|
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: 1294.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 9 RQEKIRNFSIIAHIDHGKSTLADRILEKTETVSSREMQAQLLDSMDLERERGITIKLNAIELNYTAKDGETYIFHLIDTP 88
Cdd:COG0481 2 DQKNIRNFSIIAHIDHGKSTLADRLLELTGTLSEREMKEQVLDSMDLERERGITIKAQAVRLNYKAKDGETYQLNLIDTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 89 GHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPVINKIDLPAADPERVRHEVEDVIGLDASEAV 168
Cdd:COG0481 82 GHVDFSYEVSRSLAACEGALLVVDASQGVEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKQEIEDIIGIDASDAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 169 LASAKAGIGIEEILEQIVEKVPAPTGDVDAPLQALIFDSVYDAYRGVILQVRIVNGIVKPGDKIQMMSNGKTFDVTEVGI 248
Cdd:COG0481 162 LVSAKTGIGIEEILEAIVERIPPPKGDPDAPLQALIFDSWYDSYRGVVVYVRVFDGTLKKGDKIKMMSTGKEYEVDEVGV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 249 FTPKAVGRDFLATGDVGYVAASIKTVADTRVGDTVTLANNPAKEALHGYKQMNPMVFAGIYPIESNKYNDLREALEKLQL 328
Cdd:COG0481 242 FTPKMTPVDELSAGEVGYIIAGIKDVRDARVGDTITLAKNPAAEPLPGFKEVKPMVFAGLYPVDSDDYEDLRDALEKLQL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 329 NDASLQFEPETSQALGFGFRCGFLGLLHMDVIQERLEREFNIDLIMTAPSVVYHVHTTDEDMIEVSNPSEFPDPTRVAFI 408
Cdd:COG0481 322 NDASLTYEPETSAALGFGFRCGFLGLLHMEIIQERLEREFDLDLITTAPSVVYEVTLTDGEVIEVDNPSDLPDPGKIEEI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 409 EEPYVKAQIMVPQEFVGAVMELSQRKRGDFVTMDYIDDNRVNVIYQIPLAEIVFDFFDKLKSSTRGYASFDYDMSEYRRS 488
Cdd:COG0481 402 EEPIVKATIITPSEYVGAVMELCQEKRGVQKNMEYLGENRVELTYELPLAEIVFDFFDRLKSITRGYASLDYEFIGYRES 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 489 QLVKMDILLNGDKVDALSFIVHKEFAYERGKIIVEKLKKIIPRQQFEVPIQAAIGQKIVARSDIKALRKNVLAKCYGGDV 568
Cdd:COG0481 482 DLVKLDILINGEPVDALSFIVHRDKAYSRGRALVEKLKELIPRQQFEVPIQAAIGGKIIARETIKALRKDVLAKCYGGDI 561
|
570 580 590
....*....|....*....|....*....|....*..
gi 489080006 569 SRKRKLLEKQKAGKKRMKAIGSVEVPQEAFLSVLSMD 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: 1128.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 11 EKIRNFSIIAHIDHGKSTLADRILEKTETVSSREMQAQLLDSMDLERERGITIKLNAIELNYTAKDGETYIFHLIDTPGH 90
Cdd:TIGR01393 1 KNIRNFSIIAHIDHGKSTLADRLLEYTGAISEREMREQVLDSMDLERERGITIKAQAVRLNYKAKDGETYVLNLIDTPGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 91 VDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPVINKIDLPAADPERVRHEVEDVIGLDASEAVLA 170
Cdd:TIGR01393 81 VDFSYEVSRSLAACEGALLLVDAAQGIEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKKEIEEVIGLDASEAILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 171 SAKAGIGIEEILEQIVEKVPAPTGDVDAPLQALIFDSVYDAYRGVILQVRIVNGIVKPGDKIQMMSNGKTFDVTEVGIFT 250
Cdd:TIGR01393 161 SAKTGIGIEEILEAIVKRVPPPKGDPDAPLKALIFDSHYDNYRGVVALVRVFEGTIKPGDKIRFMSTGKEYEVDEVGVFT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 251 PKAVGRDFLATGDVGYVAASIKTVADTRVGDTVTLANNPAKEALHGYKQMNPMVFAGIYPIESNKYNDLREALEKLQLND 330
Cdd:TIGR01393 241 PKLTKTDELSAGEVGYIIAGIKDVSDVRVGDTITHVKNPAKEPLPGFKEVKPMVFAGLYPIDTEDYEDLRDALEKLKLND 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 331 ASLQFEPETSQALGFGFRCGFLGLLHMDVIQERLEREFNIDLIMTAPSVVYHVHTTDEDMIEVSNPSEFPDPTRVAFIEE 410
Cdd:TIGR01393 321 ASLTYEPESSPALGFGFRCGFLGLLHMEIIQERLEREFNLDLITTAPSVIYRVYLTNGEVIEVDNPSDLPDPGKIEHVEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 411 PYVKAQIMVPQEFVGAVMELSQRKRGDFVTMDYIDDNRVNVIYQIPLAEIVFDFFDKLKSSTRGYASFDYDMSEYRRSQL 490
Cdd:TIGR01393 401 PYVKATIITPTEYLGPIMTLCQEKRGVQTNMEYLDPNRVELIYEMPLAEIVYDFFDKLKSISRGYASFDYELIGYRPSDL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 491 VKMDILLNGDKVDALSFIVHKEFAYERGKIIVEKLKKIIPRQQFEVPIQAAIGQKIVARSDIKALRKNVLAKCYGGDVSR 570
Cdd:TIGR01393 481 VKLDILINGEPVDALSFIVHRDKAYSRGREICEKLKELIPRQQFEIPIQAAIGGKIIARETIKALRKDVTAKCYGGDITR 560
|
570 580 590
....*....|....*....|....*....|....*
gi 489080006 571 KRKLLEKQKAGKKRMKAIGSVEVPQEAFLSVLSMD 605
Cdd:TIGR01393 561 KRKLLEKQKEGKKRMKQIGKVEVPQEAFLAVLKVD 595
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
14-192 |
1.41e-128 |
|
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: 374.95 E-value: 1.41e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 14 RNFSIIAHIDHGKSTLADRILEKTETVSSREMQAQLLDSMDLERERGITIKLNAIELNYTAKDGETYIFHLIDTPGHVDF 93
Cdd:cd01890 1 RNFSIIAHIDHGKSTLADRLLELTGTVSEREMKEQVLDSMDLERERGITIKAQAVRLFYKAKDGEEYLLNLIDTPGHVDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 94 TYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPVINKIDLPAADPERVRHEVEDVIGLDASEAVLASAK 173
Cdd:cd01890 81 SYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVKQEIEDVLGLDASEAILVSAK 160
|
170
....*....|....*....
gi 489080006 174 AGIGIEEILEQIVEKVPAP 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 |
8.40e-73 |
|
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: 228.44 E-value: 8.40e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 497 LNGDKVDALSFIVHKEFAYERGKIIVEKLKKIIPRQQFEVPIQAAIGQKIVARSDIKALRKNVLAKCYGGDVSRKRKLLE 576
Cdd:pfam06421 1 INGEPVDALSFIVHRSKAYRRGRALVEKLKELIPRQQFEVPIQAAIGGKIIARETIKALRKDVTAKCYGGDISRKKKLLE 80
|
90 100
....*....|....*....|....*..
gi 489080006 577 KQKAGKKRMKAIGSVEVPQEAFLSVLS 603
Cdd:pfam06421 81 KQKEGKKRMKQIGNVEIPQEAFLAVLK 107
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
8-456 |
3.15e-71 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 240.69 E-value: 3.15e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 8 KRQEKIRNFSIIAHIDHGKSTLADRILEKTETVSSRE-MQAQLLDSMDLERERGITI--KLNAIelNYtaKDgetYIFHL 84
Cdd:COG1217 1 MMREDIRNIAIIAHVDHGKTTLVDALLKQSGTFRENQeVAERVMDSNDLERERGITIlaKNTAV--RY--KG---VKINI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 85 IDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQT---LANvylALDNDLEILPVINKIDLPAADPERVRHEVEDV-I 160
Cdd:COG1217 74 VDTPGHADFGGEVERVLSMVDGVLLLVDAFEGPMPQTrfvLKK---ALELGLKPIVVINKIDRPDARPDEVVDEVFDLfI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 161 GLDASEAVL------ASAKAGI----------GIEEILEQIVEKVPAPTGDVDAPLQALIFDSVYDAYRGVILQVRIVNG 224
Cdd:COG1217 151 ELGATDEQLdfpvvyASARNGWasldlddpgeDLTPLFDTILEHVPAPEVDPDGPLQMLVTNLDYSDYVGRIAIGRIFRG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 225 IVKPGDKIQMMSNG---KTFDVTEVgiFTPKAVGRDFLATGDVGYVAAsIKTVADTRVGDTVTLANNPakEALHGYK--- 298
Cdd:COG1217 231 TIKKGQQVALIKRDgkvEKGKITKL--FGFEGLERVEVEEAEAGDIVA-IAGIEDINIGDTICDPENP--EALPPIKide 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 299 ---QMNPMV----FAGiypiESNKY---NDLREALEKLQLNDASLQFEpETSQALGF---GfRcgflGLLHMDVIQERLE 365
Cdd:COG1217 306 ptlSMTFSVndspFAG----REGKFvtsRQIRERLEKELETNVALRVE-ETDSPDAFkvsG-R----GELHLSILIETMR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 366 RE-FnidlimtapsvvyhvhttdEdmIEVSNPsefpdptRVAFIE------EPYVKAQIMVPQEFVGAVME-LSQRKrGD 437
Cdd:COG1217 376 REgY-------------------E--LQVSRP-------EVIFKEidgkklEPIEELTIDVPEEYSGAVIEkLGQRK-GE 426
|
490
....*....|....*....
gi 489080006 438 FVTMDYIDDNRVNVIYQIP 456
Cdd:COG1217 427 MTNMEPDGGGRVRLEFLIP 445
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
11-191 |
8.20e-68 |
|
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.
Pssm-ID: 425418 [Multi-domain] Cd Length: 187 Bit Score: 218.55 E-value: 8.20e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 11 EKIRNFSIIAHIDHGKSTLADRILEKTETVSSREMQAQ----LLDSMDLERERGITIKLNAIELnytakDGETYIFHLID 86
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGegeaGLDNLPEERERGITIKSAAVSF-----ETKDYLINLID 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 87 TPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPVINKIDLPA-ADPERVRHEVEDVIGLDAS 165
Cdd:pfam00009 76 TPGHVDFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDgAELEEVVEEVSRELLEKYG 155
|
170 180 190
....*....|....*....|....*....|..
