|
Name |
Accession |
Description |
Interval |
E-value |
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
1-606 |
0e+00 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 1130.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 1 MEIRNIAIIAHVDHGKTTLLDGILRQTGAVTAKED-GERIMDSNDLEKEKGITIKAKNTAVVYKGTRINVVDTPGHADFG 79
Cdd:COG1217 4 EDIRNIAIIAHVDHGKTTLVDALLKQSGTFRENQEvAERVMDSNDLERERGITILAKNTAVRYKGVKINIVDTPGHADFG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 80 GEVERVLATADSCLLLVDAFDGPMPQTRFVLGKSLQLGHRPILVINKIDRPGARPEAVVDMAFDLFSDLGATDEQLDFPI 159
Cdd:COG1217 84 GEVERVLSMVDGVLLLVDAFEGPMPQTRFVLKKALELGLKPIVVINKIDRPDARPDEVVDEVFDLFIELGATDEQLDFPV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 160 VYASAKQGWAVHNLSEsPGTNLDPLLDTVLKHVPPVQADTEAPLQFQVTSLDYNDYVGRIAVGKIYAGKMALGMNVIQLA 239
Cdd:COG1217 164 VYASARNGWASLDLDD-PGEDLTPLFDTILEHVPAPEVDPDGPLQMLVTNLDYSDYVGRIAIGRIFRGTIKKGQQVALIK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 240 AK-KTETapsadtalFRITKLYNFEGLKRNEVNAAEAGDIVAIAGLPDVFIGDTICEPGKPAPRPAIEVEEPTVSMFFMV 318
Cdd:COG1217 243 RDgKVEK--------GKITKLFGFEGLERVEVEEAEAGDIVAIAGIEDINIGDTICDPENPEALPPIKIDEPTLSMTFSV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 319 NNSPFAGKEGKFVTTRNIRERLDRELETNVAMRLEETEDKDRFKVLGRGELHLSVLIETMRREGFEIQVSRPEVILKTnE 398
Cdd:COG1217 315 NDSPFAGREGKFVTSRQIRERLEKELETNVALRVEETDSPDAFKVSGRGELHLSILIETMRREGYELQVSRPEVIFKE-I 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 399 QGQKLEPYEYLVMDVPDQFTGAIIAELNRRKGELQLMDAHPSGMTRVEFVIPTRGIIGFRGFFISETRGEGVMSSRFLRF 478
Cdd:COG1217 394 DGKKLEPIEELTIDVPEEYSGAVIEKLGQRKGEMTNMEPDGGGRVRLEFLIPSRGLIGFRTEFLTDTRGTGIMNHVFDGY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 479 DVYKGEIPGRKNGALISMDSGESTAYALWKIQERGELVIGPNTSVYPGMIIGIHSRDNDLEVNPVKEKKLSNVRSSGADE 558
Cdd:COG1217 474 EPYKGEIPGRRNGSLISMETGKATAYALFNLQERGTLFIGPGTEVYEGMIVGEHSRDNDLVVNVCKEKKLTNMRASGSDE 553
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 446328044 559 AIRLVPPRKFSLEQNIEFLDDDELLEVTPTSLRLRKKFLDANMRKRNK 606
Cdd:COG1217 554 AIRLTPPRKMSLEQALEFIEDDELVEVTPKSIRLRKKILDENERKRAA 601
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
3-604 |
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: 955.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 3 IRNIAIIAHVDHGKTTLLDGILRQTGAVTAKED-GERIMDSNDLEKEKGITIKAKNTAVVYKGTRINVVDTPGHADFGGE 81
Cdd:TIGR01394 1 IRNIAIIAHVDHGKTTLVDALLKQSGTFRANEAvAERVMDSNDLERERGITILAKNTAIRYNGTKINIVDTPGHADFGGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 82 VERVLATADSCLLLVDAFDGPMPQTRFVLGKSLQLGHRPILVINKIDRPGARPEAVVDMAFDLFSDLGATDEQLDFPIVY 161
Cdd:TIGR01394 81 VERVLGMVDGVLLLVDASEGPMPQTRFVLKKALELGLKPIVVINKIDRPSARPDEVVDEVFDLFAELGADDEQLDFPIVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 162 ASAKQGWAVHNLSEsPGTNLDPLLDTVLKHVPPVQADTEAPLQFQVTSLDYNDYVGRIAVGKIYAGKMALGMNVIQLAAK 241
Cdd:TIGR01394 161 ASGRAGWASLDLDD-PSDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVHRGTVKKGQQVALMKRD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 242 KTetapsadTALFRITKLYNFEGLKRNEVNAAEAGDIVAIAGLPDVFIGDTICEPGKPAPRPAIEVEEPTVSMFFMVNNS 321
Cdd:TIGR01394 240 GT-------IENGRISKLLGFEGLERVEIDEAGAGDIVAVAGLEDINIGETIADPEVPEALPTITVDEPTLSMTFSVNDS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 322 PFAGKEGKFVTTRNIRERLDRELETNVAMRLEETEDKDRFKVLGRGELHLSVLIETMRREGFEIQVSRPEVILKTnEQGQ 401
Cdd:TIGR01394 313 PLAGKEGKKVTSRHIRDRLMRELETNVALRVEDTESADKFEVSGRGELHLSILIETMRREGFELQVGRPQVIYKE-IDGK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 402 KLEPYEYLVMDVPDQFTGAIIAELNRRKGELQLMDAHPSGMTRVEFVIPTRGIIGFRGFFISETRGEGVMSSRFLRFDVY 481
Cdd:TIGR01394 392 KLEPIEELTIDVPEEHVGAVIEKLGKRKGEMVDMEPSGNGRTRLEFKIPSRGLIGFRTEFLTDTRGTGIMNHVFDEYEPW 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 482 KGEIPGRKNGALISMDSGESTAYALWKIQERGELVIGPNTSVYPGMIIGIHSRDNDLEVNPVKEKKLSNVRSSGADEAIR 561
Cdd:TIGR01394 472 KGEIETRRNGSLVSMEDGTATAYALWNLQERGVMFVSPGTEVYEGMIIGEHSRENDLDVNPCKAKKLTNVRSSGKDEAVK 551
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 446328044 562 LVPPRKFSLEQNIEFLDDDELLEVTPTSLRLRKKFLDANMRKR 604
Cdd:TIGR01394 552 LTPPRKLSLEQALEYIEDDELVEVTPKSIRLRKRVLDPNERKR 594
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
3-604 |
0e+00 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 654.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 3 IRNIAIIAHVDHGKTTLLDGILRQTGAVTAK-EDGERIMDSNDLEKEKGITIKAKNTAVVYKGTRINVVDTPGHADFGGE 81
Cdd:PRK10218 5 LRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRaETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 82 VERVLATADSCLLLVDAFDGPMPQTRFVLGKSLQLGHRPILVINKIDRPGARPEAVVDMAFDLFSDLGATDEQLDFPIVY 161
Cdd:PRK10218 85 VERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDFPIVY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 162 ASAKQGWAVHNlSESPGTNLDPLLDTVLKHVPPVQADTEAPLQFQVTSLDYNDYVGRIAVGKIYAGKMALGMNVIQLAAK 241
Cdd:PRK10218 165 ASALNGIAGLD-HEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIIDSE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 242 -KTETApsadtalfRITKLYNFEGLKRNEVNAAEAGDIVAIAGLPDVFIGDTICEPGKPAPRPAIEVEEPTVSMFFMVNN 320
Cdd:PRK10218 244 gKTRNA--------KVGKVLGHLGLERIETDLAEAGDIVAITGLGELNISDTVCDTQNVEALPALSVDEPTVSMFFCVNT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 321 SPFAGKEGKFVTTRNIRERLDRELETNVAMRLEETEDKDRFKVLGRGELHLSVLIETMRREGFEIQVSRPEVILKTNEqG 400
Cdd:PRK10218 316 SPFCGKEGKFVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRREGFELAVSRPKVIFREID-G 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 401 QKLEPYEYLVMDVPDQFTGAIIAELNRRKGELQLMDAHPSGMTRVEFVIPTRGIIGFRGFFISETRGEGVMSSRFLRF-D 479
Cdd:PRK10218 395 RKQEPYENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYdD 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 480 VYKGEIPGRKNGALISMDSGESTAYALWKIQERGELVIGPNTSVYPGMIIGIHSRDNDLEVNPVKEKKLSNVRSSGADEA 559
Cdd:PRK10218 475 VRPGEVGQRQNGVLISNGQGKAVAFALFGLQDRGKLFLGHGAEVYEGQIIGIHSRSNDLTVNCLTGKKLTNMRASGTDEA 554
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 446328044 560 IRLVPPRKFSLEQNIEFLDDDELLEVTPTSLRLRKKFLDANMRKR 604
Cdd:PRK10218 555 VVLVPPIRMTLEQALEFIDDDELVEVTPTSIRIRKRHLTENDRRR 599
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
2-194 |
4.23e-126 |
|
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: 369.23 E-value: 4.23e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 2 EIRNIAIIAHVDHGKTTLLDGILRQTGAVTAKED-GERIMDSNDLEKEKGITIKAKNTAVVYKGTRINVVDTPGHADFGG 80
Cdd:cd01891 1 KIRNIAIIAHVDHGKTTLVDALLKQSGTFRENEEvGERVMDSNDLERERGITILAKNTAITYKDTKINIIDTPGHADFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 81 EVERVLATADSCLLLVDAFDGPMPQTRFVLGKSLQLGHRPILVINKIDRPGARPEAVVDMAFDLFSDLGATDEQLDFPIV 160
Cdd:cd01891 81 EVERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDRPDARPEEVVDEVFDLFLELNATDEQLDFPIV 160
|
170 180 190
....*....|....*....|....*....|....
gi 446328044 161 YASAKQGWAVHNLSEsPGTNLDPLLDTVLKHVPP 194
Cdd:cd01891 161 YASAKNGWASLNLDD-PSEDLDPLFETIIEHVPA 193
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
2-194 |
5.77e-70 |
|
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: 223.94 E-value: 5.77e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 2 EIRNIAIIAHVDHGKTTLLDGILRQTGAVTA----KEDGERIMDSNDLEKEKGITIKAKNTAVVYKGTRINVVDTPGHAD 77
Cdd:pfam00009 2 RHRNIGIIGHVDHGKTTLTDRLLYYTGAISKrgevKGEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 78 FGGEVERVLATADSCLLLVDAFDGPMPQTRFVLGKSLQLGHRPILVINKIDRP-GARPEAVVDMAFDLFSDLGATDEqLD 156
Cdd:pfam00009 82 FVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVdGAELEEVVEEVSRELLEKYGEDG-EF 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 446328044 157 FPIVYASAKQGWavhnlsespgtNLDPLLDTVLKHVPP 194
Cdd:pfam00009 161 VPVVPGSALKGE-----------GVQTLLDALDEYLPS 187
|
|
| lepA |
TIGR01393 |
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a ... |
3-478 |
2.23e-63 |
|
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: 219.50 E-value: 2.23e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 3 IRNIAIIAHVDHGKTTLLDGILRQTGAVTAKEDGERIMDSNDLEKEKGITIKAKNTAVVYK-----GTRINVVDTPGHAD 77
Cdd:TIGR01393 3 IRNFSIIAHIDHGKSTLADRLLEYTGAISEREMREQVLDSMDLERERGITIKAQAVRLNYKakdgeTYVLNLIDTPGHVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 78 FGGEVERVLATADSCLLLVDAFDGPMPQTRFVLGKSLQLGHRPILVINKIDRPGARPEAVvdmAFDLFSDLGATDEQldf 157
Cdd:TIGR01393 83 FSYEVSRSLAACEGALLLVDAAQGIEAQTLANVYLALENDLEIIPVINKIDLPSADPERV---KKEIEEVIGLDASE--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 158 pIVYASAKQgwavhnlsespGTNLDPLLDTVLKHVPPVQADTEAPLQFQVTSLDYNDYVGRIAVGKIYAGKMALGMNVIQ 237
Cdd:TIGR01393 157 -AILASAKT-----------GIGIEEILEAIVKRVPPPKGDPDAPLKALIFDSHYDNYRGVVALVRVFEGTIKPGDKIRF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 238 LAAKKTetapsadtalFRITKL--YNFEGLKRNEVNAAEAGDIVA-IAGLPDVFIGDTICEPGKPA--PRPAIEVEEPTV 312
Cdd:TIGR01393 225 MSTGKE----------YEVDEVgvFTPKLTKTDELSAGEVGYIIAgIKDVSDVRVGDTITHVKNPAkePLPGFKEVKPMV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 313 -SMFFMVNNSPFagkegkfvttRNIRERLDR----------ELETNVAMRLEetedkdrFKVLGRGELHLSVLIETMRRE 381
Cdd:TIGR01393 295 fAGLYPIDTEDY----------EDLRDALEKlklndasltyEPESSPALGFG-------FRCGFLGLLHMEIIQERLERE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 382 --------------------GFEIQVSRPEVILKTNEQGQKLEPYEYLVMDVPDQFTGAIIAELNRRKGELQLMDAHpsG 441
Cdd:TIGR01393 358 fnldlittapsviyrvyltnGEVIEVDNPSDLPDPGKIEHVEEPYVKATIITPTEYLGPIMTLCQEKRGVQTNMEYL--D 435
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 446328044 442 MTRVEFV--IPTRGII-GFRGFFISETRGEGVMSSRFLRF 478
Cdd:TIGR01393 436 PNRVELIyeMPLAEIVyDFFDKLKSISRGYASFDYELIGY 475
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
3-392 |
1.50e-55 |
|
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: 199.89 E-value: 1.50e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 3 IRNIAIIAHVDHGKTTLLDGILRQTGAVTAK---EDGERIMDSNDLEKEKGITIkakNTAVV---YKGTRINVVDTPGHA 76
Cdd:COG0480 9 IRNIGIVAHIDAGKTTLTERILFYTGAIHRIgevHDGNTVMDWMPEEQERGITI---TSAATtceWKGHKINIIDTPGHV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 77 DFGGEVERVLATADSCLLLVDAFDGPMPQTRFVLgKSLQLGHRP-ILVINKIDRPGARPEAVVDM--------------- 140
Cdd:COG0480 86 DFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVW-RQADKYGVPrIVFVNKMDREGADFDRVLEQlkerlganpvplqlp 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 141 -----AF----DLFS--------DLGAT--------------------------------------DEQLD--------- 156
Cdd:COG0480 165 igaedDFkgviDLVTmkayvyddELGAKyeeeeipaelkeeaeeareelieavaetddelmekyleGEELTeeeikaglr 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 157 --------FPIVYASAKQGWAVhnlsespgtnlDPLLDTVLK------HVPPVQ-------------ADTEAPLQFQV-- 207
Cdd:COG0480 245 katlagkiVPVLCGSAFKNKGV-----------QPLLDAVVDylpsplDVPAIKgvdpdtgeeverkPDDDEPFSALVfk 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 208 TSLDynDYVGRIAVGKIYAGKMALGMNVIQLAAKKTEtapsadtalfRITKLYNFEGLKRNEVNAAEAGDIVAIAGLPDV 287
Cdd:COG0480 314 TMTD--PFVGKLSFFRVYSGTLKSGSTVYNSTKGKKE----------RIGRLLRMHGNKREEVDEAGAGDIVAVVKLKDT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 288 FIGDTICEPGKPAPRPAIEVEEPTVSMffmvnnspfA------GKEGKFVT--TRNIRE----RLDRELETNvamrleET 355
Cdd:COG0480 382 TTGDTLCDEDHPIVLEPIEFPEPVISV---------AiepktkADEDKLSTalAKLAEEdptfRVETDEETG------QT 446
|
490 500 510
....*....|....*....|....*....|....*....
