|
Name |
Accession |
Description |
Interval |
E-value |
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
14-615 |
0e+00 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 996.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 14 PVENIRNFSIVAHVDHGKSTLADRLLELTGTIDKTKNNKQVLDKLQVERERGITVKAQTASLFYNCE-GKQYLLNLIDTP 92
Cdd:COG0481 2 DQKNIRNFSIIAHIDHGKSTLADRLLELTGTLSEREMKEQVLDSMDLERERGITIKAQAVRLNYKAKdGETYQLNLIDTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 93 GHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADPERVENQIEKVFDIPSDECI 172
Cdd:COG0481 82 GHVDFSYEVSRSLAACEGALLVVDASQGVEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKQEIEDIIGIDASDAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 173 KISAKLGTNVESVLQAIIERIPPPKVHRKNPLRALVFDSTFDQYRGVIANVALFDGVVSKGDKIVSAHTQKTYEVNEVGV 252
Cdd:COG0481 162 LVSAKTGIGIEEILEAIVERIPPPKGDPDAPLQALIFDSWYDSYRGVVVYVRVFDGTLKKGDKIKMMSTGKEYEVDEVGV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 253 LNPNEQPTHKLYAGQVGYLIAGMKDVTEAQIGDTLCLHKQPV-EPLPGFKSAKPMVFAGMYPLDQSEYNNLKSAIEKLTL 331
Cdd:COG0481 242 FTPKMTPVDELSAGEVGYIIAGIKDVRDARVGDTITLAKNPAaEPLPGFKEVKPMVFAGLYPVDSDDYEDLRDALEKLQL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 332 NDSSVTVHRDSSLALGAGWRLGFLGLLHMEVFNQRLEQEYNASVILTTPTVPYKAVLSSSKlikehrekEITIINPAQFP 411
Cdd:COG0481 322 NDASLTYEPETSAALGFGFRCGFLGLLHMEIIQERLEREFDLDLITTAPSVVYEVTLTDGE--------VIEVDNPSDLP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 412 DKSKVTEYLEPVVLGTIITPDEYTGKIMMLCEARRAVQKNMIFIDQNRVMLKYLFPLNEIVVDFYDSLKSLSSGYASFDY 491
Cdd:COG0481 394 DPGKIEEIEEPIVKATIITPSEYVGAVMELCQEKRGVQKNMEYLGENRVELTYELPLAEIVFDFFDRLKSITRGYASLDY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 492 EDAGYQTAELVKMDILLNGNTVEELVTVVHKDKAHSIGKAICERLKDSLPRQLFEIAIQAAIGSKIIARETVKAYRKNVL 571
Cdd:COG0481 474 EFIGYRESDLVKLDILINGEPVDALSFIVHRDKAYSRGRALVEKLKELIPRQQFEVPIQAAIGGKIIARETIKALRKDVL 553
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1370487429 572 AKCYGGDITRKMKLLKRQAEGKKKLRKIGNVEVPKDAFIKVLKT 615
Cdd:COG0481 554 AKCYGGDISRKRKLLEKQKEGKKRMKQVGNVEIPQEAFLAVLKV 597
|
|
| lepA |
TIGR01393 |
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a ... |
16-615 |
0e+00 |
|
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a GTP-binding membrane protein related to EF-G and EF-Tu. Two types of phylogenetic tree, rooted by other GTP-binding proteins, suggest that eukaryotic homologs (including GUF1 of yeast) originated within the bacterial LepA family. The function is unknown. [Unknown function, General]
Pssm-ID: 130460 [Multi-domain] Cd Length: 595 Bit Score: 892.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 16 ENIRNFSIVAHVDHGKSTLADRLLELTGTIDKTKNNKQVLDKLQVERERGITVKAQTASLFYNCE-GKQYLLNLIDTPGH 94
Cdd:TIGR01393 1 KNIRNFSIIAHIDHGKSTLADRLLEYTGAISEREMREQVLDSMDLERERGITIKAQAVRLNYKAKdGETYVLNLIDTPGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 95 VDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADPERVENQIEKVFDIPSDECIKI 174
Cdd:TIGR01393 81 VDFSYEVSRSLAACEGALLLVDAAQGIEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKKEIEEVIGLDASEAILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 175 SAKLGTNVESVLQAIIERIPPPKVHRKNPLRALVFDSTFDQYRGVIANVALFDGVVSKGDKIVSAHTQKTYEVNEVGVLN 254
Cdd:TIGR01393 161 SAKTGIGIEEILEAIVKRVPPPKGDPDAPLKALIFDSHYDNYRGVVALVRVFEGTIKPGDKIRFMSTGKEYEVDEVGVFT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 255 PNEQPTHKLYAGQVGYLIAGMKDVTEAQIGDTLCLHKQPV-EPLPGFKSAKPMVFAGMYPLDQSEYNNLKSAIEKLTLND 333
Cdd:TIGR01393 241 PKLTKTDELSAGEVGYIIAGIKDVSDVRVGDTITHVKNPAkEPLPGFKEVKPMVFAGLYPIDTEDYEDLRDALEKLKLND 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 334 SSVTVHRDSSLALGAGWRLGFLGLLHMEVFNQRLEQEYNASVILTTPTVPYKAVLSSSKlikehrekEITIINPAQFPDK 413
Cdd:TIGR01393 321 ASLTYEPESSPALGFGFRCGFLGLLHMEIIQERLEREFNLDLITTAPSVIYRVYLTNGE--------VIEVDNPSDLPDP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 414 SKVTEYLEPVVLGTIITPDEYTGKIMMLCEARRAVQKNMIFIDQNRVMLKYLFPLNEIVVDFYDSLKSLSSGYASFDYED 493
Cdd:TIGR01393 393 GKIEHVEEPYVKATIITPTEYLGPIMTLCQEKRGVQTNMEYLDPNRVELIYEMPLAEIVYDFFDKLKSISRGYASFDYEL 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 494 AGYQTAELVKMDILLNGNTVEELVTVVHKDKAHSIGKAICERLKDSLPRQLFEIAIQAAIGSKIIARETVKAYRKNVLAK 573
Cdd:TIGR01393 473 IGYRPSDLVKLDILINGEPVDALSFIVHRDKAYSRGREICEKLKELIPRQQFEIPIQAAIGGKIIARETIKALRKDVTAK 552
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1370487429 574 CYGGDITRKMKLLKRQAEGKKKLRKIGNVEVPKDAFIKVLKT 615
Cdd:TIGR01393 553 CYGGDITRKRKLLEKQKEGKKRMKQIGKVEVPQEAFLAVLKV 594
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
19-196 |
3.50e-115 |
|
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: 341.05 E-value: 3.50e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 19 RNFSIVAHVDHGKSTLADRLLELTGTIDKTKNNKQVLDKLQVERERGITVKAQTASLFYNCE-GKQYLLNLIDTPGHVDF 97
Cdd:cd01890 1 RNFSIIAHIDHGKSTLADRLLELTGTVSEREMKEQVLDSMDLERERGITIKAQAVRLFYKAKdGEEYLLNLIDTPGHVDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 98 SYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADPERVENQIEKVFDIPSDECIKISAK 177
Cdd:cd01890 81 SYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVKQEIEDVLGLDASEAILVSAK 160
|
170
....*....|....*....
gi 1370487429 178 LGTNVESVLQAIIERIPPP 196
Cdd:cd01890 161 TGLGVEDLLEAIVERIPPP 179
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
16-195 |
8.59e-68 |
|
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: 218.55 E-value: 8.59e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 16 ENIRNFSIVAHVDHGKSTLADRLLELTGTIDKTKNNKQ----VLDKLQVERERGITVKAQTASlfynCEGKQYLLNLIDT 91
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGegeaGLDNLPEERERGITIKSAAVS----FETKDYLINLIDT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 92 PGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKN-ADPERVENQIEKVF------ 164
Cdd:pfam00009 77 PGHVDFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDgAELEEVVEEVSRELlekyge 156
|
170 180 190
....*....|....*....|....*....|.
gi 1370487429 165 DIPSDECIKISAKLGTNVESVLQAIIERIPP 195
Cdd:pfam00009 157 DGEFVPVVPGSALKGEGVQTLLDALDEYLPS 187
|
|
| LepA_C |
pfam06421 |
GTP-binding protein LepA C-terminus; This family consists of the C-terminal region of several ... |
508-614 |
2.73e-66 |
|
GTP-binding protein LepA C-terminus; This family consists of the C-terminal region of several pro- and eukaryotic GTP-binding LepA proteins.
Pssm-ID: 461905 [Multi-domain] Cd Length: 107 Bit Score: 211.88 E-value: 2.73e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 508 LNGNTVEELVTVVHKDKAHSIGKAICERLKDSLPRQLFEIAIQAAIGSKIIARETVKAYRKNVLAKCYGGDITRKMKLLK 587
Cdd:pfam06421 1 INGEPVDALSFIVHRSKAYRRGRALVEKLKELIPRQQFEVPIQAAIGGKIIARETIKALRKDVTAKCYGGDISRKKKLLE 80
|
90 100
....*....|....*....|....*..
gi 1370487429 588 RQAEGKKKLRKIGNVEVPKDAFIKVLK 614
Cdd:pfam06421 81 KQKEGKKRMKQIGNVEIPQEAFLAVLK 107
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
18-467 |
7.90e-60 |
|
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: 209.85 E-value: 7.90e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 18 IRNFSIVAHVDHGKSTLADRLLELTGTI-DKTKNNKQVLDKLQVERERGITVKAQTASLFYNcegkQYLLNLIDTPGHVD 96
Cdd:TIGR01394 1 IRNIAIIAHVDHGKTTLVDALLKQSGTFrANEAVAERVMDSNDLERERGITILAKNTAIRYN----GTKINIVDTPGHAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 97 FSYEVSRSLSACQGVLLVVDANEGIQAQTvaNFFL--AFEAQLSVIPVINKIDLKNADPERVENQIEKVF-DIPSDE--- 170
Cdd:TIGR01394 77 FGGEVERVLGMVDGVLLLVDASEGPMPQT--RFVLkkALELGLKPIVVINKIDRPSARPDEVVDEVFDLFaELGADDeql 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 171 ---CIKISAKLGT----------NVESVLQAIIERIPPPKVHRKNPLRALVFDSTFDQYRGVIANVALFDGVVSKGDKIV 237
Cdd:TIGR01394 155 dfpIVYASGRAGWasldlddpsdNMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVHRGTVKKGQQVA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 238 SAHTQKTYEVNEVGVLNPNE----QPTHKLYAGQVgYLIAGMKDvteAQIGDTLCLHKQPvEPLPGFKSAKP---MVFag 310
Cdd:TIGR01394 235 LMKRDGTIENGRISKLLGFEglerVEIDEAGAGDI-VAVAGLED---INIGETIADPEVP-EALPTITVDEPtlsMTF-- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 311 mypldqseynnlksaieklTLNDSSVtvhrdsslalgAGWRLGFLGLLHMevfNQRLEQEYNASVIL-TTPT-------V 382
Cdd:TIGR01394 308 -------------------SVNDSPL-----------AGKEGKKVTSRHI---RDRLMRELETNVALrVEDTesadkfeV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 383 PYKAVLSSSKLIKEHREK--EITIINPaQFPDKSKVTEYLEPVVLGTIITPDEYTGKIMMLCEARRAVQKNMIFIDQNRV 460
Cdd:TIGR01394 355 SGRGELHLSILIETMRREgfELQVGRP-QVIYKEIDGKKLEPIEELTIDVPEEHVGAVIEKLGKRKGEMVDMEPSGNGRT 433
|
....*..
gi 1370487429 461 MLKYLFP 467
Cdd:TIGR01394 434 RLEFKIP 440
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
16-298 |
1.03e-58 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 207.18 E-value: 1.03e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 16 ENIRNFSIVAHVDHGKSTLADRLLELTGTI-DKTKNNKQVLDKLQVERERGITVKAQTASLFYncegKQYLLNLIDTPGH 94
Cdd:COG1217 4 EDIRNIAIIAHVDHGKTTLVDALLKQSGTFrENQEVAERVMDSNDLERERGITILAKNTAVRY----KGVKINIVDTPGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 95 VDFSYEVSRSLSACQGVLLVVDANEGIQAQTvaNFFL--AFEAQLSVIPVINKIDLKNADPERVENQiekVFDI-----P 167
Cdd:COG1217 80 ADFGGEVERVLSMVDGVLLLVDAFEGPMPQT--RFVLkkALELGLKPIVVINKIDRPDARPDEVVDE---VFDLfielgA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 168 SDE-----CIKISAKLG----------TNVESVLQAIIERIPPPKVHRKNPLRALVFDSTFDQYRGVIANVALFDGVVSK 232
Cdd:COG1217 155 TDEqldfpVVYASARNGwasldlddpgEDLTPLFDTILEHVPAPEVDPDGPLQMLVTNLDYSDYVGRIAIGRIFRGTIKK 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 233 GDKIVSAH---TQKTYEVNEV-GVLNPNEQPTHKLYAGQVgYLIAGMKDVTeaqIGDTLClHKQPVEPLP 298
Cdd:COG1217 235 GQQVALIKrdgKVEKGKITKLfGFEGLERVEVEEAEAGDI-VAIAGIEDIN---IGDTIC-DPENPEALP 299
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
10-497 |
7.98e-51 |
|
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440248 [Multi-domain] Cd Length: 693 Bit Score: 186.79 E-value: 7.98e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 10 MSRFPVENIRNFSIVAHVDHGKSTLADRLLELTGTIDK---TKNNKQVLDKLQVERERGITVkaqTASLFYnCEGKQYLL 86
Cdd:COG0480 1 MAEYPLEKIRNIGIVAHIDAGKTTLTERILFYTGAIHRigeVHDGNTVMDWMPEEQERGITI---TSAATT-CEWKGHKI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 87 NLIDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADPERVENQIEKVF-- 164
Cdd:COG0480 77 NIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQLKERLga 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 165 ----------------------------------------DIPSDE---------------------------------- 170
Cdd:COG0480 157 npvplqlpigaeddfkgvidlvtmkayvyddelgakyeeeEIPAELkeeaeeareelieavaetddelmekylegeelte 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 171 -----CIKI-------------SAKLGTNVESVLQAIIERIPPP---------------KVHRK----NPLRALVFDSTF 213
Cdd:COG0480 237 eeikaGLRKatlagkivpvlcgSAFKNKGVQPLLDAVVDYLPSPldvpaikgvdpdtgeEVERKpdddEPFSALVFKTMT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 214 DQYRGVIANVALFDGVVSKGDKIVSAHTQKTYEVNEVGVLNPNEQ-PTHKLYAGQVGyLIAGMKDVTeaqIGDTLCLHKQ 292
Cdd:COG0480 317 DPFVGKLSFFRVYSGTLKSGSTVYNSTKGKKERIGRLLRMHGNKReEVDEAGAGDIV-AVVKLKDTT---TGDTLCDEDH 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 293 PVEpLPGFKSAKPMVFAGMYPLDQSEYNNLKSAIEKLTLNDSSVTVHRDSSLA--LGAGwrlgfLGLLHMEVFNQRLEQE 370
Cdd:COG0480 393 PIV-LEPIEFPEPVISVAIEPKTKADEDKLSTALAKLAEEDPTFRVETDEETGqtIISG-----MGELHLEIIVDRLKRE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 371 YNASVILTTPTVPY-----KAVLSSSKLIKE-----------------HREKEITIIN-------PAQF-P--DKS---- 414
Cdd:COG0480 467 FGVEVNVGKPQVAYretirKKAEAEGKHKKQsgghgqygdvwieieplPRGEGFEFVDkivggviPKEYiPavEKGirea 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 415 --------------KVTEY---------------------------------LEPVVLGTIITPDEYTGKIMMLCEARRA 447
Cdd:COG0480 547 mekgvlagypvvdvKVTLYdgsyhpvdssemafkiaasmafkeaakkakpvlLEPIMKVEVTVPEEYMGDVMGDLNSRRG 626
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1370487429 448 VQKNMifiDQ--NRVMLKYLFPLNEIvVDFYDSLKSLSSGYASFDYEDAGYQ 497
Cdd:COG0480 627 RILGM---ESrgGAQVIKAEVPLAEM-FGYATDLRSLTQGRGSFTMEFSHYE 674
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
20-196 |
5.60e-49 |
|
GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function.
