|
Name |
Accession |
Description |
Interval |
E-value |
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
2-598 |
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: 1286.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 2 SDLSHIRNFSIIAHIDHGKSTLADRFIQMCGGLSDREMEAQVLDSMDLERERGITIKAHSVTLHYKAQDGKTYQLNFIDT 81
Cdd:COG0481 1 MDQKNIRNFSIIAHIDHGKSTLADRLLELTGTLSEREMKEQVLDSMDLERERGITIKAQAVRLNYKAKDGETYQLNLIDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 82 PGHVDFTYEVSRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGLEVMPVLNKMDLPQAEPERVKEEIESIIGIDATDA 161
Cdd:COG0481 81 PGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKQEIEDIIGIDASDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 162 VACSAKSGMGVLEVLERLVTAIPAPEGEIEAPLQALIIDSWFDNYLGVVSLVRVKNGRVKKGDKILVKSTGKVHQVDSVG 241
Cdd:COG0481 161 ILVSAKTGIGIEEILEAIVERIPPPKGDPDAPLQALIFDSWYDSYRGVVVYVRVFDGTLKKGDKIKMMSTGKEYEVDEVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 242 VFTPKHTETVDLKAGEVGFIIAGIKDIHGAPVGDTLTLNNTPDVEVLPGFKRVKPQVYAGLFPVSSDDFEDFRDALQKLT 321
Cdd:COG0481 241 VFTPKMTPVDELSAGEVGYIIAGIKDVRDARVGDTITLAKNPAAEPLPGFKEVKPMVFAGLYPVDSDDYEDLRDALEKLQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 322 LNDSSLQYEPESSEALGFGFRCGFLGMLHMEIIQERLEREYDLDLITTAPTVVFEIVQKNGEIIYVDNPSKLPDLASIQE 401
Cdd:COG0481 321 LNDASLTYEPETSAALGFGFRCGFLGLLHMEIIQERLEREFDLDLITTAPSVVYEVTLTDGEVIEVDNPSDLPDPGKIEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 402 MREPICRATILVPKDHLGNVITLCIEKRGVQRDMHFLS-GQVQVVYDLPMNEVVLDFFDRLKSTSRGYASLDYSFDRFEP 480
Cdd:COG0481 401 IEEPIVKATIITPSEYVGAVMELCQEKRGVQKNMEYLGeNRVELTYELPLAEIVFDFFDRLKSITRGYASLDYEFIGYRE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 481 SNLVRLDVLINGEKVDALALIVHRDNAPYKGRQLVEKMKELIPRQMFDVAIQAAIGGQIIARSTVKALRKNVLAKCYGGD 560
Cdd:COG0481 481 SDLVKLDILINGEPVDALSFIVHRDKAYSRGRALVEKLKELIPRQQFEVPIQAAIGGKIIARETIKALRKDVLAKCYGGD 560
|
570 580 590
....*....|....*....|....*....|....*...
gi 15595964 561 VSRKRKLLEKQKAGKKRMKQVGSVEIPQEAFLAVLKVD 598
Cdd:COG0481 561 ISRKRKLLEKQKEGKKRMKQVGNVEIPQEAFLAVLKVD 598
|
|
| lepA |
TIGR01393 |
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a ... |
5-598 |
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: 1079.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 5 SHIRNFSIIAHIDHGKSTLADRFIQMCGGLSDREMEAQVLDSMDLERERGITIKAHSVTLHYKAQDGKTYQLNFIDTPGH 84
Cdd:TIGR01393 1 KNIRNFSIIAHIDHGKSTLADRLLEYTGAISEREMREQVLDSMDLERERGITIKAQAVRLNYKAKDGETYVLNLIDTPGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 85 VDFTYEVSRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGLEVMPVLNKMDLPQAEPERVKEEIESIIGIDATDAVAC 164
Cdd:TIGR01393 81 VDFSYEVSRSLAACEGALLLVDAAQGIEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKKEIEEVIGLDASEAILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 165 SAKSGMGVLEVLERLVTAIPAPEGEIEAPLQALIIDSWFDNYLGVVSLVRVKNGRVKKGDKILVKSTGKVHQVDSVGVFT 244
Cdd:TIGR01393 161 SAKTGIGIEEILEAIVKRVPPPKGDPDAPLKALIFDSHYDNYRGVVALVRVFEGTIKPGDKIRFMSTGKEYEVDEVGVFT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 245 PKHTETVDLKAGEVGFIIAGIKDIHGAPVGDTLTLNNTPDVEVLPGFKRVKPQVYAGLFPVSSDDFEDFRDALQKLTLND 324
Cdd:TIGR01393 241 PKLTKTDELSAGEVGYIIAGIKDVSDVRVGDTITHVKNPAKEPLPGFKEVKPMVFAGLYPIDTEDYEDLRDALEKLKLND 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 325 SSLQYEPESSEALGFGFRCGFLGMLHMEIIQERLEREYDLDLITTAPTVVFEIVQKNGEIIYVDNPSKLPDLASIQEMRE 404
Cdd:TIGR01393 321 ASLTYEPESSPALGFGFRCGFLGLLHMEIIQERLEREFNLDLITTAPSVIYRVYLTNGEVIEVDNPSDLPDPGKIEHVEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 405 PICRATILVPKDHLGNVITLCIEKRGVQRDMHFLSG-QVQVVYDLPMNEVVLDFFDRLKSTSRGYASLDYSFDRFEPSNL 483
Cdd:TIGR01393 401 PYVKATIITPTEYLGPIMTLCQEKRGVQTNMEYLDPnRVELIYEMPLAEIVYDFFDKLKSISRGYASFDYELIGYRPSDL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 484 VRLDVLINGEKVDALALIVHRDNAPYKGRQLVEKMKELIPRQMFDVAIQAAIGGQIIARSTVKALRKNVLAKCYGGDVSR 563
Cdd:TIGR01393 481 VKLDILINGEPVDALSFIVHRDKAYSRGREICEKLKELIPRQQFEIPIQAAIGGKIIARETIKALRKDVTAKCYGGDITR 560
|
570 580 590
....*....|....*....|....*....|....*
gi 15595964 564 KRKLLEKQKAGKKRMKQVGSVEIPQEAFLAVLKVD 598
Cdd:TIGR01393 561 KRKLLEKQKEGKKRMKQIGKVEVPQEAFLAVLKVD 595
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
8-186 |
1.34e-122 |
|
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: 359.15 E-value: 1.34e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 8 RNFSIIAHIDHGKSTLADRFIQMCGGLSDREMEAQVLDSMDLERERGITIKAHSVTLHYKAQDGKTYQLNFIDTPGHVDF 87
Cdd:cd01890 1 RNFSIIAHIDHGKSTLADRLLELTGTVSEREMKEQVLDSMDLERERGITIKAQAVRLFYKAKDGEEYLLNLIDTPGHVDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 88 TYEVSRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGLEVMPVLNKMDLPQAEPERVKEEIESIIGIDATDAVACSAK 167
Cdd:cd01890 81 SYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVKQEIEDVLGLDASEAILVSAK 160
|
170
....*....|....*....
gi 15595964 168 SGMGVLEVLERLVTAIPAP 186
Cdd:cd01890 161 TGLGVEDLLEAIVERIPPP 179
|
|
| LepA_C |
pfam06421 |
GTP-binding protein LepA C-terminus; This family consists of the C-terminal region of several ... |
490-596 |
5.70e-75 |
|
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: 233.84 E-value: 5.70e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 490 INGEKVDALALIVHRDNAPYKGRQLVEKMKELIPRQMFDVAIQAAIGGQIIARSTVKALRKNVLAKCYGGDVSRKRKLLE 569
Cdd:pfam06421 1 INGEPVDALSFIVHRSKAYRRGRALVEKLKELIPRQQFEVPIQAAIGGKIIARETIKALRKDVTAKCYGGDISRKKKLLE 80
|
90 100
....*....|....*....|....*..
gi 15595964 570 KQKAGKKRMKQVGSVEIPQEAFLAVLK 596
Cdd:pfam06421 81 KQKEGKKRMKQIGNVEIPQEAFLAVLK 107
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
5-480 |
1.24e-66 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 227.98 E-value: 1.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 5 SHIRNFSIIAHIDHGKSTLADRFIQMCGGLSDRE-MEAQVLDSMDLERERGITIKAHSVTLHYKaqdgkTYQLNFIDTPG 83
Cdd:COG1217 4 EDIRNIAIIAHVDHGKTTLVDALLKQSGTFRENQeVAERVMDSNDLERERGITILAKNTAVRYK-----GVKINIVDTPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 84 HVDFTYEVSRSLAACEGALLVVDAGQGVEAQsvancyT------AIEQGLEVMPVLNKMDLPQAEPERVKEEI-ESIIGI 156
Cdd:COG1217 79 HADFGGEVERVLSMVDGVLLLVDAFEGPMPQ------TrfvlkkALELGLKPIVVINKIDRPDARPDEVVDEVfDLFIEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 157 DATDA------VACSAKSGMGVLE----------VLERLVTAIPAPEGEIEAPLQALI--IDswFDNYLGVVSLVRVKNG 218
Cdd:COG1217 153 GATDEqldfpvVYASARNGWASLDlddpgedltpLFDTILEHVPAPEVDPDGPLQMLVtnLD--YSDYVGRIAIGRIFRG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 219 RVKKGDKI-LVKSTGKVHQVDSVGVFTPKHTETVDLKAGEVGFI--IAGIKDIHgapVGDTLTLNNTPdvEVLPGFKRVK 295
Cdd:COG1217 231 TIKKGQQVaLIKRDGKVEKGKITKLFGFEGLERVEVEEAEAGDIvaIAGIEDIN---IGDTICDPENP--EALPPIKIDE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 296 PQVyAGLFPVSSDDF---E-DF------RDALQKLTLNDSSLQYEP-ESSEAlgfgfrcgFL----GMLHMEIIQERLER 360
Cdd:COG1217 306 PTL-SMTFSVNDSPFagrEgKFvtsrqiRERLEKELETNVALRVEEtDSPDA--------FKvsgrGELHLSILIETMRR 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 361 E-YDLDLitTAPTVVF-EIvqkNGEiiyvdnpsKLpdlasiqemrEPICRATILVPKDHLGNVITLCIEKRGVQRDMHFL 438
Cdd:COG1217 377 EgYELQV--SRPEVIFkEI---DGK--------KL----------EPIEELTIDVPEEYSGAVIEKLGQRKGEMTNMEPD 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15595964 439 -SGQVQVVYDLP-------MNEVVLDffdrlkstSRGYASLDYSFDRFEP 480
Cdd:COG1217 434 gGGRVRLEFLIPsrgligfRTEFLTD--------TRGTGIMNHVFDGYEP 475
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
7-185 |
1.01e-65 |
|
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: 212.77 E-value: 1.01e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 7 IRNFSIIAHIDHGKSTLADRFIQMCGGLSDREMEAQ----VLDSMDLERERGITIKAHSVTLHYKaqdgkTYQLNFIDTP 82
Cdd:pfam00009 3 HRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGegeaGLDNLPEERERGITIKSAAVSFETK-----DYLINLIDTP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 83 GHVDFTYEVSRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGLEVMPVLNKMDLP-QAEPERVKEEIESIIGIDA--- 158
Cdd:pfam00009 78 GHVDFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVdGAELEEVVEEVSRELLEKYged 157
|
170 180 190
....*....|....*....|....*....|
gi 15595964 159 ---TDAVACSAKSGMGVLEVLERLVTAIPA 185
Cdd:pfam00009 158 gefVPVVPGSALKGEGVQTLLDALDEYLPS 187
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
3-373 |
3.69e-51 |
|
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: 187.18 E-value: 3.69e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 3 DLSHIRNFSIIAHIDHGKSTLADRfIQMCGGLSDR--EME--AQVLDSMDLERERGITIKAHSVTLHYKaqdgkTYQLNF 78
Cdd:COG0480 5 PLEKIRNIGIVAHIDAGKTTLTER-ILFYTGAIHRigEVHdgNTVMDWMPEEQERGITITSAATTCEWK-----GHKINI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 79 IDTPGHVDFTYEVSRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGLEVMPVLNKMDLPQAEPERVKEEIESI----- 153
Cdd:COG0480 79 IDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQLKERlganp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 154 ------IGIDAT--------------------------------------------DAVA-------------------- 163
Cdd:COG0480 159 vplqlpIGAEDDfkgvidlvtmkayvyddelgakyeeeeipaelkeeaeeareeliEAVAetddelmekylegeelteee 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 164 -------------------CSAKSGMGVLEVLERLVTAIPAP------------EGEI-------EAPLQALIIDSWFDN 205
Cdd:COG0480 239 ikaglrkatlagkivpvlcGSAFKNKGVQPLLDAVVDYLPSPldvpaikgvdpdTGEEverkpddDEPFSALVFKTMTDP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 206 YLGVVSLVRVKNGRVKKGDKILVKSTGKVHQVdsVGVFTP--KHTETVD-LKAGEVGfIIAGIKDIHgapVGDTLTLNNT 282
Cdd:COG0480 319 FVGKLSFFRVYSGTLKSGSTVYNSTKGKKERI--GRLLRMhgNKREEVDeAGAGDIV-AVVKLKDTT---TGDTLCDEDH 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 283 PDveVLPGFKRVKPQVYAGLFPVSSDDFEDFRDALQKLTLNDSSLQYE--PESSEALGFGfrcgfLGMLHMEIIQERLER 360
Cdd:COG0480 393 PI--VLEPIEFPEPVISVAIEPKTKADEDKLSTALAKLAEEDPTFRVEtdEETGQTIISG-----MGELHLEIIVDRLKR 465
|
490
....*....|...
