|
Name |
Accession |
Description |
Interval |
E-value |
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
1-605 |
0e+00 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 991.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 1 MNMIKLRNVAIIAHVDHGKTTLVDALLRQSNTkLHKDLEGTSLIMDSNELEKERGITIFSKNASVVWKGTKINIIDTPGH 80
Cdd:COG1217 1 MMREDIRNIAIIAHVDHGKTTLVDALLKQSGT-FRENQEVAERVMDSNDLERERGITILAKNTAVRYKGVKINIVDTPGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 81 ADFGGEVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDKsilrsPDSDlkidqdqINKVIGKVFD 160
Cdd:COG1217 80 ADFGGEVERVLSMVDGVLLLVDAFEGPMPQTRFVLKKALELGLKPIVVINKIDR-----PDAR-------PDEVVDEVFD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 161 LFVELGADEDAAFFPIVYTSAKNGLAGSKPDlAEMKDISPIFEAILEHVPAPGGDPSKPLQMLATTIVGDNYKGRIATCR 240
Cdd:COG1217 148 LFIELGATDEQLDFPVVYASARNGWASLDLD-DPGEDLTPLFDTILEHVPAPEVDPDGPLQMLVTNLDYSDYVGRIAIGR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 241 IYNGRVTAGQEVTHINRIGEMKKVRLTALIGFSGLDKIDIAEAEAGDIVAIAGIEDINIGETIADANEAVALPLLDIEEP 320
Cdd:COG1217 227 IFRGTIKKGQQVALIKRDGKVEKGKITKLFGFEGLERVEVEEAEAGDIVAIAGIEDINIGDTICDPENPEALPPIKIDEP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 321 TINMTFSVNSSPFAGKEGEFKTSRQIRERLFKELETDMALKVVDGEKGD-WVVSGRGELHLAILIERLRREGYEFQVARP 399
Cdd:COG1217 307 TLSMTFSVNDSPFAGREGKFVTSRQIRERLEKELETNVALRVEETDSPDaFKVSGRGELHLSILIETMRREGYELQVSRP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 400 QVITKKIEGKTLEPFEKVFIEVPESYSGVVMQKMGERGAQLQDMT-SEKAVVLVEFIIPTRKLFGYRSEFITDTKGTGII 478
Cdd:COG1217 387 EVIFKEIDGKKLEPIEELTIDVPEEYSGAVIEKLGQRKGEMTNMEpDGGGRVRLEFLIPSRGLIGFRTEFLTDTRGTGIM 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 479 NTMFHEFRENTGSSFERSRGSLVAFQDGPTTLYGLTNAQERGTLFISPAVRIYKGQVVGQNSRVDDIKVNVCKEKQQTNM 558
Cdd:COG1217 467 NHVFDGYEPYKGEIPGRRNGSLISMETGKATAYALFNLQERGTLFIGPGTEVYEGMIVGEHSRDNDLVVNVCKEKKLTNM 546
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1087948958 559 RSKGEGVSEHFNAPKLMGLEEALEYIDDSELVEVTPENIRIRKIDLN 605
Cdd:COG1217 547 RASGSDEAIRLTPPRKMSLEQALEFIEDDELVEVTPKSIRLRKKILD 593
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
6-607 |
0e+00 |
|
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, a GTP-binding protein, is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways, but the precise function is unknown. [Regulatory functions, Other, Cellular processes, Adaptations to atypical conditions, Protein synthesis, Translation factors]
Pssm-ID: 273597 [Multi-domain] Cd Length: 594 Bit Score: 858.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 6 LRNVAIIAHVDHGKTTLVDALLRQSNTkLHKDLEGTSLIMDSNELEKERGITIFSKNASVVWKGTKINIIDTPGHADFGG 85
Cdd:TIGR01394 1 IRNIAIIAHVDHGKTTLVDALLKQSGT-FRANEAVAERVMDSNDLERERGITILAKNTAIRYNGTKINIVDTPGHADFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 86 EVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDKsilrsPDSDlkidqdqINKVIGKVFDLFVEL 165
Cdd:TIGR01394 80 EVERVLGMVDGVLLLVDASEGPMPQTRFVLKKALELGLKPIVVINKIDR-----PSAR-------PDEVVDEVFDLFAEL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 166 GADEDAAFFPIVYTSAKNGLAGSKPDlAEMKDISPIFEAILEHVPAPGGDPSKPLQMLATTIVGDNYKGRIATCRIYNGR 245
Cdd:TIGR01394 148 GADDEQLDFPIVYASGRAGWASLDLD-DPSDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVHRGT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 246 VTAGQEVTHINRIGEMKKVRLTALIGFSGLDKIDIAEAEAGDIVAIAGIEDINIGETIADANEAVALPLLDIEEPTINMT 325
Cdd:TIGR01394 227 VKKGQQVALMKRDGTIENGRISKLLGFEGLERVEIDEAGAGDIVAVAGLEDINIGETIADPEVPEALPTITVDEPTLSMT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 326 FSVNSSPFAGKEGEFKTSRQIRERLFKELETDMALKVVDGEKGD-WVVSGRGELHLAILIERLRREGYEFQVARPQVITK 404
Cdd:TIGR01394 307 FSVNDSPLAGKEGKKVTSRHIRDRLMRELETNVALRVEDTESADkFEVSGRGELHLSILIETMRREGFELQVGRPQVIYK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 405 KIEGKTLEPFEKVFIEVPESYSGVVMQKMGERGAQLQDMTSE-KAVVLVEFIIPTRKLFGYRSEFITDTKGTGIINTMFH 483
Cdd:TIGR01394 387 EIDGKKLEPIEELTIDVPEEHVGAVIEKLGKRKGEMVDMEPSgNGRTRLEFKIPSRGLIGFRTEFLTDTRGTGIMNHVFD 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 484 EFRENTGSSFERSRGSLVAFQDGPTTLYGLTNAQERGTLFISPAVRIYKGQVVGQNSRVDDIKVNVCKEKQQTNMRSKGE 563
Cdd:TIGR01394 467 EYEPWKGEIETRRNGSLVSMEDGTATAYALWNLQERGVMFVSPGTEVYEGMIIGEHSRENDLDVNPCKAKKLTNVRSSGK 546
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1087948958 564 GVSEHFNAPKLMGLEEALEYIDDSELVEVTPENIRIRKIDLNSK 607
Cdd:TIGR01394 547 DEAVKLTPPRKLSLEQALEYIEDDELVEVTPKSIRLRKRVLDPN 590
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
6-601 |
0e+00 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 545.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 6 LRNVAIIAHVDHGKTTLVDALLRQSNTkLHKDLEGTSLIMDSNELEKERGITIFSKNASVVWKGTKINIIDTPGHADFGG 85
Cdd:PRK10218 5 LRNIAIIAHVDHGKTTLVDKLLQQSGT-FDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 86 EVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDKSILRsPDSdlkidqdqinkVIGKVFDLFVEL 165
Cdd:PRK10218 84 EVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGAR-PDW-----------VVDQVFDLFVNL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 166 GADEDAAFFPIVYTSAKNGLAG-SKPDLAEmkDISPIFEAILEHVPAPGGDPSKPLQMLATTIVGDNYKGRIATCRIYNG 244
Cdd:PRK10218 152 DATDEQLDFPIVYASALNGIAGlDHEDMAE--DMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 245 RVTAGQEVTHINRIGEMKKVRLTALIGFSGLDKIDIAEAEAGDIVAIAGIEDINIGETIADANEAVALPLLDIEEPTINM 324
Cdd:PRK10218 230 KVKPNQQVTIIDSEGKTRNAKVGKVLGHLGLERIETDLAEAGDIVAITGLGELNISDTVCDTQNVEALPALSVDEPTVSM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 325 TFSVNSSPFAGKEGEFKTSRQIRERLFKELETDMALKVVDGEKGD-WVVSGRGELHLAILIERLRREGYEFQVARPQVIT 403
Cdd:PRK10218 310 FFCVNTSPFCGKEGKFVTSRQILDRLNKELVHNVALRVEETEDADaFRVSGRGELHLSVLIENMRREGFELAVSRPKVIF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 404 KKIEGKTLEPFEKVFIEVPESYSGVVMQKMGERGAQLQDMTSE-KAVVLVEFIIPTRKLFGYRSEFITDTKGTGIINTMF 482
Cdd:PRK10218 390 REIDGRKQEPYENVTLDVEEQHQGSVMQALGERKGDLKNMNPDgKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 483 HEFRE-NTGSSFERSRGSLVAFQDGPTTLYGLTNAQERGTLFISPAVRIYKGQVVGQNSRVDDIKVNVCKEKQQTNMRSK 561
Cdd:PRK10218 470 SHYDDvRPGEVGQRQNGVLISNGQGKAVAFALFGLQDRGKLFLGHGAEVYEGQIIGIHSRSNDLTVNCLTGKKLTNMRAS 549
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1087948958 562 GEGVSEHFNAPKLMGLEEALEYIDDSELVEVTPENIRIRK 601
Cdd:PRK10218 550 GTDEAVVLVPPIRMTLEQALEFIDDDELVEVTPTSIRIRK 589
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
5-212 |
7.54e-111 |
|
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: 329.94 E-value: 7.54e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 5 KLRNVAIIAHVDHGKTTLVDALLRQSNTKLHKDLEGtSLIMDSNELEKERGITIFSKNASVVWKGTKINIIDTPGHADFG 84
Cdd:cd01891 1 KIRNIAIIAHVDHGKTTLVDALLKQSGTFRENEEVG-ERVMDSNDLERERGITILAKNTAITYKDTKINIIDTPGHADFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 85 GEVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDKsilrsPDSDlkidqdqINKVIGKVFDLFVE 164
Cdd:cd01891 80 GEVERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDR-----PDAR-------PEEVVDEVFDLFLE 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1087948958 165 LGADEDAAFFPIVYTSAKNGLAGSKPDlAEMKDISPIFEAILEHVPAP 212
Cdd:cd01891 148 LNATDEQLDFPIVYASAKNGWASLNLD-DPSEDLDPLFETIIEHVPAP 194
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
7-421 |
2.29e-66 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 230.52 E-value: 2.29e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 7 RNVAIIAHVDHGKTTLVDALLRQSNTkLHKDLEGTSLIMDSNELEKERGITIFSKNASVV--WKGTK--INIIDTPGHAD 82
Cdd:PRK07560 21 RNIGIIAHIDHGKTTLSDNLLAGAGM-ISEELAGEQLALDFDEEEQARGITIKAANVSMVheYEGKEylINLIDTPGHVD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 83 FGGEVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDKSIlrspdSDLKID----QDQINKVIGKV 158
Cdd:PRK07560 100 FGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKPVLFINKVDRLI-----KELKLTpqemQQRLLKIIKDV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 159 FDLfVELGADE--------DAAFFPIVYTSAKNGLAGSKPDLAE----MKDI---------------SPIFEAIL----E 207
Cdd:PRK07560 175 NKL-IKGMAPEefkekwkvDVEDGTVAFGSALYNWAISVPMMQKtgikFKDIidyyekgkqkelaekAPLHEVVLdmvvK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 208 HVPAP-------------------------GGDPSKPLQMLATTIVGDNYKGRIATCRIYNGRVTAGQEVtHInrIGEMK 262
Cdd:PRK07560 254 HLPNPieaqkyripkiwkgdlnsevgkamlNCDPNGPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEV-YL--VGAKK 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 263 KVRLTALIGFSGLDKIDIAEAEAGDIVAIAGIEDINIGETIADANEAVAL-PLLDIEEPTInmTFSVnsspfagkegEFK 341
Cdd:PRK07560 331 KNRVQQVGIYMGPEREEVEEIPAGNIAAVTGLKDARAGETVVSVEDMTPFeSLKHISEPVV--TVAI----------EAK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 342 TSRQirerLFKELET-------DMALKV-VDGEKGDWVVSGRGELHLAILIERLRRE-GYEFQVARPQV-----ITKK-- 405
Cdd:PRK07560 399 NPKD----LPKLIEVlrqlakeDPTLVVkINEETGEHLLSGMGELHLEVITYRIKRDyGIEVVTSEPIVvyretVRGKsq 474
|
490
....*....|....*..
gi 1087948958 406 -IEGKTLEPFEKVFIEV 421
Cdd:PRK07560 475 vVEGKSPNKHNRFYISV 491
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
5-211 |
1.12e-65 |
|
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.
Pssm-ID: 425418 [Multi-domain] Cd Length: 187 Bit Score: 212.77 E-value: 1.12e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 5 KLRNVAIIAHVDHGKTTLVDALLRQSNT--KLHKDLEGTSLIMDSNELEKERGITIFSKNASVVWKGTKINIIDTPGHAD 82
Cdd:pfam00009 2 RHRNIGIIGHVDHGKTTLTDRLLYYTGAisKRGEVKGEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 83 FGGEVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDksilrspdsdlKIDQDQINKVIGKVFDLF 162
Cdd:pfam00009 82 FVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMD-----------RVDGAELEEVVEEVSREL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1087948958 163 VELgADEDAAFFPIVYTSAKNGLAgskpdlaemkdISPIFEAILEHVPA 211
Cdd:pfam00009 151 LEK-YGEDGEFVPVVPGSALKGEG-----------VQTLLDALDEYLPS 187
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
5-408 |
2.99e-65 |
|
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: 226.47 E-value: 2.99e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 5 KLRNVAIIAHVDHGKTTLVDALLRQS--NTKLHKDLEGTSlIMDSNELEKERGITIFSKNASVVWKGTKINIIDTPGHAD 82
Cdd:COG0480 8 KIRNIGIVAHIDAGKTTLTERILFYTgaIHRIGEVHDGNT-VMDWMPEEQERGITITSAATTCEWKGHKINIIDTPGHVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 83 FGGEVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKID----------------------------- 133
Cdd:COG0480 87 FTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDregadfdrvleqlkerlganpvplqlpig 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 134 --------------KSILRSPDSDLKIDQDQI------------NKVIGKV--FD------LF--VELGADE-------- 169
Cdd:COG0480 167 aeddfkgvidlvtmKAYVYDDELGAKYEEEEIpaelkeeaeearEELIEAVaeTDdelmekYLegEELTEEEikaglrka 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 170 --DAAFFPIVYTSA-KNglAGSKP-------------DLAEMKDISPIFEAILEHVPapggDPSKPLQMLATTIVGDNYK 233
Cdd:COG0480 247 tlAGKIVPVLCGSAfKN--KGVQPlldavvdylpsplDVPAIKGVDPDTGEEVERKP----DDDEPFSALVFKTMTDPFV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 234 GRIATCRIYNGRVTAGQEVTHINRigeMKKVRLTALIGFSGLDKIDIAEAEAGDIVAIAGIEDINIGETIADANEAVALP 313
Cdd:COG0480 321 GKLSFFRVYSGTLKSGSTVYNSTK---GKKERIGRLLRMHGNKREEVDEAGAGDIVAVVKLKDTTTGDTLCDEDHPIVLE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 314 LLDIEEPTINMtfSVnsspfagkegEFKTsRQIRERLFKEL----ETDMALKV-VDGEKGDWVVSGRGELHLAILIERLR 388
Cdd:COG0480 398 PIEFPEPVISV--AI----------EPKT-KADEDKLSTALaklaEEDPTFRVeTDEETGQTIISGMGELHLEIIVDRLK 464
|
490 500
....*....|....*....|....*.