gi 446328044 356 edkdrfkVL-GRGELHLSVLIETMRRE-GFEIQVSRPEV 392
Cdd:COG0480 447 -------IIsGMGELHLEIIVDRLKREfGVEVNVGKPQV 478
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
1-392 |
1.98e-55 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 199.41 E-value: 1.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 1 MEIRNIAIIAHVDHGKTTLLDGILRQTGAVTAK---EDGERIMDSNDLEKEKGITIKAKNTAVVYKGTRINVVDTPGHAD 77
Cdd:PRK13351 6 MQIRNIGILAHIDAGKTTLTERILFYTGKIHKMgevEDGTTVTDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHID 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 78 FGGEVERVLATADSCLLLVDAFDGPMPQTRFVLgKSLQLGHRPILV-INKIDRPGA---------------RP------- 134
Cdd:PRK13351 86 FTGEVERSLRVLDGAVVVFDAVTGVQPQTETVW-RQADRYGIPRLIfINKMDRVGAdlfkvledieerfgkRPlplqlpi 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 135 ------EAVVDMAF----------------------DLFSDLGATDEQLD------------------------------ 156
Cdd:PRK13351 165 gsedgfEGVVDLITepelhfsegdggstveegpipeELLEEVEEAREKLIealaefddellelylegeelsaeqlraplr 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 157 --------FPIVYASAKQGWAVhnlsespgtnlDPLLDTVLKH------VPPVQ------------ADTEAPLQFQVTSL 210
Cdd:PRK13351 245 egtrsghlVPVLFGSALKNIGI-----------EPLLDAVVDYlpspleVPPPRgskdngkpvkvdPDPEKPLLALVFKV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 211 DYNDYVGRIAVGKIYAGKMALGMNVIQLAAKKTEtapsadtalfRITKLYNFEGLKRNEVNAAEAGDIVAIAGLPDVFIG 290
Cdd:PRK13351 314 QYDPYAGKLTYLRVYSGTLRAGSQLYNGTGGKRE----------KVGRLFRLQGNKREEVDRAKAGDIVAVAGLKELETG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 291 DTICEPGKPAPRPAIEVEEPTVSMFFMVNNspfAGKEGKfvttrnIRERLDRELETNVAMRLEETEDKDRFKVLGRGELH 370
Cdd:PRK13351 384 DTLHDSADPVLLELLTFPEPVVSLAVEPER---RGDEQK------LAEALEKLVWEDPSLRVEEDEETGQTILSGMGELH 454
|
490 500
....*....|....*....|...
gi 446328044 371 LSVLIETMRRE-GFEIQVSRPEV 392
Cdd:PRK13351 455 LEVALERLRREfKLEVNTGKPQV 477
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
3-478 |
5.54e-53 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 191.00 E-value: 5.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 3 IRNIAIIAHVDHGKTTLLDGILRQTGAVTAKEDGERIMDSNDLEKEKGITIKAKNTAVVYKGT-----RINVVDTPGHAD 77
Cdd:COG0481 6 IRNFSIIAHIDHGKSTLADRLLELTGTLSEREMKEQVLDSMDLERERGITIKAQAVRLNYKAKdgetyQLNLIDTPGHVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 78 FGGEVERVLATADSCLLLVDAFDGPMPQTRFVLGKSLQLGHRPILVINKIDRPGARPEAVVDMAFDLFsDLGATDeqldf 157
Cdd:COG0481 86 FSYEVSRSLAACEGALLVVDASQGVEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKQEIEDII-GIDASD----- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 158 pIVYASAKQgwavhnlsespGTNLDPLLDTVLKHVPPVQADTEAPLQ---FqvtslD--YNDYVGRIAVGKIYAGKMALG 232
Cdd:COG0481 160 -AILVSAKT-----------GIGIEEILEAIVERIPPPKGDPDAPLQaliF-----DswYDSYRGVVVYVRVFDGTLKKG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 233 MNVIQLAAKKTetapsadtalFRITKLYNFeGLKRNEVNAAEAGDI-VAIAGLPDVF---IGDTICEPGKPAPRPAIEVE 308
Cdd:COG0481 223 DKIKMMSTGKE----------YEVDEVGVF-TPKMTPVDELSAGEVgYIIAGIKDVRdarVGDTITLAKNPAAEPLPGFK 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 309 EPTvSMFFM----VNNSPFagkegkfvttRNIRERLDR----------ELETNVAmrleetedkdrfkvLG---R----G 367
Cdd:COG0481 292 EVK-PMVFAglypVDSDDY----------EDLRDALEKlqlndasltyEPETSAA--------------LGfgfRcgflG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 368 ELHLSVLIETMRRE-GFEIQVSRPEVI---LKTNeqGQKL------------------EPYEYLVMDVPDQFTGAIIAEL 425
Cdd:COG0481 347 LLHMEIIQERLEREfDLDLITTAPSVVyevTLTD--GEVIevdnpsdlpdpgkieeieEPIVKATIITPSEYVGAVMELC 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 446328044 426 NRRKGELQLMDAHpsGMTRVE--FVIPTRGIIgfRGFF---ISETRGEGVMSSRFLRF 478
Cdd:COG0481 425 QEKRGVQKNMEYL--GENRVEltYELPLAEIV--FDFFdrlKSITRGYASLDYEFIGY 478
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
9-488 |
1.03e-51 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 188.80 E-value: 1.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 9 IAHVDHGKTTLLDGILRQTGAVTAK---EDGERIMDSNDLEKEKGITIKAKNTAVVYKGTRINVVDTPGHADFGGEVERV 85
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRIgevEDGTTTMDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVERA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 86 LATADSCLLLVDAFDGPMPQTRFVLG--KSLQLGHrpILVINKIDRPGARPEAVVDM---AF------------------ 142
Cdd:PRK12740 81 LRVLDGAVVVVCAVGGVEPQTETVWRqaEKYGVPR--IIFVNKMDRAGADFFRVLAQlqeKLgapvvplqlpigegddft 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 143 ---DLFS------DLGATDEQLDFPIVYASAKQGW---AVHNLSE----------------------------------- 175
Cdd:PRK12740 159 gvvDLLSmkayryDEGGPSEEIEIPAELLDRAEEAreeLLEALAEfddelmekylegeelseeeikaglrkatlageivp 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 176 ----SPGTN--LDPLLDTVLKHVP-----------------PVQADTEAPLQFQVTSLDYNDYVGRIAVGKIYAGKMALG 232
Cdd:PRK12740 239 vfcgSALKNkgVQRLLDAVVDYLPsplevppvdgedgeegaELAPDPDGPLVALVFKTMDDPFVGKLSLVRVYSGTLKKG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 233 MNVIQLAAKKTEtapsadtalfRITKLYNFEGLKRNEVNAAEAGDIVAIAGLPDVFIGDTICEPGKPAPRPAIEVEEPTV 312
Cdd:PRK12740 319 DTLYNSGTGKKE----------RVGRLYRMHGKQREEVDEAVAGDIVAVAKLKDAATGDTLCDKGDPILLEPMEFPEPVI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 313 SMffmvnnspfAgkegkfVTTRN------IRERLDRELETNVAMRLEETEDKDRFKVLGRGELHLSVLIETMRRE-GFEI 385
Cdd:PRK12740 389 SL---------A------IEPKDkgdeekLSEALGKLAEEDPTLRVERDEETGQTILSGMGELHLDVALERLKREyGVEV 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 386 QVSRP-----EVILKTNEQ-----------GQ------KLEPYE------------------------------------ 407
Cdd:PRK12740 454 ETGPPqvpyrETIRKKAEGhgrhkkqsgghGQfgdvwlEVEPLPrgegfefvdkvvggavprqyipavekgvrealekgv 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 408 ---YLVMDV-------------------------------------------------PDQFTGAIIAELNRRKGELQLM 435
Cdd:PRK12740 534 lagYPVVDVkvtltdgsyhsvdssemafkiaarlafrealpkakpvllepimkvevsvPEEFVGDVIGDLSSRRGRILGM 613
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 446328044 436 DAHPSGmTRVEFVIPTRGIIGFRGFFISETRGEGVMSSRFLRFDvykgEIPGR 488
Cdd:PRK12740 614 ESRGGG-DVVRAEVPLAEMFGYATDLRSLTQGRGSFSMEFSHYE----EVPGN 661
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
5-194 |
2.31e-51 |
|
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: 174.79 E-value: 2.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 5 NIAIIAHVDHGKTTLLDGILRQTGAV-TAKEDGERIMDSNDLEKEKGITIKAKNTAVVYKGTRINVVDTPGHADFGGEVE 83
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIdRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 84 RVLATADSCLLLVDAFDGPMPQTRFVLGKSLQLGHRPILVINKIDRPG-ARPEAVVDMAFDLFSDLGAT-DEQLDFPIVY 161
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGeEDFDEVLREIKELLKLIGFTfLKGKDVPIIP 160
|
170 180 190
....*....|....*....|....*....|...