Pssm-ID: 206647 [Multi-domain] Cd Length: 183 Bit Score: 168.63 E-value: 5.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 20 NFSIVAHVDHGKSTLADRLLELTGTIDKTKNNKQ-VLDKLQVERERGITVKAQTASLFYNcegkQYLLNLIDTPGHVDFS 98
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKEtFLDTLKEERERGITIKTGVVEFEWP----KRRINFIDTPGHEDFS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 99 YEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDL-KNADPERVENQIEKV-------FDIPSD- 169
Cdd:cd00881 77 KETVRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRvGEEDFDEVLREIKELlkligftFLKGKDv 156
|
170 180
....*....|....*....|....*..
gi 1370487429 170 ECIKISAKLGTNVESVLQAIIERIPPP 196
Cdd:cd00881 157 PIIPISALTGEGIEELLDAIVEHLPPP 183
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
17-196 |
6.39e-47 |
|
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: 163.53 E-value: 6.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 17 NIRNFSIVAHVDHGKSTLADRLLELTGTI-DKTKNNKQVLDKLQVERERGITVKAQTASLFYncegKQYLLNLIDTPGHV 95
Cdd:cd01891 1 KIRNIAIIAHVDHGKTTLVDALLKQSGTFrENEEVGERVMDSNDLERERGITILAKNTAITY----KDTKINIIDTPGHA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 96 DFSYEVSRSLSACQGVLLVVDANEGIQAQTvaNFFL--AFEAQLSVIPVINKIDLKNADPERVENQIEKVF---DIPSDE 170
Cdd:cd01891 77 DFGGEVERVLSMVDGVLLLVDASEGPMPQT--RFVLkkALEAGLKPIVVINKIDRPDARPEEVVDEVFDLFlelNATDEQ 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1370487429 171 C----IKISAKLG----------TNVESVLQAIIERIPPP 196
Cdd:cd01891 155 LdfpiVYASAKNGwaslnlddpsEDLDPLFETIIEHVPAP 194
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
19-196 |
2.03e-45 |
|
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: 160.47 E-value: 2.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 19 RNFSIVAHVDHGKSTLADRLLELTGTI-DKTKNNKQVLDKLQVERERGITVKAQTASLFYNCE-----GKQYLLNLIDTP 92
Cdd:cd01885 1 RNICIIAHVDHGKTTLSDSLLASAGIIsEKLAGKARYLDTREDEQERGITIKSSAISLYFEYEeekmdGNDYLINLIDSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 93 GHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDL----KNADPE----RVENQIEKV- 163
Cdd:cd01885 81 GHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDRlileLKLSPEeayqRLLRIVEDVn 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1370487429 164 -----------------FDIPSDECIKISAKLG--------TNVESVLQAIIERIPPP 196
Cdd:cd01885 161 aiietyapeefkqekwkFSPQKGNVAFGSALDGwgftiikfADIYAVLEMVVKHLPSP 218
|
|
| lepA_C |
cd03709 |
lepA_C: This family represents the C-terminal region of LepA, a GTP-binding protein localized ... |
421-500 |
8.53e-45 |
|
lepA_C: This family represents the C-terminal region of LepA, a GTP-binding protein localized in the cytoplasmic membrane. LepA is ubiquitous in Bacteria and Eukaryota (e.g. Saccharomyces cerevisiae GUF1p), but is missing from Archaea. LepA exhibits significant homology to elongation factors (EFs) Tu and G. The function(s) of the proteins in this family are unknown. The N-terminal domain of LepA is homologous to a domain of similar size found in initiation factor 2 (IF2), and in EF-Tu and EF-G (factors required for translation in Escherichia coli). Two types of phylogenetic tree, rooted by other GTP-binding proteins, suggest that eukaryotic homologs (including S. cerevisiae GUF1) originated within the bacterial LepA family. LepA has never been observed in archaea, and eukaryl LepA is organellar. LepA is therefore a true bacterial GTPase, found only in the bacterial lineage.
Pssm-ID: 239680 [Multi-domain] Cd Length: 80 Bit Score: 153.80 E-value: 8.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 421 EPVVLGTIITPDEYTGKIMMLCEARRAVQKNMIFIDQNRVMLKYLFPLNEIVVDFYDSLKSLSSGYASFDYEDAGYQTAE 500
Cdd:cd03709 1 EPFVKATIITPSEYLGAIMELCQERRGVQKDMEYLDANRVMLTYELPLAEIVYDFFDKLKSISKGYASLDYELIGYRESD 80
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
11-499 |
1.53e-44 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 168.98 E-value: 1.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 11 SRFPVENIRNFSIVAHVDHGKSTLADRLLELTGTIDK---TKNNKQVLDKLQVERERGITVKAQTASLFYncegKQYLLN 87
Cdd:PRK13351 1 AEMPLMQIRNIGILAHIDAGKTTLTERILFYTGKIHKmgeVEDGTTVTDWMPQEQERGITIESAATSCDW----DNHRIN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 88 LIDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADPERV----------- 156
Cdd:PRK13351 77 LIDTPGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLFKVledieerfgkr 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 157 ----------ENQIEKVFDI---------------------------------------------------------PSD 169
Cdd:PRK13351 157 plplqlpigsEDGFEGVVDLitepelhfsegdggstveegpipeelleeveearekliealaefddellelylegeeLSA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 170 ECIKI-----------------SAKLGTNVESVLQAIIE------RIPPPKVHRKN------------PLRALVFDSTFD 214
Cdd:PRK13351 237 EQLRAplregtrsghlvpvlfgSALKNIGIEPLLDAVVDylpsplEVPPPRGSKDNgkpvkvdpdpekPLLALVFKVQYD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 215 QYRGVIANVALFDGVVSKGDKIVSAHTQKTYEVNEVGVLNPNEQPThkLYAGQVGYLIAGMKdVTEAQIGDTLCLHKQPV 294
Cdd:PRK13351 317 PYAGKLTYLRVYSGTLRAGSQLYNGTGGKREKVGRLFRLQGNKREE--VDRAKAGDIVAVAG-LKELETGDTLHDSADPV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 295 EpLPGFKSAKPMVFAGMYPLDQSEYNNLKSAIEKLTLNDSSVTVHRDS----SLALGagwrlgfLGLLHMEVFNQRLEQE 370
Cdd:PRK13351 394 L-LELLTFPEPVVSLAVEPERRGDEQKLAEALEKLVWEDPSLRVEEDEetgqTILSG-------MGELHLEVALERLRRE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 371 YNASVILTTPTVPYKAVLSSS---------------------------------------------KLIKEHREK----- 400
Cdd:PRK13351 466 FKLEVNTGKPQVAYRETIRKMaegvyrhkkqfggkgqfgevhlrveplergagfifvskvvggaipEELIPAVEKgirea 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 401 --------------EITIINPAQFPDKSKVT-------------------EYLEPVVLGTIITPDEYTGKIMMLCEARRA 447
Cdd:PRK13351 546 lasgplagypvtdlRVTVLDGKYHPVDSSESafkaaarkafleafrkanpVLLEPIMELEITVPTEHVGDVLGDLSQRRG 625
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1370487429 448 VQKNMIFIDQNRVMLKYLFPLNEiVVDFYDSLKSLSSGYASFDYEDAGYQTA 499
Cdd:PRK13351 626 RIEGTEPRGDGEVLVKAEAPLAE-LFGYATRLRSMTKGRGSFTMEFSHFDPV 676
|
|
| EF4_III |
cd16260 |
Domain III of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly ... |
305-380 |
3.61e-44 |
|
Domain III of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly conserved guanosine triphosphatase found in bacteria and eukaryotic mitochondria and chloroplasts. EF4 functions as a translation factor, which promotes back-translocation of tRNAs on posttranslocational ribosome complexes and competes with elongation factor G for interaction with pretranslocational ribosomes, inhibiting the elongation phase of protein synthesis.
Pssm-ID: 293917 [Multi-domain] Cd Length: 76 Bit Score: 151.88 E-value: 3.61e-44
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370487429 305 PMVFAGMYPLDQSEYNNLKSAIEKLTLNDSSVTVHRDSSLALGAGWRLGFLGLLHMEVFNQRLEQEYNASVILTTP 380
Cdd:cd16260 1 PMVFAGLYPVDGSDYEELRDALEKLTLNDASVTFEPETSSALGFGFRCGFLGLLHMEVFQERLEREYGLDLIITAP 76
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
15-385 |
1.56e-43 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 166.19 E-value: 1.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 15 VENIRNFSIVAHVDHGKSTLADRLLELTGTIDKTKNNKQ-VLDKLQVERERGITVKAQTASLFYNCEGKQYLLNLIDTPG 93
Cdd:PRK07560 17 PEQIRNIGIIAHIDHGKTTLSDNLLAGAGMISEELAGEQlALDFDEEEQARGITIKAANVSMVHEYEGKEYLINLIDTPG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 94 HVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQlsVIPV--INKID-----LKnADPERVENQIEKVFD- 165
Cdd:PRK07560 97 HVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRER--VKPVlfINKVDrlikeLK-LTPQEMQQRLLKIIKd 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 166 ----IPS------DECIKISAKLGT------------NV--------------------------------ESVLQAIIE 191
Cdd:PRK07560 174 vnklIKGmapeefKEKWKVDVEDGTvafgsalynwaiSVpmmqktgikfkdiidyyekgkqkelaekaplhEVVLDMVVK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 192 RIPPPKVHRKN-------------------------PLRALVFDSTFDQYRGVIANVALFDGVVSKGDKIVSAHTQKTYE 246
Cdd:PRK07560 254 HLPNPIEAQKYripkiwkgdlnsevgkamlncdpngPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLVGAKKKNR 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 247 VNEVGV-LNPNEQPTHKLYAGQVGYLIaGMKDvteAQIGDTLClhkqPVEPLPGFKSAK----PMVFAGMYPLDQSEYNN 321
Cdd:PRK07560 334 VQQVGIyMGPEREEVEEIPAGNIAAVT-GLKD---ARAGETVV----SVEDMTPFESLKhisePVVTVAIEAKNPKDLPK 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370487429 322 LKSAIEKLTLNDSS--VTVHRDSSLALGAGwrlgfLGLLHMEVFNQRLEQEYNASVILTTPTVPYK 385
Cdd:PRK07560 406 LIEVLRQLAKEDPTlvVKINEETGEHLLSG-----MGELHLEVITYRIKRDYGIEVVTSEPIVVYR 466
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
24-497 |
2.60e-43 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 164.91 E-value: 2.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 24 VAHVDHGKSTLADRLLELTGTIDK---TKNNKQVLDKLQVERERGITVKAQTASLFYNceGKQylLNLIDTPGHVDFSYE 100
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRigeVEDGTTTMDFMPEERERGISITSAATTCEWK--GHK--INLIDTPGHVDFTGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 101 VSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADPERVENQIEKVF---------------- 164
Cdd:PRK12740 77 VERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRAGADFFRVLAQLQEKLgapvvplqlpigegdd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 165 ------------------------DIPSD---------------------------------------ECIKI------- 174
Cdd:PRK12740 157 ftgvvdllsmkayrydeggpseeiEIPAElldraeeareellealaefddelmekylegeelseeeikAGLRKatlagei 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 175 ------SAKLGTNVESVLQAIIERIPPP----KVHRKN-------------PLRALVFDSTFDQYRGVIANVALFDGVVS 231
Cdd:PRK12740 237 vpvfcgSALKNKGVQRLLDAVVDYLPSPlevpPVDGEDgeegaelapdpdgPLVALVFKTMDDPFVGKLSLVRVYSGTLK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 232 KGDKIVSAHTQKTYEVNEVGVLNPNEQ-PTHKLYAGQVGyLIAGMKDvteAQIGDTLCLHKQPVePLPGFKSAKPMVFAG 310
Cdd:PRK12740 317 KGDTLYNSGTGKKERVGRLYRMHGKQReEVDEAVAGDIV-AVAKLKD---AATGDTLCDKGDPI-LLEPMEFPEPVISLA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 311 MYPLDQSEYNNLKSAIEKLTLNDSSVTVHRDSSLA---LGAgwrlgfLGLLHMEVFNQRLEQEYNASVILTTPTVPY--- 384
Cdd:PRK12740 392 IEPKDKGDEEKLSEALGKLAEEDPTLRVERDEETGqtiLSG------MGELHLDVALERLKREYGVEVETGPPQVPYret 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 385 --KAVLSSSKLIKE-----------------HREKEITIIN-------PAQF-P--DKS------------------KVT 417
Cdd:PRK12740 466 irKKAEGHGRHKKQsgghgqfgdvwleveplPRGEGFEFVDkvvggavPRQYiPavEKGvrealekgvlagypvvdvKVT 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 418 EY---------------------------------LEPVVLGTIITPDEYTGKIMMLCEARRAVQKNMiFIDQNRVMLKY 464
Cdd:PRK12740 546 LTdgsyhsvdssemafkiaarlafrealpkakpvlLEPIMKVEVSVPEEFVGDVIGDLSSRRGRILGM-ESRGGGDVVRA 624
|
650 660 670
....*....|....*....|....*....|...
gi 1370487429 465 LFPLNEIvVDFYDSLKSLSSGYASFDYEDAGYQ 497
Cdd:PRK12740 625 EVPLAEM-FGYATDLRSLTQGRGSFSMEFSHYE 656
|
|
| EF4_II |
cd03699 |
Domain II of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly ... |
204-289 |
5.75e-43 |
|
Domain II of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly conserved guanosine triphosphatase found in bacteria and eukaryotic mitochondria and chloroplasts. EF4 functions as a translation factor, which promotes back-translocation of tRNAs on posttranslocational ribosome complexes and competes with elongation factor G for interaction with pretranslocational ribosomes, inhibiting the elongation phase of protein synthesis.
