYNRRENIRNFSIIAHIDHGKSTLADRI---LENTKSVETREMqDQlLDSMDLERERGITIklNAVRLKYeakdg 77
Cdd:PRK12735 1 MAK-EKFERTKPHVNVGTIGHVDHGKTTLTAAItkvLAKKGGGEAKAY-DQ-IDNAPEEKARGITI--NTSHVEY----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 78 ETYTFHL--IDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPV-VNKIDLPAAEP--DRV 152
Cdd:PRK12735 71 ETANRHYahVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVfLNKCDMVDDEEllELV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 153 KQELEDVI---GIDQED--VVLASA-------KSNIG---IEEILEKIVDVVPAPDGDPEAPLKALIFDSEYDPYRGVIS 217
Cdd:PRK12735 151 EMEVRELLskyDFPGDDtpIIRGSAlkalegdDDEEWeakILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVV 230
|
250
....*....|....*
gi 487749293 218 SIRIIDGVVKAGDRI 232
Cdd:PRK12735 231 TGRVERGIVKVGDEV 245
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
15-128 |
5.79e-09 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 58.28 E-value: 5.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 15 NFSIIAHIDHGKSTLADRI---LENTKSVETREMqDQLlDSMDLERERGITIklNAVRLKYEakdgeTYTFHL--IDTPG 89
Cdd:PRK00049 14 NVGTIGHVDHGKTTLTAAItkvLAKKGGAEAKAY-DQI-DKAPEEKARGITI--NTAHVEYE-----TEKRHYahVDCPG 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 487749293 90 HVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLA 128
Cdd:PRK00049 85 HADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLA 123
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
19-128 |
6.33e-09 |
|
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: 58.24 E-value: 6.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 19 IAHIDHGKSTL--------ADRILENTKSVETremqdqlLDSMDLERERGITIklNAVRLKYEakdgeTYTFHL--IDTP 88
Cdd:COG0050 18 IGHVDHGKTTLtaaitkvlAKKGGAKAKAYDQ-------IDKAPEEKERGITI--NTSHVEYE-----TEKRHYahVDCP 83
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 487749293 89 GHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLA 128
Cdd:COG0050 84 GHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLA 123
|
|
| MnmE_helical |
pfam12631 |
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ... |
80-200 |
1.01e-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: 57.11 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 80 YTFHLIDTPG------HVdftyE---VSRSLAACEGA---ILVVDAAQGIEAQTLAnVYLALDNDLELLPVVNKIDLPAA 147
Cdd:pfam12631 142 IPLRLIDTAGiretddEV----EkigIERAREAIEEAdlvLLVLDASRPLDEEDLE-ILELLKDKKPIIVVLNKSDLLGE 216
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 487749293 148 EPDRVKQELEDVIGIdqedvvlaSAKSNIGIEEILEKIVDVVPAPDGDPEAPL 200
Cdd:pfam12631 217 IDELEELKGKPVLAI--------SAKTGEGLDELEEAIKELFLAGEIASDGPI 261
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
15-233 |
1.47e-08 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 57.17 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 15 NFSIIAHIDHGKSTLadrilentksveTREMQDQLLDSMDLERERGITIKLN----AVRLKYEAKDGETYT--------- 81
Cdd:PRK04000 11 NIGMVGHVDHGKTTL------------VQALTGVWTDRHSEELKRGITIRLGyadaTIRKCPDCEEPEAYTtepkcpncg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 82 --------FHLIDTPGHvdftyEV------SRSlAACEGAILVVDAAQGI-EAQTLANvYLALD-----NdleLLPVVNK 141
Cdd:PRK04000 79 setellrrVSFVDAPGH-----ETlmatmlSGA-ALMDGAILVIAANEPCpQPQTKEH-LMALDiigikN---IVIVQNK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 142 IDLPAAEP--DRVKQELEDVIGIDQED--VVLASAKSNIGIEEILEKIVDVVPAPDGDPEAPLKALI---FD-----SEY 209
Cdd:PRK04000 149 IDLVSKERalENYEQIKEFVKGTVAENapIIPVSALHKVNIDALIEAIEEEIPTPERDLDKPPRMYVarsFDvnkpgTPP 228
|
250 260
....*....|....*....|....*
gi 487749293 210 DPYR-GVISSiRIIDGVVKAGDRIK 233
Cdd:PRK04000 229 EKLKgGVIGG-SLIQGVLKVGDEIE 252
|
|
| EFG_III |
cd16262 |
Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial ... |
302-371 |
1.81e-08 |
|
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: 51.69 E-value: 1.81e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487749293 302 PMVFCGLFPIDNKDYNDLREALEKLQLNDASL--EFEPESSQALGFGyrtgfLGMLHMEIIQERIEREFGIE 371
Cdd:cd16262 3 PVISLAIEPKTKADEDKLSKALARLAEEDPTLrvSRDEETGQTILSG-----MGELHLEIIVERLKREYGVE 69
|
|
| EFG_mtEFG_II |
cd04088 |
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation ... |
202-284 |
2.10e-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: 51.37 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 202 ALIFDSEYDPYRGVISSIRIIDGVVKAGDRIKMMATGKEFEVTE-VGINTPKQLPVEELTVGDvgyIIASIKnVDDSRVG 280
Cdd:cd04088 3 ALVFKTMADPFVGKLTFFRVYSGTLKSGSTVYNSTKGKKERVGRlLRMHGKKREEVEELGAGD---IGAVVG-LKDTRTG 78
|
....