gi 446328044 162 ASAKQGWAVhnlsespgtnlDPLLDTVLKHVPP 194
Cdd:cd00881 161 ISALTGEGI-----------EELLDAIVEHLPP 182
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
3-401 |
7.96e-51 |
|
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: 187.03 E-value: 7.96e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 3 IRNIAIIAHVDHGKTTLLDGILRQTGAVTAKEDGE-RIMDSNDLEKEKGITIKAKNTAVV--YKGTR--INVVDTPGHAD 77
Cdd:TIGR00490 19 IRNIGIVAHIDHGKTTLSDNLLAGAGMISEELAGQqLYLDFDEQEQERGITINAANVSMVheYEGNEylINLIDTPGHVD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 78 FGGEVERVLATADSCLLLVDAFDGPMPQTRFVLGKSLQLGHRPILVINKIDR--------PGARPEAVV----------- 138
Cdd:TIGR00490 99 FGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKPVLFINKVDRlinelkltPQELQERFIkiitevnklik 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 139 DMAFDLFSDLGATDEQlDFPIVYASAKQGWAVH-NLSESPGTNLD------------------PL----LDTVLKHVP-P 194
Cdd:TIGR00490 179 AMAPEEFRDKWKVRVE-DGSVAFGSAYYNWAISvPSMKKTGIGFKdiykyckedkqkelakksPLhqvvLDMVIRHLPsP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 195 VQA------------------------DTEAPLQFQVTSLDYNDYVGRIAVGKIYAGKMALGMNVIQLAAKKTEtapsad 250
Cdd:TIGR00490 258 IEAqkyripviwkgdlnsevgkamlncDPKGPLALMITKIVVDKHAGEVAVGRLYSGTIRPGMEVYIVDRKAKA------ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 251 talfRITKLYNFEGLKRNEVNAAEAGDIVAIAGLPDVFIGDTICEPGKP-APRPAIE-VEEPTVSMFFMVNNSPFAGKeg 328
Cdd:TIGR00490 332 ----RIQQVGVYMGPERVEVDEIPAGNIVAVIGLKDAVAGETICTTVENiTPFESIKhISEPVVTVAIEAKNTKDLPK-- 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446328044 329 kfvttrnIRERLDRELETNVAMRLEETEDKDRFKVLGRGELHLSVLIETMRRE-GFEIQVSRPEVILKTNEQGQ 401
Cdd:TIGR00490 406 -------LIEVLRQVAKEDPTVHVEINEETGEHLISGMGELHLEIIVEKIREDyGLDVETSPPIVVYRETVTGT 472
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
3-393 |
3.11e-48 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 179.67 E-value: 3.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 3 IRNIAIIAHVDHGKTTLLDGILRQTGAVTAKEDGE-RIMDSNDLEKEKGITIKAKNTAVV--YKGTR--INVVDTPGHAD 77
Cdd:PRK07560 20 IRNIGIIAHIDHGKTTLSDNLLAGAGMISEELAGEqLALDFDEEEQARGITIKAANVSMVheYEGKEylINLIDTPGHVD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 78 FGGEVERVLATADSCLLLVDAFDGPMPQTRFVLGKSLQLGHRPILVINKIDR--------P---GARPEAVVD------- 139
Cdd:PRK07560 100 FGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKPVLFINKVDRlikelkltPqemQQRLLKIIKdvnklik 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 140 -MAFDLFSD---LGATDEQLDFpivyASAKQGWAVHN-LSESPGTNLD------------------PL----LDTVLKHV 192
Cdd:PRK07560 180 gMAPEEFKEkwkVDVEDGTVAF----GSALYNWAISVpMMQKTGIKFKdiidyyekgkqkelaekaPLhevvLDMVVKHL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 193 P-PVQA------------------------DTEAPLQFQVTSLDYNDYVGRIAVGKIYAGKMALGMNVIQLAAKKTEtap 247
Cdd:PRK07560 256 PnPIEAqkyripkiwkgdlnsevgkamlncDPNGPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLVGAKKKN--- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 248 sadtalfRITKLYNFEGLKRNEVNAAEAGDIVAIAGLPDVFIGDTICEPGKPAPRPAIE-VEEPTVSMffmvnnspfagk 326
Cdd:PRK07560 333 -------RVQQVGIYMGPEREEVEEIPAGNIAAVTGLKDARAGETVVSVEDMTPFESLKhISEPVVTV------------ 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446328044 327 egkFVTTRNIRErLDRELET--NVA-----MRLEETEDKDRFKVLGRGELHLSVLIETMRRE-GFEIQVSRPEVI 393
Cdd:PRK07560 394 ---AIEAKNPKD-LPKLIEVlrQLAkedptLVVKINEETGEHLLSGMGELHLEVITYRIKRDyGIEVVTSEPIVV 464
|
|
| BipA_III |
cd16263 |
Domain III of GTP-binding protein BipA (TypA); BipA (also called TypA) is a highly conserved ... |
310-388 |
4.16e-47 |
|
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: 159.78 E-value: 4.16e-47
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446328044 310 PTVSMFFMVNNSPFAGKEGKFVTTRNIRERLDRELETNVAMRLEETEDKDRFKVLGRGELHLSVLIETMRREGFEIQVS 388
Cdd:cd16263 1 PTVSMTFGVNTSPFAGREGKFVTSRKIRDRLEKELETNVALRVEETESPDSFIVSGRGELHLSILIETMRREGFELQVS 79
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
4-194 |
4.04e-45 |
|
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: 158.08 E-value: 4.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 4 RNIAIIAHVDHGKTTLLDGILRQTGAVTAKEDGERIMDSNDLEKEKGITIKAKNTAVVYK---GTR--INVVDTPGHADF 78
Cdd:cd01890 1 RNFSIIAHIDHGKSTLADRLLELTGTVSEREMKEQVLDSMDLERERGITIKAQAVRLFYKakdGEEylLNLIDTPGHVDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 79 GGEVERVLATADSCLLLVDAFDGPMPQTRFVLGKSLQLGHRPILVINKIDRPGARPEAVVDmafDLFSDLGATDEQldfp 158
Cdd:cd01890 81 SYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVKQ---EIEDVLGLDASE---- 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 446328044 159 IVYASAKQgwavhnlsespGTNLDPLLDTVLKHVPP 194
Cdd:cd01890 154 AILVSAKT-----------GLGVEDLLEAIVERIPP 178
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
4-194 |
2.54e-44 |
|
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: 157.01 E-value: 2.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 4 RNIAIIAHVDHGKTTLLDGILRQTGAVTAKEDGE-RIMDSNDLEKEKGITIKAKNTAVVYKGTR---------INVVDTP 73
Cdd:cd01885 1 RNICIIAHVDHGKTTLSDSLLASAGIISEKLAGKaRYLDTREDEQERGITIKSSAISLYFEYEEekmdgndylINLIDSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 74 GHADFGGEVERVLATADSCLLLVDAFDGPMPQTRFVLGKSLQLGHRPILVINKIDRP----GARPE-------------- 135
Cdd:cd01885 81 GHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDRLilelKLSPEeayqrllrivedvn 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446328044 136 AVVDMAFDlfSDLGATDEQLDFP---IVYASAKQGWAVhNLSEspGTNLDPLLDTVLKHVPP 194
Cdd:cd01885 161 AIIETYAP--EEFKQEKWKFSPQkgnVAFGSALDGWGF-TIIK--FADIYAVLEMVVKHLPS 217
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
203-303 |
9.71e-38 |
|
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: 134.62 E-value: 9.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 203 LQFQVTSLDYNDYVGRIAVGKIYAGKMALGMNVIQLAAKKTETapsadtaLFRITKLYNFEGLKRNEVNAAEAGDIVAIA 282
Cdd:cd03691 1 FQMLVTTLDYDDYLGRIAIGRIFSGTVKVGQQVTVVDEDGKIE-------KGRVTKLFGFEGLERVEVEEAEAGDIVAIA 73
|
90 100
....*....|....*....|.
gi 446328044 283 GLPDVFIGDTICEPGKPAPRP 303
Cdd:cd03691 74 GLEDITIGDTICDPEVPEPLP 94
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
5-139 |
5.38e-36 |
|
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: 135.06 E-value: 5.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 5 NIAIIAHVDHGKTTLLDGILRQTGAVT---AKEDGERIMDSNDLEKEKGITIKAKNTAVVYKGTRINVVDTPGHADFGGE 81
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIRelgSVDKGTTRTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIAE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 446328044 82 VERVLATADSCLLLVDAFDGPMPQTRfVLGKSLQ-LGHRPILVINKIDRPGARPEAVVD 139
Cdd:cd04168 81 VERSLSVLDGAILVISAVEGVQAQTR-ILFRLLRkLNIPTIIFVNKIDRAGADLEKVYQ 138
|
|
| BipA_TypA_C |
cd03710 |
BipA_TypA_C: a C-terminal portion of BipA or TypA having homology to the C terminal domains of ... |
404-482 |
2.64e-35 |
|
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: 127.62 E-value: 2.64e-35
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446328044 404 EPYEYLVMDVPDQFTGAIIAELNRRKGELQLMDAHPSGMTRVEFVIPTRGIIGFRGFFISETRGEGVMSSRFLRFDVYK 482
Cdd:cd03710 1 EPIEELTIDVPEEYSGAVIEKLGKRKGEMVDMEPDGNGRTRLEFKIPSRGLIGFRSEFLTDTRGTGIMNHVFDGYEPYK 79
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
5-140 |
1.44e-31 |
|
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: 123.37 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 5 NIAIIAHVDHGKTTLLDGILRQTGAvTAK----EDGERIMDSNDLEKEKGITIKAKNTAVVYKGTRINVVDTPGHADFGG 80
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGR-IHKigevHGGGATMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDFTI 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 81 EVERVLATADSCLLLVDAFDGPMPQTRFVLGKSLQLGHRPILVINKIDRPGARPEAVVDM 140
Cdd:cd01886 80 EVERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQ 139
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
3-129 |
1.77e-30 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 127.47 E-value: 1.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 3 IRNIAIIAHVDHGKTTLLDGILRQTGAVTAKEDGE-RIMDSNDLEKEKGITIKAKNTAVVYKGTR----------INVVD 71
Cdd:PTZ00416 19 IRNMSVIAHVDHGKSTLTDSLVCKAGIISSKNAGDaRFTDTRADEQERGITIKSTGISLYYEHDLedgddkqpflINLID 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 446328044 72 TPGHADFGGEVERVLATADSCLLLVDAFDGPMPQTRFVLGKSLQLGHRPILVINKIDR 129
Cdd:PTZ00416 99 SPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKVDR 156
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
4-139 |
1.87e-27 |
|
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: 111.92 E-value: 1.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 4 RNIAIIAHVDHGKTTLLD------GILRQTGAVTAKEDGERIM-DSNDLEKEKGITIkakNTAVV---YKGTRINVVDTP 73
Cdd:cd04169 3 RTFAIISHPDAGKTTLTEklllfgGAIQEAGAVKARKSRKHATsDWMEIEKQRGISV---TSSVMqfeYKGCVINLLDTP 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446328044 74 GHADFGGEVERVLATADSCLLLVDAFDGPMPQTRfVLGKSLQLGHRPIL-VINKIDRPGARPEAVVD 139
Cdd:cd04169 80 GHEDFSEDTYRTLTAVDSAVMVIDAAKGVEPQTR-KLFEVCRLRGIPIItFINKLDREGRDPLELLD 145
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
3-129 |
8.45e-27 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 115.98 E-value: 8.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 3 IRNIAIIAHVDHGKTTLLDGILRQTGAVTAKEDGE-RIMDSNDLEKEKGITIKAKNTAVVY----------KGTR----- 66
Cdd:PLN00116 19 IRNMSVIAHVDHGKSTLTDSLVAAAGIIAQEVAGDvRMTDTRADEAERGITIKSTGISLYYemtdeslkdfKGERdgney 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446328044 67 -INVVDTPGHADFGGEVERVLATADSCLLLVDAFDGPMPQTRFVLGKSLQLGHRPILVINKIDR 129
Cdd:PLN00116 99 lINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTETVLRQALGERIRPVLTVNKMDR 162
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
4-129 |
1.49e-26 |
|
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: 107.74 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 4 RNIAIIAHVDHGKTTLLDGILRQT----GAVTAKEDGERIMDSNDLEKEKGITIKAKNTAVVYKGTR-----INVVDTPG 74
Cdd:cd04167 1 RNVCIAGHLHHGKTSLLDMLIEQThkrtPSVKLGWKPLRYTDTRKDEQERGISIKSNPISLVLEDSKgksylINIIDTPG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 446328044 75 HADFGGEVERVLATADSCLLLVDAFDGPMPQTRFVLGKSLQLGHRPILVINKIDR 129
Cdd:cd04167 81 HVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDR 135
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
5-146 |
7.01e-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: 107.29 E-value: 7.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 5 NIAIIAHVDHGKTTLLDGILRQTGAVTAK---EDGERIMDSNDLEKEKGITIKAKNTAVVYKGTRINVVDTPGHADFGGE 81
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRLgrvEDGNTVSDYDPEEKKRKMSIETSVAPLEWNGHKINLIDTPGYADFVGE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446328044 82 VERVLATADSCLLLVDAFDGPMPQTR--FVLGKSLQLGHrpILVINKIDRPGARPEAVVDMAFDLFS 146
Cdd:cd04170 81 TLSALRAVDAALIVVEAQSGVEVGTEkvWEFLDDAKLPR--IIFINKMDRARADFDKTLAALREAFG 145
|
|
| EFG_C |
pfam00679 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
401-488 |
6.14e-25 |
|
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: 98.77 E-value: 6.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 401 QKLEPYEYLVMDVPDQFTGAIIAELNRRKGELQLMDAHPSGMTRVEFVIPTRGIIGFRGFFISETRGEGVMSSRFLRFDV 480
Cdd:pfam00679 1 VLLEPIEKVTIDVPEEYVGDVISDLNSRRGEILDMDPDDGGRVVIEAEVPLAELFGFATELRSLTKGRGSFSMEFSGYQP 80
|
....*...
gi 446328044 481 YKGEIPGR 488
Cdd:pfam00679 81 VPGDILDR 88
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
6-189 |
1.94e-23 |
|
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.
