|
Name |
Accession |
Description |
Interval |
E-value |
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
16-543 |
0e+00 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 1015.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 16 PELLRDVERRRTFGIISHPDAGKTTLTEKLLLFGGAIQLAGTVKARKSARHATSDWMEVEKQRGISVSSSVMQFEYAGHT 95
Cdd:PRK00741 1 SELAQEVAKRRTFAIISHPDAGKTTLTEKLLLFGGAIQEAGTVKGRKSGRHATSDWMEMEKQRGISVTSSVMQFPYRDCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 96 INLLDTPGHQDFSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTPIITFINKMDREVRESFDLLQEIEEVLK 175
Cdd:PRK00741 81 INLLDTPGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTRKLMEVCRLRDTPIFTFINKLDRDGREPLELLDEIEEVLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 176 IDCAPITWPIGMGKTFRGVYHLLEDRVLRFTPGEEKRS-EAEVIKGIANAQLDELFPLEV-GKLREEVDLIQGASNPFSL 253
Cdd:PRK00741 161 IACAPITWPIGMGKRFKGVYDLYNDEVELYQPGEGHTIqEVEIIKGLDNPELDELLGEDLaEQLREELELVQGASNEFDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 254 GDFLAGKQTPVFFGSGINNFGVQEILQALLDWAPPPQPRvagvtVADTRLVMPAEAPFSGFVFKIQANMDPKHRDRIAFF 333
Cdd:PRK00741 241 EAFLAGELTPVFFGSALNNFGVQEFLDAFVEWAPAPQPR-----QTDEREVEPTEEKFSGFVFKIQANMDPKHRDRIAFV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 334 RICSGRYSSGMKVKHVRMGREMKLANALTFMANERVLMEDGVAGDIIGIHNHGQLHIGDTLTEGENLGYKGIPYFSPELF 413
Cdd:PRK00741 316 RVCSGKFEKGMKVRHVRTGKDVRISNALTFMAQDREHVEEAYAGDIIGLHNHGTIQIGDTFTQGEKLKFTGIPNFAPELF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 414 SAARLRDPLKSKQLQKGLQELGEEGAIQVFEQEGGN-MLLGAVGQLQFEVVAQRLKDEYKVDAIFESADIYTARWLVFPD 492
Cdd:PRK00741 396 RRVRLKNPLKQKQLQKGLVQLSEEGAVQVFRPLDNNdLILGAVGQLQFEVVAHRLKNEYNVEAIYEPVGVATARWVECDD 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 81821127 493 EVTRRNFEREQGIRVGKDVDGNPVYLATSRYNLEVTMEKWPKVGFHATREH 543
Cdd:PRK00741 476 AKKLEEFKRKNRSNLAKDGGDNLVYLAPNEVNLRLAQERYPDVKFHATREH 526
|
|
| PrfC |
COG4108 |
Peptide chain release factor RF-3 [Translation, ribosomal structure and biogenesis]; Peptide ... |
16-544 |
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: 1015.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 16 PELLRDVERRRTFGIISHPDAGKTTLTEKLLLFGGAIQLAGTVKARKSARHATSDWMEVEKQRGISVSSSVMQFEYAGHT 95
Cdd:COG4108 1 SELAEEIARRRTFAIISHPDAGKTTLTEKLLLFGGAIQLAGAVKARKARRHATSDWMEIEKQRGISVTSSVMQFEYRGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 96 INLLDTPGHQDFSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTPIITFINKMDREVRESFDLLQEIEEVLK 175
Cdd:COG4108 81 INLLDTPGHEDFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDREGRDPLELLDEIEEVLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 176 IDCAPITWPIGMGKTFRGVYHLLEDRVLRFTPGEEKRSEA-EVIKGIANAQLDELFPLEV-GKLREEVDLIQGASNPFSL 253
Cdd:COG4108 161 IDCAPMTWPIGMGKDFKGVYDRYTDEVHLFERGAGGATEApEEIEGLDDPELDELLGEDLaEQLREEIELLDGAGPEFDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 254 GDFLAGKQTPVFFGSGINNFGVQEILQALLDWAPPPQPRvagvtVADTRLVMPAEAPFSGFVFKIQANMDPKHRDRIAFF 333
Cdd:COG4108 241 EAFLAGELTPVFFGSALNNFGVRELLDAFVELAPPPRPR-----EADEREVEPTEEKFSGFVFKIQANMDPAHRDRIAFM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 334 RICSGRYSSGMKVKHVRMGREMKLANALTFMANERVLMEDGVAGDIIGIHNHGQLHIGDTLTEGENLGYKGIPYFSPELF 413
Cdd:COG4108 316 RICSGKFERGMKVKHVRTGKKIRLSNPQQFFAQDRETVEEAYPGDIIGLHNHGTLRIGDTLTEGEKLEFTGIPSFAPELF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 414 SAARLRDPLKSKQLQKGLQELGEEGAIQVFEQE-GGNMLLGAVGQLQFEVVAQRLKDEYKVDAIFESADIYTARWLVFPD 492
Cdd:COG4108 396 RRVRLKDPMKAKQLRKGLEQLAEEGAVQVFRPLdGNDPILGAVGQLQFEVVQYRLKNEYGVEVRLEPLPYSTARWVTADD 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 81821127 493 EVTRRNFEREQGIRVGKDVDGNPVYLATSRYNLEVTMEKWPKVGFHATREHG 544
Cdd:COG4108 476 PKDLEEFKRKNRSNLAKDRDGRPVFLFPSEWNLRYAQERNPDIKFHATREHA 527
|
|
| prfC |
TIGR00503 |
peptide chain release factor 3; This translation releasing factor, RF-3 (prfC) was originally ... |
18-543 |
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: 695.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 18 LLRDVERRRTFGIISHPDAGKTTLTEKLLLFGGAIQLAGTVKARKSARHATSDWMEVEKQRGISVSSSVMQFEYAGHTIN 97
Cdd:TIGR00503 4 LLKEVDKRRTFAIISHPDAGKTTITEKVLLYGGAIQTAGAVKGRGSQRHAKSDWMEMEKQRGISITTSVMQFPYRDCLVN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 98 LLDTPGHQDFSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTPIITFINKMDREVRESFDLLQEIEEVLKID 177
Cdd:TIGR00503 84 LLDTPGHEDFSEDTYRTLTAVDNCLMVIDAAKGVETRTRKLMEVTRLRDTPIFTFMNKLDRDIRDPLELLDEVENELKIN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 178 CAPITWPIGMGKTFRGVYHLLEDRVLRFTPGE-EKRSEAEVIKGIANAQLDELFPLEVG-KLREEVDLIQGASNPFSLGD 255
Cdd:TIGR00503 164 CAPITWPIGCGKLFKGVYHLLKDETYLYQSGTgGTIQAVRQVKGLNNPALDSAVGSDLAqQLRDELELVEGASNEFDLAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 256 FLAGKQTPVFFGSGINNFGVQEILQALLDWAPPPQPRvagvtVADTRLVMPAEAPFSGFVFKIQANMDPKHRDRIAFFRI 335
Cdd:TIGR00503 244 FHGGEMTPVFFGTALGNFGVDHFLDGLLQWAPKPEAR-----QSDTRTVEPTEEKFSGFVFKIQANMDPKHRDRVAFMRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 336 CSGRYSSGMKVKHVRMGREMKLANALTFMANERVLMEDGVAGDIIGIHNHGQLHIGDTLTEGENLGYKGIPYFSPELFSA 415
Cdd:TIGR00503 319 VSGKYEKGMKLKHVRTGKDVVISDALTFMAGDREHVEEAYAGDIIGLHNHGTIQIGDTFTQGEKIKFTGIPNFAPELFRR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 416 ARLRDPLKSKQLQKGLQELGEEGAIQVFEQ-EGGNMLLGAVGQLQFEVVAQRLKDEYKVDAIFESADIYTARWLVFPDEV 494
Cdd:TIGR00503 399 IRLKDPLKQKQLLKGLVQLSEEGAVQVFRPlDNNDLIVGAVGVLQFDVVVYRLKEEYNVEARYEPVNVATARWVECADWK 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 81821127 495 TRRNFEREQGIRVGKDVDGNPVYLATSRYNLEVTMEKWPKVGFHATREH 543
Cdd:TIGR00503 479 KFEEFKRKNETVLALDGGDNLVYIAKNMVNLELAQERYPDVKFSATREH 527
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
24-289 |
0e+00 |
|
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: 521.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 24 RRRTFGIISHPDAGKTTLTEKLLLFGGAIQLAGTVKARKSARHATSDWMEVEKQRGISVSSSVMQFEYAGHTINLLDTPG 103
Cdd:cd04169 1 RRRTFAIISHPDAGKTTLTEKLLLFGGAIQEAGAVKARKSRKHATSDWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 104 HQDFSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTPIITFINKMDREVRESFDLLQEIEEVLKIDCAPITW 183
Cdd:cd04169 81 HEDFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDREGRDPLELLDEIENELGIDCAPMTW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 184 PIGMGKTFRGVYHLLEDRVLRFTPG-EEKRSEAEVIKGIANAQLDE-LFPLEVGKLREEVDLIQGASNPFSLGDFLAGKQ 261
Cdd:cd04169 161 PIGMGKDFKGVYDRYDKEIYLYERGaGGAIKAPEETKGLDDPKLDElLGEDLAEQLREELELVEGAGPEFDKELFLAGEL 240
|
250 260
....*....|....*....|....*...
