|
Name |
Accession |
Description |
Interval |
E-value |
| PrfC |
COG4108 |
Peptide chain release factor RF-3 [Translation, ribosomal structure and biogenesis]; Peptide ... |
5-533 |
0e+00 |
|
Peptide chain release factor RF-3 [Translation, ribosomal structure and biogenesis]; Peptide chain release factor RF-3 is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 443284 [Multi-domain] Cd Length: 528 Bit Score: 989.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 5 SKISQEVARRRTFAIISHPDAGKTTLTEKLLLFAGAIQIAGSVKARKAERHASSDWMEIEKQRGISVASSVMQMEYRDCV 84
Cdd:COG4108 1 SELAEEIARRRTFAIISHPDAGKTTLTEKLLLFGGAIQLAGAVKARKARRHATSDWMEIEKQRGISVTSSVMQFEYRGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 85 INLLDTPGHQDFSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILTFINKLDREVREPLELIGEIESHLE 164
Cdd:COG4108 81 INLLDTPGHEDFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDREGRDPLELLDEIEEVLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 165 MDCIPFTWPVGMGRQFSGIYDLTKDQMRMFNRANPSKSGsaEDEFIPDLSNPLLTERCPDTI-GKAREEIELIQLATPDF 243
Cdd:COG4108 161 IDCAPMTWPIGMGKDFKGVYDRYTDEVHLFERGAGGATE--APEEIEGLDDPELDELLGEDLaEQLREEIELLDGAGPEF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 244 DHAAFLDAKQTPVFFGSAVYNFGVQELLDALVEYAPPPGAREAIERTIEPSEPKFTGVVFKVQANMDPAHRDRVAFVRVS 323
Cdd:COG4108 239 DLEAFLAGELTPVFFGSALNNFGVRELLDAFVELAPPPRPREADEREVEPTEEKFSGFVFKIQANMDPAHRDRIAFMRIC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 324 SGKFERGMRLRVARTGKDIRPNNPVSFLSQRRDLVDEAYAGDVIGIPNHGVLHLGDVLTEGEKLHFTGLPFFAPELFQTV 403
Cdd:COG4108 319 SGKFERGMKVKHVRTGKKIRLSNPQQFFAQDRETVEEAYPGDIIGLHNHGTLRIGDTLTEGEKLEFTGIPSFAPELFRRV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 404 EVKDPLRSKQLHTGLTQLGEEGAIQVFKPQIaGGTLLLGAVGQLQFEVVAHRLKTEYGVDAILGPSRYNLARWVTSSNPQ 483
Cdd:COG4108 399 RLKDPMKAKQLRKGLEQLAEEGAVQVFRPLD-GNDPILGAVGQLQFEVVQYRLKNEYGVEVRLEPLPYSTARWVTADDPK 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 738649027 484 ALRKFLDANISNIAYDVVDAPAFLVSSQAQLRVAQELHPDIQFHVMREQG 533
Cdd:COG4108 478 DLEEFKRKNRSNLAKDRDGRPVFLFPSEWNLRYAQERNPDIKFHATREHA 527
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
5-531 |
0e+00 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 962.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 5 SKISQEVARRRTFAIISHPDAGKTTLTEKLLLFAGAIQIAGSVKARKAERHASSDWMEIEKQRGISVASSVMQMEYRDCV 84
Cdd:PRK00741 1 SELAQEVAKRRTFAIISHPDAGKTTLTEKLLLFGGAIQEAGTVKGRKSGRHATSDWMEMEKQRGISVTSSVMQFPYRDCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 85 INLLDTPGHQDFSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILTFINKLDREVREPLELIGEIESHLE 164
Cdd:PRK00741 81 INLLDTPGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTRKLMEVCRLRDTPIFTFINKLDRDGREPLELLDEIEEVLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 165 MDCIPFTWPVGMGRQFSGIYDLTKDQMRMFNRANPSKSGsaEDEFIPDLSNPLLTERCP-DTIGKAREEIELIQLATPDF 243
Cdd:PRK00741 161 IACAPITWPIGMGKRFKGVYDLYNDEVELYQPGEGHTIQ--EVEIIKGLDNPELDELLGeDLAEQLREELELVQGASNEF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 244 DHAAFLDAKQTPVFFGSAVYNFGVQELLDALVEYAPPPGAREAIERTIEPSEPKFTGVVFKVQANMDPAHRDRVAFVRVS 323
Cdd:PRK00741 239 DLEAFLAGELTPVFFGSALNNFGVQEFLDAFVEWAPAPQPRQTDEREVEPTEEKFSGFVFKIQANMDPKHRDRIAFVRVC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 324 SGKFERGMRLRVARTGKDIRPNNPVSFLSQRRDLVDEAYAGDVIGIPNHGVLHLGDVLTEGEKLHFTGLPFFAPELFQTV 403
Cdd:PRK00741 319 SGKFEKGMKVRHVRTGKDVRISNALTFMAQDREHVEEAYAGDIIGLHNHGTIQIGDTFTQGEKLKFTGIPNFAPELFRRV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 404 EVKDPLRSKQLHTGLTQLGEEGAIQVFKPQIaGGTLLLGAVGQLQFEVVAHRLKTEYGVDAILGPSRYNLARWVTSSNPQ 483
Cdd:PRK00741 399 RLKNPLKQKQLQKGLVQLSEEGAVQVFRPLD-NNDLILGAVGQLQFEVVAHRLKNEYNVEAIYEPVGVATARWVECDDAK 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 738649027 484 ALRKFLDANISNIAYDVVDAPAFLVSSQAQLRVAQELHPDIQFHVMRE 531
Cdd:PRK00741 478 KLEEFKRKNRSNLAKDGGDNLVYLAPNEVNLRLAQERYPDVKFHATRE 525
|
|
| prfC |
TIGR00503 |
peptide chain release factor 3; This translation releasing factor, RF-3 (prfC) was originally ... |
9-531 |
0e+00 |
|
peptide chain release factor 3; This translation releasing factor, RF-3 (prfC) was originally described as stop codon-independent, in contrast to peptide chain release factor 1 (RF-1, prfA) and RF-2 (prfB). RF-1 and RF-2 are closely related to each other, while RF-3 is similar to elongation factors EF-Tu and EF-G; RF-1 is active at UAA and UAG and RF-2 is active at UAA and UGA. More recently, RF-3 was shown to be active primarily at UGA stop codons in E. coli. All bacteria and organelles have RF-1. The Mycoplasmas and organelles, which translate UGA as Trp rather than as a stop codon, lack RF-2. RF-3, in contrast, seems to be rare among bacteria and is found so far only in Escherichia coli and some other gamma subdivision Proteobacteria, in Synechocystis PCC6803, and in Staphylococcus aureus. [Protein synthesis, Translation factors]
Pssm-ID: 129594 [Multi-domain] Cd Length: 527 Bit Score: 661.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 9 QEVARRRTFAIISHPDAGKTTLTEKLLLFAGAIQIAGSVKARKAERHASSDWMEIEKQRGISVASSVMQMEYRDCVINLL 88
Cdd:TIGR00503 6 KEVDKRRTFAIISHPDAGKTTITEKVLLYGGAIQTAGAVKGRGSQRHAKSDWMEMEKQRGISITTSVMQFPYRDCLVNLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 89 DTPGHQDFSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILTFINKLDREVREPLELIGEIESHLEMDCI 168
Cdd:TIGR00503 86 DTPGHEDFSEDTYRTLTAVDNCLMVIDAAKGVETRTRKLMEVTRLRDTPIFTFMNKLDRDIRDPLELLDEVENELKINCA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 169 PFTWPVGMGRQFSGIYDLTKDQMRMFNRANPSKSGSAedEFIPDLSNPLLTERC-PDTIGKAREEIELIQLATPDFDHAA 247
Cdd:TIGR00503 166 PITWPIGCGKLFKGVYHLLKDETYLYQSGTGGTIQAV--RQVKGLNNPALDSAVgSDLAQQLRDELELVEGASNEFDLAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 248 FLDAKQTPVFFGSAVYNFGVQELLDALVEYAPPPGAREAIERTIEPSEPKFTGVVFKVQANMDPAHRDRVAFVRVSSGKF 327
Cdd:TIGR00503 244 FHGGEMTPVFFGTALGNFGVDHFLDGLLQWAPKPEARQSDTRTVEPTEEKFSGFVFKIQANMDPKHRDRVAFMRVVSGKY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 328 ERGMRLRVARTGKDIRPNNPVSFLSQRRDLVDEAYAGDVIGIPNHGVLHLGDVLTEGEKLHFTGLPFFAPELFQTVEVKD 407
Cdd:TIGR00503 324 EKGMKLKHVRTGKDVVISDALTFMAGDREHVEEAYAGDIIGLHNHGTIQIGDTFTQGEKIKFTGIPNFAPELFRRIRLKD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 408 PLRSKQLHTGLTQLGEEGAIQVFKPqIAGGTLLLGAVGQLQFEVVAHRLKTEYGVDAILGPSRYNLARWVTSSNPQALRK 487