gi 487749293 281 DTIT 284
Cdd:cd04088 79 DTLC 82
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
18-181 |
2.21e-08 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 56.98 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 18 IIA---HIDHGKSTLadriLENTKSVETremqdqllDSMDLERERGITIKLNAVRLKYEakDGETYTFhlIDTPGHVDFt 94
Cdd:PRK10512 2 IIAtagHVDHGKTTL----LQAITGVNA--------DRLPEEKKRGMTIDLGYAYWPQP--DGRVLGF--IDVPGHEKF- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 95 yeVSRSLAACEG---AILVVDAAQGIEAQTLANV-YLALDNDLELLPVVNKIDL-PAAEPDRVKQELEDVI---GIDQED 166
Cdd:PRK10512 65 --LSNMLAGVGGidhALLVVACDDGVMAQTREHLaILQLTGNPMLTVALTKADRvDEARIAEVRRQVKAVLreyGFAEAK 142
|
170
....*....|....*
gi 487749293 167 VVLASAKSNIGIEEI 181
Cdd:PRK10512 143 LFVTAATEGRGIDAL 157
|
|
| EFG_III |
pfam14492 |
Elongation Factor G, domain III; This domain is found in Elongation Factor G. It shares a ... |
302-373 |
3.15e-08 |
|
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: 50.94 E-value: 3.15e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487749293 302 PMVFCGLFPIDNKDYNDLREALEKLQLNDASL--EFEPESSQALGFGyrtgfLGMLHMEIIQERIEREFGIELI 373
Cdd:pfam14492 4 PVISVAIEPKTKGDEDKLSKALNRLLEEDPTLrvERDEETGETILSG-----MGELHLEIVVDRLKRKYGVEVE 72
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
15-274 |
7.71e-08 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 55.10 E-value: 7.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 15 NFSIIAHIDHGKSTLADRILENTKSVETR----------EMQDQ------LLDSMDLERERGITIKLnaVRLKYEAKdge 78
Cdd:PLN00043 9 NIVVIGHVDSGKSTTTGHLIYKLGGIDKRvierfekeaaEMNKRsfkyawVLDKLKAERERGITIDI--ALWKFETT--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 79 TYTFHLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQG-------IEAQTLANVYLALDNDL-ELLPVVNKIDlpAAEPD 150
Cdd:PLN00043 84 KYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGgfeagisKDGQTREHALLAFTLGVkQMICCCNKMD--ATTPK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 151 RVKQELEDVI-----------------------GIDQEDVVLASAKSNIGIEEILEKIVDVVPAPDGDPEAPLKALIFDS 207
Cdd:PLN00043 162 YSKARYDEIVkevssylkkvgynpdkipfvpisGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQDV 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487749293 208 EYDPYRGVISSIRIIDGVVKAGDRIKMMATGKEFEVTEVGINTPKQLpvEELTVGDVGYiiaSIKNV 274
Cdd:PLN00043 242 YKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQ--EALPGDNVGF---NVKNV 303
|
|
| trmE |
PRK05291 |
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; |
80-189 |
1.32e-07 |
|
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
Pssm-ID: 235392 [Multi-domain] Cd Length: 449 Bit Score: 54.35 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 80 YTFHLIDTPG------HVdftyE---VSRSLAACEGA---ILVVDAAQGIEAQTLANvyLALDNDLELLPVVNKIDLPAa 147
