|
Name |
Accession |
Description |
Interval |
E-value |
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
41-647 |
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: 994.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 41 DMSRfpvedIRNFSIIAHVDHGKSTLADRLLELTGTIDKTKKNKQVLDKLQVERERGITVKAQTASLFY-SFGGKQYLLN 119
Cdd:COG0481 2 DQKN-----IRNFSIIAHIDHGKSTLADRLLELTGTLSEREMKEQVLDSMDLERERGITIKAQAVRLNYkAKDGETYQLN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 120 LIDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADPERVGKQIEKVFDIP 199
Cdd:COG0481 77 LIDTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKQEIEDIIGID 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 200 SEECIKISAKLGTNVDSVLQAVIERIPPPKVHRENPLKALVFDSTFDQYRGVIANIALFDGVVSKGDKIVSAHTKKAYEV 279
Cdd:COG0481 157 ASDAILVSAKTGIGIEEILEAIVERIPPPKGDPDAPLQALIFDSWYDSYRGVVVYVRVFDGTLKKGDKIKMMSTGKEYEV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 280 NEVGILNPNEQPTHKLYAGQVGFLIAGMKDVTEAQIGDTLYLHNHPV-EPLPGFKSAKPMVFAGVYPIDQSEYNNLKSAI 358
Cdd:COG0481 237 DEVGVFTPKMTPVDELSAGEVGYIIAGIKDVRDARVGDTITLAKNPAaEPLPGFKEVKPMVFAGLYPVDSDDYEDLRDAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 359 EKLTLNDSSVTVHRDSSLALGAGWRLGFLGLLHMEVFNQRLEQEYNASVILTTPTVPYKAVLSSAKlikeykekEITIIN 438
Cdd:COG0481 317 EKLQLNDASLTYEPETSAALGFGFRCGFLGLLHMEIIQERLEREFDLDLITTAPSVVYEVTLTDGE--------VIEVDN 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 439 PAQFPEKSQVTEYLEPVVLGTVITPTEYTGKIMALCQARRAIQKNMTFIDENRVMLKYLFPLNEIVVDFYDSLKSLSSGY 518
Cdd:COG0481 389 PSDLPDPGKIEEIEEPIVKATIITPSEYVGAVMELCQEKRGVQKNMEYLGENRVELTYELPLAEIVFDFFDRLKSITRGY 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 519 ASFDYEDAGYQTAELVKMDILLNGNMVEELVTVVHREKAYTVGKSICERLKESLPRQLYEIAIQAAVGSKVIARETVKAY 598
Cdd:COG0481 469 ASLDYEFIGYRESDLVKLDILINGEPVDALSFIVHRDKAYSRGRALVEKLKELIPRQQFEVPIQAAIGGKIIARETIKAL 548
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 27370038 599 RKNVLAKCYGGDITRKMKLLKRQSEGKKKLRKIGNIEIPKDAFIKVLKT 647
Cdd:COG0481 549 RKDVLAKCYGGDISRKRKLLEKQKEGKKRMKQVGNVEIPQEAFLAVLKV 597
|
|
| lepA |
TIGR01393 |
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a ... |
50-647 |
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: 892.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 50 IRNFSIIAHVDHGKSTLADRLLELTGTIDKTKKNKQVLDKLQVERERGITVKAQTASLFYSF-GGKQYLLNLIDTPGHVD 128
Cdd:TIGR01393 3 IRNFSIIAHIDHGKSTLADRLLEYTGAISEREMREQVLDSMDLERERGITIKAQAVRLNYKAkDGETYVLNLIDTPGHVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 129 FSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADPERVGKQIEKVFDIPSEECIKISA 208
Cdd:TIGR01393 83 FSYEVSRSLAACEGALLLVDAAQGIEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKKEIEEVIGLDASEAILASA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 209 KLGTNVDSVLQAVIERIPPPKVHRENPLKALVFDSTFDQYRGVIANIALFDGVVSKGDKIVSAHTKKAYEVNEVGILNPN 288
Cdd:TIGR01393 163 KTGIGIEEILEAIVKRVPPPKGDPDAPLKALIFDSHYDNYRGVVALVRVFEGTIKPGDKIRFMSTGKEYEVDEVGVFTPK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 289 EQPTHKLYAGQVGFLIAGMKDVTEAQIGDTLYLHNHPV-EPLPGFKSAKPMVFAGVYPIDQSEYNNLKSAIEKLTLNDSS 367
Cdd:TIGR01393 243 LTKTDELSAGEVGYIIAGIKDVSDVRVGDTITHVKNPAkEPLPGFKEVKPMVFAGLYPIDTEDYEDLRDALEKLKLNDAS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 368 VTVHRDSSLALGAGWRLGFLGLLHMEVFNQRLEQEYNASVILTTPTVPYKAVLSsaklikeyKEKEITIINPAQFPEKSQ 447
Cdd:TIGR01393 323 LTYEPESSPALGFGFRCGFLGLLHMEIIQERLEREFNLDLITTAPSVIYRVYLT--------NGEVIEVDNPSDLPDPGK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 448 VTEYLEPVVLGTVITPTEYTGKIMALCQARRAIQKNMTFIDENRVMLKYLFPLNEIVVDFYDSLKSLSSGYASFDYEDAG 527
Cdd:TIGR01393 395 IEHVEEPYVKATIITPTEYLGPIMTLCQEKRGVQTNMEYLDPNRVELIYEMPLAEIVYDFFDKLKSISRGYASFDYELIG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 528 YQTAELVKMDILLNGNMVEELVTVVHREKAYTVGKSICERLKESLPRQLYEIAIQAAVGSKVIARETVKAYRKNVLAKCY 607
Cdd:TIGR01393 475 YRPSDLVKLDILINGEPVDALSFIVHRDKAYSRGREICEKLKELIPRQQFEIPIQAAIGGKIIARETIKALRKDVTAKCY 554
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 27370038 608 GGDITRKMKLLKRQSEGKKKLRKIGNIEIPKDAFIKVLKT 647
Cdd:TIGR01393 555 GGDITRKRKLLEKQKEGKKRMKQIGKVEVPQEAFLAVLKV 594
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
51-228 |
1.69e-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: 342.59 E-value: 1.69e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 51 RNFSIIAHVDHGKSTLADRLLELTGTIDKTKKNKQVLDKLQVERERGITVKAQTASLFY-SFGGKQYLLNLIDTPGHVDF 129
Cdd:cd01890 1 RNFSIIAHIDHGKSTLADRLLELTGTVSEREMKEQVLDSMDLERERGITIKAQAVRLFYkAKDGEEYLLNLIDTPGHVDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 130 SYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADPERVGKQIEKVFDIPSEECIKISAK 209
Cdd:cd01890 81 SYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVKQEIEDVLGLDASEAILVSAK 160
|
170
....*....|....*....
gi 27370038 210 LGTNVDSVLQAVIERIPPP 228
Cdd:cd01890 161 TGLGVEDLLEAIVERIPPP 179
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
48-227 |
4.45e-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: 220.09 E-value: 4.45e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 48 EDIRNFSIIAHVDHGKSTLADRLLELTGTIDKTKKNKQ----VLDKLQVERERGITVKAQTASlfysFGGKQYLLNLIDT 123
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGegeaGLDNLPEERERGITIKSAAVS----FETKDYLINLIDT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 124 PGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKN-ADPERVGKQIEKVF------ 196
Cdd:pfam00009 77 PGHVDFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDgAELEEVVEEVSRELlekyge 156
|
170 180 190
....*....|....*....|....*....|.
gi 27370038 197 DIPSEECIKISAKLGTNVDSVLQAVIERIPP 227
Cdd:pfam00009 157 DGEFVPVVPGSALKGEGVQTLLDALDEYLPS 187
|
|
| LepA_C |
pfam06421 |
GTP-binding protein LepA C-terminus; This family consists of the C-terminal region of several ... |
540-646 |
1.02e-65 |
|
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: 211.11 E-value: 1.02e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 540 LNGNMVEELVTVVHREKAYTVGKSICERLKESLPRQLYEIAIQAAVGSKVIARETVKAYRKNVLAKCYGGDITRKMKLLK 619
Cdd:pfam06421 1 INGEPVDALSFIVHRSKAYRRGRALVEKLKELIPRQQFEVPIQAAIGGKIIARETIKALRKDVTAKCYGGDISRKKKLLE 80
|
90 100
....*....|....*....|....*..
gi 27370038 620 RQSEGKKKLRKIGNIEIPKDAFIKVLK 646
Cdd:pfam06421 81 KQKEGKKRMKQIGNVEIPQEAFLAVLK 107
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
48-330 |
1.11e-56 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 202.17 E-value: 1.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 48 EDIRNFSIIAHVDHGKSTLADRLLELTGTIDKtkkNKQV----LDKLQVERERGITVKAQTASLFYsfggKQYLLNLIDT 123
Cdd:COG1217 4 EDIRNIAIIAHVDHGKTTLVDALLKQSGTFRE---NQEVaervMDSNDLERERGITILAKNTAVRY----KGVKINIVDT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 124 PGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTvaNFFL--AFEAQLSVIPVINKIDLKNADPERVgkqIEKVFDI--- 198
Cdd:COG1217 77 PGHADFGGEVERVLSMVDGVLLLVDAFEGPMPQT--RFVLkkALELGLKPIVVINKIDRPDARPDEV---VDEVFDLfie 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 199 --PSEE-----CIKISAKLG----------TNVDSVLQAVIERIPPPKVHRENPLKALVFDSTFDQYRGVIANIALFDGV 261
Cdd:COG1217 152 lgATDEqldfpVVYASARNGwasldlddpgEDLTPLFDTILEHVPAPEVDPDGPLQMLVTNLDYSDYVGRIAIGRIFRGT 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27370038 262 VSKGDKIVSAH---TKKAYEVNEV-GILNPNEQPTHKLYAGQVgFLIAGMKDVTeaqIGDTLYLHNHPvEPLP 330
Cdd:COG1217 232 IKKGQQVALIKrdgKVEKGKITKLfGFEGLERVEVEEAEAGDI-VAIAGIEDIN---IGDTICDPENP-EALP 299
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
50-499 |
6.53e-56 |
|
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: 199.84 E-value: 6.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 50 IRNFSIIAHVDHGKSTLADRLLELTGTI-DKTKKNKQVLDKLQVERERGITVKAQTASLFYsfggKQYLLNLIDTPGHVD 128
Cdd:TIGR01394 1 IRNIAIIAHVDHGKTTLVDALLKQSGTFrANEAVAERVMDSNDLERERGITILAKNTAIRY----NGTKINIVDTPGHAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 129 FSYEVSRSLSACQGVLLVVDANEGIQAQTvaNFFL--AFEAQLSVIPVINKIDLKNADPERVgkqIEKVFDI------PS 200
Cdd:TIGR01394 77 FGGEVERVLGMVDGVLLLVDASEGPMPQT--RFVLkkALELGLKPIVVINKIDRPSARPDEV---VDEVFDLfaelgaDD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 201 EEC----IKISAKLGT----------NVDSVLQAVIERIPPPKVHRENPLKALVFDSTFDQYRGVIANIALFDGVVSKGD 266
Cdd:TIGR01394 152 EQLdfpiVYASGRAGWasldlddpsdNMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVHRGTVKKGQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 267 KIVSAH---TKKAYEVNEV-GILNPNEQPTHKLYAGQVgFLIAGMKDvteAQIGDTLYLHNHPvEPLPGFKSAKP---MV 339
Cdd:TIGR01394 232 QVALMKrdgTIENGRISKLlGFEGLERVEIDEAGAGDI-VAVAGLED---INIGETIADPEVP-EALPTITVDEPtlsMT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 340 FagvypidqseynnlksaieklTLNDSSVtvhrdsslalgAGWRLGFLGLLHMevfNQRLEQEYNASVIL-TTPT----- 413
Cdd:TIGR01394 307 F---------------------SVNDSPL-----------AGKEGKKVTSRHI---RDRLMRELETNVALrVEDTesadk 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 414 --VPYKAVLSSAKLIKEYKEK--EITIINPaQFPEKSQVTEYLEPVVLGTVITPTEYTGKIMALCQARRAIQKNMTFIDE 489
Cdd:TIGR01394 352 feVSGRGELHLSILIETMRREgfELQVGRP-QVIYKEIDGKKLEPIEELTIDVPEEHVGAVIEKLGKRKGEMVDMEPSGN 430
|
490
....*....|
gi 27370038 490 NRVMLKYLFP 499
Cdd:TIGR01394 431 GRTRLEFKIP 440
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
42-529 |
8.35e-50 |
|
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: 184.48 E-value: 8.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 42 MSRFPVEDIRNFSIIAHVDHGKSTLADRLLELTGTIDK---TKKNKQVLDKLQVERERGITVKAQTASLFYsfggKQYLL 118
Cdd:COG0480 1 MAEYPLEKIRNIGIVAHIDAGKTTLTERILFYTGAIHRigeVHDGNTVMDWMPEEQERGITITSAATTCEW----KGHKI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 119 NLIDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADPERVGKQIEKVF-- 196
Cdd:COG0480 77 NIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQLKERLga 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 197 ----------------------------------------DIPSEE---------------------------------- 202
Cdd:COG0480 157 npvplqlpigaeddfkgvidlvtmkayvyddelgakyeeeEIPAELkeeaeeareelieavaetddelmekylegeelte 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 203 -----CIKI-------------SAKLGTNVDSVLQAVIERIPPP---------------KVHR----ENPLKALVFDSTF 245
Cdd:COG0480 237 eeikaGLRKatlagkivpvlcgSAFKNKGVQPLLDAVVDYLPSPldvpaikgvdpdtgeEVERkpddDEPFSALVFKTMT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 246 DQYRGVIANIALFDGVVSKGDKIVSAHTKKAYEVNEVGILNPNEQ-PTHKLYAGQVGfLIAGMKDVTeaqIGDTLYLHNH 324
Cdd:COG0480 317 DPFVGKLSFFRVYSGTLKSGSTVYNSTKGKKERIGRLLRMHGNKReEVDEAGAGDIV-AVVKLKDTT---TGDTLCDEDH 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 325 PVEpLPGFKSAKPMVFAGVYPIDQSEYNNLKSAIEKLTLNDSSVTVHRDSSLA--LGAGwrlgfLGLLHMEVFNQRLEQE 402
Cdd:COG0480 393 PIV-LEPIEFPEPVISVAIEPKTKADEDKLSTALAKLAEEDPTFRVETDEETGqtIISG-----MGELHLEIIVDRLKRE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 403 YNASVILTTPTVPY-----KAVLSSAKLIKE------Y-----------KEKEITIIN-------PAQF-P--EKS---- 446
Cdd:COG0480 467 FGVEVNVGKPQVAYretirKKAEAEGKHKKQsgghgqYgdvwieieplpRGEGFEFVDkivggviPKEYiPavEKGirea 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 447 --------------QVTEY---------------------------------LEPVVLGTVITPTEYTGKIMALCQARRA 479
Cdd:COG0480 547 mekgvlagypvvdvKVTLYdgsyhpvdssemafkiaasmafkeaakkakpvlLEPIMKVEVTVPEEYMGDVMGDLNSRRG 626
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 27370038 480 IQKNMTFIDENRVmLKYLFPLNEIvVDFYDSLKSLSSGYASFDYEDAGYQ 529
Cdd:COG0480 627 RILGMESRGGAQV-IKAEVPLAEM-FGYATDLRSLTQGRGSFTMEFSHYE 674
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
52-228 |
5.00e-48 |
|
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: 166.70 E-value: 5.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 52 NFSIIAHVDHGKSTLADRLLELTGTIDKTKKNKQ-VLDKLQVERERGITVKAQTASLFYsfggKQYLLNLIDTPGHVDFS 130
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKEtFLDTLKEERERGITIKTGVVEFEW----PKRRINFIDTPGHEDFS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 131 YEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDL-KNADPERVGKQIEKVFDIPSEECIK---- 205
Cdd:cd00881 77 KETVRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRvGEEDFDEVLREIKELLKLIGFTFLKgkdv 156
|
170 180
....*....|....*....|....*..