Cdd:TIGR00503 404 PLKQKQLLKGLVQLSEEGAVQVFRP-LDNNDLIVGAVGVLQFDVVVYRLKEEYNVEARYEPVNVATARWVECADWKKFEE 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 738649027 488 FLDANISNIAYDVVDAPAFLVSSQAQLRVAQELHPDIQFHVMRE 531
Cdd:TIGR00503 483 FKRKNETVLALDGGDNLVYIAKNMVNLELAQERYPDVKFSATRE 526
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
13-281 |
9.02e-169 |
|
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: 478.24 E-value: 9.02e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 13 RRRTFAIISHPDAGKTTLTEKLLLFAGAIQIAGSVKARKAERHASSDWMEIEKQRGISVASSVMQMEYRDCVINLLDTPG 92
Cdd:cd04169 1 RRRTFAIISHPDAGKTTLTEKLLLFGGAIQEAGAVKARKSRKHATSDWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 93 HQDFSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILTFINKLDREVREPLELIGEIESHLEMDCIPFTW 172
Cdd:cd04169 81 HEDFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDREGRDPLELLDEIENELGIDCAPMTW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 173 PVGMGRQFSGIYDLTKDQMRMFNRanPSKSGSAEDEFIPDLSNPLLTERC-PDTIGKAREEIELIQLATPDFDHAAFLDA 251
Cdd:cd04169 161 PIGMGKDFKGVYDRYDKEIYLYER--GAGGAIKAPEETKGLDDPKLDELLgEDLAEQLREELELVEGAGPEFDKELFLAG 238
|
250 260 270
....*....|....*....|....*....|
gi 738649027 252 KQTPVFFGSAVYNFGVQELLDALVEYAPPP 281
Cdd:cd04169 239 ELTPVFFGSALNNFGVQELLDAFVKLAPAP 268
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
15-468 |
1.72e-96 |
|
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: 307.74 E-value: 1.72e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 15 RTFAIISHPDAGKTTLTEKLLLFAGAIQIAGSVKARKAErhasSDWMEIEKQRGISVASSVMQMEYRDCVINLLDTPGHQ 94
Cdd:COG0480 10 RNIGIVAHIDAGKTTLTERILFYTGAIHRIGEVHDGNTV----MDWMPEEQERGITITSAATTCEWKGHKINIIDTPGHV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 95 DFSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILTFINKLDREVREPLELIGEIESHLEMDCIPFTWPV 174
Cdd:COG0480 86 DFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQLKERLGANPVPLQLPI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 175 GMGRQFSGIYDLTKDQMRMFNRANPSKSgsaEDEFIPdlsnplltERCPDTIGKAREE-IEliQLAtpDFD--------- 244
Cdd:COG0480 166 GAEDDFKGVIDLVTMKAYVYDDELGAKY---EEEEIP--------AELKEEAEEAREElIE--AVA--ETDdelmekyle 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 245 -------------HAAFLDAKQTPVFFGSAVYNFGVQELLDALVEYAPPPGAREAI-----------ERTIEPSEPkFTG 300
Cdd:COG0480 231 geelteeeikaglRKATLAGKIVPVLCGSAFKNKGVQPLLDAVVDYLPSPLDVPAIkgvdpdtgeevERKPDDDEP-FSA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 301 VVFKVQAnmDPaHRDRVAFVRVSSGKFERGMRLRVARTGKDIRPNNPVSFLSQRRDLVDEAYAGDVIGIPNHGVLHLGDV 380
Cdd:COG0480 310 LVFKTMT--DP-FVGKLSFFRVYSGTLKSGSTVYNSTKGKKERIGRLLRMHGNKREEVDEAGAGDIVAVVKLKDTTTGDT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 381 LT-EGEKLHFTGLPFFAPELFQTVEVKDplRSKQ--LHTGLTQLGEE-GAIQVFKPQIAGGTLLLGaVGQLQFEVVAHRL 456
Cdd:COG0480 387 LCdEDHPIVLEPIEFPEPVISVAIEPKT--KADEdkLSTALAKLAEEdPTFRVETDEETGQTIISG-MGELHLEIIVDRL 463
|
490
....*....|..
gi 738649027 457 KTEYGVDAILGP 468
Cdd:COG0480 464 KREFGVEVNVGK 475
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
20-468 |
3.47e-88 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 285.10 E-value: 3.47e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 20 ISHPDAGKTTLTEKLLLFAGAIQIAGSVKarkaERHASSDWMEIEKQRGISVASSVMQMEYRDCVINLLDTPGHQDFSED 99
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRIGEVE----DGTTTMDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 100 TYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILTFINKLDREVREPLELIGEIESHLEMDCIPFTWPVGMGRQ 179
Cdd:PRK12740 77 VERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRAGADFFRVLAQLQEKLGAPVVPLQLPIGEGDD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 180 FSGIYDLTKDQMRMFNranpsKSGSAEDEFIPDlsnpLLTERcpdtIGKAREE-IEliQLAtpDFD-------------- 244
Cdd:PRK12740 157 FTGVVDLLSMKAYRYD-----EGGPSEEIEIPA----ELLDR----AEEAREElLE--ALA--EFDdelmekylegeels 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 245 --------HAAFLDAKQTPVFFGSAVYNFGVQELLDALVEYAPPP---------GAREAIERTIEPSEPkFTGVVFKVQa 307
Cdd:PRK12740 220 eeeikaglRKATLAGEIVPVFCGSALKNKGVQRLLDAVVDYLPSPlevppvdgeDGEEGAELAPDPDGP-LVALVFKTM- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 308 nMDPaHRDRVAFVRVSSGKFERGMRLRVARTGKDIRPNNPVSFLSQRRDLVDEAYAGDVIGIPNHGVLHLGDVLT-EGEK 386
Cdd:PRK12740 298 -DDP-FVGKLSLVRVYSGTLKKGDTLYNSGTGKKERVGRLYRMHGKQREEVDEAVAGDIVAVAKLKDAATGDTLCdKGDP 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 387 LHFTGLPFFAPELFQTVEVKDPLRSKQLHTGLTQLGEEG-AIQVFKpQIAGGTLLLGAVGQLQFEVVAHRLKTEYGVDAI 465
Cdd:PRK12740 376 ILLEPMEFPEPVISLAIEPKDKGDEEKLSEALGKLAEEDpTLRVER-DEETGQTILSGMGELHLDVALERLKREYGVEVE 454
|
...
gi 738649027 466 LGP 468
Cdd:PRK12740 455 TGP 457
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
15-470 |
1.74e-76 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 254.88 E-value: 1.74e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 15 RTFAIISHPDAGKTTLTEKLLLFAGAIQIAGSVKARKAErhasSDWMEIEKQRGISVASSVMQMEYRDCVINLLDTPGHQ 94
Cdd:PRK13351 9 RNIGILAHIDAGKTTLTERILFYTGKIHKMGEVEDGTTV----TDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 95 DFSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILTFINKLDREVREPLELIGEIESHLEMDCIPFTWPV 174
Cdd:PRK13351 85 DFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLFKVLEDIEERFGKRPLPLQLPI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 175 GMGRQFSGIYDLTKDQMRMFNRANP--------------SKSGSAEDEFIPDLSN--PLLTERCpdtigKAREEIeliql 238
Cdd:PRK13351 165 GSEDGFEGVVDLITEPELHFSEGDGgstveegpipeellEEVEEAREKLIEALAEfdDELLELY-----LEGEEL----- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 239 aTPDFDHAAFLDAKQT----PVFFGSAVYNFGVQELLDALVEYAPPP----------GAREAIERTIEPSEPkFTGVVFK 304
Cdd:PRK13351 235 -SAEQLRAPLREGTRSghlvPVLFGSALKNIGIEPLLDAVVDYLPSPlevppprgskDNGKPVKVDPDPEKP-LLALVFK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 305 VQAnmDPAHRdRVAFVRVSSGKFERGMRLRVARTGKDIRPNNPVSFLSQRRDLVDEAYAGDVIGIPNHGVLHLGDVLTE- 383
Cdd:PRK13351 313 VQY--DPYAG-KLTYLRVYSGTLRAGSQLYNGTGGKREKVGRLFRLQGNKREEVDRAKAGDIVAVAGLKELETGDTLHDs 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 384 GEKLHFTGLPFFAPELFQTVEvkdPLRSK---QLHTGLTQLGEEG-AIQVFKPQIAGGTLLLGaVGQLQFEVVAHRLKTE 459
Cdd:PRK13351 390 ADPVLLELLTFPEPVVSLAVE---PERRGdeqKLAEALEKLVWEDpSLRVEEDEETGQTILSG-MGELHLEVALERLRRE 465
|
490
....*....|.