gi 1087948958 389 RE-GYEFQVARPQV-----ITKKIEG 408
Cdd:COG0480 465 REfGVEVNVGKPQVayretIRKKAEA 490
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
6-455 |
5.52e-61 |
|
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]
Pssm-ID: 129581 [Multi-domain] Cd Length: 720 Bit Score: 215.53 E-value: 5.52e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 6 LRNVAIIAHVDHGKTTLVDALLRQSNTkLHKDLEGTSLIMDSNELEKERGITIFSKNASVV--WKGTK--INIIDTPGHA 81
Cdd:TIGR00490 19 IRNIGIVAHIDHGKTTLSDNLLAGAGM-ISEELAGQQLYLDFDEQEQERGITINAANVSMVheYEGNEylINLIDTPGHV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 82 DFGGEVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDKSIlrspdSDLKID----QDQINKVIGK 157
Cdd:TIGR00490 98 DFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKPVLFINKVDRLI-----NELKLTpqelQERFIKIITE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 158 VFDLFVELGADE-------DAAFFPIVYTSAKNGLAGSKPDLAE----MKDI---------------SPIFEAIL----E 207
Cdd:TIGR00490 173 VNKLIKAMAPEEfrdkwkvRVEDGSVAFGSAYYNWAISVPSMKKtgigFKDIykyckedkqkelakkSPLHQVVLdmviR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 208 HVPAP-------------------------GGDPSKPLQMLATTIVGDNYKGRIATCRIYNGRVTAGQEVTHINRigeMK 262
Cdd:TIGR00490 253 HLPSPieaqkyripviwkgdlnsevgkamlNCDPKGPLALMITKIVVDKHAGEVAVGRLYSGTIRPGMEVYIVDR---KA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 263 KVRLTALIGFSGLDKIDIAEAEAGDIVAIAGIEDINIGETIADANEAVAL--PLLDIEEPTINMTFSVNSSpfagkegef 340
Cdd:TIGR00490 330 KARIQQVGVYMGPERVEVDEIPAGNIVAVIGLKDAVAGETICTTVENITPfeSIKHISEPVVTVAIEAKNT--------- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 341 KTSRQIRERLFKELETDMALKV-VDGEKGDWVVSGRGELHLAILIERLRRE-GYEFQVARPQVITKK--------IEGKT 410
Cdd:TIGR00490 401 KDLPKLIEVLRQVAKEDPTVHVeINEETGEHLISGMGELHLEIIVEKIREDyGLDVETSPPIVVYREtvtgtspvVEGKS 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1087948958 411 LEPFEKVFIEVpESYSGVVMQKMGErgAQLQDMTSEKAVVLVEFI 455
Cdd:TIGR00490 481 PNKHNRFYIVV-EPLEESVIQAFKE--GKIVDMKMKKKERRRLLI 522
|
|
| lepA |
TIGR01393 |
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a ... |
5-487 |
2.04e-60 |
|
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a GTP-binding membrane protein related to EF-G and EF-Tu. Two types of phylogenetic tree, rooted by other GTP-binding proteins, suggest that eukaryotic homologs (including GUF1 of yeast) originated within the bacterial LepA family. The function is unknown. [Unknown function, General]
Pssm-ID: 130460 [Multi-domain] Cd Length: 595 Bit Score: 211.41 E-value: 2.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 5 KLRNVAIIAHVDHGKTTLVDALLRQSNTKLHKDLEgtSLIMDSNELEKERGITIFSKNASVVWK-----GTKINIIDTPG 79
Cdd:TIGR01393 2 NIRNFSIIAHIDHGKSTLADRLLEYTGAISEREMR--EQVLDSMDLERERGITIKAQAVRLNYKakdgeTYVLNLIDTPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 80 HADFGGEVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDksilrSPDSDLKIDQDQINKVIGkvf 159
Cdd:TIGR01393 80 HVDFSYEVSRSLAACEGALLLVDAAQGIEAQTLANVYLALENDLEIIPVINKID-----LPSADPERVKKEIEEVIG--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 160 dlfveLGADEdaaffpIVYTSAKNGLAgskpdlaemkdISPIFEAILEHVPAPGGDPSKPLQMLATTIVGDNYKGRIATC 239
Cdd:TIGR01393 152 -----LDASE------AILASAKTGIG-----------IEEILEAIVKRVPPPKGDPDAPLKALIFDSHYDNYRGVVALV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 240 RIYNGRVTAGQEVTHINrigeMKKVRLTALIGFSGLDKIDIAEAEAGD----IVAIAGIEDINIGETIADANEAVALPLL 315
Cdd:TIGR01393 210 RVFEGTIKPGDKIRFMS----TGKEYEVDEVGVFTPKLTKTDELSAGEvgyiIAGIKDVSDVRVGDTITHVKNPAKEPLP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 316 DIEEPTiNMTFsvnSSPFAGKEGEFKTSRQIRERL-------FKELETDMALKVvdGEKGDWVvsgrGELHLAILIERLR 388
Cdd:TIGR01393 286 GFKEVK-PMVF---AGLYPIDTEDYEDLRDALEKLklndaslTYEPESSPALGF--GFRCGFL----GLLHMEIIQERLE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 389 REgYEFQV--ARPQVITK---------------------KIEgKTLEPFEKVFIEVPESYSGVVMQK-MGERGAQL-QDM 443
Cdd:TIGR01393 356 RE-FNLDLitTAPSVIYRvyltngevievdnpsdlpdpgKIE-HVEEPYVKATIITPTEYLGPIMTLcQEKRGVQTnMEY 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1087948958 444 TSEKAVVLVeFIIPTrklfgyrSEFITD--------TKGTGIINTMFHEFRE 487
Cdd:TIGR01393 434 LDPNRVELI-YEMPL-------AEIVYDffdklksiSRGYASFDYELIGYRP 477
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
1-408 |
1.48e-58 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 208.27 E-value: 1.48e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 1 MNMIKLRNVAIIAHVDHGKTTLVDALLRQSNtKLHK--DLEGTSLIMDSNELEKERGITIFSKNASVVWKGTKINIIDTP 78
Cdd:PRK13351 3 MPLMQIRNIGILAHIDAGKTTLTERILFYTG-KIHKmgEVEDGTTVTDWMPQEQERGITIESAATSCDWDNHRINLIDTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 79 GHADFGGEVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDK------SILRSPDSDLKIDQDQIN 152
Cdd:PRK13351 82 GHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRvgadlfKVLEDIEERFGKRPLPLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 153 KVIGK------VFDLF------------------------------------VELGADEDAA------------------ 172
Cdd:PRK13351 162 LPIGSedgfegVVDLItepelhfsegdggstveegpipeelleeveeareklIEALAEFDDEllelylegeelsaeqlra 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 173 ----------FFPIVYTSAKNGlagskpdlaemKDISPIFEAILEHVPAP------------------GGDPSKPLQMLA 224
Cdd:PRK13351 242 plregtrsghLVPVLFGSALKN-----------IGIEPLLDAVVDYLPSPlevppprgskdngkpvkvDPDPEKPLLALV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 225 TTIVGDNYKGRIATCRIYNGRVTAGQEVTHINRigeMKKVRLTALIGFSGLDKIDIAEAEAGDIVAIAGIEDINIGETIA 304
Cdd:PRK13351 311 FKVQYDPYAGKLTYLRVYSGTLRAGSQLYNGTG---GKREKVGRLFRLQGNKREEVDRAKAGDIVAVAGLKELETGDTLH 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 305 DANEAVALPLLDIEEPTINMtfSVnsspfagkEGEFKTSRQ-IRERLFKELETDMALKV-VDGEKGDWVVSGRGELHLAI 382
Cdd:PRK13351 388 DSADPVLLELLTFPEPVVSL--AV--------EPERRGDEQkLAEALEKLVWEDPSLRVeEDEETGQTILSGMGELHLEV 457
|
490 500 510
....*....|....*....|....*....|..
gi 1087948958 383 LIERLRRE-GYEFQVARPQV-----ITKKIEG 408
Cdd:PRK13351 458 ALERLRREfKLEVNTGKPQVayretIRKMAEG 489
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
12-408 |
2.35e-58 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 207.29 E-value: 2.35e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 12 IAHVDHGKTTLVDALLRQSN--TKLHKDLEGTSLiMDSNELEKERGITIFSKNASVVWKGTKINIIDTPGHADFGGEVER 89
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGaiHRIGEVEDGTTT-MDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 90 VLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKID-------------KSILRSPDSDLKIDQDQINKVIG 156
Cdd:PRK12740 80 ALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDragadffrvlaqlQEKLGAPVVPLQLPIGEGDDFTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 157 kVFDLF---------------------------------VELGADEDAA----------------------------FFP 175
Cdd:PRK12740 160 -VVDLLsmkayrydeggpseeieipaelldraeeareelLEALAEFDDElmekylegeelseeeikaglrkatlageIVP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 176 IVYTSAKNGlAGSK----------PDLAEMKDISPIFEAILEHVPapgGDPSKPLQMLATTIVGDNYKGRIATCRIYNGR 245
Cdd:PRK12740 239 VFCGSALKN-KGVQrlldavvdylPSPLEVPPVDGEDGEEGAELA---PDPDGPLVALVFKTMDDPFVGKLSLVRVYSGT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 246 VTAGQEVTHINRigeMKKVRLTALIGFSGLDKIDIAEAEAGDIVAIAGIEDINIGETIADANEAVALPLLDIEEPTInmt 325
Cdd:PRK12740 315 LKKGDTLYNSGT---GKKERVGRLYRMHGKQREEVDEAVAGDIVAVAKLKDAATGDTLCDKGDPILLEPMEFPEPVI--- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 326 fSVNSSPfAGKEGEFKTSRQIReRLfkeLETDMALKV-VDGEKGDWVVSGRGELHLAILIERLRRE-GYEFQVARPQV-- 401
Cdd:PRK12740 389 -SLAIEP-KDKGDEEKLSEALG-KL---AEEDPTLRVeRDEETGQTILSGMGELHLDVALERLKREyGVEVETGPPQVpy 462
|
490
....*....|
gi 1087948958 402 ---ITKKIEG 408
Cdd:PRK12740 463 retIRKKAEG 472
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
1-471 |
9.45e-58 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 204.10 E-value: 9.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 1 MNMIKLRNVAIIAHVDHGKTTLVDALLRQSNTKLHKDLEgtSLIMDSNELEKERGITIFSKNASVVWK---GTK--INII 75
Cdd:COG0481 1 MDQKNIRNFSIIAHIDHGKSTLADRLLELTGTLSEREMK--EQVLDSMDLERERGITIKAQAVRLNYKakdGETyqLNLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 76 DTPGHADFGGEVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDksilrSPDSDLKIDQDQINKVI 155
Cdd:COG0481 79 DTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTLANVYLALENDLEIIPVINKID-----LPSADPERVKQEIEDII 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 156 GkvfdlfveLGADEdaaffpIVYTSAKNGLAgskpdlaemkdISPIFEAILEHVPAPGGDPSKPLQMLattIVG---DNY 232
Cdd:COG0481 154 G--------IDASD------AILVSAKTGIG-----------IEEILEAIVERIPPPKGDPDAPLQAL---IFDswyDSY 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 233 KGRIATCRIYNGRVTAGQEVT--HINRIGEMKKVrltaliGFSGLDKIDIAEAEAGDI-VAIAGI---EDINIGETIADA 306
Cdd:COG0481 206 RGVVVYVRVFDGTLKKGDKIKmmSTGKEYEVDEV------GVFTPKMTPVDELSAGEVgYIIAGIkdvRDARVGDTITLA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 307 NEAVALPLLDIEEPTiNMTFS----VNSSpfagkegEFKTSRQIRERL-------FKELETDMALkvvdgekgdwvvsG- 374
Cdd:COG0481 280 KNPAAEPLPGFKEVK-PMVFAglypVDSD-------DYEDLRDALEKLqlndaslTYEPETSAAL-------------Gf 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 375 --R----GELHLAILIERLRRE--------------------GYEFQVARPQVI--TKKIEgKTLEPFEKVFIEVPESYS 426
Cdd:COG0481 339 gfRcgflGLLHMEIIQERLEREfdldlittapsvvyevtltdGEVIEVDNPSDLpdPGKIE-EIEEPIVKATIITPSEYV 417
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1087948958 427 GVVMQKMGERGAQLQDMT--SEKAVVLVeFIIPTrklfgyrSEFITD 471
Cdd:COG0481 418 GAVMELCQEKRGVQKNMEylGENRVELT-YELPL-------AEIVFD 456
|
|
| EF-G |
TIGR00484 |
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ... |
1-409 |
8.87e-51 |
|
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: 186.55 E-value: 8.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 1 MNMIKLRNVAIIAHVDHGKTTLVDALLRQSNT--KLHKDLEGTSlIMDSNELEKERGITIFSKNASVVWKGTKINIIDTP 78
Cdd:TIGR00484 5 TDLNRFRNIGISAHIDAGKTTTTERILFYTGRihKIGEVHDGAA-TMDWMEQEKERGITITSAATTVFWKGHRINIIDTP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 79 GHADFGGEVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDK---SILRSPDS---DLKIDQDQIN 152
Cdd:TIGR00484 84 GHVDFTVEVERSLRVLDGAVAVLDAVGGVQPQSETVWRQANRYEVPRIAFVNKMDKtgaNFLRVVNQikqRLGANAVPIQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 153 KVIGK------VFDL-----------------------------------FVELGADEDAAFFP-----------IVYTS 180
Cdd:TIGR00484 164 LPIGAednfigVIDLvemkayffngdkgtkaiekeipsdlleqakelrenLVEAVAEFDEELMEkylegeeltieEIKNA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 181 AKNGLAGSKPDLAEM------KDISPIFEAILEHVPAP-------GGDPSK------------PLQMLATTIVGDNYKGR 235
Cdd:TIGR00484 244 IRKGVLNCEFFPVLCgsafknKGVQLLLDAVVDYLPSPtdvpaikGIDPDTekeierkasddePFSALAFKVATDPFVGQ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 236 IATCRIYNGRVTAGQEVTHINRigeMKKVRLTALIGFSGLDKIDIAEAEAGDIVAIAGIEDINIGETIADANEAVALPLL 315
Cdd:TIGR00484 324 LTFVRVYSGVLKSGSYVKNSRK---NKKERVGRLVKMHANNREEIKEVRAGDICAAIGLKDTTTGDTLCDPKIDVILERM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 316 DIEEPTInmtfSVNSSPFAGKEGEfktsrQIRERLFKELETDMALKV-VDGEKGDWVVSGRGELHLAILIERLRRE-GYE 393
Cdd:TIGR00484 401 EFPEPVI----SLAVEPKTKADQE-----KMGIALGKLAEEDPTFRTfTDPETGQTIIAGMGELHLDIIVDRMKREfKVE 471
|
490 500
....*....|....*....|...