Pssm-ID: 206674 [Multi-domain] Cd Length: 169 Bit Score: 97.16 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 6 IAIIAHVDHGKTTLLDGIlRQTgAVTAKEDGerimdsndlekekGIT--IKAKNTAVVYKGTRINVVDTPGHADFGGEVE 83
Cdd:cd01887 3 VTVMGHVDHGKTTLLDKI-RKT-NVAAGEAG-------------GITqhIGAYQVPIDVKIPGITFIDTPGHEAFTNMRA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 84 RVLATADSCLLLVDAFDGPMPQTRfvlgKSLQLGHR---PILV-INKIDRP---GARPEAVVdmafdlfSDLGATDEQL- 155
Cdd:cd01887 68 RGASVTDIAILVVAADDGVMPQTI----EAINHAKAanvPIIVaINKIDKPygtEADPERVK-------NELSELGLVGe 136
|
170 180 190
....*....|....*....|....*....|....*...
gi 446328044 156 ----DFPIVYASAKQgwavhnlsespGTNLDPLLDTVL 189
Cdd:cd01887 137 ewggDVSIVPISAKT-----------GEGIDDLLEAIL 163
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
4-295 |
3.21e-22 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 100.59 E-value: 3.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 4 RNIAIIAHVDHGKTT------LLDGILRQTGAVTAKEDGeRIMDSN--DLEKEKGITIkaknTAVV----YKGTRINVVD 71
Cdd:PRK00741 11 RTFAIISHPDAGKTTltekllLFGGAIQEAGTVKGRKSG-RHATSDwmEMEKQRGISV----TSSVmqfpYRDCLINLLD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 72 TPGHADFGGEVERVLATADSCLLLVDAFDGPMPQTRfvlgKSLQ---LGHRPILV-INKIDRPGARP-------EAVVDM 140
Cdd:PRK00741 86 TPGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTR----KLMEvcrLRDTPIFTfINKLDRDGREPlelldeiEEVLGI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 141 A-----------------FDLFSD-------------------LGATDEQLDFPI---VYASAK------QGwAVHNLSE 175
Cdd:PRK00741 162 AcapitwpigmgkrfkgvYDLYNDevelyqpgeghtiqeveiiKGLDNPELDELLgedLAEQLReelelvQG-ASNEFDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 176 --------SP---GTNL-----DPLLDTVLKHVPPVQA-DTEAplqfQVTSLDYNDYVG---------------RIAVGK 223
Cdd:PRK00741 241 eaflagelTPvffGSALnnfgvQEFLDAFVEWAPAPQPrQTDE----REVEPTEEKFSGfvfkiqanmdpkhrdRIAFVR 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446328044 224 IYAGKMALGMNVIQLAAKKTetapsadtalFRITKLYNFEGLKRNEVNAAEAGDIVaiaGLPD---VFIGDTICE 295
Cdd:PRK00741 317 VCSGKFEKGMKVRHVRTGKD----------VRISNALTFMAQDREHVEEAYAGDII---GLHNhgtIQIGDTFTQ 378
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
5-243 |
1.44e-21 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 97.69 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 5 NIAIIAHVDHGKTTLLDGILRQTGAV----------TAKEDGER------IMDSNDLEKEKGITIKAKNTAVVYKGTRIN 68
Cdd:PRK12317 8 NLAVIGHVDHGKSTLVGRLLYETGAIdehiieelreEAKEKGKEsfkfawVMDRLKEERERGVTIDLAHKKFETDKYYFT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 69 VVDTPGHADFggeVERVL---ATADSCLLLVDAFD--GPMPQTR--FVLGKSL---QLghrpILVINKIDRPG---ARPE 135
Cdd:PRK12317 88 IVDCPGHRDF---VKNMItgaSQADAAVLVVAADDagGVMPQTRehVFLARTLginQL----IVAINKMDAVNydeKRYE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 136 AVVDMAFDLFSDLGATDEqlDFPIVYASAKQGWAVHNLSESPGTNLDPLLDTVLKHVPPVQADTEAPLQFQVTSLDYNDY 215
Cdd:PRK12317 161 EVKEEVSKLLKMVGYKPD--DIPFIPVSAFEGDNVVKKSENMPWYNGPTLLEALDNLKPPEKPTDKPLRIPIQDVYSISG 238
|
250 260
....*....|....*....|....*...
gi 446328044 216 VGRIAVGKIYAGKMALGMNVIQLAAKKT 243
Cdd:PRK12317 239 VGTVPVGRVETGVLKVGDKVVFMPAGVV 266
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
5-243 |
5.60e-21 |
|
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: 95.77 E-value: 5.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 5 NIAIIAHVDHGKTTLLDGILRQTGAVT----------AKEDGER------IMDSNDLEKEKGITI----KAKNTAVVYkg 64
Cdd:COG5256 9 NLVVIGHVDHGKSTLVGRLLYETGAIDehiiekyeeeAEKKGKEsfkfawVMDRLKEERERGVTIdlahKKFETDKYY-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 65 trINVVDTPGHADFggeVERVL---ATADSCLLLVDAFDGPMPQTR--FVLGKSL---QLghrpILVINKIDRPG---AR 133
Cdd:COG5256 87 --FTIIDAPGHRDF---VKNMItgaSQADAAILVVSAKDGVMGQTRehAFLARTLginQL----IVAVNKMDAVNyseKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 134 PEAVVDMAFDLFSDLGATDEqlDFPIVYASAKQGWAVHNLSESPGTNLDPLLDTVLKHVPPVQADTEAPLQFQVTSLdYN 213
Cdd:COG5256 158 YEEVKEEVSKLLKMVGYKVD--KIPFIPVSAWKGDNVVKKSDNMPWYNGPTLLEALDNLKEPEKPVDKPLRIPIQDV-YS 234
|
250 260 270
....*....|....*....|....*....|.
gi 446328044 214 -DYVGRIAVGKIYAGKMALGMNVIQLAAKKT 243
Cdd:COG5256 235 iSGIGTVPVGRVETGVLKVGDKVVFMPAGVV 265
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
6-284 |
7.72e-21 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 96.83 E-value: 7.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 6 IAIIAHVDHGKTTLLDGIlRQTGAvTAKEDGerimdsndlekekGIT--IKAKNTAVVYKGTRINVV--DTPGHADFGGE 81
Cdd:CHL00189 247 VTILGHVDHGKTTLLDKI-RKTQI-AQKEAG-------------GITqkIGAYEVEFEYKDENQKIVflDTPGHEAFSSM 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 82 VERVLATADSCLLLVDAFDGPMPQTRFVLgKSLQLGHRPILV-INKIDRPGARPEAVVD--MAFDLFS-DLGAtdeqlDF 157
Cdd:CHL00189 312 RSRGANVTDIAILIIAADDGVKPQTIEAI-NYIQAANVPIIVaINKIDKANANTERIKQqlAKYNLIPeKWGG-----DT 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 158 PIVYASAKQgwavhnlsespGTNLDPLLDTV--LKHVPPVQADTEAPLQFQVTSLDYNDYVGRIAVGKIYAGKMALGMNV 235
Cdd:CHL00189 386 PMIPISASQ-----------GTNIDKLLETIllLAEIEDLKADPTQLAQGIILEAHLDKTKGPVATILVQNGTLHIGDII 454
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 446328044 236 IqlaakktetapsADTALFRITKLYNFEGlkrNEVNAAEAGDIVAIAGL 284
Cdd:CHL00189 455 V------------IGTSYAKIRGMINSLG---NKINLATPSSVVEIWGL 488
|
|
| Elongation_Factor_C |
cd01514 |
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ... |
404-482 |
3.84e-20 |
|
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: 84.84 E-value: 3.84e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446328044 404 EPYEYLVMDVPDQFTGAIIAELNRRKGELQLMDAHPSGMTRVEFVIPTRGIIGFRGFFISETRGEGVMSSRFLRFDVYK 482
Cdd:cd01514 1 EPIMKVEITVPEEYLGAVIGDLSKRRGEILGMEPRGTGRVVIKAELPLAEMFGFATDLRSLTQGRASFSMEFSHYEPVP 79
|
|
| tufA |
CHL00071 |
elongation factor Tu |
5-281 |
1.70e-19 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 91.17 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 5 NIAIIAHVDHGKTTLLDGI---LRQTGAVTAKEDGEriMDSNDLEKEKGITIkakNTA-VVYKGTRINV--VDTPGHADF 78
Cdd:CHL00071 14 NIGTIGHVDHGKTTLTAAItmtLAAKGGAKAKKYDE--IDSAPEEKARGITI---NTAhVEYETENRHYahVDCPGHADY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 79 ggeVERVLATA---DSCLLLVDAFDGPMPQTR--FVLGKslQLGHRPILV-INKIDRpgarpeavVD------------- 139
Cdd:CHL00071 89 ---VKNMITGAaqmDGAILVVSAADGPMPQTKehILLAK--QVGVPNIVVfLNKEDQ--------VDdeellelvelevr 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 140 ---MAFDLFSDlgatdeqlDFPIVYASAKQgwAVHNLSESPgtNLDP-----------LLDTVLKHVPPVQADTEAPLQF 205
Cdd:CHL00071 156 ellSKYDFPGD--------DIPIVSGSALL--ALEALTENP--KIKRgenkwvdkiynLMDAVDSYIPTPERDTDKPFLM 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446328044 206 QVTSLDYNDYVGRIAVGKIYAGKMALGMNVIQLAAKKTETApsadtalfRITKLYNFeglkRNEVNAAEAGDIVAI 281
Cdd:CHL00071 224 AIEDVFSITGRGTVATGRIERGTVKVGDTVEIVGLRETKTT--------TVTGLEMF----QKTLDEGLAGDNVGI 287
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
5-194 |
2.13e-19 |
|
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: 86.48 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 5 NIAIIAHVDHGKTTLldgilrqTGAVT---AKEDGERIMDSNDL-----EKEKGITIkakNTAVVYKGTRINV---VDTP 73
Cdd:cd01884 4 NVGTIGHVDHGKTTL-------TAAITkvlAKKGGAKAKKYDEIdkapeEKARGITI---NTAHVEYETANRHyahVDCP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 74 GHADFggeVERVLATA---DSCLLLVDAFDGPMPQTR--FVLGKslQLGHRPILV-INKIDRPgARPEAV--VDMAF-DL 144
Cdd:cd01884 74 GHADY---IKNMITGAaqmDGAILVVSATDGPMPQTRehLLLAR--QVGVPYIVVfLNKADMV-DDEELLelVEMEVrEL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446328044 145 FSDLGATDEqlDFPIVYASAKQgwAVHNLSESPGTN-LDPLLDTVLKHVPP 194
Cdd:cd01884 148 LSKYGFDGD--DTPIVRGSALK--ALEGDDPNKWVDkILELLDALDSYIPT 194
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
5-308 |
6.89e-19 |
|
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: 89.07 E-value: 6.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 5 NIAIIAHVDHGKTTLLDGILRqtgaVTAKEDGERIMDSNDL-----EKEKGITIkakNTAVVYKGT---RINVVDTPGHA 76
Cdd:TIGR00485 14 NVGTIGHVDHGKTTLTAAITT----VLAKEGGAAARAYDQIdnapeEKARGITI---NTAHVEYETetrHYAHVDCPGHA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 77 DFGGEVERVLATADSCLLLVDAFDGPMPQTRFVLGKSLQLGHRPILV-INKIDRpgARPEAVVDMA----FDLFSDLGAT 151
Cdd:TIGR00485 87 DYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKCDM--VDDEELLELVemevRELLSQYDFP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 152 DEqlDFPIVYASAKQgwAVHNLSESPGTNLDpLLDTVLKHVPPVQADTEAPLQFQVTSLDYNDYVGRIAVGKIYAGKMAL 231
Cdd:TIGR00485 165 GD--DTPIIRGSALK--ALEGDAEWEAKILE-LMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 232 GMNVIQLAAKKTETAPSADTALFritklynfeglkRNEVNAAEAGDIVAI----AGLPDVFIGDTICEPGKPAPRPAIEV 307
Cdd:TIGR00485 240 GEEVEIVGLKDTRKTTVTGVEMF------------RKELDEGRAGDNVGLllrgIKREEIERGMVLAKPGSIKPHTKFEA 307
|
.
gi 446328044 308 E 308
Cdd:TIGR00485 308 E 308
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
6-189 |
8.14e-19 |
|
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: 89.69 E-value: 8.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 6 IAIIAHVDHGKTTLLDGIlRQTGaVTAKEDGerimdsndlekekGIT--IKAknTAVVYKGTRINVVDTPGHADF----- 78
Cdd:COG0532 7 VTVMGHVDHGKTSLLDAI-RKTN-VAAGEAG-------------GITqhIGA--YQVETNGGKITFLDTPGHEAFtamra 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 79 -GGEVervlatADSCLLLVDAFDGPMPQTRfvlgKSLQlgHR-----PILV-INKIDRPGARPEAVVD--MAFDLFS-DL 148
Cdd:COG0532 70 rGAQV------TDIVILVVAADDGVMPQTI----EAIN--HAkaagvPIIVaINKIDKPGANPDRVKQelAEHGLVPeEW 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446328044 149 GAtdeqlDFPIVYASAKQgwavhnlsespGTNLDPLLDTVL 189
Cdd:COG0532 138 GG-----DTIFVPVSAKT-----------GEGIDELLEMIL 162
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
5-297 |
2.17e-18 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 87.69 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 5 NIAIIAHVDHGKTTLLDGI---LRQTGAVTAKeDGERImDSNDLEKEKGITIkakNTA-VVYK-GTRINV-VDTPGHADF 78
Cdd:PRK12736 14 NIGTIGHVDHGKTTLTAAItkvLAERGLNQAK-DYDSI-DAAPEEKERGITI---NTAhVEYEtEKRHYAhVDCPGHADY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 79 ggeVERVL---ATADSCLLLVDAFDGPMPQTR--FVLGKslQLGHRPILV-INKIDRPGaRPEAV--VDMAF-DLFSDLG 149
Cdd:PRK12736 89 ---VKNMItgaAQMDGAILVVAATDGPMPQTRehILLAR--QVGVPYLVVfLNKVDLVD-DEELLelVEMEVrELLSEYD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 150 ATDEqlDFPIVYASAKQGwavhnLSESPG--TNLDPLLDTVLKHVPPVQADTEAPLQFQVTslDYNDYVGR--IAVGKIY 225
Cdd:PRK12736 163 FPGD--DIPVIRGSALKA-----LEGDPKweDAIMELMDAVDEYIPTPERDTDKPFLMPVE--DVFTITGRgtVVTGRVE 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446328044 226 AGKMALGMNVIQLAAKKTETAPSADTALFRitKLynfeglkrneVNAAEAGDIVAI--AGLP--DVFIGDTICEPG 297
Cdd:PRK12736 234 RGTVKVGDEVEIVGIKETQKTVVTGVEMFR--KL----------LDEGQAGDNVGVllRGVDrdEVERGQVLAKPG 297
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
5-308 |
2.24e-17 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 84.88 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 5 NIAIIAHVDHGKTTLLDGI---LRQTGAVTAKEDGEriMDSNDLEKEKGITIkakNTA-VVYKGTRINV--VDTPGHADF 78
Cdd:PLN03127 63 NVGTIGHVDHGKTTLTAAItkvLAEEGKAKAVAFDE--IDKAPEEKARGITI---ATAhVEYETAKRHYahVDCPGHADY 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 79 GGEVERVLATADSCLLLVDAFDGPMPQTRFVLGKSLQLGhRPILV--INKIDRPgARPEAV--VDMAFdlfsdlgatDEQ 154
Cdd:PLN03127 138 VKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVG-VPSLVvfLNKVDVV-DDEELLelVEMEL---------REL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 155 LDF--------PIVYASAkqgwavhnLSESPGTN-------LDPLLDTVLKHVPPVQADTEAPLQFQVTSLDYNDYVGRI 219
Cdd:PLN03127 207 LSFykfpgdeiPIIRGSA--------LSALQGTNdeigknaILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 220 AVGKIYAGKMALGMNVIQLAAKKTETAPSADTALFRITKLYNFeglkrnevnaAEAGDIVA--IAGLP--DVFIGDTICE 295
Cdd:PLN03127 279 ATGRVEQGTIKVGEEVEIVGLRPGGPLKTTVTGVEMFKKILDQ----------GQAGDNVGllLRGLKreDVQRGQVICK 348
|
330
....*....|...