Cdd:PRK05291 263 IPLRLIDTAGiretddEV----EkigIERSREAIEEAdlvLLVLDASEPLTEEDDEI--LEELKDKPVIVVLNKADLTG- 335
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 487749293 148 EPDRVKQELEDVIGIdqedvvlaSAKSNIGIEEILEKIVDVV 189
Cdd:PRK05291 336 EIDLEEENGKPVIRI--------SAKTGEGIDELREAIKELA 369
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
17-246 |
1.85e-06 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 50.95 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 17 SIIAHIDHGKSTLADRIlENTkSVETREmqdqlldsmdlerERGIT-------IKLNAVR------LKYEAKDGETYTFH 83
Cdd:PRK04004 10 VVLGHVDHGKTTLLDKI-RGT-AVAAKE-------------AGGITqhigateVPIDVIEkiagplKKPLPIKLKIPGLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 84 LIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANvylaldndLELL-----PVV---NKID-LP--------- 145
Cdd:PRK04004 75 FIDTPGHEAFTNLRKRGGALADIAILVVDINEGFQPQTIEA--------INILkrrktPFVvaaNKIDrIPgwkstedap 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 146 -----AAEPDRVKQELEDVI----------GIDQE------------DVVLASAKSNIGIEEILEKIVdvvpapdGDPEA 198
Cdd:PRK04004 147 flesiEKQSQRVQQELEEKLyeligqlselGFSADrfdrvkdftktvAIVPVSAKTGEGIPDLLMVLA-------GLAQR 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 199 PLKALIFDSEYDPYRGVISSIR------------IIDGVVKAGDRIkMMATGKEFEVTEV 246
Cdd:PRK04004 220 YLEERLKIDVEGPGKGTVLEVKeerglgttidviLYDGTLRKGDTI-VVGGKDGPIVTKV 278
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
200-289 |
2.34e-06 |
|
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: 46.03 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 200 LKALIFDSEYDPYRGVISSIRIIDGVVKAGDRIKMMATGKE---FEVTEV----GIntpKQLPVEELTVGDvgyIIAsIK 272
Cdd:cd03691 1 FQMLVTTLDYDDYLGRIAIGRIFSGTVKVGQQVTVVDEDGKiekGRVTKLfgfeGL---ERVEVEEAEAGD---IVA-IA 73
|
90
....*....|....*..
gi 487749293 273 NVDDSRVGDTITLAERP 289
Cdd:cd03691 74 GLEDITIGDTICDPEVP 90
|
|
| YqeH |
cd01855 |
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ... |
138-185 |
3.78e-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: 47.64 E-value: 3.78e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 487749293 138 VVNKIDL--PAAEPDRVKQELEDVIGIDQ---EDVVLASAKSNIGIEEILEKI 185
Cdd:cd01855 66 VGNKIDLlpKDVKPNRLKQWVKKRLKIGGlkiKDVILVSAKKGWGVEELIEEI 118
|
|
| mtEFG1_C |
cd04097 |
mtEFG1_C: C-terminus of mitochondrial Elongation factor G1 (mtEFG1)-like proteins found in ... |
410-482 |
6.54e-06 |
|
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: 44.23 E-value: 6.54e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487749293 410 EPFVKATMMVPNDYVGAVMELCQRKRGQFINMDYLDDiRVNIVYEIPLSEvVFDFFDQLKSNTKGYASFDYEF 482
Cdd:cd04097 1 EPIMKVEVTAPTEFQGNVIGLLNKRKGTIVDTDTGED-EFTLEAEVPLND-MFGYSTELRSMTQGKGEFSMEF 71
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
15-192 |
1.52e-05 |
|