gi 81821127 262 TPVFFGSGINNFGVQEILQALLDWAPPP 289
Cdd:cd04169 241 TPVFFGSALNNFGVQELLDAFVKLAPAP 268
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
21-475 |
1.88e-94 |
|
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: 302.74 E-value: 1.88e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 21 DVERRRTFGIISHPDAGKTTLTEKLLLFGGAIQLAGTVKARKsarhATSDWMEVEKQRGISVSSSVMQFEYAGHTINLLD 100
Cdd:COG0480 5 PLEKIRNIGIVAHIDAGKTTLTERILFYTGAIHRIGEVHDGN----TVMDWMPEEQERGITITSAATTCEWKGHKINIID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 101 TPGHQDFSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTPIITFINKMDREvRESFD-LLQEIEEVLKIDCA 179
Cdd:COG0480 81 TPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDRE-GADFDrVLEQLKERLGANPV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 180 PITWPIGMGKTFRGVYHLLEDRVLRFTPG-----------EEKRSEAE-----VIKGIANA--QLDELFpLEVGKL-REE 240
Cdd:COG0480 160 PLQLPIGAEDDFKGVIDLVTMKAYVYDDElgakyeeeeipAELKEEAEeareeLIEAVAETddELMEKY-LEGEELtEEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 241 V--DLIQGasnpfslgdFLAGKQTPVFFGSGINNFGVQEILQALLDWAPPPQ--PRVAGVTVAD----TRLVMPaEAPFS 312
Cdd:COG0480 239 IkaGLRKA---------TLAGKIVPVLCGSAFKNKGVQPLLDAVVDYLPSPLdvPAIKGVDPDTgeevERKPDD-DEPFS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 313 GFVFKIQAnmDPkHRDRIAFFRICSGRYSSGMKVKHVRMGREMKLANALTFMANERVLMEDGVAGDIIGIHNHGQLHIGD 392
Cdd:COG0480 309 ALVFKTMT--DP-FVGKLSFFRVYSGTLKSGSTVYNSTKGKKERIGRLLRMHGNKREEVDEAGAGDIVAVVKLKDTTTGD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 393 TLTEGENlgykgipyfsPELFSAARLRDPL-------KSKQ----LQKGLQELGEE-GAIQV-FEQEGGNMLLGAVGQLQ 459
Cdd:COG0480 386 TLCDEDH----------PIVLEPIEFPEPVisvaiepKTKAdedkLSTALAKLAEEdPTFRVeTDEETGQTIISGMGELH 455
|
490
....*....|....*.
gi 81821127 460 FEVVAQRLKDEYKVDA 475
Cdd:COG0480 456 LEIIVDRLKREFGVEV 471
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
31-478 |
4.05e-88 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 285.10 E-value: 4.05e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 31 ISHPDAGKTTLTEKLLLFGGAIQLAGTVKARKsarhATSDWMEVEKQRGISVSSSVMQFEYAGHTINLLDTPGHQDFSED 110
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRIGEVEDGT----TTMDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 111 TYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTPIITFINKMDREvRESFD-LLQEIEEVLKIDCAPITWPIGMGK 189
Cdd:PRK12740 77 VERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRA-GADFFrVLAQLQEKLGAPVVPLQLPIGEGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 190 TFRGVYHLLEDRVLRFTPGEEKRSEA--------------EVIKGIANA--QLDELFpLEVGKLREEV---DLIQGasnp 250
Cdd:PRK12740 156 DFTGVVDLLSMKAYRYDEGGPSEEIEipaelldraeeareELLEALAEFddELMEKY-LEGEELSEEEikaGLRKA---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 251 fslgdFLAGKQTPVFFGSGINNFGVQEILQALLDWAPPPQ--PRVAGVTVADTRLVMP-AEAPFSGFVFKIQanMDPkHR 327
Cdd:PRK12740 231 -----TLAGEIVPVFCGSALKNKGVQRLLDAVVDYLPSPLevPPVDGEDGEEGAELAPdPDGPLVALVFKTM--DDP-FV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 328 DRIAFFRICSGRYSSGMKVKHVRMGREMKLANALTFMANERVLMEDGVAGDIIGIHNHGQLHIGDTLTEGENlgykgipy 407
Cdd:PRK12740 303 GKLSLVRVYSGTLKKGDTLYNSGTGKKERVGRLYRMHGKQREEVDEAVAGDIVAVAKLKDAATGDTLCDKGD-------- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 408 fsPELFSAARLRDPL-------KSKQ----LQKGLQELGEEG-AIQVF-EQEGGNMLLGAVGQLQFEVVAQRLKDEYKVD 474
Cdd:PRK12740 375 --PILLEPMEFPEPVislaiepKDKGdeekLSEALGKLAEEDpTLRVErDEETGQTILSGMGELHLDVALERLKREYGVE 452
|
....
gi 81821127 475 AIFE 478
Cdd:PRK12740 453 VETG 456
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
26-474 |
5.40e-78 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 259.11 E-value: 5.40e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 26 RTFGIISHPDAGKTTLTEKLLLFGGAIQLAGTVKARKsarhATSDWMEVEKQRGISVSSSVMQFEYAGHTINLLDTPGHQ 105
Cdd:PRK13351 9 RNIGILAHIDAGKTTLTERILFYTGKIHKMGEVEDGT----TVTDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 106 DFSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTPIITFINKMDREVRESFDLLQEIEEVLKIDCAPITWPI 185
Cdd:PRK13351 85 DFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLFKVLEDIEERFGKRPLPLQLPI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 186 GMGKTFRGVYHLLEDRVLRFTPGEEKRSEAEvikgiaNAQLDELFpLEVGKLREEvdLIQGASN--PFSLGDFLAGKQT- 262
Cdd:PRK13351 165 GSEDGFEGVVDLITEPELHFSEGDGGSTVEE------GPIPEELL-EEVEEAREK--LIEALAEfdDELLELYLEGEELs 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 263 ------------------PVFFGSGINNFGVQEILQALLDWAPPPQ---PRVAGVTVADTRLVMP-AEAPFSGFVFKIQA 320
Cdd:PRK13351 236 aeqlraplregtrsghlvPVLFGSALKNIGIEPLLDAVVDYLPSPLevpPPRGSKDNGKPVKVDPdPEKPLLALVFKVQY 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 321 nmDPKHRdRIAFFRICSGRYSSGMKVKHVRMGREMKLANALTFMANERVLMEDGVAGDIIGIHNHGQLHIGDTLTEGENL 400
Cdd:PRK13351 316 --DPYAG-KLTYLRVYSGTLRAGSQLYNGTGGKREKVGRLFRLQGNKREEVDRAKAGDIVAVAGLKELETGDTLHDSADP 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 81821127 401 GYKGIPYFSPELFSAArlRDPLKSKQLQK---GLQELGEEG-AIQVFE-QEGGNMLLGAVGQLQFEVVAQRLKDEYKVD 474
Cdd:PRK13351 393 VLLELLTFPEPVVSLA--VEPERRGDEQKlaeALEKLVWEDpSLRVEEdEETGQTILSGMGELHLEVALERLRREFKLE 469
|
|
| EF-G |
TIGR00484 |
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ... |
21-475 |
3.34e-64 |
|
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: 221.99 E-value: 3.34e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 21 DVERRRTFGIISHPDAGKTTLTEKLLLFGGAIQLAGTVKARKsarhATSDWMEVEKQRGISVSSSVMQFEYAGHTINLLD 100
Cdd:TIGR00484 6 DLNRFRNIGISAHIDAGKTTTTERILFYTGRIHKIGEVHDGA----ATMDWMEQEKERGITITSAATTVFWKGHRINIID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 101 TPGHQDFSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTPIITFINKMDREVRESFDLLQEIEEVLKIDCAP 180
Cdd:TIGR00484 82 TPGHVDFTVEVERSLRVLDGAVAVLDAVGGVQPQSETVWRQANRYEVPRIAFVNKMDKTGANFLRVVNQIKQRLGANAVP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 181 ITWPIGMGKTFRGVYHLLEDRVLRFTPGEEKRSEAE----------------VIKGIANAQlDELFPLEVGKLREEVDLI 244
Cdd:TIGR00484 162 IQLPIGAEDNFIGVIDLVEMKAYFFNGDKGTKAIEKeipsdlleqakelrenLVEAVAEFD-EELMEKYLEGEELTIEEI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 245 QGASNpfslGDFLAGKQTPVFFGSGINNFGVQEILQALLDWAPPPQ--PRVAGV---TVADTRLVMPAEAPFSGFVFKIq 319
Cdd:TIGR00484 241 KNAIR----KGVLNCEFFPVLCGSAFKNKGVQLLLDAVVDYLPSPTdvPAIKGIdpdTEKEIERKASDDEPFSALAFKV- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 320 anMDPKHRDRIAFFRICSGRYSSGMKVKHVRMGREMKLANALTFMANERVLMEDGVAGDIIGIHNHGQLHIGDTLT-EGE 398