gi 1087948958 394 FQVARPQV-----ITKK--IEGK 409
Cdd:TIGR00484 472 ANVGAPQVayretIRSKveVEGK 494
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
7-212 |
1.16e-50 |
|
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: 174.34 E-value: 1.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 7 RNVAIIAHVDHGKTTLVDALLrQSNTKLHKDLEGTSLIMDSNELEKERGITIFSKNASVVWKGTK---------INIIDT 77
Cdd:cd01885 1 RNICIIAHVDHGKTTLSDSLL-ASAGIISEKLAGKARYLDTREDEQERGITIKSSAISLYFEYEEekmdgndylINLIDS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 78 PGHADFGGEVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDKSILRSPDSDLKIDQ------DQI 151
Cdd:cd01885 80 PGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDRLILELKLSPEEAYQrllrivEDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1087948958 152 NKVIGKVFDlfvELGADEDAAFFP----IVYTSAKNGLAgskPDLAEMKDISPIFEAILEHVPAP 212
Cdd:cd01885 160 NAIIETYAP---EEFKQEKWKFSPqkgnVAFGSALDGWG---FTIIKFADIYAVLEMVVKHLPSP 218
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
8-212 |
5.50e-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: 171.32 E-value: 5.50e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 8 NVAIIAHVDHGKTTLVDALLRQSNTKlHKDLEGTSLIMDSNELEKERGITIFSKNASVVWKGTKINIIDTPGHADFGGEV 87
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAI-DRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 88 ERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDksilrspdsdlKIDQDQINKVIGKVFDLFVELGA 167
Cdd:cd00881 80 VRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKID-----------RVGEEDFDEVLREIKELLKLIGF 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1087948958 168 DED-AAFFPIVYTSAKNGLagskpdlaemkDISPIFEAILEHVPAP 212
Cdd:cd00881 149 TFLkGKDVPIIPISALTGE-----------GIEELLDAIVEHLPPP 183
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
7-212 |
1.25e-44 |
|
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: 156.54 E-value: 1.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 7 RNVAIIAHVDHGKTTLVDALLRQSNTKLHKDLEGTslIMDSNELEKERGITIFSKNASVVWKGTK-----INIIDTPGHA 81
Cdd:cd01890 1 RNFSIIAHIDHGKSTLADRLLELTGTVSEREMKEQ--VLDSMDLERERGITIKAQAVRLFYKAKDgeeylLNLIDTPGHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 82 DFGGEVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDksilrSPDSDLKIDQDQINKVIGkvfdl 161
Cdd:cd01890 79 DFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKID-----LPAADPDRVKQEIEDVLG----- 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1087948958 162 fveLGADEdaaffpIVYTSAKNGLAgskpdlaemkdISPIFEAILEHVPAP 212
Cdd:cd01890 149 ---LDASE------AILVSAKTGLG-----------VEDLLEAIVERIPPP 179
|
|
| BipA_III |
cd16263 |
Domain III of GTP-binding protein BipA (TypA); BipA (also called TypA) is a highly conserved ... |
320-397 |
1.41e-39 |
|
Domain III of GTP-binding protein BipA (TypA); 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. It is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion.
Pssm-ID: 293920 [Multi-domain] Cd Length: 79 Bit Score: 139.37 E-value: 1.41e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1087948958 320 PTINMTFSVNSSPFAGKEGEFKTSRQIRERLFKELETDMALKVVDGEKGD-WVVSGRGELHLAILIERLRREGYEFQVA 397
Cdd:cd16263 1 PTVSMTFGVNTSPFAGREGKFVTSRKIRDRLEKELETNVALRVEETESPDsFIVSGRGELHLSILIETMRREGFELQVS 79
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
8-133 |
5.67e-39 |
|
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: 143.15 E-value: 5.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 8 NVAIIAHVDHGKTTLVDALLRQSNT--KLHKDLEGTSlIMDSNELEKERGITIFSKNASVVWKGTKINIIDTPGHADFGG 85
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAirELGSVDKGTT-RTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1087948958 86 EVERVLKMADGCLLLVDAKEGPMPQTRfVLKRAL-EMGHKVIVVVNKID 133
Cdd:cd04168 80 EVERSLSVLDGAILVISAVEGVQAQTR-ILFRLLrKLNIPTIIFVNKID 127
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
7-212 |
2.24e-34 |
|
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: 129.70 E-value: 2.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 7 RNVAIIAHVDHGKTTLVDALLRQSNTKLHKDLEGTSLI--MDSNELEKERGITIFSKNASVVWKGTK-----INIIDTPG 79
Cdd:cd04167 1 RNVCIAGHLHHGKTSLLDMLIEQTHKRTPSVKLGWKPLryTDTRKDEQERGISIKSNPISLVLEDSKgksylINIIDTPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 80 HADFGGEVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDKSI--LRSPDSD--LKIDQ--DQINK 153
Cdd:cd04167 81 HVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDRLIleLKLPPTDayYKLRHtiDEINN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1087948958 154 VIGkvfdlfvELGADEDAAFFP----IVYTSAKNGLAGSkpdLAEMKDISPIFEAILEHVPAP 212
Cdd:cd04167 161 YIA-------SFSTTEGFLVSPelgnVLFASSKFGFCFT---LESFAKKYGLVDSILSHIPSP 213
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
220-313 |
5.82e-34 |
|
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: 124.22 E-value: 5.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 220 LQMLATTIVGDNYKGRIATCRIYNGRVTAGQEVTHINRIGEMKKVRLTALIGFSGLDKIDIAEAEAGDIVAIAGIEDINI 299
Cdd:cd03691 1 FQMLVTTLDYDDYLGRIAIGRIFSGTVKVGQQVTVVDEDGKIEKGRVTKLFGFEGLERVEVEEAEAGDIVAIAGLEDITI 80
|
90
....*....|....
gi 1087948958 300 GETIADANEAVALP 313
Cdd:cd03691 81 GDTICDPEVPEPLP 94
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
8-134 |
8.03e-33 |
|
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling phases of protein synthesis; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains both eukaryotic and bacterial members.
Pssm-ID: 206673 [Multi-domain] Cd Length: 270 Bit Score: 127.22 E-value: 8.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 8 NVAIIAHVDHGKTTLVDALLRQSNtKLHK--DLEGTSLIMDSNELEKERGITIFSKNASVVWKGTKINIIDTPGHADFGG 85
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTG-RIHKigEVHGGGATMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDFTI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1087948958 86 EVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDK 134
Cdd:cd01886 80 EVERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDR 128
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
1-158 |
1.54e-29 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 124.39 E-value: 1.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 1 MNMIKLRNVAIIAHVDHGKTTLVDALLRQSNTKLHKDlEGTSLIMDSNELEKERGITIFSKNASVVWKGTK--------- 71
Cdd:PTZ00416 14 DNPDQIRNMSVIAHVDHGKSTLTDSLVCKAGIISSKN-AGDARFTDTRADEQERGITIKSTGISLYYEHDLedgddkqpf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 72 -INIIDTPGHADFGGEVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDKSILrspdsDLKIDQDQ 150
Cdd:PTZ00416 93 lINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKVDRAIL-----ELQLDPEE 167
|
170
....*....|..
gi 1087948958 151 I----NKVIGKV 158
Cdd:PTZ00416 168 IyqnfVKTIENV 179
|
|
| BipA_TypA_C |
cd03710 |
BipA_TypA_C: a C-terminal portion of BipA or TypA having homology to the C terminal domains of ... |
412-486 |
4.72e-29 |
|
BipA_TypA_C: a C-terminal portion of BipA or TypA having homology to the C terminal domains of the elongation factors EF-G and EF-2. A member of the ribosome binding GTPase superfamily, BipA is widely distributed in bacteria and plants. BipA is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios and, is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion.
Pssm-ID: 239681 [Multi-domain] Cd Length: 79 Bit Score: 109.90 E-value: 4.72e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1087948958 412 EPFEKVFIEVPESYSGVVMQKMGERGAQLQDMTS-EKAVVLVEFIIPTRKLFGYRSEFITDTKGTGIINTMFHEFR 486
Cdd:cd03710 1 EPIEELTIDVPEEYSGAVIEKLGKRKGEMVDMEPdGNGRTRLEFKIPSRGLIGFRSEFLTDTRGTGIMNHVFDGYE 76
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
8-134 |
2.68e-26 |
|
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: 108.45 E-value: 2.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 8 NVAIIAHVDHGKTTLVDALLRQSN--TKLHKDLEGTSlIMDSNELEKERGITIFSKNASVVWKGTKINIIDTPGHADFGG 85
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGaiDRLGRVEDGNT-VSDYDPEEKKRKMSIETSVAPLEWNGHKINLIDTPGYADFVG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1087948958 86 EVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDK 134
Cdd:cd04170 80 ETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDR 128
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
6-401 |
4.78e-26 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 113.67 E-value: 4.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 6 LRNVAIIAHVDHGKTTLVDALLrQSNTKLHKDLEGTSLIMDSNELEKERGITIFSKNASVVWKGTK-------------- 71
Cdd:PLN00116 19 IRNMSVIAHVDHGKSTLTDSLV-AAAGIIAQEVAGDVRMTDTRADEAERGITIKSTGISLYYEMTDeslkdfkgerdgne 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 72 --INIIDTPGHADFGGEVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDKSILR----------- 138
Cdd:PLN00116 98 ylINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTETVLRQALGERIRPVLTVNKMDRCFLElqvdgeeayqt 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 139 ------------SPDSDLKIDQDQINKVIGKV----------FDL--FVEL-----GADEDA------------------ 171
Cdd:PLN00116 178 fsrvienanvimATYEDPLLGDVQVYPEKGTVafsaglhgwaFTLtnFAKMyaskfGVDESKmmerlwgenffdpatkkw 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 172 ------------AFFPIVYTSAKN----------------------GLAGSKPDL---AEMKDIS----PIFEAILE--- 207
Cdd:PLN00116 258 ttkntgsptckrGFVQFCYEPIKQiintcmndqkdklwpmleklgvTLKSDEKELmgkALMKRVMqtwlPASDALLEmii 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 208 -HVPAPGG-------------------------DPSKPLQMLATTIVGDNYKGR-IATCRIYNGRVTAGQEVthinRI-- 258
Cdd:PLN00116 338 fHLPSPAKaqryrvenlyegplddkyatairncDPNGPLMLYVSKMIPASDKGRfFAFGRVFSGTVATGMKV----RImg 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 259 -----GE-----MKKVRLTALIGFSGLDKIDiaEAEAGDIVAIAGIED-INIGETIADANEAVALPLLdieeptiNMTFS 327
Cdd:PLN00116 414 pnyvpGEkkdlyVKSVQRTVIWMGKKQESVE--DVPCGNTVAMVGLDQfITKNATLTNEKEVDAHPIK-------AMKFS 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 328 VnsSPFAGKEGEFKTSR---QIRERLFKELETD-MALKVVDgEKGDWVVSGRGELHLAILIERLRRE---GYEFQVARPQ 400
Cdd:PLN00116 485 V--SPVVRVAVQCKNASdlpKLVEGLKRLAKSDpMVQCTIE-ESGEHIIAGAGELHLEICLKDLQDDfmgGAEIKVSDPV 561
|
.