Pssm-ID: 293900 [Multi-domain] Cd Length: 86 Bit Score: 148.72 E-value: 5.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 204 LRALVFDSTFDQYRGVIANVALFDGVVSKGDKIVSAHTQKTYEVNEVGVLNPNEQPTHKLYAGQVGYLIAGMKDVTEAQI 283
Cdd:cd03699 1 LRALIFDSWYDPYRGVVVLVRVFDGTLKKGDKIRFMATGKEYEVLEVGVFTPKMVPTDELSAGEVGYIIAGIKSVKDARV 80
|
....*.
gi 1370487429 284 GDTLCL 289
Cdd:cd03699 81 GDTITL 86
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
15-493 |
3.66e-41 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 158.33 E-value: 3.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 15 VENIRNFSIVAHVDHGKSTLADRLLELTGTID-KTKNNKQVLDKLQVERERGITVKAQTASLFYNcegkQYLLNLIDTPG 93
Cdd:PRK10218 2 IEKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDsRAETQERVMDSNDLEKERGITILAKNTAIKWN----DYRINIVDTPG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 94 HVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADPERVENQIEKVF--------- 164
Cdd:PRK10218 78 HADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLFvnldatdeq 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 165 -DIPSDECIKISAKLGTNVES-------VLQAIIERIPPPKVHRKNPLRALVFDSTFDQYRGVIANVALFDGVVSKGDKI 236
Cdd:PRK10218 158 lDFPIVYASALNGIAGLDHEDmaedmtpLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 237 VSAHTQKTYEVNEVGVLNPN---EQPTHKLyaGQVGYLIAgMKDVTEAQIGDTLClHKQPVEPLPGFKSAKPMV------ 307
Cdd:PRK10218 238 TIIDSEGKTRNAKVGKVLGHlglERIETDL--AEAGDIVA-ITGLGELNISDTVC-DTQNVEALPALSVDEPTVsmffcv 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 308 ----FAGmyplDQSEYNNLKSAIEKLTLNDSSVTVHRDSSLALGAGWRLGFLGLLHMEVFNQRLEQEyNASVILTTPTVP 383
Cdd:PRK10218 314 ntspFCG----KEGKFVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRRE-GFELAVSRPKVI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 384 YKAVlsssklikEHREKeitiinpaqfpdkskvteylEPVVLGTIITPDEYTGKIMMLCEARRAVQKNMIFIDQNRVMLK 463
Cdd:PRK10218 389 FREI--------DGRKQ--------------------EPYENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLD 440
|
490 500 510
....*....|....*....|....*....|....
gi 1370487429 464 YLFPlNEIVVDFYDSLKSLSSG----YASFDYED 493
Cdd:PRK10218 441 YVIP-SRGLIGFRSEFMTMTSGtgllYSTFSHYD 473
|
|
| EF-G |
TIGR00484 |
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ... |
10-391 |
1.27e-40 |
|
translation elongation factor EF-G; After peptide bond formation, this elongation factor of bacteria and organelles catalyzes the translocation of the tRNA-mRNA complex, with its attached nascent polypeptide chain, from the A-site to the P-site of the ribosome. Every completed bacterial genome has at least one copy, but some species have additional EF-G-like proteins. The closest homolog to canonical (e.g. E. coli) EF-G in the spirochetes clusters as if it is derived from mitochondrial forms, while a more distant second copy is also present. Synechocystis PCC6803 has a few proteins more closely related to EF-G than to any other characterized protein. Two of these resemble E. coli EF-G more closely than does the best match from the spirochetes; it may be that both function as authentic EF-G. [Protein synthesis, Translation factors]
Pssm-ID: 129575 [Multi-domain] Cd Length: 689 Bit Score: 157.66 E-value: 1.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 10 MSR-FPVENIRNFSIVAHVDHGKSTLADRLLELTGTIDK---TKNNKQVLDKLQVERERGITVKAQTASLFYncegKQYL 85
Cdd:TIGR00484 1 MARtTDLNRFRNIGISAHIDAGKTTTTERILFYTGRIHKigeVHDGAATMDWMEQEKERGITITSAATTVFW----KGHR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 86 LNLIDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADPERVENQI----- 160
Cdd:TIGR00484 77 INIIDTPGHVDFTVEVERSLRVLDGAVAVLDAVGGVQPQSETVWRQANRYEVPRIAFVNKMDKTGANFLRVVNQIkqrlg 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 161 ------------------------EKVF-------------DIPSD---------------------------------- 169
Cdd:TIGR00484 157 anavpiqlpigaednfigvidlveMKAYffngdkgtkaiekEIPSDlleqakelrenlveavaefdeelmekylegeelt 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 170 -ECIKISAKLGT-----------------NVESVLQAIIERIPPP-------------------KVHRKNPLRALVFDST 212
Cdd:TIGR00484 237 iEEIKNAIRKGVlnceffpvlcgsafknkGVQLLLDAVVDYLPSPtdvpaikgidpdtekeierKASDDEPFSALAFKVA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 213 FDQYRGVIANVALFDGVVSKGDKIVSAHTQKTYEVNEVGVLNPNEQPTHK-LYAGQVGYLIaGMKDVTEaqiGDTLCLHK 291
Cdd:TIGR00484 317 TDPFVGQLTFVRVYSGVLKSGSYVKNSRKNKKERVGRLVKMHANNREEIKeVRAGDICAAI-GLKDTTT---GDTLCDPK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 292 QPVEpLPGFKSAKPMVFAGMYPLDQSEYNNLKSAIEKLTLNDSSVTVHRD--SSLALGAGwrlgfLGLLHMEVFNQRLEQ 369
Cdd:TIGR00484 393 IDVI-LERMEFPEPVISLAVEPKTKADQEKMGIALGKLAEEDPTFRTFTDpeTGQTIIAG-----MGELHLDIIVDRMKR 466
|
490 500
....*....|....*....|..
gi 1370487429 370 EYNASVILTTPTVPYKAVLSSS 391
Cdd:TIGR00484 467 EFKVEANVGAPQVAYRETIRSK 488
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
16-385 |
2.41e-38 |
|
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: 151.20 E-value: 2.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 16 ENIRNFSIVAHVDHGKSTLADRLLELTGTIDKTKNNKQV-LDKLQVERERGITVKAQTASLFYNCEGKQYLLNLIDTPGH 94
Cdd:TIGR00490 17 KFIRNIGIVAHIDHGKTTLSDNLLAGAGMISEELAGQQLyLDFDEQEQERGITINAANVSMVHEYEGNEYLINLIDTPGH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 95 VDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKID--------------------------- 147
Cdd:TIGR00490 97 VDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKPVLFINKVDrlinelkltpqelqerfikiitevnkl 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 148 LKNADPE--------RVEN------------------------QIEKVFDIPSDECIKISAKLGTNVESVLQAIIERIPP 195
Cdd:TIGR00490 177 IKAMAPEefrdkwkvRVEDgsvafgsayynwaisvpsmkktgiGFKDIYKYCKEDKQKELAKKSPLHQVVLDMVIRHLPS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 196 P-------------------------KVHRKNPLRALVFDSTFDQYRGVIANVALFDGVVSKGDKIVSAHTQKTYEVNEV 250
Cdd:TIGR00490 257 PieaqkyripviwkgdlnsevgkamlNCDPKGPLALMITKIVVDKHAGEVAVGRLYSGTIRPGMEVYIVDRKAKARIQQV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 251 GV-LNPNEQPTHKLYAGQVGYLIaGMKDvteAQIGDTLCLHKQPVEPLPGFKS-AKPMVFAGMYPLDQSEYNNLKSAIEK 328
Cdd:TIGR00490 337 GVyMGPERVEVDEIPAGNIVAVI-GLKD---AVAGETICTTVENITPFESIKHiSEPVVTVAIEAKNTKDLPKLIEVLRQ 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370487429 329 LTLNDSS--VTVHRDSSLALGAGwrlgfLGLLHMEVFNQRLEQEYNASVILTTPTVPYK 385
Cdd:TIGR00490 413 VAKEDPTvhVEINEETGEHLISG-----MGELHLEIIVEKIREDYGLDVETSPPIVVYR 466
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
20-183 |
9.22e-35 |
|
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: 131.59 E-value: 9.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 20 NFSIVAHVDHGKSTLADRLLELTGTIDKT----KNNKQvLDKLQVERERGITVKAQTASLFYN-CEgkqylLNLIDTPGH 94
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIRELgsvdKGTTR-TDSMELERQRGITIFSAVASFQWEdTK-----VNIIDTPGH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 95 VDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADPERVENQIEKVFDipSDECIKI 174
Cdd:cd04168 75 MDFIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTIIFVNKIDRAGADLEKVYQEIKEKLS--PDIVPMQ 152
|
....*....
gi 1370487429 175 SAKLGTNVE 183
Cdd:cd04168 153 KVGLYPNIC 161
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
16-147 |
2.10e-32 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 133.25 E-value: 2.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 16 ENIRNFSIVAHVDHGKSTLADRLLELTGTI-DKTKNNKQVLDKLQVERERGITVKAQTASLFY------NCEGKQYLLNL 88
Cdd:PTZ00416 17 DQIRNMSVIAHVDHGKSTLTDSLVCKAGIIsSKNAGDARFTDTRADEQERGITIKSTGISLYYehdledGDDKQPFLINL 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370487429 89 IDTPGHVDFSYEVSRSLSACQGVLLVVDANEG--IQAQTVanffLAFEAQLSVIPV--INKID 147
Cdd:PTZ00416 97 IDSPGHVDFSSEVTAALRVTDGALVVVDCVEGvcVQTETV----LRQALQERIRPVlfINKVD 155
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
20-166 |
2.98e-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: 122.60 E-value: 2.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 20 NFSIVAHVDHGKSTLADRLLELTGTIDK---TKNNKQVLDKLQVERERGITVkaQTASLfyNCEGKQYLLNLIDTPGHVD 96
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGRIHKigeVHGGGATMDWMEQERERGITI--QSAAT--TCFWKDHRINIIDTPGHVD 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 97 FSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADPERVENQIEKVFDI 166
Cdd:cd01886 77 FTIEVERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQIREKLGA 146
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
10-147 |
4.33e-31 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 129.46 E-value: 4.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 10 MSRFPVE----------NIRNFSIVAHVDHGKSTLADRLLELTGTID-KTKNNKQVLDKLQVERERGITVKAQTASLFY- 77
Cdd:PLN00116 1 MVKFTAEelrrimdkkhNIRNMSVIAHVDHGKSTLTDSLVAAAGIIAqEVAGDVRMTDTRADEAERGITIKSTGISLYYe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 78 -----------NCEGKQYLLNLIDTPGHVDFSYEVSRSLSACQGVLLVVDANEG--IQAQTVANFFLAFEaqlsVIPV-- 142
Cdd:PLN00116 81 mtdeslkdfkgERDGNEYLINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGvcVQTETVLRQALGER----IRPVlt 156
|
....*
gi 1370487429 143 INKID 147
Cdd:PLN00116 157 VNKMD 161
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
19-147 |
4.99e-31 |
|
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: 120.45 E-value: 4.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 19 RNFSIVAHVDHGKSTLADRLLELTGTIDKTKNNKQV----LDKLQVERERGITVKAQTASLFY-NCEGKQYLLNLIDTPG 93
Cdd:cd04167 1 RNVCIAGHLHHGKTSLLDMLIEQTHKRTPSVKLGWKplryTDTRKDEQERGISIKSNPISLVLeDSKGKSYLINIIDTPG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1370487429 94 HVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKID 147
Cdd:cd04167 81 HVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKID 134
|
|
| Elongation_Factor_C |
cd01514 |
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ... |
421-499 |
1.44e-25 |
|
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: 100.25 E-value: 1.44e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370487429 421 EPVVLGTIITPDEYTGKIMMLCEARRAVQKNMIFIDQNRVMLKYLFPLNEIvVDFYDSLKSLSSGYASFDYEDAGYQTA 499
Cdd:cd01514 1 EPIMKVEITVPEEYLGAVIGDLSKRRGEILGMEPRGTGRVVIKAELPLAEM-FGFATDLRSLTQGRASFSMEFSHYEPV 78
|
|
| EFG_C |
pfam00679 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
418-506 |
1.52e-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: 100.31 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 418 EYLEPVVLGTIITPDEYTGKIMMLCEARRAVQKNMIFIDQNRVMLKYLFPLNEIvVDFYDSLKSLSSGYASFDYEDAGYQ 497
Cdd:pfam00679 1 VLLEPIEKVTIDVPEEYVGDVISDLNSRRGEILDMDPDDGGRVVIEAEVPLAEL-FGFATELRSLTKGRGSFSMEFSGYQ 79
|
....*....