gi 27370038 206 ----ISAKLGTNVDSVLQAVIERIPPP 228
Cdd:cd00881 157 piipISALTGEGIEELLDAIVEHLPPP 183
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
43-531 |
9.11e-47 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 175.91 E-value: 9.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 43 SRFPVEDIRNFSIIAHVDHGKSTLADRLLELTGTIDK---TKKNKQVLDKLQVERERGITVKAQTASLFYsfggKQYLLN 119
Cdd:PRK13351 1 AEMPLMQIRNIGILAHIDAGKTTLTERILFYTGKIHKmgeVEDGTTVTDWMPQEQERGITIESAATSCDW----DNHRIN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 120 LIDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADPERVGKQIEKVF--- 196
Cdd:PRK13351 77 LIDTPGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLFKVLEDIEERFgkr 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 197 ------------------DIPSEECIKI---------------------------------------------------- 206
Cdd:PRK13351 157 plplqlpigsedgfegvvDLITEPELHFsegdggstveegpipeelleeveearekliealaefddellelylegeelsa 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 207 ----------------------SAKLGTNVDSVLQAVIE------RIPPPKVHREN------------PLKALVFDSTFD 246
Cdd:PRK13351 237 eqlraplregtrsghlvpvlfgSALKNIGIEPLLDAVVDylpsplEVPPPRGSKDNgkpvkvdpdpekPLLALVFKVQYD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 247 QYRGVIANIALFDGVVSKGDKIVSAHTKKAYEVNEVGILNPNEQPThkLYAGQVGFLIAGMKdVTEAQIGDTLYLHNHPV 326
Cdd:PRK13351 317 PYAGKLTYLRVYSGTLRAGSQLYNGTGGKREKVGRLFRLQGNKREE--VDRAKAGDIVAVAG-LKELETGDTLHDSADPV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 327 EpLPGFKSAKPMVFAGVYPIDQSEYNNLKSAIEKLTLNDSSVTVHRDS----SLALGagwrlgfLGLLHMEVFNQRLEQE 402
Cdd:PRK13351 394 L-LELLTFPEPVVSLAVEPERRGDEQKLAEALEKLVWEDPSLRVEEDEetgqTILSG-------MGELHLEVALERLRRE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 403 YNASVILTTPTVPYKAVLSSA------------------------------------------KLIKEYK---EK----- 432
Cdd:PRK13351 466 FKLEVNTGKPQVAYRETIRKMaegvyrhkkqfggkgqfgevhlrveplergagfifvskvvggAIPEELIpavEKgirea 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 433 --------------EITIINPAQFPEKSQVT-------------------EYLEPVVLGTVITPTEYTGKIMALCQARRA 479
Cdd:PRK13351 546 lasgplagypvtdlRVTVLDGKYHPVDSSESafkaaarkafleafrkanpVLLEPIMELEITVPTEHVGDVLGDLSQRRG 625
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 27370038 480 IQKNMTFIDENRVMLKYLFPLNEiVVDFYDSLKSLSSGYASFDYEDAGYQTA 531
Cdd:PRK13351 626 RIEGTEPRGDGEVLVKAEAPLAE-LFGYATRLRSMTKGRGSFTMEFSHFDPV 676
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
49-228 |
1.02e-46 |
|
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: 1.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 49 DIRNFSIIAHVDHGKSTLADRLLELTGTI-DKTKKNKQVLDKLQVERERGITVKAQTASLFYsfggKQYLLNLIDTPGHV 127
Cdd:cd01891 1 KIRNIAIIAHVDHGKTTLVDALLKQSGTFrENEEVGERVMDSNDLERERGITILAKNTAITY----KDTKINIIDTPGHA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 128 DFSYEVSRSLSACQGVLLVVDANEGIQAQTvaNFFL--AFEAQLSVIPVINKIDLKNADPERVgkqIEKVFDI------P 199
Cdd:cd01891 77 DFGGEVERVLSMVDGVLLLVDASEGPMPQT--RFVLkkALEAGLKPIVVINKIDRPDARPEEV---VDEVFDLflelnaT 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27370038 200 SEEC----IKISAKLG----------TNVDSVLQAVIERIPPP 228
Cdd:cd01891 152 DEQLdfpiVYASAKNGwaslnlddpsEDLDPLFETIIEHVPAP 194
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
51-228 |
3.49e-46 |
|
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: 162.79 E-value: 3.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 51 RNFSIIAHVDHGKSTLADRLLELTGTIDKTKKNKQ-VLDKLQVERERGITVKAQTASLFY-----SFGGKQYLLNLIDTP 124
Cdd:cd01885 1 RNICIIAHVDHGKTTLSDSLLASAGIISEKLAGKArYLDTREDEQERGITIKSSAISLYFeyeeeKMDGNDYLINLIDSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 125 GHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDL----KNADPE----RVGKQIEKVF 196
Cdd:cd01885 81 GHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDRlileLKLSPEeayqRLLRIVEDVN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27370038 197 DI----PSEECIKI--------------SAKLG--------TNVDSVLQAVIERIPPP 228
Cdd:cd01885 161 AIietyAPEEFKQEkwkfspqkgnvafgSALDGwgftiikfADIYAVLEMVVKHLPSP 218
|
|
| lepA_C |
cd03709 |
lepA_C: This family represents the C-terminal region of LepA, a GTP-binding protein localized ... |
453-532 |
1.74e-44 |
|
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: 153.03 E-value: 1.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 453 EPVVLGTVITPTEYTGKIMALCQARRAIQKNMTFIDENRVMLKYLFPLNEIVVDFYDSLKSLSSGYASFDYEDAGYQTAE 532
Cdd:cd03709 1 EPFVKATIITPSEYLGAIMELCQERRGVQKDMEYLDANRVMLTYELPLAEIVYDFFDKLKSISKGYASLDYELIGYRESD 80
|
|
| EF4_III |
cd16260 |
Domain III of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly ... |
337-412 |
2.72e-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: 152.65 E-value: 2.72e-44
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27370038 337 PMVFAGVYPIDQSEYNNLKSAIEKLTLNDSSVTVHRDSSLALGAGWRLGFLGLLHMEVFNQRLEQEYNASVILTTP 412
Cdd:cd16260 1 PMVFAGLYPVDGSDYEELRDALEKLTLNDASVTFEPETSSALGFGFRCGFLGLLHMEVFQERLEREYGLDLIITAP 76
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
56-529 |
1.18e-43 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 166.45 E-value: 1.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 56 IAHVDHGKSTLADRLLELTGTIDK----TKKNKqVLDKLQVERERGITVkaQTASLFYSFGGKQylLNLIDTPGHVDFSY 131
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRigevEDGTT-TMDFMPEERERGISI--TSAATTCEWKGHK--INLIDTPGHVDFTG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 132 EVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADPERVGKQIEKVF--------------- 196
Cdd:PRK12740 76 EVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRAGADFFRVLAQLQEKLgapvvplqlpigegd 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 197 -------------------------DIPSE---------------------------------------ECIKI------ 206
Cdd:PRK12740 156 dftgvvdllsmkayrydeggpseeiEIPAElldraeeareellealaefddelmekylegeelseeeikAGLRKatlage 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 207 -------SAKLGTNVDSVLQAVIERIPPP----KVHREN-------------PLKALVFDSTFDQYRGVIANIALFDGVV 262
Cdd:PRK12740 236 ivpvfcgSALKNKGVQRLLDAVVDYLPSPlevpPVDGEDgeegaelapdpdgPLVALVFKTMDDPFVGKLSLVRVYSGTL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 263 SKGDKIVSAHTKKAYEVNEVGILNPNEQ-PTHKLYAGQVGfLIAGMKDvteAQIGDTLYLHNHPVePLPGFKSAKPMVFA 341
Cdd:PRK12740 316 KKGDTLYNSGTGKKERVGRLYRMHGKQReEVDEAVAGDIV-AVAKLKD---AATGDTLCDKGDPI-LLEPMEFPEPVISL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 342 GVYPIDQSEYNNLKSAIEKLTLNDSSVTVHRDSSLA---LGAgwrlgfLGLLHMEVFNQRLEQEYNASVILTTPTVPY-- 416
Cdd:PRK12740 391 AIEPKDKGDEEKLSEALGKLAEEDPTLRVERDEETGqtiLSG------MGELHLDVALERLKREYGVEVETGPPQVPYre 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 417 ---KAVLSSAKLIKE------YKEKEITI-----------IN-------PAQF-P--EKS------------------QV 448
Cdd:PRK12740 465 tirKKAEGHGRHKKQsgghgqFGDVWLEVeplprgegfefVDkvvggavPRQYiPavEKGvrealekgvlagypvvdvKV 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 449 TEY---------------------------------LEPVVLGTVITPTEYTGKIMALCQARRAIQKNMTfIDENRVMLK 495
Cdd:PRK12740 545 TLTdgsyhsvdssemafkiaarlafrealpkakpvlLEPIMKVEVSVPEEFVGDVIGDLSSRRGRILGME-SRGGGDVVR 623
|
650 660 670
....*....|....*....|....*....|....