Cdd:TIGR00484 316 --ATDPFVGQLTFVRVYSGVLKSGSYVKNSRKNKKERVGRLVKMHANNREEIKEVRAGDICAAIGLKDTTTGDTLCdPKI 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 81821127 399 NLGYKGIPYFSPELFSAARLRDPLKSKQLQKGLQELGEEG-AIQVF-EQEGGNMLLGAVGQLQFEVVAQRLKDEYKVDA 475
Cdd:TIGR00484 394 DVILERMEFPEPVISLAVEPKTKADQEKMGIALGKLAEEDpTFRTFtDPETGQTIIAGMGELHLDIIVDRMKREFKVEA 472
|
|
| RF3_C |
pfam16658 |
Class II release factor RF3, C-terminal domain; |
402-528 |
6.94e-59 |
|
Class II release factor RF3, C-terminal domain;
Pssm-ID: 465221 [Multi-domain] Cd Length: 129 Bit Score: 191.50 E-value: 6.94e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 402 YKGIPYFSPELFSAARLRDPLKSKQLQKGLQELGEEGAIQVFEQE--GGNMLLGAVGQLQFEVVAQRLKDEYKVDAIFES 479
Cdd:pfam16658 1 FTGIPSFAPEHFARVRLKDPMKRKQFRKGLEQLAEEGAIQVFRPDnrGEDPILGAVGQLQFEVVQYRLKNEYGVDVRLEP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 81821127 480 ADIYTARWLVFPDEVTRRNFEREQGIRVGKDVDGNPVYLATSRYNLEVT 528
Cdd:pfam16658 81 LPYSTARWVESDDAKALDEFKRASGSNLAKDRDGRPVLLFRNEWNLRYA 129
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
23-199 |
7.44e-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: 191.20 E-value: 7.44e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 23 ERRRTFGIISHPDAGKTTLTEKLLLFGGAIQLAGTVKARKsarHATSDWMEVEKQRGISVSSSVMQFEYAGHTINLLDTP 102
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEG---EAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 103 GHQDFSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTPIITFINKMDREVRESFD-LLQEIEEVL--KIDCA 179
Cdd:pfam00009 78 GHVDFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDGAELEeVVEEVSRELleKYGED 157
|
170 180
....*....|....*....|..
gi 81821127 180 PITWPI--GMGKTFRGVYHLLE 199
Cdd:pfam00009 158 GEFVPVvpGSALKGEGVQTLLD 179
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
27-289 |
8.10e-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: 191.27 E-value: 8.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 27 TFGIISHPDAGKTTLTEKLLLFGGAIQLAGTVKARKSarhaTSDWMEVEKQRGISVSSSVMQFEYAGHTINLLDTPGHQD 106
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRLGRVEDGNT----VSDYDPEEKKRKMSIETSVAPLEWNGHKINLIDTPGYAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 107 FSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTPIITFINKMDREvRESFD-LLQEIEEVLKIDCAPITWPI 185
Cdd:cd04170 77 FVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRA-RADFDkTLAALREAFGRPVVPIQLPI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 186 GMGKTFRGVYHLLEDRVLRFTPGEekrseaevikGIANAQLDELFPLEVGKLREEVdLIQGASN---------------- 249
Cdd:cd04170 156 GEGDEFTGVVDLLSEKAYRYDPGE----------PSVEIEIPEELKEKVAEAREEL-LEAVAETdeelmekyleegelte 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 81821127 250 -----PFSLGdFLAGKQTPVFFGSGINNFGVQEILQALLDWAPPP 289
Cdd:cd04170 225 eelraGLRRA-LRAGLIVPVFFGSALTGIGVRRLLDALVELAPSP 268
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
28-289 |
3.95e-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: 181.54 E-value: 3.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 28 FGIISHPDAGKTTLTEKLLLFGGAIQLAGTVKARKsarhATSDWMEVEKQRGISVSSSVMQFEYAGHTINLLDTPGHQDF 107
Cdd:cd01886 2 IGIIAHIDAGKTTTTERILYYTGRIHKIGEVHGGG----ATMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 108 SEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTPIITFINKMDREVRESFDLLQEIEEVLKIDCAPITWPIGM 187
Cdd:cd01886 78 TIEVERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQIREKLGANPVPLQLPIGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 188 GKTFRGVYHLLEDRVLRFTPGEEKRSEAEVIkgiaNAQLDElfplEVGKLREEvdLIQGASNpFS-------LGDF---- 256
Cdd:cd01886 158 EDDFEGVVDLIEMKALYWDGELGEKIEETDI----PEDLLE----EAEEAREE--LIETLAE-VDdelmekyLEGEeite 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 81821127 257 -----------LAGKQTPVFFGSGINNFGVQEILQALLDWAPPP 289
Cdd:cd01886 227 eeikaairkgtIANKIVPVLCGSAFKNKGVQPLLDAVVDYLPSP 270
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
27-289 |
4.41e-50 |
|
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: 170.55 E-value: 4.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 27 TFGIISHPDAGKTTLTEKLLLFGGAIQLAGTVKARKSarhatsDWMEVEKQRGISVSSSVMQFEYAGHTINLLDTPGHQD 106
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFL------DTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 107 FSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTPIITFINKMDREVRESFD-LLQEIEEVLKIDCAPitwpi 185
Cdd:cd00881 75 FSKETVRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGEEDFDeVLREIKELLKLIGFT----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 186 gmgktfrgvyhlledrvlrftpgeekrseaevikgianaqldelfplevgklreevdliqgasnpfslgdFLAGKQTPVF 265
Cdd:cd00881 150 ----------------------------------------------------------------------FLKGKDVPII 159
|
250 260
....*....|....*....|....
gi 81821127 266 FGSGINNFGVQEILQALLDWAPPP 289
Cdd:cd00881 160 PISALTGEGIEELLDAIVEHLPPP 183
|
|
| RF3_II |
cd03689 |
Domain II of bacterial Release Factor 3; This subfamily represents domain II of bacterial ... |
311-397 |
1.81e-47 |
|
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: 160.13 E-value: 1.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 311 FSGFVFKIQANMDPKHRDRIAFFRICSGRYSSGMKVKHVRMGREMKLANALTFMANERVLMEDGVAGDIIGIHNHGQLHI 390
Cdd:cd03689 1 FSGFVFKIQANMDPKHRDRIAFLRVCSGKFERGMKVKHVRTGKEVRLSNATTFMAQDRETVEEAYPGDIIGLPNHGTFQI 80
|
....*..
gi 81821127 391 GDTLTEG 397
Cdd:cd03689 81 GDTFTEG 87
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
27-289 |
7.49e-46 |
|
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: 160.86 E-value: 7.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 27 TFGIISHPDAGKTTLTEKLLLFGGAIQLAGTVkarkSARHATSDWMEVEKQRGISVSSSVMQFEYAGHTINLLDTPGHQD 106
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIRELGSV----DKGTTRTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 107 FSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTPIITFINKMDREVRESFDLLQEIEEVLKIDCAPitwpig 186
Cdd:cd04168 77 FIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTIIFVNKIDRAGADLEKVYQEIKEKLSPDIVP------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 187 mgktfrgvyhlLEDRVLRFTPGEEKRSEAEVIKGIANAQlDELF-------PLEVGKLREE-VDLIQgasnpfslgdflA 258
Cdd:cd04168 151 -----------MQKVGLYPNICDTNNIDDEQIETVAEGN-DELLekylsggPLEELELDNElSARIQ------------K 206
|
250 260 270
....*....|....*....|....*....|.