gi 1370487429 498 TAELVKMDI 506
Cdd:pfam00679 80 PVPGDILDR 88
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
19-166 |
1.32e-23 |
|
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: 100.75 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 19 RNFSIVAHVDHGKSTLADRLL------ELTGTIDKTKNNKQVL-DKLQVERERGITVkaqTASL--FyncEGKQYLLNLI 89
Cdd:cd04169 3 RTFAIISHPDAGKTTLTEKLLlfggaiQEAGAVKARKSRKHATsDWMEIEKQRGISV---TSSVmqF---EYKGCVINLL 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370487429 90 DTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADPERVENQIEKVFDI 166
Cdd:cd04169 77 DTPGHEDFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDREGRDPLELLDEIENELGI 153
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
22-241 |
2.50e-23 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 104.91 E-value: 2.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 22 SIVAHVDHGKSTLADRlleltgtIDKTKN-NKQVldklqvereRGIT--VKAQTASLFYNCEGKQylLNLIDTPGHVDFS 98
Cdd:CHL00189 248 TILGHVDHGKTTLLDK-------IRKTQIaQKEA---------GGITqkIGAYEVEFEYKDENQK--IVFLDTPGHEAFS 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 99 YEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADPERVENQIEKVFDIPSD-----ECIK 173
Cdd:CHL00189 310 SMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANTERIKQQLAKYNLIPEKwggdtPMIP 389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 174 ISAKLGTNVESVLQAIIER--IPPPKVHRKNPLRALVFDSTFDQYRGVIANVALFDGVVSKGDKIVSAHT 241
Cdd:CHL00189 390 ISASQGTNIDKLLETILLLaeIEDLKADPTQLAQGIILEAHLDKTKGPVATILVQNGTLHIGDIIVIGTS 459
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
20-237 |
5.15e-23 |
|
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: 101.93 E-value: 5.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 20 NFSIVAHVDHGKSTLADRLLELTG-----TIDKTKNNKQ-----------VLDKLQVERERGITVKAQtaslFYNCEGKQ 83
Cdd:COG5256 9 NLVVIGHVDHGKSTLVGRLLYETGaidehIIEKYEEEAEkkgkesfkfawVMDRLKEERERGVTIDLA----HKKFETDK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 84 YLLNLIDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFE---AQLSVipVINKIDLKNADPER---VE 157
Cdd:COG5256 85 YYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTlgiNQLIV--AVNKMDAVNYSEKRyeeVK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 158 NQIEKV-----FDIPSDECIKISAKLGTNV------------ESVLQAIIERIPPPKVHRKnPLRALVFDStfdqYrgVI 220
Cdd:COG5256 163 EEVSKLlkmvgYKVDKIPFIPVSAWKGDNVvkksdnmpwyngPTLLEALDNLKEPEKPVDK-PLRIPIQDV----Y--SI 235
|
250 260
....*....|....*....|...
gi 1370487429 221 ANVALF------DGVVSKGDKIV 237
Cdd:COG5256 236 SGIGTVpvgrveTGVLKVGDKVV 258
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
20-182 |
5.69e-23 |
|
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: 97.26 E-value: 5.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 20 NFSIVAHVDHGKSTLADRLLELTGTI--DK-------TKNNKQ--------VLDKLQVERERGITVkaQTASLFYNCEGK 82
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSIfeDQlaalersKSSGTQgekldlalLVDGLQAEREQGITI--DVAYRYFSTPKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 83 QYLlnLIDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAfeAQLS---VIPVINKIDLKNADPERVEnQ 159
Cdd:cd04166 79 KFI--IADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIA--SLLGirhVVVAVNKMDLVDYDEEVFE-E 153
|
170 180 190
....*....|....*....|....*....|
gi 1370487429 160 IEKVF-------DIPSDECIKISAKLGTNV 182
Cdd:cd04166 154 IKADYlafaaslGIEDITFIPISALEGDNV 183
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
23-191 |
6.29e-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: 96.00 E-value: 6.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 23 IVAHVDHGKSTLadrlleltgtidktknnkqvLDKLQ----VERE-RGIT--VKAQTASLfyncEGKQYLLNLIDTPGHV 95
Cdd:cd01887 5 VMGHVDHGKTTL--------------------LDKIRktnvAAGEaGGITqhIGAYQVPI----DVKIPGITFIDTPGHE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 96 DFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDL---KNADPERVENQIEKvFDIPSDE-- 170
Cdd:cd01887 61 AFTNMRARGASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKpygTEADPERVKNELSE-LGLVGEEwg 139
|
170 180
....*....|....*....|....*
gi 1370487429 171 ----CIKISAKLGTNVESVLQAIIE 191
Cdd:cd01887 140 gdvsIVPISAKTGEGIDDLLEAILL 164
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
22-237 |
7.37e-23 |
|
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: 102.92 E-value: 7.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 22 SIVAHVDHGKSTLADrlleltgTIDKTKNNkqvldklQVErERGITVKAQTASLFYNcEGKQylLNLIDTPGHVDFSYEV 101
Cdd:TIGR00487 91 TIMGHVDHGKTSLLD-------SIRKTKVA-------QGE-AGGITQHIGAYHVENE-DGKM--ITFLDTPGHEAFTSMR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 102 SRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADPERVENQIEKVFDIPSD-----ECIKISA 176
Cdd:TIGR00487 153 ARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVPIIVAINKIDKPEANPDRVKQELSEYGLVPEDwggdtIFVPVSA 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370487429 177 KLGTNVESVLQAII--ERIPPPKVHRKNPLRALVFDSTFDQYRGVIANVALFDGVVSKGDKIV 237
Cdd:TIGR00487 233 LTGDGIDELLDMILlqSEVEELKANPNGQASGVVIEAQLDKGRGPVATVLVQSGTLRVGDIVV 295
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
20-167 |
1.49e-22 |
|
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: 97.66 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 20 NFSIVAHVDHGKSTLADRLLELTGTIDK---TKNNKQVLDKLQVERERGITVKAQTASLFYNceGKQylLNLIDTPGHVD 96
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRlgrVEDGNTVSDYDPEEKKRKMSIETSVAPLEWN--GHK--INLIDTPGYAD 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370487429 97 FSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADPERVENQIEKVFDIP 167
Cdd:cd04170 77 FVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRARADFDKTLAALREAFGRP 147
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
20-237 |
5.89e-22 |
|
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: 99.01 E-value: 5.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 20 NFSIVAHVDHGKSTLADRLLELTGTI----------DKTKNNKQ------VLDKLQVERERGITVkaQTASLFYNCEGKQ 83
Cdd:COG2895 19 RFITCGSVDDGKSTLIGRLLYDTKSIfedqlaalerDSKKRGTQeidlalLTDGLQAEREQGITI--DVAYRYFSTPKRK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 84 YLlnLIDTPGHVDFsyevSRSL----SACQGVLLVVDANEGIQAQTVANFFLAfeAQL---SVIPVINKIDLKNADPERV 156
Cdd:COG2895 97 FI--IADTPGHEQY----TRNMvtgaSTADLAILLIDARKGVLEQTRRHSYIA--SLLgirHVVVAVNKMDLVDYSEEVF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 157 EnQIEKVF-------DIPSDECIKISAKLGTNV------------ESVLQAiIERIPPPKVHRKNPLRALV-----FDST 212
Cdd:COG2895 169 E-EIVADYrafaaklGLEDITFIPISALKGDNVversenmpwydgPTLLEH-LETVEVAEDRNDAPFRFPVqyvnrPNLD 246
|
250 260
....*....|....*....|....*
gi 1370487429 213 FDQYRGVIAnvalfDGVVSKGDKIV 237
Cdd:COG2895 247 FRGYAGTIA-----SGTVRVGDEVV 266
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
20-205 |
6.80e-21 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 95.38 E-value: 6.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 20 NFSIVAHVDHGKSTLADRLLELTGTIDK----------TKNNKQ------VLDKLQVERERGITVKAQtaslFYNCEGKQ 83
Cdd:PRK12317 8 NLAVIGHVDHGKSTLVGRLLYETGAIDEhiieelreeaKEKGKEsfkfawVMDRLKEERERGVTIDLA----HKKFETDK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 84 YLLNLIDTPGHVDFSYEVSRSLSACQGVLLVVDANE--GIQAQTVANFFLAFE---AQLSVipVINKIDLKNADPER--- 155
Cdd:PRK12317 84 YYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTlgiNQLIV--AINKMDAVNYDEKRyee 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370487429 156 VENQIEKV-----FDIPSDECIKISAKLGTNV------------ESVLQAIIERIPPPKVHRKnPLR 205
Cdd:PRK12317 162 VKEEVSKLlkmvgYKPDDIPFIPVSAFEGDNVvkksenmpwyngPTLLEALDNLKPPEKPTDK-PLR 227
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
26-191 |
2.17e-18 |
|
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: 83.04 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 26 HVDHGKSTLadrLLELTGtIDKtknnkqvlDKLQVERERGITVKAQTASLFYNCEGKqylLNLIDTPGHVDFSYEVSRSL 105
Cdd:cd04171 7 HIDHGKTTL---IKALTG-IET--------DRLPEEKKRGITIDLGFAYLDLPDGKR---LGFIDVPGHEKFVKNMLAGA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 106 SACQGVLLVVDANEGIQAQTVANF----FLAFEaqlSVIPVINKIDLknADPERVENQIEKV------FDIPSDECIKIS 175
Cdd:cd04171 72 GGIDAVLLVVAADEGIMPQTREHLeileLLGIK---KGLVVLTKADL--VDEDRLELVEEEIlellagTFLADAPIFPVS 146
|
170
....*....|....*.
gi 1370487429 176 AKLGTNVESVLQAIIE 191
Cdd:cd04171 147 SVTGEGIEELKNYLDE 162
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
23-191 |
4.47e-18 |
|
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: 81.73 E-value: 4.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 23 IVAHVDHGKSTLADRLLELTGTIdktknnkqvldklqVERERGITVKAQTASLFYncEGKQYLLNLIDTPGHVDFSYEVS 102
Cdd:cd00882 2 VVGRGGVGKSSLLNALLGGEVGE--------------VSDVPGTTRDPDVYVKEL--DKGKVKLVLVDTPGLDEFGGLGR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 103 RSLSA-----CQGVLLVVDANEGIQAQTVANFFLA--FEAQLSVIPVINKIDLKNADPERVENQIEKVFDIPSDECIKIS 175
Cdd:cd00882 66 EELARlllrgADLILLVVDSTDRESEEDAKLLILRrlRKEGIPIILVGNKIDLLEEREVEELLRLEELAKILGVPVFEVS 145
|
170
....*....|....*.
gi 1370487429 176 AKLGTNVESVLQAIIE 191
Cdd:cd00882 146 AKTGEGVDELFEKLIE 161
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
20-267 |
9.68e-18 |
|
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]
Pssm-ID: 129567 [Multi-domain] Cd Length: 581 Bit Score: 86.85 E-value: 9.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 20 NFSIVAHVDHGKSTLADrllELTGTidktknnkqVLDKLQVERERGITVKAQTASLFYNcegkQYLLNLIDTPGHVDFSY 99
Cdd:TIGR00475 2 IIATAGHVDHGKTTLLK---ALTGI---------AADRLPEEKKRGMTIDLGFAYFPLP----DYRLGFIDVPGHEKFIS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 100 EVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQL-SVIPVINKIDLKN-ADPERVENQIEKVFD----IPSDECIK 173
Cdd:TIGR00475 66 NAIAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIpHTIVVITKADRVNeEEIKRTEMFMKQILNsyifLKNAKIFK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 174 ISAKLGTNVESV---LQAIIERIPPPKVHRknPLRaLVFDSTFD-QYRGVIANVALFDGVVSKGDKIVSAHTQKTYEVNE 249
Cdd:TIGR00475 146 TSAKTGQGIGELkkeLKNLLESLDIKRIQK--PLR-MAIDRAFKvKGAGTVVTGTAFSGEVKVGDNLRLLPINHEVRVKA 222
|
250
....*....|....*...
gi 1370487429 250 VGVLNpneQPTHKLYAGQ 267
Cdd:TIGR00475 223 IQAQN---QDVEIAYAGQ 237
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
20-236 |
1.92e-17 |
|
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: 84.72 E-value: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 20 NFSIVAHVDHGKSTLAdrlLELTGTIdktknnkqvLDKLQVERERGITVKAQTA-SLFYNCEGKQYL------------- 85
Cdd:TIGR03680 6 NIGMVGHVDHGKTTLT---KALTGVW---------TDTHSEELKRGISIRLGYAdAEIYKCPECDGPecyttepvcpncg 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 86 --------LNLIDTPGHVDFSYEVSRSLSACQGVLLVVDANEGI-QAQTVANfFLAFEA--QLSVIPVINKIDLknADPE 154
Cdd:TIGR03680 74 setellrrVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPCpQPQTKEH-LMALEIigIKNIVIVQNKIDL--VSKE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 155 R-VEN--QIEKVFD--IPSD-ECIKISAKLGTNVESVLQAIIERIPPPKVHRKNPLRALV---FD-----STFDQYRGVI 220
Cdd:TIGR03680 151 KaLENyeEIKEFVKgtVAENaPIIPVSALHNANIDALLEAIEKFIPTPERDLDKPPLMYVarsFDvnkpgTPPEKLKGGV 230
|
250
....*....|....*.
gi 1370487429 221 ANVALFDGVVSKGDKI 236
Cdd:TIGR03680 231 IGGSLIQGKLKVGDEI 246
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
20-182 |
2.55e-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: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 20 NFSIVAHVDHGKSTLADRLLELTGTIDKT----------KNNKQ------VLDKLQVERERGITVKAQTASLfyncEGKQ 83
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRtiekyekeakEMGKEsfkyawVLDKLKEERERGVTIDVGLAKF----ETEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 84 YLLNLIDTPGHVDFsyeVSRSLS-ACQG--VLLVVDANEG-------IQAQTVANFFLAFEAQLS-VIPVINKIDLK--N 150
Cdd:cd01883 77 YRFTIIDAPGHRDF---VKNMITgASQAdvAVLVVSARKGefeagfeKGGQTREHALLARTLGVKqLIVAVNKMDDVtvN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1370487429 151 ADPERVENQIEKV--------FDIPSDECIKISAKLGTNV 182
Cdd:cd01883 154 WSQERYDEIKKKVspflkkvgYNPKDVPFIPISGFTGDNL 193
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
20-200 |
1.71e-16 |
|
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: 78.18 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 20 NFSIVAHVDHGKSTLADRLLELTGTidktknnkQVLDKLQVERERGITV----------KAQTASLFYNCEGKQYLLNLI 89
Cdd:cd01889 2 NVGLLGHVDSGKTSLAKALSEIAST--------AAFDKNPQSQERGITLdlgfssfevdKPKHLEDNENPQIENYQITLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 90 DTPGHVDFSYEVsrsLSACQ---GVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLknADPERVENQIEKVFDI 166
Cdd:cd01889 74 DCPGHASLIRTI---IGGAQiidLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDL--IPEEERKRKIEKMKKR 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1370487429 167 ----------PSDECIKISAKLGTNVESVLQAIIERIPPPKVHR 200
Cdd:cd01889 149 lqktlektrlKDSPIIPVSAKPGEGEAELGGELKNLIVLPLINL 192
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
23-192 |
4.88e-16 |
|
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]
Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 75.87 E-value: 4.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 23 IVAHVDHGKSTLADRLLELTGTIdktknnkqvldklqVERERGITVKAQTASLFYNceGKQYLLNLIDTPGHVDFSY--- 99
Cdd:TIGR00231 6 IVGHPNVGKSTLLNSLLGNKGSI--------------TEYYPGTTRNYVTTVIEED--GKTYKFNLLDTAGQEDYDAirr 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 100 ----EVSRSLSACQGVLLVVDANEGIQAQTVANFFLAfEAQLSVIPVINKIDLKNAD-PERVENQIEKVFDIPSdecIKI 174
Cdd:TIGR00231 70 lyypQVERSLRVFDIVILVLDVEEILEKQTKEIIHHA-DSGVPIILVGNKIDLKDADlKTHVASEFAKLNGEPI---IPL 145
|
170
....*....|....*...