gi 27370038 496 YLFPLNEIvVDFYDSLKSLSSGYASFDYEDAGYQ 529
Cdd:PRK12740 624 AEVPLAEM-FGYATDLRSLTQGRGSFSMEFSHYE 656
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
47-417 |
2.39e-42 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 163.50 E-value: 2.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 47 VEDIRNFSIIAHVDHGKSTLADRLLELTGTIDKTKKNKQ-VLDKLQVERERGITVKAQTASLFYSFGGKQYLLNLIDTPG 125
Cdd:PRK07560 17 PEQIRNIGIIAHIDHGKTTLSDNLLAGAGMISEELAGEQlALDFDEEEQARGITIKAANVSMVHEYEGKEYLINLIDTPG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 126 HVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQlsVIPV--INKID-----LKnADPERVGKQIEKVFD- 197
Cdd:PRK07560 97 HVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRER--VKPVlfINKVDrlikeLK-LTPQEMQQRLLKIIKd 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 198 ----I----PSE--ECIKISAKLGT------------NVDS--------------------------------VLQAVIE 223
Cdd:PRK07560 174 vnklIkgmaPEEfkEKWKVDVEDGTvafgsalynwaiSVPMmqktgikfkdiidyyekgkqkelaekaplhevVLDMVVK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 224 RIPPPKV---HR----------------------ENPLKALVFDSTFDQYRGVIANIALFDGVVSKGDKIVSAHTKKAYE 278
Cdd:PRK07560 254 HLPNPIEaqkYRipkiwkgdlnsevgkamlncdpNGPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLVGAKKKNR 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 279 VNEVGI-LNPNEQPTHKLYAGQvgflIAGMKDVTEAQIGDTLYlhnhPVEPLPGFKSAK----PMVFAGVYPIDQSEYNN 353
Cdd:PRK07560 334 VQQVGIyMGPEREEVEEIPAGN----IAAVTGLKDARAGETVV----SVEDMTPFESLKhisePVVTVAIEAKNPKDLPK 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27370038 354 LKSAIEKLTLNDSS--VTVHRDSSLALGAGwrlgfLGLLHMEVFNQRLEQEYNASVILTTPTVPYK 417
Cdd:PRK07560 406 LIEVLRQLAKEDPTlvVKINEETGEHLLSG-----MGELHLEVITYRIKRDYGIEVVTSEPIVVYR 466
|
|
| EF4_II |
cd03699 |
Domain II of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly ... |
236-321 |
7.76e-42 |
|
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: 146.02 E-value: 7.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 236 LKALVFDSTFDQYRGVIANIALFDGVVSKGDKIVSAHTKKAYEVNEVGILNPNEQPTHKLYAGQVGFLIAGMKDVTEAQI 315
Cdd:cd03699 1 LRALIFDSWYDPYRGVVVLVRVFDGTLKKGDKIRFMATGKEYEVLEVGVFTPKMVPTDELSAGEVGYIIAGIKSVKDARV 80
|
....*.
gi 27370038 316 GDTLYL 321
Cdd:cd03699 81 GDTITL 86
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
47-525 |
1.91e-37 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 147.55 E-value: 1.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 47 VEDIRNFSIIAHVDHGKSTLADRLLELTGTID-KTKKNKQVLDKLQVERERGITVKAQTASLFYSfggkQYLLNLIDTPG 125
Cdd:PRK10218 2 IEKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDsRAETQERVMDSNDLEKERGITILAKNTAIKWN----DYRINIVDTPG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 126 HVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADPERVGKQIEKVF---DIPSEE 202
Cdd:PRK10218 78 HADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLFvnlDATDEQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 203 ----CIKISA----------KLGTNVDSVLQAVIERIPPPKVHRENPLKALVFDSTFDQYRGVIANIALFDGVVSKGDKI 268
Cdd:PRK10218 158 ldfpIVYASAlngiagldheDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 269 VSAHTKKAYEVNEVGILNPN---EQPTHKLyaGQVGFLIAgMKDVTEAQIGDTLyLHNHPVEPLPGFKSAKPMV------ 339
Cdd:PRK10218 238 TIIDSEGKTRNAKVGKVLGHlglERIETDL--AEAGDIVA-ITGLGELNISDTV-CDTQNVEALPALSVDEPTVsmffcv 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 340 ----FAGvypiDQSEYNNLKSAIEKLTLNDSSVTVHRDSSLALGAGWRLGFLGLLHMEVFNQRLEQEyNASVILTTPTVP 415
Cdd:PRK10218 314 ntspFCG----KEGKFVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRRE-GFELAVSRPKVI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 416 YKAVLSSAKlikeykekeitiinpaqfpeksqvteylEPVVLGTVITPTEYTGKIMALCQARRAIQKNMTFIDENRVMLK 495
Cdd:PRK10218 389 FREIDGRKQ----------------------------EPYENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLD 440
|
490 500 510
....*....|....*....|....*....|....
gi 27370038 496 YLFPlNEIVVDFYDSLKSLSSG----YASFDYED 525
Cdd:PRK10218 441 YVIP-SRGLIGFRSEFMTMTSGtgllYSTFSHYD 473
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
35-430 |
5.33e-37 |
|
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: 147.35 E-value: 5.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 35 ELKEKPDMsrfpvedIRNFSIIAHVDHGKSTLADRLLELTGTIDKTKKNKQV-LDKLQVERERGITVKAQTASLFYSFGG 113
Cdd:TIGR00490 11 ELMWKPKF-------IRNIGIVAHIDHGKTTLSDNLLAGAGMISEELAGQQLyLDFDEQEQERGITINAANVSMVHEYEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 114 KQYLLNLIDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKID-------------- 179
Cdd:TIGR00490 84 NEYLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKPVLFINKVDrlinelkltpqelq 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 180 -------------LKNADPE--------------------------------RVGKQIEKVFDIPSEECIKISAKLGTNV 214
Cdd:TIGR00490 164 erfikiitevnklIKAMAPEefrdkwkvrvedgsvafgsayynwaisvpsmkKTGIGFKDIYKYCKEDKQKELAKKSPLH 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 215 DSVLQAVIERIPPP-------------------------KVHRENPLKALVFDSTFDQYRGVIANIALFDGVVSKGDKIV 269
Cdd:TIGR00490 244 QVVLDMVIRHLPSPieaqkyripviwkgdlnsevgkamlNCDPKGPLALMITKIVVDKHAGEVAVGRLYSGTIRPGMEVY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 270 SAHTKKAYEVNEVGI-LNPNEQPTHKLYAGQVGFLIaGMKDvteAQIGDTLYLHNHPVEPLPGFKS-AKPMVFAGVYPID 347
Cdd:TIGR00490 324 IVDRKAKARIQQVGVyMGPERVEVDEIPAGNIVAVI-GLKD---AVAGETICTTVENITPFESIKHiSEPVVTVAIEAKN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 348 QSEYNNLKSAIEKLTLNDSS--VTVHRDSSLALGAGwrlgfLGLLHMEVFNQRLEQEYNASVILTTPTVPYKAVLSSAKL 425
Cdd:TIGR00490 400 TKDLPKLIEVLRQVAKEDPTvhVEINEETGEHLISG-----MGELHLEIIVEKIREDYGLDVETSPPIVVYRETVTGTSP 474
|
....*
gi 27370038 426 IKEYK 430
Cdd:TIGR00490 475 VVEGK 479
|
|
| EF-G |
TIGR00484 |
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ... |
42-433 |
8.15e-37 |
|
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: 146.49 E-value: 8.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 42 MSR-FPVEDIRNFSIIAHVDHGKSTLADRLLELTGTIDK---TKKNKQVLDKLQVERERGITVKAQTASLFYsfggKQYL 117
Cdd:TIGR00484 1 MARtTDLNRFRNIGISAHIDAGKTTTTERILFYTGRIHKigeVHDGAATMDWMEQEKERGITITSAATTVFW----KGHR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 118 LNLIDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADPERVGKQI----- 192
Cdd:TIGR00484 77 INIIDTPGHVDFTVEVERSLRVLDGAVAVLDAVGGVQPQSETVWRQANRYEVPRIAFVNKMDKTGANFLRVVNQIkqrlg 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 193 ------------------------EKVF-------------DIPS----------------------------------- 200
Cdd:TIGR00484 157 anavpiqlpigaednfigvidlveMKAYffngdkgtkaiekEIPSdlleqakelrenlveavaefdeelmekylegeelt 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 201 EECIKISAKLGT-----------------NVDSVLQAVIERIPPP-------------------KVHRENPLKALVFDST 244
Cdd:TIGR00484 237 IEEIKNAIRKGVlnceffpvlcgsafknkGVQLLLDAVVDYLPSPtdvpaikgidpdtekeierKASDDEPFSALAFKVA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 245 FDQYRGVIANIALFDGVVSKGDKIVSAHTKKAYEVNEVGILNPNEQPTHK-LYAGQVGFLIaGMKDVTEaqiGDTLYLHN 323
Cdd:TIGR00484 317 TDPFVGQLTFVRVYSGVLKSGSYVKNSRKNKKERVGRLVKMHANNREEIKeVRAGDICAAI-GLKDTTT---GDTLCDPK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 324 HPVEpLPGFKSAKPMVFAGVYPIDQSEYNNLKSAIEKLTLNDSSVTVHRD--SSLALGAGwrlgfLGLLHMEVFNQRLEQ 401
Cdd:TIGR00484 393 IDVI-LERMEFPEPVISLAVEPKTKADQEKMGIALGKLAEEDPTFRTFTDpeTGQTIIAG-----MGELHLDIIVDRMKR 466
|
490 500 510
....*....|....*....|....*....|..
gi 27370038 402 EYNASVILTTPTVPYKAVLSSaKLIKEYKEKE 433
Cdd:TIGR00484 467 EFKVEANVGAPQVAYRETIRS-KVEVEGKHAK 497
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
52-194 |
5.40e-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: 132.36 E-value: 5.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 52 NFSIIAHVDHGKSTLADRLLELTGTIDKT----KKNKQvLDKLQVERERGITVKAQTASLFYsfggKQYLLNLIDTPGHV 127
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIRELgsvdKGTTR-TDSMELERQRGITIFSAVASFQW----EDTKVNIIDTPGHM 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27370038 128 DFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADPERVGKQIEK 194
Cdd:cd04168 76 DFIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTIIFVNKIDRAGADLEKVYQEIKE 142
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
48-195 |
7.07e-32 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 132.09 E-value: 7.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 48 EDIRNFSIIAHVDHGKSTLADRLLELTGTI-DKTKKNKQVLDKLQVERERGITVKAQTASLFYSF------GGKQYLLNL 120
Cdd:PTZ00416 17 DQIRNMSVIAHVDHGKSTLTDSLVCKAGIIsSKNAGDARFTDTRADEQERGITIKSTGISLYYEHdledgdDKQPFLINL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 121 IDTPGHVDFSYEVSRSLSACQGVLLVVDANEG--IQAQTVanffLAFEAQLSVIPV--INKID-----LKNaDPE----R 187
Cdd:PTZ00416 97 IDSPGHVDFSSEVTAALRVTDGALVVVDCVEGvcVQTETV----LRQALQERIRPVlfINKVDraileLQL-DPEeiyqN 171
|
....*...
gi 27370038 188 VGKQIEKV 195
Cdd:PTZ00416 172 FVKTIENV 179
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
52-198 |
1.36e-31 |
|
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling phases of protein synthesis; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains both eukaryotic and bacterial members.