gi 15595964 361 EYDLDLITTAPTV 373
Cdd:COG0480 466 EFGVEVNVGKPQV 478
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
4-479 |
4.57e-50 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 182.99 E-value: 4.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 4 LSHIRNFSIIAHIDHGKSTLADRFIQMCGGLSDR-EMEAQVLDSMDLERERGITIKAHSVTLHYKaqdgkTYQLNFIDTP 82
Cdd:PRK10218 2 IEKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRaETQERVMDSNDLEKERGITILAKNTAIKWN-----DYRINIVDTP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 83 GHVDFTYEVSRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGLEVMPVLNKMDLPQAEPERVKEEI-ESIIGIDATDA 161
Cdd:PRK10218 77 GHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVfDLFVNLDATDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 162 ------VACSAKSGMGVLE----------VLERLVTAIPAPEGEIEAPLQALIIDSWFDNYLGVVSLVRVKNGRVKKGDK 225
Cdd:PRK10218 157 qldfpiVYASALNGIAGLDhedmaedmtpLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 226 I-LVKSTGKVHQVDSVGVFTPKHTETVDLKAGEVGFIIAgIKDIHGAPVGDTLTlnNTPDVEVLPGFKRVKPQVyAGLFP 304
Cdd:PRK10218 237 VtIIDSEGKTRNAKVGKVLGHLGLERIETDLAEAGDIVA-ITGLGELNISDTVC--DTQNVEALPALSVDEPTV-SMFFC 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 305 VSSDDF----------EDFRDALQKLTLNDSSLQY-EPESSEAlgfgFRCGFLGMLHMEIIQERLEREyDLDLITTAPTV 373
Cdd:PRK10218 313 VNTSPFcgkegkfvtsRQILDRLNKELVHNVALRVeETEDADA----FRVSGRGELHLSVLIENMRRE-GFELAVSRPKV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 374 VFEIVQKNGEiiyvdnpsklpdlasiqemrEPICRATILVPKDHLGNVITLCIEKRGVQRDMH-FLSGQVQVVYDLPmNE 452
Cdd:PRK10218 388 IFREIDGRKQ--------------------EPYENVTLDVEEQHQGSVMQALGERKGDLKNMNpDGKGRVRLDYVIP-SR 446
|
490 500
....*....|....*....|....*..
gi 15595964 453 VVLDFFDRLKSTSRGYASLDYSFDRFE 479
Cdd:PRK10218 447 GLIGFRSEFMTMTSGTGLLYSTFSHYD 473
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
3-480 |
9.21e-49 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 180.53 E-value: 9.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 3 DLSHIRNFSIIAHIDHGKSTLADRFIQMCGGLSDR-EME--AQVLDSMDLERERGITIKAHSVTLHYKaqdgkTYQLNFI 79
Cdd:PRK13351 4 PLMQIRNIGILAHIDAGKTTLTERILFYTGKIHKMgEVEdgTTVTDWMPQEQERGITIESAATSCDWD-----NHRINLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 80 DTPGHVDFTYEVSRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGLEVMPVLNKMDLPQAEPERVKEEIESIIGIDA- 158
Cdd:PRK13351 79 DTPGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLFKVLEDIEERFGKRPl 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 159 -------------------------------------------------------TDAVA-------------------- 163
Cdd:PRK13351 159 plqlpigsedgfegvvdlitepelhfsegdggstveegpipeelleeveeareklIEALAefddellelylegeelsaeq 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 164 -----------------C--SAKSGMGVLEVLERLVTAIPAP-EGEI-----------------EAPLQALIIDSWFDNY 206
Cdd:PRK13351 239 lraplregtrsghlvpvLfgSALKNIGIEPLLDAVVDYLPSPlEVPPprgskdngkpvkvdpdpEKPLLALVFKVQYDPY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 207 LGVVSLVRVKNGRVKKGDKILVKSTGKVHQVDS-VGVFTPKHTETVDLKAGEVGfIIAGIKDIHgapVGDTLTLNNTPDV 285
Cdd:PRK13351 319 AGKLTYLRVYSGTLRAGSQLYNGTGGKREKVGRlFRLQGNKREEVDRAKAGDIV-AVAGLKELE---TGDTLHDSADPVL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 286 EVLPGFkrVKPQVYAGLFPVSSDDFEDFRDALQKLTLNDSSLQYE--PESSEALGFGfrcgfLGMLHMEIIQERLEREYD 363
Cdd:PRK13351 395 LELLTF--PEPVVSLAVEPERRGDEQKLAEALEKLVWEDPSLRVEedEETGQTILSG-----MGELHLEVALERLRREFK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 364 LDLITTAPTVV-FEIVQK-----------------NGEIIYVDNPS---------------KLP---------------- 394
Cdd:PRK13351 468 LEVNTGKPQVAyRETIRKmaegvyrhkkqfggkgqFGEVHLRVEPLergagfifvskvvggAIPeelipavekgireala 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 395 ----------DL---------------------ASIQEMR-----------EPICRATILVPKDHLGNVITLCIEKRGVQ 432
Cdd:PRK13351 548 sgplagypvtDLrvtvldgkyhpvdssesafkaAARKAFLeafrkanpvllEPIMELEITVPTEHVGDVLGDLSQRRGRI 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 15595964 433 RDMHFLSGQ-VQVVYDLPMNEvVLDFFDRLKSTSRGYASLDYSFDRFEP 480
Cdd:PRK13351 628 EGTEPRGDGeVLVKAEAPLAE-LFGYATRLRSMTKGRGSFTMEFSHFDP 675
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
1-392 |
1.38e-47 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 177.75 E-value: 1.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 1 MSDLSHIRNFSIIAHIDHGKSTLADRFIQMCGGLSDR-EMEAQVLDSMDLERERGITIKAHSVTLhYKAQDGKTYQLNFI 79
Cdd:PRK07560 14 MKNPEQIRNIGIIAHIDHGKTTLSDNLLAGAGMISEElAGEQLALDFDEEEQARGITIKAANVSM-VHEYEGKEYLINLI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 80 DTPGHVDFTYEVSRSLAACEGALLVVDAGQGVEAQSvancYTAIEQGLE--VMPVL--NKMD-----LpQAEPERVKEEI 150
Cdd:PRK07560 93 DTPGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQT----ETVLRQALRerVKPVLfiNKVDrlikeL-KLTPQEMQQRL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 151 ESIIG-------------------IDATDA-VAC-SA------------KSGMG---VLE-------------------V 175
Cdd:PRK07560 168 LKIIKdvnklikgmapeefkekwkVDVEDGtVAFgSAlynwaisvpmmqKTGIKfkdIIDyyekgkqkelaekaplhevV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 176 LERLVTAIPAP------------EGEIEA-------------PLQALIIDSWFDNYLGVVSLVRVKNGRVKKGDKILVKS 230
Cdd:PRK07560 248 LDMVVKHLPNPieaqkyripkiwKGDLNSevgkamlncdpngPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLVG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 231 TGKVHQVDSVGVFT-PKHTETVDLKAGEVGFIIaGIKDihgAPVGDTLTlnntpDVEVLPGFKRVK----PQVYAGLFPV 305
Cdd:PRK07560 328 AKKKNRVQQVGIYMgPEREEVEEIPAGNIAAVT-GLKD---ARAGETVV-----SVEDMTPFESLKhisePVVTVAIEAK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 306 SSDDFEDFRDALQKLTLNDSSLQYE--PESSEALGFGfrcgfLGMLHMEIIQERLEREYDLDLITTAPTVVF-EIVQKNG 382
Cdd:PRK07560 399 NPKDLPKLIEVLRQLAKEDPTLVVKinEETGEHLLSG-----MGELHLEVITYRIKRDYGIEVVTSEPIVVYrETVRGKS 473
|
490
....*....|
gi 15595964 383 EIIYVDNPSK 392
Cdd:PRK07560 474 QVVEGKSPNK 483
|
|
| EF4_III |
cd16260 |
Domain III of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly ... |
296-371 |
2.54e-47 |
|
Domain III of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly conserved guanosine triphosphatase found in bacteria and eukaryotic mitochondria and chloroplasts. EF4 functions as a translation factor, which promotes back-translocation of tRNAs on posttranslocational ribosome complexes and competes with elongation factor G for interaction with pretranslocational ribosomes, inhibiting the elongation phase of protein synthesis.
Pssm-ID: 293917 [Multi-domain] Cd Length: 76 Bit Score: 159.97 E-value: 2.54e-47
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15595964 296 PQVYAGLFPVSSDDFEDFRDALQKLTLNDSSLQYEPESSEALGFGFRCGFLGMLHMEIIQERLEREYDLDLITTAP 371
Cdd:cd16260 1 PMVFAGLYPVDGSDYEELRDALEKLTLNDASVTFEPETSSALGFGFRCGFLGLLHMEVFQERLEREYGLDLIITAP 76
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
9-186 |
3.46e-44 |
|
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: 155.53 E-value: 3.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 9 NFSIIAHIDHGKSTLADRFIQMCGGLSDREMEAQ-VLDSMDLERERGITIKAHSVTLHYKaqdgkTYQLNFIDTPGHVDF 87
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKEtFLDTLKEERERGITIKTGVVEFEWP-----KRRINFIDTPGHEDF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 88 TYEVSRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGLEVMPVLNKMDL-PQAEPERVKEEIESIIGI--------DA 158
Cdd:cd00881 76 SKETVRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRvGEEDFDEVLREIKELLKLigftflkgKD 155
|
170 180
....*....|....*....|....*...