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: 46.11 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 15 NFSIIAHIDHGKSTLAdRILENTKSVETREmqdqlldsmdlERERGITIKL---------------NAVRLKYEAK---- 75
Cdd:cd01888 2 NIGTIGHVAHGKTTLV-KALSGVWTVRHKE-----------ELKRNITIKLgyanakiykcpncgcPRPYDTPECEcpgc 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 76 DGET---YTFHLIDTPGHvdftyEVsrsLAAC--------EGAILVVDAAQGI-EAQTLANVyLALDN-DLELLPVV-NK 141
Cdd:cd01888 70 GGETklvRHVSFVDCPGH-----EI---LMATmlsgaavmDGALLLIAANEPCpQPQTSEHL-AALEImGLKHIIILqNK 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 487749293 142 IDLPAAEP--DRVKQELEDVIGIDQED--VVLASAKSNIGIEEILEKIVDVVPAP 192
Cdd:cd01888 141 IDLVKEEQalENYEQIKEFVKGTIAENapIIPISAQLKYNIDVLCEYIVKKIPTP 195
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
69-204 |
3.45e-05 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 46.56 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 69 RLKYEAKDGEtYTFHLIDTPGHVD-----FTYEVSR-SLAACEGA---ILVVDAAQGIeaqtlanvyLALDNDL-ELL-- 136
Cdd:COG1160 40 RIYGEAEWGG-REFTLIDTGGIEPddddgLEAEIREqAELAIEEAdviLFVVDGRAGL---------TPLDEEIaKLLrr 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 137 ---PV---VNKIDLPAAEPDRVkqE-----LEDVIGIdqedvvlaSAKSNIGIEEILEKIVDVVPAPDGDPEA--PLK-A 202
Cdd:COG1160 110 sgkPVilvVNKVDGPKREADAA--EfyslgLGEPIPI--------SAEHGRGVGDLLDAVLELLPEEEEEEEEddPIKiA 179
|
..
gi 487749293 203 LI 204
Cdd:COG1160 180 IV 181
|
|
| Tet_II |
cd03690 |
Domain II of ribosomal protection proteins Tet(M) and Tet(O); This subfamily represents domain ... |
197-283 |
6.21e-05 |
|
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: 41.84 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 197 EAPLKALIFDSEYDPYRGVISSIRIIDGVVKAGDRIKMMATGKEFEVTEV-GINTPKQLPVEELTVGDvgyiIASIKNVD 275
Cdd:cd03690 1 ESELSGTVFKIEYDPKGERLAYLRLYSGTLRLRDSVRVSGEEEKIKITELrTFENGELVKVDRVYAGD----IAILVGLK 76
|
....*...
gi 487749293 276 DSRVGDTI 283
Cdd:cd03690 77 SLRVGDVL 84
|
|
| HflX |
cd01878 |
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
108-189 |
8.33e-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: 43.99 E-value: 8.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 108 ILVVDAAQGIEAQTLANVyLALDNDLEL-----LPVVNKIDLpaAEPDRVKQELEDvigiDQEDVVLASAKSNIGIEEIL 182
Cdd:cd01878 125 LHVVDASDPDREEQIETV-EEVLKELGAddipiILVLNKIDL--LDDEELEERLRA----GRPDAVFISAKTGEGLDLLK 197
|
....*..
gi 487749293 183 EKIVDVV 189
Cdd:cd01878 198 EAIEELL 204
|
|
| mtEFG2_II_like |
cd04092 |
Domain II of mitochondrial elongation factor G2-like proteins found in eukaryotes; Eukaryotic ... |
202-283 |
1.44e-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: 40.76 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 202 ALIFDSEYDPYRGVISSIRIIDGVVKAGDRIKMMATGKEFEVTE-VGINTPKQLPVEELTVGDVGyIIASIKNVddsRVG 280
Cdd:cd04092 3 ALAFKVIHDPQRGPLVFVRVYSGTLKAGSNVYNTTTGKKERISRlLKMHADQTEEVDSLSAGNIG-VITGLKVT---STG 78
|
...