gi 738649027 460 YGVDAILGPSR 470
Cdd:PRK13351 466 FKLEVNTGKPQ 476
|
|
| EF-G |
TIGR00484 |
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ... |
11-467 |
5.46e-65 |
|
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: 223.92 E-value: 5.46e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 11 VARRRTFAIISHPDAGKTTLTEKLLLFAGAIQIAGSVKarkaERHASSDWMEIEKQRGISVASSVMQMEYRDCVINLLDT 90
Cdd:TIGR00484 7 LNRFRNIGISAHIDAGKTTTTERILFYTGRIHKIGEVH----DGAATMDWMEQEKERGITITSAATTVFWKGHRINIIDT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 91 PGHQDFSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILTFINKLDREVREPLELIGEIESHLEMDCIPF 170
Cdd:TIGR00484 83 PGHVDFTVEVERSLRVLDGAVAVLDAVGGVQPQSETVWRQANRYEVPRIAFVNKMDKTGANFLRVVNQIKQRLGANAVPI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 171 TWPVGMGRQFSGIYDLTKDQMRMFnraNPSKSGSAEDEFIPD--------LSNPLLTERC-------PDTIGKAREEIEL 235
Cdd:TIGR00484 163 QLPIGAEDNFIGVIDLVEMKAYFF---NGDKGTKAIEKEIPSdlleqakeLRENLVEAVAefdeelmEKYLEGEELTIEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 236 IQLATpdfdHAAFLDAKQTPVFFGSAVYNFGVQELLDALVEYAPPP-----------GAREAIERTIEPSEPkFTGVVFK 304
Cdd:TIGR00484 240 IKNAI----RKGVLNCEFFPVLCGSAFKNKGVQLLLDAVVDYLPSPtdvpaikgidpDTEKEIERKASDDEP-FSALAFK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 305 VqanMDPAHRDRVAFVRVSSGKFERGMRLRVARTGKDIRPNNPVSFLSQRRDLVDEAYAGDVIGIPNHGVLHLGDVLT-E 383
Cdd:TIGR00484 315 V---ATDPFVGQLTFVRVYSGVLKSGSYVKNSRKNKKERVGRLVKMHANNREEIKEVRAGDICAAIGLKDTTTGDTLCdP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 384 GEKLHFTGLPFFAPELFQTVEVKDPLRSKQLHTGLTQLGEEG-AIQVFKPQIAGGTLLLGaVGQLQFEVVAHRLKTEYGV 462
Cdd:TIGR00484 392 KIDVILERMEFPEPVISLAVEPKTKADQEKMGIALGKLAEEDpTFRTFTDPETGQTIIAG-MGELHLDIIVDRMKREFKV 470
|
....*
gi 738649027 463 DAILG 467
Cdd:TIGR00484 471 EANVG 475
|
|
| RF3_C |
pfam16658 |
Class II release factor RF3, C-terminal domain; |
389-517 |
1.69e-61 |
|
Class II release factor RF3, C-terminal domain;
Pssm-ID: 465221 [Multi-domain] Cd Length: 129 Bit Score: 198.05 E-value: 1.69e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 389 FTGLPFFAPELFQTVEVKDPLRSKQLHTGLTQLGEEGAIQVFKPQIAGGTLLLGAVGQLQFEVVAHRLKTEYGVDAILGP 468
Cdd:pfam16658 1 FTGIPSFAPEHFARVRLKDPMKRKQFRKGLEQLAEEGAIQVFRPDNRGEDPILGAVGQLQFEVVQYRLKNEYGVDVRLEP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 738649027 469 SRYNLARWVTSSNPQALRKFLDANISNIAYDVVDAPAFLVSSQAQLRVA 517
Cdd:pfam16658 81 LPYSTARWVESDDAKALDEFKRASGSNLAKDRDGRPVLLFRNEWNLRYA 129
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
13-280 |
7.98e-58 |
|
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: 190.81 E-value: 7.98e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 13 RRRTFAIISHPDAGKTTLTEKLLLFAGAIQIAGSVKArkaERHASSDWMEIEKQRGISVASSVMQMEYRDCVINLLDTPG 92
Cdd:pfam00009 2 RHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKG---EGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 93 HQDFSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILTFINKLDREVREPLELIgeieshlemdcipftw 172
Cdd:pfam00009 79 HVDFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDGAELEEV---------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 173 pvgmgrqfsgiydltKDQMrmfnranpsksgsaEDEFIpdlsnplltercpdtigkareeieliqlatpdfdHAAFLDAK 252
Cdd:pfam00009 143 ---------------VEEV--------------SRELL----------------------------------EKYGEDGE 159
|
250 260
....*....|....*....|....*...
gi 738649027 253 QTPVFFGSAVYNFGVQELLDALVEYAPP 280
Cdd:pfam00009 160 FVPVVPGSALKGEGVQTLLDALDEYLPS 187
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
16-281 |
5.02e-57 |
|
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: 191.65 E-value: 5.02e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 16 TFAIISHPDAGKTTLTEKLLLFAGAIQIAGSVKARKAerhaSSDWMEIEKQRGISVASSVMQMEYRDCVINLLDTPGHQD 95
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRLGRVEDGNT----VSDYDPEEKKRKMSIETSVAPLEWNGHKINLIDTPGYAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 96 FSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILTFINKLDREvREPL-ELIGEIESHLEMDCIPFTWPV 174
Cdd:cd04170 77 FVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRA-RADFdKTLAALREAFGRPVVPIQLPI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 175 GMGRQFSGIYDLTKDQMRMFNranpSKSGSAEDEFIPDLsnplltercPDTIGKAREEIeLIQLAtpDFD---------- 244
Cdd:cd04170 156 GEGDEFTGVVDLLSEKAYRYD----PGEPSVEIEIPEEL---------KEKVAEAREEL-LEAVA--ETDeelmekylee 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 738649027 245 ------------HAAFLDAKQTPVFFGSAVYNFGVQELLDALVEYAPPP 281
Cdd:cd04170 220 gelteeelraglRRALRAGLIVPVFFGSALTGIGVRRLLDALVELAPSP 268
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
19-281 |
9.64e-53 |
|
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: 180.38 E-value: 9.64e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 19 IISHPDAGKTTLTEKLLLFAGAIQIAGSVKarkaERHASSDWMEIEKQRGISVASSVMQMEYRDCVINLLDTPGHQDFSE 98
Cdd:cd01886 4 IIAHIDAGKTTTTERILYYTGRIHKIGEVH----GGGATMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDFTI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 99 DTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILTFINKLDREVREPLELIGEIESHLEMDCIPFTWPVGMGR 178
Cdd:cd01886 80 EVERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQIREKLGANPVPLQLPIGAED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 179 QFSGIYDLTKDQMRMFNRANPSKsgsAEDEFIPDLSNPLLTER---CPDTIGKAREEIELIQLA----TPDFDHAAF--- 248
Cdd:cd01886 160 DFEGVVDLIEMKALYWDGELGEK---IEETDIPEDLLEEAEEAreeLIETLAEVDDELMEKYLEgeeiTEEEIKAAIrkg 236
|
250 260 270
....*....|....*....|....*....|....
gi 738649027 249 -LDAKQTPVFFGSAVYNFGVQELLDALVEYAPPP 281
Cdd:cd01886 237 tIANKIVPVLCGSAFKNKGVQPLLDAVVDYLPSP 270
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
16-281 |
1.33e-49 |
|
GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function.
Pssm-ID: 206647 [Multi-domain] Cd Length: 183 Bit Score: 169.01 E-value: 1.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 16 TFAIISHPDAGKTTLTEKLLLFAGAIQIAGSVKARKaerhasSDWMEIEKQRGISVASSVMQMEYRDCVINLLDTPGHQD 95
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETF------LDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 96 FSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILTFINKLDRevrepleligeieshlemdcipftwpVG 175
Cdd:cd00881 75 FSKETVRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDR--------------------------VG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 176 MGRqfsgiYDLTKDQMrmfnranpsksgsaedefipdlsnplltercpdtigkaREEIELIqlatpdfdHAAFLDAKQTP 255
Cdd:cd00881 129 EED-----FDEVLREI--------------------------------------KELLKLI--------GFTFLKGKDVP 157
|
250 260
....*....|....*....|....*.
gi 738649027 256 VFFGSAVYNFGVQELLDALVEYAPPP 281
Cdd:cd00881 158 IIPISALTGEGIEELLDAIVEHLPPP 183
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
19-281 |
9.34e-47 |
|
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: 163.18 E-value: 9.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 19 IISHPDAGKTTLTEKLLLFAGAIQIAGSVKarkaERHASSDWMEIEKQRGISVASSVMQMEYRDCVINLLDTPGHQDFSE 98
Cdd:cd04168 4 ILAHVDAGKTTLTESLLYTSGAIRELGSVD----KGTTRTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 99 DTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILTFINKLDREVREPLELIGEIESHLEMDCIPFTWPVgmgr 178
Cdd:cd04168 80 EVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTIIFVNKIDRAGADLEKVYQEIKEKLSPDIVPMQKVG---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 179 qfsgiydlTKDQMRMFNranpsKSGSAEDEFIPDLSNPLLT----ERCPDTIGKAREEIELIQlatpdfdhaaflDAKQT 254
Cdd:cd04168 156 --------LYPNICDTN-----NIDDEQIETVAEGNDELLEkylsGGPLEELELDNELSARIQ------------KASLF 210
|
250 260
....*....|....*....|....*..
gi 738649027 255 PVFFGSAVYNFGVQELLDALVEYAPPP 281
Cdd:cd04168 211 PVYHGSALKGIGIDELLEGITNLFPTS 237
|
|
| RF3_II |
cd03689 |
Domain II of bacterial Release Factor 3; This subfamily represents domain II of bacterial ... |
298-384 |
2.71e-46 |
|
Domain II of bacterial Release Factor 3; This subfamily represents domain II of bacterial Release Factor 3 (RF3). Termination of protein synthesis by the ribosome requires two release factor (RF) classes. The class II RF3 is a GTPase that removes class I RFs (RF1 or RF2) from the ribosome after release of the nascent polypeptide. RF3 in the GDP state binds to the ribosomal class I RF complex, followed by an exchange of GDP for GTP and release of the class I RF. Sequence comparison of class II release factors with elongation factors shows that prokaryotic RF3 is more similar to EF-G whereas eukaryotic eRF3 is more similar to eEF1A, implying that their precise function may differ.
Pssm-ID: 293890 [Multi-domain] Cd Length: 87 Bit Score: 156.66 E-value: 2.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 298 FTGVVFKVQANMDPAHRDRVAFVRVSSGKFERGMRLRVARTGKDIRPNNPVSFLSQRRDLVDEAYAGDVIGIPNHGVLHL 377
Cdd:cd03689 1 FSGFVFKIQANMDPKHRDRIAFLRVCSGKFERGMKVKHVRTGKEVRLSNATTFMAQDRETVEEAYPGDIIGLPNHGTFQI 80
|
....*..