gi 81821127 259 GKQTPVFFGSGINNFGVQEILQALLDWAPPP 289
Cdd:cd04168 207 ASLFPVYHGSALKGIGIDELLEGITNLFPTS 237
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
17-474 |
7.85e-34 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 136.53 E-value: 7.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 17 ELLRDVERRRTFGIISHPDAGKTTLTEKLLLFGGAI--QLAGTVKARksarhatsDWMEVEKQRGISVSSSV--MQFEYA 92
Cdd:PRK07560 12 ELMKNPEQIRNIGIIAHIDHGKTTLSDNLLAGAGMIseELAGEQLAL--------DFDEEEQARGITIKAANvsMVHEYE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 93 G--HTINLLDTPGHQDFSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLL-EVCRLRNTPIItFINKMDREVREsfdllqe 169
Cdd:PRK07560 84 GkeYLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLrQALRERVKPVL-FINKVDRLIKE------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 170 ieevlkidcapitwpigmgktfrgvyhlledrvLRFTPGEEKRSEAEVIKgianaqldelfplEVGKlreevdLIQGASN 249
Cdd:PRK07560 156 ---------------------------------LKLTPQEMQQRLLKIIK-------------DVNK------LIKGMAP 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 250 P-FSLG---DFLAGKqtpVFFGSGINNFGV------------QEIL------------------QALLD----WAPPP-- 289
Cdd:PRK07560 184 EeFKEKwkvDVEDGT---VAFGSALYNWAIsvpmmqktgikfKDIIdyyekgkqkelaekaplhEVVLDmvvkHLPNPie 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 290 -QP-RVAGV-------TVADTRLVMPAEAPFSGFVFKIqaNMDPkHRDRIAFFRICSGRYSSGMKVKHVRMGREMKLANA 360
Cdd:PRK07560 261 aQKyRIPKIwkgdlnsEVGKAMLNCDPNGPLVMMVTDI--IVDP-HAGEVATGRVFSGTLRKGQEVYLVGAKKKNRVQQV 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 361 LTFMANERVLMEDGVAGDIIGIHNHGQLHIGDTLTEGENLG-YKGIPYFSPELFSAArlRDPLKSKQLQK---GLQELG- 435
Cdd:PRK07560 338 GIYMGPEREEVEEIPAGNIAAVTGLKDARAGETVVSVEDMTpFESLKHISEPVVTVA--IEAKNPKDLPKlieVLRQLAk 415
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 81821127 436 EEGAIQV-FEQEGGNMLLGAVGQLQFEVVAQRLKDEYKVD 474
Cdd:PRK07560 416 EDPTLVVkINEETGEHLLSGMGELHLEVITYRIKRDYGIE 455
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
26-207 |
8.23e-33 |
|
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: 123.80 E-value: 8.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 26 RTFGIISHPDAGKTTLTEKLLlfggaiQLAGTVKARKSaRHATSDWMEVEKQRGISVSSSVMQFEYA---GHT--INLLD 100
Cdd:cd01890 1 RNFSIIAHIDHGKSTLADRLL------ELTGTVSEREM-KEQVLDSMDLERERGITIKAQAVRLFYKakdGEEylLNLID 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 101 TPGHQDFSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTPIITFINKMDREVRESFDLLQEIEEVLKIDCAP 180
Cdd:cd01890 74 TPGHVDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVKQEIEDVLGLDASE 153
|
170 180
....*....|....*....|....*...
gi 81821127 181 ItwpIGM-GKTFRGVYHLLEDRVLRFTP 207
Cdd:cd01890 154 A---ILVsAKTGLGVEDLLEAIVERIPP 178
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
26-173 |
2.00e-28 |
|
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: 112.71 E-value: 2.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 26 RTFGIISHPDAGKTTLTEKLLLFGGAI--QLAGTVKArksarhatSDWMEVEKQRGISV-SSSV-MQFEYAGHT------ 95
Cdd:cd01885 1 RNICIIAHVDHGKTTLSDSLLASAGIIseKLAGKARY--------LDTREDEQERGITIkSSAIsLYFEYEEEKmdgndy 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 96 -INLLDTPGHQDFSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLL-EVCRLRNTPIItFINKMDREVRE-SFD------- 165
Cdd:cd01885 73 lINLIDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLrQALEERVKPVL-VINKIDRLILElKLSpeeayqr 151
|
....*...
gi 81821127 166 LLQEIEEV 173
Cdd:cd01885 152 LLRIVEDV 159
|
|
| RF3_III |
cd16259 |
Domain III of bacterial Release Factor 3 (RF3); The class II RF3 is a member of one of two ... |
410-478 |
5.73e-27 |
|
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: 103.49 E-value: 5.73e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 410 PELFSAARLRDPLKSKQLQKGLQELGEEGAIQVFEQE-GGNMLLGAVGQLQFEVVAQRLKDEYKVDAIFE 478
Cdd:cd16259 1 PEHFRRVRLKDPMKAKQLRKGLEQLAEEGAVQVFRPMdGSDPIVGAVGPLQFEVLQARLENEYGVEVVFE 70
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
26-170 |
4.72e-26 |
|
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: 105.37 E-value: 4.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 26 RTFGIISHPDAGKTTLTEKLLlfggaiQLAGTVKARKSARHATSDWMEVEKQRGISVSSSVMQFEYAGHTINLLDTPGHQ 105
Cdd:cd01891 3 RNIAIIAHVDHGKTTLVDALL------KQSGTFRENEEVGERVMDSNDLERERGITILAKNTAITYKDTKINIIDTPGHA 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81821127 106 DFSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTPIITFINKMDRE-------VRESFDLLQEI 170
Cdd:cd01891 77 DFGGEVERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDRPdarpeevVDEVFDLFLEL 148
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
30-399 |
3.17e-23 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 103.56 E-value: 3.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 30 IISHPDAGKTTLTEKLLlfggaiQLAGTVKARKSARHATSDWMEVEKQRGISVSSSVMQFEYAGHTINLLDTPGHQDFSE 109
Cdd:COG1217 11 IIAHVDHGKTTLVDALL------KQSGTFRENQEVAERVMDSNDLERERGITILAKNTAVRYKGVKINIVDTPGHADFGG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 110 DTYRVLTAVDAAVMVIDAAKGVETQT----IKLLEvcrlRNTPIITFINKMDREvresfDllQEIEEVLkidcapitwpi 185
Cdd:COG1217 85 EVERVLSMVDGVLLLVDAFEGPMPQTrfvlKKALE----LGLKPIVVINKIDRP-----D--ARPDEVV----------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 186 gmgktfrgvyhlleDRVLrftpgeekrseaevikgianaqldELFplevgklreeVDLiqGASNpfSLGDFlagkqtPVF 265
Cdd:COG1217 143 --------------DEVF------------------------DLF----------IEL--GATD--EQLDF------PVV 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 266 FGSGINNFGVQE----------ILQALLDWAPPPQprvagvtvADtrlvmpAEAPFSGFVFKIQANmdpKHRDRIAFFRI 335
Cdd:COG1217 165 YASARNGWASLDlddpgedltpLFDTILEHVPAPE--------VD------PDGPLQMLVTNLDYS---DYVGRIAIGRI 227
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 336 CSGRYSSGMKVKHVRMG---REMKLANALTFMANERVLMEDGVAGDII---GIHNhgqLHIGDTLTEGEN 399
Cdd:COG1217 228 FRGTIKKGQQVALIKRDgkvEKGKITKLFGFEGLERVEVEEAEAGDIVaiaGIED---INIGDTICDPEN 294
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
21-178 |
6.68e-23 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 102.40 E-value: 6.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 21 DVERRRTFGIISHPDAGKTTLTEKLllfggaIQLAGTVKARKsARHATSDWMEVEKQRGISVSSSVMQFEYA---GHT-- 95
Cdd:COG0481 2 DQKNIRNFSIIAHIDHGKSTLADRL------LELTGTLSERE-MKEQVLDSMDLERERGITIKAQAVRLNYKakdGETyq 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 96 INLLDTPGHQDFSEDTYRVLTAVDAAVMVIDAAKGVETQTI----KLLEvcrlRNTPIITFINKMD------REVResfd 165
Cdd:COG0481 75 LNLIDTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTLanvyLALE----NDLEIIPVINKIDlpsadpERVK---- 146
|
170
....*....|...