Pssm-ID: 206673 [Multi-domain] Cd Length: 270 Bit Score: 123.76 E-value: 1.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 52 NFSIIAHVDHGKSTLADRLLELTGTIDK---TKKNKQVLDKLQVERERGITVKAQTASLFYsfggKQYLLNLIDTPGHVD 128
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGRIHKigeVHGGGATMDWMEQERERGITIQSAATTCFW----KDHRINIIDTPGHVD 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 129 FSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADPERVGKQIEKVFDI 198
Cdd:cd01886 77 FTIEVERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQIREKLGA 146
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
51-179 |
1.13e-30 |
|
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: 119.68 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 51 RNFSIIAHVDHGKSTLADRLLELTGTIDKTKKNKQV----LDKLQVERERGITVKAQTASLFYSFG-GKQYLLNLIDTPG 125
Cdd:cd04167 1 RNVCIAGHLHHGKTSLLDMLIEQTHKRTPSVKLGWKplryTDTRKDEQERGISIKSNPISLVLEDSkGKSYLINIIDTPG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 27370038 126 HVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKID 179
Cdd:cd04167 81 HVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKID 134
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
42-179 |
3.39e-30 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 126.76 E-value: 3.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 42 MSRFPVED----------IRNFSIIAHVDHGKSTLADRLLELTGTID-KTKKNKQVLDKLQVERERGITVKAQTASLFYS 110
Cdd:PLN00116 1 MVKFTAEElrrimdkkhnIRNMSVIAHVDHGKSTLTDSLVAAAGIIAqEVAGDVRMTDTRADEAERGITIKSTGISLYYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 111 FG------------GKQYLLNLIDTPGHVDFSYEVSRSLSACQGVLLVVDANEG--IQAQTVANFFLAFEaqlsVIPV-- 174
Cdd:PLN00116 81 MTdeslkdfkgerdGNEYLINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGvcVQTETVLRQALGER----IRPVlt 156
|
....*
gi 27370038 175 INKID 179
Cdd:PLN00116 157 VNKMD 161
|
|
| EFG_C |
pfam00679 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
450-538 |
3.63e-27 |
|
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: 105.32 E-value: 3.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 450 EYLEPVVLGTVITPTEYTGKIMALCQARRAIQKNMTFIDENRVMLKYLFPLNEIvVDFYDSLKSLSSGYASFDYEDAGYQ 529
Cdd:pfam00679 1 VLLEPIEKVTIDVPEEYVGDVISDLNSRRGEILDMDPDDGGRVVIEAEVPLAEL-FGFATELRSLTKGRGSFSMEFSGYQ 79
|
....*....
gi 27370038 530 TAELVKMDI 538
Cdd:pfam00679 80 PVPGDILDR 88
|
|
| Elongation_Factor_C |
cd01514 |
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ... |
453-531 |
5.42e-26 |
|
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: 101.40 E-value: 5.42e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27370038 453 EPVVLGTVITPTEYTGKIMALCQARRAIQKNMTFIDENRVMLKYLFPLNEIvVDFYDSLKSLSSGYASFDYEDAGYQTA 531
Cdd:cd01514 1 EPIMKVEITVPEEYLGAVIGDLSKRRGEILGMEPRGTGRVVIKAELPLAEM-FGFATDLRSLTQGRASFSMEFSHYEPV 78
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
51-198 |
1.82e-24 |
|
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: 103.44 E-value: 1.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 51 RNFSIIAHVDHGKSTLADRLLELTGTID-----KTKKNKQ--VLDKLQVERERGITVkaqTASLFySFGGKQYLLNLIDT 123
Cdd:cd04169 3 RTFAIISHPDAGKTTLTEKLLLFGGAIQeagavKARKSRKhaTSDWMEIEKQRGISV---TSSVM-QFEYKGCVINLLDT 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27370038 124 PGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADPERVGKQIEKVFDI 198
Cdd:cd04169 79 PGHEDFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDREGRDPLELLDEIENELGI 153
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
55-223 |
3.23e-24 |
|
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: 99.47 E-value: 3.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 55 IIAHVDHGKSTLadrlleltgtidktkknkqvLDKLQ----VERE-RGIT--VKAQTASLFYSFGGkqylLNLIDTPGHV 127
Cdd:cd01887 5 VMGHVDHGKTTL--------------------LDKIRktnvAAGEaGGITqhIGAYQVPIDVKIPG----ITFIDTPGHE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 128 DFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDL---KNADPERVGKQIEKvFDIPSEE-- 202
Cdd:cd01887 61 AFTNMRARGASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKpygTEADPERVKNELSE-LGLVGEEwg 139
|
170 180
....*....|....*....|....*
gi 27370038 203 ----CIKISAKLGTNVDSVLQAVIE 223
Cdd:cd01887 140 gdvsIVPISAKTGEGIDDLLEAILL 164
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
37-214 |
6.34e-24 |
|
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: 105.02 E-value: 6.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 37 KEKPDMsrfpvedirNFSIIAHVDHGKSTLADRLLELTGTIDKT----------KKNKQ------VLDKLQVERERGITV 100
Cdd:COG5256 3 SEKPHL---------NLVVIGHVDHGKSTLVGRLLYETGAIDEHiiekyeeeaeKKGKEsfkfawVMDRLKEERERGVTI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 101 KAQtaslFYSFGGKQYLLNLIDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFE---AQLSVipVINK 177
Cdd:COG5256 74 DLA----HKKFETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTlgiNQLIV--AVNK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27370038 178 IDLKNADPER---VGKQIEKV-----FDIPSEECIKISAKLGTNV 214
Cdd:COG5256 148 MDAVNYSEKRyeeVKEEVSKLlkmvgYKVDKIPFIPVSAWKGDNV 192
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
54-273 |
5.07e-23 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 104.14 E-value: 5.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 54 SIIAHVDHGKSTLADRlleltgtIDKTK-KNKQVldklqvereRGITVKAQTASLFYSFGGKQYLLNLIDTPGHVDFSYE 132
Cdd:CHL00189 248 TILGHVDHGKTTLLDK-------IRKTQiAQKEA---------GGITQKIGAYEVEFEYKDENQKIVFLDTPGHEAFSSM 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 133 VSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADPERVGKQIEKVFDIPSE-----ECIKIS 207
Cdd:CHL00189 312 RSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANTERIKQQLAKYNLIPEKwggdtPMIPIS 391
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27370038 208 AKLGTNVDSVLQAVIER--IPPPKVHRENPLKALVFDSTFDQYRGVIANIALFDGVVSKGDKIVSAHT 273
Cdd:CHL00189 392 ASQGTNIDKLLETILLLaeIEDLKADPTQLAQGIILEAHLDKTKGPVATILVQNGTLHIGDIIVIGTS 459
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
52-214 |
6.81e-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: 6.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 52 NFSIIAHVDHGKSTLADRLLELTGTI--DK-------TKKNKQ--------VLDKLQVERERGITVkaQTASLFYSFGGK 114
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSIfeDQlaalersKSSGTQgekldlalLVDGLQAEREQGITI--DVAYRYFSTPKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 115 QYLlnLIDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAfeAQLS---VIPVINKIDLKNADPERVgKQ 191
Cdd:cd04166 79 KFI--IADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIA--SLLGirhVVVAVNKMDLVDYDEEVF-EE 153
|
170 180 190
....*....|....*....|....*....|
gi 27370038 192 IEKVF-------DIPSEECIKISAKLGTNV 214
Cdd:cd04166 154 IKADYlafaaslGIEDITFIPISALEGDNV 183
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
32-269 |
8.14e-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: 8.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 32 SAAELKEKPdmsrfPVedirnFSIIAHVDHGKSTLADrlleltgTIDKTKKNK-------QVLDKLQVERERGITVkaqt 104
Cdd:TIGR00487 79 SGDLLVERP-----PV-----VTIMGHVDHGKTSLLD-------SIRKTKVAQgeaggitQHIGAYHVENEDGKMI---- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 105 aslfySFggkqyllnlIDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNAD 184
Cdd:TIGR00487 138 -----TF---------LDTPGHEAFTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVPIIVAINKIDKPEAN 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 185 PERVGKQIEKvFDIPSEE------CIKISAKLGTNVDSVLQAVI--ERIPPPKVHRENPLKALVFDSTFDQYRGVIANIA 256
Cdd:TIGR00487 204 PDRVKQELSE-YGLVPEDwggdtiFVPVSALTGDGIDELLDMILlqSEVEELKANPNGQASGVVIEAQLDKGRGPVATVL 282
|
250
....*....|...
gi 27370038 257 LFDGVVSKGDKIV 269
Cdd:TIGR00487 283 VQSGTLRVGDIVV 295
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
37-214 |
1.95e-22 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 100.39 E-value: 1.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 37 KEKPDMsrfpvedirNFSIIAHVDHGKSTLADRLLELTGTIDK----------TKKNKQ------VLDKLQVERERGITV 100
Cdd:PRK12317 2 KEKPHL---------NLAVIGHVDHGKSTLVGRLLYETGAIDEhiieelreeaKEKGKEsfkfawVMDRLKEERERGVTI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 101 KAQtaslFYSFGGKQYLLNLIDTPGHVDFSYEVSRSLSACQGVLLVVDANE--GIQAQTVANFFLAFE---AQLSVipVI 175
Cdd:PRK12317 73 DLA----HKKFETDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTlgiNQLIV--AI 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27370038 176 NKIDLKNADPER---VGKQIEKV-----FDIPSEECIKISAKLGTNV 214
Cdd:PRK12317 147 NKMDAVNYDEKRyeeVKEEVSKLlkmvgYKPDDIPFIPVSAFEGDNV 193
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
52-199 |
6.51e-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: 95.74 E-value: 6.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 52 NFSIIAHVDHGKSTLADRLLELTGTIDK---TKKNKQVLDKLQVERERGITVkaQTASLFYSFGGKQylLNLIDTPGHVD 128
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRlgrVEDGNTVSDYDPEEKKRKMSI--ETSVAPLEWNGHK--INLIDTPGYAD 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27370038 129 FSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADPERVGKQIEKVFDIP 199
Cdd:cd04170 77 FVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRARADFDKTLAALREAFGRP 147
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
55-269 |
1.67e-19 |
|
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: 91.30 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 55 IIA-HVDHGKSTLADRLLELTGTI----------DKTKKNKQ------VLDKLQVERERGITVkaQTASLFYSFGGKQYL 117
Cdd:COG2895 21 ITCgSVDDGKSTLIGRLLYDTKSIfedqlaalerDSKKRGTQeidlalLTDGLQAEREQGITI--DVAYRYFSTPKRKFI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 118 lnLIDTPGHVDFsyevSRSL----SACQGVLLVVDANEGIQAQTVANFFLAfeAQL---SVIPVINKIDLKNADPERVgK 190
Cdd:COG2895 99 --IADTPGHEQY----TRNMvtgaSTADLAILLIDARKGVLEQTRRHSYIA--SLLgirHVVVAVNKMDLVDYSEEVF-E 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 191 QIEKVF-------DIPSEECIKISAKLGTNV------------DSVLQAvIERIPPPKVHRENPLKALV-----FDstfD 246
Cdd:COG2895 170 EIVADYrafaaklGLEDITFIPISALKGDNVversenmpwydgPTLLEH-LETVEVAEDRNDAPFRFPVqyvnrPN---L 245
|
250 260
....*....|....*....|...
gi 27370038 247 QYRGVIANIAlfDGVVSKGDKIV 269
Cdd:COG2895 246 DFRGYAGTIA--SGTVRVGDEVV 266
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
52-214 |
1.78e-18 |
|
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: 84.46 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 52 NFSIIAHVDHGKSTLADRLLELTGTIDKT----------KKNKQ------VLDKLQVERERGITVKAQTAslfySFGGKQ 115
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRtiekyekeakEMGKEsfkyawVLDKLKEERERGVTIDVGLA----KFETEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 116 YLLNLIDTPGHVDFsyeVSRSLS-ACQG--VLLVVDANEG-------IQAQTVANFFLAFEAQLS-VIPVINKIDLK--N 182
Cdd:cd01883 77 YRFTIIDAPGHRDF---VKNMITgASQAdvAVLVVSARKGefeagfeKGGQTREHALLARTLGVKqLIVAVNKMDDVtvN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27370038 183 ADPER-------VGKQIEKV-FDIPSEECIKISAKLGTNV 214
Cdd:cd01883 154 WSQERydeikkkVSPFLKKVgYNPKDVPFIPISGFTGDNL 193
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
58-228 |
3.33e-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: 82.27 E-value: 3.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 58 HVDHGKSTLadrLLELTGtIDKtkknkqvlDKLQVERERGITVKAQTASLFYSFGGKqylLNLIDTPGHVDFSYEVSRSL 137
Cdd:cd04171 7 HIDHGKTTL---IKALTG-IET--------DRLPEEKKRGITIDLGFAYLDLPDGKR---LGFIDVPGHEKFVKNMLAGA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 138 SACQGVLLVVDANEGIQAQTVANF----FLAFEaqlSVIPVINKIDLknADPERVGKQIEKV------FDIPSEECIKIS 207
Cdd:cd04171 72 GGIDAVLLVVAADEGIMPQTREHLeileLLGIK---KGLVVLTKADL--VDEDRLELVEEEIlellagTFLADAPIFPVS 146
|
170 180
....*....|....*....|.