gi 446328044 296 PGKPAPRPAIEVE 308
Cdd:PLN03127 349 PGSIKTYKKFEAE 361
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
5-159 |
2.97e-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: 81.00 E-value: 2.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 5 NIAIIAHVDHGKTTLLDGILRQTGAVT----------AKEDGER------IMDSNDLEKEKGITIKAKNTAVVYKGTRIN 68
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDkrtiekyekeAKEMGKEsfkyawVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 69 VVDTPGHADF-----GGEvervlATADSCLLLVDAFDG-------PMPQTR--FVLGKSL---QLghrpILVINKIDRPG 131
Cdd:cd01883 81 IIDAPGHRDFvknmiTGA-----SQADVAVLVVSARKGefeagfeKGGQTRehALLARTLgvkQL----IVAVNKMDDVT 151
|
170 180 190
....*....|....*....|....*....|....
gi 446328044 132 -----ARPEAVVDMAFDLFSDLGATDEQLDF-PI 159
Cdd:cd01883 152 vnwsqERYDEIKKKVSPFLKKVGYNPKDVPFiPI 185
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
5-306 |
1.27e-16 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 82.74 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 5 NIAIIAHVDHGKTTL---LDGILRQTGAVTAKEDGEriMDSNDLEKEKGITIkakNTAVVYKGTR---INVVDTPGHADF 78
Cdd:PLN03126 83 NIGTIGHVDHGKTTLtaaLTMALASMGGSAPKKYDE--IDAAPEERARGITI---NTATVEYETEnrhYAHVDCPGHADY 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 79 GGEVERVLATADSCLLLVDAFDGPMPQTRFVLGKSLQLGHRPILV-INKIDRpgARPEAVVDMAFDLFSDLGATDE--QL 155
Cdd:PLN03126 158 VKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVfLNKQDQ--VDDEELLELVELEVRELLSSYEfpGD 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 156 DFPIVYASAKQgwAVHNLSESP----GTN-----LDPLLDTVLKHVPPVQADTEAPLQFQVTSLDYNDYVGRIAVGKIYA 226
Cdd:PLN03126 236 DIPIISGSALL--ALEALMENPnikrGDNkwvdkIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVER 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 227 GKMALGMNVIQLAAKKTETAPSADTALFritklynfeglkRNEVNAAEAGDIVAI--AGLPDVFI--GDTICEPGKPAPR 302
Cdd:PLN03126 314 GTVKVGETVDIVGLRETRSTTVTGVEMF------------QKILDEALAGDNVGLllRGIQKADIqrGMVLAKPGSITPH 381
|
....
gi 446328044 303 PAIE 306
Cdd:PLN03126 382 TKFE 385
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
5-307 |
3.92e-16 |
|
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]
Pssm-ID: 129567 [Multi-domain] Cd Length: 581 Bit Score: 81.84 E-value: 3.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 5 NIAIIAHVDHGKTTLLDGIlrqTGavtakedgeriMDSNDL--EKEKGITIKAKNTAVVYKGTRINVVDTPGHADFGGEV 82
Cdd:TIGR00475 2 IIATAGHVDHGKTTLLKAL---TG-----------IAADRLpeEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 83 ERVLATADSCLLLVDAFDGPMPQTRFVLGKSLQLG-HRPILVINKIDRPGARPEAVVDMAFDLFsdLGATDEQLDFPIVY 161
Cdd:TIGR00475 68 IAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGiPHTIVVITKADRVNEEEIKRTEMFMKQI--LNSYIFLKNAKIFK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 162 ASAKQGWAVHNLSESPgTNLDPLLDTVLKHvppvqadteAPLQFQVTSLDYNDYVGRIAVGKIYAGKMALGMNVIQLAAK 241
Cdd:TIGR00475 146 TSAKTGQGIGELKKEL-KNLLESLDIKRIQ---------KPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPIN 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446328044 242 KTetapsadtalFRITKLYNFeglkRNEVNAAEAGDIVAIAgLPDV-----FIGDTICEPGKPAPRPAIEV 307
Cdd:TIGR00475 216 HE----------VRVKAIQAQ----NQDVEIAYAGQRIALN-LMDVepeslKRGLLILTPEDPKLRVVVKF 271
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
1-304 |
6.52e-16 |
|
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: 80.13 E-value: 6.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 1 MEIRNIAIIAHVDHGKTTLLDGILRQTGAVTA------KEDGERI-MDSNDL---------EKEKGITIkakNTAVVYKG 64
Cdd:COG2895 15 KDLLRFITCGSVDDGKSTLIGRLLYDTKSIFEdqlaalERDSKKRgTQEIDLalltdglqaEREQGITI---DVAYRYFS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 65 T--R--InVVDTPGHADF------GGevervlATADSCLLLVDAFDGPMPQTR---FVLgkSLqLGHRPILV-INKIDRP 130
Cdd:COG2895 92 TpkRkfI-IADTPGHEQYtrnmvtGA------STADLAILLIDARKGVLEQTRrhsYIA--SL-LGIRHVVVaVNKMDLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 131 G---ARPEAVVDMAFDLFSDLGATDEQLdFPIvyaSAKQGWavhNLSEsPGTNLD-----PLLDTvLKHVPPVQADTEAP 202
Cdd:COG2895 162 DyseEVFEEIVADYRAFAAKLGLEDITF-IPI---SALKGD---NVVE-RSENMPwydgpTLLEH-LETVEVAEDRNDAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 203 LQFQV-----TSLDYNDYVGRIAvgkiyAGKMALGMNVIQLaakktetaPSADTAlfRITKLYNFEGlkrnEVNAAEAGD 277
Cdd:COG2895 233 FRFPVqyvnrPNLDFRGYAGTIA-----SGTVRVGDEVVVL--------PSGKTS--TVKSIVTFDG----DLEEAFAGQ 293
|
330 340
....*....|....*....|....*....
gi 446328044 278 IVAIAGLPDVFI--GDTICEPGKPaPRPA 304
Cdd:COG2895 294 SVTLTLEDEIDIsrGDVIVAADAP-PEVA 321
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
6-189 |
1.15e-15 |
|
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: 80.20 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 6 IAIIAHVDHGKTTLLDGIlRQTgAVTAKEDGerimdsndlekekGITIKAKNTAVVYK-GTRINVVDTPGHADFGGEVER 84
Cdd:TIGR00487 90 VTIMGHVDHGKTSLLDSI-RKT-KVAQGEAG-------------GITQHIGAYHVENEdGKMITFLDTPGHEAFTSMRAR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 85 VLATADSCLLLVDAFDGPMPQTRFVL--GKSLQLghrPILV-INKIDRPGARPEAVVD--MAFDLFSDLGATDEQLdfpi 159
Cdd:TIGR00487 155 GAKVTDIVVLVVAADDGVMPQTIEAIshAKAANV---PIIVaINKIDKPEANPDRVKQelSEYGLVPEDWGGDTIF---- 227
|
170 180 190
....*....|....*....|....*....|
gi 446328044 160 VYASAKQgwavhnlsespGTNLDPLLDTVL 189
Cdd:TIGR00487 228 VPVSALT-----------GDGIDELLDMIL 246
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
5-202 |
1.29e-15 |
|
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: 79.04 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 5 NIAIIAHVDHGKTTLldgilrqTGAVT---AKEDGERIMDSNDL-----EKEKGITIkakNTAVVYKGTRIN---VVDTP 73
Cdd:COG0050 14 NIGTIGHVDHGKTTL-------TAAITkvlAKKGGAKAKAYDQIdkapeEKERGITI---NTSHVEYETEKRhyaHVDCP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 74 GHADF------GGevervlATADSCLLLVDAFDGPMPQTR--FVLGKslQLGHRPILV-INKIDRpGARPEAV--VDMAF 142
Cdd:COG0050 84 GHADYvknmitGA------AQMDGAILVVSATDGPMPQTRehILLAR--QVGVPYIVVfLNKCDM-VDDEELLelVEMEV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446328044 143 -DLFSDLGATDEqlDFPIVYASAKQgwAVHNLSESPGTN-LDPLLDTVLKHVPPVQADTEAP 202
Cdd:COG0050 155 rELLSKYGFPGD--DTPIIRGSALK--ALEGDPDPEWEKkILELMDAVDSYIPEPERDTDKP 212
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
3-133 |
1.53e-15 |
|
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]
Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 74.33 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 3 IRNIAIIAHVDHGKTTLLDGILRQTGAVTAKEDGERIMDSNDLEKEKGITIKakntavvykgtrINVVDTPGHADF---- 78
Cdd:TIGR00231 1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNYVTTVIEEDGKTYK------------FNLLDTAGQEDYdair 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 446328044 79 ---GGEVERVLATADSCLLLVDAFDGPMPQTRfVLGKSLQLGHRPILVINKIDRPGAR 133
Cdd:TIGR00231 69 rlyYPQVERSLRVFDIVILVLDVEEILEKQTK-EIIHHADSGVPIILVGNKIDLKDAD 125
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
5-202 |
2.70e-15 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 77.92 E-value: 2.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 5 NIAIIAHVDHGKTTLldgilrqTGAVT---AKEDGERIMDSNDL-----EKEKGITIkakNTA-VVYK-GTRINV-VDTP 73
Cdd:PRK00049 14 NVGTIGHVDHGKTTL-------TAAITkvlAKKGGAEAKAYDQIdkapeEKARGITI---NTAhVEYEtEKRHYAhVDCP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 74 GHADFggeVERVLATA---DSCLLLVDAFDGPMPQTR--FVLGKslQLGHRPILV-INKIDRPgARPEAV--VDMAF-DL 144
Cdd:PRK00049 84 GHADY---VKNMITGAaqmDGAILVVSAADGPMPQTRehILLAR--QVGVPYIVVfLNKCDMV-DDEELLelVEMEVrEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446328044 145 FSDLGATDEqlDFPIVYASAKQgwAVHNLSESPGTN-LDPLLDTVLKHVPPVQADTEAP 202
Cdd:PRK00049 158 LSKYDFPGD--DTPIIRGSALK--ALEGDDDEEWEKkILELMDAVDSYIPTPERAIDKP 212
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
5-128 |
7.97e-15 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 76.80 E-value: 7.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 5 NIAIIAHVDHGKTTLldgilrqTGAVT---AKEDGERIMDSNDL-----EKEKGITIkakNTAVVYKGTRIN---VVDTP 73
Cdd:PRK12735 14 NVGTIGHVDHGKTTL-------TAAITkvlAKKGGGEAKAYDQIdnapeEKARGITI---NTSHVEYETANRhyaHVDCP 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446328044 74 GHADFggeVERVLATA---DSCLLLVDAFDGPMPQTR--FVLGKslQLGHRPILV-INKID 128
Cdd:PRK12735 84 GHADY---VKNMITGAaqmDGAILVVSAADGPMPQTRehILLAR--QVGVPYIVVfLNKCD 139
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
11-167 |
1.92e-14 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.