gi 487749293 281 DTI 283
Cdd:cd04092 79 DTL 81
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
84-190 |
1.48e-04 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 44.21 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 84 LIDTPG-H----------VDFtyeVSRSLAACEGAILVVDAAQGIEAQtlanvylalDND-LELLP--------VVNKID 143
Cdd:COG1159 55 FVDTPGiHkpkrklgrrmNKA---AWSALEDVDVILFVVDATEKIGEG---------DEFiLELLKklktpvilVINKID 122
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 487749293 144 LpaAEPDRVKQELEDVIG-IDQEDVVLASAKSNIGIEEILEKIVDVVP 190
Cdd:COG1159 123 L--VKKEELLPLLAEYSElLDFAEIVPISALKGDNVDELLDEIAKLLP 168
|
|
| Srp102 |
COG2229 |
Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, ... |
77-186 |
1.48e-04 |
|
Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 441830 [Multi-domain] Cd Length: 189 Bit Score: 42.89 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 77 GETYTFHLIDTPGHV--DFTYE--VSRSLaaceGAILVVDaAQGIEAQTLANVYLALDNDLELLPVV---NKIDLPAAEP 149
Cdd:COG2229 67 GDGLRLHLFGTPGQVrfDFMWDilLRGAD----GVVFLAD-SRRLEDSFNAESLDFFEERLEKLPFVvavNKRDLPDALS 141
|
90 100 110
....*....|....*....|....*....|....*...
gi 487749293 150 DrvkQELEDVIGIDQE-DVVLASAKSNIGIEEILEKIV 186
Cdd:COG2229 142 L---EELREALDLGPDvPVVEADARDGESVKETLIALL 176
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
84-190 |
1.79e-04 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 43.88 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 84 LIDTPG-H----------VDFtyeVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLpAAEPDRV 152
Cdd:PRK00089 57 FVDTPGiHkpkralnramNKA---AWSSLKDVDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDL-VKDKEEL 132
|
90 100 110
....*....|....*....|....*....|....*....
gi 487749293 153 KQELEDV-IGIDQEDVVLASAKSNIGIEEILEKIVDVVP 190
Cdd:PRK00089 133 LPLLEELsELMDFAEIVPISALKGDNVDELLDVIAKYLP 171
|
|
| YihA_EngB |
cd01876 |
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
82-187 |
2.80e-04 |
|
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: 41.73 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 82 FHLIDTPG----------HVDFTYEVSRSLAACE---GAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKID-LPAA 147
Cdd:cd01876 47 FRLVDLPGygyakvskevREKWGKLIEEYLENREnlkGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADkLKKS 126
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 487749293 148 EPDRVKQELEDVIGIDQED--VVLASAKSNIGIEEILEKIVD 187
Cdd:cd01876 127 ELAKVLKKIKEELNLFNILppVILFSSKKGTGIDELRALIAE 168
|
|
| FeoB |
cd01879 |
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ... |
73-191 |
6.84e-04 |
|
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) subfamily. E. coli has an iron(II) transport system, known as feo, which may make an important contribution to the iron supply of the cell under anaerobic conditions. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent.
Pssm-ID: 206667 [Multi-domain] Cd Length: 159 Bit Score: 40.52 E-value: 6.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 73 EAKDGET----YTFHLIDTPGhvdfTY---------EVSRSL---AACEGAILVVDAAQgIEAqtlaNVYLALDNdLEL- 135
Cdd:cd01879 33 EKKEGEFklggKEIEIVDLPG----TYsltpysedeKVARDFllgEEPDLIVNVVDATN-LER----NLYLTLQL-LELg 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487749293 136 LPVV---NKIDLpaAEPDRVK---QELEDVIGIDqedVVLASAKSNIGIEEILEKIVDVVPA 191
Cdd:cd01879 103 LPVVvalNMIDE--AEKRGIKidlDKLSELLGVP---VVPTSARKGEGIDELLDAIAKLAES 159
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
126-185 |
7.97e-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: 41.23 E-value: 7.97e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487749293 126 YLAL--DNDLELLPVVNKIDLpaAEPDRVKQELEDV--IGIDqedVVLASAKSNIGIEEILEKI 185
Cdd:cd01854 25 YLVAaeASGIEPVIVLNKADL--VDDEELEELLEIYekLGYP---VLAVSAKTGEGLDELRELL 83
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|
| Rab |
cd00154 |
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ... |