gi 489080006 166 EA------VLASAKAGIGIEEILEQIVEKVPA 191
Cdd:pfam00009 156 EDgefvpvVPGSALKGEGVQTLLDALDEYLPS 187
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
10-485 |
2.05e-53 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 194.01 E-value: 2.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 10 QEKIRNFSIIAHIDHGKSTLADRILEKTETVSSR---EMQAQLLDSMDLERERGITIKLNAIELNYtakdgETYIFHLID 86
Cdd:PRK13351 5 LMQIRNIGILAHIDAGKTTLTERILFYTGKIHKMgevEDGTTVTDWMPQEQERGITIESAATSCDW-----DNHRINLID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 87 TPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPVINKID----------------------- 143
Cdd:PRK13351 80 TPGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDrvgadlfkvledieerfgkrplp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 144 --LPAAD--------------------------------PERVRHEV--------EDVIGLD--ASEAVLA--------- 170
Cdd:PRK13351 160 lqLPIGSedgfegvvdlitepelhfsegdggstveegpiPEELLEEVeearekliEALAEFDdeLLELYLEgeelsaeql 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 171 -------------------SAKAGIGIEEILEQIVEKVPAP------------------TGDVDAPLQALIFDSVYDAYR 213
Cdd:PRK13351 240 raplregtrsghlvpvlfgSALKNIGIEPLLDAVVDYLPSPlevppprgskdngkpvkvDPDPEKPLLALVFKVQYDPYA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 214 GVILQVRIVNGIVKPGDKIQMMSNGKTFDVTevGIFTPKAVGR---DFLATGDVGYVAAsiktVADTRVGDTVTLANNPa 290
Cdd:PRK13351 320 GKLTYLRVYSGTLRAGSQLYNGTGGKREKVG--RLFRLQGNKReevDRAKAGDIVAVAG----LKELETGDTLHDSADP- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 291 kEALHGYKQMNPMVFAGIYPIESNKYNDLREALEKLQLNDASLQFE--PETSQALGFGfrcgfLGLLHMDVIQERLEREF 368
Cdd:PRK13351 393 -VLLELLTFPEPVVSLAVEPERRGDEQKLAEALEKLVWEDPSLRVEedEETGQTILSG-----MGELHLEVALERLRREF 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 369 NIDLIMTAPSVVY-------------HVHTTD------------------------EDMIEVSNPSEF------------ 399
Cdd:PRK13351 467 KLEVNTGKPQVAYretirkmaegvyrHKKQFGgkgqfgevhlrveplergagfifvSKVVGGAIPEELipavekgireal 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 400 ---------------------PDPT-----------RVAFIE----------EPYVKAQIMVPQEFVGAVMELSQRKRGD 437
Cdd:PRK13351 547 asgplagypvtdlrvtvldgkYHPVdssesafkaaaRKAFLEafrkanpvllEPIMELEITVPTEHVGDVLGDLSQRRGR 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 489080006 438 FVTMDYIDDNRVNVIYQIPLAEiVFDFFDKLKSSTRGYASFDYDMSEY 485
Cdd:PRK13351 627 IEGTEPRGDGEVLVKAEAPLAE-LFGYATRLRSMTKGRGSFTMEFSHF 673
|
|
| EF4_III |
cd16260 |
Domain III of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly ... |
302-377 |
1.22e-50 |
|
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: 169.22 E-value: 1.22e-50
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489080006 302 PMVFAGIYPIESNKYNDLREALEKLQLNDASLQFEPETSQALGFGFRCGFLGLLHMDVIQERLEREFNIDLIMTAP 377
Cdd:cd16260 1 PMVFAGLYPVDGSDYEELRDALEKLTLNDASVTFEPETSSALGFGFRCGFLGLLHMEVFQERLEREYGLDLIITAP 76
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
1-485 |
3.05e-49 |
|
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: 182.17 E-value: 3.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 1 MNSQDLkkrqEKIRNFSIIAHIDHGKSTLADRILEKT------------ETVSsremqaqllDSMDLERERGITIKLNAI 68
Cdd:COG0480 1 MAEYPL----EKIRNIGIVAHIDAGKTTLTERILFYTgaihrigevhdgNTVM---------DWMPEEQERGITITSAAT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 69 ELNYtaKDgetYIFHLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPVINKIDLPAAD 148
Cdd:COG0480 68 TCEW--KG---HKINIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGAD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 149 PERVRHEVED---------------------VIGL-----------------------------------------DASE 166
Cdd:COG0480 143 FDRVLEQLKErlganpvplqlpigaeddfkgVIDLvtmkayvyddelgakyeeeeipaelkeeaeeareelieavaETDD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 167 AVL--------------------------------ASAKAGIGIEEILEQIVEKVPAPT-------------------GD 195
Cdd:COG0480 223 ELMekylegeelteeeikaglrkatlagkivpvlcGSAFKNKGVQPLLDAVVDYLPSPLdvpaikgvdpdtgeeverkPD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 196 VDAPLQALIFDSVYDAYRGVILQVRIVNGIVKPGDKIQMMSNGKTFDVTevGIFTPKA---VGRDFLATGDVGyVAASIK 272
Cdd:COG0480 303 DDEPFSALVFKTMTDPFVGKLSFFRVYSGTLKSGSTVYNSTKGKKERIG--RLLRMHGnkrEEVDEAGAGDIV-AVVKLK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 273 tvaDTRVGDTVTLANNPAKeaLHGYKQMNPMVFAGIYPiESNKYND-LREALEKLQLNDASLQFE--PETSQALGFGfrc 349
Cdd:COG0480 380 ---DTTTGDTLCDEDHPIV--LEPIEFPEPVISVAIEP-KTKADEDkLSTALAKLAEEDPTFRVEtdEETGQTIISG--- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 350 gfLGLLHMDVIQERLEREFNIDLIMTAPSVVY-------------------------HVHttdedmIEVSnPSE------ 398
Cdd:COG0480 451 --MGELHLEIIVDRLKREFGVEVNVGKPQVAYretirkkaeaegkhkkqsgghgqygDVW------IEIE-PLPrgegfe 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 399 ---------------------------------FP----------------DPTRVAF------------------IEEP 411
Cdd:COG0480 522 fvdkivggvipkeyipavekgireamekgvlagYPvvdvkvtlydgsyhpvDSSEMAFkiaasmafkeaakkakpvLLEP 601
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489080006 412 YVKAQIMVPQEFVGAVM-ELSQRkRGDFVTMDYIDDNRVnVIYQIPLAEIvFDFFDKLKSSTRGYASFDYDMSEY 485
Cdd:COG0480 602 IMKVEVTVPEEYMGDVMgDLNSR-RGRILGMESRGGAQV-IKAEVPLAEM-FGYATDLRSLTQGRGSFTMEFSHY 673
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
11-480 |
9.58e-49 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 179.52 E-value: 9.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 11 EKIRNFSIIAHIDHGKSTLADRILEKTETVSSR-EMQAQLLDSMDLERERGITI--KLNAIELNytakdgeTYIFHLIDT 87
Cdd:PRK10218 3 EKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRaETQERVMDSNDLEKERGITIlaKNTAIKWN-------DYRINIVDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 88 PGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPVINKIDLPAADPERVRHEVEDV-IGLDASE 166
Cdd:PRK10218 76 PGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLfVNLDATD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 167 AVL------ASAKAGIG----------IEEILEQIVEKVPAPTGDVDAPLQALIFDSVYDAYRGVILQVRIVNGIVKPGD 230
Cdd:PRK10218 156 EQLdfpivyASALNGIAgldhedmaedMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 231 KIQMM-SNGKTFD------VTEVGIftpKAVGRDFLATGDVgyvaASIKTVADTRVGDTVTLANNpaKEALHGYKQMNPM 303
Cdd:PRK10218 236 QVTIIdSEGKTRNakvgkvLGHLGL---ERIETDLAEAGDI----VAITGLGELNISDTVCDTQN--VEALPALSVDEPT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 304 V----------FAGiypiESNKYNDLREALEKLQ---LNDASLQFEpETSQAlgFGFRCGFLGLLHMDVIQERLEREfNI 370
Cdd:PRK10218 307 VsmffcvntspFCG----KEGKFVTSRQILDRLNkelVHNVALRVE-ETEDA--DAFRVSGRGELHLSVLIENMRRE-GF 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 371 DLIMTAPSVVYHvhttdedmiEVSNPSefpdptrvafiEEPYVKAQIMVPQEFVGAVMELSQRKRGDFVTMDYIDDNRVN 450
Cdd:PRK10218 379 ELAVSRPKVIFR---------EIDGRK-----------QEPYENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVR 438
|
490 500 510
....*....|....*....|....*....|....
gi 489080006 451 VIYQIPLAEIVfDFFDKLKSSTRG----YASFDY 480
Cdd:PRK10218 439 LDYVIPSRGLI-GFRSEFMTMTSGtgllYSTFSH 471
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
15-192 |
1.57e-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: 167.47 E-value: 1.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 15 NFSIIAHIDHGKSTLADRILEKTETVSSREM-QAQLLDSMDLERERGITIKLNAIELNYtakdgETYIFHLIDTPGHVDF 93
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTrKETFLDTLKEERERGITIKTGVVEFEW-----PKRRINFIDTPGHEDF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 94 TYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPVINKIDL-PAADPERVRHEVEDVIGL--------DA 164
Cdd:cd00881 76 SKETVRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRvGEEDFDEVLREIKELLKLigftflkgKD 155
|
170 180
....*....|....*....|....*...
gi 489080006 165 SEAVLASAKAGIGIEEILEQIVEKVPAP 192
Cdd:cd00881 156 VPIIPISALTGEGIEELLDAIVEHLPPP 183
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
19-485 |
2.83e-48 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 179.17 E-value: 2.83e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 19 IAHIDHGKSTLADRILEKTETVSSR---EMQAQLLDSMDLERERGITIKLNAIELNYtakDGETyiFHLIDTPGHVDFTY 95
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRIgevEDGTTTMDFMPEERERGISITSAATTCEW---KGHK--INLIDTPGHVDFTG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 96 EVSRSLAACEGAILVVDAAQGIEAQTLAnvYLALDNDLEI--LPVINKIDLPAADPERV--------RHEV--------- 156
Cdd:PRK12740 76 EVERALRVLDGAVVVVCAVGGVEPQTET--VWRQAEKYGVprIIFVNKMDRAGADFFRVlaqlqeklGAPVvplqlpige 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 157 -EDVIGL------------------------------------------DASEAVL------------------------ 169
Cdd:PRK12740 154 gDDFTGVvdllsmkayrydeggpseeieipaelldraeeareellealaEFDDELMekylegeelseeeikaglrkatla 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 170 --------ASAKAGIGIEEILEQIVEKVPAPT-----------------GDVDAPLQALIFDSVYDAYRGVILQVRIVNG 224
Cdd:PRK12740 234 geivpvfcGSALKNKGVQRLLDAVVDYLPSPLevppvdgedgeegaelaPDPDGPLVALVFKTMDDPFVGKLSLVRVYSG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 225 IVKPGDKIQMMSNGKTFDVTevGIFTPKA---VGRDFLATGDVGYVAAsiktVADTRVGDTVTLANNPAkealhgykQMN 301
Cdd:PRK12740 314 TLKKGDTLYNSGTGKKERVG--RLYRMHGkqrEEVDEAVAGDIVAVAK----LKDAATGDTLCDKGDPI--------LLE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 302 PMVFA------GIYPIESNKYNDLREALEKLQLNDASLQFE--PETSQALGFGfrcgfLGLLHMDVIQERLEREFNIDLI 373
Cdd:PRK12740 380 PMEFPepvislAIEPKDKGDEEKLSEALGKLAEEDPTLRVErdEETGQTILSG-----MGELHLDVALERLKREYGVEVE 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 374 MTAPSVVY-------------------------HVHttdedmIEVS-NPS----EFPD-------PT------------- 403
Cdd:PRK12740 455 TGPPQVPYretirkkaeghgrhkkqsgghgqfgDVW------LEVEpLPRgegfEFVDkvvggavPRqyipavekgvrea 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 404 -------------------------------------RVAFIE----------EPYVKAQIMVPQEFVGAVMELSQRKRG 436
Cdd:PRK12740 529 lekgvlagypvvdvkvtltdgsyhsvdssemafkiaaRLAFREalpkakpvllEPIMKVEVSVPEEFVGDVIGDLSSRRG 608
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 489080006 437 DFVTMDYiDDNRVNVIYQIPLAEIvFDFFDKLKSSTRGYASFDYDMSEY 485
Cdd:PRK12740 609 RILGMES-RGGGDVVRAEVPLAEM-FGYATDLRSLTQGRGSFSMEFSHY 655
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
12-192 |
1.96e-44 |
|
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity.
Pssm-ID: 206678 [Multi-domain] Cd Length: 194 Bit Score: 156.60 E-value: 1.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 12 KIRNFSIIAHIDHGKSTLADRILEKTETVSSRE-MQAQLLDSMDLERERGITIKLNAIELNYtaKDgetYIFHLIDTPGH 90
Cdd:cd01891 1 KIRNIAIIAHVDHGKTTLVDALLKQSGTFRENEeVGERVMDSNDLERERGITILAKNTAITY--KD---TKINIIDTPGH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 91 VDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPVINKIDLPAADPERVRHEVEDV-IGLDASE--- 166
Cdd:cd01891 76 ADFGGEVERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDRPDARPEEVVDEVFDLfLELNATDeql 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 489080006 167 ---AVLASAKAGIG----------IEEILEQIVEKVPAP 192
Cdd:cd01891 156 dfpIVYASAKNGWAslnlddpsedLDPLFETIIEHVPAP 194
|
|
| EF4_II |
cd03699 |
Domain II of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly ... |
200-285 |
8.91e-43 |
|
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: 148.34 E-value: 8.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 200 LQALIFDSVYDAYRGVILQVRIVNGIVKPGDKIQMMSNGKTFDVTEVGIFTPKAVGRDFLATGDVGYVAASIKTVADTRV 279
Cdd:cd03699 1 LRALIFDSWYDPYRGVVVLVRVFDGTLKKGDKIRFMATGKEYEVLEVGVFTPKMVPTDELSAGEVGYIIAGIKSVKDARV 80
|
....*.