gi 15595964 159 TDAVACSAKSGMGVLEVLERLVTAIPAP 186
Cdd:cd00881 156 VPIIPISALTGEGIEELLDAIVEHLPPP 183
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
7-186 |
9.55e-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: 154.67 E-value: 9.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 7 IRNFSIIAHIDHGKSTLADRFIQMCGGLSDRE-MEAQVLDSMDLERERGITIKAHSVTLHYKAqdgktYQLNFIDTPGHV 85
Cdd:cd01891 2 IRNIAIIAHVDHGKTTLVDALLKQSGTFRENEeVGERVMDSNDLERERGITILAKNTAITYKD-----TKINIIDTPGHA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 86 DFTYEVSRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGLEVMPVLNKMDLPQAEPERVKEEI-ESIIGIDATD---- 160
Cdd:cd01891 77 DFGGEVERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDRPDARPEEVVDEVfDLFLELNATDeqld 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 15595964 161 --AVACSAKSGMGVLE----------VLERLVTAIPAP 186
Cdd:cd01891 157 fpIVYASAKNGWASLNlddpsedldpLFETIIEHVPAP 194
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
8-154 |
6.97e-43 |
|
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: 153.16 E-value: 6.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 8 RNFSIIAHIDHGKSTLADRFIQMCGGLSDREM-EAQVLDSMDLERERGITIKAHSVTLHYK----AQDGKTYQLNFIDTP 82
Cdd:cd01885 1 RNICIIAHVDHGKTTLSDSLLASAGIISEKLAgKARYLDTREDEQERGITIKSSAISLYFEyeeeKMDGNDYLINLIDSP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15595964 83 GHVDFTYEVSRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGLEVMPVLNKMDLPQAE----PERVKEEIESII 154
Cdd:cd01885 81 GHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDRLILElklsPEEAYQRLLRIV 156
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
13-375 |
2.96e-42 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 161.83 E-value: 2.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 13 IAHIDHGKSTLADRFIQMCGGLSDR---EMEAQVLDSMDLERERGITIKAHSVTLHYKAqdgktYQLNFIDTPGHVDFTY 89
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRIgevEDGTTTMDFMPEERERGISITSAATTCEWKG-----HKINLIDTPGHVDFTG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 90 EVSRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGLEVMPVLNKMDLPQAEPERVKEEI------------------E 151
Cdd:PRK12740 76 EVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRAGADFFRVLAQLqeklgapvvplqlpigegD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 152 SIIGI------------------------DATDAVA-------------------------------------------- 163
Cdd:PRK12740 156 DFTGVvdllsmkayrydeggpseeieipaELLDRAEeareellealaefddelmekylegeelseeeikaglrkatlage 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 164 ------CSAKSGMGVLEVLERLVTAIPAP-----------------EGEIEAPLQALIIDSWFDNYLGVVSLVRVKNGRV 220
Cdd:PRK12740 236 ivpvfcGSALKNKGVQRLLDAVVDYLPSPlevppvdgedgeegaelAPDPDGPLVALVFKTMDDPFVGKLSLVRVYSGTL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 221 KKGDKILVKSTGKVHQVDSVGVFTPKHTETVD-LKAGEVGfIIAGIKDIHgapVGDTLTlnnTPDVEVLPGFKRVKPQVY 299
Cdd:PRK12740 316 KKGDTLYNSGTGKKERVGRLYRMHGKQREEVDeAVAGDIV-AVAKLKDAA---TGDTLC---DKGDPILLEPMEFPEPVI 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595964 300 A-GLFPVSSDDFEDFRDALQKLTLNDSSLQYE--PESSEALGFGfrcgfLGMLHMEIIQERLEREYDLDLITTAPTVVF 375
Cdd:PRK12740 389 SlAIEPKDKGDEEKLSEALGKLAEEDPTLRVErdEETGQTILSG-----MGELHLDVALERLKREYGVEVETGPPQVPY 462
|
|
| EF4_II |
cd03699 |
Domain II of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly ... |
194-279 |
8.56e-41 |
|
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: 142.56 E-value: 8.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 194 LQALIIDSWFDNYLGVVSLVRVKNGRVKKGDKILVKSTGKVHQVDSVGVFTPKHTETVDLKAGEVGFIIAGIKDIHGAPV 273
Cdd:cd03699 1 LRALIFDSWYDPYRGVVVLVRVFDGTLKKGDKIRFMATGKEYEVLEVGVFTPKMVPTDELSAGEVGYIIAGIKSVKDARV 80
|
....*.
gi 15595964 274 GDTLTL 279
Cdd:cd03699 81 GDTITL 86
|
|
| EF-G |
TIGR00484 |
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ... |
3-375 |
2.46e-37 |
|
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: 147.65 E-value: 2.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 3 DLSHIRNFSIIAHIDHGKSTLADRFIQMCG---GLSDREMEAQVLDSMDLERERGITIKAHSVTLHYKAqdgktYQLNFI 79
Cdd:TIGR00484 6 DLNRFRNIGISAHIDAGKTTTTERILFYTGrihKIGEVHDGAATMDWMEQEKERGITITSAATTVFWKG-----HRINII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 80 DTPGHVDFTYEVSRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGLEVMPVLNKMDLPQAEPERVKEEIESIIGIDAT 159
Cdd:TIGR00484 81 DTPGHVDFTVEVERSLRVLDGAVAVLDAVGGVQPQSETVWRQANRYEVPRIAFVNKMDKTGANFLRVVNQIKQRLGANAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 160 -------------------------------------------------------DAVA--------------------- 163
Cdd:TIGR00484 161 piqlpigaednfigvidlvemkayffngdkgtkaiekeipsdlleqakelrenlvEAVAefdeelmekylegeeltieei 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 164 -----------------C-SAKSGMGVLEVLERLVTAIPAP---------------EGEI----EAPLQALIIDSWFDNY 206
Cdd:TIGR00484 241 knairkgvlnceffpvlCgSAFKNKGVQLLLDAVVDYLPSPtdvpaikgidpdtekEIERkasdDEPFSALAFKVATDPF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 207 LGVVSLVRVKNGRVKKGDKILVKSTGKVHQVDS-VGVFTPKHTETVDLKAGEVGFIIaGIKDihgAPVGDTLTlnnTPDV 285
Cdd:TIGR00484 321 VGQLTFVRVYSGVLKSGSYVKNSRKNKKERVGRlVKMHANNREEIKEVRAGDICAAI-GLKD---TTTGDTLC---DPKI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 286 EV-LPGFKRVKPQVYAGLFPVSSDDFEDFRDALQKLTLNDSSL--QYEPESSEALGFGfrcgfLGMLHMEIIQERLEREY 362
Cdd:TIGR00484 394 DViLERMEFPEPVISLAVEPKTKADQEKMGIALGKLAEEDPTFrtFTDPETGQTIIAG-----MGELHLDIIVDRMKREF 468
|
490
....*....|...
gi 15595964 363 DLDLITTAPTVVF 375
Cdd:TIGR00484 469 KVEANVGAPQVAY 481
|
|
| lepA_C |
cd03709 |
lepA_C: This family represents the C-terminal region of LepA, a GTP-binding protein localized ... |
404-482 |
6.39e-37 |
|
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: 131.85 E-value: 6.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 404 EPICRATILVPKDHLGNVITLCIEKRGVQRDMHFLSG-QVQVVYDLPMNEVVLDFFDRLKSTSRGYASLDYSFDRFEPSN 482
Cdd:cd03709 1 EPFVKATIITPSEYLGAIMELCQERRGVQKDMEYLDAnRVMLTYELPLAEIVYDFFDKLKSISKGYASLDYELIGYRESD 80
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
1-392 |
8.87e-36 |
|
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]
Pssm-ID: 129581 [Multi-domain] Cd Length: 720 Bit Score: 143.11 E-value: 8.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 1 MSDLSHIRNFSIIAHIDHGKSTLADRFIQMCGGLSDREMEAQV-LDSMDLERERGITIKAHSVTLHYkAQDGKTYQLNFI 79
Cdd:TIGR00490 13 MWKPKFIRNIGIVAHIDHGKTTLSDNLLAGAGMISEELAGQQLyLDFDEQEQERGITINAANVSMVH-EYEGNEYLINLI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 80 DTPGHVDFTYEVSRSLAACEGALLVVDAGQGVEAQSvancYTAIEQGLE--VMPVL--NKMDLPQAE----PERVKEEIE 151
Cdd:TIGR00490 92 DTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQT----ETVLRQALKenVKPVLfiNKVDRLINElkltPQELQERFI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 152 SIIG-------------------IDATD--------------AVACSAKSGMGVLE----------------------VL 176
Cdd:TIGR00490 168 KIITevnklikamapeefrdkwkVRVEDgsvafgsayynwaiSVPSMKKTGIGFKDiykyckedkqkelakksplhqvVL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 177 ERLVTAIPAP------------EGEIEA-------------PLQALIIDSWFDNYLGVVSLVRVKNGRVKKGDKILVKST 231
Cdd:TIGR00490 248 DMVIRHLPSPieaqkyripviwKGDLNSevgkamlncdpkgPLALMITKIVVDKHAGEVAVGRLYSGTIRPGMEVYIVDR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 232 GKVHQVDSVGVFT-PKHTETVDLKAGEVGFIIaGIKDihgAPVGDTLTlnnTPDvEVLPGFKRVK----PQVYAGLFPVS 306
Cdd:TIGR00490 328 KAKARIQQVGVYMgPERVEVDEIPAGNIVAVI-GLKD---AVAGETIC---TTV-ENITPFESIKhisePVVTVAIEAKN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 307 SDDFEDFRDALQKLTLNDSSLQYE--PESSEALGFGfrcgfLGMLHMEIIQERLEREYDLDLITTAPTVVF-EIVQKNGE 383
Cdd:TIGR00490 400 TKDLPKLIEVLRQVAKEDPTVHVEinEETGEHLISG-----MGELHLEIIVEKIREDYGLDVETSPPIVVYrETVTGTSP 474
|
....*....
gi 15595964 384 IIYVDNPSK 392
Cdd:TIGR00490 475 VVEGKSPNK 483
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
9-158 |
2.07e-33 |
|
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: 128.76 E-value: 2.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 9 NFSIIAHIDHGKSTLADRfIQMCGGLSDREME----AQVLDSMDLERERGITIKAHSVTLHYKaqdgkTYQLNFIDTPGH 84
Cdd:cd01886 1 NIGIIAHIDAGKTTTTER-ILYYTGRIHKIGEvhggGATMDWMEQERERGITIQSAATTCFWK-----DHRINIIDTPGH 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595964 85 VDFTYEVSRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGLEVMPVLNKMDLPQAEPERVKEEIESIIGIDA 158
Cdd:cd01886 75 VDFTIEVERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQIREKLGANP 148
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
1-155 |
3.03e-30 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 126.70 E-value: 3.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 1 MSDLSHIRNFSIIAHIDHGKSTLADRFIQMCGGLSDREM-EAQVLDSMDLERERGITIKAHSVTLHYK-----AQDGKTY 74
Cdd:PTZ00416 13 MDNPDQIRNMSVIAHVDHGKSTLTDSLVCKAGIISSKNAgDARFTDTRADEQERGITIKSTGISLYYEhdledGDDKQPF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 75 QLNFIDTPGHVDFTYEVSRSLAACEGALLVVDAGQGVEAQSvancYTAIEQGLE--VMPVL--NKMDLP----QAEPE-- 144
Cdd:PTZ00416 93 LINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQT----ETVLRQALQerIRPVLfiNKVDRAilelQLDPEei 168
|
170
....*....|....*.
gi 15595964 145 -----RVKEEIESIIG 155
Cdd:PTZ00416 169 yqnfvKTIENVNVIIA 184
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
8-137 |
1.77e-29 |
|
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: 115.83 E-value: 1.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 8 RNFSIIAHIDHGKSTLADRFI----QMCGGLSDREMEAQVLDSMDLERERGITIKAHSVTLHYKAQDGKTYQLNFIDTPG 83
Cdd:cd04167 1 RNVCIAGHLHHGKTSLLDMLIeqthKRTPSVKLGWKPLRYTDTRKDEQERGISIKSNPISLVLEDSKGKSYLINIIDTPG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 15595964 84 HVDFTYEVSRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGLEVMPVLNKMD 137
Cdd:cd04167 81 HVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKID 134
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
1-137 |
2.95e-29 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 123.30 E-value: 2.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 1 MSDLSHIRNFSIIAHIDHGKSTLADRFIQMCGGLS-DREMEAQVLDSMDLERERGITIKAHSVTLHYK-----------A 68
Cdd:PLN00116 13 MDKKHNIRNMSVIAHVDHGKSTLTDSLVAAAGIIAqEVAGDVRMTDTRADEAERGITIKSTGISLYYEmtdeslkdfkgE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15595964 69 QDGKTYQLNFIDTPGHVDFTYEVSRSLAACEGALLVVDAGQGVEAQSvancYTAIEQGL--EVMPVL--NKMD 137
Cdd:PLN00116 93 RDGNEYLINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQT----ETVLRQALgeRIRPVLtvNKMD 161
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
1-285 |
1.23e-26 |
|
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444074 [Multi-domain] Cd Length: 423 Bit Score: 112.72 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 1 MSDLSHIrNFSIIAHIDHGKSTLADRFIQMCGGLSDREME----------------AQVLDSMDLERERGITIKahsvtL 64
Cdd:COG5256 2 ASEKPHL-NLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEkyeeeaekkgkesfkfAWVMDRLKEERERGVTID-----L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 65 HYKAQDGKTYQLNFIDTPGHVDFTYEVSRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGLEVMPV-LNKMDLP---Q 140
Cdd:COG5256 76 AHKKFETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVaVNKMDAVnysE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 141 AEPERVKEEIESI---IGIDATDA--VACSAKSGMGVLE-----------VLERLVTAIPAPEGEIEAPLQALIIDSWFD 204
Cdd:COG5256 156 KRYEEVKEEVSKLlkmVGYKVDKIpfIPVSAWKGDNVVKksdnmpwyngpTLLEALDNLKEPEKPVDKPLRIPIQDVYSI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 205 NYLGVVSLVRVKNGRVKKGDKILVKSTGKVHQVDSVGVftpKHTETVDLKAGE-VGFIIAGI--KDIH-GAPVGDTltlN 280
Cdd:COG5256 236 SGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEM---HHEELEQAEPGDnIGFNVRGVekNDIKrGDVAGHP---D 309
|
....*
gi 15595964 281 NTPDV 285
Cdd:COG5256 310 NPPTV 314
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
9-198 |
2.01e-25 |
|
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: 105.01 E-value: 2.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 9 NFSIIAHIDHGKSTLADRFIQMCGGLSDR----EMEAQvLDSMDLERERGITIKAHSVTLHYKAQDgktyqLNFIDTPGH 84
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIRELgsvdKGTTR-TDSMELERQRGITIFSAVASFQWEDTK-----VNIIDTPGH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 85 VDFTYEVSRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGLEVMPVLNKMDLPQAEPERVKEEI-------------- 150
Cdd:cd04168 75 MDFIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTIIFVNKIDRAGADLEKVYQEIkeklspdivpmqkv 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15595964 151 --------ESIIGIDATDAVAcsaksgMGVLEVLERLVTAIPAPEGEIEAPLQALI 198
Cdd:cd04168 155 glypnicdTNNIDDEQIETVA------EGNDELLEKYLSGGPLEELELDNELSARI 204
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
8-159 |
1.14e-24 |
|
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.