gi 1087948958 401 V 401
Cdd:PLN00116 562 V 562
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
8-304 |
1.38e-23 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 103.10 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 8 NVAIIAHVDHGKTTLVDAL---LRQSNTKLHKDLEGtsliMDSNELEKERGITIfsKNASVVWKGTKINI--IDTPGHAD 82
Cdd:PRK12736 14 NIGTIGHVDHGKTTLTAAItkvLAERGLNQAKDYDS----IDAAPEEKERGITI--NTAHVEYETEKRHYahVDCPGHAD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 83 FggeVERVLKMA---DGCLLLVDAKEGPMPQTR--FVLKRALEMGHkVIVVVNKIdksilrspdsDLKIDQDQINKVIGK 157
Cdd:PRK12736 88 Y---VKNMITGAaqmDGAILVVAATDGPMPQTRehILLARQVGVPY-LVVFLNKV----------DLVDDEELLELVEME 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 158 VFDLFVELGADEDAAffPIVYTSAKNGLAGSKPdlaEMKDISPIFEAILEHVPAPGGDPSKPLQMLAT---TIVGdnyKG 234
Cdd:PRK12736 154 VRELLSEYDFPGDDI--PVIRGSALKALEGDPK---WEDAIMELMDAVDEYIPTPERDTDKPFLMPVEdvfTITG---RG 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1087948958 235 RIATCRIYNGRVTAGQEVtHINRIGEMKKVRLTALIGFSGLdkidIAEAEAGDIVAI--AGI--EDINIGETIA 304
Cdd:PRK12736 226 TVVTGRVERGTVKVGDEV-EIVGIKETQKTVVTGVEMFRKL----LDEGQAGDNVGVllRGVdrDEVERGQVLA 294
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
8-304 |
5.43e-23 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 102.21 E-value: 5.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 8 NVAIIAHVDHGKTTLVDALlrqsnTKLHKDLEGTSLI----MDSNELEKERGITIFSknASVVWKGTKINI--IDTPGHA 81
Cdd:PLN03127 63 NVGTIGHVDHGKTTLTAAI-----TKVLAEEGKAKAVafdeIDKAPEEKARGITIAT--AHVEYETAKRHYahVDCPGHA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 82 DFggeVERVLKMA---DGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVV-VNKIdksilrspdsDLKIDQDQINKVIGK 157
Cdd:PLN03127 136 DY---VKNMITGAaqmDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVfLNKV----------DVVDDEELLELVEME 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 158 VFDL--FVELGADEdaafFPIVYTSAKNGLAGSKPDLAEmKDISPIFEAILEHVPAPGGDPSKPLQMLATTIVGDNYKGR 235
Cdd:PLN03127 203 LRELlsFYKFPGDE----IPIIRGSALSALQGTNDEIGK-NAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGT 277
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1087948958 236 IATCRIYNGRVTAGQEVTHIN-RIGEMKKVRLTALIGFsgldKIDIAEAEAGDIVA--IAGI--EDINIGETIA 304
Cdd:PLN03127 278 VATGRVEQGTIKVGEEVEIVGlRPGGPLKTTVTGVEMF----KKILDQGQAGDNVGllLRGLkrEDVQRGQVIC 347
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
8-304 |
4.15e-22 |
|
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: 98.70 E-value: 4.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 8 NVAIIAHVDHGKTTLVDALlrqsNTKLHKDLEGTSLI---MDSNELEKERGITIFSKNASVVWKGTKINIIDTPGHADFg 84
Cdd:TIGR00485 14 NVGTIGHVDHGKTTLTAAI----TTVLAKEGGAAARAydqIDNAPEEKARGITINTAHVEYETETRHYAHVDCPGHADY- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 85 geVERVLKMA---DGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVV-VNKIdksilrspdsDLKIDQDQINKVIGKVFD 160
Cdd:TIGR00485 89 --VKNMITGAaqmDGAILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKC----------DMVDDEELLELVEMEVRE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 161 LFVELGADEDAAffPIVYTSAKNGLAGskpDLAEMKDISPIFEAILEHVPAPGGDPSKPLQMLATTIVGDNYKGRIATCR 240
Cdd:TIGR00485 157 LLSQYDFPGDDT--PIIRGSALKALEG---DAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGR 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1087948958 241 IYNGRVTAGQEVthinRIGEMKKVRLTALIGFSGLDKIdIAEAEAGDIVAI--AGI--EDINIGETIA 304
Cdd:TIGR00485 232 VERGIIKVGEEV----EIVGLKDTRKTTVTGVEMFRKE-LDEGRAGDNVGLllRGIkrEEIERGMVLA 294
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
7-156 |
6.85e-22 |
|
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: 95.74 E-value: 6.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 7 RNVAIIAHVDHGKTTLVDALLR-----QSNTKLHKDLEGTSLIMDSNELEKERGITIFSknaSVV---WKGTKINIIDTP 78
Cdd:cd04169 3 RTFAIISHPDAGKTTLTEKLLLfggaiQEAGAVKARKSRKHATSDWMEIEKQRGISVTS---SVMqfeYKGCVINLLDTP 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1087948958 79 GHADFGGEVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDKSIlRSPDSDLkidqDQINKVIG 156
Cdd:cd04169 80 GHEDFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDREG-RDPLELL----DEIENELG 152
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
9-184 |
9.39e-22 |
|
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: 92.54 E-value: 9.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 9 VAIIAHVDHGKTTLVDALlRQSNTKlhkdlegtslimdsnelEKE-RGIT--IFSKNASVVWKGTKINIIDTPGHADFGG 85
Cdd:cd01887 3 VTVMGHVDHGKTTLLDKI-RKTNVA-----------------AGEaGGITqhIGAYQVPIDVKIPGITFIDTPGHEAFTN 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 86 EVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDKSilrspdSDLKIDQDQINKVIGKvFDLFVE- 164
Cdd:cd01887 65 MRARGASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKP------YGTEADPERVKNELSE-LGLVGEe 137
|
170 180
....*....|....*....|
gi 1087948958 165 LGADedaafFPIVYTSAKNG 184
Cdd:cd01887 138 WGGD-----VSIVPISAKTG 152
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
5-303 |
2.40e-21 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 97.90 E-value: 2.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 5 KLRNVAIIAHVDHGKTTLVDALL--------------RQSNTKlhkdleGTSLIMdsnELEKERGITIFSknaSVV---W 67
Cdd:PRK00741 9 KRRTFAIISHPDAGKTTLTEKLLlfggaiqeagtvkgRKSGRH------ATSDWM---EMEKQRGISVTS---SVMqfpY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 68 KGTKINIIDTPGHADFGGEVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDKSIlRSP------- 140
Cdd:PRK00741 77 RDCLINLLDTPGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTRKLMEVCRLRDTPIFTFINKLDRDG-REPlelldei 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 141 DSDLKIDQDQINKVIGK------VFDL---------------------FVELGADE-DAAFFPIVYTSAKNGL-----AG 187
Cdd:PRK00741 156 EEVLGIACAPITWPIGMgkrfkgVYDLyndevelyqpgeghtiqeveiIKGLDNPElDELLGEDLAEQLREELelvqgAS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 188 SKPDLAE--MKDISPIF--------------EAILEHVPAPGG--------DPSKP--------LQ--MlattivgD-NY 232
Cdd:PRK00741 236 NEFDLEAflAGELTPVFfgsalnnfgvqeflDAFVEWAPAPQPrqtderevEPTEEkfsgfvfkIQanM-------DpKH 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1087948958 233 KGRIATCRIYNGRVTAGQEVTHInRIGemKKVRLT-ALIGFSGlDKIDIAEAEAGDIVaiaGIED---INIGETI 303
Cdd:PRK00741 309 RDRIAFVRVCSGKFEKGMKVRHV-RTG--KDVRISnALTFMAQ-DREHVEEAYAGDII---GLHNhgtIQIGDTF 376
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
8-304 |
7.98e-21 |
|
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: 94.83 E-value: 7.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 8 NVAIIAHVDHGKTTLVDALlrqsnTK-LHKDLEGTSLIMDS----NElEKERGITIfskNASVVWKGTKIN---IIDTPG 79
Cdd:COG0050 14 NIGTIGHVDHGKTTLTAAI-----TKvLAKKGGAKAKAYDQidkaPE-EKERGITI---NTSHVEYETEKRhyaHVDCPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 80 HADFggeverVLKM------ADGCLLLVDAKEGPMPQTR--FVLKRALEMGHkVIVVVNKIdksilrspdsDLKIDQDQI 151
Cdd:COG0050 85 HADY------VKNMitgaaqMDGAILVVSATDGPMPQTRehILLARQVGVPY-IVVFLNKC----------DMVDDEELL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 152 NKVIGKVFDLFVELGADEDAAffPIVYTSAKNGLAGSKPDLAEmKDISPIFEAILEHVPAPGGDPSKPLQMLAT---TIV 228
Cdd:COG0050 148 ELVEMEVRELLSKYGFPGDDT--PIIRGSALKALEGDPDPEWE-KKILELMDAVDSYIPEPERDTDKPFLMPVEdvfSIT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 229 GdnyKGRIATCRIYNGRVTAGQEVtHINRIGEMKKVRLTALIGFSGLdkidIAEAEAGDIVAI--AGI--EDINIGETIA 304
Cdd:COG0050 225 G---RGTVVTGRVERGIIKVGDEV-EIVGIRDTQKTVVTGVEMFRKL----LDEGEAGDNVGLllRGIkrEDVERGQVLA 296
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
8-212 |
2.21e-20 |
|
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: 89.18 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 8 NVAIIAHVDHGKTTLVDALLR-QSNTKLHKDLEGTSLimDSNELEKERGITIfskNASVVWKGTKINI---IDTPGHADF 83
Cdd:cd01884 4 NVGTIGHVDHGKTTLTAAITKvLAKKGGAKAKKYDEI--DKAPEEKARGITI---NTAHVEYETANRHyahVDCPGHADY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 84 ggeverVLKM------ADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVV-VNKIdksilrspdsDLKIDQDQINKVIG 156
Cdd:cd01884 79 ------IKNMitgaaqMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVfLNKA----------DMVDDEELLELVEM 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1087948958 157 KVFDLFVELGADEDAAffPIVYTSAKNGLAGSKPDLAeMKDISPIFEAILEHVPAP 212
Cdd:cd01884 143 EVRELLSKYGFDGDDT--PIVRGSALKALEGDDPNKW-VDKILELLDALDSYIPTP 195
|
|
| tufA |
CHL00071 |
elongation factor Tu |
8-304 |
6.34e-20 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 92.33 E-value: 6.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 8 NVAIIAHVDHGKTTLVDA----LLRQSNTKLHKDLEgtsliMDSNELEKERGITIfsKNASVVWKGTKINI--IDTPGHA 81
Cdd:CHL00071 14 NIGTIGHVDHGKTTLTAAitmtLAAKGGAKAKKYDE-----IDSAPEEKARGITI--NTAHVEYETENRHYahVDCPGHA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 82 DFggeVERVLKMA---DGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVV-VNKIDksilrspdsdlKIDQDQINKVIGK 157
Cdd:CHL00071 87 DY---VKNMITGAaqmDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVfLNKED-----------QVDDEELLELVEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 158 -VFDLFVELGADEDaaFFPIVYTSAKNGL----AGSKPDLAEMKDISPIF---EAILEHVPAPGGDPSKPLQMLATTIVG 229
Cdd:CHL00071 153 eVRELLSKYDFPGD--DIPIVSGSALLALealtENPKIKRGENKWVDKIYnlmDAVDSYIPTPERDTDKPFLMAIEDVFS 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1087948958 230 DNYKGRIATCRIYNGRVTAGQEVThinrIGEMKKVRLTALIGFSGLDKIdIAEAEAGDIVAIA--GI--EDINIGETIA 304
Cdd:CHL00071 231 ITGRGTVATGRIERGTVKVGDTVE----IVGLRETKTTTVTGLEMFQKT-LDEGLAGDNVGILlrGIqkEDIERGMVLA 304
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
8-304 |
6.79e-20 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 92.21 E-value: 6.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 8 NVAIIAHVDHGKTTLVDALLRQSNTKLHKDLEGTSLImDSNELEKERGITIfskNASVVWKGTKIN---IIDTPGHADFg 84
Cdd:PRK12735 14 NVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQI-DNAPEEKARGITI---NTSHVEYETANRhyaHVDCPGHADY- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 85 geVERVLKMA---DGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVV-VNKIdksilrspdsDLKIDQDQINKVIGKVFD 160
Cdd:PRK12735 89 --VKNMITGAaqmDGAILVVSAADGPMPQTREHILLARQVGVPYIVVfLNKC----------DMVDDEELLELVEMEVRE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 161 LFVELGADEDAAffPIVYTSAKNGLAGSKPDLAEMKdISPIFEAILEHVPAPGGDPSKPLQMLAT---TIVGdnyKGRIA 237
Cdd:PRK12735 157 LLSKYDFPGDDT--PIIRGSALKALEGDDDEEWEAK-ILELMDAVDSYIPEPERAIDKPFLMPIEdvfSISG---RGTVV 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1087948958 238 TCRIYNGRVTAGQEVtHINRIGEMKKVRLTALIGFSGLdkidIAEAEAGDIVAI--AGI--EDINIGETIA 304
Cdd:PRK12735 231 TGRVERGIVKVGDEV-EIVGIKETQKTTVTGVEMFRKL----LDEGQAGDNVGVllRGTkrEDVERGQVLA 296
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
8-184 |
8.35e-20 |
|
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: 92.30 E-value: 8.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 8 NVAIIAHVDHGKTTLVDALL--------------RQSNTKLHKDLEGTSLIMDSNELEKERGITIfsknaSVVWKG--TK 71
Cdd:COG5256 9 NLVVIGHVDHGKSTLVGRLLyetgaidehiiekyEEEAEKKGKESFKFAWVMDRLKEERERGVTI-----DLAHKKfeTD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 72 ---INIIDTPGHADFggeverVLKM------ADGCLLLVDAKEGPMPQTR--FVLKRALEMGHkVIVVVNKIDKSilrsp 140
Cdd:COG5256 84 kyyFTIIDAPGHRDF------VKNMitgasqADAAILVVSAKDGVMGQTRehAFLARTLGINQ-LIVAVNKMDAV----- 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1087948958 141 dsdlKIDQDQINKVIGKVFDLFVELGADEDAafFPIVYTSAKNG 184
Cdd:COG5256 152 ----NYSEKRYEEVKEEVSKLLKMVGYKVDK--IPFIPVSAWKG 189
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
8-304 |
5.29e-19 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 89.48 E-value: 5.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 8 NVAIIAHVDHGKTTLVDALlrqsnTK-LHKDLEGTSLI---MDSNELEKERGITIfskNASVVWKGTKIN---IIDTPGH 80
Cdd:PRK00049 14 NVGTIGHVDHGKTTLTAAI-----TKvLAKKGGAEAKAydqIDKAPEEKARGITI---NTAHVEYETEKRhyaHVDCPGH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 81 ADFggeverVLKM------ADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVV-VNKidksilrspdSDLKIDQDQINK 153
Cdd:PRK00049 86 ADY------VKNMitgaaqMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVfLNK----------CDMVDDEELLEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 154 VIGKVFDLFVELGADEDAAffPIVYTSAKNGLAGSKPDLAEMKdISPIFEAILEHVPAPGGDPSKPLQMLAT---TIVGd 230
Cdd:PRK00049 150 VEMEVRELLSKYDFPGDDT--PIIRGSALKALEGDDDEEWEKK-ILELMDAVDSYIPTPERAIDKPFLMPIEdvfSISG- 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1087948958 231 nyKGRIATCRIYNGRVTAGQEVtHINRIGEMKKVRLTALIGFSGLdkIDiaEAEAGDIVAI--AGI--EDINIGETIA 304
Cdd:PRK00049 226 --RGTVVTGRVERGIIKVGEEV-EIVGIRDTQKTTVTGVEMFRKL--LD--EGQAGDNVGAllRGIkrEDVERGQVLA 296
|
|
| EFG_C |
pfam00679 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
411-495 |
5.97e-19 |
|
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of Elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopt a ferredoxin-like fold.
Pssm-ID: 425814 [Multi-domain] Cd Length: 88 Bit Score: 81.82 E-value: 5.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 411 LEPFEKVFIEVPESYSGVVMQKMGERGAQLQDMTS-EKAVVLVEFIIPTRKLFGYRSEFITDTKGTGIINTMFHEFRENT 489
Cdd:pfam00679 3 LEPIEKVTIDVPEEYVGDVISDLNSRRGEILDMDPdDGGRVVIEAEVPLAELFGFATELRSLTKGRGSFSMEFSGYQPVP 82
|
....*.
gi 1087948958 490 GSSFER 495
Cdd:pfam00679 83 GDILDR 88
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
7-134 |
1.60e-18 |
|
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: 82.80 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 7 RNVAIIAHVDHGKTTLVDALLRQSNTKlHKDLEGTSLiMDSNELEKERGITIfsknasvvwkgtKINIIDTPGHADF--- 83
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGNKGSI-TEYYPGTTR-NYVTTVIEEDGKTY------------KFNLLDTAGQEDYdai 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1087948958 84 ----GGEVERVLKMADGCLLLVDAKEGPMPQTRfVLKRALEMGHKVIVVVNKIDK 134
Cdd:TIGR00231 68 rrlyYPQVERSLRVFDIVILVLDVEEILEKQTK-EIIHHADSGVPIILVGNKIDL 121
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
8-176 |
2.27e-18 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 87.67 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 8 NVAIIAHVDHGKTTLVDALL--------------RQSNTKLHKDLEGTSLIMDSNELEKERGITIFSKNASVVWKGTKIN 73
Cdd:PRK12317 8 NLAVIGHVDHGKSTLVGRLLyetgaidehiieelREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDKYYFT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 74 IIDTPGHADFggeverVLKM------ADGCLLLVDAKE--GPMPQTR--FVLKRALEMGHkVIVVVNKIDksilrspdsD 143
Cdd:PRK12317 88 IVDCPGHRDF------VKNMitgasqADAAVLVVAADDagGVMPQTRehVFLARTLGINQ-LIVAINKMD---------A 151
|
170 180 190
....*....|....*....|....*....|....