gi 489080006 280 GDTVTL 285
Cdd:cd03699 81 GDTITL 86
|
|
| lepA_C |
cd03709 |
lepA_C: This family represents the C-terminal region of LepA, a GTP-binding protein localized ... |
410-489 |
1.87e-42 |
|
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: 147.25 E-value: 1.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 410 EPYVKAQIMVPQEFVGAVMELSQRKRGDFVTMDYIDDNRVNVIYQIPLAEIVFDFFDKLKSSTRGYASFDYDMSEYRRSQ 489
Cdd:cd03709 1 EPFVKATIITPSEYLGAIMELCQERRGVQKDMEYLDANRVMLTYELPLAEIVYDFFDKLKSISKGYASLDYELIGYRESD 80
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
14-192 |
2.12e-41 |
|
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: 149.30 E-value: 2.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 14 RNFSIIAHIDHGKSTLADRILEKTETVSSREM-QAQLLDSMDLERERGITIKLNAIELNYTAK----DGETYIFHLIDTP 88
Cdd:cd01885 1 RNICIIAHVDHGKTTLSDSLLASAGIISEKLAgKARYLDTREDEQERGITIKSSAISLYFEYEeekmDGNDYLINLIDSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 89 GHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPVINKIDL--------PAADPERVRHEVEDV- 159
Cdd:cd01885 81 GHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDRlilelklsPEEAYQRLLRIVEDVn 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489080006 160 --IGLDASEA---------------VLASAKAGIG--------IEEILEQIVEKVPAP 192
Cdd:cd01885 161 aiIETYAPEEfkqekwkfspqkgnvAFGSALDGWGftiikfadIYAVLEMVVKHLPSP 218
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
4-381 |
6.37e-37 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 146.55 E-value: 6.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 4 QDLKKRQEKIRNFSIIAHIDHGKSTLADRILEKTETVSSREMQAQL-LDSMDLERERGITIKLNAIELnYTAKDGETYIF 82
Cdd:PRK07560 11 LELMKNPEQIRNIGIIAHIDHGKTTLSDNLLAGAGMISEELAGEQLaLDFDEEEQARGITIKAANVSM-VHEYEGKEYLI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 83 HLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPVINKID-------LpaaDPERVRHE 155
Cdd:PRK07560 90 NLIDTPGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKPVLFINKVDrlikelkL---TPQEMQQR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 156 VEDVIG-------------------LDASEAVLA--SA------------KAGIGIEEI--------------------- 181
Cdd:PRK07560 167 LLKIIKdvnklikgmapeefkekwkVDVEDGTVAfgSAlynwaisvpmmqKTGIKFKDIidyyekgkqkelaekaplhev 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 182 -LEQIVEKVPAPT------------GDV-------------DAPLQALIFDSVYDAYRGVILQVRIVNGIVKPGDKIQMM 235
Cdd:PRK07560 247 vLDMVVKHLPNPIeaqkyripkiwkGDLnsevgkamlncdpNGPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 236 SNGKTFDVTEVGIFT-PKAVGRDFLATGDVGYVAAsiktVADTRVGDTV-TLANNPAKEALHGYKQmnPMVFAGIYPIES 313
Cdd:PRK07560 327 GAKKKNRVQQVGIYMgPEREEVEEIPAGNIAAVTG----LKDARAGETVvSVEDMTPFESLKHISE--PVVTVAIEAKNP 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 314 NKYNDLREALEKLQLNDASLQFE--PETSQALGFGfrcgfLGLLHMDVIQERLEREFNIDLIMTAPSVVY 381
Cdd:PRK07560 401 KDLPKLIEVLRQLAKEDPTLVVKinEETGEHLLSG-----MGELHLEVITYRIKRDYGIEVVTSEPIVVY 465
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
4-435 |
1.29e-35 |
|
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: 142.73 E-value: 1.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 4 QDLKKRQEKIRNFSIIAHIDHGKSTLADRILEKTETVSSREMQAQL-LDSMDLERERGITIKLNAIELNYTAkDGETYIF 82
Cdd:TIGR00490 10 KELMWKPKFIRNIGIVAHIDHGKTTLSDNLLAGAGMISEELAGQQLyLDFDEQEQERGITINAANVSMVHEY-EGNEYLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 83 HLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPVINKID------------------- 143
Cdd:TIGR00490 89 NLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKPVLFINKVDrlinelkltpqelqerfik 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 144 --------LPAADPERVRHEVEdvIGLDASEAVLASA------------KAGIGIEEI---------------------- 181
Cdd:TIGR00490 169 iitevnklIKAMAPEEFRDKWK--VRVEDGSVAFGSAyynwaisvpsmkKTGIGFKDIykyckedkqkelakksplhqvv 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 182 LEQIVEKVPAP------------TGDVDA-------------PLQALIFDSVYDAYRGVILQVRIVNGIVKPGDKIQMMS 236
Cdd:TIGR00490 247 LDMVIRHLPSPieaqkyripviwKGDLNSevgkamlncdpkgPLALMITKIVVDKHAGEVAVGRLYSGTIRPGMEVYIVD 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 237 NGKTFDVTEVGIFT-PKAVGRDFLATGDVGYVAASIKTVADTRVGDTVTlaNNPAKEALHGYKQmnPMVFAGIYPIESNK 315
Cdd:TIGR00490 327 RKAKARIQQVGVYMgPERVEVDEIPAGNIVAVIGLKDAVAGETICTTVE--NITPFESIKHISE--PVVTVAIEAKNTKD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 316 YNDLREALEKLQLNDASLQFE--PETSQALGFGfrcgfLGLLHMDVIQERLEREFNIDLIMTAPSVVYHvhttdEDMIEV 393
Cdd:TIGR00490 403 LPKLIEVLRQVAKEDPTVHVEinEETGEHLISG-----MGELHLEIIVEKIREDYGLDVETSPPIVVYR-----ETVTGT 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 489080006 394 SNPSEFPDP---TRVAFIEEPYVKAQIMVPQEfvGAVMELSQRKR 435
Cdd:TIGR00490 473 SPVVEGKSPnkhNRFYIVVEPLEESVIQAFKE--GKIVDMKMKKK 515
|
|
| EF-G |
TIGR00484 |
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ... |
11-485 |
4.80e-35 |
|
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: 140.71 E-value: 4.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 11 EKIRNFSIIAHIDHGKSTLADRIL---EKTETVSSREMQAQLLDSMDLERERGITIKLNAielnyTAKDGETYIFHLIDT 87
Cdd:TIGR00484 8 NRFRNIGISAHIDAGKTTTTERILfytGRIHKIGEVHDGAATMDWMEQEKERGITITSAA-----TTVFWKGHRINIIDT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 88 PGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPVINKIDLPAADPERVRHEVEDVIG------ 161
Cdd:TIGR00484 83 PGHVDFTVEVERSLRVLDGAVAVLDAVGGVQPQSETVWRQANRYEVPRIAFVNKMDKTGANFLRVVNQIKQRLGanavpi 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 162 -------------------------------------------------------------------LDASEAVLASAKA 174
Cdd:TIGR00484 163 qlpigaednfigvidlvemkayffngdkgtkaiekeipsdlleqakelrenlveavaefdeelmekyLEGEELTIEEIKN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 175 GI---------------------GIEEILEQIVEKVPAPTgDV--------------------DAPLQALIFDSVYDAYR 213
Cdd:TIGR00484 243 AIrkgvlnceffpvlcgsafknkGVQLLLDAVVDYLPSPT-DVpaikgidpdtekeierkasdDEPFSALAFKVATDPFV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 214 GVILQVRIVNGIVKPGDKIQMMSNGKTFDVTEvgIFTPKAVGRDFLATGDVGYVAASIKtVADTRVGDTVTLANNPAkeA 293
Cdd:TIGR00484 322 GQLTFVRVYSGVLKSGSYVKNSRKNKKERVGR--LVKMHANNREEIKEVRAGDICAAIG-LKDTTTGDTLCDPKIDV--I 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 294 LHGYKQMNPMVFAGIYPIESNKYNDLREALEKLQLNDASL--QFEPETSQALGFGfrcgfLGLLHMDVIQERLEREFNID 371
Cdd:TIGR00484 397 LERMEFPEPVISLAVEPKTKADQEKMGIALGKLAEEDPTFrtFTDPETGQTIIAG-----MGELHLDIIVDRMKREFKVE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 372 LIMTAPSVVY-------------------------HV----HTTDEDMIEVSN-------PSE----------------- 398
Cdd:TIGR00484 472 ANVGAPQVAYretirskvevegkhakqsggrgqygHVkirfEPLEPKGYEFVNeikggviPREyipavdkglqeamesgp 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 399 ---FP----------------DPTRVAF------------------IEEPYVKAQIMVPQEFVGAVMELSQRKRGDFVTM 441
Cdd:TIGR00484 552 lagYPvvdikatlfdgsyhdvDSSEMAFklaaslafkeagkkanpvLLEPIMKVEVEVPEEYMGDVMGDLSSRRGIIEGM 631
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 489080006 442 DYiDDNRVNVIYQIPLAEIvFDFFDKLKSSTRGYASFDYDMSEY 485
Cdd:TIGR00484 632 EA-RGNVQKIKAEVPLSEM-FGYATDLRSFTQGRGTYSMEFLHY 673
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
14-192 |
5.92e-31 |
|
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: 120.07 E-value: 5.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 14 RNFSIIAHIDHGKSTLADRILEKT--ETVSSREMQAQL--LDSMDLERERGITIKLNAIELNYTAKDGETYIFHLIDTPG 89
Cdd:cd04167 1 RNVCIAGHLHHGKTSLLDMLIEQThkRTPSVKLGWKPLryTDTRKDEQERGISIKSNPISLVLEDSKGKSYLINIIDTPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 90 HVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPVINKID-------LPAADPER-VRHEVEDVIG 161
Cdd:cd04167 81 HVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDrlilelkLPPTDAYYkLRHTIDEINN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489080006 162 LDASEAVL--------------ASAKAGI--------GIEEILEQIVEKVPAP 192
Cdd:cd04167 161 YIASFSTTegflvspelgnvlfASSKFGFcftlesfaKKYGLVDSILSHIPSP 213
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
9-143 |
9.74e-30 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 125.16 E-value: 9.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 9 RQEKIRNFSIIAHIDHGKSTLADRILEKTETVSSREM-QAQLLDSMDLERERGITIKLNAIELNY-----TAKDGETYIF 82
Cdd:PTZ00416 15 NPDQIRNMSVIAHVDHGKSTLTDSLVCKAGIISSKNAgDARFTDTRADEQERGITIKSTGISLYYehdleDGDDKQPFLI 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489080006 83 HLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNdlEILPV--INKID 143
Cdd:PTZ00416 95 NLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQE--RIRPVlfINKVD 155
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
15-164 |
1.26e-29 |
|
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: 117.98 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 15 NFSIIAHIDHGKSTLADRILEKTETVSS----REMQAQLlDSMDLERERGITIKLNAIelNYTAKDgetYIFHLIDTPGH 90
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGRIHKigevHGGGATM-DWMEQERERGITIQSAAT--TCFWKD---HRINIIDTPGH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 91 VDFTYEVSRSLAACEGAILVVDAAQGIEAQTL-----ANVYLaldndleiLPVI---NKIDLPAADPERVRHEVEDVIGL 162
Cdd:cd01886 75 VDFTIEVERSLRVLDGAVAVFDAVAGVQPQTEtvwrqADRYG--------VPRIafvNKMDRTGADFYRVVEQIREKLGA 146
|
..
gi 489080006 163 DA 164
Cdd:cd01886 147 NP 148
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
14-213 |
3.78e-28 |
|
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.