gi 27370038 208 AKLGTNVDSvLQAVIERIPPP 228
Cdd:cd04171 147 SVTGEGIEE-LKNYLDELAEP 166
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
55-223 |
9.15e-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: 80.96 E-value: 9.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 55 IIAHVDHGKSTLADRLLELTGTIdktkknkqvldklqVERERGITVKAQTASLfySFGGKQYLLNLIDTPGHVDFSYEVS 134
Cdd:cd00882 2 VVGRGGVGKSSLLNALLGGEVGE--------------VSDVPGTTRDPDVYVK--ELDKGKVKLVLVDTPGLDEFGGLGR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 135 RSLSA-----CQGVLLVVDANEGIQAQTVANFFLA--FEAQLSVIPVINKIDLKNADPERVGKQIEKVFDIPSEECIKIS 207
Cdd:cd00882 66 EELARlllrgADLILLVVDSTDRESEEDAKLLILRrlRKEGIPIILVGNKIDLLEEREVEELLRLEELAKILGVPVFEVS 145
|
170
....*....|....*.
gi 27370038 208 AKLGTNVDSVLQAVIE 223
Cdd:cd00882 146 AKTGEGVDELFEKLIE 161
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
52-299 |
1.18e-16 |
|
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]
Pssm-ID: 129567 [Multi-domain] Cd Length: 581 Bit Score: 83.38 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 52 NFSIIAHVDHGKSTLADrllELTGTidktkknkqVLDKLQVERERGITVKAQtaslFYSFGGKQYLLNLIDTPGHVDFSY 131
Cdd:TIGR00475 2 IIATAGHVDHGKTTLLK---ALTGI---------AADRLPEEKKRGMTIDLG----FAYFPLPDYRLGFIDVPGHEKFIS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 132 EVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQL-SVIPVINKIDLKNADP----ERVGKQI-EKVFDIPSEECIK 205
Cdd:TIGR00475 66 NAIAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIpHTIVVITKADRVNEEEikrtEMFMKQIlNSYIFLKNAKIFK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 206 ISAKLGTNVDSV---LQAVIERIPPPKVHRenPLKaLVFDSTFD-QYRGVIANIALFDGVVSKGDKIVSAHTKKAYEVNE 281
Cdd:TIGR00475 146 TSAKTGQGIGELkkeLKNLLESLDIKRIQK--PLR-MAIDRAFKvKGAGTVVTGTAFSGEVKVGDNLRLLPINHEVRVKA 222
|
250
....*....|....*...
gi 27370038 282 VGILNpneQPTHKLYAGQ 299
Cdd:TIGR00475 223 IQAQN---QDVEIAYAGQ 237
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
55-217 |
1.21e-16 |
|
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]
Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 77.80 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 55 IIAHVDHGKSTLADRLLeltgtidktkKNKQVLdklqVERERGITVKAQTASLFYsfGGKQYLLNLIDTPGHVDFSY--- 131
Cdd:TIGR00231 6 IVGHPNVGKSTLLNSLL----------GNKGSI----TEYYPGTTRNYVTTVIEE--DGKTYKFNLLDTAGQEDYDAirr 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 132 ----EVSRSLSACQGVLLVVDANEGIQAQTVANFFLAfEAQLSVIPVINKIDLKNAD-PERVGKQIEKVFDIPSeecIKI 206
Cdd:TIGR00231 70 lyypQVERSLRVFDIVILVLDVEEILEKQTKEIIHHA-DSGVPIILVGNKIDLKDADlKTHVASEFAKLNGEPI---IPL 145
|
170
....*....|.
gi 27370038 207 SAKLGTNVDSV 217
Cdd:TIGR00231 146 SAETGKNIDSA 156
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
52-232 |
9.93e-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: 75.87 E-value: 9.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 52 NFSIIAHVDHGKSTLADRLLELTGTidktkknkQVLDKLQVERERGITV----------KAQTASLFYSFGGKQYLLNLI 121
Cdd:cd01889 2 NVGLLGHVDSGKTSLAKALSEIAST--------AAFDKNPQSQERGITLdlgfssfevdKPKHLEDNENPQIENYQITLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 122 DTPGHVDFSYEVsrsLSACQ---GVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLknADPERVGKQIEKVFDI 198
Cdd:cd01889 74 DCPGHASLIRTI---IGGAQiidLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDL--IPEEERKRKIEKMKKR 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27370038 199 ----------PSEECIKISAKLGTNVDSVLQAVIERIPPPKVHR 232
Cdd:cd01889 149 lqktlektrlKDSPIIPVSAKPGEGEAELGGELKNLIVLPLINL 192
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
58-273 |
1.10e-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: 80.06 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 58 HVDHGKSTLADrlleltgTIDKTKknkqVldklqVERE-RGIT-------VKAQtaslfysfGGKqylLNLIDTPGHVDF 129
Cdd:COG0532 12 HVDHGKTSLLD-------AIRKTN----V-----AAGEaGGITqhigayqVETN--------GGK---ITFLDTPGHEAF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 130 SYEVSRSLSACQGVLLVVDANEGIQAQTV-A-NFflAFEAQLSVIPVINKIDLKNADPERVGKQIEKvFDIPSEE----- 202
Cdd:COG0532 65 TAMRARGAQVTDIVILVVAADDGVMPQTIeAiNH--AKAAGVPIIVAINKIDKPGANPDRVKQELAE-HGLVPEEwggdt 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27370038 203 -CIKISAKLGTNVDS-----VLQAVIERIpppKVHRENPLKALVFDSTFDQYRGVIANIALFDGVVSKGDKIVSAHT 273
Cdd:COG0532 142 iFVPVSAKTGEGIDEllemiLLQAEVLEL---KANPDRPARGTVIEAKLDKGRGPVATVLVQNGTLKVGDIVVAGTA 215
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
52-237 |
1.23e-15 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 79.79 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 52 NFSIIAHVDHGKSTLADRLLELTGTIDKTKKNK----------------QVLDKLQVERERGITVKAQTaslfYSFGGKQ 115
Cdd:PTZ00141 9 NLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKfekeaaemgkgsfkyaWVLDKLKAERERGITIDIAL----WKFETPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 116 YLLNLIDTPGHVDFSYEVSRSLSACQGVLLVVDANEGI-------QAQTVANFFLAFeaQLSV---IPVINKIDLKNAD- 184
Cdd:PTZ00141 85 YYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEfeagiskDGQTREHALLAF--TLGVkqmIVCINKMDDKTVNy 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27370038 185 ---------------PERVGKQIEKVFDIP-----SEECIKISAKLGTNVDSVLQAVIERIPPPKVHRENPLK 237
Cdd:PTZ00141 163 sqerydeikkevsayLKKVGYNPEKVPFIPisgwqGDNMIEKSDNMPWYKGPTLLEALDTLEPPKRPVDKPLR 235
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
51-200 |
1.53e-15 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 79.79 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 51 RNFSIIAHVDHGKSTLADRLL------ELTGTIdKTKKNKQ--VLDKLQVERERGITVkaqTASLFySFGGKQYLLNLID 122
Cdd:PRK00741 11 RTFAIISHPDAGKTTLTEKLLlfggaiQEAGTV-KGRKSGRhaTSDWMEMEKQRGISV---TSSVM-QFPYRDCLINLLD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 123 TPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVAnfflAFE-AQLSVIPV---INKIDLKNADPERVGKQIEKVFDI 198
Cdd:PRK00741 86 TPGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTRK----LMEvCRLRDTPIftfINKLDRDGREPLELLDEIEEVLGI 161
|
..
gi 27370038 199 PS 200
Cdd:PRK00741 162 AC 163
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
55-232 |
5.17e-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: 5.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 55 IIA---HVDHGKSTLadrLLELTGtIDkTkknkqvlDKLQVERERGITVkaqtaSLFYSF----GGKQylLNLIDTPGHV 127
Cdd:COG3276 2 IIGtagHIDHGKTTL---VKALTG-ID-T-------DRLKEEKKRGITI-----DLGFAYlplpDGRR--LGFVDVPGHE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 128 DFsyeVSRSLSACQG---VLLVVDANEGIQAQTVANF----FLAFEaQLSVipVINKIDLknADPERVGKQIEKVFDI-- 198
Cdd:COG3276 63 KF---IKNMLAGAGGidlVLLVVAADEGVMPQTREHLaildLLGIK-RGIV--VLTKADL--VDEEWLELVEEEIRELla 134
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 27370038 199 ----PSEECIKISAKLGTNVD---SVLQAVIERIPPPKVHR 232
Cdd:COG3276 135 gtflEDAPIVPVSAVTGEGIDelrAALDALAAAVPARDADG 175
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
52-315 |
4.75e-14 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 74.86 E-value: 4.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 52 NFSIIAHVDHGKSTLADrllELTGTIDKTKKNKQV----LDKLQVERERGITVkaQTASLFYSFGGKQYllNLIDTPGHV 127
Cdd:PLN03127 63 NVGTIGHVDHGKTTLTA---AITKVLAEEGKAKAVafdeIDKAPEEKARGITI--ATAHVEYETAKRHY--AHVDCPGHA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 128 DFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQL-SVIPVINKIDLKNaDPERVG------KQIEKVFDIPS 200
Cdd:PLN03127 136 DYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVpSLVVFLNKVDVVD-DEELLElvemelRELLSFYKFPG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 201 EEcIKI------SAKLGTN-------VDSVLQAVIERIPPPKVHRENPLKALVFDSTFDQYRGVIANIALFDGVVSKGDk 267
Cdd:PLN03127 215 DE-IPIirgsalSALQGTNdeigknaILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGE- 292
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27370038 268 ivsahtkkayevnEVGILNPNEQPTHK------------LYAGQ----VGFLIAGMK--DVTEAQI 315
Cdd:PLN03127 293 -------------EVEIVGLRPGGPLKttvtgvemfkkiLDQGQagdnVGLLLRGLKreDVQRGQV 345
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
62-223 |
5.37e-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: 64.19 E-value: 5.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 62 GKSTLADRLLeltgtidktkkNKQVLDklqVERERGITVKAQTASLFYSFGGKqylLNLIDTPGHVD-------FSYEVS 134
Cdd:cd00880 9 GKSSLLNALL-----------GQNVGI---VSPIPGTTRDPVRKEWELLPLGP---VVLIDTPGLDEegglgreRVEEAR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 135 RSLSACQGVLLVVDA--NEGIQAQTVANFFlafEAQLSVIPVINKIDLKNADPERVGKQIEKVFDIPSEECIKISAKLGT 212
Cdd:cd00880 72 QVADRADLVLLVVDSdlTPVEEEAKLGLLR---ERGKPVLLVLNKIDLVPESEEEELLRERKLELLPDLPVIAVSALPGE 148
|
170
....*....|.
gi 27370038 213 NVDSVLQAVIE 223
Cdd:cd00880 149 GIDELRKKIAE 159
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
52-268 |
5.45e-12 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 67.95 E-value: 5.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 52 NFSIIAHVDHGKSTLAdrlLELTGTidKTKKNKQvldklqvERERGITVK---AQTAslFY------------------S 110
Cdd:PRK04000 11 NIGMVGHVDHGKTTLV---QALTGV--WTDRHSE-------ELKRGITIRlgyADAT--IRkcpdceepeayttepkcpN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 111 FGGKQYLL---NLIDTPGHvdfsyEV--SRSLSAC---QGVLLVVDANEGI-QAQTVANFfLAFEA--QLSVIPVINKID 179
Cdd:PRK04000 77 CGSETELLrrvSFVDAPGH-----ETlmATMLSGAalmDGAILVIAANEPCpQPQTKEHL-MALDIigIKNIVIVQNKID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 180 LknADPERVGK---QI---------EKVFDIPseecikISAKLGTNVDSVLQAVIERIPPPKVHRENPLKALV---FD-- 242
Cdd:PRK04000 151 L--VSKERALEnyeQIkefvkgtvaENAPIIP------VSALHKVNIDALIEAIEEEIPTPERDLDKPPRMYVarsFDvn 222
|
250 260 270
....*....|....*....|....*....|
gi 27370038 243 ---STFDQYR-GVIANiALFDGVVSKGDKI 268
Cdd:PRK04000 223 kpgTPPEKLKgGVIGG-SLIQGVLKVGDEI 251
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
49-223 |
7.75e-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: 63.99 E-value: 7.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 49 DIRNFSIIAHVDHGKSTLADRLLeltgtidktkKNKQVLdklqVERERGITVKAqtASLFYSFGGKQYLLnlIDTPG--- 125
Cdd:cd01895 1 DPIKIAIIGRPNVGKSSLLNALL----------GEERVI----VSDIAGTTRDS--IDVPFEYDGQKYTL--IDTAGirk 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 126 ------HVDFsYEVSRSLSA---CQGVLLVVDANEGI--QAQTVANFflAFEAQLSVIPVINKIDLKNADPER---VGKQ 191
Cdd:cd01895 63 kgkvteGIEK-YSVLRTLKAierADVVLLVLDASEGIteQDLRIAGL--ILEEGKALIIVVNKWDLVEKDEKTmkeFEKE 139
|
170 180 190
....*....|....*....|....*....|....*.