gi 1087948958 144 LKIDQDQINKVIGKVFDLFVELGAD-EDAAFFPI 176
Cdd:PRK12317 152 VNYDEKRYEEVKEEVSKLLKMVGYKpDDIPFIPV 185
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
11-318 |
3.69e-18 |
|
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: 88.43 E-value: 3.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 11 IIA---HVDHGKTTLVDALlrqsnTklhkdleGTslimDSNEL--EKERGITI---FSknasvvW----KGTKINIIDTP 78
Cdd:COG3276 2 IIGtagHIDHGKTTLVKAL-----T-------GI----DTDRLkeEKKRGITIdlgFA------YlplpDGRRLGFVDVP 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 79 GHADF--------GGevervlkmADGCLLLVDAKEGPMPQTR--FVLKRALEMgHKVIVVVNKIDksilrspdsdlKIDQ 148
Cdd:COG3276 60 GHEKFiknmlagaGG--------IDLVLLVVAADEGVMPQTRehLAILDLLGI-KRGIVVLTKAD-----------LVDE 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 149 DQINKVIGKVFDLFVELGAdEDAaffPIVYTSAKNGlAGskpdLAEMKDispIFEAILEHVPAPggDPSKPLQML---AT 225
Cdd:COG3276 120 EWLELVEEEIRELLAGTFL-EDA---PIVPVSAVTG-EG----IDELRA---ALDALAAAVPAR--DADGPFRLPidrVF 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 226 TIVGdnyKGRIATCRIYNGRVTAGQEVThINRIGEMKKVRltaligfsGL---DKiDIAEAEAGDIVAI--AGI--EDIN 298
Cdd:COG3276 186 SIKG---FGTVVTGTLLSGTVRVGDELE-LLPSGKPVRVR--------GIqvhGQ-PVEEAYAGQRVALnlAGVekEEIE 252
|
330 340
....*....|....*....|
gi 1087948958 299 IGETIADANEAVALPLLDIE 318
Cdd:COG3276 253 RGDVLAAPGALRPTDRIDVR 272
|
|
| Elongation_Factor_C |
cd01514 |
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ... |
412-487 |
9.57e-18 |
|
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of elongation factors (EFs) bacterial EF-G, eukaryotic and archeal EF-2 and eukaryotic mitochondrial mtEFG1s and mtEFG2s. This group also includes proteins similar to the ribosomal protection proteins Tet(M) and Tet(O), BipA, LepA and, spliceosomal proteins: human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and yeast counterpart Snu114p. This domain adopts a ferredoxin-like fold consisting of an alpha-beta sandwich with anti-parallel beta-sheets, resembling the topology of domain III found in the elongation factors EF-G and eukaryotic EF-2, with which it forms the C-terminal block. The two domains however are not superimposable and domain III lacks some of the characteristics of this domain. EF-2/EF-G in complex with GTP, promotes the translocation step of translation. During translocation the peptidyl-tRNA is moved from the A site to the P site, the uncharged tRNA from the P site to the E-site and, the mRNA is shifted one codon relative to the ribosome. Tet(M) and Tet(O) mediate Tc resistance. Typical Tcs bind to the ribosome and inhibit the elongation phase of protein synthesis, by inhibiting the occupation of site A by aminoacyl-tRNA. Tet(M) and Tet(O) catalyze the release of tetracycline (Tc) from the ribosome in a GTP-dependent manner. BipA is a highly conserved protein with global regulatory properties in Escherichia coli. Yeast Snu114p is essential for cell viability and for splicing in vivo. Experiments suggest that GTP binding and probably GTP hydrolysis is important for the function of the U5-116 kD/Snu114p. The function of LepA proteins is unknown.
Pssm-ID: 238772 [Multi-domain] Cd Length: 79 Bit Score: 77.91 E-value: 9.57e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1087948958 412 EPFEKVFIEVPESYSGVVMQKMGERGAQLQDMTS-EKAVVLVEFIIPTRKLFGYRSEFITDTKGTGIINTMFHEFRE 487
Cdd:cd01514 1 EPIMKVEITVPEEYLGAVIGDLSKRRGEILGMEPrGTGRVVIKAELPLAEMFGFATDLRSLTQGRASFSMEFSHYEP 77
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
8-292 |
9.80e-18 |
|
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]
Pssm-ID: 129567 [Multi-domain] Cd Length: 581 Bit Score: 86.85 E-value: 9.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 8 NVAIIAHVDHGKTTLVDALLRQSNTKLHKdlegtslimdsnelEKERGITIFSKNASVVWKGTKINIIDTPGHADFGGEV 87
Cdd:TIGR00475 2 IIATAGHVDHGKTTLLKALTGIAADRLPE--------------EKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 88 ERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMG-HKVIVVVNKIDksilRSPDSDLKIDQDQINKVigkvfdlfveLG 166
Cdd:TIGR00475 68 IAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGiPHTIVVITKAD----RVNEEEIKRTEMFMKQI----------LN 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 167 ADEDAAFFPIVYTSAKNG-----LAGSKPDLAEMKDISPIfeailehvpapggdpSKPLQML---ATTIVGdnyKGRIAT 238
Cdd:TIGR00475 134 SYIFLKNAKIFKTSAKTGqgigeLKKELKNLLESLDIKRI---------------QKPLRMAidrAFKVKG---AGTVVT 195
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1087948958 239 CRIYNGRVTAGQEVtHINRIGemKKVRLTALIGFsgldKIDIAEAEAGDIVAIA 292
Cdd:TIGR00475 196 GTAFSGEVKVGDNL-RLLPIN--HEVRVKAIQAQ----NQDVEIAYAGQRIALN 242
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
14-184 |
2.10e-17 |
|
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: 79.96 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 14 HVDHGKTTLVDALlrqsntklhkdlegTSLIMDSNELEKERGITIfskNASVVW----KGTKINIIDTPGHADFggever 89
Cdd:cd04171 7 HIDHGKTTLIKAL--------------TGIETDRLPEEKKRGITI---DLGFAYldlpDGKRLGFIDVPGHEKF------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 90 VLKM------ADGCLLLVDAKEGPMPQTRFVLK--RALEMGHkVIVVVNKIDksilrspdsdlKIDQDQINKVIGKVFDL 161
Cdd:cd04171 64 VKNMlagaggIDAVLLVVAADEGIMPQTREHLEilELLGIKK-GLVVLTKAD-----------LVDEDRLELVEEEILEL 131
|
170 180
....*....|....*....|...
gi 1087948958 162 FVELGAdEDAaffPIVYTSAKNG 184
Cdd:cd04171 132 LAGTFL-ADA---PIFPVSSVTG 150
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
8-176 |
4.08e-17 |
|
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: 80.61 E-value: 4.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 8 NVAIIAHVDHGKTTLVDALL--------------RQSNTKLHKDLEGTSLIMDSNELEKERGITIFSKNASVVWKGTKIN 73
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLyklggvdkrtiekyEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 74 IIDTPGHADFggeverVLKM------ADGCLLLVDAKEG-------PMPQTR--FVLKRALEMGHkVIVVVNKIDksilr 138
Cdd:cd01883 81 IIDAPGHRDF------VKNMitgasqADVAVLVVSARKGefeagfeKGGQTRehALLARTLGVKQ-LIVAVNKMD----- 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 1087948958 139 spDSDLKIDQDQINKVIGKVFDLFVELG-ADEDAAFFPI 176
Cdd:cd01883 149 --DVTVNWSQERYDEIKKKVSPFLKKVGyNPKDVPFIPI 185
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
8-299 |
2.45e-16 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 81.97 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 8 NVAIIAHVDHGKTTLVDALLRQ----SNTKLHKDLEgtsliMDSNELEKERGITIFSKNASVVWKGTKINIIDTPGHADF 83
Cdd:PLN03126 83 NIGTIGHVDHGKTTLTAALTMAlasmGGSAPKKYDE-----IDAAPEERARGITINTATVEYETENRHYAHVDCPGHADY 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 84 GGEVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMG-HKVIVVVNKidksilrspdSDLKIDQDQINKVIGKVFDLF 162
Cdd:PLN03126 158 VKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGvPNMVVFLNK----------QDQVDDEELLELVELEVRELL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 163 VELGADEDAafFPIVYTSAKNGLAG--SKPDL--AEMKDISPIFE---AILEHVPAPGGDPSKPLQMLATTIVGDNYKGR 235
Cdd:PLN03126 228 SSYEFPGDD--IPIISGSALLALEAlmENPNIkrGDNKWVDKIYElmdAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGT 305
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1087948958 236 IATCRIYNGRVTAGQEVThinrIGEMKKVRLTALIGFSGLDKIdIAEAEAGDIVAI--AGIEDINI 299
Cdd:PLN03126 306 VATGRVERGTVKVGETVD----IVGLRETRSTTVTGVEMFQKI-LDEALAGDNVGLllRGIQKADI 366
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
8-223 |
8.43e-15 |
|
translation initiation factor 2 subunit gamma; This model represents the archaeal translation initiation factor 2 subunit gamma and is found in all known archaea. eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.
Pssm-ID: 274720 [Multi-domain] Cd Length: 406 Bit Score: 76.63 E-value: 8.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 8 NVAIIAHVDHGKTTLVDALlrqsntklhkdlegTSLIMDSNELEKERGITI--------------------FSKNASVVW 67
Cdd:TIGR03680 6 NIGMVGHVDHGKTTLTKAL--------------TGVWTDTHSEELKRGISIrlgyadaeiykcpecdgpecYTTEPVCPN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 68 KGT------KINIIDTPGHADFGGEVERVLKMADGCLLLVDAKEG-PMPQTRFVLKrALE-MGHKVIVVV-NKIDksiLR 138
Cdd:TIGR03680 72 CGSetellrRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLM-ALEiIGIKNIVIVqNKID---LV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 139 SPDSDLKiDQDQINKvigkvfdlFVELGADEDAaffPIVYTSAKNGLagskpdlaemkDISPIFEAILEHVPAPGGDPSK 218
Cdd:TIGR03680 148 SKEKALE-NYEEIKE--------FVKGTVAENA---PIIPVSALHNA-----------NIDALLEAIEKFIPTPERDLDK 204
|
....*
gi 1087948958 219 PLQML 223
Cdd:TIGR03680 205 PPLMY 209
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
11-309 |
1.90e-14 |
|
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: 75.89 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 11 IIA-HVDHGKTTLV---------------DALLRQS----NTKLhkDLegtSLIMDSNELEKERGITI------FSknas 64
Cdd:COG2895 21 ITCgSVDDGKSTLIgrllydtksifedqlAALERDSkkrgTQEI--DL---ALLTDGLQAEREQGITIdvayryFS---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 65 vvwkgT---KINIIDTPGHADFggevervLK-M------ADGCLLLVDAKEGPMPQTR---FVLkrALeMG-HKVIVVVN 130
Cdd:COG2895 92 -----TpkrKFIIADTPGHEQY-------TRnMvtgastADLAILLIDARKGVLEQTRrhsYIA--SL-LGiRHVVVAVN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 131 KIDksiLrspdsdLKIDQDQINKVIGKVFDLFVELGAdEDAAFFPIvytSAKNGlagskpD-LAEMKDISPIFE-----A 204
Cdd:COG2895 157 KMD---L------VDYSEEVFEEIVADYRAFAAKLGL-EDITFIPI---SALKG------DnVVERSENMPWYDgptllE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 205 ILEHVPAPGGDPSKPLQMLATTIVGDN-----YKGRIATcriynGRVTAGQEVTHinrIGEMKKVRLTALIGFSGldkiD 279
Cdd:COG2895 218 HLETVEVAEDRNDAPFRFPVQYVNRPNldfrgYAGTIAS-----GTVRVGDEVVV---LPSGKTSTVKSIVTFDG----D 285
|
330 340 350
....*....|....*....|....*....|..
gi 1087948958 280 IAEAEAGDIVAIAGIEDINI--GETIADANEA 309
Cdd:COG2895 286 LEEAFAGQSVTLTLEDEIDIsrGDVIVAADAP 317
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
8-184 |
3.15e-14 |
|
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN.
Pssm-ID: 206729 [Multi-domain] Cd Length: 209 Bit Score: 71.83 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 8 NVAIIAHVDHGKTTLVDALLRQSNTKLHKDLE--------GT-------SLIMDSNELEKERGITI------FSKNASvv 66
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSIFEDQLAalerskssGTqgekldlALLVDGLQAEREQGITIdvayryFSTPKR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 67 wkgtKINIIDTPGHADFggevervLK-MADG------CLLLVDAKEGPMPQTR---FVLkRALEMGHkVIVVVNKIDKsi 136
Cdd:cd04166 79 ----KFIIADTPGHEQY-------TRnMVTGastadlAILLVDARKGVLEQTRrhsYIA-SLLGIRH-VVVAVNKMDL-- 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1087948958 137 lrspdsdLKIDQDQINKvIGKVFDLFVELGADEDAAFFPIvytSAKNG 184
Cdd:cd04166 144 -------VDYDEEVFEE-IKADYLAFAASLGIEDITFIPI---SALEG 180
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
8-223 |
1.14e-13 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 73.35 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 8 NVAIIAHVDHGKTTLVDALlrqsntklhkdlegTSLIMDSNELEKERGITI--------FSK-------NASVVWK---- 68
Cdd:PRK04000 11 NIGMVGHVDHGKTTLVQAL--------------TGVWTDRHSEELKRGITIrlgyadatIRKcpdceepEAYTTEPkcpn 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 69 -GT------KINIIDTPGHadfggeveRVLkMA---------DGCLLLVDAKEG-PMPQTRFVLKrALE-MGHKVIVVV- 129
Cdd:PRK04000 77 cGSetellrRVSFVDAPGH--------ETL-MAtmlsgaalmDGAILVIAANEPcPQPQTKEHLM-ALDiIGIKNIVIVq 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 130 NKIDksiLRSPDSDLKiDQDQINKvigkvfdlFVELGADEDAaffPIVYTSAKNGLagskpdlaemkDISPIFEAILEHV 209
Cdd:PRK04000 147 NKID---LVSKERALE-NYEQIKE--------FVKGTVAENA---PIIPVSALHKV-----------NIDALIEAIEEEI 200
|
250
....*....|....
gi 1087948958 210 PAPGGDPSKPLQML 223
Cdd:PRK04000 201 PTPERDLDKPPRMY 214
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
10-207 |
3.01e-13 |
|
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: 67.87 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 10 AIIAHVDHGKTTLVDALLRQSNTKlhkdlegtslimDSNELEKERGITIFSKnaSVVWKGTKINIIDTPGHADFGG---- 85
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGGEVGE------------VSDVPGTTRDPDVYVK--ELDKGKVKLVLVDTPGLDEFGGlgre 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 86 -EVERVLKMADGCLLLVDAKEGPMP--QTRFVLKRALEMGHKVIVVVNKIDksiLRSPDSDLKIDQDQINKVIGKVfdlf 162
Cdd:cd00882 67 eLARLLLRGADLILLVVDSTDRESEedAKLLILRRLRKEGIPIILVGNKID---LLEEREVEELLRLEELAKILGV---- 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1087948958 163 velgadedaaffPIVYTSAKNGlagskpdlaemKDISPIFEAILE 207
Cdd:cd00882 140 ------------PVFEVSAKTG-----------EGVDELFEKLIE 161
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
9-134 |
2.15e-12 |
|
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: 69.66 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 9 VAIIAHVDHGKTTLVDALlRQSNTklhkdlegtslimdsneLEKE-RGIT--IfskNAS-VVWKGTKINIIDTPGHADF- 83
Cdd:COG0532 7 VTVMGHVDHGKTSLLDAI-RKTNV-----------------AAGEaGGITqhI---GAYqVETNGGKITFLDTPGHEAFt 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1087948958 84 -----GGEVervlkmADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDK 134
Cdd:COG0532 66 amrarGAQV------TDIVILVVAADDGVMPQTIEAINHAKAAGVPIIVAINKIDK 115
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
8-184 |
2.50e-12 |
|
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: 65.85 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 8 NVAIIAHVDHGKTTLVDALLRQSNTKLHkdlegtslimDSNELEKERGITI---FS-----------KNASVVWKGTKIN 73
Cdd:cd01889 2 NVGLLGHVDSGKTSLAKALSEIASTAAF----------DKNPQSQERGITLdlgFSsfevdkpkhleDNENPQIENYQIT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 74 IIDTPGHADFGGEVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDKsilrSPDSDLKIDQDQINK 153
Cdd:cd01889 72 LVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDL----IPEEERKRKIEKMKK 147
|
170 180 190
....*....|....*....|....*....|.