Pssm-ID: 206732 [Multi-domain] Cd Length: 268 Bit Score: 113.85 E-value: 3.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 14 RNFSIIAHIDHGKSTLADRIL------EKTETVSSR-EMQAQLLDSMDLERERGITIKLNAIELNYtaKDgetYIFHLID 86
Cdd:cd04169 3 RTFAIISHPDAGKTTLTEKLLlfggaiQEAGAVKARkSRKHATSDWMEIEKQRGISVTSSVMQFEY--KG---CVINLLD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 87 TPGHVDF---TYevsRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPVINKIDLPAADPERVRHEVEDVIGLD 163
Cdd:cd04169 78 TPGHEDFsedTY---RTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDREGRDPLELLDEIENELGID 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489080006 164 ASEAV--LASAKAGIGIEEILEQIVE-----------KVPAPTGDVDAPLQALIFDSVYDAYR 213
Cdd:cd04169 155 CAPMTwpIGMGKDFKGVYDRYDKEIYlyergaggaikAPEETKGLDDPKLDELLGEDLAEQLR 217
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
15-189 |
3.82e-27 |
|
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: 110.02 E-value: 3.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 15 NFSIIAHIDHGKSTLADRILEKTETVSSR----EMQAQLlDSMDLERERGITIKLNAIELNYtaKDGETYIfhlIDTPGH 90
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIRELgsvdKGTTRT-DSMELERQRGITIFSAVASFQW--EDTKVNI---IDTPGH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 91 VDFTYEVSRSLAACEGAILVVDAAQGIEAQTlaNVYLALDNDLEIlPVI---NKIDLPAADPERVRHEVEDVIgldaSEA 167
Cdd:cd04168 75 MDFIAEVERSLSVLDGAILVISAVEGVQAQT--RILFRLLRKLNI-PTIifvNKIDRAGADLEKVYQEIKEKL----SPD 147
|
170 180
....*....|....*....|....*..
gi 489080006 168 VLASAKAG-----IGIEEILEQIVEKV 189
Cdd:cd04168 148 IVPMQKVGlypniCDTNNIDDEQIETV 174
|
|
| EFG_C |
pfam00679 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
408-495 |
3.89e-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: 3.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 408 IEEPYVKAQIMVPQEFVGAVMELSQRKRGDFVTMDYIDDNRVNVIYQIPLAEIvFDFFDKLKSSTRGYASFDYDMSEYRR 487
Cdd:pfam00679 2 LLEPIEKVTIDVPEEYVGDVISDLNSRRGEILDMDPDDGGRVVIEAEVPLAEL-FGFATELRSLTKGRGSFSMEFSGYQP 80
|
....*...
gi 489080006 488 SQLVKMDI 495
Cdd:pfam00679 81 VPGDILDR 88
|
|
| Elongation_Factor_C |
cd01514 |
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ... |
410-486 |
1.66e-26 |
|
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: 102.95 E-value: 1.66e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489080006 410 EPYVKAQIMVPQEFVGAVMELSQRKRGDFVTMDYIDDNRVNVIYQIPLAEIvFDFFDKLKSSTRGYASFDYDMSEYR 486
Cdd:cd01514 1 EPIMKVEITVPEEYLGAVIGDLSKRRGEILGMEPRGTGRVVIKAELPLAEM-FGFATDLRSLTQGRASFSMEFSHYE 76
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
9-143 |
7.16e-26 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 112.90 E-value: 7.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 9 RQEKIRNFSIIAHIDHGKSTLADRILEKTETVSSREM-QAQLLDSMDLERERGITIKLNAIELNYT-----------AKD 76
Cdd:PLN00116 15 KKHNIRNMSVIAHVDHGKSTLTDSLVAAAGIIAQEVAgDVRMTDTRADEAERGITIKSTGISLYYEmtdeslkdfkgERD 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489080006 77 GETYIFHLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNdlEILPV--INKID 143
Cdd:PLN00116 95 GNEYLINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTETVLRQALGE--RIRPVltVNKMD 161
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
15-285 |
8.67e-25 |
|
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444074 [Multi-domain] Cd Length: 423 Bit Score: 107.33 E-value: 8.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 15 NFSIIAHIDHGKSTLADRILEKTETVSSREMQ----------------AQLLDSMDLERERGITIKLNAIELNyTAKdge 78
Cdd:COG5256 9 NLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEkyeeeaekkgkesfkfAWVMDRLKEERERGVTIDLAHKKFE-TDK--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 79 tYIFHLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPV-INKIDLPAADPER---VRH 154
Cdd:COG5256 85 -YYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVaVNKMDAVNYSEKRyeeVKE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 155 EVEDV---IGLDASEA--VLASAKAGIGIEE-----------ILEQIVEKVPAPTGDVDAPLQALIFDsVYD-AYRGVIL 217
Cdd:COG5256 164 EVSKLlkmVGYKVDKIpfIPVSAWKGDNVVKksdnmpwyngpTLLEALDNLKEPEKPVDKPLRIPIQD-VYSiSGIGTVP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 218 QVRIVNGIVKPGDKIQMMSNGKTFDV-------TE---------VGiFTPKAVGRDFLATGDVGYVAASIKTVADTRVGD 281
Cdd:COG5256 243 VGRVETGVLKVGDKVVFMPAGVVGEVksiemhhEEleqaepgdnIG-FNVRGVEKNDIKRGDVAGHPDNPPTVAEEFTAQ 321
|
....
gi 489080006 282 TVTL 285
Cdd:COG5256 322 IVVL 325
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
15-285 |
2.25e-24 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 106.16 E-value: 2.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 15 NFSIIAHIDHGKSTLADRILEKTETVSSREMQ----------------AQLLDSMDLERERGITiklnaIELNYTAKDGE 78
Cdd:PRK12317 8 NLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEelreeakekgkesfkfAWVMDRLKEERERGVT-----IDLAHKKFETD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 79 TYIFHLIDTPGHVDFTYEVSRSLAACEGAILVVDA--AQGIEAQTLANVYLALDNDLEILPV-INKIDLPAADPER---V 152
Cdd:PRK12317 83 KYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAAddAGGVMPQTREHVFLARTLGINQLIVaINKMDAVNYDEKRyeeV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 153 RHEVEDV---IGLDASEA--VLASAKAGIGIEE-----------ILEQIVEKVPAPTGDVDAPLQALIfdsvYDAYR--- 213
Cdd:PRK12317 163 KEEVSKLlkmVGYKPDDIpfIPVSAFEGDNVVKksenmpwyngpTLLEALDNLKPPEKPTDKPLRIPI----QDVYSisg 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 214 -GVILQVRIVNGIVKPGDKIQMMSNGKTFDVTEVGI---------------FTPKAVGRDFLATGDVGYVAASIKTVADT 277
Cdd:PRK12317 239 vGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMhheelpqaepgdnigFNVRGVGKKDIKRGDVCGHPDNPPTVAEE 318
|
....*...
gi 489080006 278 RVGDTVTL 285
Cdd:PRK12317 319 FTAQIVVL 326
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
18-187 |
1.96e-23 |
|
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: 97.16 E-value: 1.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 18 IIAHIDHGKSTLADRIlEKTeTVSSREMqaqlldsmdlereRGITIKLNAIELNYtAKDGETYIFhlIDTPGHVDFTYEV 97
Cdd:cd01887 5 VMGHVDHGKTTLLDKI-RKT-NVAAGEA-------------GGITQHIGAYQVPI-DVKIPGITF--IDTPGHEAFTNMR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 98 SRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPVINKIDLP---AADPERVRHEV--EDVIGLDASE---AVL 169
Cdd:cd01887 67 ARGASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKPygtEADPERVKNELseLGLVGEEWGGdvsIVP 146
|
170
....*....|....*...
gi 489080006 170 ASAKAGIGIEEILEQIVE 187
Cdd:cd01887 147 ISAKTGEGIDDLLEAILL 164
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
17-232 |
4.53e-19 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 91.43 E-value: 4.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 17 SIIAHIDHGKSTLADRIlEKTETvSSREMQaqlldsmdlererGITIKLNAIELNYTAKDGETYIFHLiDTPGHVDFTYE 96
Cdd:CHL00189 248 TILGHVDHGKTTLLDKI-RKTQI-AQKEAG-------------GITQKIGAYEVEFEYKDENQKIVFL-DTPGHEAFSSM 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 97 VSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPVINKIDLPAADPERVRHEV--EDVI----GLDASeAVLA 170
Cdd:CHL00189 312 RSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANTERIKQQLakYNLIpekwGGDTP-MIPI 390
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489080006 171 SAKAGIGIEEILEQI-----VEKVPAptgDVDAPLQALIFDSVYDAYRGVILQVRIVNGIVKPGDKI 232
Cdd:CHL00189 391 SASQGTNIDKLLETIlllaeIEDLKA---DPTQLAQGIILEAHLDKTKGPVATILVQNGTLHIGDII 454
|
|
| EFG_III-like |
cd16257 |
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G ... |
302-375 |
6.30e-19 |
|
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: 81.24 E-value: 6.30e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489080006 302 PMVFAGIYPIESNKYNDLREALEKLQLNDASLQFEPETSQalgFGFRCGFLGLLHMDVIQERLEREFNIDLIMT 375
Cdd:cd16257 1 PVVFVTVEVKNPLDQEKLLEGLERLSEEDPALQVYREEST---GEFILSGLGELHLEIIVARLEREYGVELVVS 71
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
4-164 |
7.06e-19 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 90.19 E-value: 7.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 4 QDLKKRqekiRNFSIIAHIDHGKSTLADRIL------EKTETVSSREMQAQLL-DSMDLERERGITIKLNAIELNYtaKD 76
Cdd:PRK00741 5 QEVAKR----RTFAIISHPDAGKTTLTEKLLlfggaiQEAGTVKGRKSGRHATsDWMEMEKQRGISVTSSVMQFPY--RD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 77 getYIFHLIDTPGHVDF---TYevsRSLAACEGAILVVDAAQGIEAQT--LANVYLAldNDLEILPVINKIDLPAADPER 151
Cdd:PRK00741 79 ---CLINLLDTPGHEDFsedTY---RTLTAVDSALMVIDAAKGVEPQTrkLMEVCRL--RDTPIFTFINKLDRDGREPLE 150
|
170
....*....|...
gi 489080006 152 VRHEVEDVIGLDA 164
Cdd:PRK00741 151 LLDEIEEVLGIAC 163
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
15-235 |
8.09e-18 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 86.42 E-value: 8.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 15 NFSIIAHIDHGKSTLADRILE-KTETVSSREMQAQLLDSMDLERERGITIKLNAIELNyTAKdgeTYIFHlIDTPGHVDF 93
Cdd:PLN03127 63 NVGTIGHVDHGKTTLTAAITKvLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYE-TAK---RHYAH-VDCPGHADY 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 94 TYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPV-INKIDLpAADPE---RVRHEVEDVIGL-----DA 164
Cdd:PLN03127 138 VKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVfLNKVDV-VDDEElleLVEMELRELLSFykfpgDE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 165 SEAVLASAKAGI----------GIEEILEQIVEKVPAPTGDVDAPLQALIFDSVYDAYRGVILQVRIVNGIVKPGDKIQM 234
Cdd:PLN03127 217 IPIIRGSALSALqgtndeigknAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEEVEI 296
|
.
gi 489080006 235 M 235
Cdd:PLN03127 297 V 297
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
15-248 |
2.31e-17 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 84.23 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 15 NFSIIAHIDHGKSTLADRIlekTETVSSREM-QAQLLDSMDL---ERERGITIKLNAIElnYtakdgETYIFHL--IDTP 88
Cdd:PRK12736 14 NIGTIGHVDHGKTTLTAAI---TKVLAERGLnQAKDYDSIDAapeEKERGITINTAHVE--Y-----ETEKRHYahVDCP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 89 GHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPV-INKIDLpAADPER---VRHEVED------ 158
Cdd:PRK12736 84 GHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVfLNKVDL-VDDEELlelVEMEVREllseyd 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 159 -------VIGLDASEAVLASAKAGIGIEEILEQIVEKVPAPTGDVDAPLQALIFDSVYDAYRGVILQVRIVNGIVKPGDK 231
Cdd:PRK12736 163 fpgddipVIRGSALKALEGDPKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGDE 242
|
250
....*....|....*..
gi 489080006 232 IQMMSNGKTFDVTEVGI 248
Cdd:PRK12736 243 VEIVGIKETQKTVVTGV 259
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
15-248 |
7.89e-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: 82.90 E-value: 7.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 15 NFSIIAHIDHGKSTLADRI---LEKTETVSSREMQAqlLDSMDLERERGITIKLNAIELnytakDGETYIFHLIDTPGHV 91
Cdd:TIGR00485 14 NVGTIGHVDHGKTTLTAAIttvLAKEGGAAARAYDQ--IDNAPEEKARGITINTAHVEY-----ETETRHYAHVDCPGHA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 92 DFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPV-INKIDLpAADPE---RVRHEVED--------- 158
Cdd:TIGR00485 87 DYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKCDM-VDDEElleLVEMEVREllsqydfpg 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 159 ----VIGLDASEAVLASAKAGIGIEEILEQIVEKVPAPTGDVDAPLQALIFDSVYDAYRGVILQVRIVNGIVKPGDKIQM 234
Cdd:TIGR00485 166 ddtpIIRGSALKALEGDAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEI 245
|
250
....*....|....
gi 489080006 235 MSNGKTFDVTEVGI 248
Cdd:TIGR00485 246 VGLKDTRKTTVTGV 259
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
15-260 |
1.51e-16 |
|
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: 83.00 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 15 NFSIIAHIDHGKSTLADRIlekTETVSSREMQaqlldsmdlERERGITiklnaIELNYTAKDGETYIFHLIDTPGHVDFT 94
Cdd:TIGR00475 2 IIATAGHVDHGKTTLLKAL---TGIAADRLPE---------EKKRGMT-----IDLGFAYFPLPDYRLGFIDVPGHEKFI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 95 YEVSRSLAACEGAILVVDAAQGIEAQTLANV-YLALDNDLEILPVINKIDLpaADPERVrHEVE--------DVIGLDAS 165
Cdd:TIGR00475 65 SNAIAGGGGIDAALLVVDADEGVMTQTGEHLaVLDLLGIPHTIVVITKADR--VNEEEI-KRTEmfmkqilnSYIFLKNA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 166 EAVLASAKAGIGIEEI---LEQIVEKvpAPTGDVDAPLQALIfDSVYdAYRGVILQVR--IVNGIVKPGDKIQMMSNGKT 240
Cdd:TIGR00475 142 KIFKTSAKTGQGIGELkkeLKNLLES--LDIKRIQKPLRMAI-DRAF-KVKGAGTVVTgtAFSGEVKVGDNLRLLPINHE 217
|
250 260
....*....|....*....|...