gi 1370487429 175 SAKLGTNVESvLQAIIER 192
Cdd:TIGR00231 146 SAETGKNIDS-AFKIVEA 162
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
26-241 |
3.04e-15 |
|
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: 78.52 E-value: 3.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 26 HVDHGKSTLADrlleltgTIDKTKnnkqVldklqVERE-RGIT--VKAqtaslfYNCEGKQYLLNLIDTPGHVDFSYEVS 102
Cdd:COG0532 12 HVDHGKTSLLD-------AIRKTN----V-----AAGEaGGITqhIGA------YQVETNGGKITFLDTPGHEAFTAMRA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 103 RSLSACQGVLLVVDANEGIQAQTV-A-NFflAFEAQLSVIPVINKIDLKNADPERVENQIEKVFDIPSD-----ECIKIS 175
Cdd:COG0532 70 RGAQVTDIVILVVAADDGVMPQTIeAiNH--AKAAGVPIIVAINKIDKPGANPDRVKQELAEHGLVPEEwggdtIFVPVS 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370487429 176 AKLGTNV----ESV-LQAIIERIpppKVHRKNPLRALVFDSTFDQYRGVIANVALFDGVVSKGDKIVSAHT 241
Cdd:COG0532 148 AKTGEGIdellEMIlLQAEVLEL---KANPDRPARGTVIEAKLDKGRGPVATVLVQNGTLKVGDIVVAGTA 215
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
26-200 |
4.93e-15 |
|
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: 78.42 E-value: 4.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 26 HVDHGKSTLadrLLELTGtIDkTknnkqvlDKLQVERERGITVKAQTASLFYNCeGKQylLNLIDTPGHVDFsyeVSRSL 105
Cdd:COG3276 8 HIDHGKTTL---VKALTG-ID-T-------DRLKEEKKRGITIDLGFAYLPLPD-GRR--LGFVDVPGHEKF---IKNML 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 106 SACQG---VLLVVDANEGIQAQTVANF----FLAFEaQLSVipVINKIDLknADPERVENQIEKVFDIPSD------ECI 172
Cdd:COG3276 70 AGAGGidlVLLVVAADEGVMPQTREHLaildLLGIK-RGIV--VLTKADL--VDEEWLELVEEEIRELLAGtfledaPIV 144
|
170 180 190
....*....|....*....|....*....|.
gi 1370487429 173 KISAKLGTNVE---SVLQAIIERIPPPKVHR 200
Cdd:COG3276 145 PVSAVTGEGIDelrAALDALAAAVPARDADG 175
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
20-283 |
7.05e-15 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 77.17 E-value: 7.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 20 NFSIVAHVDHGKSTLADRLLELTGTIDKTKNNK-QVLDKLQVERERGITVkaQTASLFYNCEGKQYllNLIDTPGHVDFS 98
Cdd:PLN03127 63 NVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAfDEIDKAPEEKARGITI--ATAHVEYETAKRHY--AHVDCPGHADYV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 99 YEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQL-SVIPVINKIDLKNaDPERVE------NQIEKVFDIPSDEc 171
Cdd:PLN03127 139 KNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVpSLVVFLNKVDVVD-DEELLElvemelRELLSFYKFPGDE- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 172 IKI------SAKLGTNVE-------SVLQAIIERIPPPKVHRKNPLRALVFDSTFDQYRGVIANVALFDGVVSKGD--KI 236
Cdd:PLN03127 217 IPIirgsalSALQGTNDEigknailKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEevEI 296
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1370487429 237 VSAHTQKTYEVNEVGVlnpnEQPTHKLYAGQ----VGYLIAGMK--DVTEAQI 283
Cdd:PLN03127 297 VGLRPGGPLKTTVTGV----EMFKKILDQGQagdnVGLLLRGLKreDVQRGQV 345
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
20-236 |
7.67e-15 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 76.81 E-value: 7.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 20 NFSIVAHVDHGKSTLAdrlLELTGTidKTknnkqvlDKLQVERERGITVK---AQTAslFY---NCEGKQYL-------- 85
Cdd:PRK04000 11 NIGMVGHVDHGKTTLV---QALTGV--WT-------DRHSEELKRGITIRlgyADAT--IRkcpDCEEPEAYttepkcpn 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 86 ----------LNLIDTPGHvdfsyEV--SRSLSAC---QGVLLVVDANEGI-QAQTVANFfLAFEA--QLSVIPVINKID 147
Cdd:PRK04000 77 cgsetellrrVSFVDAPGH-----ETlmATMLSGAalmDGAILVIAANEPCpQPQTKEHL-MALDIigIKNIVIVQNKID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 148 LknADPER-VEN--QI---------EKVFDIPsdecikISAKLGTNVESVLQAIIERIPPPKVHRKNPLRALV---FD-- 210
Cdd:PRK04000 151 L--VSKERaLENyeQIkefvkgtvaENAPIIP------VSALHKVNIDALIEAIEEEIPTPERDLDKPPRMYVarsFDvn 222
|
250 260 270
....*....|....*....|....*....|
gi 1370487429 211 ---STFDQYR-GVIANvALFDGVVSKGDKI 236
Cdd:PRK04000 223 kpgTPPEKLKgGVIGG-SLIQGVLKVGDEI 251
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
19-168 |
1.15e-14 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 77.10 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 19 RNFSIVAHVDHGKSTLADRLL------ELTGTIDKTKNNKQVL-DKLQVERERGITVkaqTASL--FyncEGKQYLLNLI 89
Cdd:PRK00741 11 RTFAIISHPDAGKTTLTEKLLlfggaiQEAGTVKGRKSGRHATsDWMEMEKQRGISV---TSSVmqF---PYRDCLINLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 90 DTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVAnfflAFE-AQLSVIPV---INKIDLKNADPERVENQIEKVFD 165
Cdd:PRK00741 85 DTPGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTRK----LMEvCRLRDTPIftfINKLDRDGREPLELLDEIEEVLG 160
|
...
gi 1370487429 166 IPS 168
Cdd:PRK00741 161 IAC 163
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
20-250 |
1.15e-14 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 76.71 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 20 NFSIVAHVDHGKSTLADRLLELTGTIDKTKNNK----------------QVLDKLQVERERGITVKAQTaslfYNCEGKQ 83
Cdd:PTZ00141 9 NLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKfekeaaemgkgsfkyaWVLDKLKAERERGITIDIAL----WKFETPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 84 YLLNLIDTPGHVDFSYEVSRSLSACQGVLLVVDANEGI-------QAQTVANFFLAFeaQLSV---IPVINKIDLK--NA 151
Cdd:PTZ00141 85 YYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEfeagiskDGQTREHALLAF--TLGVkqmIVCINKMDDKtvNY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 152 DPER-------VENQIEKV-FDIPSDECIKISAKLGTNV------------ESVLQAiIERIPPPKVHRKNPLRALVFDS 211
Cdd:PTZ00141 163 SQERydeikkeVSAYLKKVgYNPEKVPFIPISGWQGDNMieksdnmpwykgPTLLEA-LDTLEPPKRPVDKPLRLPLQDV 241
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1370487429 212 tfdqYR-GVIANVA---LFDGVVSKGDKIVSAHTQKTYEVNEV 250
Cdd:PTZ00141 242 ----YKiGGIGTVPvgrVETGILKPGMVVTFAPSGVTTEVKSV 280
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
27-237 |
8.71e-13 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 70.71 E-value: 8.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 27 VDHGKSTLADRLLELTGTI----------DKTKNNKQ--------VLDKLQVERERGITVkaQTASLFYNCEGKQYLlnL 88
Cdd:PRK05124 36 VDDGKSTLIGRLLHDTKQIyedqlaslhnDSKRHGTQgekldlalLVDGLQAEREQGITI--DVAYRYFSTEKRKFI--I 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 89 IDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAfeAQLS---VIPVINKIDLKNADPERVEN------- 158
Cdd:PRK05124 112 ADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIA--TLLGikhLVVAVNKMDLVDYSEEVFERiredylt 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 159 ---QIEKVFDIpsdECIKISAKLGTNV------------ESVLQaIIERIPPPKVHRKNPLRALVfdstfdQY------- 216
Cdd:PRK05124 190 faeQLPGNLDI---RFVPLSALEGDNVvsqsesmpwysgPTLLE-VLETVDIQRVVDAQPFRFPV------QYvnrpnld 259
|
250 260
....*....|....*....|..
gi 1370487429 217 -RGVIANVAlfDGVVSKGDKIV 237
Cdd:PRK05124 260 fRGYAGTLA--SGVVKVGDRVK 279
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
27-250 |
8.71e-13 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 71.11 E-value: 8.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 27 VDHGKSTLADRLL---------ELT---------GTIDKTKNNKQVLDKLQVERERGITVkaQTASLFYNCEGKQYLLnl 88
Cdd:PRK05506 33 VDDGKSTLIGRLLydskmifedQLAalerdskkvGTQGDEIDLALLVDGLAAEREQGITI--DVAYRYFATPKRKFIV-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 89 IDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAfeAQLS---VIPVINKIDLKNADPERVEnQIEKVF- 164
Cdd:PRK05506 109 ADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIA--SLLGirhVVLAVNKMDLVDYDQEVFD-EIVADYr 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 165 ------DIPSDECIKISAKLGTNV------------------------ESVLQAIIERIPPPKVHRKNplralvfdstfD 214
Cdd:PRK05506 186 afaaklGLHDVTFIPISALKGDNVvtrsarmpwyegpsllehletveiASDRNLKDFRFPVQYVNRPN-----------L 254
|
250 260 270
....*....|....*....|....*....|....*.
gi 1370487429 215 QYRGVIANVAlfDGVVSKGDKIVSAHTQKTYEVNEV 250
Cdd:PRK05506 255 DFRGFAGTVA--SGVVRPGDEVVVLPSGKTSRVKRI 288
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
5-288 |
1.61e-12 |
|
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: 69.42 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 5 REKLDMSRFPVenirNFSIVAHVDHGKSTLA---DRLLELTGTIDKTKNNKqvLDKLQVERERGITVkaQTASLFYNCEG 81
Cdd:TIGR00485 3 KEKFERTKPHV----NVGTIGHVDHGKTTLTaaiTTVLAKEGGAAARAYDQ--IDNAPEEKARGITI--NTAHVEYETET 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 82 KQYLlnLIDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPV-INKIDLKNaDPERVENQI 160
Cdd:TIGR00485 75 RHYA--HVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKCDMVD-DEELLELVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 161 EKV------FDIPSDECIKIS----------AKLGTNVESVLQAIIERIPPPKVHRKNPLRALVFDSTFDQYRGVIANVA 224
Cdd:TIGR00485 152 MEVrellsqYDFPGDDTPIIRgsalkalegdAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGR 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370487429 225 LFDGVVSKGDKIVSAHTQKTYEVNEVGVlnpnEQPTHKLYAGQ----VGYLIAGMKDvTEAQIGDTLC 288
Cdd:TIGR00485 232 VERGIIKVGEEVEIVGLKDTRKTTVTGV----EMFRKELDEGRagdnVGLLLRGIKR-EEIERGMVLA 294
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
16-191 |
2.77e-12 |
|
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: 65.53 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 16 ENIRnFSIVAHVDHGKSTLADRLLeltgtidktkNNKQVLdklqVERERGITVKAQTASLFYNceGKQYLLnlIDTPG-- 93
Cdd:cd01895 1 DPIK-IAIIGRPNVGKSSLLNALL----------GEERVI----VSDIAGTTRDSIDVPFEYD--GQKYTL--IDTAGir 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 94 -------HVDFsYEVSRSLSA---CQGVLLVVDANEGI--QAQTVANFflAFEAQLSVIPVINKIDLKNADPER---VEN 158
Cdd:cd01895 62 kkgkvteGIEK-YSVLRTLKAierADVVLLVLDASEGIteQDLRIAGL--ILEEGKALIIVVNKWDLVEKDEKTmkeFEK 138
|
170 180 190
....*....|....*....|....*....|....*..
gi 1370487429 159 QIEKVF----DIPsdeCIKISAKLGTNVESVLQAIIE 191
Cdd:cd01895 139 ELRRKLpfldYAP---IVFISALTGQGVDKLFDAIKE 172
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
30-191 |
2.82e-12 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 64.96 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 30 GKSTLADRLLeltgtidktknNKQVLDklqVERERGITVKAQTASLFYNCEGKqylLNLIDTPGHVD-------FSYEVS 102
Cdd:cd00880 9 GKSSLLNALL-----------GQNVGI---VSPIPGTTRDPVRKEWELLPLGP---VVLIDTPGLDEegglgreRVEEAR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 103 RSLSACQGVLLVVDA--NEGIQAQTVANFFlafEAQLSVIPVINKIDLKNADPERVENQIEKVFDIPSDECIKISAKLGT 180
Cdd:cd00880 72 QVADRADLVLLVVDSdlTPVEEEAKLGLLR---ERGKPVLLVLNKIDLVPESEEEELLRERKLELLPDLPVIAVSALPGE 148
|
170
....*....|.