Pssm-ID: 206734 [Multi-domain] Cd Length: 170 Bit Score: 71.48 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 11 HVDHGKTTLldgILRQTGAVTakedgerimDSNDLEKEKGITIkakNTAVVY----KGTRINVVDTPGHADFggeVERVL 86
Cdd:cd04171 7 HIDHGKTTL---IKALTGIET---------DRLPEEKKRGITI---DLGFAYldlpDGKRLGFIDVPGHEKF---VKNML 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 87 ATA---DSCLLLVDAFDGPMPQTRFVLG--KSLQLGHrPILVINKIDR-PGARPEAVVDmafDLFSDLGATDEQlDFPIV 160
Cdd:cd04171 69 AGAggiDAVLLVVAADEGIMPQTREHLEilELLGIKK-GLVVLTKADLvDEDRLELVEE---EILELLAGTFLA-DAPIF 143
|
....*..
gi 446328044 161 YASAKQG 167
Cdd:cd04171 144 PVSSVTG 150
|
|
| EFG_mtEFG_II |
cd04088 |
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation ... |
215-295 |
6.41e-14 |
|
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: 67.16 E-value: 6.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 215 YVGRIAVGKIYAGKMALGMNVIQLAAKKTEtapsadtalfRITKLYNFEGLKRNEVNAAEAGDIVAIAGLPDVFIGDTIC 294
Cdd:cd04088 13 FVGKLTFFRVYSGTLKSGSTVYNSTKGKKE----------RVGRLLRMHGKKREEVEELGAGDIGAVVGLKDTRTGDTLC 82
|
.
gi 446328044 295 E 295
Cdd:cd04088 83 D 83
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
8-308 |
6.55e-14 |
|
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 442507 [Multi-domain] Cd Length: 630 Bit Score: 74.95 E-value: 6.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 8 IIA---HVDHGKTTLldgILRQTGavtakedgeriMDSNDL--EKEKGITI-------KAKNtavvykGTRINVVDTPGH 75
Cdd:COG3276 2 IIGtagHIDHGKTTL---VKALTG-----------IDTDRLkeEKKRGITIdlgfaylPLPD------GRRLGFVDVPGH 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 76 ADFggeVERVLATA---DSCLLLVDAFDGPMPQTR---FVLgkSLqLG-HRPILVINKIDR-PGARPEAVVDMAFDLFSD 147
Cdd:COG3276 62 EKF---IKNMLAGAggiDLVLLVVAADEGVMPQTRehlAIL--DL-LGiKRGIVVLTKADLvDEEWLELVEEEIRELLAG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 148 LGatdeqL-DFPIVYASAKQgwavhnlsespGTNLDPL---LDTVLKHVPPvqADTEAPLQ------FQVTSldyndyVG 217
Cdd:COG3276 136 TF-----LeDAPIVPVSAVT-----------GEGIDELraaLDALAAAVPA--RDADGPFRlpidrvFSIKG------FG 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 218 RIAVGKIYAGKMALGMNViqlaakktETAPSADTAlfRItklynfeglkRN------EVNAAEAGDIVAI--AGLP--DV 287
Cdd:COG3276 192 TVVTGTLLSGTVRVGDEL--------ELLPSGKPV--RV----------RGiqvhgqPVEEAYAGQRVALnlAGVEkeEI 251
|
330 340
....*....|....*....|.
gi 446328044 288 FIGDTICEPGKPAPRPAIEVE 308
Cdd:COG3276 252 ERGDVLAAPGALRPTDRIDVR 272
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
7-190 |
4.50e-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: 67.48 E-value: 4.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 7 AIIAHVDHGKTTLLDGILRQTGAVTAKEDGErimdsndlekekGITIKAKNTAVVYKGTRINVVDTPGHADFGG-----E 81
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGT------------TRDPDVYVKELDKGKVKLVLVDTPGLDEFGGlgreeL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 82 VERVLATADSCLLLVDAFDGPMP--QTRFVLGKSLQLGHRPILVINKIDRPGARPEAVVDMAFDLFsdlgatdEQLDFPI 159
Cdd:cd00882 69 ARLLLRGADLILLVVDSTDRESEedAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELA-------KILGVPV 141
|
170 180 190
....*....|....*....|....*....|.
gi 446328044 160 VYASAKQGWavhnlsespgtNLDPLLDTVLK 190
Cdd:cd00882 142 FEVSAKTGE-----------GVDELFEKLIE 161
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
5-167 |
3.48e-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: 65.46 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 5 NIAIIAHVDHGKTTLLDGIlrQTGAVTAKedgeriMDSNDLEKEKGITI--------------KAKNTAVVYKGTRINVV 70
Cdd:cd01889 2 NVGLLGHVDSGKTSLAKAL--SEIASTAA------FDKNPQSQERGITLdlgfssfevdkpkhLEDNENPQIENYQITLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 71 DTPGHADFggeVERVLATA---DSCLLLVDAFDGPMPQTR--FVLGKSLQLghRPILVINKID--RPGARPEAVVDMAFD 143
Cdd:cd01889 74 DCPGHASL---IRTIIGGAqiiDLMLLVVDAKKGIQTQTAecLVIGELLCK--PLIVVLNKIDliPEEERKRKIEKMKKR 148
|
170 180
....*....|....*....|....
gi 446328044 144 LFSDLGATdEQLDFPIVYASAKQG 167
Cdd:cd01889 149 LQKTLEKT-RLKDSPIIPVSAKPG 171
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
5-232 |
1.24e-11 |
|
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: 66.61 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 5 NIAIIAHVDHGKTTLLDGIlrqTGAVTakedgerimDSNDLEKEKGITIKAKNT-AVVYK-------------------G 64
Cdd:TIGR03680 6 NIGMVGHVDHGKTTLTKAL---TGVWT---------DTHSEELKRGISIRLGYAdAEIYKcpecdgpecyttepvcpncG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 65 T------RINVVDTPGHadfggevERVLAT-------ADSCLLLVDAFDG-PMPQTRFVLgKSLQ-LGHRPILVI-NKID 128
Cdd:TIGR03680 74 SetellrRVSFVDAPGH-------ETLMATmlsgaalMDGALLVIAANEPcPQPQTKEHL-MALEiIGIKNIVIVqNKID 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 129 rpgarpeaVVD--MAFDLFSDL-----GATDEqlDFPIVYASAKQgwavhnlsespGTNLDPLLDTVLKHVPPVQADTEA 201
Cdd:TIGR03680 146 --------LVSkeKALENYEEIkefvkGTVAE--NAPIIPVSALH-----------NANIDALLEAIEKFIPTPERDLDK 204
|
250 260 270
....*....|....*....|....*....|....*....
gi 446328044 202 PLQFQVT-SLDYN-------DYVGRIAVGKIYAGKMALG 232
Cdd:TIGR03680 205 PPLMYVArSFDVNkpgtppeKLKGGVIGGSLIQGKLKVG 243
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
12-279 |
2.33e-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: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 12 VDHGKTTLLDGILRQTGAVTAK-------------EDGERI-----MDSNDLEKEKGITIkakNTAVVYKGT---RINVV 70
Cdd:TIGR02034 9 VDDGKSTLIGRLLHDTKQIYEDqlaalerdskkhgTQGGEIdlallVDGLQAEREQGITI---DVAYRYFSTdkrKFIVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 71 DTPGHADFGGEVERVLATADSCLLLVDAFDGPMPQTRFVLGKSLQLGHRPILV-INKIDrpgarpeaVVDMAFDLFSDLG 149
Cdd:TIGR02034 86 DTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLaVNKMD--------LVDYDEEVFENIK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 150 AT----DEQLDFPIVYA---SAKQGWAVHNLSES----PGTNLDPLLDTVlkhvpPVQADTEA-PLQFQVT-----SLDY 212
Cdd:TIGR02034 158 KDylafAEQLGFRDVTFiplSALKGDNVVSRSESmpwySGPTLLEILETV-----EVERDAQDlPLRFPVQyvnrpNLDF 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446328044 213 NDYVGRIAvgkiyAGKMALGMNVIQLaakktetaPSADTAlfRITKLYNFEGlkrnEVNAAEAGDIV 279
Cdd:TIGR02034 233 RGYAGTIA-----SGSVHVGDEVVVL--------PSGRSS--RVARIVTFDG----DLEQARAGQAV 280
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
6-134 |
3.44e-11 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 65.97 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 6 IAIIAHVDHGKTTLLDGIlRQTgAVTAKEDGE-------RIMDSNDLEKEKGITIKAKNTAVVYKGtrINVVDTPGHADF 78
Cdd:PRK04004 9 VVVLGHVDHGKTTLLDKI-RGT-AVAAKEAGGitqhigaTEVPIDVIEKIAGPLKKPLPIKLKIPG--LLFIDTPGHEAF 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446328044 79 ------GGevervlATADSCLLLVDAFDGPMPQTRfvlgKSLQLGHR---P-ILVINKIDR-PGARP 134
Cdd:PRK04004 85 tnlrkrGG------ALADIAILVVDINEGFQPQTI----EAINILKRrktPfVVAANKIDRiPGWKS 141
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
5-239 |
2.47e-10 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 62.84 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 5 NIAIIAHVDHGKTTL-------LDGILRQTGAVTAKEDGER---------IMDSNDLEKEKGITI-----KAKNTAVVYk 63
Cdd:PTZ00141 9 NLVVIGHVDSGKSTTtghliykCGGIDKRTIEKFEKEAAEMgkgsfkyawVLDKLKAERERGITIdialwKFETPKYYF- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 64 gtriNVVDTPGHADFGGEVERVLATADSCLLLVDA----FDGPMP---QTRFVLGKSLQLGHRPILV-INKIDRPG---- 131
Cdd:PTZ00141 88 ----TIIDAPGHRDFIKNMITGTSQADVAILVVAStageFEAGISkdgQTREHALLAFTLGVKQMIVcINKMDDKTvnys 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 132 -ARPEAVVDMAFDLFSDLGATDEQLDF-PIvyasakQGWAVHNLSEsPGTNL----DPLLDTVLKHVPPVQADTEAPLQF 205
Cdd:PTZ00141 164 qERYDEIKKEVSAYLKKVGYNPEKVPFiPI------SGWQGDNMIE-KSDNMpwykGPTLLEALDTLEPPKRPVDKPLRL 236
|
250 260 270
....*....|....*....|....*....|....
gi 446328044 206 QVTSLDYNDYVGRIAVGKIYAGKMALGMnVIQLA 239
Cdd:PTZ00141 237 PLQDVYKIGGIGTVPVGRVETGILKPGM-VVTFA 269
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
5-128 |
2.74e-10 |
|
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: 60.28 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 5 NIAIIAHVDHGKTTLLDGILRQTGAV------------TAKEDGERI-----MDSNDLEKEKGITIkakNTAVVYKGT-- 65
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSIfedqlaalerskSSGTQGEKLdlallVDGLQAEREQGITI---DVAYRYFSTpk 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446328044 66 -RINVVDTPGHADFGGEVERVLATADSCLLLVDAFDGPMPQTR---FVLgkSLqLGHRPILV-INKID 128
Cdd:cd04166 78 rKFIIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRrhsYIA--SL-LGIRHVVVaVNKMD 142
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
217-294 |
6.16e-10 |
|
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: 55.73 E-value: 6.16e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446328044 217 GRIAVGKIYAGKMALGMNVIQLAAKKTEtapsaDTALFRITKLYNFEGLKRNEVNAAEAGDIVAIAGLPDVFIGDTIC 294
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTGK-----KKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
6-167 |
8.39e-10 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 61.61 E-value: 8.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 6 IAIIAHVDHGKTTLLDGIlrqTGAvtakeDGERIMDsndlEKEKGITIkakNTAVVY----KGTRINVVDTPGHADFgge 81
Cdd:PRK10512 3 IATAGHVDHGKTTLLQAI---TGV-----NADRLPE----EKKRGMTI---DLGYAYwpqpDGRVLGFIDVPGHEKF--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 82 VERVLATA---DSCLLLVDAFDGPMPQTRFVLGkSLQLGHRPIL--VINKIDR-PGARPEAVVDMAFDLFSDLGATDEQL 155
Cdd:PRK10512 65 LSNMLAGVggiDHALLVVACDDGVMAQTREHLA-ILQLTGNPMLtvALTKADRvDEARIAEVRRQVKAVLREYGFAEAKL 143
|
170
....*....|..
gi 446328044 156 dFPIVyASAKQG 167
Cdd:PRK10512 144 -FVTA-ATEGRG 153
|
|
| EFG_III-like |
cd16257 |
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G ... |
329-388 |
2.71e-09 |
|
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: 53.89 E-value: 2.71e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446328044 329 KFVTTRNIRERLDRELETNVAMRLEETEDKDRFKVLGRGELHLSVLIETMRRE-GFEIQVS 388
Cdd:cd16257 11 NPLDQEKLLEGLERLSEEDPALQVYREESTGEFILSGLGELHLEIIVARLEREyGVELVVS 71
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
70-194 |
4.92e-09 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 57.69 E-value: 4.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 70 VDTPG-----HAdFG----GEVERVLATADSCLLLVDAFDGPMPQTRFVLGKsLQLGHRP-ILVINKIDRpgARPEAVVD 139
Cdd:COG1159 56 VDTPGihkpkRK-LGrrmnKAAWSALEDVDVILFVVDATEKIGEGDEFILEL-LKKLKTPvILVINKIDL--VKKEELLP 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 446328044 140 MAfDLFSDLGATDEqldfpIVYASAKQgwavhnlsespGTNLDPLLDTVLKHVPP 194
Cdd:COG1159 132 LL-AEYSELLDFAE-----IVPISALK-----------GDNVDELLDEIAKLLPE 169
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
15-191 |
6.47e-09 |
|
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: 55.55 E-value: 6.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 15 GKTTLLDGILRQTGAVTAKEDG---ERIMdsndlekekGITIKaKNTAVVYkgtrinvVDTPG-HADFGG-------EVE 83
Cdd:cd04163 15 GKSTLLNALVGQKISIVSPKPQttrNRIR---------GIYTD-DDAQIIF-------VDTPGiHKPKKKlgermvkAAW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 84 RVLATADSCLLLVDAFDGPMPQTRFVLgKSLQLGHRP-ILVINKIDRpgARPEAVVDMAFDLFSDLGATDEqldfpIVYA 162
Cdd:cd04163 78 SALKDVDLVLFVVDASEWIGEGDEFIL-ELLKKSKTPvILVLNKIDL--VKDKEDLLPLLEKLKELHPFAE-----IFPI 149
|
170 180
....*....|....*....|....*....