gi 489080006 241 FDVTEV---GIFTPKAVGRDFLA 260
Cdd:TIGR00475 218 VRVKAIqaqNQDVEIAYAGQRIA 240
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
18-195 |
1.91e-16 |
|
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 442507 [Multi-domain] Cd Length: 630 Bit Score: 82.65 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 18 IIA---HIDHGKSTL--------ADRILEktetvssremqaqlldsmdlERERGITiklnaIELNY---TAKDGETYIFh 83
Cdd:COG3276 2 IIGtagHIDHGKTTLvkaltgidTDRLKE--------------------EKKRGIT-----IDLGFaylPLPDGRRLGF- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 84 lIDTPGHVDFtyeVSRSLAACEG---AILVVDAAQGIEAQT---LAnvYLALdndLEI---LPVINKIDLpaADPER--- 151
Cdd:COG3276 56 -VDVPGHEKF---IKNMLAGAGGidlVLLVVAADEGVMPQTrehLA--ILDL---LGIkrgIVVLTKADL--VDEEWlel 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489080006 152 VRHEVEDVI---GLDASEAVLASAKAGIGIEEI---LEQIVEKVPAPTGD 195
Cdd:COG3276 125 VEEEIRELLagtFLEDAPIVPVSAVTGEGIDELraaLDALAAAVPARDAD 174
|
|
| tufA |
CHL00071 |
elongation factor Tu |
15-248 |
3.17e-16 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 81.16 E-value: 3.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 15 NFSIIAHIDHGKSTLADRIlekTETVSSREMQAQL----LDSMDLERERGITIKLNAIElnYtakdgETYIFHL--IDTP 88
Cdd:CHL00071 14 NIGTIGHVDHGKTTLTAAI---TMTLAAKGGAKAKkydeIDSAPEEKARGITINTAHVE--Y-----ETENRHYahVDCP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 89 GHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPV-INKIDLpAADPE---RVRHEVEDVI---- 160
Cdd:CHL00071 84 GHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVfLNKEDQ-VDDEElleLVELEVRELLskyd 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 161 ------------GLDASEAVLASAKAGIG-------IEEILEQIVEKVPAPTGDVDAPLQALIFDSVYDAYRGVILQVRI 221
Cdd:CHL00071 163 fpgddipivsgsALLALEALTENPKIKRGenkwvdkIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGRI 242
|
250 260
....*....|....*....|....*..
gi 489080006 222 VNGIVKPGDKIQMMSNGKTFDVTEVGI 248
Cdd:CHL00071 243 ERGTVKVGDTVEIVGLRETKTTTVTGL 269
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
21-187 |
5.26e-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: 76.10 E-value: 5.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 21 HIDHGKSTLAdRILEKTETvssremqaqllDSMDLERERGITIKLNAIELNYtaKDGETYIFhlIDTPGHVDFtyeVSRS 100
Cdd:cd04171 7 HIDHGKTTLI-KALTGIET-----------DRLPEEKKRGITIDLGFAYLDL--PDGKRLGF--IDVPGHEKF---VKNM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 101 LAACEG---AILVVDAAQGIEAQTLAnvYLALDNDLEI---LPVINKIDLpaADPERVRHEVEDVI------GLDASEAV 168
Cdd:cd04171 68 LAGAGGidaVLLVVAADEGIMPQTRE--HLEILELLGIkkgLVVLTKADL--VDEDRLELVEEEILellagtFLADAPIF 143
|
170
....*....|....*....
gi 489080006 169 LASAKAGIGIEEILEQIVE 187
Cdd:cd04171 144 PVSSVTGEGIEELKNYLDE 162
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
15-161 |
5.85e-16 |
|
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: 78.40 E-value: 5.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 15 NFSIIAHIDHGKSTLADRILEKTETVS---SREMQAQLLDSMDLERERGITIKLNAIELNYTAKDgetyiFHLIDTPGHV 91
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDrlgRVEDGNTVSDYDPEEKKRKMSIETSVAPLEWNGHK-----INLIDTPGYA 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489080006 92 DFTYEVSRSLAACEGAILVVDAAQGIEAQTlANVYLALDnDLEI--LPVINKIDLPAADPERVRHEVEDVIG 161
Cdd:cd04170 76 DFVGETLSALRAVDAALIVVEAQSGVEVGT-EKVWEFLD-DAKLprIIFINKMDRARADFDKTLAALREAFG 145
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
15-240 |
1.39e-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: 79.36 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 15 NFSIIAHIDHGKSTLADRIL-----------EKTETVS-SREMQ----AQLLDSMDLERERGITIKLNAIelnYTAKDGE 78
Cdd:COG2895 19 RFITCGSVDDGKSTLIGRLLydtksifedqlAALERDSkKRGTQeidlALLTDGLQAEREQGITIDVAYR---YFSTPKR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 79 TYIfhLIDTPGHVDFTyevsRSLA----ACEGAILVVDAAQGIEAQT-----LA------NVYLAldndleilpvINKID 143
Cdd:COG2895 96 KFI--IADTPGHEQYT----RNMVtgasTADLAILLIDARKGVLEQTrrhsyIAsllgirHVVVA----------VNKMD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 144 LPAADPERVRHEVEDV------IGLDASEAVLASAKAGIGIEE------------ILEqIVEKVPAPTGDVDAPL----Q 201
Cdd:COG2895 160 LVDYSEEVFEEIVADYrafaakLGLEDITFIPISALKGDNVVErsenmpwydgptLLE-HLETVEVAEDRNDAPFrfpvQ 238
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 489080006 202 AlifdsVY---DAYRGVilQVRIVNGIVKPGDKIQMMSNGKT 240
Cdd:COG2895 239 Y-----VNrpnLDFRGY--AGTIASGTVRVGDEVVVLPSGKT 273
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
15-144 |
3.16e-15 |
|
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN.
Pssm-ID: 206729 [Multi-domain] Cd Length: 209 Bit Score: 74.91 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 15 NFSIIAHIDHGKSTLADRILEKT--------ETVSSREMQ---------AQLLDSMDLERERGITIKLNAIelnYTAKDG 77
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSksifedqlAALERSKSSgtqgekldlALLVDGLQAEREQGITIDVAYR---YFSTPK 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489080006 78 ETYIfhLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLAldnDL----EILPVINKIDL 144
Cdd:cd04166 78 RKFI--IADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIA---SLlgirHVVVAVNKMDL 143
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
25-187 |
3.31e-15 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 73.26 E-value: 3.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 25 GKSTLADRILEKTETVSSREMqaqlldsmdlererGITIKLNAIELNYtakDGETYIFHLIDTPGHVDFTYEVSRSLAA- 103
Cdd:cd00882 9 GKSSLLNALLGGEVGEVSDVP--------------GTTRDPDVYVKEL---DKGKVKLVLVDTPGLDEFGGLGREELARl 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 104 ----CEGAILVVDAAQGIEAQTLANVYLAL--DNDLEILPVINKIDLPAADPERVRHEVEDVIGLDASEAVLASAKAGIG 177
Cdd:cd00882 72 llrgADLILLVVDSTDRESEEDAKLLILRRlrKEGIPIILVGNKIDLLEEREVEELLRLEELAKILGVPVFEVSAKTGEG 151
|
170
....*....|
gi 489080006 178 IEEILEQIVE 187
Cdd:cd00882 152 VDELFEKLIE 161
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
15-274 |
7.21e-15 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 77.35 E-value: 7.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 15 NFSIIAHIDHGKSTLADRILEKTETV-SSREMQAQLLDSMDLERERGITIKLNAIELnytakDGETYIFHLIDTPGHVDF 93
Cdd:PLN03126 83 NIGTIGHVDHGKTTLTAALTMALASMgGSAPKKYDEIDAAPEERARGITINTATVEY-----ETENRHYAHVDCPGHADY 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 94 TYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPV-INKIDLpaADPER----VRHEVEDVI-------- 160
Cdd:PLN03126 158 VKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVfLNKQDQ--VDDEEllelVELEVRELLssyefpgd 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 161 --------GLDASEAVLASAKAGIG-------IEEILEQIVEKVPAPTGDVDAPLQALIFDSVYDAYRGVILQVRIVNGI 225
Cdd:PLN03126 236 dipiisgsALLALEALMENPNIKRGdnkwvdkIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGT 315
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 489080006 226 VKPGDKIQMMSNGKTFDVTEVGIFTPKAVGRDFLATGDVGYVAASIKTV 274
Cdd:PLN03126 316 VKVGETVDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKA 364
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
15-248 |
8.59e-15 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 76.42 E-value: 8.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 15 NFSIIAHIDHGKSTLADRILekteTVSSREMQAQLL--DSMDL---ERERGITIKLNAIElnYtakdgETYIFHL--IDT 87
Cdd:PRK12735 14 NVGTIGHVDHGKTTLTAAIT----KVLAKKGGGEAKayDQIDNapeEKARGITINTSHVE--Y-----ETANRHYahVDC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 88 PGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPV-INKIDLpAADPER---VRHEVED----- 158
Cdd:PRK12735 83 PGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVfLNKCDM-VDDEELlelVEMEVREllsky 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 159 --------VI---GLDASEAVlASAKAGIGIEEILEQIVEKVPAPTGDVDAPLQALIFDSVYDAYRGVILQVRIVNGIVK 227
Cdd:PRK12735 162 dfpgddtpIIrgsALKALEGD-DDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVK 240
|
250 260
....*....|....*....|.
gi 489080006 228 PGDKIQMMSNGKTFDVTEVGI 248
Cdd:PRK12735 241 VGDEVEIVGIKETQKTTVTGV 261
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
18-181 |
9.97e-15 |
|
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]
Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 72.02 E-value: 9.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 18 IIAHIDHGKSTLADRILEKTETVSSREMQAQLLDSMDLERERGITIKLNaielnytakdgetyifhLIDTPGHVDF---- 93
Cdd:TIGR00231 6 IVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNYVTTVIEEDGKTYKFN-----------------LLDTAGQEDYdair 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 94 ---TYEVSRSLAACEGAILVVDAAQGIEAQT--LANVylaLDNDLEILPVINKIDLPAAD-PERVRHEVEDVIGLDASEa 167
Cdd:TIGR00231 69 rlyYPQVERSLRVFDIVILVLDVEEILEKQTkeIIHH---ADSGVPIILVGNKIDLKDADlKTHVASEFAKLNGEPIIP- 144
|
170
....*....|....
gi 489080006 168 vlASAKAGIGIEEI 181
Cdd:TIGR00231 145 --LSAETGKNIDSA 156
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
15-148 |
1.04e-14 |
|
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 206670 [Multi-domain] Cd Length: 219 Bit Score: 73.68 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 15 NFSIIAHIDHGKSTLADRILEKTETVSSREMQ----------------AQLLDSMDLERERGITIKLNaielnyTAK-DG 77
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEkyekeakemgkesfkyAWVLDKLKEERERGVTIDVG------LAKfET 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 78 ETYIFHLIDTPGHVDFTYE--VSRSLAACegAILVVDAAQG-------IEAQTLANVYLAldNDL---EILPVINKIDLP 145
Cdd:cd01883 75 EKYRFTIIDAPGHRDFVKNmiTGASQADV--AVLVVSARKGefeagfeKGGQTREHALLA--RTLgvkQLIVAVNKMDDV 150
|
...
gi 489080006 146 AAD 148
Cdd:cd01883 151 TVN 153
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
19-248 |
2.78e-14 |
|
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: 74.80 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 19 IAHIDHGKSTLADRILekteTVSSREMQAQLL--DSMDL---ERERGITIKLNAIElnYtakdgETYIFHL--IDTPGHV 91
Cdd:COG0050 18 IGHVDHGKTTLTAAIT----KVLAKKGGAKAKayDQIDKapeEKERGITINTSHVE--Y-----ETEKRHYahVDCPGHA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 92 DFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPV-INKIDLpAADPER---VRHEVED--------- 158
Cdd:COG0050 87 DYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKCDM-VDDEELlelVEMEVREllskygfpg 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 159 ----VIGLDASEAVLA--SAKAGIGIEEILEQIVEKVPAPTGDVDAPLQALIFDSVYDAYRGVILQVRIVNGIVKPGDKI 232
Cdd:COG0050 166 ddtpIIRGSALKALEGdpDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEV 245
|
250
....*....|....*.