gi 1087948958 154 VIGKVFDLFVELGAdedaaffPIVYTSAKNG 184
Cdd:cd01889 148 RLQKTLEKTRLKDS-------PIIPVSAKPG 171
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
9-206 |
3.89e-12 |
|
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]
Pssm-ID: 273102 [Multi-domain] Cd Length: 587 Bit Score: 69.03 E-value: 3.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 9 VAIIAHVDHGKTTLVDALlrqSNTKL-HKDLEGTSLIMDSNELEKErgitifsknasvvwKGTKINIIDTPGHADFGGEV 87
Cdd:TIGR00487 90 VTIMGHVDHGKTSLLDSI---RKTKVaQGEAGGITQHIGAYHVENE--------------DGKMITFLDTPGHEAFTSMR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 88 ERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDKsilrsPDSDLKIDQDQINKvigkvFDLF-VELG 166
Cdd:TIGR00487 153 ARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVPIIVAINKIDK-----PEANPDRVKQELSE-----YGLVpEDWG 222
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1087948958 167 AdeDAAFFPIvytSAKNGlagskpdlaemKDISPIFEAIL 206
Cdd:TIGR00487 223 G--DTIFVPV---SALTG-----------DGIDELLDMIL 246
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
9-331 |
4.63e-12 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 69.09 E-value: 4.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 9 VAIIAHVDHGKTTLVDAlLRQSNTKlhkdlegtslimdsnelEKER-GITIFSKNASVVWK----GTKINIIDTPGHADF 83
Cdd:CHL00189 247 VTILGHVDHGKTTLLDK-IRKTQIA-----------------QKEAgGITQKIGAYEVEFEykdeNQKIVFLDTPGHEAF 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 84 GGEVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDKSilrspDSDLKIDQDQINKvigkvFDLFV 163
Cdd:CHL00189 309 SSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKA-----NANTERIKQQLAK-----YNLIP 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 164 E-LGADedaafFPIVYTSAKNGlagskpdlaemKDISPIFEAI-----LEHVPApggDPSKPLQ--MLATTIvgDNYKGR 235
Cdd:CHL00189 379 EkWGGD-----TPMIPISASQG-----------TNIDKLLETIlllaeIEDLKA---DPTQLAQgiILEAHL--DKTKGP 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 236 IATCRIYNGRVTAGQEVThinrIGE-MKKVRltALIGFSGlDKIDiaEAEAGDIVAIAGIEDINIGETIA-------DAN 307
Cdd:CHL00189 438 VATILVQNGTLHIGDIIV----IGTsYAKIR--GMINSLG-NKIN--LATPSSVVEIWGLSSVPATGEHFqvfnsekEAK 508
|
330 340
....*....|....*....|....*
gi 1087948958 308 EAVAL-PLLDIEEPTINMTFSVNSS 331
Cdd:CHL00189 509 LKIIKnKENNKKDTTKRITLSTTKT 533
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
1-208 |
2.42e-11 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 62.69 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 1 MNMIKlrnVAIIAHVDHGKTTLVDALLRQSNTKlhKDLEGTslimdsnelekeRGITIFSKNASVVWKGTKINIIDTPGH 80
Cdd:COG1100 1 MGEKK---IVVVGTGGVGKTSLVNRLVGDIFSL--EKYLST------------NGVTIDKKELKLDGLDVDLVIWDTPGQ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 81 ADF---GGEVERVLKMADGCLLLVDakeGPMPQTRFVLKRALEM------GHKVIVVVNKIDksilRSPDSDLKiDQDQI 151
Cdd:COG1100 64 DEFretRQFYARQLTGASLYLFVVD---GTREETLQSLYELLESlrrlgkKSPIILVLNKID----LYDEEEIE-DEERL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1087948958 152 NKVIGkvfdlfvelgadeDAAFFPIVYTSAKNGlagskpdlaemKDISPIFEAILEH 208
Cdd:COG1100 136 KEALS-------------EDNIVEVVATSAKTG-----------EGVEELFAALAEI 168
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
15-309 |
2.77e-11 |
|
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules. With members of the Rhizobiaceae family, nodQ often appears as a fusion of cysN (large subunit of ATP sulfurase) and cysC (APS kinase). [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 213679 [Multi-domain] Cd Length: 406 Bit Score: 65.86 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 15 VDHGKTTLVDALLRQSNTKLHKDLE---------GT-------SLIMDSNELEKERGITI------FSKNasvvwKGTKI 72
Cdd:TIGR02034 9 VDDGKSTLIGRLLHDTKQIYEDQLAalerdskkhGTqggeidlALLVDGLQAEREQGITIdvayryFSTD-----KRKFI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 73 nIIDTPGHADFGGEVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHK-VIVVVNKIdksilrspdsDLKIDQDQI 151
Cdd:TIGR02034 84 -VADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRhVVLAVNKM----------DLVDYDEEV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 152 NKVIGKVFDLFVELGADEDAAFFPIvytSAKNGlagskPDLAEMKDISPIFEA-----ILEHVPAPGGDPSKPLQMLATT 226
Cdd:TIGR02034 153 FENIKKDYLAFAEQLGFRDVTFIPL---SALKG-----DNVVSRSESMPWYSGptlleILETVEVERDAQDLPLRFPVQY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 227 IVGDN-----YKGRIATcriynGRVTAGQEVThinRIGEMKKVRLTALIGFSGldkiDIAEAEAGDIVAIAGIEDINI-- 299
Cdd:TIGR02034 225 VNRPNldfrgYAGTIAS-----GSVHVGDEVV---VLPSGRSSRVARIVTFDG----DLEQARAGQAVTLTLDDEIDIsr 292
|
330
....*....|
gi 1087948958 300 GETIADANEA 309
Cdd:TIGR02034 293 GDLLAAADSA 302
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
234-304 |
3.60e-11 |
|
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: 59.20 E-value: 3.60e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1087948958 234 GRIATCRIYNGRVTAGQEVT--HINRIGEMKKVRLTALIGFSGLDKIDIAEAEAGDIVAIAGIEDINIGETIA 304
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRilPNGTGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
8-223 |
4.02e-11 |
|
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal structure and biogenesis]; Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444075 [Multi-domain] Cd Length: 408 Bit Score: 65.24 E-value: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 8 NVAIIAHVDHGKTTLVDALlrqsntklhkdlegTSLIMDSNELEKERGITI--------FSK--------NASVVWK--- 68
Cdd:COG5257 7 NIGVVGHVDHGKTTLVQAL--------------TGVWTDRHSEELKRGITIrlgyadatFYKcpnceppeAYTTEPKcpn 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 69 -GTK------INIIDTPGHadfggeveRVLkMA---------DGCLLLVDAKEG-PMPQTRFVLKrALE-MGHKVIVVV- 129
Cdd:COG5257 73 cGSEtellrrVSFVDAPGH--------ETL-MAtmlsgaalmDGAILVIAANEPcPQPQTKEHLM-ALDiIGIKNIVIVq 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 130 NKIDksiLRSPDSDLKiDQDQINKvigkvfdlFVELGADEDAaffPIVYTSAKNGLagskpdlaemkDISPIFEAILEHV 209
Cdd:COG5257 143 NKID---LVSKERALE-NYEQIKE--------FVKGTVAENA---PIIPVSAQHKV-----------NIDALIEAIEEEI 196
|
250
....*....|....
gi 1087948958 210 PAPGGDPSKPLQML 223
Cdd:COG5257 197 PTPERDLSKPPRML 210
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
8-295 |
1.67e-10 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 63.80 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 8 NVAIIAHVDHGKTTLVDALLrqsnTKLHKDLEGTSLIM-DSNELEKERGIT---------------IFSKN-------AS 64
Cdd:COG5258 124 VVGVAGHVDHGKSTLVGTLV----TGKLDDGNGGTRSFlDVQPHEVERGLSadlsyavygfdddgpVRMKNplrktdrAR 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 65 VVWKGTKI-NIIDTPGHadfggevERVLKMA---------DGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDk 134
Cdd:COG5258 200 VVEESDKLvSFVDTVGH-------EPWLRTTirglvgqklDYGLLVVAADDGPTHTTREHLGILLAMDLPVIVAITKID- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 135 silrspdsdlKIDQDQINKVIGKVFDLFVELG------ADEDAAFF----------PIVYTSA--KNGLagskpdlaemk 196
Cdd:COG5258 272 ----------KVDDERVEEVEREIENLLRIVGrtplevESRHDVDAaieeingrvvPILKTSAvtGEGL----------- 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 197 disPIFEAILEHVPAPGGDPSKPLQMLattiVGDNYK----GRIATCRIYNGRVTAGQEVtHI--NRIGEMKKVRLTALi 270
Cdd:COG5258 331 ---DLLDELFERLPKRATDEDEPFLMY----IDRIYNvtgvGTVVSGTVKSGKVEAGDEL-LIgpTKDGSFREVEVKSI- 401
|
330 340
....*....|....*....|....*..
gi 1087948958 271 gfsGLDKIDIAEAEAGDIVAIA--GIE 295
Cdd:COG5258 402 ---EMHYHRVDKAEAGRIVGIAlkGVE 425
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
9-207 |
2.11e-10 |
|
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206682 [Multi-domain] Cd Length: 174 Bit Score: 59.75 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 9 VAIIAHVDHGKTTLVDALLRQsntklhkdlegTSLIMDSnelekERGITIFSKNASVVWKGTKINIIDTPG-----HADF 83
Cdd:cd01895 5 IAIIGRPNVGKSSLLNALLGE-----------ERVIVSD-----IAGTTRDSIDVPFEYDGQKYTLIDTAGirkkgKVTE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 84 GGE------VERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDKsilrspdsdLKIDQDQINKVIGK 157
Cdd:cd01895 69 GIEkysvlrTLKAIERADVVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKWDL---------VEKDEKTMKEFEKE 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1087948958 158 VFDLFVELGadedaaFFPIVYTSAKNGlagskpdlaemKDISPIFEAILE 207
Cdd:cd01895 140 LRRKLPFLD------YAPIVFISALTG-----------QGVDKLFDAIKE 172
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
8-212 |
4.14e-10 |
|
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.
Pssm-ID: 206675 [Multi-domain] Cd Length: 197 Bit Score: 59.59 E-value: 4.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 8 NVAIIAHVDHGKTTLVdallrqsntklhKDLEGTSLIMDSNELekERGITI--------FSK-------NASVVWKGT-- 70
Cdd:cd01888 2 NIGTIGHVAHGKTTLV------------KALSGVWTVRHKEEL--KRNITIklgyanakIYKcpncgcpRPYDTPECEcp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 71 ----------KINIIDTPGHadfggeveRVLkMA---------DGCLLLVDAKEG-PMPQTRFVLKrALE-MGHKVIVVV 129
Cdd:cd01888 68 gcggetklvrHVSFVDCPGH--------EIL-MAtmlsgaavmDGALLLIAANEPcPQPQTSEHLA-ALEiMGLKHIIIL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 130 -NKIDksiLRSPDSDLKiDQDQINKvigkvfdlFVELGADEDAAFFPIvytSAKNGLagskpdlaemkDISPIFEAILEH 208
Cdd:cd01888 138 qNKID---LVKEEQALE-NYEQIKE--------FVKGTIAENAPIIPI---SAQLKY-----------NIDVLCEYIVKK 191
|
....
gi 1087948958 209 VPAP 212
Cdd:cd01888 192 IPTP 195
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
8-131 |
1.29e-09 |
|
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: 56.09 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 8 NVAIIAHVDHGKTTLVDALLRQ----SNTKlhkdlegtslimdsnelekerGITIFSKNASVVWKGTKINIIDTPG---- 79
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAkaivSDYP---------------------GTTRDPNEGRLELKGKQIILVDTPGlieg 59
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1087948958 80 -HADFG-GEVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNK 131
Cdd:pfam01926 60 aSEGEGlGRAFLAIIEADLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
|
|
| EFG_mtEFG_II |
cd04088 |
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation ... |
223-305 |
2.50e-09 |
|
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation factors G1 and G2; This family represents the domain II of bacterial Elongation factor G (EF-G)and mitochondrial Elongation factors G1 (mtEFG1) and G2 (mtEFG2). During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. In bacteria this translocation step is catalyzed by EF-G_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. mtEFG1 and mtEFG2 show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. No clear phenotype has been found for mutants in the yeast homolog of mtEFG2, MEF2.
Pssm-ID: 293905 [Multi-domain] Cd Length: 83 Bit Score: 54.07 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 223 LATTIVGDNYKGRIATCRIYNGRVTAGQEVTHINRigeMKKVRLTALIGFSGLDKIDIAEAEAGDIVAIAGIEDINIGET 302
Cdd:cd04088 4 LVFKTMADPFVGKLTFFRVYSGTLKSGSTVYNSTK---GKKERVGRLLRMHGKKREEVEELGAGDIGAVVGLKDTRTGDT 80
|
...
gi 1087948958 303 IAD 305
Cdd:cd04088 81 LCD 83
|
|
| EngA1 |
cd01894 |
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
67-133 |
5.55e-09 |
|
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: 55.52 E-value: 5.55e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1087948958 67 WKGTKINIIDTPGHADFGGE--------VERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKID 133
Cdd:cd01894 42 WGGREFILIDTGGIEPDDEGiskeireqAEIAIEEADVILFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKID 116
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
8-209 |
5.56e-09 |
|
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.