Pssm-ID: 206732 [Multi-domain] Cd Length: 268 Bit Score: 103.83 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 8 RNFSIIAHIDHGKSTLADRF------IQMCGGLSDR-EMEAQVLDSMDLERERGITIKAHSVTLHYKAqdgktYQLNFID 80
Cdd:cd04169 3 RTFAIISHPDAGKTTLTEKLllfggaIQEAGAVKARkSRKHATSDWMEIEKQRGISVTSSVMQFEYKG-----CVINLLD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 81 TPGHVDF---TYevsRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGLEVMPVLNKMDLPQAEPERVKEEIESIIGID 157
Cdd:cd04169 78 TPGHEDFsedTY---RTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDREGRDPLELLDEIENELGID 154
|
..
gi 15595964 158 AT 159
Cdd:cd04169 155 CA 156
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
1-268 |
4.49e-24 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 105.01 E-value: 4.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 1 MSDLSHIrNFSIIAHIDHGKSTLADRFIQMCGGLSDREME----------------AQVLDSMDLERERGITIKahsvtL 64
Cdd:PRK12317 1 AKEKPHL-NLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEelreeakekgkesfkfAWVMDRLKEERERGVTID-----L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 65 HYKAQDGKTYQLNFIDTPGHVDFTYEVSRSLAACEGALLVVDA--GQGVEAQSVANCYTAIEQGLEVMPV-LNKMDLP-- 139
Cdd:PRK12317 75 AHKKFETDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAAddAGGVMPQTREHVFLARTLGINQLIVaINKMDAVny 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 140 -QAEPERVKEEIESI---IGIDATDA--VACSAKSGMGVLE-----------VLERLVTAIPAPEGEIEAPLQALIIDSW 202
Cdd:PRK12317 155 dEKRYEEVKEEVSKLlkmVGYKPDDIpfIPVSAFEGDNVVKksenmpwyngpTLLEALDNLKPPEKPTDKPLRIPIQDVY 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595964 203 FDNYLGVVSLVRVKNGRVKKGDKILVKSTGKVHQVDSVGVftpKHTETVDLKAGE-VGFIIAGI--KDI 268
Cdd:PRK12317 235 SISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEM---HHEELPQAEPGDnIGFNVRGVgkKDI 300
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
3-286 |
3.90e-20 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 93.27 E-value: 3.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 3 DLSHIrNFSIIAHIDHGKSTLADRFIQMCGGLSDREME----------------AQVLDSMDLERERGITIkahSVTLhY 66
Cdd:PTZ00141 4 EKTHI-NLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEkfekeaaemgkgsfkyAWVLDKLKAERERGITI---DIAL-W 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 67 KAQDGKtYQLNFIDTPGHVDFTYEVSRSLAACEGALLVVDAGQGV-------EAQSVANCYTAIEQGLEVMPV-LNKMDL 138
Cdd:PTZ00141 79 KFETPK-YYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEfeagiskDGQTREHALLAFTLGVKQMIVcINKMDD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 139 P-----QAEPERVKEEIESII-----GIDATDAVACSAKSGMGVLE------------VLERLVTAIPaPEGEIEAPLQA 196
Cdd:PTZ00141 158 KtvnysQERYDEIKKEVSAYLkkvgyNPEKVPFIPISGWQGDNMIEksdnmpwykgptLLEALDTLEP-PKRPVDKPLRL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 197 LIIDSWFDNYLGVVSLVRVKNGRVKKGDKILVKSTGKVHQVDSVGVFtpkHTETVDLKAGE-VGFIIAGI--KDI-HGAP 272
Cdd:PTZ00141 237 PLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMH---HEQLAEAVPGDnVGFNVKNVsvKDIkRGYV 313
|
330
....*....|....
gi 15595964 273 VGDTltlNNTPDVE 286
Cdd:PTZ00141 314 ASDS---KNDPAKE 324
|
|
| EFG_C |
pfam00679 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
401-488 |
7.98e-20 |
|
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: 84.13 E-value: 7.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 401 EMREPICRATILVPKDHLGNVITLCIEKRGVQRDMHFLSGQVQVV-YDLPMNEVVlDFFDRLKSTSRGYASLDYSFDRFE 479
Cdd:pfam00679 1 VLLEPIEKVTIDVPEEYVGDVISDLNSRRGEILDMDPDDGGRVVIeAEVPLAELF-GFATELRSLTKGRGSFSMEFSGYQ 79
|
....*....
gi 15595964 480 PSNLVRLDV 488
Cdd:pfam00679 80 PVPGDILDR 88
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
11-234 |
2.32e-19 |
|
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]
Pssm-ID: 273102 [Multi-domain] Cd Length: 587 Bit Score: 91.75 E-value: 2.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 11 SIIAHIDHGKSTLAD--RFIQMCGGlsdremEAQvldsmdlererGITikAHSVTLHYKAQDGKtyQLNFIDTPGHVDFT 88
Cdd:TIGR00487 91 TIMGHVDHGKTSLLDsiRKTKVAQG------EAG-----------GIT--QHIGAYHVENEDGK--MITFLDTPGHEAFT 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 89 YEVSRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGLEVMPVLNKMDLPQAEPERVKEEIeSIIGIDA------TDAV 162
Cdd:TIGR00487 150 SMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVPIIVAINKIDKPEANPDRVKQEL-SEYGLVPedwggdTIFV 228
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15595964 163 ACSAKSGMGVLEVLER--LVTAIPAPEGEIEAPLQALIIDSWFDNYLGVVSLVRVKNGRVKKGDKILVKST-GKV 234
Cdd:TIGR00487 229 PVSALTGDGIDELLDMilLQSEVEELKANPNGQASGVVIEAQLDKGRGPVATVLVQSGTLRVGDIVVVGAAyGRV 303
|
|
| Elongation_Factor_C |
cd01514 |
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ... |
404-482 |
2.61e-19 |
|
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: 82.53 E-value: 2.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 404 EPICRATILVPKDHLGNVITLCIEKRGVQRDMHFL-SGQVQVVYDLPMNEvVLDFFDRLKSTSRGYASLDYSFDRFEPSN 482
Cdd:cd01514 1 EPIMKVEITVPEEYLGAVIGDLSKRRGEILGMEPRgTGRVVIKAELPLAE-MFGFATDLRSLTQGRASFSMEFSHYEPVP 79
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
12-180 |
3.93e-19 |
|
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.
Pssm-ID: 206674 [Multi-domain] Cd Length: 169 Bit Score: 84.83 E-value: 3.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 12 IIAHIDHGKSTLADRfIQmcgGLSDREMEAqvldsmdlereRGIT--IKAHSVTLHYKAQdgktyQLNFIDTPGHVDFTY 89
Cdd:cd01887 5 VMGHVDHGKTTLLDK-IR---KTNVAAGEA-----------GGITqhIGAYQVPIDVKIP-----GITFIDTPGHEAFTN 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 90 EVSRSLAACEGALLVVDAGQGVEAQSVAncytAIE----QGLEVMPVLNKMDLP---QAEPERVKEEIES--IIGIDATD 160
Cdd:cd01887 65 MRARGASVTDIAILVVAADDGVMPQTIE----AINhakaANVPIIVAINKIDKPygtEADPERVKNELSElgLVGEEWGG 140
|
170 180
....*....|....*....|...
gi 15595964 161 AVAC---SAKSGMGVLEVLERLV 180
Cdd:cd01887 141 DVSIvpiSAKTGEGIDDLLEAIL 163
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
8-158 |
3.79e-18 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 87.88 E-value: 3.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 8 RNFSIIAHIDHGKSTLADRF------IQMCGGL----SDREMEAqvlDSMDLERERGITIkAHSV-TLHYKaqdgkTYQL 76
Cdd:PRK00741 11 RTFAIISHPDAGKTTLTEKLllfggaIQEAGTVkgrkSGRHATS---DWMEMEKQRGISV-TSSVmQFPYR-----DCLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 77 NFIDTPGHVDF---TYevsRSLAACEGALLVVDAGQGVEAQSVancytaieQGLEV-----MPVL---NKMDLPQAEPER 145
Cdd:PRK00741 82 NLLDTPGHEDFsedTY---RTLTAVDSALMVIDAAKGVEPQTR--------KLMEVcrlrdTPIFtfiNKLDRDGREPLE 150
|
170
....*....|...
gi 15595964 146 VKEEIESIIGIDA 158
Cdd:PRK00741 151 LLDEIEEVLGIAC 163
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
11-241 |
5.07e-18 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 87.97 E-value: 5.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 11 SIIAHIDHGKSTLADRfiqmcgglsdremeaqVLDSMDLERER-GIT--IKAHSVTLHYKaqdGKTYQLNFIDTPGHVDF 87
Cdd:CHL00189 248 TILGHVDHGKTTLLDK----------------IRKTQIAQKEAgGITqkIGAYEVEFEYK---DENQKIVFLDTPGHEAF 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 88 TYEVSRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGLEVMPVLNKMDLPQAEPERVKEEI--ESIIGID---ATDAV 162
Cdd:CHL00189 309 SSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANTERIKQQLakYNLIPEKwggDTPMI 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 163 ACSAKSGMGVLEVLER--LVTAIPAPEGEIEAPLQALIIDSWFDNYLGVVSLVRVKNGRVKKGDKILVKST-GKVHQ-VD 238
Cdd:CHL00189 389 PISASQGTNIDKLLETilLLAEIEDLKADPTQLAQGIILEAHLDKTKGPVATILVQNGTLHIGDIIVIGTSyAKIRGmIN 468
|
...