gi 1370487429 181 NVESVLQAIIE 191
Cdd:cd00880 149 GIDELRKKIAE 159
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
20-197 |
3.78e-12 |
|
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: 65.37 E-value: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 20 NFSIVAHVDHGKSTLadrLLELTGTidKTKNNKQvldklqvERERGITVKAQTA-SLFY-------------------NC 79
Cdd:cd01888 2 NIGTIGHVAHGKTTL---VKALSGV--WTVRHKE-------ELKRNITIKLGYAnAKIYkcpncgcprpydtpececpGC 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 80 EGKQYLL---NLIDTPGHvdfsyEV--SRSLSAC---QGVLLVVDANEGI-QAQTVANFF-LAFEAQLSVIPVINKIDLk 149
Cdd:cd01888 70 GGETKLVrhvSFVDCPGH-----EIlmATMLSGAavmDGALLLIAANEPCpQPQTSEHLAaLEIMGLKHIIILQNKIDL- 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370487429 150 nADPERVENQIEKV---------FDIPsdeCIKISAKLGTNVESVLQAIIERIPPPK 197
Cdd:cd01888 144 -VKEEQALENYEQIkefvkgtiaENAP---IIPISAQLKYNIDVLCEYIVKKIPTPP 196
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
77-200 |
1.06e-11 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 67.38 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 77 YNCEGKQYLLnlIDTPG-----HVDFS---YEVSRSLSA---CQGVLLVVDANEGI--QAQTVANFflAFEAQLSVIPVI 143
Cdd:PRK00093 216 FERDGQKYTL--IDTAGirrkgKVTEGvekYSVIRTLKAierADVVLLVIDATEGIteQDLRIAGL--ALEAGRALVIVV 291
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370487429 144 NKIDLKNADP-ERVENQIEKVF----DIPSdecIKISAKLGTNVESVLQAIIE-------RIPPPKVHR 200
Cdd:PRK00093 292 NKWDLVDEKTmEEFKKELRRRLpfldYAPI---VFISALTGQGVDKLLEAIDEayenanrRISTSVLNR 357
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
77-194 |
1.14e-11 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 66.97 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 77 YNCEGKQYLLnlIDTPG-----HVD-----FSyeVSRSLSA---CQGVLLVVDANEGIQAQ--TVANffLAFEAQLSVIP 141
Cdd:COG1160 218 FERDGKKYTL--IDTAGirrkgKVDegiekYS--VLRTLRAierADVVLLVIDATEGITEQdlKIAG--LALEAGKALVI 291
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370487429 142 VINKIDL---KNADPERVENQIEKVF----DIPsdeCIKISAKLGTNVESVLQAIIE-------RIP 194
Cdd:COG1160 292 VVNKWDLvekDRKTREELEKEIRRRLpfldYAP---IVFISALTGQGVDKLLEAVDEvyesankRIS 355
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
30-193 |
4.70e-11 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 61.92 E-value: 4.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 30 GKSTLADRLLEltGTIDktknnkqvldklqvERERGITVKAQTASLFYNCEGKQYLLNLIDTPGHVDFSYE---VSRSLS 106
Cdd:COG1100 15 GKTSLVNRLVG--DIFS--------------LEKYLSTNGVTIDKKELKLDGLDVDLVIWDTPGQDEFRETrqfYARQLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 107 ACQGVLLVVDaneGIQAQTVANFFLAFEA------QLSVIPVINKIDLknADPERVENQ---IEKVFDIPSDECIKISAK 177
Cdd:COG1100 79 GASLYLFVVD---GTREETLQSLYELLESlrrlgkKSPIILVLNKIDL--YDEEEIEDEerlKEALSEDNIVEVVATSAK 153
|
170
....*....|....*.
gi 1370487429 178 LGTNVESVLQAIIERI 193
Cdd:COG1100 154 TGEGVEELFAALAEIL 169
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
20-244 |
6.05e-11 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 64.58 E-value: 6.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 20 NFSIVAHVDHGKSTladrlleLTGTIDKTKNNKQV--------LDKLQVERERGITVkaQTASLFYNCEGKQYLlnLIDT 91
Cdd:PRK12736 14 NIGTIGHVDHGKTT-------LTAAITKVLAERGLnqakdydsIDAAPEEKERGITI--NTAHVEYETEKRHYA--HVDC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 92 PGHVDfsYEVSRSLSACQ--GVLLVVDANEGIQAQTVANFFLAFEAQLSVIPV-INKIDLKNaDPER---VENQIEKV-- 163
Cdd:PRK12736 83 PGHAD--YVKNMITGAAQmdGAILVVAATDGPMPQTREHILLARQVGVPYLVVfLNKVDLVD-DEELlelVEMEVRELls 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 164 -FDIPSDEC--IKISA--------KLGTNVESVLQAIIERIPPPKVHRKNPLRALVFDSTFDQYRGVIANVALFDGVVSK 232
Cdd:PRK12736 160 eYDFPGDDIpvIRGSAlkalegdpKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKV 239
|
250
....*....|....*
gi 1370487429 233 GD--KIVSAH-TQKT 244
Cdd:PRK12736 240 GDevEIVGIKeTQKT 254
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
20-278 |
1.29e-10 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 63.87 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 20 NFSIVAHVDHGKSTLADRLLELTGTIDKTKNNK-QVLDKLQVERERGITVkaQTASLFYNCEGKQYLLnlIDTPGHVDFS 98
Cdd:PLN03126 83 NIGTIGHVDHGKTTLTAALTMALASMGGSAPKKyDEIDAAPEERARGITI--NTATVEYETENRHYAH--VDCPGHADYV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 99 YEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQL-SVIPVINKIDLKNADP--ERVENQIEKV---FDIPSDECI 172
Cdd:PLN03126 159 KNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVpNMVVFLNKQDQVDDEEllELVELEVRELlssYEFPGDDIP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 173 KISA---------------KLGTN-----VESVLQAIIERIPPPKVHRKNPLRALVFDSTFDQYRGVIANVALFDGVVSK 232
Cdd:PLN03126 239 IISGsallalealmenpniKRGDNkwvdkIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKV 318
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1370487429 233 GDKIVSAHTQKTYEVNEVGVLNPNEQPTHKLYAGQVGYLIAGMKDV 278
Cdd:PLN03126 319 GETVDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKA 364
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
88-195 |
2.06e-10 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 61.93 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 88 LIDTPG-H----------VDFsyeVSRSLSACQGVLLVVDANEGIQAQTvaNFFLAFEAQLS--VIPVINKIDLknADPE 154
Cdd:COG1159 55 FVDTPGiHkpkrklgrrmNKA---AWSALEDVDVILFVVDATEKIGEGD--EFILELLKKLKtpVILVINKIDL--VKKE 127
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1370487429 155 RVENQIEKVFD-IPSDECIKISAKLGTNVESVLQAIIERIPP 195
Cdd:COG1159 128 ELLPLLAEYSElLDFAEIVPISALKGDNVDELLDEIAKLLPE 169
|
|
| EFG_III-like |
cd16257 |
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G ... |
305-378 |
2.90e-10 |
|
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: 56.59 E-value: 2.90e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370487429 305 PMVFAGMYPLDQSEYNNLKSAIEKLTLNDSSVTVHRDSSlalGAGWRLGFLGLLHMEVFNQRLEQEYNASVILT 378
Cdd:cd16257 1 PVVFVTVEVKNPLDQEKLLEGLERLSEEDPALQVYREES---TGEFILSGLGELHLEIIVARLEREYGVELVVS 71
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
26-196 |
5.49e-10 |
|
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.
Pssm-ID: 206671 [Multi-domain] Cd Length: 195 Bit Score: 59.13 E-value: 5.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 26 HVDHGKSTLAD---RLLELTGtIDKTKNNKQVlDKLQVERERGITVkaQTASLFYNCEGKQYllNLIDTPGHVDFSYEVS 102
Cdd:cd01884 10 HVDHGKTTLTAaitKVLAKKG-GAKAKKYDEI-DKAPEEKARGITI--NTAHVEYETANRHY--AHVDCPGHADYIKNMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 103 RSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPV-INKIDLKnADPERVE------NQIEKVFDIPSDEC--IK 173
Cdd:cd01884 84 TGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVfLNKADMV-DDEELLElvemevRELLSKYGFDGDDTpiVR 162
|
170 180 190
....*....|....*....|....*....|...
gi 1370487429 174 ISA---------KLGTN-VESVLQAIIERIPPP 196
Cdd:cd01884 163 GSAlkalegddpNKWVDkILELLDALDSYIPTP 195
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
218-288 |
8.69e-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: 55.35 E-value: 8.69e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370487429 218 GVIANVALFDGVVSKGDKI--VSAHTQKTYEVNEVGVLNPNEQPTHKLYAGQVGYLIAGMKDVTEAQIGDTLC 288
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVriLPNGTGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
20-147 |
9.28e-10 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 61.26 E-value: 9.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 20 NFSIVAHVDHGKSTLADRLLELTGTIDK----------TKNNKQ------VLDKLQVERERGITVKAQtaslFYNCEGKQ 83
Cdd:PLN00043 9 NIVVIGHVDSGKSTTTGHLIYKLGGIDKrvierfekeaAEMNKRsfkyawVLDKLKAERERGITIDIA----LWKFETTK 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370487429 84 YLLNLIDTPGHVDFSYEVSRSLSACQGVLLVVDANEG-------IQAQTVANFFLAFEAQL-SVIPVINKID 147
Cdd:PLN00043 85 YYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGgfeagisKDGQTREHALLAFTLGVkQMICCCNKMD 156
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
22-239 |
9.64e-10 |
|
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: 61.37 E-value: 9.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 22 SIVAHVDHGKSTLADRLL----------ELTGTIDKTKNNKQVLDKLQVERERGITVKAQTASLFYncegkqyllnlIDT 91
Cdd:TIGR00491 8 VVLGHVDHGKTTLLDKIRgtavvkkeagGITQHIGASEVPTDVIEKICGDLLKSFKIKLKIPGLLF-----------IDT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 92 PGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDL-----------------KNADP- 153
Cdd:TIGR00491 77 PGHEAFTNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTPFVVAANKIDRipgwkshegypflesinKQEQRv 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 154 -----ERVENQI-------------EKVFDIPSDEC-IKISAKLGTNVESVLQAII--------ERIpppKVHRKNPLRA 206
Cdd:TIGR00491 157 rqnldKQVYNLViqlaeqgfnaerfDRIRDFTKTVAiIPVSAKTGEGIPELLAILAglaqnyleNKL---KLAIEGPAKG 233
|
250 260 270
....*....|....*....|....*....|...
gi 1370487429 207 LVFDSTFDQYRGVIANVALFDGVVSKGDKIVSA 239
Cdd:TIGR00491 234 TILEVKEEQGLGYTIDAVIYDGILRKGDIIVLA 266
|
|
| EFG_mtEFG_C |
cd03713 |
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational ... |
421-497 |
2.98e-09 |
|
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: 53.69 E-value: 2.98e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370487429 421 EPVVLGTIITPDEYTGKIMMLCEARRAVQKNMIfIDQNRVMLKYLFPLNEIvVDFYDSLKSLSSGYASFDYEDAGYQ 497
Cdd:cd03713 1 EPIMKVEVTVPEEYMGDVIGDLSSRRGQILGTE-SRGGWKVIKAEVPLAEM-FGYSTDLRSLTQGRGSFTMEFSHYE 75
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
30-195 |
7.44e-09 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 57.36 E-value: 7.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 30 GKSTLADRLLeltGT---IdktknnkqVLDKLQVERER--GItvkaqtaslfYNCEGKQYLLnlIDTPG-H--------- 94
Cdd:PRK00089 17 GKSTLLNALV---GQkisI--------VSPKPQTTRHRirGI----------VTEDDAQIIF--VDTPGiHkpkralnra 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 95 -VDFsyeVSRSLSACQGVLLVVDANEGIQAQTvaNFFLAF--EAQLSVIPVINKIDLKNaDPERVENQIEKVFD-IPSDE 170
Cdd:PRK00089 74 mNKA---AWSSLKDVDLVLFVVDADEKIGPGD--EFILEKlkKVKTPVILVLNKIDLVK-DKEELLPLLEELSElMDFAE 147
|
170 180
....*....|....*....|....*
gi 1370487429 171 CIKISAKLGTNVESVLQAIIERIPP 195
Cdd:PRK00089 148 IVPISALKGDNVDELLDVIAKYLPE 172
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
26-296 |
1.10e-08 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 58.14 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 26 HVDHGKSTLadrLLELTGtIDKtknnkqvlDKLQVERERGITVKAQTAslfYNCEGKQYLLNLIDTPGHVDFsyeVSRSL 105
Cdd:PRK10512 8 HVDHGKTTL---LQAITG-VNA--------DRLPEEKKRGMTIDLGYA---YWPQPDGRVLGFIDVPGHEKF---LSNML 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 106 SACQGV---LLVVDANEGIQAQT---VANFFLAFEAQLSVipVINKIDLknADPER---VENQIEKV---FDIPSDECIK 173
Cdd:PRK10512 70 AGVGGIdhaLLVVACDDGVMAQTrehLAILQLTGNPMLTV--ALTKADR--VDEARiaeVRRQVKAVlreYGFAEAKLFV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 174 ISAKLGTNVESV---LQAIIERIPPPkvHRKnpLRaLVFDSTFdQYRG---VIANVALfDGVVSKGDKIVSAHTQKTYEV 247
Cdd:PRK10512 146 TAATEGRGIDALrehLLQLPEREHAA--QHR--FR-LAIDRAF-TVKGaglVVTGTAL-SGEVKVGDTLWLTGVNKPMRV 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1370487429 248 NEvgvLNPNEQPTHKLYAGQ-VGYLIAGmkDVTEAQI--GDTLcLHKQPVEP 296
Cdd:PRK10512 219 RG---LHAQNQPTEQAQAGQrIALNIAG--DAEKEQInrGDWL-LADAPPEP 264
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
26-176 |
3.41e-08 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 55.97 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 26 HVDHGKSTLAdrlLELTGTIDKTKNNKQV----LDKLQVERERGITVkaQTASLFYNCEGKQYllNLIDTPGHVDFsyeV 101
Cdd:PRK00049 20 HVDHGKTTLT---AAITKVLAKKGGAEAKaydqIDKAPEEKARGITI--NTAHVEYETEKRHY--AHVDCPGHADY---V 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 102 SRSLS-ACQ--GVLLVVDANEGIQAQTVANFFLAFEAQLSVIPV-INKIDLKNaDPE---RVENQIEKV---FDIPSDEC 171
Cdd:PRK00049 90 KNMITgAAQmdGAILVVSAADGPMPQTREHILLARQVGVPYIVVfLNKCDMVD-DEElleLVEMEVRELlskYDFPGDDT 168
|
....*..
gi 1370487429 172 --IKISA 176
Cdd:PRK00049 169 piIRGSA 175
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
84-193 |
3.80e-08 |
|
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.