gi 81821127 166 llQEIEEVLKIDC 178
Cdd:COG0481 147 --QEIEDIIGIDA 157
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
26-158 |
1.86e-21 |
|
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: 92.72 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 26 RTFGIISHPDAGKTTLTEKLLLFGGAiQLAGTVKARKSARHatSDWMEVEKQRGISVSSSVMQF-----EYAGHTINLLD 100
Cdd:cd04167 1 RNVCIAGHLHHGKTSLLDMLIEQTHK-RTPSVKLGWKPLRY--TDTRKDEQERGISIKSNPISLvledsKGKSYLINIID 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 81821127 101 TPGHQDFSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTPIITFINKMDR 158
Cdd:cd04167 78 TPGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDR 135
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
22-470 |
2.03e-19 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 91.69 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 22 VERRRTFGIISHPDAGKTTLTEKLLlfggaiQLAGTVKARKSARHATSDWMEVEKQRGISVSSSVMQFEYAGHTINLLDT 101
Cdd:PRK10218 2 IEKLRNIAIIAHVDHGKTTLVDKLL------QQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 102 PGHQDFSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTPIITFINKMDRE-------VRESFDLLQEIEEVL 174
Cdd:PRK10218 76 PGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPgarpdwvVDQVFDLFVNLDATD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 175 KIDCAPITWpigmgktfrgvyhlledrvlrftpgeekrseAEVIKGIANAQLDElfplevgklreevdliqgasnpfslg 254
Cdd:PRK10218 156 EQLDFPIVY-------------------------------ASALNGIAGLDHED-------------------------- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 255 dfLAGKQTPVFfgsginnfgvqeilQALLDWAPPPqprvagvtvaDTRLVMPAEAPFSGFVFKIQANMdpkhrdrIAFFR 334
Cdd:PRK10218 179 --MAEDMTPLY--------------QAIVDHVPAP----------DVDLDGPFQMQISQLDYNSYVGV-------IGIGR 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 335 ICSGRYSSGMKVKHVR---MGREMKLANALTFMANERVLMEDGVAGDIIGIHNHGQLHIGDTLTEGENLgyKGIPYFSPE 411
Cdd:PRK10218 226 IKRGKVKPNQQVTIIDsegKTRNAKVGKVLGHLGLERIETDLAEAGDIVAITGLGELNISDTVCDTQNV--EALPALSVD 303
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81821127 412 LFSAARL----RDPLKSKQ---------LQKGLQELGEEGAIQVFEQEGGNML-LGAVGQLQFEVVAQRLKDE 470
Cdd:PRK10218 304 EPTVSMFfcvnTSPFCGKEgkfvtsrqiLDRLNKELVHNVALRVEETEDADAFrVSGRGELHLSVLIENMRRE 376
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
17-162 |
1.54e-18 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 89.34 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 17 ELLRDVERRRTFGIISHPDAGKTTLTEKLllfggaIQLAGTVKARKSARHATSDWMEVEKQRGISVSSS--VMQFEYAGH 94
Cdd:PTZ00416 11 EIMDNPDQIRNMSVIAHVDHGKSTLTDSL------VCKAGIISSKNAGDARFTDTRADEQERGITIKSTgiSLYYEHDLE 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81821127 95 T--------INLLDTPGHQDFSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLL-EVCRLRNTPIItFINKMDREVRE 162
Cdd:PTZ00416 85 DgddkqpflINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLrQALQERIRPVL-FINKVDRAILE 160
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
30-195 |
1.04e-16 |
|
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: 77.90 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 30 IISHPDAGKTTLTEKLllfggaiqlagtvkaRKSARHAtsdwMEVekqRGI--SVSSSVMQFEYAGHTINLLDTPGHQDF 107
Cdd:cd01887 5 VMGHVDHGKTTLLDKI---------------RKTNVAA----GEA---GGItqHIGAYQVPIDVKIPGITFIDTPGHEAF 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 108 SEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTPIITFINKMDREVRESFDLLQEIEEVLKIDCAPITWpigm 187
Cdd:cd01887 63 TNMRARGASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKPYGTEADPERVKNELSELGLVGEEW---- 138
|
....*...
gi 81821127 188 GKTFRGVY 195
Cdd:cd01887 139 GGDVSIVP 146
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
29-157 |
1.04e-16 |
|
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: 77.80 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 29 GIISHPDAGKTTLTEKLLlfggaiqlagTVKARKSARHAT---SDWMEVEKQRGISVsssvmqfeyaghTINLLDTPGHQ 105
Cdd:TIGR00231 5 VIVGHPNVGKSTLLNSLL----------GNKGSITEYYPGttrNYVTTVIEEDGKTY------------KFNLLDTAGQE 62
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 81821127 106 DFSED-------TYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRlRNTPIITFINKMD 157
Cdd:TIGR00231 63 DYDAIrrlyypqVERSLRVFDIVILVLDVEEILEKQTKEIIHHAD-SGVPIILVGNKID 120
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
26-181 |
4.39e-14 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 75.15 E-value: 4.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 26 RTFGIISHPDAGKTTLTEKLLLFGGAIQL--AGTVKarksarhaTSDWMEVEKQRGISVSSS--VMQFEYAGHT------ 95
Cdd:PLN00116 20 RNMSVIAHVDHGKSTLTDSLVAAAGIIAQevAGDVR--------MTDTRADEAERGITIKSTgiSLYYEMTDESlkdfkg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 96 --------INLLDTPGHQDFSEDTYRVLTAVDAAVMVIDAAKG--VETQTI---KLLEvcRLRntPIITfINKMDREVRE 162
Cdd:PLN00116 92 erdgneylINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGvcVQTETVlrqALGE--RIR--PVLT-VNKMDRCFLE 166
|
170
....*....|....*....
gi 81821127 163 sfdLLQEIEEVLKIDCAPI 181
Cdd:PLN00116 167 ---LQVDGEEAYQTFSRVI 182
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
30-157 |
1.51e-12 |
|
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: 69.58 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 30 IISHPDAGKTTLTEKLLLFGGAIQ---LAGTVKARKSARHAT------SDWMEVEKQRGISVSSSVMQFEYAGHTINLLD 100
Cdd:COG5256 12 VIGHVDHGKSTLVGRLLYETGAIDehiIEKYEEEAEKKGKESfkfawvMDRLKEERERGVTIDLAHKKFETDKYYFTIID 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 101 TPGHQDFSEDTYRVLTAVDAAVMVIDAAKGVETQT---IKLLEVCRLRNtpIITFINKMD 157
Cdd:COG5256 92 APGHRDFVKNMITGASQADAAILVVSAKDGVMGQTrehAFLARTLGINQ--LIVAVNKMD 149
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
29-200 |
4.58e-12 |
|
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: 64.40 E-value: 4.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 29 GIISHPDAGKTTLTEklllfggaiQLAGTVKARKSARHATSDWMEVEkqrgisvsssVMQFEYAGHTINLLDTPGHQDFS 108
Cdd:cd00882 1 VVVGRGGVGKSSLLN---------ALLGGEVGEVSDVPGTTRDPDVY----------VKELDKGKVKLVLVDTPGLDEFG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 109 -----EDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLR--NTPIITFINKMDR---EVRESFDLLQEIEEVLKIDC 178
Cdd:cd00882 62 glgreELARLLLRGADLILLVVDSTDRESEEDAKLLILRRLRkeGIPIILVGNKIDLleeREVEELLRLEELAKILGVPV 141
|
170 180
....*....|....*....|..
gi 81821127 179 APITwpigmGKTFRGVYHLLED 200
Cdd:cd00882 142 FEVS-----AKTGEGVDELFEK 158
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
30-159 |
1.57e-11 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 67.16 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 30 IISHPDAGKTTLTEKLLLFGGAIQLAGTVKARKSArhatsdwMEVEkqrgisvsssvmqFEYAGHTINL--LDTPGHQDF 107
Cdd:CHL00189 249 ILGHVDHGKTTLLDKIRKTQIAQKEAGGITQKIGA-------YEVE-------------FEYKDENQKIvfLDTPGHEAF 308
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 81821127 108 SEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTPIITFINKMDRE 159
Cdd:CHL00189 309 SSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKA 360
|
|
| EFG_mtEFG_II |
cd04088 |
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation ... |
311-396 |
2.01e-11 |
|
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: 59.84 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 311 FSGFVFKIQAnmDPKHRdRIAFFRICSGRYSSGMKVKHVRMGREMKLANALTFMANERVLMEDGVAGDIIGIHNHGQLHI 390
Cdd:cd04088 1 FSALVFKTMA--DPFVG-KLTFFRVYSGTLKSGSTVYNSTKGKKERVGRLLRMHGKKREEVEELGAGDIGAVVGLKDTRT 77
|
....*.
gi 81821127 391 GDTLTE 396
Cdd:cd04088 78 GDTLCD 83
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
30-157 |
4.64e-11 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 64.95 E-value: 4.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 30 IISHPDAGKTTLTEKLLLFGGAIQLAGTVKARKSARHATS---------DWMEVEKQRGISVSSSVMQFEYAGHTINLLD 100
Cdd:PRK12317 11 VIGHVDHGKSTLVGRLLYETGAIDEHIIEELREEAKEKGKesfkfawvmDRLKEERERGVTIDLAHKKFETDKYYFTIVD 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 101 TPGHQDFSEDTYRVLTAVDAAVMVIDA--AKGVETQTIKLLEVCR-LRNTPIITFINKMD 157
Cdd:PRK12317 91 CPGHRDFVKNMITGASQADAAVLVVAAddAGGVMPQTREHVFLARtLGINQLIVAINKMD 150
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
30-157 |
1.26e-10 |
|
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: 61.35 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 30 IISHPDAGKTTLTEKLLLFGGAI---QLAgtvKARKSARHATS---------DWMEVEKQRGISVSSSVMQFEYAGHTIN 97
Cdd:cd01883 4 VIGHVDAGKSTLTGHLLYKLGGVdkrTIE---KYEKEAKEMGKesfkyawvlDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81821127 98 LLDTPGHQDFSEDTYRVLTAVDAAVMVIDAAKG-------VETQT------IKLLEVCRLrntpiITFINKMD 157
Cdd:cd01883 81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTrehallARTLGVKQL-----IVAVNKMD 148
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
4-171 |
1.61e-10 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 63.48 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 4 IPAATPSATPFPPELLRDV---------ERRR---TFGIISHPDAGKTTLTEKLLLfggAIQLAGTVKARKsarHATSDW 71
Cdd:PLN03126 48 LSPFSTTTTSTSQRRRRSFtvraargkfERKKphvNIGTIGHVDHGKTTLTAALTM---ALASMGGSAPKK---YDEIDA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 72 MEVEKQRGISVSSSVMQFEYAGHTINLLDTPGHQDFSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTP-II 150
Cdd:PLN03126 122 APEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPnMV 201
|
170 180
....*....|....*....|.
gi 81821127 151 TFINKMDREVREsfDLLQEIE 171
Cdd:PLN03126 202 VFLNKQDQVDDE--ELLELVE 220
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
28-175 |
2.25e-10 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.