gi 15595964 239 SVG 241
Cdd:CHL00189 469 SLG 471
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
9-156 |
2.11e-17 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 82.64 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 9 NFSIIAHIDHGKSTLADRfIQMCGGLSDR----EMEAQVLDSMDLERERGITIKAHSVTLHYKaqdgkTYQLNFIDTPGH 84
Cdd:cd04170 1 NIALVGHSGSGKTTLAEA-LLYATGAIDRlgrvEDGNTVSDYDPEEKKRKMSIETSVAPLEWN-----GHKINLIDTPGY 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15595964 85 VDFTYEVSRSLAACEGALLVVDAGQGVEAQsVANCYTAIEQ-GLEVMPVLNKMDLPQAEPERVKEEIESIIGI 156
Cdd:cd04170 75 ADFVGETLSALRAVDAALIVVEAQSGVEVG-TEKVWEFLDDaKLPRIIFINKMDRARADFDKTLAALREAFGR 146
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
9-174 |
2.84e-16 |
|
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: 77.92 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 9 NFSIIAHIDHGKSTLADRFIQMCGGLSDREME----------------AQVLDSMDLERERGITIkahSVTLHYKAQDGK 72
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEkyekeakemgkesfkyAWVLDKLKEERERGVTI---DVGLAKFETEKY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 73 TYQLnfIDTPGHVDFTYE--VSRSLAACegALLVVDAGQGveaqsvancytAIEQGLEVMP------------------- 131
Cdd:cd01883 78 RFTI--IDAPGHRDFVKNmiTGASQADV--AVLVVSARKG-----------EFEAGFEKGGqtrehallartlgvkqliv 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15595964 132 VLNKMDLP-----QAEPERVKEEIESI---IGIDATDA--VACSAKSGMGVLE 174
Cdd:cd01883 143 AVNKMDDVtvnwsQERYDEIKKKVSPFlkkVGYNPKDVpfIPISGFTGDNLIE 195
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
5-226 |
5.01e-15 |
|
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: 77.12 E-value: 5.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 5 SHIrNFSIIAHIDHGKSTLADRFIQMCGGLSDREMEA-QVLDSMDLERERGITIKAHSV-----TLHYKaqdgktyqlnF 78
Cdd:TIGR00485 11 PHV-NVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAyDQIDNAPEEKARGITINTAHVeyeteTRHYA----------H 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 79 IDTPGHVDFTYEVSRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGLEVMPV-LNKMDLPQAEP--ERVKEEIES--- 152
Cdd:TIGR00485 80 VDCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKCDMVDDEEllELVEMEVRElls 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 153 ----------IIGIDATDAVACSAKSGMGVLEVLERLVTAIPAPEGEIEAPLQALIIDSWFDNYLGVVSLVRVKNGRVKK 222
Cdd:TIGR00485 160 qydfpgddtpIIRGSALKALEGDAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKV 239
|
....
gi 15595964 223 GDKI 226
Cdd:TIGR00485 240 GEEV 243
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
9-300 |
7.37e-15 |
|
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: 77.61 E-value: 7.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 9 NFSIIAHIDHGKSTLADrfiQMCGGLSDREMEaqvldsmdlERERGITIKahsvtLHYKAQDGKTYQLNFIDTPGHVDFT 88
Cdd:TIGR00475 2 IIATAGHVDHGKTTLLK---ALTGIAADRLPE---------EKKRGMTID-----LGFAYFPLPDYRLGFIDVPGHEKFI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 89 YEVSRSLAACEGALLVVDAGQGVEAQSVAncYTAIEQGL---EVMPVLNKMD-LPQAEPERVKEEIESI----IGIDATD 160
Cdd:TIGR00475 65 SNAIAGGGGIDAALLVVDADEGVMTQTGE--HLAVLDLLgipHTIVVITKADrVNEEEIKRTEMFMKQIlnsyIFLKNAK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 161 AVACSAKSGMGVLEV---LERLVTAIPAPegEIEAPLQaLIIDSWFdNYLGVVSLVR--VKNGRVKKGDKILVKSTGKVH 235
Cdd:TIGR00475 143 IFKTSAKTGQGIGELkkeLKNLLESLDIK--RIQKPLR-MAIDRAF-KVKGAGTVVTgtAFSGEVKVGDNLRLLPINHEV 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15595964 236 QVDSVgvftpkHTETVDLKAGEVGFIIA-GIKDIHGAPVGDTLtLNNTPdvevLPGFKRVKPQVYA 300
Cdd:TIGR00475 219 RVKAI------QAQNQDVEIAYAGQRIAlNLMDVEPESLKRGL-LILTP----EDPKLRVVVKFIA 273
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
15-187 |
1.97e-14 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.
Pssm-ID: 206734 [Multi-domain] Cd Length: 170 Bit Score: 71.48 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 15 HIDHGKSTLadrfIQMCGGlsdreMEAqvlDSMDLERERGITIKAHSVTLHYKaqDGKTyqLNFIDTPGHVDFtyeVSRS 94
Cdd:cd04171 7 HIDHGKTTL----IKALTG-----IET---DRLPEEKKRGITIDLGFAYLDLP--DGKR--LGFIDVPGHEKF---VKNM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 95 LAACEG---ALLVVDAGQGVEAQSVAncYTAIEQGLEV---MPVLNKMDL-PQAEPERVKEEI----ESIIGIDATdAVA 163
Cdd:cd04171 68 LAGAGGidaVLLVVAADEGIMPQTRE--HLEILELLGIkkgLVVLTKADLvDEDRLELVEEEIlellAGTFLADAP-IFP 144
|
170 180
....*....|....*....|....
gi 15595964 164 CSAKSGMGVLEVLERLvTAIPAPE 187
Cdd:cd04171 145 VSSVTGEGIEELKNYL-DELAEPQ 167
|
|
| EFG_III-like |
cd16257 |
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G ... |
296-367 |
1.98e-14 |
|
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G (EF-G) and related proteins play a role in translation and share a similar domain architecture. Elongation factor EFG participates in the elongation phase during protein biosynthesis on the ribosome by stimulating translocation. Its functional cycles depend on GTP binding and its hydrolysis. Domain III is involved in the activation of GTP hydrolysis. This domain III, which is different from domain III in EF-TU and related elongation factors, is found in several translation factors, like bacterial release factors RF3, elongation factor 4, elongation factor 2, GTP-binding protein BipA and tetracycline resistance protein Tet.
Pssm-ID: 293914 [Multi-domain] Cd Length: 71 Bit Score: 68.14 E-value: 1.98e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15595964 296 PQVYAGLFPVSSDDFEDFRDALQKLTLNDSSLQYEPESSEalgFGFRCGFLGMLHMEIIQERLEREYDLDLI 367
Cdd:cd16257 1 PVVFVTVEVKNPLDQEKLLEGLERLSEEDPALQVYREEST---GEFILSGLGELHLEIIVARLEREYGVELV 69
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
12-186 |
2.17e-14 |
|
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 442507 [Multi-domain] Cd Length: 630 Bit Score: 76.11 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 12 IIA---HIDHGKSTL--------ADRFiqmcgglsdREmeaqvldsmdlERERGITIK---AHsVTLHykaqDGKTyqLN 77
Cdd:COG3276 2 IIGtagHIDHGKTTLvkaltgidTDRL---------KE-----------EKKRGITIDlgfAY-LPLP----DGRR--LG 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 78 FIDTPGHVDFtyeVSRSLAACEG---ALLVVDAGQGVEAQSV---ANC-YTAIEQGlevMPVLNKMDLpqAEPER---VK 147
Cdd:COG3276 55 FVDVPGHEKF---IKNMLAGAGGidlVLLVVAADEGVMPQTRehlAILdLLGIKRG---IVVLTKADL--VDEEWlelVE 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15595964 148 EEIESII---GIDATDAVACSAKSGMGV---LEVLERLVTAIPAP 186
Cdd:COG3276 127 EEIRELLagtFLEDAPIVPVSAVTGEGIdelRAALDALAAAVPAR 171
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
9-169 |
3.57e-14 |
|
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: 71.83 E-value: 3.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 9 NFSIIAHIDHGKSTLADRFIQMCGGLSDREME-----------------AQVLDSMDLERERGITIkahSVTLHYKAQDG 71
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSIFEDQLAalerskssgtqgekldlALLVDGLQAEREQGITI---DVAYRYFSTPK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 72 KTYQLnfIDTPGHVDFTYEVSRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGL-EVMPVLNKMDL---PQAEPERVK 147
Cdd:cd04166 78 RKFII--ADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIrHVVVAVNKMDLvdyDEEVFEEIK 155
|
170 180
....*....|....*....|....*
gi 15595964 148 EEIESI---IGIDATDAVACSAKSG 169
Cdd:cd04166 156 ADYLAFaasLGIEDITFIPISALEG 180
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
19-181 |
3.63e-14 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 70.56 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 19 GKSTLADRFIQmcgglsdremeaqvLDSMDLERERGITIKAHSVTLHYkaqDGKTYQLNFIDTPGHVDFTYEVSRSLAA- 97
Cdd:cd00882 9 GKSSLLNALLG--------------GEVGEVSDVPGTTRDPDVYVKEL---DKGKVKLVLVDTPGLDEFGGLGREELARl 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 98 ----CEGALLVVDAGQGVEAQSVANCY--TAIEQGLEVMPVLNKMDLPQAEPERVKEEIESIIGIDATDAVACSAKSGMG 171
Cdd:cd00882 72 llrgADLILLVVDSTDRESEEDAKLLIlrRLRKEGIPIILVGNKIDLLEEREVEELLRLEELAKILGVPVFEVSAKTGEG 151
|
170
....*....|
gi 15595964 172 VLEVLERLVT 181
Cdd:cd00882 152 VDELFEKLIE 161
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
15-245 |
9.93e-14 |
|
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: 73.90 E-value: 9.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 15 HIDHGKSTLADRFIQmcgglsdremeAQVLdsmdlERE-RGIT--IKAHSVTLhykaqDGKtyQLNFIDTPGHVDFTYEV 91
Cdd:COG0532 12 HVDHGKTSLLDAIRK-----------TNVA-----AGEaGGITqhIGAYQVET-----NGG--KITFLDTPGHEAFTAMR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 92 SRslaaceGA------LLVVDAGQGVEAQSVAncytAIE--QGLEVmPV---LNKMDLPQAEPERVKEEI--ESII---- 154
Cdd:COG0532 69 AR------GAqvtdivILVVAADDGVMPQTIE----AINhaKAAGV-PIivaINKIDKPGANPDRVKQELaeHGLVpeew 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 155 GIDaTDAVACSAKSGMGVLEVLERLV--------TAIPapegeiEAPLQALIIDSWFDNYLGVVSLVRVKNGRVKKGDKI 226
Cdd:COG0532 138 GGD-TIFVPVSAKTGEGIDELLEMILlqaevlelKANP------DRPARGTVIEAKLDKGRGPVATVLVQNGTLKVGDIV 210
|
250 260
....*....|....*....|....*...
gi 15595964 227 LVKST-GKV--------HQVDSVGVFTP 245
Cdd:COG0532 211 VAGTAyGRVramfddrgKRVKEAGPSTP 238
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
19-183 |
1.15e-13 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 69.24 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 19 GKSTLADRFIQmcgglsdremeaqvlDSMDLERE---RGITIKAHSVTLhykaqDGKTYQLNFIDTPGHVDftYEVSRSL 95
Cdd:COG1100 15 GKTSLVNRLVG---------------DIFSLEKYlstNGVTIDKKELKL-----DGLDVDLVIWDTPGQDE--FRETRQF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 96 AACE-----GALLVVDAGQGVEAQSVANCYTAIEQ---GLEVMPVLNKMDLPQAEPERVKEEIESIIGIDATDA-VACSA 166
Cdd:COG1100 73 YARQltgasLYLFVVDGTREETLQSLYELLESLRRlgkKSPIILVLNKIDLYDEEEIEDEERLKEALSEDNIVEvVATSA 152
|
170
....*....|....*..
gi 15595964 167 KSGMGVLEVLERLVTAI 183
Cdd:COG1100 153 KTGEGVEELFAALAEIL 169
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
12-175 |
5.00e-13 |
|
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]
Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 67.01 E-value: 5.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 12 IIAHIDHGKSTLADRFIQmcgglsdremeaqvldsmdleRERGITIKAHSVTLHYKAQ----DGKTYQLNFIDTPGHVDF 87
Cdd:TIGR00231 6 IVGHPNVGKSTLLNSLLG---------------------NKGSITEYYPGTTRNYVTTvieeDGKTYKFNLLDTAGQEDY 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 88 -------TYEVSRSLAACEGALLVVDAGQGVEAQ--SVANcytAIEQGLEVMPVLNKMDLPQA-EPERVKEEIESIIGId 157
Cdd:TIGR00231 65 dairrlyYPQVERSLRVFDIVILVLDVEEILEKQtkEIIH---HADSGVPIILVGNKIDLKDAdLKTHVASEFAKLNGE- 140
|
170
....*....|....*...