gi 27370038 192 IEKVF----DIPseeCIKISAKLGTNVDSVLQAVIE 223
Cdd:cd01895 140 LRRKLpfldYAP---IVFISALTGQGVDKLFDAIKE 172
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
52-229 |
7.84e-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: 64.60 E-value: 7.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 52 NFSIIAHVDHGKSTLadrLLELTGTidKTKKNKQvldklqvERERGITVKAQTA-SLFY-------------------SF 111
Cdd:cd01888 2 NIGTIGHVAHGKTTL---VKALSGV--WTVRHKE-------ELKRNITIKLGYAnAKIYkcpncgcprpydtpececpGC 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 112 GGKQYLL---NLIDTPGHvdfsyEV--SRSLSAC---QGVLLVVDANEGI-QAQTVANFF-LAFEAQLSVIPVINKIDLk 181
Cdd:cd01888 70 GGETKLVrhvSFVDCPGH-----EIlmATMLSGAavmDGALLLIAANEPCpQPQTSEHLAaLEIMGLKHIIILQNKIDL- 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27370038 182 nADPERVGKQIEKVFDIPSEEC------IKISAKLGTNVDSVLQAVIERIPPPK 229
Cdd:cd01888 144 -VKEEQALENYEQIKEFVKGTIaenapiIPISAQLKYNIDVLCEYIVKKIPTPP 196
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
59-269 |
9.39e-12 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 67.63 E-value: 9.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 59 VDHGKSTLADRLLELTGTI----------DKTKKNKQ--------VLDKLQVERERGITVkaQTASLFYSFGGKQYLLNl 120
Cdd:PRK05124 36 VDDGKSTLIGRLLHDTKQIyedqlaslhnDSKRHGTQgekldlalLVDGLQAEREQGITI--DVAYRYFSTEKRKFIIA- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 121 iDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAfeAQLS---VIPVINKIDLKNADPER---------- 187
Cdd:PRK05124 113 -DTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIA--TLLGikhLVVAVNKMDLVDYSEEVferiredylt 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 188 VGKQIEKVFDIpseECIKISAKLGTNVDS-----------VLQAVIERIPPPKVHRENPLKALVfdstfdQY-------- 248
Cdd:PRK05124 190 FAEQLPGNLDI---RFVPLSALEGDNVVSqsesmpwysgpTLLEVLETVDIQRVVDAQPFRFPV------QYvnrpnldf 260
|
250 260
....*....|....*....|.
gi 27370038 249 RGVIANIAlfDGVVSKGDKIV 269
Cdd:PRK05124 261 RGYAGTLA--SGVVKVGDRVK 279
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
59-282 |
9.48e-12 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 68.03 E-value: 9.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 59 VDHGKSTLADRLLELTGTI----------DKTKKNKQ--------VLDKLQVERERGITVkaQTASLFYSFGGKQYLLnl 120
Cdd:PRK05506 33 VDDGKSTLIGRLLYDSKMIfedqlaalerDSKKVGTQgdeidlalLVDGLAAEREQGITI--DVAYRYFATPKRKFIV-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 121 IDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAfeAQLS---VIPVINKIDLKNADPERVgKQIEKVF- 196
Cdd:PRK05506 109 ADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIA--SLLGirhVVLAVNKMDLVDYDQEVF-DEIVADYr 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 197 ------DIPSEECIKISAKLGTNV------------------------DSVLQAVIERIPPPKVHRENplkalvfdstfD 246
Cdd:PRK05506 186 afaaklGLHDVTFIPISALKGDNVvtrsarmpwyegpsllehletveiASDRNLKDFRFPVQYVNRPN-----------L 254
|
250 260 270
....*....|....*....|....*....|....*.
gi 27370038 247 QYRGVIANIAlfDGVVSKGDKIVSAHTKKAYEVNEV 282
Cdd:PRK05506 255 DFRGFAGTVA--SGVVRPGDEVVVLPSGKTSRVKRI 288
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
109-226 |
1.93e-11 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 66.59 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 109 YSFGGKQYLLnlIDTPG-----HVD-----FSyeVSRSLSA---CQGVLLVVDANEGIQAQ--TVANffLAFEAQLSVIP 173
Cdd:COG1160 218 FERDGKKYTL--IDTAGirrkgKVDegiekYS--VLRTLRAierADVVLLVIDATEGITEQdlKIAG--LALEAGKALVI 291
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27370038 174 VINKIDL---KNADPERVGKQIEKVF----DIPseeCIKISAKLGTNVDSVLQAVIE-------RIP 226
Cdd:COG1160 292 VVNKWDLvekDRKTREELEKEIRRRLpfldYAP---IVFISALTGQGVDKLLEAVDEvyesankRIS 355
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
52-268 |
1.97e-11 |
|
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: 66.34 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 52 NFSIIAHVDHGKSTLA---DRLLELTGTIDKTKKNKqvLDKLQVERERGITVkaQTASLFYSFGGKQYLlnLIDTPGHVD 128
Cdd:TIGR00485 14 NVGTIGHVDHGKTTLTaaiTTVLAKEGGAAARAYDQ--IDNAPEEKARGITI--NTAHVEYETETRHYA--HVDCPGHAD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 129 FSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPV-INKIDLknADPERVGKQIE-------KVFDIPS 200
Cdd:TIGR00485 88 YVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKCDM--VDDEELLELVEmevrellSQYDFPG 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27370038 201 EEC--IKISAKLGTNVDS--------VLQAVIERIPPPKVHRENPLKALVFDSTFDQYRGVIANIALFDGVVSKGDKI 268
Cdd:TIGR00485 166 DDTpiIRGSALKALEGDAeweakileLMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEV 243
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
109-232 |
3.26e-11 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 65.84 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 109 YSFGGKQYLLnlIDTPG-----HVDFS---YEVSRSLSA---CQGVLLVVDANEGI--QAQTVANFflAFEAQLSVIPVI 175
Cdd:PRK00093 216 FERDGQKYTL--IDTAGirrkgKVTEGvekYSVIRTLKAierADVVLLVIDATEGIteQDLRIAGL--ALEAGRALVIVV 291
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27370038 176 NKIDLKNADP-ERVGKQIEKVF----DIPSeecIKISAKLGTNVDSVLQAVIE-------RIPPPKVHR 232
Cdd:PRK00093 292 NKWDLVDEKTmEEFKKELRRRLpfldYAPI---VFISALTGQGVDKLLEAIDEayenanrRISTSVLNR 357
|
|
| EFG_III-like |
cd16257 |
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G ... |
337-410 |
4.46e-11 |
|
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: 58.90 E-value: 4.46e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27370038 337 PMVFAGVYPIDQSEYNNLKSAIEKLTLNDSSVTVHRDSSlalGAGWRLGFLGLLHMEVFNQRLEQEYNASVILT 410
Cdd:cd16257 1 PVVFVTVEVKNPLDQEKLLEGLERLSEEDPALQVYREES---TGEFILSGLGELHLEIIVARLEREYGVELVVS 71
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
52-217 |
1.07e-10 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 64.34 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 52 NFSIIAHVDHGKSTLADRLLELTGTIDK----------TKKNKQ------VLDKLQVERERGITVKAQtaslFYSFGGKQ 115
Cdd:PLN00043 9 NIVVIGHVDSGKSTTTGHLIYKLGGIDKrvierfekeaAEMNKRsfkyawVLDKLKAERERGITIDIA----LWKFETTK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 116 YLLNLIDTPGHVDFSYEVSRSLSACQGVLLVVDANEG-------IQAQTVANFFLAFEAQL-SVIPVINKIDLKNAdper 187
Cdd:PLN00043 85 YYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGgfeagisKDGQTREHALLAFTLGVkQMICCCNKMDATTP---- 160
|
170 180 190
....*....|....*....|....*....|
gi 27370038 188 vgKQIEKVFDIPSEECIKISAKLGTNVDSV 217
Cdd:PLN00043 161 --KYSKARYDEIVKEVSSYLKKVGYNPDKI 188
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
54-287 |
1.48e-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: 64.07 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 54 SIIAHVDHGKSTLADRLL----------ELTGTIDKTKKNKQVLDKLQVERERGITVKAQTASLFYsfggkqyllnlIDT 123
Cdd:TIGR00491 8 VVLGHVDHGKTTLLDKIRgtavvkkeagGITQHIGASEVPTDVIEKICGDLLKSFKIKLKIPGLLF-----------IDT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 124 PGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDL-----------------KNADPE 186
Cdd:TIGR00491 77 PGHEAFTNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTPFVVAANKIDRipgwkshegypflesinKQEQRV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 187 R----------VGKQIEKVF---------DIPSEEC-IKISAKLGTNVDSVLQAVI--------ERIpppKVHRENPLKA 238
Cdd:TIGR00491 157 RqnldkqvynlVIQLAEQGFnaerfdrirDFTKTVAiIPVSAKTGEGIPELLAILAglaqnyleNKL---KLAIEGPAKG 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 27370038 239 LVFDSTFDQYRGVIANIALFDGVVSKGDKIVSAHTKKAYEVNEVGILNP 287
Cdd:TIGR00491 234 TILEVKEEQGLGYTIDAVIYDGILRKGDIIVLAGIDDVIVTRVRAILKP 282
|
|
| EFG_mtEFG_C |
cd03713 |
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational ... |
453-529 |
4.41e-10 |
|
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: 56.38 E-value: 4.41e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27370038 453 EPVVLGTVITPTEYTGKIMALCQARRAIQKNMTfIDENRVMLKYLFPLNEIvVDFYDSLKSLSSGYASFDYEDAGYQ 529
Cdd:cd03713 1 EPIMKVEVTVPEEYMGDVIGDLSSRRGQILGTE-SRGGWKVIKAEVPLAEM-FGYSTDLRSLTQGRGSFTMEFSHYE 75
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
120-227 |
6.04e-10 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 60.77 E-value: 6.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 120 LIDTPG-H----------VDFsyeVSRSLSACQGVLLVVDANEGIQAQTvaNFFLAFEAQLS--VIPVINKIDLknADPE 186
Cdd:COG1159 55 FVDTPGiHkpkrklgrrmNKA---AWSALEDVDVILFVVDATEKIGEGD--EFILELLKKLKtpVILVINKIDL--VKKE 127
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 27370038 187 RVGKQIEKVFD-IPSEECIKISAKLGTNVDSVLQAVIERIPP 227
Cdd:COG1159 128 ELLPLLAEYSElLDFAEIVPISALKGDNVDELLDEIAKLLPE 169
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
52-310 |
6.12e-10 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 61.94 E-value: 6.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 52 NFSIIAHVDHGKSTLADRL-LELTGTIDKTKKNKQVLDKLQVERERGITVkaQTASLFYSFGGKQYLLnlIDTPGHVDFS 130
Cdd:PLN03126 83 NIGTIGHVDHGKTTLTAALtMALASMGGSAPKKYDEIDAAPEERARGITI--NTATVEYETENRHYAH--VDCPGHADYV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 131 YEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQL-SVIPVINKIDLknADPERVGKQIE-------KVFDIPSEE 202
Cdd:PLN03126 159 KNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVpNMVVFLNKQDQ--VDDEELLELVElevrellSSYEFPGDD 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 203 CIKISA---------------KLGTN--VDSV---LQAVIERIPPPKVHRENPLKALVFDSTFDQYRGVIANIALFDGVV 262
Cdd:PLN03126 237 IPIISGsallalealmenpniKRGDNkwVDKIyelMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTV 316
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 27370038 263 SKGD--KIVSAHTKKAYEVNEVGILnpnEQPTHKLYAG-QVGFLIAGMKDV 310
Cdd:PLN03126 317 KVGEtvDIVGLRETRSTTVTGVEMF---QKILDEALAGdNVGLLLRGIQKA 364
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
52-268 |
2.05e-09 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 59.96 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 52 NFSIIAHVDHGKSTladrlleLTGTIDKTKKNKQV--------LDKLQVERERGITVkaQTASLFYSFGGKQYLlnLIDT 123
Cdd:PRK12736 14 NIGTIGHVDHGKTT-------LTAAITKVLAERGLnqakdydsIDAAPEEKERGITI--NTAHVEYETEKRHYA--HVDC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 124 PGHVDfsYEVSRSLSACQ--GVLLVVDANEGIQAQTVANFFLAFEAQLSVIPV-INKIDLKNaDPERVG------KQIEK 194
Cdd:PRK12736 83 PGHAD--YVKNMITGAAQmdGAILVVAATDGPMPQTREHILLARQVGVPYLVVfLNKVDLVD-DEELLElvemevRELLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 195 VFDIPSEEC--IKISA--------KLGTNVDSVLQAVIERIPPPKVHRENPLKALVFDSTFDQYRGVIANIALFDGVVSK 264
Cdd:PRK12736 160 EYDFPGDDIpvIRGSAlkalegdpKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKV 239
|
....