gi 489080006 233 QMMSNGKTFDVTEVGI 248
Cdd:COG0050 246 EIVGIRDTQKTVVTGV 261
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
15-293 |
3.63e-14 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 74.78 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 15 NFSIIAHIDHGKSTLA-----------DRILEKTETVSSrEM------QAQLLDSMDLERERGITIKLNAIELNyTAKdg 77
Cdd:PTZ00141 9 NLVVIGHVDSGKSTTTghliykcggidKRTIEKFEKEAA-EMgkgsfkYAWVLDKLKAERERGITIDIALWKFE-TPK-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 78 etYIFHLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGI-------EAQTLANVYLALDNDL-EILPVINKIDLPAADP 149
Cdd:PTZ00141 85 --YYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEfeagiskDGQTREHALLAFTLGVkQMIVCINKMDDKTVNY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 150 ERVRHE--VEDV------IGLDAsEAVLASAKAGIGIEEILEQI--------------VEKVPAPTGDVDAPLQaLIFDS 207
Cdd:PTZ00141 163 SQERYDeiKKEVsaylkkVGYNP-EKVPFIPISGWQGDNMIEKSdnmpwykgptlleaLDTLEPPKRPVDKPLR-LPLQD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 208 VYDAyrGVILQV---RIVNGIVKPGDKIQMMSNGKTFDVTEVGIF---TPKAVGRDflatgDVGYvaaSIKTVA--DTRV 279
Cdd:PTZ00141 241 VYKI--GGIGTVpvgRVETGILKPGMVVTFAPSGVTTEVKSVEMHheqLAEAVPGD-----NVGF---NVKNVSvkDIKR 310
|
330
....*....|....*
gi 489080006 280 GDTVTLA-NNPAKEA 293
Cdd:PTZ00141 311 GYVASDSkNDPAKEC 325
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
15-233 |
1.75e-13 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 72.53 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 15 NFSIIAHIDHGKSTLADRILekteTVSSREMQAQLL--DSMDL---ERERGITIKLNAIElnYtakdgETYIFHL--IDT 87
Cdd:PRK00049 14 NVGTIGHVDHGKTTLTAAIT----KVLAKKGGAEAKayDQIDKapeEKARGITINTAHVE--Y-----ETEKRHYahVDC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 88 PGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPV-INKIDLpAADPE---RVRHEVED----- 158
Cdd:PRK00049 83 PGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVfLNKCDM-VDDEElleLVEMEVREllsky 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 159 --------VI---GLDASEAVlASAKAGIGIEEILEQIVEKVPAPTGDVDAPLQALIFDSVYDAYRGVILQVRIVNGIVK 227
Cdd:PRK00049 162 dfpgddtpIIrgsALKALEGD-DDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIK 240
|
....*.
gi 489080006 228 PGDKIQ 233
Cdd:PRK00049 241 VGEEVE 246
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
25-187 |
8.39e-13 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 66.93 E-value: 8.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 25 GKSTLADRILEktETVSSREMQAqlldsmdlerERGITIKLNAIELNYTAKDgetyiFHLIDTPGHVDftYEVSRSLAAC 104
Cdd:COG1100 15 GKTSLVNRLVG--DIFSLEKYLS----------TNGVTIDKKELKLDGLDVD-----LVIWDTPGQDE--FRETRQFYAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 105 E-----GAILVVDAAQgieAQTLANVYLALDN------DLEILPVINKIDLPAADPERVRHEVEDVIGLDASEAVLA-SA 172
Cdd:COG1100 76 QltgasLYLFVVDGTR---EETLQSLYELLESlrrlgkKSPIILVLNKIDLYDEEEIEDEERLKEALSEDNIVEVVAtSA 152
|
170
....*....|....*
gi 489080006 173 KAGIGIEEILEQIVE 187
Cdd:COG1100 153 KTGEGVEELFAALAE 167
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
21-232 |
8.52e-13 |
|
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: 70.81 E-value: 8.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 21 HIDHGKSTLADRILeKTEtVSSREmqaqlldsmdlerERGITIKLNAielnYTAK-DGETYIFhlIDTPGHVDFTYEVSR 99
Cdd:COG0532 12 HVDHGKTSLLDAIR-KTN-VAAGE-------------AGGITQHIGA----YQVEtNGGKITF--LDTPGHEAFTAMRAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 100 slaaceGA------ILVVDAAQGIEAQTL--------ANVylaldndlEILPVINKIDLPAADPERVRHE-------VE- 157
Cdd:COG0532 71 ------GAqvtdivILVVAADDGVMPQTIeainhakaAGV--------PIIVAINKIDKPGANPDRVKQElaehglvPEe 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 158 ---DVIgldaseAVLASAKAGIGIEEILEQI-----VEKVPAptgDVDAPLQALIFDSVYDAYRGVILQVRIVNGIVKPG 229
Cdd:COG0532 137 wggDTI------FVPVSAKTGEGIDELLEMIllqaeVLELKA---NPDRPARGTVIEAKLDKGRGPVATVLVQNGTLKVG 207
|
...
gi 489080006 230 DKI 232
Cdd:COG0532 208 DIV 210
|
|
| EFG_mtEFG_C |
cd03713 |
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational ... |
410-486 |
3.16e-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: 59.46 E-value: 3.16e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489080006 410 EPYVKAQIMVPQEFVGAVM-ELSQRkRGDFVTMDyIDDNRVNVIYQIPLAEIvFDFFDKLKSSTRGYASFDYDMSEYR 486
Cdd:cd03713 1 EPIMKVEVTVPEEYMGDVIgDLSSR-RGQILGTE-SRGGWKVIKAEVPLAEM-FGYSTDLRSLTQGRGSFTMEFSHYE 75
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
15-144 |
1.13e-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: 61.23 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 15 NFSIIAHIDHGKSTLADRILEKTETVSsremqaqlLDSMDLERERGITIKL---------NAIELNYTAKDGETYIFHLI 85
Cdd:cd01889 2 NVGLLGHVDSGKTSLAKALSEIASTAA--------FDKNPQSQERGITLDLgfssfevdkPKHLEDNENPQIENYQITLV 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 489080006 86 DTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPVINKIDL 144
Cdd:cd01889 74 DCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDL 132
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
84-189 |
1.16e-10 |
|
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: 60.34 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 84 LIDTPGHVD-------FTYEVSRSLAACEGAILVVDAAQGIEAQTlANVYLALDNDLEILPVINKIDLPAADPERVRHEV 156
Cdd:cd00880 50 LIDTPGLDEegglgreRVEEARQVADRADLVLLVVDSDLTPVEEE-AKLGLLRERGKPVLLVLNKIDLVPESEEEELLRE 128
|
90 100 110
....*....|....*....|....*....|...
gi 489080006 157 EDVIGLDASEAVLASAKAGIGIEEILEQIVEKV 189
Cdd:cd00880 129 RKLELLPDLPVIAVSALPGEGIDELRKKIAELL 161
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
19-150 |
1.76e-10 |
|
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: 60.68 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 19 IAHIDHGKSTLADRILekteTVSSREMQAQLLDSMDL-----ERERGITIklNAIELNYtakdgETYIFHL--IDTPGHV 91
Cdd:cd01884 8 IGHVDHGKTTLTAAIT----KVLAKKGGAKAKKYDEIdkapeEKARGITI--NTAHVEY-----ETANRHYahVDCPGHA 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 92 DFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPV-INKIDLpAADPE 150
Cdd:cd01884 77 DYIKNMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVfLNKADM-VDDEE 135
|
|
| EFG_C |
smart00838 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
410-487 |
6.07e-10 |
|
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: 55.97 E-value: 6.07e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489080006 410 EPYVKAQIMVPQEFVGAVMELSQRKRGDFVTMDYIDDNRVnVIYQIPLAEIvFDFFDKLKSSTRGYASFDYDMSEYRR 487
Cdd:smart00838 3 EPIMKVEVTVPEEYMGDVIGDLNSRRGKIEGMEQRGGAQV-IKAKVPLSEM-FGYATDLRSATQGRATWSMEFSHYEE 78
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
10-293 |
2.88e-09 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 59.72 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 10 QEKIR-NFSIIAHIDHGKSTLADRILEKTETVSSREMQ----------------AQLLDSMDLERERGITIKLNAIELNY 72
Cdd:PLN00043 3 KEKVHiNIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIErfekeaaemnkrsfkyAWVLDKLKAERERGITIDIALWKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 73 TakdgeTYIFHLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQG-------IEAQTLANVYLALDNDL-EILPVINKIDl 144
Cdd:PLN00043 83 T-----KYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGgfeagisKDGQTREHALLAFTLGVkQMICCCNKMD- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 145 pAADPERVRHEVEDVI-----------------------GLDASEAVLASAK----AGIGIEEILEQIVEkvpaPTGDVD 197
Cdd:PLN00043 157 -ATTPKYSKARYDEIVkevssylkkvgynpdkipfvpisGFEGDNMIERSTNldwyKGPTLLEALDQINE----PKRPSD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 198 APLQALIFDSVYDAYRGVILQVRIVNGIVKPGDKIQMMSNGKTFDVTEVGIFTPKAVgrDFLATGDVGYVAASIkTVADT 277
Cdd:PLN00043 232 KPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQ--EALPGDNVGFNVKNV-AVKDL 308
|
330
....*....|....*..
gi 489080006 278 RVGDTVTLA-NNPAKEA 293
Cdd:PLN00043 309 KRGYVASNSkDDPAKEA 325
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
25-187 |
4.45e-09 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 58.91 E-value: 4.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 25 GKSTLADRILEKtetvssremqaqlldsmdlER-----ERGITIklNAIELNYTaKDGETYIfhLIDTPG-----HVDFT 94
Cdd:PRK00093 185 GKSSLINALLGE-------------------ERvivsdIAGTTR--DSIDTPFE-RDGQKYT--LIDTAGirrkgKVTEG 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 95 ---YEVSRSLAACEGA---ILVVDAAQGIEAQ--TLANvyLALDNDLEILPVINKIDL-PAADPERVRHEVEDVIG-LDA 164
Cdd:PRK00093 241 vekYSVIRTLKAIERAdvvLLVIDATEGITEQdlRIAG--LALEAGRALVIVVNKWDLvDEKTMEEFKKELRRRLPfLDY 318
|
170 180
....*....|....*....|...
gi 489080006 165 SEAVLASAKAGIGIEEILEQIVE 187
Cdd:PRK00093 319 APIVFISALTGQGVDKLLEAIDE 341
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
80-189 |
5.01e-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: 55.58 E-value: 5.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 80 YIFHLIDTPGHVDFTYEV-----SRSLAACEGA---ILVVDAAQGIEAQTLANvyLALDNDLEILPVINKIDLPAADPER 151
Cdd:cd04164 51 IPVRLIDTAGLRETEDEIekigiERAREAIEEAdlvLLVVDASEGLDEEDLEI--LELPAKKPVIVVLNKSDLLSDAEGI 128
|
90 100 110
....*....|....*....|....*....|....*...
gi 489080006 152 VRHEVEDVIGLdaseavlaSAKAGIGIEEILEQIVEKV 189
Cdd:cd04164 129 SELNGKPIIAI--------SAKTGEGIDELKEALLELA 158
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
22-249 |
5.86e-09 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 58.77 E-value: 5.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 22 IDHGKSTLADRILEKTETV----------SSREMQAQ--------LLDSMDLERERGITIKlnaIELNYTAKDGETYIfh 83
Cdd:PRK05124 36 VDDGKSTLIGRLLHDTKQIyedqlaslhnDSKRHGTQgekldlalLVDGLQAEREQGITID---VAYRYFSTEKRKFI-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 84 LIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLAldNDLEILPV---INKIDLPAADPER---VRHEVE 157
Cdd:PRK05124 111 IADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIA--TLLGIKHLvvaVNKMDLVDYSEEVferIREDYL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 158 DVIG---------------LDASEAVLASAK----AGIGIEEILEQIVEKVPAPTGDVDAPLQ-----ALIFdsvydayR 213
Cdd:PRK05124 189 TFAEqlpgnldirfvplsaLEGDNVVSQSESmpwySGPTLLEVLETVDIQRVVDAQPFRFPVQyvnrpNLDF-------R 261
|
250 260 270
....*....|....*....|....*....|....*.