gi 15595964 158 atDAVACSAKSGMGVLEV 175
Cdd:TIGR00231 141 --PIIPLSAETGKNIDSA 156
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
9-266 |
8.75e-13 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 70.80 E-value: 8.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 9 NFSIIAHIDHGKSTLAD----RFIQMCGGLSDREMEaqvLDSMDLERERGITIkaHSVTLHYKAQdgkTYQLNFIDTPGH 84
Cdd:PLN03126 83 NIGTIGHVDHGKTTLTAaltmALASMGGSAPKKYDE---IDAAPEERARGITI--NTATVEYETE---NRHYAHVDCPGH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 85 VDFTYEVSRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGLEVMPV-LNKMDLPQAEP--ERVKEEIESIIGI----- 156
Cdd:PLN03126 155 ADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVfLNKQDQVDDEEllELVELEVRELLSSyefpg 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 157 DATDAVACSAKSGMGVL------------------EVLERLVTAIPAPEGEIEAPLQALIIDSWFDNYLGVVSLVRVKNG 218
Cdd:PLN03126 235 DDIPIISGSALLALEALmenpnikrgdnkwvdkiyELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERG 314
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 15595964 219 RVKKGDKILVKSTGKVHQVDSVGVFTPKHTETVDLKAGEVGFIIAGIK 266
Cdd:PLN03126 315 TVKVGETVDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQ 362
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
49-180 |
2.19e-12 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 65.34 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 49 LERERGITIKAHSVTLH---YKAQDGKTYQLNFIDTPGHVD-------FTYEVSRSLAACEGALLVVDAGQGVEAQsVAN 118
Cdd:cd00880 18 LGQNVGIVSPIPGTTRDpvrKEWELLPLGPVVLIDTPGLDEegglgreRVEEARQVADRADLVLLVVDSDLTPVEE-EAK 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15595964 119 CYTAIEQGLEVMPVLNKMDLPQAEPERVKEEIESIIGIDATDAVACSAKSGMGVLEVLERLV 180
Cdd:cd00880 97 LGLLRERGKPVLLVLNKIDLVPESEEEELLRERKLELLPDLPVIAVSALPGEGIDELRKKIA 158
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
9-226 |
2.45e-12 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 68.82 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 9 NFSIIAHIDHGKSTLAdrfIQMCGGLSDREM-EAQVLDSMDL---ERERGITIK-AH----SVTLHYKaqdgktyqlnFI 79
Cdd:PRK12736 14 NIGTIGHVDHGKTTLT---AAITKVLAERGLnQAKDYDSIDAapeEKERGITINtAHveyeTEKRHYA----------HV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 80 DTPGHVDFTYEVSRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGLEVMPV-LNKMDLPQAEP--ERVKEEIESII-- 154
Cdd:PRK12736 81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVfLNKVDLVDDEEllELVEMEVRELLse 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 155 ---GIDATDAVACSAKSGM--------GVLEVLERLVTAIPAPEGEIEAPLQALIIDSWFDNYLGVVSLVRVKNGRVKKG 223
Cdd:PRK12736 161 ydfPGDDIPVIRGSALKALegdpkwedAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVG 240
|
...
gi 15595964 224 DKI 226
Cdd:PRK12736 241 DEV 243
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
6-268 |
5.71e-12 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 68.19 E-value: 5.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 6 HIrNFSIIAHIDHGKSTLADRFIQMCGGLSDREME----------------AQVLDSMDLERERGITIkahSVTLhYKAQ 69
Cdd:PLN00043 7 HI-NIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIErfekeaaemnkrsfkyAWVLDKLKAERERGITI---DIAL-WKFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 70 DGKtYQLNFIDTPGHVDFTYEVSRSLAACEGALLVVD-------AGQGVEAQSVANCYTAIEQGLEVMP-VLNKMD---- 137
Cdd:PLN00043 82 TTK-YYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDsttggfeAGISKDGQTREHALLAFTLGVKQMIcCCNKMDattp 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 138 -LPQAEPERVKEEIES----------------IIGIDATDAVACSAK----SGMGVLEVLERlvtaIPAPEGEIEAPLQA 196
Cdd:PLN00043 161 kYSKARYDEIVKEVSSylkkvgynpdkipfvpISGFEGDNMIERSTNldwyKGPTLLEALDQ----INEPKRPSDKPLRL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15595964 197 LIIDSWFDNYLGVVSLVRVKNGRVKKGDKILVKSTGKVHQVDSVGVftpKHTETVDLKAGE-VGFII--AGIKDI 268
Cdd:PLN00043 237 PLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEM---HHESLQEALPGDnVGFNVknVAVKDL 308
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
9-266 |
1.20e-10 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 64.08 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 9 NFSIIAHIDHGKSTLADRFIQMcggLSDREM-EAQVLDSMDL---ERERGITIKahsvTLHYKAQDGKTYQLNfIDTPGH 84
Cdd:PLN03127 63 NVGTIGHVDHGKTTLTAAITKV---LAEEGKaKAVAFDEIDKapeEKARGITIA----TAHVEYETAKRHYAH-VDCPGH 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 85 VDFTYEVSRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGLEVMPV-LNKMDLPQAEP--ERVKEEIESIIGI----- 156
Cdd:PLN03127 135 ADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVfLNKVDVVDDEEllELVEMELRELLSFykfpg 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 157 DATDAVACSAKSGM----------GVLEVLERLVTAIPAPEGEIEAPLQALIIDSWFDNYLGVVSLVRVKNGRVKKGD-- 224
Cdd:PLN03127 215 DEIPIIRGSALSALqgtndeigknAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEev 294
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 15595964 225 KILVKSTGKVHQVDSVGVFTPKHTETVDLKAGEVGFIIAGIK 266
Cdd:PLN03127 295 EIVGLRPGGPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLK 336
|
|
| tufA |
CHL00071 |
elongation factor Tu |
6-226 |
1.70e-10 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 63.05 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 6 HIrNFSIIAHIDHGKSTLADRfIQMC----GGLSDREMEAqvLDSMDLERERGITIKAHSV-----TLHYKaqdgktyql 76
Cdd:CHL00071 12 HV-NIGTIGHVDHGKTTLTAA-ITMTlaakGGAKAKKYDE--IDSAPEEKARGITINTAHVeyeteNRHYA--------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 77 nFIDTPGHVDFTYEVSRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGLEVMPV-LNKMDLPQAEP--ERVKEEIESI 153
Cdd:CHL00071 79 -HVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVfLNKEDQVDDEEllELVELEVREL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 154 I----------------GIDATDAVACSAKSGMG-------VLEVLERLVTAIPAPEGEIEAPLQALIIDSWFDNYLGVV 210
Cdd:CHL00071 158 LskydfpgddipivsgsALLALEALTENPKIKRGenkwvdkIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTV 237
|
250
....*....|....*.
gi 15595964 211 SLVRVKNGRVKKGDKI 226
Cdd:CHL00071 238 ATGRIERGTVKVGDTV 253
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
9-240 |
2.41e-10 |
|
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: 62.80 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 9 NFSIIAHIDHGKSTLADRFIQMCGGLSDREMEAQVLDS-------MDL---------ERERGITIkahSVTLHYKAQDGK 72
Cdd:COG2895 19 RFITCGSVDDGKSTLIGRLLYDTKSIFEDQLAALERDSkkrgtqeIDLalltdglqaEREQGITI---DVAYRYFSTPKR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 73 TYQLnfIDTPGHVDFTyevsRSLA----ACEGALLVVDAGQGVEAQSVANCYTA----IEQgleVMPVLNKMDL---PQA 141
Cdd:COG2895 96 KFII--ADTPGHEQYT----RNMVtgasTADLAILLIDARKGVLEQTRRHSYIAsllgIRH---VVVAVNKMDLvdySEE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 142 EPERVKEEIESI---IGIDATDAVACSAKSG---------MG------VLEVLErlvtAIPAPEGEIEAPL----QALII 199
Cdd:COG2895 167 VFEEIVADYRAFaakLGLEDITFIPISALKGdnvversenMPwydgptLLEHLE----TVEVAEDRNDAPFrfpvQYVNR 242
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 15595964 200 DSwfDNYLGVVSlvRVKNGRVKKGDKILVKSTGKVHQVDSV 240
Cdd:COG2895 243 PN--LDFRGYAG--TIASGTVRVGDEVVVLPSGKTSTVKSI 279
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
19-177 |
8.34e-10 |
|
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206682 [Multi-domain] Cd Length: 174 Bit Score: 58.21 E-value: 8.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 19 GKSTLADRFIQmcgglSDRemeaqVLDSmdleRERGITIKAHSVTLHYkaqDGKTYQLnfIDTPG---------HVDFtY 89
Cdd:cd01895 14 GKSSLLNALLG-----EER-----VIVS----DIAGTTRDSIDVPFEY---DGQKYTL--IDTAGirkkgkvteGIEK-Y 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 90 EVSRSLAACEGA---LLVVDAGQGVEAQ--SVANcyTAIEQGLEVMPVLNKMDL---PQAEPERVKEEIESIIG-IDATD 160
Cdd:cd01895 74 SVLRTLKAIERAdvvLLVLDASEGITEQdlRIAG--LILEEGKALIIVVNKWDLvekDEKTMKEFEKELRRKLPfLDYAP 151
|
170
....*....|....*..
gi 15595964 161 AVACSAKSGMGVLEVLE 177
Cdd:cd01895 152 IVFISALTGQGVDKLFD 168
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
9-183 |
2.57e-09 |
|
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: 56.99 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 9 NFSIIAHIDHGKSTLADrfiqmcgGLSDREMEAqVLDSMDLERERGITI---------KAHSVTLHYKAQDGKTYQLNFI 79
Cdd:cd01889 2 NVGLLGHVDSGKTSLAK-------ALSEIASTA-AFDKNPQSQERGITLdlgfssfevDKPKHLEDNENPQIENYQITLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 80 DTPGHVDFTYEVSRSLAACEGALLVVDAGQGVEAQSvANCYTAIEQ-GLEVMPVLNKMDLPQAEPERVKEEIESIIGIDA 158
Cdd:cd01889 74 DCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQT-AECLVIGELlCKPLIVVLNKIDLIPEEERKRKIEKMKKRLQKT 152
|
170 180 190
....*....|....*....|....*....|...
gi 15595964 159 TDA--------VACSAKSGMGVLEVLERLVTAI 183
Cdd:cd01889 153 LEKtrlkdspiIPVSAKPGEGEAELGGELKNLI 185
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
208-278 |
3.86e-09 |
|
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.
Pssm-ID: 427163 [Multi-domain] Cd Length: 73 Bit Score: 53.42 E-value: 3.86e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15595964 208 GVVSLVRVKNGRVKKGDKILV--KSTGKVHQVDSVGVFTPKHTETVDLKAGEVGFIIAGIKDIHGAPVGDTLT 278
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRIlpNGTGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
12-181 |
1.21e-08 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 57.75 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 12 IIA---HIDHGKSTLadrfIQMCGGL-SDREMEaqvldsmdlERERGITIkahSVTLHYKAQ-DGKTyqLNFIDTPGHVD 86
Cdd:PRK10512 2 IIAtagHVDHGKTTL----LQAITGVnADRLPE---------EKKRGMTI---DLGYAYWPQpDGRV--LGFIDVPGHEK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 87 FtyeVSRSLAACEG---ALLVVDAGQGVEAQSVAncYTAIEQ-----GLEVmpVLNKMDLpqAEPER---VKEEIESII- 154
Cdd:PRK10512 64 F---LSNMLAGVGGidhALLVVACDDGVMAQTRE--HLAILQltgnpMLTV--ALTKADR--VDEARiaeVRRQVKAVLr 134
|
170 180
....*....|....*....|....*....
gi 15595964 155 --GIDATDAVACSAKSGMGVLEVLERLVT 181
Cdd:PRK10512 135 eyGFAEAKLFVTAATEGRGIDALREHLLQ 163
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
9-226 |
1.70e-08 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 56.77 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 9 NFSIIAHIDHGKSTL--ADRFIQMCGGLSdremEAQVLDSMDL---ERERGITIK-AH----SVTLHYKaqdgktyqlnF 78
Cdd:PRK12735 14 NVGTIGHVDHGKTTLtaAITKVLAKKGGG----EAKAYDQIDNapeEKARGITINtSHveyeTANRHYA----------H 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 79 IDTPGHVDFTYEVSRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGLEVMPV-LNKMDLPQAEP--ERVKEEIESII- 154
Cdd:PRK12735 80 VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVfLNKCDMVDDEEllELVEMEVRELLs 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 155 -----GiDATDAVACSAKSGM----------GVLEVLERLVTAIPAPEGEIEAPLQALIIDSWFDNYLGVVSLVRVKNGR 219
Cdd:PRK12735 160 kydfpG-DDTPIIRGSALKALegdddeeweaKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGI 238
|
....*..