gi 738649027 378 GDVLTEG 384
Cdd:cd03689 81 GDTFTEG 87
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
6-468 |
1.40e-36 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 144.62 E-value: 1.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 6 KISQEVARRRTFAIISHPDAGKTTLTEKLLLFAGAI--QIAGSVKARkaerhassDWMEIEKQRGISV-ASSV-MQMEY- 80
Cdd:PRK07560 12 ELMKNPEQIRNIGIIAHIDHGKTTLSDNLLAGAGMIseELAGEQLAL--------DFDEEEQARGITIkAANVsMVHEYe 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 81 -RDCVINLLDTPGHQDFSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVC-RARNTPILtFINKLDRevrepleLIGE 158
Cdd:PRK07560 84 gKEYLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQAlRERVKPVL-FINKVDR-------LIKE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 159 IEshlemdcipftwpvgmgrqfsgiydLTKDQMRmfnranpsksgsaedefipdlsnplltERCPDTIGKAREEIELiqL 238
Cdd:PRK07560 156 LK-------------------------LTPQEMQ---------------------------QRLLKIIKDVNKLIKG--M 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 239 ATPDFDHAAFLDAKQTPVFFGSAVYNFGV------------------------QEL----------LDALVEYAPPPgaR 284
Cdd:PRK07560 182 APEEFKEKWKVDVEDGTVAFGSALYNWAIsvpmmqktgikfkdiidyyekgkqKELaekaplhevvLDMVVKHLPNP--I 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 285 EAIERTI-------------------EPSEPkftgVVFKVQA-NMDPaHRDRVAFVRVSSGKFERGMRLRVARTGKDIRP 344
Cdd:PRK07560 260 EAQKYRIpkiwkgdlnsevgkamlncDPNGP----LVMMVTDiIVDP-HAGEVATGRVFSGTLRKGQEVYLVGAKKKNRV 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 345 NNPVSFLSQRRDLVDEAYAGDVIgipnhGVLHLGD------VLTEGEKLHFTGLPFFA-PELFQTVEVKDPLRSKQLHTG 417
Cdd:PRK07560 335 QQVGIYMGPEREEVEEIPAGNIA-----AVTGLKDaragetVVSVEDMTPFESLKHISePVVTVAIEAKNPKDLPKLIEV 409
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 738649027 418 LTQLG-EEGAIQVFKPQIAGGTLLLGaVGQLQFEVVAHRLKTEYGVDAILGP 468
Cdd:PRK07560 410 LRQLAkEDPTLVVKINEETGEHLLSG-MGELHLEVITYRIKRDYGIEVVTSE 460
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
15-468 |
1.14e-30 |
|
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: 126.94 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 15 RTFAIISHPDAGKTTLTEKLLlfAGAiqiaGSVKARKAERHASSDWMEIEKQRGISV----ASSVMQMEYRDCVINLLDT 90
Cdd:TIGR00490 20 RNIGIVAHIDHGKTTLSDNLL--AGA----GMISEELAGQQLYLDFDEQEQERGITInaanVSMVHEYEGNEYLINLIDT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 91 PGHQDFSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLK-VCRARNTPILtFINKLDRevrepleLIGEIEshlemdcip 169
Cdd:TIGR00490 94 PGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRqALKENVKPVL-FINKVDR-------LINELK--------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 170 ftwpvgmgrqfsgiydLTKDQMRmfnranpsksgsaedefipdlsnplltERCPDTIGKAReeiELIQLATPD-FDHAAF 248
Cdd:TIGR00490 157 ----------------LTPQELQ---------------------------ERFIKIITEVN---KLIKAMAPEeFRDKWK 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 249 LDAKQTPVFFGSAVYNFGV----------------------------------QELLDALVEYAPPPGAREAiERTIEPS 294
Cdd:TIGR00490 191 VRVEDGSVAFGSAYYNWAIsvpsmkktgigfkdiykyckedkqkelakksplhQVVLDMVIRHLPSPIEAQK-YRIPVIW 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 295 EPKFTGVVFKVQANMDP--------------AHRDRVAFVRVSSGKFERGMRLRVARTGKDIRPNNPVSFLSQRRDLVDE 360
Cdd:TIGR00490 270 KGDLNSEVGKAMLNCDPkgplalmitkivvdKHAGEVAVGRLYSGTIRPGMEVYIVDRKAKARIQQVGVYMGPERVEVDE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 361 AYAGDVIGIPNHGVLHLGDVL-TEGEKLH-FTGLPFFA-PELFQTVEVKDPLRSKQLHTGLTQLGEEGAIQVFKPQIAGG 437
Cdd:TIGR00490 350 IPAGNIVAVIGLKDAVAGETIcTTVENITpFESIKHISePVVTVAIEAKNTKDLPKLIEVLRQVAKEDPTVHVEINEETG 429
|
490 500 510
....*....|....*....|....*....|.
gi 738649027 438 TLLLGAVGQLQFEVVAHRLKTEYGVDAILGP 468
Cdd:TIGR00490 430 EHLISGMGELHLEIIVEKIREDYGLDVETSP 460
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
15-159 |
9.36e-30 |
|
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: 115.77 E-value: 9.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 15 RTFAIISHPDAGKTTLTEKLLLFAGAIQIAGSVkarkAERhaSSDWMEIEKQRGISVASSVMQMEYRDCVINLLDTPGHQ 94
Cdd:cd01891 3 RNIAIIAHVDHGKTTLVDALLKQSGTFRENEEV----GER--VMDSNDLERERGITILAKNTAITYKDTKINIIDTPGHA 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738649027 95 DFSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILTFINKLDREVREPLELIGEI 159
Cdd:cd01891 77 DFGGEVERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDRPDARPEEVVDEV 141
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
15-155 |
1.05e-29 |
|
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: 116.18 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 15 RTFAIISHPDAGKTTLTEKLLLFAGAI--QIAGSVKArkaerhasSDWMEIEKQRGISVASSVMQMEYR---------DC 83
Cdd:cd01885 1 RNICIIAHVDHGKTTLSDSLLASAGIIseKLAGKARY--------LDTREDEQERGITIKSSAISLYFEyeeekmdgnDY 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738649027 84 VINLLDTPGHQDFSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKV-CRARNTPILtFINKLDREVRE----PLEL 155
Cdd:cd01885 73 LINLIDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQaLEERVKPVL-VINKIDRLILElklsPEEA 148
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
15-167 |
2.40e-29 |
|
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: 113.78 E-value: 2.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 15 RTFAIISHPDAGKTTLTEKLLlfagaiQIAGSVKARKAeRHASSDWMEIEKQRGISVASSVMQMEYR-----DCVINLLD 89
Cdd:cd01890 1 RNFSIIAHIDHGKSTLADRLL------ELTGTVSEREM-KEQVLDSMDLERERGITIKAQAVRLFYKakdgeEYLLNLID 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 90 TPGHQDFSEDTYRVLTAVDAAVMVVDAANGIEPQTerlLKVCRA---RNTPILTFINKLDREVREPLELIGEIESHLEMD 166
Cdd:cd01890 74 TPGHVDFSYEVSRSLAACEGALLVVDATQGVEAQT---LANFYLaleNNLEIIPVINKIDLPAADPDRVKQEIEDVLGLD 150
|
.
gi 738649027 167 C 167
Cdd:cd01890 151 A 151
|
|
| RF3_III |
cd16259 |
Domain III of bacterial Release Factor 3 (RF3); The class II RF3 is a member of one of two ... |
397-466 |
2.59e-29 |
|
Domain III of bacterial Release Factor 3 (RF3); The class II RF3 is a member of one of two release factor (RF) classes required for the termination of protein synthesis by the ribosome. RF3 is a GTPase that removes class I RFs (RF1 or RF2) from the ribosome after release of the nascent polypeptide. RF3 in the GDP state binds to the ribosomal class I RF complex, followed by an exchange of GDP for GTP and release of the class I RF. Sequence comparison of class II release factors with elongation factors shows that prokaryotic RF3 is more similar to EF-G whereas eukaryotic eRF3 is more similar to eEF1A, implying that their precise function may differ.
Pssm-ID: 293916 [Multi-domain] Cd Length: 70 Bit Score: 110.04 E-value: 2.59e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 397 PELFQTVEVKDPLRSKQLHTGLTQLGEEGAIQVFKPQIaGGTLLLGAVGQLQFEVVAHRLKTEYGVDAIL 466
Cdd:cd16259 1 PEHFRRVRLKDPMKAKQLRKGLEQLAEEGAVQVFRPMD-GSDPIVGAVGPLQFEVLQARLENEYGVEVVF 69
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
15-408 |
2.30e-28 |
|
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, a GTP-binding protein, is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways, but the precise function is unknown. [Regulatory functions, Other, Cellular processes, Adaptations to atypical conditions, Protein synthesis, Translation factors]
Pssm-ID: 273597 [Multi-domain] Cd Length: 594 Bit Score: 119.33 E-value: 2.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 15 RTFAIISHPDAGKTTLTEKLLLFAGAIQIAGSVkarkAERHASSDwmEIEKQRGISVASSVMQMEYRDCVINLLDTPGHQ 94
Cdd:TIGR01394 2 RNIAIIAHVDHGKTTLVDALLKQSGTFRANEAV----AERVMDSN--DLERERGITILAKNTAIRYNGTKINIVDTPGHA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 95 DFSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILTFINKLDREVREPLELIGEIeshlemdcipftwpv 174
Cdd:TIGR01394 76 DFGGEVERVLGMVDGVLLLVDASEGPMPQTRFVLKKALELGLKPIVVINKIDRPSARPDEVVDEV--------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 175 gmgrqFSGIYDL--TKDQMrmfnranpsksgsaedEFipdlsnplltercPDTIGKAREEIeliqlatpdfdhaAFLDAK 252
Cdd:TIGR01394 141 -----FDLFAELgaDDEQL----------------DF-------------PIVYASGRAGW-------------ASLDLD 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 253 QTPVFFGsavynfgvqELLDALVEYAPPPgareaierTIEPSEPkFTGVVFKVQANmdpAHRDRVAFVRVSSGKFERGMR 332
Cdd:TIGR01394 174 DPSDNMA---------PLFDAIVRHVPAP--------KGDLDEP-LQMLVTNLDYD---EYLGRIAIGRVHRGTVKKGQQ 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 333 LRVAR---TGKDIRPNNPVSFLSQRRDLVDEAYAGD---VIGIPNHGVlhlGDVLTEGEklhftglpffAPELFQTVEVK 406
Cdd:TIGR01394 233 VALMKrdgTIENGRISKLLGFEGLERVEIDEAGAGDivaVAGLEDINI---GETIADPE----------VPEALPTITVD 299
|
..