Pssm-ID: 206739 [Multi-domain] Cd Length: 180 Bit Score: 56.02 E-value: 5.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 8 NVAIIAHVDHGKTTLVDALlrqsntkLHKDLEGTslimdsnelekerGITIFSKNASVVWKGTK--INIIDTPG------ 79
Cdd:cd09912 2 LLAVVGEFSAGKSTLLNAL-------LGEEVLPT-------------GVTPTTAVITVLRYGLLkgVVLVDTPGlnstie 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 80 -HADfggEVERVLKMADGCLLLVDAKEgpmPQTR----FVLKRALEMGHKVIVVVNKIDksilrspdsdlKIDQDQINKV 154
Cdd:cd09912 62 hHTE---ITESFLPRADAVIFVLSADQ---PLTEsereFLKEILKWSGKKIFFVLNKID-----------LLSEEELEEV 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1087948958 155 IGKVFDLFVELgaDEDAAFFPIVYTSAKNGLAGSKPDLAEMKDISPI--FEAILEHV 209
Cdd:cd09912 125 LEYSREELGVL--ELGGGEPRIFPVSAKEALEARLQGDEELLEQSGFeeLEEHLEEF 179
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
9-207 |
6.46e-09 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 58.52 E-value: 6.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 9 VAIIAHVDHGKTTLVDALLRQsntklhkdlegtslimdsnelekER-------GITIFSKNASVVWKGTKINIIDTPG-- 79
Cdd:PRK00093 176 IAIIGRPNVGKSSLINALLGE-----------------------ERvivsdiaGTTRDSIDTPFERDGQKYTLIDTAGir 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 80 -----HADfggeVE--------RVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDksilrspdsdlKI 146
Cdd:PRK00093 233 rkgkvTEG----VEkysvirtlKAIERADVVLLVIDATEGITEQDLRIAGLALEAGRALVIVVNKWD-----------LV 297
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1087948958 147 DQDQINKVIGKVFDLFVELGadedaaFFPIVYTSAKNGlagskpdlaemKDISPIFEAILE 207
Cdd:PRK00093 298 DEKTMEEFKKELRRRLPFLD------YAPIVFISALTG-----------QGVDKLLEAIDE 341
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
5-134 |
1.53e-08 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 57.50 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 5 KLRN--VAIIAHVDHGKTTLVDallrqsntklhkDLEGTSLImdsnelEKERG-IT-----------IFSKNASVVWKGT 70
Cdd:PRK04004 3 KLRQpiVVVLGHVDHGKTTLLD------------KIRGTAVA------AKEAGgITqhigatevpidVIEKIAGPLKKPL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 71 KINI-------IDTPGHADF------GGEVervlkmADGCLLLVDAKEGPMPQTrfvlKRALEM--GHKV--IVVVNKID 133
Cdd:PRK04004 65 PIKLkipgllfIDTPGHEAFtnlrkrGGAL------ADIAILVVDINEGFQPQT----IEAINIlkRRKTpfVVAANKID 134
|
.
gi 1087948958 134 K 134
Cdd:PRK04004 135 R 135
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
75-210 |
2.25e-08 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 55.77 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 75 IDTPG-----HAdFG----GEVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDksilrspdsdlK 145
Cdd:COG1159 56 VDTPGihkpkRK-LGrrmnKAAWSALEDVDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKID-----------L 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1087948958 146 IDQDQINKVIGKVFDLFvelgadEDAAFFPIvytSAKNGlagskpdlaemKDISPIFEAILEHVP 210
Cdd:COG1159 124 VKKEELLPLLAEYSELL------DFAEIVPI---SALKG-----------DNVDELLDEIAKLLP 168
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
65-229 |
3.92e-08 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 55.80 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 65 VVWKGTKINIIDTPG-----HADFGGE----VERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDks 135
Cdd:COG1160 45 AEWGGREFTLIDTGGiepddDDGLEAEireqAELAIEEADVILFVVDGRAGLTPLDEEIAKLLRRSGKPVILVVNKVD-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 136 ilrSPDSDLKIDQdqinkvigkvfdlFVELGADEdaaffpIVYTSAKNGLaGskpdLAEMKDispifeAILEHVPAPGG- 214
Cdd:COG1160 123 ---GPKREADAAE-------------FYSLGLGE------PIPISAEHGR-G----VGDLLD------AVLELLPEEEEe 169
|
170
....*....|....*.
gi 1087948958 215 -DPSKPLQmLAttIVG 229
Cdd:COG1160 170 eEEDDPIK-IA--IVG 182
|
|
| EFG_C |
smart00838 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
411-487 |
7.38e-08 |
|
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of Elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopt a ferredoxin-like fold.
Pssm-ID: 197906 [Multi-domain] Cd Length: 85 Bit Score: 50.19 E-value: 7.38e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1087948958 411 LEPFEKVFIEVPESYSGVVMQKMGERGAQLQDMTSEKAVVLVEFIIPTRKLFGYRSEFITDTKGTGIINTMFHEFRE 487
Cdd:smart00838 2 LEPIMKVEVTVPEEYMGDVIGDLNSRRGKIEGMEQRGGAQVIKAKVPLSEMFGYATDLRSATQGRATWSMEFSHYEE 78
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
8-250 |
9.20e-08 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 54.75 E-value: 9.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 8 NVAIIAHVDHGKTTLVDALL--------------RQSNTKLHKDLEGTSLIMDSNELEKERGITI------FSKNASVVw 67
Cdd:PTZ00141 9 NLVVIGHVDSGKSTTTGHLIykcggidkrtiekfEKEAAEMGKGSFKYAWVLDKLKAERERGITIdialwkFETPKYYF- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 68 kgtkiNIIDTPGHADFGGEVERVLKMADGCLLLVDA----------KEGpmpQTRFVLKRALEMGHK-VIVVVNKIDksi 136
Cdd:PTZ00141 88 -----TIIDAPGHRDFIKNMITGTSQADVAILVVAStagefeagisKDG---QTREHALLAFTLGVKqMIVCINKMD--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 137 lrspDSDLKIDQDQINKVIGKVFDLFVELGAD-EDAAFFPIvytsakNGLAGSkpDLAEMKDISP------IFEAiLEHV 209
Cdd:PTZ00141 157 ----DKTVNYSQERYDEIKKEVSAYLKKVGYNpEKVPFIPI------SGWQGD--NMIEKSDNMPwykgptLLEA-LDTL 223
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1087948958 210 PAPGGDPSKPLQMlattIVGDNYK-GRIATCRIynGRVTAGQ 250
Cdd:PTZ00141 224 EPPKRPVDKPLRL----PLQDVYKiGGIGTVPV--GRVETGI 259
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
11-185 |
9.30e-08 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 55.06 E-value: 9.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 11 IIA---HVDHGKTTLVDALlrqsntklhkdlegTSLIMDSNELEKERGITIFSKNAsvVW---KGTKINIIDTPGHADF- 83
Cdd:PRK10512 2 IIAtagHVDHGKTTLLQAI--------------TGVNADRLPEEKKRGMTIDLGYA--YWpqpDGRVLGFIDVPGHEKFl 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 84 -------GGevervlkmADGCLLLVDAKEGPMPQTRFVL-------KRALEmghkviVVVNKIDksilrspdsdlKIDQD 149
Cdd:PRK10512 66 snmlagvGG--------IDHALLVVACDDGVMAQTREHLailqltgNPMLT------VALTKAD-----------RVDEA 120
|
170 180 190
....*....|....*....|....*....|....*.
gi 1087948958 150 QINKVIGKVFDLFVELGADeDAAFFPivyTSAKNGL 185
Cdd:PRK10512 121 RIAEVRRQVKAVLREYGFA-EAKLFV---TAATEGR 152
|
|
| EFG_III-like |
cd16257 |
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G ... |
320-390 |
1.03e-07 |
|
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G (EF-G) and related proteins play a role in translation and share a similar domain architecture. Elongation factor EFG participates in the elongation phase during protein biosynthesis on the ribosome by stimulating translocation. Its functional cycles depend on GTP binding and its hydrolysis. Domain III is involved in the activation of GTP hydrolysis. This domain III, which is different from domain III in EF-TU and related elongation factors, is found in several translation factors, like bacterial release factors RF3, elongation factor 4, elongation factor 2, GTP-binding protein BipA and tetracycline resistance protein Tet.
Pssm-ID: 293914 [Multi-domain] Cd Length: 71 Bit Score: 49.27 E-value: 1.03e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1087948958 320 PTINMTFSVNSspfagkegeFKTSRQIRERLFKELETDMALKV-VDGEKGDWVVSGRGELHLAILIERLRRE 390
Cdd:cd16257 1 PVVFVTVEVKN---------PLDQEKLLEGLERLSEEDPALQVyREESTGEFILSGLGELHLEIIVARLERE 63
|
|
| EFG_mtEFG_C |
cd03713 |
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational ... |
412-487 |
1.74e-07 |
|
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational elongation factor (EF) EF-G. Included in this group is the C-terminus of mitochondrial Elongation factor G1 (mtEFG1) and G2 (mtEFG2) proteins. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. In bacteria this translocation step is catalyzed by EF-G_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. No clear phenotype has been found for mutants in the yeast homologue of mtEFG2, MEF2.
Pssm-ID: 239683 [Multi-domain] Cd Length: 78 Bit Score: 48.68 E-value: 1.74e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1087948958 412 EPFEKVFIEVPESYSGVVMQKMGERGAQLQDMTSEKAVVLVEFIIPTRKLFGYRSEFITDTKGTGIINTMFHEFRE 487
Cdd:cd03713 1 EPIMKVEVTVPEEYMGDVIGDLSSRRGQILGTESRGGWKVIKAEVPLAEMFGYSTDLRSLTQGRGSFTMEFSHYEE 76
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
15-184 |
2.00e-07 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 53.76 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 15 VDHGKTTLVDALLRQSN-------TKLHKDLE--GT-------SLIMDSNELEKERGITI------FSKNasvvwkGTKI 72
Cdd:PRK05124 36 VDDGKSTLIGRLLHDTKqiyedqlASLHNDSKrhGTqgekldlALLVDGLQAEREQGITIdvayryFSTE------KRKF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 73 NIIDTPGHADFggevERvlKMADG---C---LLLVDAKEGPMPQTR---FVlkrALEMGHK-VIVVVNKIDKsilrspds 142
Cdd:PRK05124 110 IIADTPGHEQY----TR--NMATGastCdlaILLIDARKGVLDQTRrhsFI---ATLLGIKhLVVAVNKMDL-------- 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1087948958 143 dLKIDQDQINKvIGKVFDLFVE-LGADEDAAFFPIvytSAKNG 184
Cdd:PRK05124 173 -VDYSEEVFER-IREDYLTFAEqLPGNLDIRFVPL---SALEG 210
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
18-134 |
2.06e-07 |
|
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: 51.09 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 18 GKTTLVDALLRQSNTKlhkdlegTSLIMdsnelekerGITIFSKNASVVWKGT-KINIIDTPGHADFGG-------EVER 89
Cdd:cd00880 9 GKSSLLNALLGQNVGI-------VSPIP---------GTTRDPVRKEWELLPLgPVVLIDTPGLDEEGGlgrerveEARQ 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1087948958 90 VLKMADGCLLLVDAKEGPMPQtRFVLKRALEMGHKVIVVVNKIDK 134
Cdd:cd00880 73 VADRADLVLLVVDSDLTPVEE-EAKLGLLRERGKPVLLVLNKIDL 116
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
9-134 |
2.46e-07 |
|
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic orthologs of bacterial IF-2. Like IF-2, it helps convey the initiator tRNA to the ribosome, although the initiator is N-formyl-Met in bacteria and Met here. This protein is not closely related to the subunits of eIF-2 of eukaryotes, which is also involved in the initiation of translation. The aIF-2 of Methanococcus jannaschii contains a large intein interrupting a region of very strongly conserved sequence very near the amino end; the alignment generated by this model does not correctly align the sequences from Methanococcus jannaschii and Pyrococcus horikoshii in this region. [Protein synthesis, Translation factors]
Pssm-ID: 273104 [Multi-domain] Cd Length: 591 Bit Score: 53.67 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 9 VAIIAHVDHGKTTLVDALlRQSNTKLHKDLEGTSLIMDSnelekERGITIFSKNASVVWKGTKINI-------IDTPGHA 81
Cdd:TIGR00491 7 VVVLGHVDHGKTTLLDKI-RGTAVVKKEAGGITQHIGAS-----EVPTDVIEKICGDLLKSFKIKLkipgllfIDTPGHE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1087948958 82 DFGGEVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDK 134
Cdd:TIGR00491 81 AFTNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTPFVVAANKIDR 133
|
|
| Tet_C |
cd03711 |
Tet_C: C-terminus of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology ... |
412-487 |
4.09e-07 |
|
Tet_C: C-terminus of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology to the C terminal domains of the elongation factors EF-G and EF-2. Tet(M) and Tet(O) catalyze the release of tetracycline (Tc) from the ribosome in a GTP-dependent manner thereby mediating Tc resistance. Tcs are broad-spectrum antibiotics. Typical Tcs bind to the ribosome and inhibit the elongation phase of protein synthesis, by inhibiting the occupation of site A by aminoacyl-tRNA.
Pssm-ID: 239682 [Multi-domain] Cd Length: 78 Bit Score: 47.62 E-value: 4.09e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1087948958 412 EPFEKVFIEVPESYSGVVMQKMGERGAQLQDMTSEKAVVLVEFIIPTRKLFGYRSEFITDTKGTGIINTMFHEFRE 487
Cdd:cd03711 1 EPYLRFELEVPQDALGRAMSDLAKMGATFEDPQIKGDEVTLEGTIPVATSQDYQSELPSYTHGEGVLETEFKGYRP 76
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
75-208 |
4.47e-07 |
|
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: 50.15 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 75 IDTPG-HADFGG-------EVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIdksilrspdsDLKI 146
Cdd:cd04163 56 VDTPGiHKPKKKlgermvkAAWSALKDVDLVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKI----------DLVK 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1087948958 147 DQDQINKVIGKVFDLFvelgadedaAFFPIVYTSAKNGlagskpdlaemKDISPIFEAILEH 208
Cdd:cd04163 126 DKEDLLPLLEKLKELH---------PFAEIFPISALKG-----------ENVDELLEYIVEY 167
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
75-210 |
6.38e-07 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 51.20 E-value: 6.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 75 IDTPG----HADFG----GEVERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDKSilrspdsdlkI 146
Cdd:PRK00089 58 VDTPGihkpKRALNramnKAAWSSLKDVDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLV----------K 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1087948958 147 DQDQINKVIGKVFDLFvelgadEDAAFFPIvytSAKNGlagskpdlaemKDISPIFEAILEHVP 210
Cdd:PRK00089 128 DKEELLPLLEELSELM------DFAEIVPI---SALKG-----------DNVDELLDVIAKYLP 171
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
8-253 |
8.35e-07 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 51.63 E-value: 8.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 8 NVAIIAHVDHGKTTLVDALL--------------RQSNTKLHKDLEGTSLIMDSNELEKERGITIfsknASVVWKGTKI- 72
Cdd:PLN00043 9 NIVVIGHVDSGKSTTTGHLIyklggidkrvierfEKEAAEMNKRSFKYAWVLDKLKAERERGITI----DIALWKFETTk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 73 ---NIIDTPGHADFGGEVERVLKMADGCLLLVDAKEGPMP-------QTRFVLKRALEMGHK-VIVVVNKIDKSilrSPd 141
Cdd:PLN00043 85 yycTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKqMICCCNKMDAT---TP- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 142 sdlKIDQDQINKVIGKVFDLFVELGADEDA-AFFPIVYTSAKNGLAGSKpDLAEMKdiSPIFEAILEHVPAPGGDPSKPL 220
Cdd:PLN00043 161 ---KYSKARYDEIVKEVSSYLKKVGYNPDKiPFVPISGFEGDNMIERST-NLDWYK--GPTLLEALDQINEPKRPSDKPL 234
|
250 260 270
....*....|....*....|....*....|...
gi 1087948958 221 QMLATTIVGDNYKGRIATCRIYNGRVTAGQEVT 253
Cdd:PLN00043 235 RLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVT 267
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
63-219 |
1.09e-06 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 51.20 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 63 ASVVWKGTKINIIDTPG----HADFGGEV----ERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDK 134
Cdd:PRK00093 42 GEAEWLGREFILIDTGGiepdDDGFEKQIreqaELAIEEADVILFVVDGRAGLTPADEEIAKILRKSNKPVILVVNKVDG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 135 SILRSPDSDlkidqdqinkvigkvfdlFVELGADEdaaFFPIvytSAKNGLaGskpdLAEMkdispiFEAILEHVPAPGG 214
Cdd:PRK00093 122 PDEEADAYE------------------FYSLGLGE---PYPI---SAEHGR-G----IGDL------LDAILEELPEEEE 166
|
....*
gi 1087948958 215 DPSKP 219
Cdd:PRK00093 167 EDEED 171
|
|
| EF2_II |
cd16268 |
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 ... |
219-305 |
1.52e-06 |
|
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: 46.83 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 219 PLQMLATTIV-GDNYKGRIATCRIYNGRVTAGQEVT------HINRIGEMKKVRLTALIGFSGLDKIDIAEAEAGDIVAI 291
Cdd:cd16268 1 PLVMYVSKMVpTDKGAGFVAFGRVFSGTVRRGQEVYilgpkyVPGKKDDLKKKRIQQTYLMMGREREPVDEVPAGNIVGL 80
|
90
....*....|....*.