gi 15595964 220 VKKGDKI 226
Cdd:PRK12735 239 VKVGDEV 245
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
19-177 |
2.13e-08 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 56.60 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 19 GKSTLADRFIQmcgglSDRemeAQVLDsmdlerERGITIKAHSVTLHYkaqDGKTYQLnfIDTPG-----HVDFT---YE 90
Cdd:PRK00093 185 GKSSLINALLG-----EER---VIVSD------IAGTTRDSIDTPFER---DGQKYTL--IDTAGirrkgKVTEGvekYS 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 91 VSRSLAACEGA---LLVVDAGQGVEAQ--SVANcyTAIEQGLEVMPVLNKMDL-PQAEPERVKEEIESIIG-IDATDAVA 163
Cdd:PRK00093 246 VIRTLKAIERAdvvLLVIDATEGITEQdlRIAG--LALEAGRALVIVVNKWDLvDEKTMEEFKKELRRRLPfLDYAPIVF 323
|
170
....*....|....
gi 15595964 164 CSAKSGMGVLEVLE 177
Cdd:PRK00093 324 ISALTGQGVDKLLE 337
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
6-226 |
3.52e-08 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 55.97 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 6 HIrNFSIIAHIDHGKSTL--AdrfIQMCggLSDREM-EAQVLDSMDL---ERERGITIK-AH----SVTLHYkAQdgkty 74
Cdd:PRK00049 12 HV-NVGTIGHVDHGKTTLtaA---ITKV--LAKKGGaEAKAYDQIDKapeEKARGITINtAHveyeTEKRHY-AH----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 75 qlnfIDTPGHVDFTYEVSRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGLEVMPV-LNKMDLPQAEP--ERVKEEIE 151
Cdd:PRK00049 80 ----VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVfLNKCDMVDDEEllELVEMEVR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 152 SII------GiDATDAVACSAKSGM----------GVLEVLERLVTAIPAPEGEIEAPLQALIIDSWFDNYLGVVSLVRV 215
Cdd:PRK00049 156 ELLskydfpG-DDTPIIRGSALKALegdddeewekKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRV 234
|
250
....*....|.
gi 15595964 216 KNGRVKKGDKI 226
Cdd:PRK00049 235 ERGIIKVGEEV 245
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
16-240 |
6.13e-08 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 55.71 E-value: 6.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 16 IDHGKSTLADRFIQMCGGLSDREMEAQVLDS---------MDL---------ERERGITIkahSVTLHYKAqdgkTYQLN 77
Cdd:PRK05506 33 VDDGKSTLIGRLLYDSKMIFEDQLAALERDSkkvgtqgdeIDLallvdglaaEREQGITI---DVAYRYFA----TPKRK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 78 FI--DTPGHVDFTYEVSRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGLE--VMPVlNKMDL---PQAEPERVKEEI 150
Cdd:PRK05506 106 FIvaDTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRhvVLAV-NKMDLvdyDQEVFDEIVADY 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 151 ESI---IGIDATDAVACSAKSGMGV---------------LEVLERLVTAIPAPEGEIEAPLQALI---IDswFDNYLGV 209
Cdd:PRK05506 185 RAFaakLGLHDVTFIPISALKGDNVvtrsarmpwyegpslLEHLETVEIASDRNLKDFRFPVQYVNrpnLD--FRGFAGT 262
|
250 260 270
....*....|....*....|....*....|.
gi 15595964 210 VSlvrvkNGRVKKGDKILVKSTGKVHQVDSV 240
Cdd:PRK05506 263 VA-----SGVVRPGDEVVVLPSGKTSRVKRI 288
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
41-243 |
7.46e-08 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 54.92 E-value: 7.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 41 AQVLDSMDLERERGITIkahSVTLHYKAQDGKtyqlNFI--DTPGHVDFTYEVSRSLAACEGALLVVDAGQGVEAQSVAN 118
Cdd:PRK05124 79 ALLVDGLQAEREQGITI---DVAYRYFSTEKR----KFIiaDTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRH 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 119 CYTAIEQGLE--VMPVlNKMDL---PQAEPERVKEE----IESIIGIDATDAVACSAKSGMGV---------------LE 174
Cdd:PRK05124 152 SFIATLLGIKhlVVAV-NKMDLvdySEEVFERIREDyltfAEQLPGNLDIRFVPLSALEGDNVvsqsesmpwysgptlLE 230
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15595964 175 VLERLVTAIPAPEGEIEAPLQALI---IDswFDNYLGVVSlvrvkNGRVKKGDKILVKSTGKVHQVDSVGVF 243
Cdd:PRK05124 231 VLETVDIQRVVDAQPFRFPVQYVNrpnLD--FRGYAGTLA-----SGVVKVGDRVKVLPSGKESNVARIVTF 295
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
194-278 |
8.88e-08 |
|
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: 49.57 E-value: 8.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 194 LQALIIDSWFDNYLGVVSLVRVKNGRVKKGDKILVKSTGKVHQVDSVGVFtpkHTETVDLKAGE-VGFIIAGIKDIHgap 272
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERF---HEEVDEAKAGDiVGIGILGVKDIL--- 74
|
....*.
gi 15595964 273 VGDTLT 278
Cdd:cd01342 75 TGDTLT 80
|
|
| EFG_mtEFG_C |
cd03713 |
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational ... |
404-480 |
9.00e-08 |
|
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational elongation factor (EF) EF-G. Included in this group is the C-terminus of mitochondrial Elongation factor G1 (mtEFG1) and G2 (mtEFG2) proteins. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. In bacteria this translocation step is catalyzed by EF-G_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. No clear phenotype has been found for mutants in the yeast homologue of mtEFG2, MEF2.
Pssm-ID: 239683 [Multi-domain] Cd Length: 78 Bit Score: 49.45 E-value: 9.00e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15595964 404 EPICRATILVPKDHLGNVITLCIEKRGVQRDMHFLSGQVQVVYDLPMNEvVLDFFDRLKSTSRGYASLDYSFDRFEP 480
Cdd:cd03713 1 EPIMKVEVTVPEEYMGDVIGDLSSRRGQILGTESRGGWKVIKAEVPLAE-MFGYSTDLRSLTQGRGSFTMEFSHYEE 76
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
6-226 |
9.51e-08 |
|
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: 54.39 E-value: 9.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 6 HIrNFSIIAHIDHGKSTL--AdrfIQMCggLSDREM-EAQVLDSMDL---ERERGITIK-AH----SVTLHYkAQdgkty 74
Cdd:COG0050 12 HV-NIGTIGHVDHGKTTLtaA---ITKV--LAKKGGaKAKAYDQIDKapeEKERGITINtSHveyeTEKRHY-AH----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 75 qlnfIDTPGHVDFTYEVSRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGLEVMPV-LNKMDLPQAEP--ERVKEEIE 151
Cdd:COG0050 80 ----VDCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKCDMVDDEEllELVEMEVR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 152 ---SIIGIDATDA--VACSAKSGM----------GVLEVLERLVTAIPAPEGEIEAPLQALIIDSWFDNYLGVVSLVRVK 216
Cdd:COG0050 156 ellSKYGFPGDDTpiIRGSALKALegdpdpewekKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVE 235
|
250
....*....|
gi 15595964 217 NGRVKKGDKI 226
Cdd:COG0050 236 RGIIKVGDEV 245
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
70-177 |
1.02e-07 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 54.64 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 70 DGKTYQLnfIDTPG-----HVDFT---YEVSRSLAA---CEGALLVVDAGQGVEAQ--SVANcyTAIEQGLEVMPVLNKM 136
Cdd:COG1160 221 DGKKYTL--IDTAGirrkgKVDEGiekYSVLRTLRAierADVVLLVIDATEGITEQdlKIAG--LALEAGKALVIVVNKW 296
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 15595964 137 DL---PQAEPERVKEEIESIIG-IDATDAVACSAKSGMGVLEVLE 177
Cdd:COG1160 297 DLvekDRKTREELEKEIRRRLPfLDYAPIVFISALTGQGVDKLLE 341
|
|
| EFG_III |
cd16262 |
Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial ... |
304-371 |
4.18e-07 |
|
Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial Elongation factor G (EF-G), and mitochondrial Elongation factor G1 (mtEFG1) and G2 (mtEFG2), which play an important role during peptide synthesis and tRNA site changes. In bacteria, this translocation step is catalyzed by EF-G_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. mtEFG1 and mtEFG2 show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects, and a tendency to lose mitochondrial DNA. No clear phenotype has been found for mutants of the yeast homolog of mtEFG2, MEF2.
Pssm-ID: 293919 [Multi-domain] Cd Length: 76 Bit Score: 47.45 E-value: 4.18e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 304 PVSSDDFEDFRDALQKLTLNDSSLQYE--PESSEALGFGfrcgfLGMLHMEIIQERLEREYDLDLITTAP 371
Cdd:cd16262 11 PKTKADEDKLSKALARLAEEDPTLRVSrdEETGQTILSG-----MGELHLEIIVERLKREYGVEVEVGKP 75
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
6-138 |
4.66e-07 |
|
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: 50.66 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 6 HIrNFSIIAHIDHGKSTLADRfIQMCggLSDREMEAQV----LDSMDLERERGITIKAHSV-----TLHYKAqdgktyql 76
Cdd:cd01884 2 HV-NVGTIGHVDHGKTTLTAA-ITKV--LAKKGGAKAKkydeIDKAPEEKARGITINTAHVeyetaNRHYAH-------- 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15595964 77 nfIDTPGHVDFTYEVSRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGLEVMPV-LNKMDL 138
Cdd:cd01884 70 --VDCPGHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVfLNKADM 130
|
|
| EFG_III |
pfam14492 |
Elongation Factor G, domain III; This domain is found in Elongation Factor G. It shares a ... |
295-368 |
5.64e-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: 47.09 E-value: 5.64e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15595964 295 KPQVYAGLFPVSSDDFEDFRDALQKLTLNDSSLQYE--PESSEALGFGfrcgfLGMLHMEIIQERLEREYDLDLIT 368
Cdd:pfam14492 3 EPVISVAIEPKTKGDEDKLSKALNRLLEEDPTLRVErdEETGETILSG-----MGELHLEIVVDRLKRKYGVEVEL 73
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
194-289 |
8.12e-07 |
|
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios and is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion. The domain II of BipA shows similarity to the domain II of the elongation factors (EFs) EF-G and EF-Tu.