76-187 |
1.34e-03 |
|
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: 39.75 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 76 DGETYTFHLIDTPGHvdftyEVSRSLAA-----CEGAILVVDaaqGIEAQTLANVY----LALDNDLELLPVV---NKID 143
Cdd:cd00154 45 DGKKVKLQIWDTAGQ-----ERFRSITSsyyrgAHGAILVYD---VTNRESFENLDkwlnELKEYAPPNIPIIlvgNKSD 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 487749293 144 LpaaEPDRV--KQELEDVIGIDQEDVVLASAKSNIGIEEILEKIVD 187
Cdd:cd00154 117 L---EDERQvsTEEAQQFAKENGLLFFETSAKTGENVDEAFESLAR 159
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|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
80-204 |
1.55e-03 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 41.19 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 80 YTFHLIDTPGHV----DFTYEVSR-SLAACEGA---ILVVDAAQGIEAQ--TLAN--------VYLaldndlellpVVNK 141
Cdd:PRK00093 49 REFILIDTGGIEpdddGFEKQIREqAELAIEEAdviLFVVDGRAGLTPAdeEIAKilrksnkpVIL----------VVNK 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487749293 142 IDLPAAEPDRVkqE-----LEDVIGIdqedvvlaSAKSNIGIEEILEKIVDVVPAPDGDPEA--PLK-ALI 204
Cdd:PRK00093 119 VDGPDEEADAY--EfyslgLGEPYPI--------SAEHGRGIGDLLDAILEELPEEEEEDEEdePIKiAII 179
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|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
84-187 |
1.60e-03 |
|
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: 39.75 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 84 LIDTPG-HVDFT-------YEVSRSLAACEGAILVVDAAQGIEAQTlANVYLAL-DNDLELLPVVNKIDLpAAEPDRVKQ 154
Cdd:cd04163 55 FVDTPGiHKPKKklgermvKAAWSALKDVDLVLFVVDASEWIGEGD-EFILELLkKSKTPVILVLNKIDL-VKDKEDLLP 132
|
90 100 110
....*....|....*....|....*....|....
gi 487749293 155 ELEDV-IGIDQEDVVLASAKSNIGIEEILEKIVD 187
Cdd:cd04163 133 LLEKLkELHPFAEIFPISALKGENVDELLEYIVE 166
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|
| obgE |
PRK12299 |
GTPase CgtA; Reviewed |
108-197 |
4.75e-03 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237048 [Multi-domain] Cd Length: 335 Bit Score: 39.67 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 108 ILVVDAAQGI---EAQTLANVYLALDNDLELLP---VVNKIDLPAAEPDRvKQELEDVIGIDQEDVVLASAKSNIGIEEI 181
Cdd:PRK12299 241 LHLVDIEAVDpveDYKTIRNELEKYSPELADKPrilVLNKIDLLDEEEER-EKRAALELAALGGPVFLISAVTGEGLDEL 319
|
90
....*....|....*.
gi 487749293 182 LEKIVDVVPAPDGDPE 197
Cdd:PRK12299 320 LRALWELLEEARREEE 335
|
|
| Tet_C |
cd03711 |
Tet_C: C-terminus of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology ... |
410-482 |
4.79e-03 |
|
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: 36.06 E-value: 4.79e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487749293 410 EPFVKATMMVPNDYVGAVMELCQRKRGQFINMdYLDDIRVNIVYEIPLSEVVfDFFDQLKSNTKGYASFDYEF 482
Cdd:cd03711 1 EPYLRFELEVPQDALGRAMSDLAKMGATFEDP-QIKGDEVTLEGTIPVATSQ-DYQSELPSYTHGEGVLETEF 71
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
25-141 |
6.82e-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: 36.83 E-value: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749293 25 GKSTLADRILENTKSVEtremqDQLldsmdlererGITIKLNAVRLKYEAKDgetytFHLIDTPGHVD---FTYEVSRSL 101
Cdd:pfam01926 11 GKSTLINALTGAKAIVS-----DYP----------GTTRDPNEGRLELKGKQ-----IILVDTPGLIEgasEGEGLGRAF 70
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 487749293 102 AA---CEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNK 141
Cdd:pfam01926 71 LAiieADLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
|
|
| Obg |
cd01898 |
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ... |
138-189 |
8.68e-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: 37.40 E-value: 8.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 487749293 138 VVNKIDLPAAEP--DRVKQELEDVIGIDqedVVLASAKSNIGIEEILEKIVDVV 189
Cdd:cd01898 120 VLNKIDLLDAEErfEKLKELLKELKGKK---VFPISALTGEGLDELLKKLAKLL 170
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