gi 738649027 407 DP 408
Cdd:TIGR01394 300 EP 301
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
15-382 |
1.28e-24 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 107.80 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 15 RTFAIISHPDAGKTTLTEKLLLFAGAIQIAGSVkarkAERhaSSDWMEIEKQRGISVAS---SVMqmeYRDCVINLLDTP 91
Cdd:COG1217 7 RNIAIIAHVDHGKTTLVDALLKQSGTFRENQEV----AER--VMDSNDLERERGITILAkntAVR---YKGVKINIVDTP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 92 GHQDFSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILTFINKLDREVREPLELIGEieshlemdcipft 171
Cdd:COG1217 78 GHADFGGEVERVLSMVDGVLLLVDAFEGPMPQTRFVLKKALELGLKPIVVINKIDRPDARPDEVVDE------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 172 wpvgmgrqfsgIYDLtkdqmrmfnranpsksgsaedeFIpDLSnplltercpdtigkAREEieliQLatpDFdhaaflda 251
Cdd:COG1217 145 -----------VFDL----------------------FI-ELG--------------ATDE----QL---DF-------- 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 252 kqtPVFFGS-----AVYNFGVQE-----LLDALVEYAPPPgareaierTIEPSEPkftgvvFKVQ-ANMDpaHRD---RV 317
Cdd:COG1217 162 ---PVVYASarngwASLDLDDPGedltpLFDTILEHVPAP--------EVDPDGP------LQMLvTNLD--YSDyvgRI 222
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738649027 318 AFVRVSSGKFERGMRLRVARTGKDIRPNNPVSFLS----QRRDlVDEAYAGDVI---GIPNhgvLHLGDVLT 382
Cdd:COG1217 223 AIGRIFRGTIKKGQQVALIKRDGKVEKGKITKLFGfeglERVE-VEEAEAGDIVaiaGIED---INIGDTIC 290
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
15-366 |
7.10e-24 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 105.49 E-value: 7.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 15 RTFAIISHPDAGKTTLTEKLLLFAGAIqiagsvkarkAERHASS---DWMEIEKQRGISVASSVMQMEYR-----DCVIN 86
Cdd:COG0481 7 RNFSIIAHIDHGKSTLADRLLELTGTL----------SEREMKEqvlDSMDLERERGITIKAQAVRLNYKakdgeTYQLN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 87 LLDTPGHQDFSedtYRV---LTAVDAAVMVVDAANGIEPQT--------ERLLKvcrarntpILTFINKLDREVREPLEL 155
Cdd:COG0481 77 LIDTPGHVDFS---YEVsrsLAACEGALLVVDASQGVEAQTlanvylalENDLE--------IIPVINKIDLPSADPERV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 156 IGEIEshlemdcipftwpvgmgrqfsgiydltkdqmrmfnranpsksgsaedefipdlsnplltercpDTIGKAREEIEL 235
Cdd:COG0481 146 KQEIE---------------------------------------------------------------DIIGIDASDAIL 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 236 IqlatpdfdhaafldakqtpvffgSAVYNFGVQELLDALVEYAPPPgareaierTIEPSEP-----------KFTGVvfk 304
Cdd:COG0481 163 V-----------------------SAKTGIGIEEILEAIVERIPPP--------KGDPDAPlqalifdswydSYRGV--- 208
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738649027 305 vqanmdpahrdrVAFVRVSSGKFERGMRLRVARTGKDIRPNNpVSFLSQRRDLVDEAYAGDV 366
Cdd:COG0481 209 ------------VVYVRVFDGTLKKGDKIKMMSTGKEYEVDE-VGVFTPKMTPVDELSAGEV 257
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
15-175 |
2.35e-23 |
|
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: 98.11 E-value: 2.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 15 RTFAIISHPDAGKTTLTEKLLLFAGAiQIAGSVKARKAERHasSDWMEIEKQRGISVASSVMQM-----EYRDCVINLLD 89
Cdd:cd04167 1 RNVCIAGHLHHGKTSLLDMLIEQTHK-RTPSVKLGWKPLRY--TDTRKDEQERGISIKSNPISLvledsKGKSYLINIID 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 90 TPGHQDFSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILTFINKLDREVRE----PLE-------LIGE 158
Cdd:cd04167 78 TPGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDRLILElklpPTDayyklrhTIDE 157
|
170
....*....|....*..
gi 738649027 159 IESHLEMDCIPFTWPVG 175
Cdd:cd04167 158 INNYIASFSTTEGFLVS 174
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
15-191 |
1.02e-21 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 99.01 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 15 RTFAIISHPDAGKTTLTEKLLlfagaiQIAGSVKARKAERHASSDWMEIEKQRGISVASSVMQMEYRDCVINLLDTPGHQ 94
Cdd:PRK10218 6 RNIAIIAHVDHGKTTLVDKLL------QQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 95 DFSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILTFINKLDREVREP---LELIGEIESHLEMDCIPFT 171
Cdd:PRK10218 80 DFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPdwvVDQVFDLFVNLDATDEQLD 159
|
170 180
....*....|....*....|
gi 738649027 172 WPVGMGRQFSGIYDLTKDQM 191
Cdd:PRK10218 160 FPIVYASALNGIAGLDHEDM 179
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
15-158 |
1.80e-21 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 98.58 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 15 RTFAIISHPDAGKTTLTEKLLLFAGAIQIAGSVKARkaerhaSSDWMEIEKQRGISVASSVMQMEY----------RDCV 84
Cdd:PTZ00416 20 RNMSVIAHVDHGKSTLTDSLVCKAGIISSKNAGDAR------FTDTRADEQERGITIKSTGISLYYehdledgddkQPFL 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738649027 85 INLLDTPGHQDFSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLK-VCRARNTPILtFINKLDREVREpLELIGE 158
Cdd:PTZ00416 94 INLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRqALQERIRPVL-FINKVDRAILE-LQLDPE 166
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
15-158 |
1.78e-17 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 85.93 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 15 RTFAIISHPDAGKTTLTEKLLLFAGAI--QIAGSVKArkaerhasSDWMEIEKQRGISVASSVMQMEY------------ 80
Cdd:PLN00116 20 RNMSVIAHVDHGKSTLTDSLVAAAGIIaqEVAGDVRM--------TDTRADEAERGITIKSTGISLYYemtdeslkdfkg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 81 -RDC---VINLLDTPGHQDFSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRA-RNTPILTfINKLDREVREpLEL 155
Cdd:PLN00116 92 eRDGneyLINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTETVLRQALGeRIRPVLT-VNKMDRCFLE-LQV 169
|
...
gi 738649027 156 IGE 158
Cdd:PLN00116 170 DGE 172
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
18-146 |
2.31e-17 |
|
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: 79.34 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 18 AIISHPDAGKTTLTEKLLLFAGAIQIAGSvkarKAERHassDWMEIEKQRGISvassvmqmeyrdCVINLLDTPGHQDFS 97
Cdd:TIGR00231 5 VIVGHPNVGKSTLLNSLLGNKGSITEYYP----GTTRN---YVTTVIEEDGKT------------YKFNLLDTAGQEDYD 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 738649027 98 ED-------TYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRArNTPILTFINKLD 146
Cdd:TIGR00231 66 AIrrlyypqVERSLRVFDIVILVLDVEEILEKQTKEIIHHADS-GVPIILVGNKID 120
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
18-184 |
1.41e-15 |
|
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: 74.43 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 18 AIISHPDAGKTTLTEKLllfagaiqiagsVKARKAERHAssdwmeiekqRGI--SVASSVMQMEYRDCVINLLDTPGHQD 95
Cdd:cd01887 4 TVMGHVDHGKTTLLDKI------------RKTNVAAGEA----------GGItqHIGAYQVPIDVKIPGITFIDTPGHEA 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 96 FSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILTFINKLDRE--VREPLELIGEIEShlEMDCIPFTWp 173
Cdd:cd01887 62 FTNMRARGASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKPygTEADPERVKNELS--ELGLVGEEW- 138
|
170
....*....|.
gi 738649027 174 vgmGRQFSGIY 184
Cdd:cd01887 139 ---GGDVSIVP 146
|
|
| EFG_III-like |
cd16257 |
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G ... |
397-467 |
3.85e-15 |
|
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G (EF-G) and related proteins play a role in translation and share a similar domain architecture. Elongation factor EFG participates in the elongation phase during protein biosynthesis on the ribosome by stimulating translocation. Its functional cycles depend on GTP binding and its hydrolysis. Domain III is involved in the activation of GTP hydrolysis. This domain III, which is different from domain III in EF-TU and related elongation factors, is found in several translation factors, like bacterial release factors RF3, elongation factor 4, elongation factor 2, GTP-binding protein BipA and tetracycline resistance protein Tet.