Pssm-ID: 206727 [Multi-domain] Cd Length: 159 Bit Score: 52.88 E-value: 3.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 84 YLLNLIDTPG------HVdfsyE---VSRSLSACQG---VLLVVDANEGIQAQTVAnfFLAFEAQLSVIPVINKIDLKNA 151
Cdd:cd04164 51 IPVRLIDTAGlretedEI----EkigIERAREAIEEadlVLLVVDASEGLDEEDLE--ILELPAKKPVIVVLNKSDLLSD 124
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1370487429 152 DPERvenqiekvFDIPSDECIKISAKLGTNVESVLQAIIERI 193
Cdd:cd04164 125 AEGI--------SELNGKPIIAISAKTGEGIDELKEALLELA 158
|
|
| tufA |
CHL00071 |
elongation factor Tu |
20-236 |
6.00e-08 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 55.35 E-value: 6.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 20 NFSIVAHVDHGKSTLADRL---LELTGTiDKTKNNKQVlDKLQVERERGITVKaqTASLFYNCEGKQYllNLIDTPGHVD 96
Cdd:CHL00071 14 NIGTIGHVDHGKTTLTAAItmtLAAKGG-AKAKKYDEI-DSAPEEKARGITIN--TAHVEYETENRHY--AHVDCPGHAD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 97 FSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPV-INKIDLKNaDPERVE------NQIEKVFDIPSD 169
Cdd:CHL00071 88 YVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVfLNKEDQVD-DEELLElvelevRELLSKYDFPGD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 170 E--CIKISA-------------KLGTN--VESVLQ---AIIERIPPPKVHRKNPLRALVFDSTFDQYRGVIANVALFDGV 229
Cdd:CHL00071 167 DipIVSGSAllalealtenpkiKRGENkwVDKIYNlmdAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGT 246
|
....*..
gi 1370487429 230 VSKGDKI 236
Cdd:CHL00071 247 VKVGDTV 253
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
20-197 |
6.44e-08 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 55.23 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 20 NFSIVAHVDHGKSTladrlleLTGTIDKTKNNK--------QVLDKLQVERERGITVkaQTASLFYNCEGKQYllNLIDT 91
Cdd:PRK12735 14 NVGTIGHVDHGKTT-------LTAAITKVLAKKgggeakayDQIDNAPEEKARGITI--NTSHVEYETANRHY--AHVDC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 92 PGHVDFsyeVSRSLS-ACQ--GVLLVVDANEGIQAQTVANFFLAFEAQLSVIPV-INKIDLKNaDPER---VENQIEKV- 163
Cdd:PRK12735 83 PGHADY---VKNMITgAAQmdGAILVVSAADGPMPQTREHILLARQVGVPYIVVfLNKCDMVD-DEELlelVEMEVRELl 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1370487429 164 --FDIPSDEC--IKISAKLGTN----------VESVLQAIIERIPPPK 197
Cdd:PRK12735 159 skYDFPGDDTpiIRGSALKALEgdddeeweakILELMDAVDSYIPEPE 206
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
26-157 |
7.27e-08 |
|
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-Tu, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 439820 [Multi-domain] Cd Length: 396 Bit Score: 54.77 E-value: 7.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 26 HVDHGKSTL--AdrlleLTGTIDKTKNNKQV----LDKLQVERERGITVkaQTASLFYNCEGKQYllNLIDTPGHVDFsy 99
Cdd:COG0050 20 HVDHGKTTLtaA-----ITKVLAKKGGAKAKaydqIDKAPEEKERGITI--NTSHVEYETEKRHY--AHVDCPGHADY-- 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370487429 100 eVSRSLS-ACQ--GVLLVVDANEGIQAQTVANFFLAfeAQLSV--IPV-INKIDLKNaDPERVE 157
Cdd:COG0050 89 -VKNMITgAAQmdGAILVVSATDGPMPQTREHILLA--RQVGVpyIVVfLNKCDMVD-DEELLE 148
|
|
| MnmE |
COG0486 |
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
84-193 |
1.23e-07 |
|
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: 54.30 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 84 YLLNLIDTPG------HVdfsyE---VSRSLSACQG---VLLVVDANEGIQAQTVAnfFLAFEAQLSVIPVINKIDLKNA 151
Cdd:COG0486 261 IPVRLIDTAGlretedEV----EkigIERAREAIEEadlVLLLLDASEPLTEEDEE--ILEKLKDKPVIVVLNKIDLPSE 334
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1370487429 152 DPERVEnqiekvfDIPSDECIKISAKLGTNVESVLQAIIERI 193
Cdd:COG0486 335 ADGELK-------SLPGEPVIAISAKTGEGIDELKEAILELV 369
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
23-237 |
1.64e-07 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 54.42 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 23 IVA---HVDHGKSTLADRlleltgtIDKTKnnkqVldklqVERERG-IT------------VKAQTASLFYNCEGKQYL- 85
Cdd:PRK04004 8 IVVvlgHVDHGKTTLLDK-------IRGTA----V-----AAKEAGgITqhigatevpidvIEKIAGPLKKPLPIKLKIp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 86 -LNLIDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVanfflafEA----QLSVIPVI---NKIDL--------- 148
Cdd:PRK04004 72 gLLFIDTPGHEAFTNLRKRGGALADIAILVVDINEGFQPQTI-------EAinilKRRKTPFVvaaNKIDRipgwksted 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 149 ------KNADPERVENQIE-KVFDI---------PSDE------------CIKISAKLGTNVESVLQAII--------ER 192
Cdd:PRK04004 145 apflesIEKQSQRVQQELEeKLYELigqlselgfSADRfdrvkdftktvaIVPVSAKTGEGIPDLLMVLAglaqryleER 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1370487429 193 IpppKVHRKNPLRALVFDSTFDQYRGVIANVALFDGVVSKGDKIV 237
Cdd:PRK04004 225 L---KIDVEGPGKGTVLEVKEERGLGTTIDVILYDGTLRKGDTIV 266
|
|
| trmE |
PRK05291 |
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; |
84-193 |
1.84e-07 |
|
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
Pssm-ID: 235392 [Multi-domain] Cd Length: 449 Bit Score: 53.96 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 84 YLLNLIDTPG------HVdfsyE---VSRSLSACQG---VLLVVDANEGIQAQTVANFFLafEAQLSVIPVINKIDLKNA 151
Cdd:PRK05291 263 IPLRLIDTAGiretddEV----EkigIERSREAIEEadlVLLVLDASEPLTEEDDEILEE--LKDKPVIVVLNKADLTGE 336
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1370487429 152 DPERVENqiekvfdipSDECIKISAKLGTNVESVLQAIIERI 193
Cdd:PRK05291 337 IDLEEEN---------GKPVIRISAKTGEGIDELREAIKELA 369
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
20-236 |
5.09e-07 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 52.31 E-value: 5.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 20 NFSIVAHVDHGKSTLADrllELTGTidKTKNNKQvldklqvERERGITVKA--QTASLF----------Y---------- 77
Cdd:PTZ00327 36 NIGTIGHVAHGKSTVVK---ALSGV--KTVRFKR-------EKVRNITIKLgyANAKIYkcpkcprptcYqsygsskpdn 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 78 ----NCEGKQYLL---NLIDTPGHvDFSyeVSRSLS-AC--QGVLLVVDANEGI-QAQTVANFFLAFEAQLSVIPVI-NK 145
Cdd:PTZ00327 104 ppcpGCGHKMTLKrhvSFVDCPGH-DIL--MATMLNgAAvmDAALLLIAANESCpQPQTSEHLAAVEIMKLKHIIILqNK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 146 IDL-KNADPERVENQIEKVFDIPSDE---CIKISAKLGTNVESVLQAIIERIPPPKVHRKNPLRALV---FD-----STF 213
Cdd:PTZ00327 181 IDLvKEAQAQDQYEEIRNFVKGTIADnapIIPISAQLKYNIDVVLEYICTQIPIPKRDLTSPPRMIVirsFDvnkpgEDI 260
|
250 260
....*....|....*....|...
gi 1370487429 214 DQYRGVIANVALFDGVVSKGDKI 236
Cdd:PTZ00327 261 ENLKGGVAGGSILQGVLKVGDEI 283
|
|
| MnmE_helical |
pfam12631 |
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ... |
84-191 |
1.06e-06 |
|
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An N-terminal domain, a helical domain and a GTPase domain which is nested within the helical domain. This family represents the helical domain.
Pssm-ID: 463649 [Multi-domain] Cd Length: 326 Bit Score: 50.94 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 84 YLLNLIDTPG------HVdfsyE---VSRSLSACQG---VLLVVDANEGIQAQTvANFFLAFEAQLSVIPVINKIDLKNA 151
Cdd:pfam12631 142 IPLRLIDTAGiretddEV----EkigIERAREAIEEadlVLLVLDASRPLDEED-LEILELLKDKKPIIVVLNKSDLLGE 216
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1370487429 152 DPERVENqiekvfdiPSDECIKISAKLGTNVESVLQAIIE 191
Cdd:pfam12631 217 IDELEEL--------KGKPVLAISAKTGEGLDELEEAIKE 248
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
30-191 |
1.50e-06 |
|
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: 48.61 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 30 GKSTLADRLLELTGTIdktknnkqVLDKLQVERER--GItvkaqtaslfYNCEGKQYLLnlIDTPG-HVDFS-------Y 99
Cdd:cd04163 15 GKSTLLNALVGQKISI--------VSPKPQTTRNRirGI----------YTDDDAQIIF--VDTPGiHKPKKklgermvK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 100 EVSRSLSACQGVLLVVDANEGI--QAQTVANffLAFEAQLSVIPVINKIDLKNaDPERVENQIEKVFD-IPSDECIKISA 176
Cdd:cd04163 75 AAWSALKDVDLVLFVVDASEWIgeGDEFILE--LLKKSKTPVILVLNKIDLVK-DKEDLLPLLEKLKElHPFAEIFPISA 151
|
170
....*....|....*
gi 1370487429 177 KLGTNVESVLQAIIE 191
Cdd:cd04163 152 LKGENVDELLEYIVE 166
|
|
| HflX |
cd01878 |
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
111-193 |
4.45e-06 |
|
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment N-terminal of the GTPase domain characterizes the HflX subfamily. The E. coli HflX has been implicated in the control of the lambda cII repressor proteolysis, but the actual biological functions of these GTPases remain unclear. HflX is widespread, but not universally represented in all three superkingdoms.
Pssm-ID: 206666 [Multi-domain] Cd Length: 204 Bit Score: 47.84 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 111 VLLVVDA---NEGIQAQTVANFfLAfEAQLSVIPVI---NKIDLknADPERVENQIEKvfdiPSDECIKISAKLGTNVES 184
Cdd:cd01878 124 LLHVVDAsdpDREEQIETVEEV-LK-ELGADDIPIIlvlNKIDL--LDDEELEERLRA----GRPDAVFISAKTGEGLDL 195
|
....*....
gi 1370487429 185 VLQAIIERI 193
Cdd:cd01878 196 LKEAIEELL 204
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
204-288 |
1.53e-05 |
|
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: 43.41 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 204 LRALVFDSTFDQYRGVIANVALFDGVVSKGDKIVSAHTQKTYEVNEVGVlnpNEQPTHKLYAGQVGYLiaGMKDVTEAQI 283
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIER---FHEEVDEAKAGDIVGI--GILGVKDILT 75
|
....*
gi 1370487429 284 GDTLC 288
Cdd:cd01342 76 GDTLT 80
|
|
| YihA_EngB |
cd01876 |
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
76-193 |
1.87e-05 |
|
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.
Pssm-ID: 206665 [Multi-domain] Cd Length: 170 Bit Score: 45.58 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 76 FYNCEGKQYLlnlIDTPG----------HVDFSYEVSRSLSACQ---GVLLVVDANEGIQAQTVANFFLAFEAQLSVIPV 142
Cdd:cd01876 40 FFNVGDKFRL---VDLPGygyakvskevREKWGKLIEEYLENREnlkGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIV 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1370487429 143 INKID-LKNADPERVENQIEKVFD--IPSDECIKISAKLGTNVESVLQAIIERI 193
Cdd:cd01876 117 LTKADkLKKSELAKVLKKIKEELNlfNILPPVILFSSKKGTGIDELRALIAEWL 170
|
|
| EFG_mtEFG_II |
cd04088 |
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation ... |
204-288 |
4.58e-05 |
|
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: 42.12 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 204 LRALVFDSTFDQYRGVIANVALFDGVVSKGDKIVSAHTQKTYEVNEVGVLNPNEQ-PTHKLYAGQVGyLIAGMKDvteAQ 282
Cdd:cd04088 1 FSALVFKTMADPFVGKLTFFRVYSGTLKSGSTVYNSTKGKKERVGRLLRMHGKKReEVEELGAGDIG-AVVGLKD---TR 76
|
....*.
gi 1370487429 283 IGDTLC 288
Cdd:cd04088 77 TGDTLC 82
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
85-217 |
6.46e-05 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 45.53 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 85 LLNLIDTPGHVDFSY------EVSRSLSACQGVLLVVDANEgIQAQTVANFFLAFEAQLSVIP---VINKIDLknADPER 155
Cdd:COG3596 89 GLVLLDTPGLGEVNErdreyrELRELLPEADLILWVVKADD-RALATDEEFLQALRAQYPDPPvlvVLTQVDR--LEPER 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 156 VEN-------------------QIEKVFDIPSDECIKISAKL---GTNVESVLQAIIERIPPPKVHRknpLRALVFDSTF 213
Cdd:COG3596 166 EWDppynwpsppkeqnirraleAIAEQLGVPIDRVIPVSAAEdrtGYGLEELVDALAEALPEAKRSR---LARLLRAKAI 242
|
....
gi 1370487429 214 DQYR 217
Cdd:COG3596 243 DRYT 246
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
30-145 |
1.05e-04 |
|
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: 41.84 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 30 GKSTLADRLleltgtidkTKNNKQVLDKLqvererGITVKAQTASLFYNceGKQYLLnlIDTPGHVDFSYE---VSRSLS 106
Cdd:pfam01926 11 GKSTLINAL---------TGAKAIVSDYP------GTTRDPNEGRLELK--GKQIIL--VDTPGLIEGASEgegLGRAFL 71
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1370487429 107 A---CQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINK 145
Cdd:pfam01926 72 AiieADLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
|
|
| PRK09518 |
PRK09518 |
bifunctional cytidylate kinase/GTPase Der; Reviewed |
80-198 |
3.76e-04 |
|
bifunctional cytidylate kinase/GTPase Der; Reviewed
Pssm-ID: 236546 [Multi-domain] Cd Length: 712 Bit Score: 43.63 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 80 EGKQYLLnlIDTPG----------HVDFSYEVSRS-LSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDL 148
Cdd:PRK09518 496 DGEDWLF--IDTAGikrrqhkltgAEYYSSLRTQAaIERSELALFLFDASQPISEQDLKVMSMAVDAGRALVLVFNKWDL 573
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370487429 149 KNADP-ERVENQIEKVFD-IPSDECIKISAKLGTNVESVLQAIIE-------RIPPPKV 198
Cdd:PRK09518 574 MDEFRrQRLERLWKTEFDrVTWARRVNLSAKTGWHTNRLAPAMQEaleswdqRIPTGKL 632
|
|
| BipA_TypA_C |
cd03710 |
BipA_TypA_C: a C-terminal portion of BipA or TypA having homology to the C terminal domains of ... |
421-467 |
3.88e-04 |
|
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: 39.41 E-value: 3.88e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1370487429 421 EPVVLGTIITPDEYTGKIMMLCEARRAVQKNMIFIDQNRVMLKYLFP 467
Cdd:cd03710 1 EPIEELTIDVPEEYSGAVIEKLGKRKGEMVDMEPDGNGRTRLEFKIP 47
|
|
| SR_beta |
cd04105 |
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ... |
67-162 |
6.91e-04 |
|
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms the heterodimeric signal recognition particle (SRP); Signal recognition particle receptor, beta subunit (SR-beta). SR-beta and SR-alpha form the heterodimeric signal recognition particle (SRP or SR) receptor that binds SRP to regulate protein translocation across the ER membrane. Nascent polypeptide chains are synthesized with an N-terminal hydrophobic signal sequence that binds SRP54, a component of the SRP. SRP directs targeting of the ribosome-nascent chain complex (RNC) to the ER membrane via interaction with the SR, which is localized to the ER membrane. The RNC is then transferred to the protein-conducting channel, or translocon, which facilitates polypeptide translation across the ER membrane or integration into the ER membrane. SR-beta is found only in eukaryotes; it is believed to control the release of the signal sequence from SRP54 upon binding of the ribosome to the translocon. High expression of SR-beta has been observed in human colon cancer, suggesting it may play a role in the development of this type of cancer.