Pssm-ID: 206734 [Multi-domain] Cd Length: 170 Bit Score: 59.54 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 28 FGIISHPDAGKTTLTEKLLLFGGaiqlagtvkarksarhatsDWMEVEKQRGISVSSSVMQFEYA-GHTINLLDTPGHQD 106
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALTGIET-------------------DRLPEEKKRGITIDLGFAYLDLPdGKRLGFIDVPGHEK 62
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81821127 107 FSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCR-LRNTPIITFINKMDREVRESFDLL-QEIEEVLK 175
Cdd:cd04171 63 FVKNMLAGAGGIDAVLLVVAADEGIMPQTREHLEILElLGIKKGLVVLTKADLVDEDRLELVeEEILELLA 133
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
29-157 |
3.73e-10 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.
Pssm-ID: 206676 [Multi-domain] Cd Length: 192 Bit Score: 59.30 E-value: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 29 GIISHPDAGKTTLteklllfggAIQLAGTvkarksARHATSDWMEVEKQRGI-----------SVSSSVMQFEYAGH--- 94
Cdd:cd01889 4 GLLGHVDSGKTSL---------AKALSEI------ASTAAFDKNPQSQERGItldlgfssfevDKPKHLEDNENPQIeny 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 81821127 95 TINLLDTPGHQDFsedtyrVLTAV------DAAVMVIDAAKGVETQTIKLLEVCRLRNTPIITFINKMD 157
Cdd:cd01889 69 QITLVDCPGHASL------IRTIIggaqiiDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKID 131
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
29-174 |
4.40e-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: 4.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 29 GIISHPDAGKTTLTeklllfgGAIQ--LAGTVKARKSARHATSDWMEvEKQRGISVSSSVMQFE-----YAgHTinllDT 101
Cdd:cd01884 6 GTIGHVDHGKTTLT-------AAITkvLAKKGGAKAKKYDEIDKAPE-EKARGITINTAHVEYEtanrhYA-HV----DC 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81821127 102 PGHQDFSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTP-IITFINKMDR-EVRESFDLLQ-EIEEVL 174
Cdd:cd01884 73 PGHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPyIVVFLNKADMvDDEELLELVEmEVRELL 148
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
29-171 |
3.35e-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: 59.02 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 29 GIISHPDAGKTTLTEKLllfggAIQLAGTVKArKSARHATSDWMEVEKQRGISVSSSVMQFEYAGHTINLLDTPGHQDFS 108
Cdd:TIGR00485 16 GTIGHVDHGKTTLTAAI-----TTVLAKEGGA-AARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHVDCPGHADYV 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81821127 109 EDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTP-IITFINKMDREVRESFDLLQEIE 171
Cdd:TIGR00485 90 KNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPyIVVFLNKCDMVDDEELLELVEME 153
|
|
| tufA |
CHL00071 |
elongation factor Tu |
29-165 |
3.39e-09 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 58.82 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 29 GIISHPDAGKTTLTEKLLLfggAIQLAGTVKARKsarHATSDWMEVEKQRGISVSSSVMQFE-----YAgHTinllDTPG 103
Cdd:CHL00071 16 GTIGHVDHGKTTLTAAITM---TLAAKGGAKAKK---YDEIDSAPEEKARGITINTAHVEYEtenrhYA-HV----DCPG 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81821127 104 HQDFSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTP-IITFINKMDR------------EVRESFD 165
Cdd:CHL00071 85 HADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPnIVVFLNKEDQvddeellelvelEVRELLS 159
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
29-174 |
3.85e-09 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 59.07 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 29 GIISHPDAGKTTLTeklllfgGAIQ--LAGTVKArKSARHATSDWMEVEKQRGISVSSSVMQFEYAGHTINLLDTPGHQD 106
Cdd:PLN03127 65 GTIGHVDHGKTTLT-------AAITkvLAEEGKA-KAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVDCPGHAD 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81821127 107 FSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTP-IITFINKMDR-EVRESFDLLQ-EIEEVL 174
Cdd:PLN03127 137 YVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPsLVVFLNKVDVvDDEELLELVEmELRELL 207
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
33-157 |
6.09e-09 |
|
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: 56.04 E-value: 6.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 33 HPDAGKTTLTEKLLLFGGAI---QLAGTVKARKSARHATS-------DWMEVEKQRGISVSSSVMQFEYAGHTINLLDTP 102
Cdd:cd04166 7 SVDDGKSTLIGRLLYDSKSIfedQLAALERSKSSGTQGEKldlallvDGLQAEREQGITIDVAYRYFSTPKRKFIIADTP 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 81821127 103 GHQDFSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTP-IITFINKMD 157
Cdd:cd04166 87 GHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRhVVVAVNKMD 142
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
30-157 |
1.40e-08 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 57.06 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 30 IISHPDAGKTTLTEKLLLFGGAIQLAGTVKARKSA--------RHA-TSDWMEVEKQRGISVSSSVMQFEYAGHTINLLD 100
Cdd:PTZ00141 12 VIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAaemgkgsfKYAwVLDKLKAERERGITIDIALWKFETPKYYFTIID 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81821127 101 TPGHQDFSEDTYRVLTAVDAAVMVIDAAKGV-------ETQTiklLEVCRLRNT----PIITFINKMD 157
Cdd:PTZ00141 92 APGHRDFIKNMITGTSQADVAILVVASTAGEfeagiskDGQT---REHALLAFTlgvkQMIVCINKMD 156
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
329-395 |
3.24e-08 |
|
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.
Pssm-ID: 427163 [Multi-domain] Cd Length: 73 Bit Score: 50.73 E-value: 3.24e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81821127 329 RIAFFRICSGRYSSGMKVKHVRMGREMKLANA-----LTFMANERVLMEDGVAGDIIGIHNHGQLHIGDTLT 395
Cdd:pfam03144 2 TVATGRVESGTLKKGDKVRILPNGTGKKKIVTrvtslLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
30-130 |
4.33e-08 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 55.48 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 30 IISHPDAGKTTLTEKLLLFGGAI---------QLAGTVKARKSARHATSDWMEVEKQRGISVSSSVMQFEYAGHTINLLD 100
Cdd:PLN00043 12 VIGHVDSGKSTTTGHLIYKLGGIdkrvierfeKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYYCTVID 91
|
90 100 110
....*....|....*....|....*....|
gi 81821127 101 TPGHQDFSEDTYRVLTAVDAAVMVIDAAKG 130
Cdd:PLN00043 92 APGHRDFIKNMITGTSQADCAVLIIDSTTG 121
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
27-155 |
8.18e-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: 50.70 E-value: 8.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 27 TFGIISHPDAGKTTLTEKLLlfggaiqlagtvkarkSARHATSDWMEV--EKQRGIsvsssvmqFEYAGHTINLLDTPG- 103
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALT----------------GAKAIVSDYPGTtrDPNEGR--------LELKGKQIILVDTPGl 56
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 81821127 104 ----HQDFS-EDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTPIITFINK 155
Cdd:pfam01926 57 iegaSEGEGlGRAFLAIIEADLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
311-395 |
1.95e-07 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 48.41 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 311 FSGFVFKIQANMdpkHRDRIAFFRICSGRYSSGMKVKHVRMGREMKLANALTFMANervlMEDGVAGDIIGIHNHGQ--L 388
Cdd:cd01342 1 LVMQVFKVFYIP---GRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEE----VDEAKAGDIVGIGILGVkdI 73
|
....*..
gi 81821127 389 HIGDTLT 395
Cdd:cd01342 74 LTGDTLT 80
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
29-174 |
4.28e-07 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 52.25 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 29 GIISHPDAGKTTLTeklllfgGAIQlagTVKARKSARHATS----DWMEVEKQRGISVSSSVMQFE-----YAgHtinlL 99
Cdd:PRK12736 16 GTIGHVDHGKTTLT-------AAIT---KVLAERGLNQAKDydsiDAAPEEKERGITINTAHVEYEtekrhYA-H----V 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81821127 100 DTPGHQDFSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTP-IITFINKMDR-EVRESFDLLQ-EIEEVL 174
Cdd:PRK12736 81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPyLVVFLNKVDLvDDEELLELVEmEVRELL 158
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
329-399 |
1.24e-06 |
|
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios and is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion. The domain II of BipA shows similarity to the domain II of the elongation factors (EFs) EF-G and EF-Tu.