Pssm-ID: 293914 [Multi-domain] Cd Length: 71 Bit Score: 70.07 E-value: 3.85e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738649027 397 PELFQTVEVKDPLRSKQLHTGLTQLGEEGAIQVFKPQIAGGTLLLGAVGQLQFEVVAHRLKTEYGVDAILG 467
Cdd:cd16257 1 PVVFVTVEVKNPLDQEKLLEGLERLSEEDPALQVYREESTGEFILSGLGELHLEIIVARLEREYGVELVVS 71
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
19-172 |
3.41e-13 |
|
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: 72.11 E-value: 3.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 19 IISHPDAGKTTLTEKLLlfagaiqiagsvKARKAERHASsdwmeiekqrGISVASSVMQMEYRD-CVINLLDTPGHQDFS 97
Cdd:TIGR00487 92 IMGHVDHGKTSLLDSIR------------KTKVAQGEAG----------GITQHIGAYHVENEDgKMITFLDTPGHEAFT 149
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738649027 98 EDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILTFINKLDREVREPLELIGEIeshLEMDCIPFTW 172
Cdd:TIGR00487 150 SMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVPIIVAINKIDKPEANPDRVKQEL---SEYGLVPEDW 221
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
17-163 |
5.06e-12 |
|
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: 68.36 E-value: 5.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 17 FAIISHPDAGKTTLTEklllfagaiQIAGSVKARKAErhassdwmeiEKQRGISVASSVMQMEYRDCVINLLDTPGHQDF 96
Cdd:TIGR00475 3 IATAGHVDHGKTTLLK---------ALTGIAADRLPE----------EKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKF 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738649027 97 SEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILT-FINKLDReVREplELIGEIESHL 163
Cdd:TIGR00475 64 ISNAIAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIvVITKADR-VNE--EEIKRTEMFM 128
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
18-148 |
2.07e-11 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 66.78 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 18 AIISHPDAGKTTLTEKlllfagaiqIAGSVKARKaerhassdwmEIEkqrGI--SVASSVMQMEYRDCVINL--LDTPGH 93
Cdd:CHL00189 248 TILGHVDHGKTTLLDK---------IRKTQIAQK----------EAG---GItqKIGAYEVEFEYKDENQKIvfLDTPGH 305
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 738649027 94 QDFSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILTFINKLDRE 148
Cdd:CHL00189 306 EAFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKA 360
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
20-160 |
1.38e-10 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 63.48 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 20 ISHPDAGKTTLTEKLLLFAGAIqiAGSVKARKAERHASSDwmeiEKQRGISVASSVMQMEYRDCVINLLDTPGHQDFSED 99
Cdd:PLN03126 87 IGHVDHGKTTLTAALTMALASM--GGSAPKKYDEIDAAPE----ERARGITINTATVEYETENRHYAHVDCPGHADYVKN 160
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738649027 100 TYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTP-ILTFINKLDR-EVREPLELIgEIE 160
Cdd:PLN03126 161 MITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPnMVVFLNKQDQvDDEELLELV-ELE 222
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
18-146 |
2.18e-10 |
|
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: 62.64 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 18 AIISHPDAGKTTLTEKLLLFAGAIQ---IAGSVKARKAERHAS------SDWMEIEKQRGISVASSVMQMEYRDCVINLL 88
Cdd:COG5256 11 VVIGHVDHGKSTLVGRLLYETGAIDehiIEKYEEEAEKKGKESfkfawvMDRLKEERERGVTIDLAHKKFETDKYYFTII 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738649027 89 DTPGHQDFSEDTYRVLTAVDAAVMVVDAANGIEPQTER---LLKVCRARNtpILTFINKLD 146
Cdd:COG5256 91 DAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREhafLARTLGINQ--LIVAVNKMD 149
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
298-382 |
4.28e-10 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 56.12 E-value: 4.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 298 FTGVVFKVQANMdpaHRDRVAFVRVSSGKFERGMRLRVARTGKDIRpnnpVSFLSQRRDLVDEAYAGDVIGIPNHGV--L 375
Cdd:cd01342 1 LVMQVFKVFYIP---GRGRVAGGRVESGTLKVGDEIRILPKGITGR----VTSIERFHEEVDEAKAGDIVGIGILGVkdI 73
|
....*..
gi 738649027 376 HLGDVLT 382
Cdd:cd01342 74 LTGDTLT 80
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
20-160 |
5.34e-10 |
|
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.
Pssm-ID: 206671 [Multi-domain] Cd Length: 195 Bit Score: 59.13 E-value: 5.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 20 ISHPDAGKTTLTeklllfaGAIQI----AGSVKARKAErhassdwmEI-----EKQRGISVASSVMQMEYRDCVINLLDT 90
Cdd:cd01884 8 IGHVDHGKTTLT-------AAITKvlakKGGAKAKKYD--------EIdkapeEKARGITINTAHVEYETANRHYAHVDC 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738649027 91 PGHQDFSEDTYRVLTAVDAAVMVVDAANGIEPQT-ERLLkVCRARNTP-ILTFINKLDrEVREP--LELIgEIE 160
Cdd:cd01884 73 PGHADYIKNMITGAAQMDGAILVVSATDGPMPQTrEHLL-LARQVGVPyIVVFLNKAD-MVDDEelLELV-EME 143
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
18-124 |
9.48e-10 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 60.71 E-value: 9.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 18 AIISHPDAGKTTLTEKLLLFAGAI--QIAGSVKARKAERHASS-------DWMEIEKQRGISVASSVMQMEYRDCVINLL 88
Cdd:PRK12317 10 AVIGHVDHGKSTLVGRLLYETGAIdeHIIEELREEAKEKGKESfkfawvmDRLKEERERGVTIDLAHKKFETDKYYFTIV 89
|
90 100 110
....*....|....*....|....*....|....*...
gi 738649027 89 DTPGHQDFSEDTYRVLTAVDAAVMVVDA--ANGIEPQT 124
Cdd:PRK12317 90 DCPGHRDFVKNMITGASQADAAVLVVAAddAGGVMPQT 127
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
22-164 |
1.44e-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 bacterial SelBs, as well as, one from archaea.
Pssm-ID: 206734 [Multi-domain] Cd Length: 170 Bit Score: 57.23 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 22 HPDAGKTTLTEKLLLFAGAiqiagsvkaRKAErhassdwmeiEKQRGISVASSVMQMEYRDC-VINLLDTPGHQDFSEDT 100
Cdd:cd04171 7 HIDHGKTTLIKALTGIETD---------RLPE----------EKKRGITIDLGFAYLDLPDGkRLGFIDVPGHEKFVKNM 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738649027 101 YRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTP-ILTFINKLDR-EVREPLELIGEIESHLE 164
Cdd:cd04171 68 LAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKkGLVVLTKADLvDEDRLELVEEEILELLA 133
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
20-160 |
1.48e-09 |
|
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: 60.18 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 20 ISHPDAGKTTLTeklllfaGAIQIAGSVKAR-KAERHASSDWMEIEKQRGISVASSVMQMEYRDCVINLLDTPGHQDFSE 98
Cdd:TIGR00485 18 IGHVDHGKTTLT-------AAITTVLAKEGGaAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHVDCPGHADYVK 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738649027 99 DTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTP-ILTFINKLDR-EVREPLELIgEIE 160
Cdd:TIGR00485 91 NMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPyIVVFLNKCDMvDDEELLELV-EME 153
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
20-160 |
2.52e-09 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 59.45 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 20 ISHPDAGKTTLTeklllfAGAIQIAGSVKARKAERHASSDWMEIEKQRGISVASSVMQMEYRDCVINLLDTPGHQDFSED 99
Cdd:PLN03127 67 IGHVDHGKTTLT------AAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVDCPGHADYVKN 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738649027 100 TYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTP-ILTFINKLDR-EVREPLELIgEIE 160
Cdd:PLN03127 141 MITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPsLVVFLNKVDVvDDEELLELV-EME 202
|
|
| EFG_mtEFG_II |
cd04088 |
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation ... |
298-383 |
8.09e-09 |
|
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: 52.52 E-value: 8.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 298 FTGVVFKVQAnmDPaHRDRVAFVRVSSGKFERGMRLRVARTGKDIRPNNPVSFLSQRRDLVDEAYAGD---VIGIPNhgv 374
Cdd:cd04088 1 FSALVFKTMA--DP-FVGKLTFFRVYSGTLKSGSTVYNSTKGKKERVGRLLRMHGKKREEVEELGAGDigaVVGLKD--- 74
|
....*....
gi 738649027 375 LHLGDVLTE 383
Cdd:cd04088 75 TRTGDTLCD 83
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
18-147 |
8.28e-09 |
|
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic orthologs of bacterial IF-2. Like IF-2, it helps convey the initiator tRNA to the ribosome, although the initiator is N-formyl-Met in bacteria and Met here. This protein is not closely related to the subunits of eIF-2 of eukaryotes, which is also involved in the initiation of translation. The aIF-2 of Methanococcus jannaschii contains a large intein interrupting a region of very strongly conserved sequence very near the amino end; the alignment generated by this model does not correctly align the sequences from Methanococcus jannaschii and Pyrococcus horikoshii in this region. [Protein synthesis, Translation factors]
Pssm-ID: 273104 [Multi-domain] Cd Length: 591 Bit Score: 58.29 E-value: 8.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 18 AIISHPDAGKTTLTEKLLLFAGAIQIAGSVKarkaeRHASSDWMEIEKQRGISvaSSVMQMEYRDCVIN---LLDTPGHQ 94
Cdd:TIGR00491 8 VVLGHVDHGKTTLLDKIRGTAVVKKEAGGIT-----QHIGASEVPTDVIEKIC--GDLLKSFKIKLKIPgllFIDTPGHE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 738649027 95 DFSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILTFINKLDR 147
Cdd:TIGR00491 81 AFTNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTPFVVAANKIDR 133
|
|
| tufA |
CHL00071 |
elongation factor Tu |
20-154 |
9.65e-09 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 57.66 E-value: 9.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 20 ISHPDAGKTTLTEKLllfAGAIQIAGSVKARKAErhassdwmEI-----EKQRGISVASSVMQME--YR-----DCvinl 87
Cdd:CHL00071 18 IGHVDHGKTTLTAAI---TMTLAAKGGAKAKKYD--------EIdsapeEKARGITINTAHVEYEteNRhyahvDC---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 88 ldtPGHQDFSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTP-ILTFINKLDR------------EVREPLE 154
Cdd:CHL00071 83 ---PGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPnIVVFLNKEDQvddeellelvelEVRELLS 159
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
18-170 |
1.15e-08 |
|
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: 54.38 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 18 AIISHPDAGKTTLTEKLLlfagaiqiaGSVKARKAERHASSDWMEIEkqrgisvassVMQMEYRDCVINLLDTPGHQDFS 97
Cdd:cd00882 1 VVVGRGGVGKSSLLNALL---------GGEVGEVSDVPGTTRDPDVY----------VKELDKGKVKLVLVDTPGLDEFG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 98 -----EDTYRVLTAVDAAVMVVDAANG--IEPQTERLLKVCRARNTPILTFINKLDR---EVREPLELIGEIESHLEMDC 167
Cdd:cd00882 62 glgreELARLLLRGADLILLVVDSTDResEEDAKLLILRRLRKEGIPIILVGNKIDLleeREVEELLRLEELAKILGVPV 141
|
...