Pssm-ID: 206691 [Multi-domain] Cd Length: 202 Bit Score: 41.15 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 67 TVKAQTAS--LFYNCEGKQYLLNLIDTPGHVDFSYEVSRSLS-ACQGVLLVVDANEGIQ-AQTVANF----FLAFEAQLS 138
Cdd:cd04105 28 TVTSIEPNvaSFYSNSSKGKKLTLVDVPGHEKLRDKLLEYLKaSLKAIVFVVDSATFQKnIRDVAEFlydiLTDLEKIKN 107
|
90 100
....*....|....*....|....*...
gi 1370487429 139 VIPVI---NKIDLKNA-DPERVENQIEK 162
Cdd:cd04105 108 KIPILiacNKQDLFTAkPAKKIKELLEK 135
|
|
| Ras |
pfam00071 |
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ... |
78-194 |
8.39e-04 |
|
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop motif with GTP_EFTU, arf and myosin_head. See pfam00009 pfam00025, pfam00063. As regards Rab GTPases, these are important regulators of vesicle formation, motility and fusion. They share a fold in common with all Ras GTPases: this is a six-stranded beta-sheet surrounded by five alpha-helices.
Pssm-ID: 425451 [Multi-domain] Cd Length: 162 Bit Score: 40.58 E-value: 8.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 78 NCEGKQYLLNLIDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLS-VIPVI---NKIDLKNA-- 151
Cdd:pfam00071 42 EVDGKTVKLQIWDTAGQERFRALRPLYYRGADGFLLVYDITSRDSFENVKKWVEEILRHADeNVPIVlvgNKCDLEDQrv 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1370487429 152 -DPERVEnQIEKVFDIPSDECikiSAKLGTNVESVLQAIIERIP 194
Cdd:pfam00071 122 vSTEEGE-ALAKELGLPFMET---SAKTNENVEEAFEELAREIL 161
|
|
| YqeH |
cd01855 |
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ... |
111-197 |
8.74e-04 |
|
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases.
Pssm-ID: 206748 [Multi-domain] Cd Length: 191 Bit Score: 40.71 E-value: 8.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 111 VLLVVDanegiqaqtVANFFLAFEAQL-------SVIPVINKIDL--KNADPERVENQIEKVF---DIPSDECIKISAKL 178
Cdd:cd01855 37 VVHVVD---------IFDFPGSLIPGLaeligakPVILVGNKIDLlpKDVKPNRLKQWVKKRLkigGLKIKDVILVSAKK 107
|
90
....*....|....*....
gi 1370487429 179 GTNVESVLQAIIERIPPPK 197
Cdd:cd01855 108 GWGVEELIEEIKKLAKYRG 126
|
|
| Obg |
cd01898 |
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ... |
108-193 |
1.06e-03 |
|
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress response, chromosome partitioning, replication initiation, mycelium development, and sporulation. Obg proteins are among a large group of GTP binding proteins conserved from bacteria to humans. The E. coli homolog, ObgE is believed to function in ribosomal biogenesis. Members of the subfamily contain two equally and highly conserved domains, a C-terminal GTP binding domain and an N-terminal glycine-rich domain.
Pssm-ID: 206685 [Multi-domain] Cd Length: 170 Bit Score: 40.10 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 108 CQGVLLVVDANEGIQAqtVANFFL------AFEAQLS---VIPVINKIDLkNADPERVENQIEKVFDIPSDECIKISAKL 178
Cdd:cd01898 79 TRVLLHVIDLSGEDDP--VEDYETirneleAYNPGLAekpRIVVLNKIDL-LDAEERFEKLKELLKELKGKKVFPISALT 155
|
90
....*....|....*
gi 1370487429 179 GTNVESVLQAIIERI 193
Cdd:cd01898 156 GEGLDELLKKLAKLL 170
|
|
| EFG_III |
cd16262 |
Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial ... |
304-380 |
1.50e-03 |
|
Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial Elongation factor G (EF-G), and mitochondrial Elongation factor G1 (mtEFG1) and G2 (mtEFG2), which play an important role during peptide synthesis and tRNA site changes. In bacteria, this translocation step is catalyzed by EF-G_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. mtEFG1 and mtEFG2 show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects, and a tendency to lose mitochondrial DNA. No clear phenotype has been found for mutants of the yeast homolog of mtEFG2, MEF2.
Pssm-ID: 293919 [Multi-domain] Cd Length: 76 Bit Score: 37.44 E-value: 1.50e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370487429 304 KPMVFAGMYPLDQSEYNNLKSAIEKLTLNDSSVTVHRD--SSLALGAGwrlgfLGLLHMEVFNQRLEQEYNASVILTTP 380
Cdd:cd16262 2 EPVISLAIEPKTKADEDKLSKALARLAEEDPTLRVSRDeeTGQTILSG-----MGELHLEIIVERLKREYGVEVEVGKP 75
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
20-178 |
1.54e-03 |
|
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: 39.84 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 20 NFSIVAHVDHGKSTLADRLL--ELTGT-IDKTKNNKQVldkLQVERERGITvkaqtaslfyncegkqyllnLIDTPG--- 93
Cdd:cd09912 2 LLAVVGEFSAGKSTLLNALLgeEVLPTgVTPTTAVITV---LRYGLLKGVV--------------------LVDTPGlns 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 94 HVDFSYEVSRS-LSACQGVLLVVDANegiQAQTVANF-FLAFEAQLSVIP---VINKIDLKNADPERVENQIEKVFDIPS 168
Cdd:cd09912 59 TIEHHTEITESfLPRADAVIFVLSAD---QPLTESEReFLKEILKWSGKKiffVLNKIDLLSEEELEEVLEYSREELGVL 135
|
170
....*....|....*.
gi 1370487429 169 DECIK------ISAKL 178
Cdd:cd09912 136 ELGGGeprifpVSAKE 151
|
|
| NOG |
cd01897 |
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ... |
139-192 |
2.18e-03 |
|
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in eukaryotes ranging from trypanosomes to humans. NOG1 is functionally linked to ribosome biogenesis and found in association with the nuclear pore complexes and identified in many preribosomal complexes. Thus, defects in NOG1 can lead to defects in 60S biogenesis. The S. cerevisiae NOG1 gene is essential for cell viability, and mutations in the predicted G motifs abrogate function. It is a member of the ODN family of GTP-binding proteins that also includes the bacterial Obg and DRG proteins.
Pssm-ID: 206684 [Multi-domain] Cd Length: 167 Bit Score: 39.08 E-value: 2.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1370487429 139 VIPVINKIDLKNADPervENQIEKVFDIPSDECIKISAKLGTNVESVLQAIIER 192
Cdd:cd01897 115 VIVVLNKIDLLTEED---LSEIEKELEKEGEEVIKISTLTEEGVDELKNKACEL 165
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
86-237 |
2.26e-03 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 41.02 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 86 LNLIDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDL---------------KN 150
Cdd:PRK14845 528 LLFIDTPGHEAFTSLRKRGGSLADLAVLVVDINEGFKPQTIEAINILRQYKTPFVVAANKIDLipgwnisedepfllnFN 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 151 ADPERVENQIE---------------------KVFDIPSDECI-KISAKLGTNVESVLQAII--------ERIpppKVHR 200
Cdd:PRK14845 608 EQDQHALTELEiklyeligklyelgfdadrfdRVQDFTRTVAIvPVSAKTGEGIPELLMMVAglaqkyleERL---KLNV 684
|
170 180 190
....*....|....*....|....*....|....*..
gi 1370487429 201 KNPLRALVFDSTFDQYRGVIANVALFDGVVSKGDKIV 237
Cdd:PRK14845 685 EGYAKGTILEVKEEKGLGTTIDAIIYDGTLRRGDTIV 721
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
30-196 |
2.34e-03 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 40.78 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 30 GKSTLADRLlelTGT---IdktknnkqvldklqVERERGIT--VKAQTASLfyncEGKQYLLnlIDTPGHVD-----FSY 99
Cdd:COG1160 14 GKSTLFNRL---TGRrdaI--------------VDDTPGVTrdRIYGEAEW----GGREFTL--IDTGGIEPddddgLEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 100 EVSR-SLSACQG---VLLVVDANEGIQA--QTVANffLAFEAQLSVIPVINKIDLKNADPErvenqiekVFDIPS---DE 170
Cdd:COG1160 71 EIREqAELAIEEadvILFVVDGRAGLTPldEEIAK--LLRRSGKPVILVVNKVDGPKREAD--------AAEFYSlglGE 140
|
170 180
....*....|....*....|....*.
gi 1370487429 171 CIKISAKLGTNVESVLQAIIERIPPP 196
Cdd:COG1160 141 PIPISAEHGRGVGDLLDAVLELLPEE 166
|
|
| obgE |
PRK12299 |
GTPase CgtA; Reviewed |
142-193 |
3.61e-03 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237048 [Multi-domain] Cd Length: 335 Bit Score: 40.05 E-value: 3.61e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1370487429 142 VINKIDLKNADPERvENQIEKVFDIPSDECIKISAKLGTNVESVLQAIIERI 193
Cdd:PRK12299 277 VLNKIDLLDEEEER-EKRAALELAALGGPVFLISAVTGEGLDELLRALWELL 327
|
|
| Arf_Arl |
cd00878 |
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ... |
108-192 |
4.61e-03 |
|
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl (Arf-like) small GTPases. Arf proteins are activators of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. Arfs are N-terminally myristoylated. Members of the Arf family are regulators of vesicle formation in intracellular traffic that interact reversibly with membranes of the secretory and endocytic compartments in a GTP-dependent manner. They depart from other small GTP-binding proteins by a unique structural device, interswitch toggle, that implements front-back communication from N-terminus to the nucleotide binding site. Arf-like (Arl) proteins are close relatives of the Arf, but only Arl1 has been shown to function in membrane traffic like the Arf proteins. Arl2 has an unrelated function in the folding of native tubulin, and Arl4 may function in the nucleus. Most other Arf family proteins are so far relatively poorly characterized. Thus, despite their significant sequence homologies, Arf family proteins may regulate unrelated functions.
Pssm-ID: 206644 [Multi-domain] Cd Length: 158 Bit Score: 38.33 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 108 CQGVLLVVDANEGIQAQTVANFFLAF--EAQLSVIPVI---NKIDLKNADPERvenQIEKVFDIPSD-----ECIKISAK 177
Cdd:cd00878 67 TDGLIFVVDSSDRERIEEAKNELHKLlnEEELKGAPLLilaNKQDLPGALTES---ELIELLGLESIkgrrwHIQPCSAV 143
|
90
....*....|....*
gi 1370487429 178 LGTNVESVLQAIIER 192
Cdd:cd00878 144 TGDGLDEGLDWLIEQ 158
|
|
| EFG_C |
smart00838 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
420-497 |
5.84e-03 |
|
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: 36.33 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370487429 420 LEPVVLGTIITPDEYTGKIMMLCEARRAVQKNMifiDQNRVM--LKYLFPLNEIvVDFYDSLKSLSSGYASFDYEDAGYQ 497
Cdd:smart00838 2 LEPIMKVEVTVPEEYMGDVIGDLNSRRGKIEGM---EQRGGAqvIKAKVPLSEM-FGYATDLRSATQGRATWSMEFSHYE 77
|
|
| EFG_III |
pfam14492 |
Elongation Factor G, domain III; This domain is found in Elongation Factor G. It shares a ... |
304-377 |
8.13e-03 |
|
Elongation Factor G, domain III; This domain is found in Elongation Factor G. It shares a similar structure with domain V (pfam00679). Structural studies in drosophila indicate this is domain 3.
Pssm-ID: 464188 [Multi-domain] Cd Length: 75 Bit Score: 35.53 E-value: 8.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370487429 304 KPMVFAGMYPLDQSEYNNLKSAIEKLTLNDSSVTVHRDSslalGAG-WRLGFLGLLHMEVFNQRLEQEYNASVIL 377
Cdd:pfam14492 3 EPVISVAIEPKTKGDEDKLSKALNRLLEEDPTLRVERDE----ETGeTILSGMGELHLEIVVDRLKRKYGVEVEL 73
|
|
| RF3_III |
cd16259 |
Domain III of bacterial Release Factor 3 (RF3); The class II RF3 is a member of one of two ... |
305-378 |
8.75e-03 |
|
Domain III of bacterial Release Factor 3 (RF3); The class II RF3 is a member of one of two release factor (RF) classes required for the termination of protein synthesis by the ribosome. RF3 is a GTPase that removes class I RFs (RF1 or RF2) from the ribosome after release of the nascent polypeptide. RF3 in the GDP state binds to the ribosomal class I RF complex, followed by an exchange of GDP for GTP and release of the class I RF. Sequence comparison of class II release factors with elongation factors shows that prokaryotic RF3 is more similar to EF-G whereas eukaryotic eRF3 is more similar to eEF1A, implying that their precise function may differ.
Pssm-ID: 293916 [Multi-domain] Cd Length: 70 Bit Score: 35.31 E-value: 8.75e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370487429 305 PMVFAGMYPLDQSEYNNLKSAIEKLTlNDSSVTVHRDSSlalGAGWRLGFLGLLHMEVFNQRLEQEYNASVILT 378
Cdd:cd16259 1 PEHFRRVRLKDPMKAKQLRKGLEQLA-EEGAVQVFRPMD---GSDPIVGAVGPLQFEVLQARLENEYGVEVVFE 70
|
|
| |