gi 489080006 214 GviLQVRIVNGIVKPGDKIQMMSNGKTFDVTEVGIF 249
Cdd:PRK05124 262 G--YAGTLASGVVKVGDRVKVLPSGKESNVARIVTF 295
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
25-187 |
6.32e-09 |
|
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: 55.52 E-value: 6.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 25 GKSTLADRIL-EKTETVSSremqaqlldsmdlerERGITIklNAIELNYTaKDGETYIFhlIDTPG---------HVDFt 94
Cdd:cd01895 14 GKSSLLNALLgEERVIVSD---------------IAGTTR--DSIDVPFE-YDGQKYTL--IDTAGirkkgkvteGIEK- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 95 YEVSRSLAACEGA---ILVVDAAQGIEAQ--TLANvyLALDNDLEILPVINKIDLPAADPER---VRHEVEDVIG-LDAS 165
Cdd:cd01895 73 YSVLRTLKAIERAdvvLLVLDASEGITEQdlRIAG--LILEEGKALIIVVNKWDLVEKDEKTmkeFEKELRRKLPfLDYA 150
|
170 180
....*....|....*....|..
gi 489080006 166 EAVLASAKAGIGIEEILEQIVE 187
Cdd:cd01895 151 PIVFISALTGQGVDKLFDAIKE 172
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
25-187 |
1.22e-08 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 57.34 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 25 GKSTLADRILEKtetvssremqaqlldsmdlerER-------GITIklNAIELNYTaKDGETYIfhLIDTPG-----HVD 92
Cdd:COG1160 187 GKSSLINALLGE---------------------ERvivsdiaGTTR--DSIDTPFE-RDGKKYT--LIDTAGirrkgKVD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 93 FT---YEVSRSLAA---CEGAILVVDAAQGIEAQ--TLANvyLALDNDLEILPVINKIDLPAADP---ERVRHEVEDVIG 161
Cdd:COG1160 241 EGiekYSVLRTLRAierADVVLLVIDATEGITEQdlKIAG--LALEAGKALVIVVNKWDLVEKDRktrEELEKEIRRRLP 318
|
170 180
....*....|....*....|....*..
gi 489080006 162 -LDASEAVLASAKAGIGIEEILEQIVE 187
Cdd:COG1160 319 fLDYAPIVFISALTGQGVDKLLEAVDE 345
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
15-240 |
1.76e-08 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 56.78 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 15 NFSIIAHIDHGKSTLAdRIL--EKTETvSSREMQaqlldsmdlereRGITIKLNAIELN------------YTAK----- 75
Cdd:PRK04000 11 NIGMVGHVDHGKTTLV-QALtgVWTDR-HSEELK------------RGITIRLGYADATirkcpdceepeaYTTEpkcpn 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 76 -DGETYIFH---LIDTPGHvdftyEV------SRSlAACEGAILVVDAAQGI-EAQTLANvYLALD----NDLEIlpVIN 140
Cdd:PRK04000 77 cGSETELLRrvsFVDAPGH-----ETlmatmlSGA-ALMDGAILVIAANEPCpQPQTKEH-LMALDiigiKNIVI--VQN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 141 KIDLpaADPERVR---HEVEDVI-GLDASEA--VLASAKAGIGIEEILEQIVEKVPAPTGDVDAPLQALI---FD----- 206
Cdd:PRK04000 148 KIDL--VSKERALenyEQIKEFVkGTVAENApiIPVSALHKVNIDALIEAIEEEIPTPERDLDKPPRMYVarsFDvnkpg 225
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 489080006 207 SVYDAYRGVILQVRIVNGIVKPGDKI------QMMSNGKT 240
Cdd:PRK04000 226 TPPEKLKGGVIGGSLIQGVLKVGDEIeirpgiKVEEGGKT 265
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
22-251 |
2.18e-08 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 57.25 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 22 IDHGKSTLADRILEKTETV----------SSREMQAQ--------LLDSMDLERERGITIKlnaIELNYTAKDGETYIfh 83
Cdd:PRK05506 33 VDDGKSTLIGRLLYDSKMIfedqlaalerDSKKVGTQgdeidlalLVDGLAAEREQGITID---VAYRYFATPKRKFI-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 84 LIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLA-LDNDLEILPVINKIDLPAADPERVRHEVEDV--- 159
Cdd:PRK05506 108 VADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIAsLLGIRHVVLAVNKMDLVDYDQEVFDEIVADYraf 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 160 ---IGLDASEAVLASAKAGIGIEE-----------ILEQIVEKVPAptgDVDAPLQALIFDSVYdayrgVI---LQVR-- 220
Cdd:PRK05506 188 aakLGLHDVTFIPISALKGDNVVTrsarmpwyegpSLLEHLETVEI---ASDRNLKDFRFPVQY-----VNrpnLDFRgf 259
|
250 260 270
....*....|....*....|....*....|....
gi 489080006 221 ---IVNGIVKPGDKIQMMSNGKTFDVTEvgIFTP 251
Cdd:PRK05506 260 agtVASGVVRPGDEVVVLPSGKTSRVKR--IVTP 291
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
214-284 |
2.31e-08 |
|
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.
Pssm-ID: 427163 [Multi-domain] Cd Length: 73 Bit Score: 51.11 E-value: 2.31e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489080006 214 GVILQVRIVNGIVKPGDKIQMMSN--GKTFDVTEV-GIFTPKAvGRDFLATGDVGYVAASIKTVADTRVGDTVT 284
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNgtGKKKIVTRVtSLLMFHA-PLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| MnmE_helical |
pfam12631 |
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ... |
80-200 |
2.54e-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: 55.95 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 80 YIFHLIDTPG------HVdftyE---VSRSLAACEGA---ILVVDAAQGIEAQTLAnVYLALDNDLEILPVINKIDLPAA 147
Cdd:pfam12631 142 IPLRLIDTAGiretddEV----EkigIERAREAIEEAdlvLLVLDASRPLDEEDLE-ILELLKDKKPIIVVLNKSDLLGE 216
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 489080006 148 DPERVRHEVEDVIGLdaseavlaSAKAGIGIEEILEQIVEKVPAPTGDVDAPL 200
Cdd:pfam12631 217 IDELEELKGKPVLAI--------SAKTGEGLDELEEAIKELFLAGEIASDGPI 261
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
18-181 |
4.37e-08 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 56.21 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 18 IIA---HIDHGKSTL--------ADRILEktetvssremqaqlldsmdlERERGITiklnaIELNYT---AKDGETYIFh 83
Cdd:PRK10512 2 IIAtagHVDHGKTTLlqaitgvnADRLPE--------------------EKKRGMT-----IDLGYAywpQPDGRVLGF- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 84 lIDTPGHVDFtyeVSRSLAACEG---AILVVDAAQGIEAQTLANV-YLALDNDLEILPVINKIDLpaADPER---VRHEV 156
Cdd:PRK10512 56 -IDVPGHEKF---LSNMLAGVGGidhALLVVACDDGVMAQTREHLaILQLTGNPMLTVALTKADR--VDEARiaeVRRQV 129
|
170 180
....*....|....*....|....*...
gi 489080006 157 EDVI---GLDASEAVLASAKAGIGIEEI 181
Cdd:PRK10512 130 KAVLreyGFAEAKLFVTAATEGRGIDAL 157
|
|
| EFG_III |
cd16262 |
Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial ... |
302-377 |
5.40e-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: 50.15 E-value: 5.40e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489080006 302 PMVFAGIYPIESNKYNDLREALEKLQLNDASLQFE--PETSQALGFGfrcgfLGLLHMDVIQERLEREFNIDLIMTAP 377
Cdd:cd16262 3 PVISLAIEPKTKADEDKLSKALARLAEEDPTLRVSrdEETGQTILSG-----MGELHLEIIVERLKREYGVEVEVGKP 75
|
|
| BipA_TypA_C |
cd03710 |
BipA_TypA_C: a C-terminal portion of BipA or TypA having homology to the C terminal domains of ... |
410-486 |
7.56e-08 |
|
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: 49.81 E-value: 7.56e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489080006 410 EPYVKAQIMVPQEFVGAVME-LSQRKrGDFVTMDYIDDNRVNVIYQIPlAEIVFDFFDKLKSSTRGYASFDYDMSEYR 486
Cdd:cd03710 1 EPIEELTIDVPEEYSGAVIEkLGKRK-GEMVDMEPDGNGRTRLEFKIP-SRGLIGFRSEFLTDTRGTGIMNHVFDGYE 76
|
|
| EFG_III |
pfam14492 |
Elongation Factor G, domain III; This domain is found in Elongation Factor G. It shares a ... |
302-374 |
1.02e-07 |
|
Elongation Factor G, domain III; This domain is found in Elongation Factor G. It shares a similar structure with domain V (pfam00679). Structural studies in drosophila indicate this is domain 3.
Pssm-ID: 464188 [Multi-domain] Cd Length: 75 Bit Score: 49.40 E-value: 1.02e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489080006 302 PMVFAGIYPIESNKYNDLREALEKLQLNDASLQFE--PETSQALGFGfrcgfLGLLHMDVIQERLEREFNIDLIM 374
Cdd:pfam14492 4 PVISVAIEPKTKGDEDKLSKALNRLLEEDPTLRVErdEETGETILSG-----MGELHLEIVVDRLKRKYGVEVEL 73
|
|
| MnmE |
COG0486 |
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
82-200 |
1.05e-07 |
|
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: 54.68 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 82 FHLIDTPG------HVdftyE---VSRSLAACEGA---ILVVDAAQGIEAQTLAnvYLALDNDLEILPVINKIDLPAADP 149
Cdd:COG0486 263 VRLIDTAGlretedEV----EkigIERAREAIEEAdlvLLLLDASEPLTEEDEE--ILEKLKDKPVIVVLNKIDLPSEAD 336
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 489080006 150 ERVRHevedvigLDASEAVLASAKAGIGIEEILEQIVEKVPAPTGDVDAPL 200
Cdd:COG0486 337 GELKS-------LPGEPVIAISAKTGEGIDELKEAILELVGEGALEGEGVL 380
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
200-284 |
1.92e-07 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 48.80 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 200 LQALIFDSVYDAYRGVILQVRIVNGIVKPGDKIQMMSNGKTFDVTEVGIFTPKAvgrDFLATGDVgyVAASIKTVADTRV 279
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEV---DEAKAGDI--VGIGILGVKDILT 75
|
....*
gi 489080006 280 GDTVT 284
Cdd:cd01342 76 GDTLT 80
|
|
| trmE |
PRK05291 |
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; |
80-189 |
2.39e-07 |
|
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
Pssm-ID: 235392 [Multi-domain] Cd Length: 449 Bit Score: 53.58 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 80 YIFHLIDTPG------HVdftyE---VSRSLAACEGA---ILVVDAAQGIEAQTLANvyLALDNDLEILPVINKIDLPAA 147
Cdd:PRK05291 263 IPLRLIDTAGiretddEV----EkigIERSREAIEEAdlvLLVLDASEPLTEEDDEI--LEELKDKPVIVVLNKADLTGE 336
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 489080006 148 DpervrheveDVIGLDASEAVLASAKAGIGIEEILEQIVEKV 189
Cdd:PRK05291 337 I---------DLEEENGKPVIRISAKTGEGIDELREAIKELA 369
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
17-276 |
5.66e-07 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 52.49 E-value: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 17 SIIAHIDHGKSTLADRIleKTETVSSREmqaqlldsmdlerERGIT-------IKLNAIE------LNYTAKDGETYIFH 83
Cdd:PRK04004 10 VVLGHVDHGKTTLLDKI--RGTAVAAKE-------------AGGITqhigateVPIDVIEkiagplKKPLPIKLKIPGLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 84 LIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANvylaldndLEIL-----PVI---NKID-LP--------- 145
Cdd:PRK04004 75 FIDTPGHEAFTNLRKRGGALADIAILVVDINEGFQPQTIEA--------INILkrrktPFVvaaNKIDrIPgwkstedap 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 146 -----AADPERVRHEVE----DVIGlDASEA-------------------VLASAKAGIGIEEIL------------EQI 185
Cdd:PRK04004 147 flesiEKQSQRVQQELEeklyELIG-QLSELgfsadrfdrvkdftktvaiVPVSAKTGEGIPDLLmvlaglaqryleERL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 186 VEKVPAPTgdvdaplqalifdsvydayRGVILQVR------------IVNGIVKPGDKIQMMSNGKTFdVTEV-GIFTPK 252
Cdd:PRK04004 226 KIDVEGPG-------------------KGTVLEVKeerglgttidviLYDGTLRKGDTIVVGGKDGPI-VTKVrALLKPR 285
|
330 340 350
....*....|....*....|....*....|
gi 489080006 253 A------VGRDFLATGDVgYVAASIKTVAD 276
Cdd:PRK04004 286 PldemrdPEDKFKPVDEV-VAAAGVKISAP 314
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
15-192 |
1.30e-06 |
|
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.