gi 27370038 265 GDKI 268
Cdd:PRK12736 240 GDEV 243
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
62-225 |
2.64e-09 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 56.91 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 62 GKSTLADRLLEltGTIDktkknkqvldklqvERERGITVKAQTASLFYSFGGKQYLLNLIDTPGHVDFSYE---VSRSLS 138
Cdd:COG1100 15 GKTSLVNRLVG--DIFS--------------LEKYLSTNGVTIDKKELKLDGLDVDLVIWDTPGQDEFRETrqfYARQLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 139 ACQGVLLVVDaneGIQAQTVANFFLAFEA------QLSVIPVINKIDLKNADPERVGKQIEKVF-DIPSEECIKISAKLG 211
Cdd:COG1100 79 GASLYLFVVD---GTREETLQSLYELLESlrrlgkKSPIILVLNKIDLYDEEEIEDEERLKEALsEDNIVEVVATSAKTG 155
|
170
....*....|....
gi 27370038 212 TNVDSVLQAVIERI 225
Cdd:COG1100 156 EGVEELFAALAEIL 169
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
56-186 |
3.88e-09 |
|
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: 56.82 E-value: 3.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 56 IAHVDHGKSTLAD---RLLELTGtIDKTKKNKQVlDKLQVERERGITVkaQTASLFYSFGGKQYllNLIDTPGHVDFsye 132
Cdd:cd01884 8 IGHVDHGKTTLTAaitKVLAKKG-GAKAKKYDEI-DKAPEEKARGITI--NTAHVEYETANRHY--AHVDCPGHADY--- 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 27370038 133 VSRSLS-ACQ--GVLLVVDANEGIQAQTVANFFLAFEAQLSVIPV-INKIDLKnADPE 186
Cdd:cd01884 79 IKNMITgAAQmdGAILVVSATDGPMPQTREHLLLARQVGVPYIVVfLNKADMV-DDEE 135
|
|
| tufA |
CHL00071 |
elongation factor Tu |
52-268 |
4.89e-09 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 58.82 E-value: 4.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 52 NFSIIAHVDHGKSTL-ADRLLELTGTIDKTKKNKQVLDKLQVERERGITVKaqTASLFYSFGGKQYllNLIDTPGHVDFS 130
Cdd:CHL00071 14 NIGTIGHVDHGKTTLtAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITIN--TAHVEYETENRHY--AHVDCPGHADYV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 131 YEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPV-INKIDLKNaDPERVG------KQIEKVFDIPSEE- 202
Cdd:CHL00071 90 KNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVfLNKEDQVD-DEELLElvelevRELLSKYDFPGDDi 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 203 -CIKISA-------------KLGTN--VDSVLQ---AVIERIPPPKVHRENPLKALVFDSTFDQYRGVIANIALFDGVVS 263
Cdd:CHL00071 169 pIVSGSAllalealtenpkiKRGENkwVDKIYNlmdAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVK 248
|
....*
gi 27370038 264 KGDKI 268
Cdd:CHL00071 249 VGDTV 253
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
55-328 |
1.03e-08 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 58.14 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 55 IIA---HVDHGKSTLadrLLELTGtIDKtkknkqvlDKLQVERERGITVkaqtaSLFYSF----GGKqyLLNLIDTPGHV 127
Cdd:PRK10512 2 IIAtagHVDHGKTTL---LQAITG-VNA--------DRLPEEKKRGMTI-----DLGYAYwpqpDGR--VLGFIDVPGHE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 128 DFsyeVSRSLSACQGV---LLVVDANEGIQAQT---VANFFLAFEAQLSVipVINKIDLknADPER---VGKQIEKV--- 195
Cdd:PRK10512 63 KF---LSNMLAGVGGIdhaLLVVACDDGVMAQTrehLAILQLTGNPMLTV--ALTKADR--VDEARiaeVRRQVKAVlre 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 196 FDIPSEECIKISAKLGTNVDSV---LQAVIERiPPPKVHRENplkaLVFDSTFdQYRG---VIANIALfDGVVSKGDKIV 269
Cdd:PRK10512 136 YGFAEAKLFVTAATEGRGIDALrehLLQLPER-EHAAQHRFR----LAIDRAF-TVKGaglVVTGTAL-SGEVKVGDTLW 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27370038 270 SAHTKKAYEVNEvgiLNPNEQPTHKLYAGQ-VGFLIAGmkDVTEAQI--GDTLyLHNHPVEP 328
Cdd:PRK10512 209 LTGVNKPMRVRG---LHAQNQPTEQAQAGQrIALNIAG--DAEKEQInrGDWL-LADAPPEP 264
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
120-227 |
1.22e-08 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 56.59 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 120 LIDTPG-H----------VDFsyeVSRSLSACQGVLLVVDANEGIQAQTvaNFFLAF--EAQLSVIPVINKIDLKNaDPE 186
Cdd:PRK00089 57 FVDTPGiHkpkralnramNKA---AWSSLKDVDLVLFVVDADEKIGPGD--EFILEKlkKVKTPVILVLNKIDLVK-DKE 130
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 27370038 187 RVGKQIEKVFD-IPSEECIKISAKLGTNVDSVLQAVIERIPP 227
Cdd:PRK00089 131 ELLPLLEELSElMDFAEIVPISALKGDNVDELLDVIAKYLPE 172
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
250-319 |
3.92e-08 |
|
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.
Pssm-ID: 427163 [Multi-domain] Cd Length: 73 Bit Score: 50.73 E-value: 3.92e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27370038 250 GVIANIALFDGVVSKGDKI--VSAHTKKAYEVNEVGILNPNEQPTHKLYAGQVGFLIAGMKDVTEAQIGDTL 319
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVriLPNGTGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTL 72
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
116-225 |
1.02e-07 |
|
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: 51.73 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 116 YLLNLIDTPG------HVdfsyE---VSRSLSACQG---VLLVVDANEGIQAQTVAnfFLAFEAQLSVIPVINKIDLKna 183
Cdd:cd04164 51 IPVRLIDTAGlretedEI----EkigIERAREAIEEadlVLLVVDASEGLDEEDLE--ILELPAKKPVIVVLNKSDLL-- 122
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 27370038 184 dpervgKQIEKVFDIPSEECIKISAKLGTNVDSVLQAVIERI 225
Cdd:cd04164 123 ------SDAEGISELNGKPIIAISAKTGEGIDELKEALLELA 158
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
56-186 |
1.09e-07 |
|
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: 54.39 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 56 IAHVDHGKSTL--AdrlleLTGTIDKTKKNKQV----LDKLQVERERGIT-----VKAQTASLFYSFggkqyllnlIDTP 124
Cdd:COG0050 18 IGHVDHGKTTLtaA-----ITKVLAKKGGAKAKaydqIDKAPEEKERGITintshVEYETEKRHYAH---------VDCP 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27370038 125 GHVDFsyeVSRSLS-ACQ--GVLLVVDANEGIQAQTVANFFLAfeAQLSV--IPV-INKIDLKNaDPE 186
Cdd:COG0050 84 GHADY---VKNMITgAAQmdGAILVVSATDGPMPQTREHILLA--RQVGVpyIVVfLNKCDMVD-DEE 145
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
52-268 |
1.66e-07 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 54.24 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 52 NFSIIAHVDHGKSTLADrllELTGTidKTKKNKQvldklqvERERGITVKAQTA-------------SLFYSFG------ 112
Cdd:PTZ00327 36 NIGTIGHVAHGKSTVVK---ALSGV--KTVRFKR-------EKVRNITIKLGYAnakiykcpkcprpTCYQSYGsskpdn 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 113 ------GKQYLL----NLIDTPGHvDFSyeVSRSLS-AC--QGVLLVVDANEGI-QAQTVANFFLAFEAQLSVIPVI-NK 177
Cdd:PTZ00327 104 ppcpgcGHKMTLkrhvSFVDCPGH-DIL--MATMLNgAAvmDAALLLIAANESCpQPQTSEHLAAVEIMKLKHIIILqNK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 178 IDL-KNADPERVGKQIEKVFDIPSEE---CIKISAKLGTNVDSVLQAVIERIPPPKVHRENPLKALV---FD-----STF 245
Cdd:PTZ00327 181 IDLvKEAQAQDQYEEIRNFVKGTIADnapIIPISAQLKYNIDVVLEYICTQIPIPKRDLTSPPRMIVirsFDvnkpgEDI 260
|
250 260
....*....|....*....|...