gi 738649027 168 IPF 170
Cdd:cd00882 142 FEV 144
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
16-144 |
1.69e-08 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 52.62 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 16 TFAIISHPDAGKTTLTEKLLlfaGAIQIAgsvkarkaerhasSDWME--IEKQRGIsvassvmqMEYRDCVINLLDTPG- 92
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALT---GAKAIV-------------SDYPGttRDPNEGR--------LELKGKQIILVDTPGl 56
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 738649027 93 ----HQDFS-EDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILTFINK 144
Cdd:pfam01926 57 iegaSEGEGlGRAFLAIIEADLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
20-153 |
9.23e-08 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 54.18 E-value: 9.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 20 ISHPDAGKTTLTeklllfAGAIQIAGSVKARKAERHASSDWMEIEKQRGISVASSvmQMEYR---------DCvinlldt 90
Cdd:PRK12736 18 IGHVDHGKTTLT------AAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTA--HVEYEtekrhyahvDC------- 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738649027 91 PGHQDFSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTP-ILTFINKLDR------------EVREPL 153
Cdd:PRK12736 83 PGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPyLVVFLNKVDLvddeellelvemEVRELL 158
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
17-124 |
1.39e-07 |
|
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: 52.49 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 17 FAIISHPDAGKTTLTEKLLLFAGAI---QIAgsvKARK--AERHASS-------DWMEIEKQRGISVASSVMQMEYRDCV 84
Cdd:cd01883 2 LVVIGHVDAGKSTLTGHLLYKLGGVdkrTIE---KYEKeaKEMGKESfkyawvlDKLKEERERGVTIDVGLAKFETEKYR 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 738649027 85 INLLDTPGHQDFSEDTYRVLTAVDAAVMVVDAANG-------IEPQT 124
Cdd:cd01883 79 FTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQT 125
|
|
| Tet_II |
cd03690 |
Domain II of ribosomal protection proteins Tet(M) and Tet(O); This subfamily represents domain ... |
295-381 |
5.44e-07 |
|
Domain II of ribosomal protection proteins Tet(M) and Tet(O); This subfamily represents domain II of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology to domain II of the elongation factors EF-G and EF-2. Tet(M) and Tet(O) catalyze the release of tetracycline (Tc) from the ribosome in a GTP-dependent manner thereby mediating Tc resistance. Tcs are broad-spectrum antibiotics. Typical Tcs bind to the ribosome and inhibit the elongation phase of protein synthesis, by inhibiting the occupation of site A by aminoacyl-tRNA.
Pssm-ID: 293891 [Multi-domain] Cd Length: 86 Bit Score: 47.62 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 295 EPKFTGVVFKVQanMDPAhRDRVAFVRVSSGKFERGMRLRVARTGKDIRPNNPVSFLSQRRDLVDEAYAGDVIGIPNHGV 374
Cdd:cd03690 1 ESELSGTVFKIE--YDPK-GERLAYLRLYSGTLRLRDSVRVSGEEEKIKITELRTFENGELVKVDRVYAGDIAILVGLKS 77
|
....*..
gi 738649027 375 LHLGDVL 381
Cdd:cd03690 78 LRVGDVL 84
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
19-119 |
6.16e-07 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 52.01 E-value: 6.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 19 IISHPDAGKTTLTEKLLLFAGAI--QIAGSVKARKAERHASS-------DWMEIEKQRGISVASSVMQMEYRDCVINLLD 89
Cdd:PLN00043 12 VIGHVDSGKSTTTGHLIYKLGGIdkRVIERFEKEAAEMNKRSfkyawvlDKLKAERERGITIDIALWKFETTKYYCTVID 91
|
90 100 110
....*....|....*....|....*....|
gi 738649027 90 TPGHQDFSEDTYRVLTAVDAAVMVVDAANG 119
Cdd:PLN00043 92 APGHRDFIKNMITGTSQADCAVLIIDSTTG 121
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
17-146 |
6.23e-07 |
|
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: 50.26 E-value: 6.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 17 FAIISHPDAGKTTLTEKLL-----LFAGAI-QIAGSVKARKAERHAS----SDWMEIEKQRGIS--VASSVMQMEYRDCV 84
Cdd:cd04166 2 FITCGSVDDGKSTLIGRLLydsksIFEDQLaALERSKSSGTQGEKLDlallVDGLQAEREQGITidVAYRYFSTPKRKFI 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738649027 85 InlLDTPGHQDFSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTP-ILTFINKLD 146
Cdd:cd04166 82 I--ADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRhVVVAVNKMD 142
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
18-147 |
9.65e-07 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 51.33 E-value: 9.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 18 AIISHPDAGKTTLTEKlllfagaiqIAGS-VKARKA---ERH--ASS-DWMEIEKqrgisVASSVMQMEYRDCVI-NLL- 88
Cdd:PRK04004 10 VVLGHVDHGKTTLLDK---------IRGTaVAAKEAggiTQHigATEvPIDVIEK-----IAGPLKKPLPIKLKIpGLLf 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 89 -DTPGHQDFSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILTFINKLDR 147
Cdd:PRK04004 76 iDTPGHEAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVAANKIDR 135
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
20-160 |
1.15e-06 |
|
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: 50.92 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 20 ISHPDAGKTTLTeklllfaGAIQI----AGSVKARKAErhassdwmEI-----EKQRGISVASSvmQMEYR--------- 81
Cdd:COG0050 18 IGHVDHGKTTLT-------AAITKvlakKGGAKAKAYD--------QIdkapeEKERGITINTS--HVEYEtekrhyahv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 82 DCvinlldtPGHQDFSEDtyrVLTA---VDAAVMVVDAANGIEPQT-ERLLkVCRARNTP-ILTFINK---LDREvrEPL 153
Cdd:COG0050 81 DC-------PGHADYVKN---MITGaaqMDGAILVVSATDGPMPQTrEHIL-LARQVGVPyIVVFLNKcdmVDDE--ELL 147
|
....*..
gi 738649027 154 ELIgEIE 160
Cdd:COG0050 148 ELV-EME 153
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
20-160 |
1.17e-06 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 50.99 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 20 ISHPDAGKTTLTeklllfaGAIQIAGSVKAR-KAERHASSDWMEIEKQRGISVASSvmQMEYR---------DCvinlld 89
Cdd:PRK12735 18 IGHVDHGKTTLT-------AAITKVLAKKGGgEAKAYDQIDNAPEEKARGITINTS--HVEYEtanrhyahvDC------ 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738649027 90 tPGHQDFSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTP-ILTFINKLDReVREP--LELIgEIE 160
Cdd:PRK12735 83 -PGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPyIVVFLNKCDM-VDDEelLELV-EME 153
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
19-119 |
1.55e-06 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 50.52 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 19 IISHPDAGKTTLTEKLLLFAGAIQiagSVKARKAERHASS------------DWMEIEKQRGISVASSVMQMEYRDCVIN 86
Cdd:PTZ00141 12 VIGHVDSGKSTTTGHLIYKCGGID---KRTIEKFEKEAAEmgkgsfkyawvlDKLKAERERGITIDIALWKFETPKYYFT 88
|
90 100 110
....*....|....*....|....*....|...
gi 738649027 87 LLDTPGHQDFSEDTYRVLTAVDAAVMVVDAANG 119
Cdd:PTZ00141 89 IIDAPGHRDFIKNMITGTSQADVAILVVASTAG 121
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
20-153 |
1.71e-06 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 50.19 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 20 ISHPDAGKTTLTeklllfaGAIQIAGSVKAR-KAERHASSDWMEIEKQRGISVASSvmQMEYR---------DCvinlld 89
Cdd:PRK00049 18 IGHVDHGKTTLT-------AAITKVLAKKGGaEAKAYDQIDKAPEEKARGITINTA--HVEYEtekrhyahvDC------ 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738649027 90 tPGHQDFSEDTYRVLTAVDAAVMVVDAANGIEPQT-ERLLkVCRARNTP-ILTFINKLDR------------EVREPL 153
Cdd:PRK00049 83 -PGHADYVKNMITGAAQMDGAILVVSAADGPMPQTrEHIL-LARQVGVPyIVVFLNKCDMvddeellelvemEVRELL 158
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
88-147 |
2.32e-06 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 50.65 E-value: 2.32e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 88 LDTPGHQDFSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILTFINKLDR 147
Cdd:PRK14845 531 IDTPGHEAFTSLRKRGGSLADLAVLVVDINEGFKPQTIEAINILRQYKTPFVVAANKIDL 590
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
316-382 |
3.73e-06 |
|
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: 44.56 E-value: 3.73e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738649027 316 RVAFVRVSSGKFERGMRLRV--ARTGKDIRPNNPVS---FLSQRRDLVDEAYAGDVIGIPNHGVLHLGDVLT 382
Cdd:pfam03144 2 TVATGRVESGTLKKGDKVRIlpNGTGKKKIVTRVTSllmFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
18-166 |
1.02e-05 |
|
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: 45.92 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 18 AIISHPDAGKTTLTEKLLlfaGA-IQIAgsvkARKAE--RHASsdwmeiekqRGIsvassvmqMEYRDCVINLLDTPG-- 92
Cdd:cd04163 7 AIIGRPNVGKSTLLNALV---GQkISIV----SPKPQttRNRI---------RGI--------YTDDDAQIIFVDTPGih 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 93 ------HQDFSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILTFINKLDReVREPLELIGEIESHLEMD 166
Cdd:cd04163 63 kpkkklGERMVKAAWSALKDVDLVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDL-VKDKEDLLPLLEKLKELH 141
|
|
| EFG_III |
pfam14492 |
Elongation Factor G, domain III; This domain is found in Elongation Factor G. It shares a ... |
397-468 |
1.14e-05 |
|
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: 43.24 E-value: 1.14e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738649027 397 PELFQTVEVKDPLRSKQLHTGLTQLGEEG-AIQVFKPQIAGGTLLLGaVGQLQFEVVAHRLKTEYGVDAILGP 468
Cdd:pfam14492 4 PVISVAIEPKTKGDEDKLSKALNRLLEEDpTLRVERDEETGETILSG-MGELHLEIVVDRLKRKYGVEVELGP 75
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
18-164 |
1.24e-05 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 47.29 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 18 AIISHPDAGKTTLTEKLLlfaGA-IQIAgsvkARKAE--RHassdwmeieKQRGIsvassVMQmeyRDCVINLLDTPG-H 93
Cdd:COG1159 7 AIVGRPNVGKSTLLNALV---GQkVSIV----SPKPQttRH---------RIRGI-----VTR---EDAQIVFVDTPGiH 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 94 Q----------DFSEDTyrvLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILTFINKLDREVREPL-ELIGEIESH 162
Cdd:COG1159 63 KpkrklgrrmnKAAWSA---LEDVDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDLVKKEELlPLLAEYSEL 139
|
..