Pssm-ID: 293892 [Multi-domain] Cd Length: 94 Bit Score: 47.57 E-value: 8.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 194 LQALIIDSWFDNYLGVVSLVRVKNGRVKKGDKI-LVKSTGKVHQVDSVGVFTPKHTETVDLKAGEVGFI--IAGIKDIHg 270
Cdd:cd03691 1 FQMLVTTLDYDDYLGRIAIGRIFSGTVKVGQQVtVVDEDGKIEKGRVTKLFGFEGLERVEVEEAEAGDIvaIAGLEDIT- 79
|
90 100
....*....|....*....|
gi 15595964 271 apVGDTLTlnnTPDV-EVLP 289
Cdd:cd03691 80 --IGDTIC---DPEVpEPLP 94
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
9-256 |
1.58e-06 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 50.62 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 9 NFSIIAHIDHGKSTLADrfiQMCGGLSDREMEaqvldsmdlERERGITIK------------------AHSVTLHYKAQD 70
Cdd:PRK04000 11 NIGMVGHVDHGKTTLVQ---ALTGVWTDRHSE---------ELKRGITIRlgyadatirkcpdceepeAYTTEPKCPNCG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 71 GKTYQL---NFIDTPGHvdftyEV------SRSlAACEGALLVVDAGQGV-EAQSVANcYTAieqgLEVMP------VLN 134
Cdd:PRK04000 79 SETELLrrvSFVDAPGH-----ETlmatmlSGA-ALMDGAILVIAANEPCpQPQTKEH-LMA----LDIIGikniviVQN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 135 KMDLpqAEPERVKE---EIESII-GIDATDA--VACSAKSGMGVLEVLERLVTAIPAPEGEIEAPLQALIIDSwFD---- 204
Cdd:PRK04000 148 KIDL--VSKERALEnyeQIKEFVkGTVAENApiIPVSALHKVNIDALIEAIEEEIPTPERDLDKPPRMYVARS-FDvnkp 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15595964 205 ----NYL--GVV--SLVRvknGRVKKGDKI------LVKSTGKVHqvdsvgvFTPKHTETVDLKAG 256
Cdd:PRK04000 225 gtppEKLkgGVIggSLIQ---GVLKVGDEIeirpgiKVEEGGKTK-------WEPITTKIVSLRAG 280
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
74-190 |
6.60e-06 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 48.06 E-value: 6.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 74 YQLNFIDTPG-H----------VDFtyeVSRSLAACEGALLVVDAGQGV--EAQSVANcyTAIEQGLEVMPVLNKMDLpq 140
Cdd:COG1159 51 AQIVFVDTPGiHkpkrklgrrmNKA---AWSALEDVDVILFVVDATEKIgeGDEFILE--LLKKLKTPVILVINKIDL-- 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 15595964 141 AEPERVKEEIESIIG-IDATDAVACSAKSGMGVLEVLERLVTAIPA-----PEGEI 190
Cdd:COG1159 124 VKKEELLPLLAEYSElLDFAEIVPISALKGDNVDELLDEIAKLLPEgppyyPEDQI 179
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
74-189 |
2.56e-05 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 46.19 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 74 YQLNFIDTPG-H----------VDFtyeVSRSLAACEGALLVVDAGQGV--EAQSVANcyTAIEQGLEVMPVLNKMDLpQ 140
Cdd:PRK00089 53 AQIIFVDTPGiHkpkralnramNKA---AWSSLKDVDLVLFVVDADEKIgpGDEFILE--KLKKVKTPVILVLNKIDL-V 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 15595964 141 AEPERVKEEIESI-IGIDATDAVACSAKSGMGVLEVLERLVTAipAPEGE 189
Cdd:PRK00089 127 KDKEELLPLLEELsELMDFAEIVPISALKGDNVDELLDVIAKY--LPEGP 174
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
9-255 |
3.32e-05 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 46.54 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 9 NFSIIAHIDHGKSTLAD--------RFIQmcgglsdremeaqvldsmdlERERGITIK------------AHSVTLHYKA 68
Cdd:PTZ00327 36 NIGTIGHVAHGKSTVVKalsgvktvRFKR--------------------EKVRNITIKlgyanakiykcpKCPRPTCYQS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 69 QD------------GKTYQL----NFIDTPGHvDFTYEVSRSLAAC-EGALLVVDAGQGVEAQSVANCYTAIE-QGLEVM 130
Cdd:PTZ00327 96 YGsskpdnppcpgcGHKMTLkrhvSFVDCPGH-DILMATMLNGAAVmDAALLLIAANESCPQPQTSEHLAAVEiMKLKHI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 131 PVL-NKMDL-PQAEPERVKEEIESII-GIDATDA--VACSAKSGMGVLEVLERLVTAIPAPEGEIEAPLQALIIDSwFD- 204
Cdd:PTZ00327 175 IILqNKIDLvKEAQAQDQYEEIRNFVkGTIADNApiIPISAQLKYNIDVVLEYICTQIPIPKRDLTSPPRMIVIRS-FDv 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15595964 205 --------NYLGVVSLVRVKNGRVKKGDKILVKStGKVHQvDSVGVFT--PKHTETVDLKA 255
Cdd:PTZ00327 254 nkpgedieNLKGGVAGGSILQGVLKVGDEIEIRP-GIISK-DSGGEFTcrPIRTRIVSLFA 312
|
|
| Rab |
cd00154 |
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ... |
19-181 |
4.93e-05 |
|
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: 43.98 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 19 GKSTLADRFiqmCGGLSDREMEAQVldsmdlererGITIKAHSVTLhykaqDGKTYQLNFIDTPGHvdftyEVSRSLAA- 97
Cdd:cd00154 12 GKTSLLLRF---VDNKFSENYKSTI----------GVDFKSKTIEV-----DGKKVKLQIWDTAGQ-----ERFRSITSs 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 98 ----CEGALLVVDAGQgveAQSVANCYT----AIEQGLEVMPVL---NKMDLpqaEPERV--KEEIESIIGIDATDAVAC 164
Cdd:cd00154 69 yyrgAHGAILVYDVTN---RESFENLDKwlneLKEYAPPNIPIIlvgNKSDL---EDERQvsTEEAQQFAKENGLLFFET 142
|
170
....*....|....*..
gi 15595964 165 SAKSGMGVLEVLERLVT 181
Cdd:cd00154 143 SAKTGENVDEAFESLAR 159
|
|
| MnmE |
COG0486 |
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
91-194 |
4.96e-05 |
|
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: 46.21 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 91 VSRSLAACEGA---LLVVDAGQGVEAQSVAncYTAIEQGLEVMPVLNKMDLPQAEPERVKEeiesiigIDATDAVACSAK 167
Cdd:COG0486 283 IERAREAIEEAdlvLLLLDASEPLTEEDEE--ILEKLKDKPVIVVLNKIDLPSEADGELKS-------LPGEPVIAISAK 353
|
90 100
....*....|....*....|....*..
gi 15595964 168 SGMGVLEVLERLVTAIPAPEGEIEAPL 194
Cdd:COG0486 354 TGEGIDELKEAILELVGEGALEGEGVL 380
|
|
| MnmE_helical |
pfam12631 |
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ... |
91-194 |
1.58e-04 |
|
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: 44.01 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 91 VSRSLAACEGA---LLVVDAGQGVEaQSVANCYTAIEQGLEVMPVLNKMDLPQAEPERVKEEIESIIGIdatdavacSAK 167
Cdd:pfam12631 164 IERAREAIEEAdlvLLVLDASRPLD-EEDLEILELLKDKKPIIVVLNKSDLLGEIDELEELKGKPVLAI--------SAK 234
|
90 100
....*....|....*....|....*..
gi 15595964 168 SGMGVLEVLERLVTAIPAPEGEIEAPL 194
Cdd:pfam12631 235 TGEGLDELEEAIKELFLAGEIASDGPI 261
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
91-180 |
3.38e-04 |
|
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.
Pssm-ID: 206727 [Multi-domain] Cd Length: 159 Bit Score: 41.33 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 91 VSRSLAACEGA---LLVVDAGQGVEAQSVANcyTAIEQGLEVMPVLNKMDLPQAEPERVKEEIESIIGIdatdavacSAK 167
Cdd:cd04164 73 IERAREAIEEAdlvLLVVDASEGLDEEDLEI--LELPAKKPVIVVLNKSDLLSDAEGISELNGKPIIAI--------SAK 142
|
90
....*....|...
gi 15595964 168 SGMGVLEVLERLV 180
Cdd:cd04164 143 TGEGIDELKEALL 155
|
|
| Ras |
pfam00071 |
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ... |
19-184 |
3.58e-04 |
|
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop motif with GTP_EFTU, arf and myosin_head. See pfam00009 pfam00025, pfam00063. As regards Rab GTPases, these are important regulators of vesicle formation, motility and fusion. They share a fold in common with all Ras GTPases: this is a six-stranded beta-sheet surrounded by five alpha-helices.
Pssm-ID: 425451 [Multi-domain] Cd Length: 162 Bit Score: 41.35 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 19 GKSTLADRFIQmcgglsdremeaqvlDSMDLERERGITIKAHSVTLHYkaqDGKTYQLNFIDTPGHVDFtyevsRSLA-- 96
Cdd:pfam00071 11 GKSSLLIRFTQ---------------NKFPEEYIPTIGVDFYTKTIEV---DGKTVKLQIWDTAGQERF-----RALRpl 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 97 ---ACEGALLVVDAgqgVEAQSVANCYTAIEQGLEV----MPVL---NKMDLpqaEPERV--KEEIESI---IGIdatDA 161
Cdd:pfam00071 68 yyrGADGFLLVYDI---TSRDSFENVKKWVEEILRHadenVPIVlvgNKCDL---EDQRVvsTEEGEALakeLGL---PF 138
|
170 180
....*....|....*....|...
gi 15595964 162 VACSAKSGMGVLEVLERLVTAIP 184
Cdd:pfam00071 139 METSAKTNENVEEAFEELAREIL 161
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|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
72-180 |
4.20e-04 |
|
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.
Pssm-ID: 206726 [Multi-domain] Cd Length: 168 Bit Score: 41.29 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 72 KTYQLNFIDTPG-HVDFT-------YEVSRSLAACEGALLVVDAGQGV--EAQSVANCYtaIEQGLEVMPVLNKMDLpQA 141
Cdd:cd04163 49 DDAQIIFVDTPGiHKPKKklgermvKAAWSALKDVDLVLFVVDASEWIgeGDEFILELL--KKSKTPVILVLNKIDL-VK 125
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15595964 142 EPERVKEEIESI-IGIDATDAVACSAKSGMGVLEVLERLV 180
Cdd:cd04163 126 DKEDLLPLLEKLkELHPFAEIFPISALKGENVDELLEYIV 165
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|
| EFG_mtEFG_II |
cd04088 |
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation ... |
204-278 |
9.11e-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: 9.11e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15595964 204 DNYLGVVSLVRVKNGRVKKGDKILVKSTGKVHQVDSVGVFTPKHTETVD-LKAGEVGfIIAGIKDIHgapVGDTLT 278
Cdd:cd04088 11 DPFVGKLTFFRVYSGTLKSGSTVYNSTKGKKERVGRLLRMHGKKREEVEeLGAGDIG-AVVGLKDTR---TGDTLC 82
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|
| Arf_Arl |
cd00878 |
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ... |
127-180 |
1.65e-03 |
|
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl (Arf-like) small GTPases. Arf proteins are activators of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. Arfs are N-terminally myristoylated. Members of the Arf family are regulators of vesicle formation in intracellular traffic that interact reversibly with membranes of the secretory and endocytic compartments in a GTP-dependent manner. They depart from other small GTP-binding proteins by a unique structural device, interswitch toggle, that implements front-back communication from N-terminus to the nucleotide binding site. Arf-like (Arl) proteins are close relatives of the Arf, but only Arl1 has been shown to function in membrane traffic like the Arf proteins. Arl2 has an unrelated function in the folding of native tubulin, and Arl4 may function in the nucleus. Most other Arf family proteins are so far relatively poorly characterized. Thus, despite their significant sequence homologies, Arf family proteins may regulate unrelated functions.
Pssm-ID: 206644 [Multi-domain] Cd Length: 158 Bit Score: 39.48 E-value: 1.65e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15595964 127 LEVMPVL---NKMDLPQAEPErvkEEIESIIGIDATD-----AVACSAKSGMGVLEVLERLV 180
Cdd:cd00878 98 LKGAPLLilaNKQDLPGALTE---SELIELLGLESIKgrrwhIQPCSAVTGDGLDEGLDWLI 156
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|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
124-179 |
4.43e-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: 38.92 E-value: 4.43e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 15595964 124 EQGLEVMPVLNKMDLpqAEPERVKEEIESIIGIDAtDAVACSAKSGMGVLEVLERL 179
Cdd:cd01854 31 ASGIEPVIVLNKADL--VDDEELEELLEIYEKLGY-PVLAVSAKTGEGLDELRELL 83
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
124-179 |
6.65e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 37.91 E-value: 6.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 15595964 124 EQGLEVMPVLNKMDLPqAEPERVKEEIESIIGIDaTDAVACSAKSGMGVLEVLERL 179
Cdd:pfam03193 51 ASGIEPVIVLNKIDLL-DEEEELEELLKIYRAIG-YPVLFVSAKTGEGIEALKELL 104
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
11-116 |
8.58e-03 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 39.01 E-value: 8.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595964 11 SIIAHIDHGKSTLADRfiqmcgglsdremeaqVLDSMDLERERG-IT--IKAHSV---TLHYKAQDGKTYQ--------L 76
Cdd:PRK04004 10 VVLGHVDHGKTTLLDK----------------IRGTAVAAKEAGgITqhIGATEVpidVIEKIAGPLKKPLpiklkipgL 73
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15595964 77 NFIDTPGHVDFTYEVSRSLAACEGALLVVDAGQGVEAQSV 116
Cdd:PRK04004 74 LFIDTPGHEAFTNLRKRGGALADIAILVVDINEGFQPQTI 113
|
|
| BipA_TypA_C |
cd03710 |
BipA_TypA_C: a C-terminal portion of BipA or TypA having homology to the C terminal domains of ... |
404-480 |
9.65e-03 |
|
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: 35.56 E-value: 9.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15595964 404 EPICRATILVPKDHLGNVITLCIEKRGVQRDMHFLS-GQVQVVYDLPmNEVVLDFFDRLKSTSRGYASLDYSFDRFEP 480
Cdd:cd03710 1 EPIEELTIDVPEEYSGAVIEKLGKRKGEMVDMEPDGnGRTRLEFKIP-SRGLIGFRSEFLTDTRGTGIMNHVFDGYEP 77
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