gi 1087948958 292 AGIED--INIGETIAD 305
Cdd:cd16268 81 VGLDDflAKSGTTTSS 96
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
220-304 |
3.98e-06 |
|
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: 44.95 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 220 LQMLATTIVGDNYKGRIATCRIYNGRVTAGQEvthINRIGEMKKVRLTALIGFsgldKIDIAEAEAGDIVAIA--GIEDI 297
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDE---IRILPKGITGRVTSIERF----HEEVDEAKAGDIVGIGilGVKDI 73
|
....*..
gi 1087948958 298 NIGETIA 304
Cdd:cd01342 74 LTGDTLT 80
|
|
| RF3_II |
cd03689 |
Domain II of bacterial Release Factor 3; This subfamily represents domain II of bacterial ... |
231-304 |
4.80e-06 |
|
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: 44.96 E-value: 4.80e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1087948958 231 NYKGRIATCRIYNGRVTAGQEVTHiNRIGemKKVRLTALIGFSGLDKIDIAEAEAGDIVAIAGIEDINIGETIA 304
Cdd:cd03689 15 KHRDRIAFLRVCSGKFERGMKVKH-VRTG--KEVRLSNATTFMAQDRETVEEAYPGDIIGLPNHGTFQIGDTFT 85
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
18-207 |
5.76e-06 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 48.87 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 18 GKTTLVDALLRQsntklhkdlegtslimdsnelekER-------GITIFSKNASVVWKGTKINIIDTPG-------HADf 83
Cdd:COG1160 187 GKSSLINALLGE-----------------------ERvivsdiaGTTRDSIDTPFERDGKKYTLIDTAGirrkgkvDEG- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 84 ggeVE--------RVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDKsilrspdsdLKIDQDQINKVI 155
Cdd:COG1160 243 ---IEkysvlrtlRAIERADVVLLVIDATEGITEQDLKIAGLALEAGKALVIVVNKWDL---------VEKDRKTREELE 310
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1087948958 156 GKVFDLFVELgadedaAFFPIVYTSAKNGlagskpdlaemKDISPIFEAILE 207
Cdd:COG1160 311 KEIRRRLPFL------DYAPIVFISALTG-----------QGVDKLLEAVDE 345
|
|
| EFG_III |
cd16262 |
Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial ... |
348-400 |
5.91e-06 |
|
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: 44.37 E-value: 5.91e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1087948958 348 ERLFKEletDMALKV-VDGEKGDWVVSGRGELHLAILIERLRRE-GYEFQVARPQ 400
Cdd:cd16262 25 ARLAEE---DPTLRVsRDEETGQTILSGMGELHLEIIVERLKREyGVEVEVGKPQ 76
|
|
| YihA_EngB |
cd01876 |
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
69-184 |
7.26e-06 |
|
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.
Pssm-ID: 206665 [Multi-domain] Cd Length: 170 Bit Score: 46.73 E-value: 7.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 69 GTKINIIDTPG----------HADFGGEVERVLKMAD---GCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKIDks 135
Cdd:cd01876 44 GDKFRLVDLPGygyakvskevREKWGKLIEEYLENREnlkGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKAD-- 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1087948958 136 ilrspdsdlKIDQDQINKVIGKVFDLFvelgaDEDAAFFPIVYTSAKNG 184
Cdd:cd01876 122 ---------KLKKSELAKVLKKIKEEL-----NLFNILPPVILFSSKKG 156
|
|
| EFG_III |
pfam14492 |
Elongation Factor G, domain III; This domain is found in Elongation Factor G. It shares a ... |
346-390 |
9.06e-06 |
|
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: 44.01 E-value: 9.06e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1087948958 346 IRERLFKELETDMALKV-VDGEKGDWVVSGRGELHLAILIERLRRE 390
Cdd:pfam14492 21 LSKALNRLLEEDPTLRVeRDEETGETILSGMGELHLEIVVDRLKRK 66
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
15-133 |
2.75e-05 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 47.23 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 15 VDHGKTTLVDALLRQSNTkLHKD----LEGTS-------------LIMDSNELEKERGITI------FSKNASvvwkgtK 71
Cdd:PRK05506 33 VDDGKSTLIGRLLYDSKM-IFEDqlaaLERDSkkvgtqgdeidlaLLVDGLAAEREQGITIdvayryFATPKR------K 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1087948958 72 INIIDTPGHADFGGEVERVLKMADGCLLLVDAKEGPMPQTR---FvLKRALEMGHkVIVVVNKID 133
Cdd:PRK05506 106 FIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRrhsF-IASLLGIRH-VVLAVNKMD 168
|
|
| mtEFG1_II_like |
cd04091 |
Domain II of mitochondrial elongation factor G1-like proteins found in eukaryotes; Eukaryotic ... |
230-305 |
9.30e-05 |
|
Domain II of mitochondrial elongation factor G1-like proteins found in eukaryotes; Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. Eukaryotic EF-2 operates in the cytosolic protein synthesis machinery of eukaryotes, EF-Gs in protein synthesis in bacteria. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. There are two forms of mtEFG present in mammals (designated mtEFG1s and mtEFG2s); mtEFG2s are not present in this group.
Pssm-ID: 293908 [Multi-domain] Cd Length: 81 Bit Score: 41.12 E-value: 9.30e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1087948958 230 DNYKGRIATCRIYNGRVTAGQEVTHINrigEMKKVRLTALIGFSGLDKIDIAEAEAGDIVAIAGIeDINIGETIAD 305
Cdd:cd04091 10 EGRFGQLTYMRVYQGVLRKGDTIYNVR---TGKKVRVPRLVRMHSDEMEDIEEVYAGDICALFGI-DCASGDTFTD 81
|
|
| Tet_II |
cd03690 |
Domain II of ribosomal protection proteins Tet(M) and Tet(O); This subfamily represents domain ... |
235-305 |
1.17e-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: 41.07 E-value: 1.17e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1087948958 235 RIATCRIYNGRVTAGQEVTHInriGEMKKVRLTALIGFSGLDKIDIAEAEAGDIVAIAGIEDINIGETIAD 305
Cdd:cd03690 19 RLAYLRLYSGTLRLRDSVRVS---GEEEKIKITELRTFENGELVKVDRVYAGDIAILVGLKSLRVGDVLGD 86
|
|
| MnmE |
COG0486 |
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
63-184 |
5.69e-04 |
|
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440253 [Multi-domain] Cd Length: 448 Bit Score: 42.74 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 63 ASVVWKGTKINIIDTPGHADFGGEVER--------VLKMADGCLLLVDAKEGPMPQTRFVLKRALEMghKVIVVVNKIDk 134
Cdd:COG0486 254 ERINIGGIPVRLIDTAGLRETEDEVEKigierareAIEEADLVLLLLDASEPLTEEDEEILEKLKDK--PVIVVLNKID- 330
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1087948958 135 sILRSPDSDLKIDQDqinkvigkvfdlfvelgadedaafFPIVYTSAKNG 184
Cdd:COG0486 331 -LPSEADGELKSLPG------------------------EPVIAISAKTG 355
|
|
| trmE |
PRK05291 |
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; |
63-151 |
1.16e-03 |
|
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
Pssm-ID: 235392 [Multi-domain] Cd Length: 449 Bit Score: 41.63 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 63 ASVVWKGTKINIIDTPGHADFGGEVER--------VLKMADGCLLLVDAKEGPMPQTRFVLkrALEMGHKVIVVVNKIDk 134
Cdd:PRK05291 256 EHINLDGIPLRLIDTAGIRETDDEVEKigiersreAIEEADLVLLVLDASEPLTEEDDEIL--EELKDKPVIVVLNKAD- 332
|
90
....*....|....*..
gi 1087948958 135 sILRSPDSDLKIDQDQI 151
Cdd:PRK05291 333 -LTGEIDLEEENGKPVI 348
|
|
| mtEFG1_C |
cd04097 |
mtEFG1_C: C-terminus of mitochondrial Elongation factor G1 (mtEFG1)-like proteins found in ... |
412-476 |
1.50e-03 |
|
mtEFG1_C: C-terminus of mitochondrial Elongation factor G1 (mtEFG1)-like proteins found in eukaryotes. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. Eukaryotic EF-2 operates in the cytosolic protein synthesis machinery of eukaryotes, EF-Gs in protein synthesis in bacteria. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. There are two forms of mtEFG present in mammals (designated mtEFG1s and mtEFG2s) mtEFG2s are not present in this group.
Pssm-ID: 239764 [Multi-domain] Cd Length: 78 Bit Score: 37.68 E-value: 1.50e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1087948958 412 EPFEKVFIEVPESYSGVVMQKMGERGAQLQDMTSEKAVVLVEFIIPTRKLFGYRSEFITDTKGTG 476
Cdd:cd04097 1 EPIMKVEVTAPTEFQGNVIGLLNKRKGTIVDTDTGEDEFTLEAEVPLNDMFGYSTELRSMTQGKG 65
|
|
| FeoB |
cd01879 |
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ... |
55-184 |
3.19e-03 |
|
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: 38.59 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 55 GITIFSKNASVVWKGTKINIIDTPGHADFGG--EVERV------LKMADGCLLLVDAKEgpmpqtrfvLKRAL------- 119
Cdd:cd01879 29 GVTVEKKEGEFKLGGKEIEIVDLPGTYSLTPysEDEKVardfllGEEPDLIVNVVDATN---------LERNLyltlqll 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1087948958 120 EMGHKVIVVVNKIDksILRSpdSDLKIDQDQINKvigkvfdlfvELGAdedaaffPIVYTSAKNG 184
Cdd:cd01879 100 ELGLPVVVALNMID--EAEK--RGIKIDLDKLSE----------LLGV-------PVVPTSARKG 143
|
|
| MnmE_helical |
pfam12631 |
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ... |
63-184 |
3.36e-03 |
|
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An N-terminal domain, a helical domain and a GTPase domain which is nested within the helical domain. This family represents the helical domain.
Pssm-ID: 463649 [Multi-domain] Cd Length: 326 Bit Score: 39.77 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 63 ASVVWKGTKINIIDTPG---HADfggEVER--------VLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHkVIVVVNK 131
Cdd:pfam12631 135 ETINIGGIPLRLIDTAGireTDD---EVEKigierareAIEEADLVLLVLDASRPLDEEDLEILELLKDKKP-IIVVLNK 210
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1087948958 132 IdksilrspdsdlkidqdqinkvigkvfDLFVELGADEDAAFFPIVYTSAKNG 184
Cdd:pfam12631 211 S---------------------------DLLGEIDELEELKGKPVLAISAKTG 236
|
|
| AIG1 |
pfam04548 |
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria. |
52-107 |
4.32e-03 |
|
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
Pssm-ID: 398307 [Multi-domain] Cd Length: 200 Bit Score: 38.74 E-value: 4.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1087948958 52 KERGITIFSKNASVVWKGTKINIIDTPGHADFGGEVERVLKMADGCLLLvdAKEGP 107
Cdd:pfam04548 31 RAQGVTKTCQLVSRTWDGRIINVIDTPGLFDLSVSNDFISKEIIRCLLL--AEPGP 84
|
|
| MJ1464 |
cd01859 |
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ... |
87-133 |
5.95e-03 |
|
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents archaeal GTPase typified by the protein MJ1464 from Methanococcus jannaschii. The members of this family show a circular permutation of the GTPase signature motifs so that C-terminal strands 5, 6, and 7 (strands 6 contain the NKxD motif) are relocated to the N terminus.
Pssm-ID: 206752 [Multi-domain] Cd Length: 157 Bit Score: 37.68 E-value: 5.95e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1087948958 87 VERVLKMADGCLLLVDAKEGPMPQTRFVLKRALEMGHKVIVVVNKID 133
Cdd:cd01859 5 VRRIIKEADVVLEVVDARDPELTRSRKLERMALELGKKLIIVLNKAD 51
|
|
| PRK09518 |
PRK09518 |
bifunctional cytidylate kinase/GTPase Der; Reviewed |
67-133 |
6.39e-03 |
|
bifunctional cytidylate kinase/GTPase Der; Reviewed
Pssm-ID: 236546 [Multi-domain] Cd Length: 712 Bit Score: 39.39 E-value: 6.39e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1087948958 67 WKGTKINIIDTPG--------HADFGGEVERVLKMADGCLLLVDAKEGPMpQTRFVLKRALEMGHK-VIVVVNKID 133
Cdd:PRK09518 320 WAGTDFKLVDTGGweadvegiDSAIASQAQIAVSLADAVVFVVDGQVGLT-STDERIVRMLRRAGKpVVLAVNKID 394
|
|
| mtEFG2_II_like |
cd04092 |
Domain II of mitochondrial elongation factor G2-like proteins found in eukaryotes; Eukaryotic ... |
223-303 |
7.86e-03 |
|
Domain II of mitochondrial elongation factor G2-like proteins found in eukaryotes; Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. Eukaryotic EF-2 operates in the cytosolic protein synthesis machinery of eukaryotes, EF-Gs in protein synthesis in bacteria. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. No clear phenotype has been found for mutants in the yeast homolog of mtEFG2, MEF2. There are two forms of mtEFG present in mammals (designated mtEFG1s and mtEFG2s); mtEFG1s are not present in this group.
Pssm-ID: 293909 [Multi-domain] Cd Length: 83 Bit Score: 35.76 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 223 LATTIVGDNYKGRIATCRIYNGRVTAGQEVTHINRigeMKKVRLTALIGFSGLDKIDIAEAEAGDIVAIAGIEDINIGET 302
Cdd:cd04092 4 LAFKVIHDPQRGPLVFVRVYSGTLKAGSNVYNTTT---GKKERISRLLKMHADQTEEVDSLSAGNIGVITGLKVTSTGDT 80
|
.
gi 1087948958 303 I 303
Cdd:cd04092 81 L 81
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|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
63-184 |
8.12e-03 |
|
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.
Pssm-ID: 206727 [Multi-domain] Cd Length: 159 Bit Score: 37.47 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087948958 63 ASVVWKGTKINIIDTPGHADFGGEVERV--------LKMADGCLLLVDAKEGPmpQTRFVLKRALEMGHKVIVVVNKIdk 134
Cdd:cd04164 44 EEIDLGGIPVRLIDTAGLRETEDEIEKIgierareaIEEADLVLLVVDASEGL--DEEDLEILELPAKKPVIVVLNKS-- 119
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1087948958 135 silrspdsDLKIDQDQINKVIGKvfdlfvelgadedaaffPIVYTSAKNG 184
Cdd:cd04164 120 --------DLLSDAEGISELNGK-----------------PIIAISAKTG 144
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