Pssm-ID: 206675 [Multi-domain] Cd Length: 197 Bit Score: 49.19 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 15 NFSIIAHIDHGKSTLAdRILEKTETVSSREmqaqlldsmdlERERGITIKL---NA--------------IELNYTAKDG 77
Cdd:cd01888 2 NIGTIGHVAHGKTTLV-KALSGVWTVRHKE-----------ELKRNITIKLgyaNAkiykcpncgcprpyDTPECECPGC 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 78 ---ETYIFH--LIDTPGHvdftyEVsrsLAAC--------EGAILVVDAAQGI-EAQTLANVyLALDN-DLE-ILPVINK 141
Cdd:cd01888 70 ggeTKLVRHvsFVDCPGH-----EI---LMATmlsgaavmDGALLLIAANEPCpQPQTSEHL-AALEImGLKhIIILQNK 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489080006 142 IDLPAADPERVRHE-----VEDVIGLDASeAVLASAKAGIGIEEILEQIVEKVPAP 192
Cdd:cd01888 141 IDLVKEEQALENYEqikefVKGTIAENAP-IIPISAQLKYNIDVLCEYIVKKIPTP 195
|
|
| mtEFG1_C |
cd04097 |
mtEFG1_C: C-terminus of mitochondrial Elongation factor G1 (mtEFG1)-like proteins found in ... |
410-485 |
4.23e-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: 45.00 E-value: 4.23e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489080006 410 EPYVKAQIMVPQEFVGAVMELSQRKRGDFVTMDYIDDNrVNVIYQIPLAEIvFDFFDKLKSSTRGYASFDYDMSEY 485
Cdd:cd04097 1 EPIMKVEVTAPTEFQGNVIGLLNKRKGTIVDTDTGEDE-FTLEAEVPLNDM-FGYSTELRSMTQGKGEFSMEFSRY 74
|
|
| Tet_C |
cd03711 |
Tet_C: C-terminus of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology ... |
410-487 |
7.16e-06 |
|
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: 44.15 E-value: 7.16e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489080006 410 EPYVKAQIMVPQEFVGAVMELSQRKRGDFVTMdYIDDNRVNVIYQIPLAEiVFDFFDKLKSSTRGYASFDYDMSEYRR 487
Cdd:cd03711 1 EPYLRFELEVPQDALGRAMSDLAKMGATFEDP-QIKGDEVTLEGTIPVAT-SQDYQSELPSYTHGEGVLETEFKGYRP 76
|
|
| HflX |
cd01878 |
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
108-189 |
9.20e-06 |
|
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment N-terminal of the GTPase domain characterizes the HflX subfamily. The E. coli HflX has been implicated in the control of the lambda cII repressor proteolysis, but the actual biological functions of these GTPases remain unclear. HflX is widespread, but not universally represented in all three superkingdoms.
Pssm-ID: 206666 [Multi-domain] Cd Length: 204 Bit Score: 46.68 E-value: 9.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 108 ILVVDAAQGIEAQTLANVYLALD----NDLEILPVINKIDLpaADPERVRHEVEDVIGldasEAVLASAKAGIGIEEILE 183
Cdd:cd01878 125 LHVVDASDPDREEQIETVEEVLKelgaDDIPIILVLNKIDL--LDDEELEERLRAGRP----DAVFISAKTGEGLDLLKE 198
|
....*.
gi 489080006 184 QIVEKV 189
Cdd:cd01878 199 AIEELL 204
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
84-190 |
8.60e-05 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 44.65 E-value: 8.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 84 LIDTPG-H----------VDFtyeVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPVINKIDLpAADPERV 152
Cdd:PRK00089 57 FVDTPGiHkpkralnramNKA---AWSSLKDVDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDL-VKDKEEL 132
|
90 100 110
....*....|....*....|....*....|....*....
gi 489080006 153 RHEVEDVIGLDASEAVLA-SAKAGIGIEEILEQIVEKVP 190
Cdd:PRK00089 133 LPLLEELSELMDFAEIVPiSALKGDNVDELLDVIAKYLP 171
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
25-141 |
1.85e-04 |
|
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: 41.07 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 25 GKSTLADRILEKTETVSSREmqaqlldsmdlererGITIKLNAIELNYTAKDgetyiFHLIDTPGHVD---FTYEVSRSL 101
Cdd:pfam01926 11 GKSTLINALTGAKAIVSDYP---------------GTTRDPNEGRLELKGKQ-----IILVDTPGLIEgasEGEGLGRAF 70
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 489080006 102 AA---CEGAILVVDAAQGIEAQTLANVYLALDNDLEILPVINK 141
Cdd:pfam01926 71 LAiieADLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
84-190 |
2.13e-04 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 43.44 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 84 LIDTPG-H----------VDFtyeVSRSLAACEGAILVVDAAQGIEaqtlanvylalDNDLEILP-----------VINK 141
Cdd:COG1159 55 FVDTPGiHkpkrklgrrmNKA---AWSALEDVDVILFVVDATEKIG-----------EGDEFILEllkklktpvilVINK 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 489080006 142 IDLpaADPERVRHEVEDVIGL-DASEAVLASAKAGIGIEEILEQIVEKVP 190
Cdd:COG1159 121 IDL--VKKEELLPLLAEYSELlDFAEIVPISALKGDNVDELLDEIAKLLP 168
|
|
| Srp102 |
COG2229 |
Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, ... |
77-189 |
3.54e-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: 41.73 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 77 GETYIFHLIDTPGHV--DFTYE--VSRSLaaceGAILVVDaAQGIEAQTLANVYLALDNDLEILPVI---NKIDLPAADP 149
Cdd:COG2229 67 GDGLRLHLFGTPGQVrfDFMWDilLRGAD----GVVFLAD-SRRLEDSFNAESLDFFEERLEKLPFVvavNKRDLPDALS 141
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 489080006 150 ERvrhEVEDVIGLDASEAVL-ASAKAGIGIEEILEQIVEKV 189
Cdd:COG2229 142 LE---ELREALDLGPDVPVVeADARDGESVKETLIALLELV 179
|
|
| YqeH |
cd01855 |
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ... |
131-196 |
5.66e-04 |
|
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: 41.48 E-value: 5.66e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489080006 131 NDLEILPVINKIDL--PAADPERVRHEVEDVI---GLDASEAVLASAKAGIGIEEILEQIvEKVPAPTGDV 196
Cdd:cd01855 59 GAKPVILVGNKIDLlpKDVKPNRLKQWVKKRLkigGLKIKDVILVSAKKGWGVEELIEEI-KKLAKYRGDV 128
|
|
| EFG_mtEFG_II |
cd04088 |
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation ... |
202-284 |
9.29e-04 |
|
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation factors G1 and G2; This family represents the domain II of bacterial Elongation factor G (EF-G)and mitochondrial Elongation factors G1 (mtEFG1) and G2 (mtEFG2). During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. In bacteria this translocation step is catalyzed by EF-G_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. mtEFG1 and mtEFG2 show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. No clear phenotype has been found for mutants in the yeast homolog of mtEFG2, MEF2.
Pssm-ID: 293905 [Multi-domain] Cd Length: 83 Bit Score: 38.27 E-value: 9.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 202 ALIFDSVYDAYRGVILQVRIVNGIVKPGDKIQMMSNGKTFDVTEvgIFTPKAVGR---DFLATGDVGYVAAsiktVADTR 278
Cdd:cd04088 3 ALVFKTMADPFVGKLTFFRVYSGTLKSGSTVYNSTKGKKERVGR--LLRMHGKKReevEELGAGDIGAVVG----LKDTR 76
|
....*.
gi 489080006 279 VGDTVT 284
Cdd:cd04088 77 TGDTLC 82
|
|
| mtEFG2_II_like |
cd04092 |
Domain II of mitochondrial elongation factor G2-like proteins found in eukaryotes; Eukaryotic ... |
202-283 |
1.42e-03 |
|
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: 38.07 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 202 ALIFDSVYDAYRGVILQVRIVNGIVKPGDKIQMMSNGKTFDVTE-VGIFTPKAVGRDFLATGDVGyVAASIKTvadTRVG 280
Cdd:cd04092 3 ALAFKVIHDPQRGPLVFVRVYSGTLKAGSNVYNTTTGKKERISRlLKMHADQTEEVDSLSAGNIG-VITGLKV---TSTG 78
|
...
gi 489080006 281 DTV 283
Cdd:cd04092 79 DTL 81
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
126-189 |
1.83e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 40.07 E-value: 1.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489080006 126 YLAL--DNDLEILPVINKIDLpaADPERVRHEVEDVIGLDAsEAVLASAKAGIGIEEILEQIVEKV 189
Cdd:cd01854 25 YLVAaeASGIEPVIVLNKADL--VDDEELEELLEIYEKLGY-PVLAVSAKTGEGLDELRELLKGKT 87
|
|
| Rab |
cd00154 |
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ... |
76-187 |
2.04e-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: 39.36 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 76 DGETYIFHLIDTPGHvdftyEVSRSLAA-----CEGAILVVDaaqGIEAQTLANVYL-------ALDNDLEILPVINKID 143
Cdd:cd00154 45 DGKKVKLQIWDTAGQ-----ERFRSITSsyyrgAHGAILVYD---VTNRESFENLDKwlnelkeYAPPNIPIILVGNKSD 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 489080006 144 LPAadpERV--RHEVEDVIGLDASEAVLASAKAGIGIEEILEQIVE 187
Cdd:cd00154 117 LED---ERQvsTEEAQQFAKENGLLFFETSAKTGENVDEAFESLAR 159
|
|
| eEF2_snRNP_like_C |
cd04096 |
eEF2_snRNP_like_C: this family represents a C-terminal domain of eukaryotic elongation factor ... |
410-480 |
2.66e-03 |
|
eEF2_snRNP_like_C: this family represents a C-terminal domain of eukaryotic elongation factor 2 (eEF-2) and a homologous domain of the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and, its yeast counterpart Snu114p. Yeast Snu114p is essential for cell viability and for splicing in vivo. U5-116 kD binds GTP. Experiments suggest that GTP binding and probably GTP hydrolysis is important for the function of the U5-116 kD/Snu114p. In complex with GTP, EF-2 promotes the translocation step of translation. During translocation the peptidyl-tRNA is moved from the A site to the P site, the uncharged tRNA from the P site to the E-site and, the mRNA is shifted one codon relative to the ribosome.
Pssm-ID: 239763 [Multi-domain] Cd Length: 80 Bit Score: 37.13 E-value: 2.66e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489080006 410 EPYVKAQIMVPQEFVGAVMELSQRKRGDFVTMDYIDDN-RVNVIYQIPLAEIvFDFFDKLKSSTRGYAS----FDY 480
Cdd:cd04096 1 EPIYLVEIQCPEDALGKVYSVLSKRRGHVLSEEPKEGTpLFEIKAYLPVIES-FGFETDLRSATSGQAFpqlvFSH 75
|
|
| PRK09518 |
PRK09518 |
bifunctional cytidylate kinase/GTPase Der; Reviewed |
76-204 |
4.04e-03 |
|
bifunctional cytidylate kinase/GTPase Der; Reviewed
Pssm-ID: 236546 [Multi-domain] Cd Length: 712 Bit Score: 40.16 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 76 DGETYIFhlIDTPG----------HVDFTYEVSRS-LAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPVINKIDL 144
Cdd:PRK09518 496 DGEDWLF--IDTAGikrrqhkltgAEYYSSLRTQAaIERSELALFLFDASQPISEQDLKVMSMAVDAGRALVLVFNKWDL 573
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 145 paADPERvRHEVEDVIGLDAS-----EAVLASAKAGIGIEEILEQIVEKVPA-----PTGDVDAPLQALI 204
Cdd:PRK09518 574 --MDEFR-RQRLERLWKTEFDrvtwaRRVNLSAKTGWHTNRLAPAMQEALESwdqriPTGKLNAFLGKIQ 640
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
25-188 |
6.28e-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: 37.83 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 25 GKSTLADRILEKTETVSSREMQA---QLldsmdlereRGItiklnaielnYTAKDGEtYIFhlIDTPG-HVDFT------ 94
Cdd:cd04163 15 GKSTLLNALVGQKISIVSPKPQTtrnRI---------RGI----------YTDDDAQ-IIF--VDTPGiHKPKKklgerm 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080006 95 -YEVSRSLAACEGAILVVDAAQGIEAQTlANVYLAL-DNDLEILPVINKIDLpAADPERVRHEVEDVIGLDASEAVLA-S 171
Cdd:cd04163 73 vKAAWSALKDVDLVLFVVDASEWIGEGD-EFILELLkKSKTPVILVLNKIDL-VKDKEDLLPLLEKLKELHPFAEIFPiS 150
|
170
....*....|....*..
gi 489080006 172 AKAGIGIEEILEQIVEK 188
Cdd:cd04163 151 ALKGENVDELLEYIVEY 167
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