Pssm-ID: 293892 [Multi-domain] Cd Length: 94 Bit Score: 46.80 E-value: 1.24e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81821127 329 RIAFFRICSGRYSSGMKVKHVRMGREMKLANA---LTFMANERVLMEDGVAGDIIGIHNHGQLHIGDTLTEGEN 399
Cdd:cd03691 16 RIAIGRIFSGTVKVGQQVTVVDEDGKIEKGRVtklFGFEGLERVEVEEAEAGDIVAIAGLEDITIGDTICDPEV 89
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
29-157 |
4.69e-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: 48.99 E-value: 4.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 29 GIISHPDAGKTTLTeklllfgGAIQlagTVKARKSARHATS----DWMEVEKQRGISVSSSVMQFE-----YAgHtinlL 99
Cdd:COG0050 16 GTIGHVDHGKTTLT-------AAIT---KVLAKKGGAKAKAydqiDKAPEEKERGITINTSHVEYEtekrhYA-H----V 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81821127 100 DTPGHQDFSEDtyrVLTA---VDAAVMVIDAAKGVETQTIKLLEVCRLRNTP-IITFINKMD 157
Cdd:COG0050 81 DCPGHADYVKN---MITGaaqMDGAILVVSATDGPMPQTREHILLARQVGVPyIVVFLNKCD 139
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
29-171 |
5.30e-06 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 48.65 E-value: 5.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 29 GIISHPDAGKTTLTeklllfgGAIQlagTVKARKSARHATS----DWMEVEKQRGISVSSSVMQFE-----YAgHtinlL 99
Cdd:PRK00049 16 GTIGHVDHGKTTLT-------AAIT---KVLAKKGGAEAKAydqiDKAPEEKARGITINTAHVEYEtekrhYA-H----V 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 100 DTPGHQDFSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTP-IITFINKMDR------------EVREsfdL 166
Cdd:PRK00049 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPyIVVFLNKCDMvddeellelvemEVRE---L 157
|
....*
gi 81821127 167 LQEIE 171
Cdd:PRK00049 158 LSKYD 162
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
33-158 |
5.85e-06 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 49.02 E-value: 5.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 33 HPDAGKTTLTEKLllfggaiqlAGTVKARKSA----RH--ATS-DWMEVEKQRGISVSSSVMQFEYAGhtinLL--DTPG 103
Cdd:PRK04004 14 HVDHGKTTLLDKI---------RGTAVAAKEAggitQHigATEvPIDVIEKIAGPLKKPLPIKLKIPG----LLfiDTPG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 81821127 104 HQDFSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTPIITFINKMDR 158
Cdd:PRK04004 81 HEAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVAANKIDR 135
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
99-158 |
9.49e-06 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 48.73 E-value: 9.49e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 99 LDTPGHQDFSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTPIITFINKMDR 158
Cdd:PRK14845 531 IDTPGHEAFTSLRKRGGSLADLAVLVVDINEGFKPQTIEAINILRQYKTPFVVAANKIDL 590
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
88-159 |
1.11e-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: 48.09 E-value: 1.11e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81821127 88 QFEYAGHTINLLDTPGHQDFSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTPIITFINKMDRE 159
Cdd:COG0532 45 QVETNGGKITFLDTPGHEAFTAMRARGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVPIIVAINKIDKP 116
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
27-175 |
1.24e-05 |
|
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: 47.99 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 27 TFGiisHPDAGKTTLteklllfggaIQ-LAGTvkarksarhATSDWMEvEKQRGISVSSSvmqfeYA------GHTINLL 99
Cdd:COG3276 5 TAG---HIDHGKTTL----------VKaLTGI---------DTDRLKE-EKKRGITIDLG-----FAylplpdGRRLGFV 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 100 DTPGHQDFsedtyrV------LTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTP-IITFINKMDR-------EVREsfd 165
Cdd:COG3276 57 DVPGHEKF------IknmlagAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKrGIVVLTKADLvdeewleLVEE--- 127
|
170
....*....|
gi 81821127 166 llqEIEEVLK 175
Cdd:COG3276 128 ---EIRELLA 134
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
29-162 |
1.81e-05 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 47.14 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 29 GIISHPDAGKTTLTeklllfgGAIQlagTVKARKSARHATS----DWMEVEKQRGISVSSSVMQFE-----YAgHtinlL 99
Cdd:PRK12735 16 GTIGHVDHGKTTLT-------AAIT---KVLAKKGGGEAKAydqiDNAPEEKARGITINTSHVEYEtanrhYA-H----V 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81821127 100 DTPGHQDFSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTP-IITFINKMDR------------EVRE 162
Cdd:PRK12735 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPyIVVFLNKCDMvddeellelvemEVRE 156
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
29-181 |
2.88e-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: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 29 GIISHPDAGKTTLTEKLLlfgGAIQLA-----GTVKARKSARhatsdwMEVEKQRgisvsssvmqfeyaghTINLLDTPG 103
Cdd:cd00880 1 AIFGRPNVGKSSLLNALL---GQNVGIvspipGTTRDPVRKE------WELLPLG----------------PVVLIDTPG 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 104 -------HQDFSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVcRLRNTPIITFINKMD-REVRESFDLLQEI--EEV 173
Cdd:cd00880 56 ldeegglGRERVEEARQVADRADLVLLVVDSDLTPVEEEAKLGLL-RERGKPVLLVLNKIDlVPESEEEELLRERklELL 134
|
....*...
gi 81821127 174 LKIDCAPI 181
Cdd:cd00880 135 PDLPVIAV 142
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
98-175 |
9.99e-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: 43.22 E-value: 9.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 98 LLDTPG--------HQDFSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTPIITFINKMDREVRESfDLLQE 169
Cdd:cd04163 55 FVDTPGihkpkkklGERMVKAAWSALKDVDLVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDLVKDKE-DLLPL 133
|
....*.
gi 81821127 170 IEEVLK 175
Cdd:cd04163 134 LEKLKE 139
|
|
| EFG_III |
pfam14492 |
Elongation Factor G, domain III; This domain is found in Elongation Factor G. It shares a ... |
425-477 |
1.22e-04 |
|
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: 40.54 E-value: 1.22e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 81821127 425 KQLQKGLQELGEEG-AIQV-FEQEGGNMLLGAVGQLQFEVVAQRLKDEYKVDAIF 477
Cdd:pfam14492 19 DKLSKALNRLLEEDpTLRVeRDEETGETILSGMGELHLEIVVDRLKRKYGVEVEL 73
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
100-157 |
1.73e-04 |
|
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and metabolism]; Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 442140 [Multi-domain] Cd Length: 430 Bit Score: 43.92 E-value: 1.73e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81821127 100 DTPGHQDF--------SedtyrvlTAvDAAVMVIDAAKGVETQT------IKLLevcRLRNtpIITFINKMD 157
Cdd:COG2895 101 DTPGHEQYtrnmvtgaS-------TA-DLAILLIDARKGVLEQTrrhsyiASLL---GIRH--VVVAVNKMD 159
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
36-169 |
1.76e-04 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 42.66 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 36 AGKTTLTEKLLlfggaiqlagtvkarksarhatSDWMEVEKQ---RGISVSSSVMQFEYAGHTINLLDTPGhQDFSEDT- 111
Cdd:COG1100 14 VGKTSLVNRLV----------------------GDIFSLEKYlstNGVTIDKKELKLDGLDVDLVIWDTPG-QDEFRETr 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81821127 112 ---YRVLTAVDAAVMVIDAAKGVETQTIK-LLEVCRLRN--TPIITFINKMDR---EVRESFDLLQE 169
Cdd:COG1100 71 qfyARQLTGASLYLFVVDGTREETLQSLYeLLESLRRLGkkSPIILVLNKIDLydeEEIEDEERLKE 137
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
28-181 |
1.77e-04 |
|
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206682 [Multi-domain] Cd Length: 174 Bit Score: 42.42 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 28 FGIISHPDAGKTTLTEKLLlfggaiqlagtvkarKSARHATSDwmevekQRGI---SVSSSvmqFEYAGHTINLLDTPG- 103
Cdd:cd01895 5 IAIIGRPNVGKSSLLNALL---------------GEERVIVSD------IAGTtrdSIDVP---FEYDGQKYTLIDTAGi 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 104 ----HQDFSEDTY---RVLTAVDAA---VMVIDAAKGVETQTIKLLEVCRLRNTPIITFINKMD-----REVRESFDllQ 168
Cdd:cd01895 61 rkkgKVTEGIEKYsvlRTLKAIERAdvvLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKWDlvekdEKTMKEFE--K 138
|
170
....*....|....