gi 738649027 163 LE 164
Cdd:COG1159 140 LD 141
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
19-146 |
2.34e-05 |
|
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: 45.43 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 19 IISHPDAGKTTLTEKLllfagaiqiagSVKARKA--ERHASSdwmeieKQRGI--------------SVASSVMQMEYRD 82
Cdd:cd01889 5 LLGHVDSGKTSLAKAL-----------SEIASTAafDKNPQS------QERGItldlgfssfevdkpKHLEDNENPQIEN 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 83 CVINLLDTPGHQDFsedtyrVLTAV------DAAVMVVDAANGIEPQTERLLKVCRARNTPILTFINKLD 146
Cdd:cd01889 68 YQITLVDCPGHASL------IRTIIggaqiiDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKID 131
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
18-170 |
2.65e-05 |
|
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: 44.54 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 18 AIISHPDAGKTTLTEKLLLfagaiQIAGSVKARKAE-RHASSDWMEIEKQRGIsvassvmqmeyrdcviNLLDTPG---- 92
Cdd:cd00880 1 AIFGRPNVGKSSLLNALLG-----QNVGIVSPIPGTtRDPVRKEWELLPLGPV----------------VLIDTPGldee 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 93 ---HQDFSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVcRARNTPILTFINKLDREVREPLELIG---EIESHLEMD 166
Cdd:cd00880 60 gglGRERVEEARQVADRADLVLLVVDSDLTPVEEEAKLGLL-RERGKPVLLVLNKIDLVPESEEEELLrerKLELLPDLP 138
|
....
gi 738649027 167 CIPF 170
Cdd:cd00880 139 VIAV 142
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
85-148 |
4.19e-05 |
|
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: 46.16 E-value: 4.19e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738649027 85 INLLDTPGHQDFSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILTFINKLDRE 148
Cdd:COG0532 53 ITFLDTPGHEAFTAMRARGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVPIIVAINKIDKP 116
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
18-164 |
8.15e-05 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 44.65 E-value: 8.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 18 AIISHPDAGKTTLTEKLLlfaGA-IQIAgsvkARKAE--RHAssdwmeIekqRGIsvassVMQMEYRdcvINLLDTPG-H 93
Cdd:PRK00089 9 AIVGRPNVGKSTLLNALV---GQkISIV----SPKPQttRHR------I---RGI-----VTEDDAQ---IIFVDTPGiH 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 94 Q----------DFSEDTyrvLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILTFINKLDREVREP--LELIGEIES 161
Cdd:PRK00089 65 KpkralnramnKAAWSS---LKDVDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLVKDKEelLPLLEELSE 141
|
...
gi 738649027 162 HLE 164
Cdd:PRK00089 142 LMD 144
|
|
| mtEFG1_II_like |
cd04091 |
Domain II of mitochondrial elongation factor G1-like proteins found in eukaryotes; Eukaryotic ... |
298-369 |
1.15e-04 |
|
Domain II of mitochondrial elongation factor G1-like proteins found in eukaryotes; Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. Eukaryotic EF-2 operates in the cytosolic protein synthesis machinery of eukaryotes, EF-Gs in protein synthesis in bacteria. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. There are two forms of mtEFG present in mammals (designated mtEFG1s and mtEFG2s); mtEFG2s are not present in this group.
Pssm-ID: 293908 [Multi-domain] Cd Length: 81 Bit Score: 40.73 E-value: 1.15e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738649027 298 FTGVVFKVQANmdpaHRDRVAFVRVSSGKFERGMRLRVARTGKDIRPNNPVSFLSQRRDLVDEAYAGDVIGI 369
Cdd:cd04091 1 FVGLAFKLEEG----RFGQLTYMRVYQGVLRKGDTIYNVRTGKKVRVPRLVRMHSDEMEDIEEVYAGDICAL 68
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
18-162 |
5.69e-04 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 41.12 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 18 AIISHPDAGKTTLTEKLLlfagaiqiagsvkarkaerhasSDWMEIEKQ---RGISVASSVMQMEYRDCVINLLDTPGhQ 94
Cdd:COG1100 7 VVVGTGGVGKTSLVNRLV----------------------GDIFSLEKYlstNGVTIDKKELKLDGLDVDLVIWDTPG-Q 63
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738649027 95 DFSEDT----YRVLTAVDAAVMVVDAANGIEPQTER-LLKVCRARN--TPILTFINKLDR----EVREPLELIGEIESH 162
Cdd:COG1100 64 DEFRETrqfyARQLTGASLYLFVVDGTREETLQSLYeLLESLRRLGkkSPIILVLNKIDLydeeEIEDEERLKEALSED 142
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
22-417 |
1.09e-03 |
|
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: 41.82 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 22 HPDAGKTTLteklllfagaiqiagsVKA-------RKAErhassdwmeiEKQRGISVASSVMQMEYRD-CVINLLDTPGH 93
Cdd:COG3276 8 HIDHGKTTL----------------VKAltgidtdRLKE----------EKKRGITIDLGFAYLPLPDgRRLGFVDVPGH 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 94 QDFsedtyrV------LTAVDAAVMVVDAANGIEPQTerllkvcrarntpiltfinkldREVREPLELIGeieshlemdc 167
Cdd:COG3276 62 EKF------IknmlagAGGIDLVLLVVAADEGVMPQT----------------------REHLAILDLLG---------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 168 IPftwpvgmgrqfSGIYDLTK-DqmrmfnRANpsksgsaedefipdlsnplltercPDTIGKAREEI-ELIQlatpdfdh 245
Cdd:COG3276 104 IK-----------RGIVVLTKaD------LVD------------------------EEWLELVEEEIrELLA-------- 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 246 AAFLdaKQTPVFFGSAVYNFGVQELLDALVEYAPPPGARE-------AIERTiepsepkFT----GVVfkvqanmdpahr 314
Cdd:COG3276 135 GTFL--EDAPIVPVSAVTGEGIDELRAALDALAAAVPARDadgpfrlPIDRV-------FSikgfGTV------------ 193
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 315 drvafVR--VSSGKFERGMRLRVARTGKDIRpnnpVSFL-SQRRDlVDEAYAGDVIGIPNHGV----LHLGDVLTEGEKL 387
Cdd:COG3276 194 -----VTgtLLSGTVRVGDELELLPSGKPVR----VRGIqVHGQP-VEEAYAGQRVALNLAGVekeeIERGDVLAAPGAL 263
|
410 420 430
....*....|....*....|....*....|....*...
gi 738649027 388 H--------FTGLPFFAPELFQtvevKDPLRskqLHTG 417
Cdd:COG3276 264 RptdridvrLRLLPSAPRPLKH----WQRVH---LHHG 294
|
|
| mtEFG2_II_like |
cd04092 |
Domain II of mitochondrial elongation factor G2-like proteins found in eukaryotes; Eukaryotic ... |
303-381 |
2.10e-03 |
|
Domain II of mitochondrial elongation factor G2-like proteins found in eukaryotes; Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. Eukaryotic EF-2 operates in the cytosolic protein synthesis machinery of eukaryotes, EF-Gs in protein synthesis in bacteria. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. No clear phenotype has been found for mutants in the yeast homolog of mtEFG2, MEF2. There are two forms of mtEFG present in mammals (designated mtEFG1s and mtEFG2s); mtEFG1s are not present in this group.
Pssm-ID: 293909 [Multi-domain] Cd Length: 83 Bit Score: 37.30 E-value: 2.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738649027 303 FKVqanMDPAHRDRVAFVRVSSGKFERGMRLRVARTGKDIRPNNPVSFLSQRRDLVDEAYAGDVIGIPNHGVLHLGDVL 381
Cdd:cd04092 6 FKV---IHDPQRGPLVFVRVYSGTLKAGSNVYNTTTGKKERISRLLKMHADQTEEVDSLSAGNIGVITGLKVTSTGDTL 81
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
17-154 |
3.54e-03 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 40.03 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649027 17 FAIISHPDAGKTTLTEKlllfagaiqIAGSVKARKAErhassdwmeiEKQRGISVASSVMQMEYRDC-VINLLDTPGHQD 95
Cdd:PRK10512 3 IATAGHVDHGKTTLLQA---------ITGVNADRLPE----------EKKRGMTIDLGYAYWPQPDGrVLGFIDVPGHEK 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738649027 96 FSEDTYRVLTAVDAAVMVVDAANGIEPQTERLLKVCRARNTPILTF-INKLDR-------EVREPLE 154
Cdd:PRK10512 64 FLSNMLAGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVaLTKADRvdeariaEVRRQVK 130
|
|
| EFG_III |
cd16262 |
Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial ... |
437-468 |
4.12e-03 |
|
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: 36.28 E-value: 4.12e-03
10 20 30
....*....|....*....|....*....|..
gi 738649027 437 GTLLLGAVGQLQFEVVAHRLKTEYGVDAILGP 468
Cdd:cd16262 43 GQTILSGMGELHLEIIVERLKREYGVEVEVGK 74
|
|
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