gi 446328044 163 SAKQgwavhnlsespGTNLDPLLDTVLKH 191
Cdd:cd04163 150 SALK-----------GENVDELLEYIVEY 167
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
6-173 |
2.16e-08 |
|
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: 53.98 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 6 IAIIAHVDHGKTTLLDGILRQtgavtakedgERIMDSNdlekEKGITIKAKNTAVVYKGTRINVVDTPG-----HADFGG 80
Cdd:cd01895 5 IAIIGRPNVGKSSLLNALLGE----------ERVIVSD----IAGTTRDSIDVPFEYDGQKYTLIDTAGirkkgKVTEGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 81 E---VERVLAT---ADSCLLLVDAFDGPMPQTRFVLGKSLQLGHRPILVINKIDRPGARPEAVVDMAFDLFSDLGatdeQ 154
Cdd:cd01895 71 EkysVLRTLKAierADVVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKWDLVEKDEKTMKEFEKELRRKLP----F 146
|
170 180
....*....|....*....|
gi 446328044 155 LDF-PIVYASAKQGWAVHNL 173
Cdd:cd01895 147 LDYaPIVFISALTGQGVDKL 166
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
6-133 |
2.41e-08 |
|
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: 56.75 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 6 IAIIAHVDHGKTTLLDGIlRQTgAVTAKEDG----------------ERImdSNDLEKEKGITIKAKNtavvykgtrINV 69
Cdd:TIGR00491 7 VVVLGHVDHGKTTLLDKI-RGT-AVVKKEAGgitqhigasevptdviEKI--CGDLLKSFKIKLKIPG---------LLF 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446328044 70 VDTPGHADFGGEVERVLATADSCLLLVDAFDGPMPQTRFVLgKSLQLGHRPILV-INKIDR-PGAR 133
Cdd:TIGR00491 74 IDTPGHEAFTNLRKRGGALADIAILVVDINEGFKPQTLEAL-NILRSRKTPFVVaANKIDRiPGWK 138
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
12-314 |
3.08e-08 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 56.48 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 12 VDHGKTTLLDGILR--------QTGAVTA--KEDGER--------IMDSNDLEKEKGITIkakNTAVVYKGT---RINVV 70
Cdd:PRK05506 33 VDDGKSTLIGRLLYdskmifedQLAALERdsKKVGTQgdeidlalLVDGLAAEREQGITI---DVAYRYFATpkrKFIVA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 71 DTPGHADFggevERVLAT----ADSCLLLVDAFDGPMPQTR---FVLgkSLqLGHRPILV-INKIDrpgarpeaVVDMAF 142
Cdd:PRK05506 110 DTPGHEQY----TRNMVTgastADLAIILVDARKGVLTQTRrhsFIA--SL-LGIRHVVLaVNKMD--------LVDYDQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 143 DLF----SDLGATDEQLDFPIVYA---SAKQGWAVHNLSE-SP---GTNLDPLLDTvlkhVPPVQADTEAPLQFQVT--- 208
Cdd:PRK05506 175 EVFdeivADYRAFAAKLGLHDVTFipiSALKGDNVVTRSArMPwyeGPSLLEHLET----VEIASDRNLKDFRFPVQyvn 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 209 --SLDYNDYVGRIAvgkiyAGKMALGMNVIQLAAKKTEtapsadtalfRITKLYNFEGlkrnEVNAAEAGDIVAI--AGL 284
Cdd:PRK05506 251 rpNLDFRGFAGTVA-----SGVVRPGDEVVVLPSGKTS----------RVKRIVTPDG----DLDEAFAGQAVTLtlADE 311
|
330 340 350
....*....|....*....|....*....|
gi 446328044 285 PDVFIGDTICEPGKPaPRPAIEVEEPTVSM 314
Cdd:PRK05506 312 IDISRGDMLARADNR-PEVADQFDATVVWM 340
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
5-126 |
3.82e-08 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 51.85 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 5 NIAIIAHVDHGKTTLLDGILRQTGAVTAKEdgerimdsndlekekGITIKAKNTAVVYKGTRINVVDTPG-----HADFG 79
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKAIVSDYP---------------GTTRDPNEGRLELKGKQIILVDTPGliegaSEGEG 65
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 446328044 80 -GEVERVLATADSCLLLVDAFDGPMPQTRFVLGKSLQLGHRPILVINK 126
Cdd:pfam01926 66 lGRAFLAIIEADLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
1-173 |
4.12e-08 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 53.45 E-value: 4.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 1 MEIRNIAIIAHVDHGKTTLLDGILRqtgavtakedgerimDSNDLEKEK---GITIKAKNTAVVYKGTRINVVDTPGHAD 77
Cdd:COG1100 1 MGEKKIVVVGTGGVGKTSLVNRLVG---------------DIFSLEKYLstnGVTIDKKELKLDGLDVDLVIWDTPGQDE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 78 F---GGEVERVLATADSCLLLvdaFDGPMPQTR----FVLGKSLQLG-HRP-ILVINKIDRpgaRPEAVVDMAFDLFSDL 148
Cdd:COG1100 66 FretRQFYARQLTGASLYLFV---VDGTREETLqslyELLESLRRLGkKSPiILVLNKIDL---YDEEEIEDEERLKEAL 139
|
170 180
....*....|....*....|....*
gi 446328044 149 GatdEQLDFPIVYASAKQGWAVHNL 173
Cdd:COG1100 140 S---EDNIVEVVATSAKTGEGVEEL 161
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
15-192 |
4.20e-08 |
|
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: 53.02 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 15 GKTTLLDGILRQTGAVTAKEDGErimdsndlekekgiTIKAKNTAVVYKGTR-INVVDTPGHADFGG-------EVERVL 86
Cdd:cd00880 9 GKSSLLNALLGQNVGIVSPIPGT--------------TRDPVRKEWELLPLGpVVLIDTPGLDEEGGlgrerveEARQVA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 87 ATADSCLLLVDAfDGPMPQTRFVLGKSLQLGHRPILVINKIDRPGARPEAVVDMAFDLfsdlgatDEQLDFPIVYASAKq 166
Cdd:cd00880 75 DRADLVLLVVDS-DLTPVEEEAKLGLLRERGKPVLLVLNKIDLVPESEEEELLRERKL-------ELLPDLPVIAVSAL- 145
|
170 180
....*....|....*....|....*.
gi 446328044 167 gwavhnlsesPGTNLDPLLDTVLKHV 192
Cdd:cd00880 146 ----------PGEGIDELRKKIAELL 161
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
70-194 |
8.42e-08 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 53.90 E-value: 8.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 70 VDTPG----HADFG----GEVERVLATADSCLLLVDAFDGPMPQTRFVLGKsLQLGHRP-ILVINKIDRPGARPEavvdm 140
Cdd:PRK00089 58 VDTPGihkpKRALNramnKAAWSSLKDVDLVLFVVDADEKIGPGDEFILEK-LKKVKTPvILVLNKIDLVKDKEE----- 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 446328044 141 afdLFSDLGATDEQLDF-PIVYASAKQgwavhnlsespGTNLDPLLDTVLKHVPP 194
Cdd:PRK00089 132 ---LLPLLEELSELMDFaEIVPISALK-----------GDNVDELLDVIAKYLPE 172
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
5-213 |
1.32e-07 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 54.09 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 5 NIAIIAHVDHGKTTLLDGIlrqTGAVTakedgerimDSNDLEKEKGITIK---AKntAVVYK------------------ 63
Cdd:PRK04000 11 NIGMVGHVDHGKTTLVQAL---TGVWT---------DRHSEELKRGITIRlgyAD--ATIRKcpdceepeayttepkcpn 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 64 -GT------RINVVDTPGHadfggevERVLAT-------ADSCLLLVDAFDG-PMPQTRFVLgKSLQ-LGHRPILVI-NK 126
Cdd:PRK04000 77 cGSetellrRVSFVDAPGH-------ETLMATmlsgaalMDGAILVIAANEPcPQPQTKEHL-MALDiIGIKNIVIVqNK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 127 IDrpgarpeaVVD--MAFDLFSDL-----GATDEqlDFPIVYASAKQgwavhnlsespGTNLDPLLDTVLKHVPPVQADT 199
Cdd:PRK04000 149 ID--------LVSkeRALENYEQIkefvkGTVAE--NAPIIPVSALH-----------KVNIDALIEAIEEEIPTPERDL 207
|
250
....*....|....*
gi 446328044 200 EAPLQFQVT-SLDYN 213
Cdd:PRK04000 208 DKPPRMYVArSFDVN 222
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
12-281 |
1.52e-07 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 54.15 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 12 VDHGKTTLLDGILRQTGAVtaKED---------------GERI-----MDSNDLEKEKGITIkakNTAVVYKGT---RIN 68
Cdd:PRK05124 36 VDDGKSTLIGRLLHDTKQI--YEDqlaslhndskrhgtqGEKLdlallVDGLQAEREQGITI---DVAYRYFSTekrKFI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 69 VVDTPGHADFggevERVLAT----ADSCLLLVDAFDGPMPQTR---FVlgkSLQLGHRPILV-INKIDRPG---ARPEAV 137
Cdd:PRK05124 111 IADTPGHEQY----TRNMATgastCDLAILLIDARKGVLDQTRrhsFI---ATLLGIKHLVVaVNKMDLVDyseEVFERI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 138 VDMAFDLFSDLGAtdeQLDFPIVYASAKQGWAVHNLSES-PGTNLDPLLDtVLKHVPPVQADTEAPLQFQVT-----SLD 211
Cdd:PRK05124 184 REDYLTFAEQLPG---NLDIRFVPLSALEGDNVVSQSESmPWYSGPTLLE-VLETVDIQRVVDAQPFRFPVQyvnrpNLD 259
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446328044 212 YNDYVGRIAVGKIYAGK--MALgmnviqlaakktetaPSADTAlfRITKLYNFEGlkrnEVNAAEAGDIVAI 281
Cdd:PRK05124 260 FRGYAGTLASGVVKVGDrvKVL---------------PSGKES--NVARIVTFDG----DLEEAFAGEAITL 310
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
5-282 |
1.89e-07 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 53.78 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 5 NIAIIAHVDHGKTTLLdGILrqtgaVTAK-EDGE---RIM-DSNDLEKEKGIT----------------------IKAKN 57
Cdd:COG5258 124 VVGVAGHVDHGKSTLV-GTL-----VTGKlDDGNggtRSFlDVQPHEVERGLSadlsyavygfdddgpvrmknplRKTDR 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 58 TAVVYKGTRI-NVVDTPGHadfggevERVLATA---------DSCLLLVDAFDGPMPQTRFVLGKSLQLGHRPILVINKI 127
Cdd:COG5258 198 ARVVEESDKLvSFVDTVGH-------EPWLRTTirglvgqklDYGLLVVAADDGPTHTTREHLGILLAMDLPVIVAITKI 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 128 DR-PGARPEAVVDMAFDLFSDLG--------------ATDEQLDF--PIVYASAkqgwavhnlseSPGTNLDpLLDTVLK 190
Cdd:COG5258 271 DKvDDERVEEVEREIENLLRIVGrtplevesrhdvdaAIEEINGRvvPILKTSA-----------VTGEGLD-LLDELFE 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 191 HVPPVQADTEAPLQ------FQVTSldyndyVGRIAVGKIYAGKMALGMNVIqlaakkteTAPSADTAlFRITKLYNFEg 264
Cdd:COG5258 339 RLPKRATDEDEPFLmyidriYNVTG------VGTVVSGTVKSGKVEAGDELL--------IGPTKDGS-FREVEVKSIE- 402
|
330
....*....|....*...
gi 446328044 265 LKRNEVNAAEAGDIVAIA 282
Cdd:COG5258 403 MHYHRVDKAEAGRIVGIA 420
|
|
| EFG_C |
smart00838 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
403-479 |
5.04e-07 |
|
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: 47.88 E-value: 5.04e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446328044 403 LEPYEYLVMDVPDQFTGAIIAELNRRKGELQLMDAHpSGMTRVEFVIPTRGIIGFRGFFISETRGEGVMSSRFLRFD 479
Cdd:smart00838 2 LEPIMKVEVTVPEEYMGDVIGDLNSRRGKIEGMEQR-GGAQVIKAKVPLSEMFGYATDLRSATQGRATWSMEFSHYE 77
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
5-235 |
6.40e-07 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 52.01 E-value: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 5 NIAIIAHVDHGKTTLLDGILRQTGAV----------TAKEDGER------IMDSNDLEKEKGITIKA---KNTAVVYKGT 65
Cdd:PLN00043 9 NIVVIGHVDSGKSTTTGHLIYKLGGIdkrvierfekEAAEMNKRsfkyawVLDKLKAERERGITIDIalwKFETTKYYCT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 66 rinVVDTPGHADFGGEVERVLATADSCLLLVDAFDGPMP-------QTRFVLGKSLQLG-HRPILVINKIDR-----PGA 132
Cdd:PLN00043 89 ---VIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGvKQMICCCNKMDAttpkySKA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 133 RPEAVVDMAFDLFSDLGATDEQLDF-PIvyasakQGWAVHNLSESpGTNLD----PLLDTVLKHVPPVQADTEAPLQFQV 207
Cdd:PLN00043 166 RYDEIVKEVSSYLKKVGYNPDKIPFvPI------SGFEGDNMIER-STNLDwykgPTLLEALDQINEPKRPSDKPLRLPL 238
|
250 260
....*....|....*....|....*...
gi 446328044 208 TSLDYNDYVGRIAVGKIYAGKMALGMNV 235
Cdd:PLN00043 239 QDVYKIGGIGTVPVGRVETGVIKPGMVV 266
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
5-128 |
9.63e-07 |
|
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.