gi 81821127 169 EIEEVLK-IDCAPI 181
Cdd:cd01895 139 ELRRKLPfLDYAPI 152
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
13-199 |
3.58e-04 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 43.11 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 13 PFPPELLRDVERRRT-FGIISHPDAGKTTLTEKLLlfggaiqlagtvkarKSARHATSDwmevekQRGI---SVSSSvmq 88
Cdd:PRK00093 160 ELPEEEEEDEEDEPIkIAIIGRPNVGKSSLINALL---------------GEERVIVSD------IAGTtrdSIDTP--- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 89 FEYAGHTINLLDTPG-------HQD---FS-EDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTPIITFINK-- 155
Cdd:PRK00093 216 FERDGQKYTLIDTAGirrkgkvTEGvekYSvIRTLKAIERADVVLLVIDATEGITEQDLRIAGLALEAGRALVIVVNKwd 295
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 81821127 156 -MDREVRESFdlLQEIEEVLK-IDCAPITwPIGmGKTFRGVYHLLE 199
Cdd:PRK00093 296 lVDEKTMEEF--KKELRRRLPfLDYAPIV-FIS-ALTGQGVDKLLE 337
|
|
| Tet_II |
cd03690 |
Domain II of ribosomal protection proteins Tet(M) and Tet(O); This subfamily represents domain ... |
308-394 |
4.10e-04 |
|
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: 39.53 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 308 EAPFSGFVFKIQAnmDPKhRDRIAFFRICSGRYSSGMKVKHVRMGREMKLANALTFMANERVLMEDGVAGDIIGIHNHGQ 387
Cdd:cd03690 1 ESELSGTVFKIEY--DPK-GERLAYLRLYSGTLRLRDSVRVSGEEEKIKITELRTFENGELVKVDRVYAGDIAILVGLKS 77
|
....*..
gi 81821127 388 LHIGDTL 394
Cdd:cd03690 78 LRVGDVL 84
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
35-157 |
4.31e-04 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 42.98 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 35 DAGKTTLTEKLLLFGGAI---QLAgTVKaRKSARHATS----------DWMEVEKQRGISV-------SSSVMQFEYAgh 94
Cdd:PRK05124 37 DDGKSTLIGRLLHDTKQIyedQLA-SLH-NDSKRHGTQgekldlallvDGLQAEREQGITIdvayryfSTEKRKFIIA-- 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 81821127 95 tinllDTPGHQDFSEDTYRVLTAVDAAVMVIDAAKGVETQTIK------LLEVCRLrntpiITFINKMD 157
Cdd:PRK05124 113 -----DTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRhsfiatLLGIKHL-----VVAVNKMD 171
|
|
| FeoB |
cd01879 |
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ... |
34-199 |
4.88e-04 |
|
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) subfamily. E. coli has an iron(II) transport system, known as feo, which may make an important contribution to the iron supply of the cell under anaerobic conditions. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent.
Pssm-ID: 206667 [Multi-domain] Cd Length: 159 Bit Score: 40.90 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 34 PDAGKTTLteklllFGgaiQLAGtvkarksARHATSDW--MEVEKQRGisvsssvmQFEYAGHTINLLDTPGH---QDFS 108
Cdd:cd01879 6 PNVGKTTL------FN---ALTG-------ARQKVGNWpgVTVEKKEG--------EFKLGGKEIEIVDLPGTyslTPYS 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 109 ED---TYRVL--TAVDAAVMVIDAakgveTQ-------TIKLLEvcrlRNTPIITFINKMDREVRESFDL-LQEIEEVLK 175
Cdd:cd01879 62 EDekvARDFLlgEEPDLIVNVVDA-----TNlernlylTLQLLE----LGLPVVVALNMIDEAEKRGIKIdLDKLSELLG 132
|
170 180
....*....|....*....|....
gi 81821127 176 IDCAPITwpigmGKTFRGVYHLLE 199
Cdd:cd01879 133 VPVVPTS-----ARKGEGIDELLD 151
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
98-173 |
8.23e-04 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 41.51 E-value: 8.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 98 LLDTPG-HQ----------DFSEDTyrvLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTPIITFINKMDREVREsfDL 166
Cdd:COG1159 55 FVDTPGiHKpkrklgrrmnKAAWSA---LEDVDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDLVKKE--EL 129
|
....*..
gi 81821127 167 LQEIEEV 173
Cdd:COG1159 130 LPLLAEY 136
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
33-174 |
1.18e-03 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 41.58 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 33 HPDAGKTTLteklllfggaIQLAGTVKArksarhatsDWMEVEKQRGISVSssvmqFEYA------GHTINLLDTPGHQD 106
Cdd:PRK10512 8 HVDHGKTTL----------LQAITGVNA---------DRLPEEKKRGMTID-----LGYAywpqpdGRVLGFIDVPGHEK 63
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81821127 107 FSEDTYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTPIITF-INKMDR-------EVResfdllQEIEEVL 174
Cdd:PRK10512 64 FLSNMLAGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVaLTKADRvdeariaEVR------RQVKAVL 133
|
|
| EFG_III |
cd16262 |
Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial ... |
425-478 |
1.40e-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: 37.44 E-value: 1.40e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 81821127 425 KQLQKGLQELGEEG-AIQV-FEQEGGNMLLGAVGQLQFEVVAQRLKDEYKVDAIFE 478
Cdd:cd16262 18 DKLSKALARLAEEDpTLRVsRDEETGQTILSGMGELHLEIIVERLKREYGVEVEVG 73
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
35-157 |
1.43e-03 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 41.45 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 35 DAGKTTLTEKLLLFGGAI---QLAGTvkARKSARHATS----------DWMEVEKQRGISVSSSVMQFEYAGHTINLLDT 101
Cdd:PRK05506 34 DDGKSTLIGRLLYDSKMIfedQLAAL--ERDSKKVGTQgdeidlallvDGLAAEREQGITIDVAYRYFATPKRKFIVADT 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81821127 102 PGHQDFSEDTYRVLTAVDAAVMVIDAAKGVETQT------IKLLEVcrlRNtpIITFINKMD 157
Cdd:PRK05506 112 PGHEQYTRNMVTGASTADLAIILVDARKGVLTQTrrhsfiASLLGI---RH--VVLAVNKMD 168
|
|
| feoB |
PRK09554 |
Fe(2+) transporter permease subunit FeoB; |
27-157 |
1.62e-03 |
|
Fe(2+) transporter permease subunit FeoB;
Pssm-ID: 236563 [Multi-domain] Cd Length: 772 Bit Score: 41.24 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 27 TFGIISHPDAGKTTltekllLFGgaiQLAGtvkarksARHATSDWMevekqrGISVSSSVMQFEYAGHTINLLDTPGHQD 106
Cdd:PRK09554 5 TIGLIGNPNSGKTT------LFN---QLTG-------ARQRVGNWA------GVTVERKEGQFSTTDHQVTLVDLPGTYS 62
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81821127 107 F---SEDT---------YRVLTAVDAAVMVIDAAKgVETQ---TIKLLEVcrlrNTPIITFINKMD 157
Cdd:PRK09554 63 LttiSSQTsldeqiachYILSGDADLLINVVDASN-LERNlylTLQLLEL----GIPCIVALNMLD 123
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
98-175 |
2.29e-03 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 40.03 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 98 LLDTPG-HQ----------DFSEDTyrvLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTPIITFINKMDReVRESFDL 166
Cdd:PRK00089 57 FVDTPGiHKpkralnramnKAAWSS---LKDVDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDL-VKDKEEL 132
|
....*....
gi 81821127 167 LQEIEEVLK 175
Cdd:PRK00089 133 LPLLEELSE 141
|
|
| EngA1 |
cd01894 |
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
88-157 |
7.73e-03 |
|
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206681 [Multi-domain] Cd Length: 157 Bit Score: 37.41 E-value: 7.73e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81821127 88 QFEYAGHTINLLDTPGHQDFSED--------TYRVLTAVDAAVMVIDAAKGVETQTIKLLEVCRLRNTPIITFINKMD 157
Cdd:cd01894 39 EAEWGGREFILIDTGGIEPDDEGiskeireqAEIAIEEADVILFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKID 116
|
|
| EF2_II |
cd16268 |
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 ... |
310-382 |
8.76e-03 |
|
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 (EF-2) found in eukaryotes and archaea. 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. This translocation step is catalyzed by EF-2_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.
Pssm-ID: 293913 [Multi-domain] Cd Length: 96 Bit Score: 36.04 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81821127 310 PFSGFVFKIQANmdPKHRDRIAFFRICSGRYSSGMKV-----KHVRMGREMKLANALT----FMANERVLMEDGVAGDII 380
Cdd:cd16268 1 PLVMYVSKMVPT--DKGAGFVAFGRVFSGTVRRGQEVyilgpKYVPGKKDDLKKKRIQqtylMMGREREPVDEVPAGNIV 78
|
..
gi 81821127 381 GI 382
Cdd:cd16268 79 GL 80
|
|
| |