Pssm-ID: 206675 [Multi-domain] Cd Length: 197 Bit Score: 49.57 E-value: 9.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 5 NIAIIAHVDHGKTTL---LDGIlrQTgaVTAKEdgerimdsndlEKEKGITIK-----AK----------NTAVVYKGTR 66
Cdd:cd01888 2 NIGTIGHVAHGKTTLvkaLSGV--WT--VRHKE-----------ELKRNITIKlgyanAKiykcpncgcpRPYDTPECEC 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 67 ------------INVVDTPGHadfggevERVLAT-------ADSCLLLVDAFDG-PMPQTR--FVLGKSLQLGHRpILVI 124
Cdd:cd01888 67 pgcggetklvrhVSFVDCPGH-------EILMATmlsgaavMDGALLLIAANEPcPQPQTSehLAALEIMGLKHI-IILQ 138
|
....
gi 446328044 125 NKID 128
Cdd:cd01888 139 NKID 142
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
203-294 |
1.02e-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: 46.87 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 203 LQFQVTSLDYNDYVGRIAVGKIYAGKMALGMNVIQLAAKKTEtapsadtalfRITKLYNFEGlkrnEVNAAEAGDIVAIA 282
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITG----------RVTSIERFHE----EVDEAKAGDIVGIG 66
|
90
....*....|....
gi 446328044 283 GLP--DVFIGDTIC 294
Cdd:cd01342 67 ILGvkDILTGDTLT 80
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
60-223 |
1.10e-06 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 51.18 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 60 VVYKGTRINVVDTPG-----HADFGGE----VERVLATADSCLLLVDAFDGPMPQTRFVlGKSLQLGHRP-ILVINKIDR 129
Cdd:COG1160 45 AEWGGREFTLIDTGGiepddDDGLEAEireqAELAIEEADVILFVVDGRAGLTPLDEEI-AKLLRRSGKPvILVVNKVDG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 130 PGARPEavvdmAFDLFSdLGatdeqLD--FPIvyaSAKQgwavhnlsespGTNLDPLLDTVLKHVPPVQADTEA--PLQF 205
Cdd:COG1160 124 PKREAD-----AAEFYS-LG-----LGepIPI---SAEH-----------GRGVGDLLDAVLELLPEEEEEEEEddPIKI 178
|
170
....*....|....*...
gi 446328044 206 QVtsldyndyVGRIAVGK 223
Cdd:COG1160 179 AI--------VGRPNVGK 188
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
5-213 |
2.35e-06 |
|
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: 50.22 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 5 NIAIIAHVDHGKTTLLDGIlrqTGAVTAKedgerimdsNDLEKEKGITIK---AknTAVVYK------------------ 63
Cdd:COG5257 7 NIGVVGHVDHGKTTLVQAL---TGVWTDR---------HSEELKRGITIRlgyA--DATFYKcpnceppeayttepkcpn 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 64 -GT------RINVVDTPGHadfggevERVLATA-------DSCLLLVDAFDG-PMPQTRFVLgKSLQ-LGHRPILVI-NK 126
Cdd:COG5257 73 cGSetellrRVSFVDAPGH-------ETLMATMlsgaalmDGAILVIAANEPcPQPQTKEHL-MALDiIGIKNIVIVqNK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 127 IDrpgarpeaVVDM--AFDLFSDL-----GATDEqlDFPIVYASAKQgwavhnlsespGTNLDPLLDTVLKHVPPVQADT 199
Cdd:COG5257 145 ID--------LVSKerALENYEQIkefvkGTVAE--NAPIIPVSAQH-----------KVNIDALIEAIEEEIPTPERDL 203
|
250
....*....|....*
gi 446328044 200 EA-PLQFQVTSLDYN 213
Cdd:COG5257 204 SKpPRMLVARSFDVN 218
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
64-223 |
7.60e-06 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 48.51 E-value: 7.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 64 GTRINVVDTPG----HADFGGEV----ERVLATADSCLLLVDAFDGPMPQTRFVlGKSLQLGHRP-ILVINKIDRPGARp 134
Cdd:PRK00093 48 GREFILIDTGGiepdDDGFEKQIreqaELAIEEADVILFVVDGRAGLTPADEEI-AKILRKSNKPvILVVNKVDGPDEE- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 135 eavvDMAFDLFSdLGATDEqldFPIvyaSakqgwAVHnlsespGTNLDPLLDTVLKHVPPVQADTEAPLQFQVTsldynd 214
Cdd:PRK00093 126 ----ADAYEFYS-LGLGEP---YPI---S-----AEH------GRGIGDLLDAILEELPEEEEEDEEDEPIKIA------ 177
|
....*....
gi 446328044 215 YVGRIAVGK 223
Cdd:PRK00093 178 IIGRPNVGK 186
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
5-166 |
3.83e-05 |
|
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: 44.46 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 5 NIAIIAHVDHGKTTLLDGILrqtgavtakedGERIMDSndlekekGIT-IKAKNTAVVY---KGTRInvVDTPG------ 74
Cdd:cd09912 2 LLAVVGEFSAGKSTLLNALL-----------GEEVLPT-------GVTpTTAVITVLRYgllKGVVL--VDTPGlnstie 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 75 -HADfggEVERVLATADSCLLLVDAfDGPMPQT--RFVLGKSLQLGHRPILVINKIDRpgARPEAVVDMAFDLFSDLGAT 151
Cdd:cd09912 62 hHTE---ITESFLPRADAVIFVLSA-DQPLTESerEFLKEILKWSGKKIFFVLNKIDL--LSEEELEEVLEYSREELGVL 135
|
170
....*....|....*.
gi 446328044 152 DEQLDFPIVYA-SAKQ 166
Cdd:cd09912 136 ELGGGEPRIFPvSAKE 151
|
|
| EngA1 |
cd01894 |
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
62-191 |
5.15e-05 |
|
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: 43.96 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 62 YKGTRINVVDTPGHADFGGE--------VERVLATADSCLLLVDAFDGPMPQTRFVLgKSLQLGHRP-ILVINKIDRPGA 132
Cdd:cd01894 42 WGGREFILIDTGGIEPDDEGiskeireqAEIAIEEADVILFVVDGREGLTPADEEIA-KYLRKSKKPvILVVNKIDNIKE 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 446328044 133 RpeavvDMAFDLFSdLGATDeqldfpIVYASakqgwAVHnlsespGTNLDPLLDTVLKH 191
Cdd:cd01894 121 E-----EEAAEFYS-LGFGE------PIPIS-----AEH------GRGIGDLLDAILEL 156
|
|
| EFG_mtEFG_C |
cd03713 |
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational ... |
404-479 |
1.16e-04 |
|
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: 40.97 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 404 EPYEYLVMDVPDQFTGAIIAELNRRKGELQLMDAHpSGMTRVEFVIPTRGIIGF----RgffiSETRGEGVMSSRFLRFD 479
Cdd:cd03713 1 EPIMKVEVTVPEEYMGDVIGDLSSRRGQILGTESR-GGWKVIKAEVPLAEMFGYstdlR----SLTQGRGSFTMEFSHYE 75
|
|
| mtEFG2_II_like |
cd04092 |
Domain II of mitochondrial elongation factor G2-like proteins found in eukaryotes; Eukaryotic ... |
223-293 |
1.23e-04 |
|
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: 40.76 E-value: 1.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446328044 223 KIYAGKMALGMNVIQLAAKKTEtapsadtalfRITKLYNFEGLKRNEVNAAEAGDIVAIAGLPDVFIGDTI 293
Cdd:cd04092 21 RVYSGTLKAGSNVYNTTTGKKE----------RISRLLKMHADQTEEVDSLSAGNIGVITGLKVTSTGDTL 81
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
2-190 |
2.34e-04 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 43.89 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 2 EIRnIAIIAHVDHGKTTLLDGILRQtgavtakedgERIMDSNdlekEKGITIKAKNTAVVYKGTRINVVDTPG------- 74
Cdd:PRK00093 173 PIK-IAIIGRPNVGKSSLINALLGE----------ERVIVSD----IAGTTRDSIDTPFERDGQKYTLIDTAGirrkgkv 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 75 HADfggeVER--VLAT------ADSCLLLVDAFDGPMPQTRFVLGKSLQLGhRP-ILVINKIDrpgarpeAVVDMAFDLF 145
Cdd:PRK00093 238 TEG----VEKysVIRTlkaierADVVLLVIDATEGITEQDLRIAGLALEAG-RAlVIVVNKWD-------LVDEKTMEEF 305
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446328044 146 -SDLGATDEQLDF-PIVYASAKQgwavhnlsespGTNLDPLLDTVLK 190
Cdd:PRK00093 306 kKELRRRLPFLDYaPIVFISALT-----------GQGVDKLLEAIDE 341
|
|
| PRK09518 |
PRK09518 |
bifunctional cytidylate kinase/GTPase Der; Reviewed |
6-130 |
4.85e-04 |
|
bifunctional cytidylate kinase/GTPase Der; Reviewed
Pssm-ID: 236546 [Multi-domain] Cd Length: 712 Bit Score: 43.24 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 6 IAIIAHVDHGKTTLLDGILRQTGAVtakedgerimdsndLEKEKGITIKAKNTAVVYKGTRINVVDTPG--------HAD 77
Cdd:PRK09518 278 VAIVGRPNVGKSTLVNRILGRREAV--------------VEDTPGVTRDRVSYDAEWAGTDFKLVDTGGweadvegiDSA 343
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 446328044 78 FGGEVERVLATADSCLLLVDAFDGPMpQTRFVLGKSLQLGHRPI-LVINKIDRP 130
Cdd:PRK09518 344 IASQAQIAVSLADAVVFVVDGQVGLT-STDERIVRMLRRAGKPVvLAVNKIDDQ 396
|
|
| MnmE |
COG0486 |
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
60-203 |
7.42e-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: 42.36 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 60 VVYKGTRINVVDTPGHADFGGEVER--------VLATADSCLLLVDAFDGPMPQTRFVLGKslqLGHRP-ILVINKIDRP 130
Cdd:COG0486 256 INIGGIPVRLIDTAGLRETEDEVEKigierareAIEEADLVLLLLDASEPLTEEDEEILEK---LKDKPvIVVLNKIDLP 332
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446328044 131 GARPEAVVDMAfdlfsdlgatdeqlDFPIVYASAKQgwavhnlsespGTNLDPLLDTVLKHVPPVQADTEAPL 203
Cdd:COG0486 333 SEADGELKSLP--------------GEPVIAISAKT-----------GEGIDELKEAILELVGEGALEGEGVL 380
|
|
| Tet_C |
cd03711 |
Tet_C: C-terminus of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology ... |
404-482 |
1.47e-03 |
|
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: 37.60 E-value: 1.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446328044 404 EPYEYLVMDVPDQFTGAIIAELNRRKGELQLMDAHpSGMTRVEFVIPTRGIIGFRGFFISETRGEGVMSSRFLRFDVYK 482
Cdd:cd03711 1 EPYLRFELEVPQDALGRAMSDLAKMGATFEDPQIK-GDEVTLEGTIPVATSQDYQSELPSYTHGEGVLETEFKGYRPCH 78
|
|
| Tet_II |
cd03690 |
Domain II of ribosomal protection proteins Tet(M) and Tet(O); This subfamily represents domain ... |
200-293 |
2.73e-03 |
|
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: 37.22 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 200 EAPLQFQVTSLDYNDYVGRIAVGKIYAGKMALgMNVIQLAAKKTEtapsadtalFRITKLYNFEGLKRNEVNAAEAGDIV 279
Cdd:cd03690 1 ESELSGTVFKIEYDPKGERLAYLRLYSGTLRL-RDSVRVSGEEEK---------IKITELRTFENGELVKVDRVYAGDIA 70
|
90
....*....|....
gi 446328044 280 AIAGLPDVFIGDTI 293
Cdd:cd03690 71 ILVGLKSLRVGDVL 84
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
2-173 |
4.68e-03 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 39.62 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 2 EIRNIAIIAHVDHGKTTLLDGILRQtgavtakedgERIMDSNdlekEKGITIKAKNTAVVYKGTRINVVDTPG------- 74
Cdd:COG1160 174 DPIKIAIVGRPNVGKSSLINALLGE----------ERVIVSD----IAGTTRDSIDTPFERDGKKYTLIDTAGirrkgkv 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328044 75 HADfggeVER--VLAT------ADSCLLLVDAFDGPMPQ----TRFVL--GKSLqlghrpILVINKIDRPGARPEAVVDM 140
Cdd:COG1160 240 DEG----IEKysVLRTlraierADVVLLVIDATEGITEQdlkiAGLALeaGKAL------VIVVNKWDLVEKDRKTREEL 309
|
170 180 190
....*....|....*....|....*....|....
gi 446328044 141 AFDLFSDLGatdeQLDF-PIVYASAKQGWAVHNL 173
Cdd:COG1160 310 EKEIRRRLP----FLDYaPIVFISALTGQGVDKL 339
|
|
| RF3_II |
cd03689 |
Domain II of bacterial Release Factor 3; This subfamily represents domain II of bacterial ... |
218-295 |
8.67e-03 |
|
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: 35.71 E-value: 8.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446328044 218 RIAVGKIYAGKMALGMNVIQLAAKKTetapsadtalFRITKLYNFEGLKRNEVNAAEAGDIVAIAGLPDVFIGDTICE 295
Cdd:cd03689 19 RIAFLRVCSGKFERGMKVKHVRTGKE----------VRLSNATTFMAQDRETVEEAYPGDIIGLPNHGTFQIGDTFTE 86
|
|
| mtEFG1_II_like |
cd04091 |
Domain II of mitochondrial elongation factor G1-like proteins found in eukaryotes; Eukaryotic ... |
223-294 |
9.85e-03 |
|
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: 35.34 E-value: 9.85e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446328044 223 KIYAGKMALGMNVIQLAAKKTetapsadtalFRITKLYNFEGLKRNEVNAAEAGDIVAIAGLpDVFIGDTIC 294
Cdd:cd04091 20 RVYQGVLRKGDTIYNVRTGKK----------VRVPRLVRMHSDEMEDIEEVYAGDICALFGI-DCASGDTFT 80
|
|
| |