gi 27370038 246 DQYRGVIANIALFDGVVSKGDKI 268
Cdd:PTZ00327 261 ENLKGGVAGGSILQGVLKVGDEI 283
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
52-186 |
2.26e-07 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 53.65 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 52 NFSIIAHVDHGKSTLAdrlLELTGTIDKTKKNKQV----LDKLQVERERGIT-----VKAQTASLFYSFggkqyllnlID 122
Cdd:PRK00049 14 NVGTIGHVDHGKTTLT---AAITKVLAKKGGAEAKaydqIDKAPEEKARGITintahVEYETEKRHYAH---------VD 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27370038 123 TPGHVDFsyeVSRSLS-ACQ--GVLLVVDANEGIQAQTVANFFLAFEAQLSVIPV-INKIDLKNaDPE 186
Cdd:PRK00049 82 CPGHADY---VKNMITgAAQmdGAILVVSAADGPMPQTREHILLARQVGVPYIVVfLNKCDMVD-DEE 145
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
54-269 |
2.92e-07 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 53.65 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 54 SIIAHVDHGKSTLADRlleltgtIDKTKknkqVldklqVERERG-IT------------VKAQTASLFYSFGGKQYL--L 118
Cdd:PRK04004 10 VVLGHVDHGKTTLLDK-------IRGTA----V-----AAKEAGgITqhigatevpidvIEKIAGPLKKPLPIKLKIpgL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 119 NLIDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVanfflafEA----QLSVIPVI---NKID------------ 179
Cdd:PRK04004 74 LFIDTPGHEAFTNLRKRGGALADIAILVVDINEGFQPQTI-------EAinilKRRKTPFVvaaNKIDripgwkstedap 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 180 ----LKNADPERVGKQIEKVFDIPSE---------------------ECIKISAKLGTNVDSVLqAVI---------ERI 225
Cdd:PRK04004 147 flesIEKQSQRVQQELEEKLYELIGQlselgfsadrfdrvkdftktvAIVPVSAKTGEGIPDLL-MVLaglaqryleERL 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 27370038 226 pppKVHRENPLKALVFDSTFDQYRGVIANIALFDGVVSKGDKIV 269
Cdd:PRK04004 226 ---KIDVEGPGKGTVLEVKEERGLGTTIDVILYDGTLRKGDTIV 266
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
52-186 |
5.08e-07 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 52.53 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 52 NFSIIAHVDHGKSTladrlleLTGTIDKT--------KKNKQVLDKLQVERERGIT-----VKAQTASLFYSFggkqyll 118
Cdd:PRK12735 14 NVGTIGHVDHGKTT-------LTAAITKVlakkgggeAKAYDQIDNAPEEKARGITintshVEYETANRHYAH------- 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27370038 119 nlIDTPGHVDFsyeVSRSLS-ACQ--GVLLVVDANEGIQAQTVANFFLAFEAQLSVIPV-INKIDLKNaDPE 186
Cdd:PRK12735 80 --VDCPGHADY---VKNMITgAAQmdGAILVVSAADGPMPQTREHILLARQVGVPYIVVfLNKCDMVD-DEE 145
|
|
| MnmE |
COG0486 |
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
116-225 |
5.85e-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: 52.37 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 116 YLLNLIDTPG------HVdfsyE---VSRSLSACQG---VLLVVDANEGIQAQTVAnfFLAFEAQLSVIPVINKIDLKNA 183
Cdd:COG0486 261 IPVRLIDTAGlretedEV----EkigIERAREAIEEadlVLLLLDASEPLTEEDEE--ILEKLKDKPVIVVLNKIDLPSE 334
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 27370038 184 DPERVGKqiekvfdIPSEECIKISAKLGTNVDSVLQAVIERI 225
Cdd:COG0486 335 ADGELKS-------LPGEPVIAISAKTGEGIDELKEAILELV 369
|
|
| trmE |
PRK05291 |
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; |
116-225 |
9.55e-07 |
|
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
Pssm-ID: 235392 [Multi-domain] Cd Length: 449 Bit Score: 51.65 E-value: 9.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 116 YLLNLIDTPG------HVdfsyE---VSRSLSACQG---VLLVVDANEGIQAQTVANFFLafEAQLSVIPVINKIDLKNA 183
Cdd:PRK05291 263 IPLRLIDTAGiretddEV----EkigIERSREAIEEadlVLLVLDASEPLTEEDDEILEE--LKDKPVIVVLNKADLTGE 336
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 27370038 184 DPERvgkqiekvfDIPSEECIKISAKLGTNVDSVLQAVIERI 225
Cdd:PRK05291 337 IDLE---------EENGKPVIRISAKTGEGIDELREAIKELA 369
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
62-223 |
1.99e-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: 48.23 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 62 GKSTLADRLLELTGTIdktkknkqVLDKLQVERER--GItvkaqtaslfYSFGGKQYLLnlIDTPG-HVDFS-------Y 131
Cdd:cd04163 15 GKSTLLNALVGQKISI--------VSPKPQTTRNRirGI----------YTDDDAQIIF--VDTPGiHKPKKklgermvK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 132 EVSRSLSACQGVLLVVDANEGI--QAQTVANffLAFEAQLSVIPVINKIDLKNaDPERVGKQIEKVFD-IPSEECIKISA 208
Cdd:cd04163 75 AAWSALKDVDLVLFVVDASEWIgeGDEFILE--LLKKSKTPVILVLNKIDLVK-DKEDLLPLLEKLKElHPFAEIFPISA 151
|
170
....*....|....*
gi 27370038 209 KLGTNVDSVLQAVIE 223
Cdd:cd04163 152 LKGENVDELLEYIVE 166
|
|
| MnmE_helical |
pfam12631 |
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ... |
116-236 |
2.72e-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: 49.79 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 116 YLLNLIDTPG------HVdfsyE---VSRSLSACQG---VLLVVDANEGIQAQTvANFFLAFEAQLSVIPVINKIDLKNA 183
Cdd:pfam12631 142 IPLRLIDTAGiretddEV----EkigIERAREAIEEadlVLLVLDASRPLDEED-LEILELLKDKKPIIVVLNKSDLLGE 216
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 27370038 184 DPERVGKqiekvfdiPSEECIKISAKLGTNVDSVLQAVIERIPPPKVHRENPL 236
Cdd:pfam12631 217 IDELEEL--------KGKPVLAISAKTGEGLDELEEAIKELFLAGEIASDGPI 261
|
|
| HflX |
cd01878 |
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
143-225 |
3.15e-05 |
|
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: 45.53 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 143 VLLVVDA---NEGIQAQTVANFfLAfEAQLSVIPVI---NKIDLknADPERVGKQIEKvfdiPSEECIKISAKLGTNVDS 216
Cdd:cd01878 124 LLHVVDAsdpDREEQIETVEEV-LK-ELGADDIPIIlvlNKIDL--LDDEELEERLRA----GRPDAVFISAKTGEGLDL 195
|
....*....
gi 27370038 217 VLQAVIERI 225
Cdd:cd01878 196 LKEAIEELL 204
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
62-177 |
3.25e-05 |
|
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: 43.38 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 62 GKSTLADRLleltgtidkTKKNKQVLDKLqvererGITVKAQTASLfySFGGKQYLLnlIDTPGHVDFSYE---VSRSLS 138
Cdd:pfam01926 11 GKSTLINAL---------TGAKAIVSDYP------GTTRDPNEGRL--ELKGKQIIL--VDTPGLIEGASEgegLGRAFL 71
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 27370038 139 A---CQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINK 177
Cdd:pfam01926 72 AiieADLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
|
|
| EFG_C |
smart00838 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
452-529 |
3.34e-05 |
|
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: 42.49 E-value: 3.34e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27370038 452 LEPVVLGTVITPTEYTGKIMALCQARRAIQKNMTfiDENRVM-LKYLFPLNEIvVDFYDSLKSLSSGYASFDYEDAGYQ 529
Cdd:smart00838 2 LEPIMKVEVTVPEEYMGDVIGDLNSRRGKIEGME--QRGGAQvIKAKVPLSEM-FGYATDLRSATQGRATWSMEFSHYE 77
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
62-240 |
1.30e-04 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 45.01 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 62 GKSTLADRLleltgtidkTKKNKQVldklqVERERGIT--VKAQTASLfysfGGKQYLLnlIDTPGHVD-----FSYEVS 134
Cdd:COG1160 14 GKSTLFNRL---------TGRRDAI-----VDDTPGVTrdRIYGEAEW----GGREFTL--IDTGGIEPddddgLEAEIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 135 R-SLSACQG---VLLVVDANEGIQA--QTVANffLAFEAQLSVIPVINKIDLKNADPErvgkqiekVFDIPS---EECIK 205
Cdd:COG1160 74 EqAELAIEEadvILFVVDGRAGLTPldEEIAK--LLRRSGKPVILVVNKVDGPKREAD--------AAEFYSlglGEPIP 143
|
170 180 190
....*....|....*....|....*....|....*...
gi 27370038 206 ISAKLGTNVDSVLQAVIERIPPPKV--HRENPLK-ALV 240
Cdd:COG1160 144 ISAEHGRGVGDLLDAVLELLPEEEEeeEEDDPIKiAIV 181
|
|
| YihA_EngB |
cd01876 |
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
108-225 |
1.43e-04 |
|
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: 42.88 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 108 FYSFGGKQYLlnlIDTPG----------HVDFSYEVSRSLSACQ---GVLLVVDANEGIQAQTVANFFLAFEAQLSVIPV 174
Cdd:cd01876 40 FFNVGDKFRL---VDLPGygyakvskevREKWGKLIEEYLENREnlkGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIV 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 27370038 175 INKID-LKNADPERVGKQIEKVFD--IPSEECIKISAKLGTNVDSVLQAVIERI 225
Cdd:cd01876 117 LTKADkLKKSELAKVLKKIKEELNlfNILPPVILFSSKKGTGIDELRALIAEWL 170
|
|
| EFG_III |
cd16262 |
Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial ... |
336-412 |
2.96e-04 |
|
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: 39.75 E-value: 2.96e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27370038 336 KPMVFAGVYPIDQSEYNNLKSAIEKLTLNDSSVTVHRD--SSLALGAGwrlgfLGLLHMEVFNQRLEQEYNASVILTTP 412
Cdd:cd16262 2 EPVISLAIEPKTKADEDKLSKALARLAEEDPTLRVSRDeeTGQTILSG-----MGELHLEIIVERLKREYGVEVEVGKP 75
|
|
| BipA_TypA_C |
cd03710 |
BipA_TypA_C: a C-terminal portion of BipA or TypA having homology to the C terminal domains of ... |
453-499 |
3.20e-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: 39.80 E-value: 3.20e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 27370038 453 EPVVLGTVITPTEYTGKIMALCQARRAIQKNMTFIDENRVMLKYLFP 499
Cdd:cd03710 1 EPIEELTIDVPEEYSGAVIEKLGKRKGEMVDMEPDGNGRTRLEFKIP 47
|
|
| Ras |
pfam00071 |
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ... |
112-226 |
3.70e-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: 41.35 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 112 GGKQYLLNLIDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLS-VIPVI---NKIDLKNadpER 187
Cdd:pfam00071 44 DGKTVKLQIWDTAGQERFRALRPLYYRGADGFLLVYDITSRDSFENVKKWVEEILRHADeNVPIVlvgNKCDLED---QR 120
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 27370038 188 V-----GKQIEKVFDIPSEECikiSAKLGTNVDSVLQAVIERIP 226
Cdd:pfam00071 121 VvsteeGEALAKELGLPFMET---SAKTNENVEEAFEELAREIL 161
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
118-287 |
4.63e-04 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 43.33 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 118 LNLIDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDL---------------KN 182
Cdd:PRK14845 528 LLFIDTPGHEAFTSLRKRGGSLADLAVLVVDINEGFKPQTIEAINILRQYKTPFVVAANKIDLipgwnisedepfllnFN 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 183 ADPERVGKQIE---------------------KVFDIPSEECI-KISAKLGTNVDSVLQAVI--------ERIpppKVHR 232
Cdd:PRK14845 608 EQDQHALTELEiklyeligklyelgfdadrfdRVQDFTRTVAIvPVSAKTGEGIPELLMMVAglaqkyleERL---KLNV 684
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27370038 233 ENPLKALVFDSTFDQYRGVIANIALFDGVVSKGDKIVSAHTKKAYEVNEVGILNP 287
Cdd:PRK14845 685 EGYAKGTILEVKEEKGLGTTIDAIIYDGTLRRGDTIVVGGPDDVIVTKVRALLKP 739
|
|
| EngA1 |
cd01894 |
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
62-225 |
4.82e-04 |
|
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206681 [Multi-domain] Cd Length: 157 Bit Score: 41.27 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 62 GKSTLADRLleltgtidkTKKNKQVldklqVERERGIT--VKAQTASLfysfGGKQYLLnlIDTPGHVDFS--------Y 131
Cdd:cd01894 9 GKSTLFNRL---------TGRRDAI-----VSDTPGVTrdRKYGEAEW----GGREFIL--IDTGGIEPDDegiskeirE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 132 EVSRSLSACQGVLLVVDANEGIQA--QTVANFflAFEAQLSVIPVINKIDLKNADPE-----RVGkqiekvFdipsEECI 204
Cdd:cd01894 69 QAEIAIEEADVILFVVDGREGLTPadEEIAKY--LRKSKKPVILVVNKIDNIKEEEEaaefySLG------F----GEPI 136
|
170 180
....*....|....*....|.
gi 27370038 205 KISAKLGTNVDSVLQAVIERI 225
Cdd:cd01894 137 PISAEHGRGIGDLLDAILELL 157
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
236-320 |
4.90e-04 |
|
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: 39.17 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 236 LKALVFDSTFDQYRGVIANIALFDGVVSKGDKIVSAHTKKAYEVNEVGIlnpNEQPTHKLYAGQ-VGFLIAGMKDVteaQ 314
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIER---FHEEVDEAKAGDiVGIGILGVKDI---L 74
|
....*.
gi 27370038 315 IGDTLY 320
Cdd:cd01342 75 TGDTLT 80
|
|
| EFG_mtEFG_II |
cd04088 |
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation ... |
238-319 |
5.37e-04 |
|
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: 39.04 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 238 ALVFDSTFDQYRGVIANIALFDGVVSKGDKIVSAHTKKAYEVNEVGILNPNEQ-PTHKLYAGQVGfLIAGMKDvteAQIG 316
Cdd:cd04088 3 ALVFKTMADPFVGKLTFFRVYSGTLKSGSTVYNSTKGKKERVGRLLRMHGKKReEVEELGAGDIG-AVVGLKD---TRTG 78
|
...
gi 27370038 317 DTL 319
Cdd:cd04088 79 DTL 81
|
|
| NOG |
cd01897 |
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ... |
171-224 |
6.15e-04 |
|
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: 41.01 E-value: 6.15e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 27370038 171 VIPVINKIDLKNADPErvgKQIEKVFDIPSEECIKISAKLGTNVDSVLQAVIER 224
Cdd:cd01897 115 VIVVLNKIDLLTEEDL---SEIEKELEKEGEEVIKISTLTEEGVDELKNKACEL 165
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
117-258 |
1.09e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 41.68 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 117 LLNLIDTPGHVDFSY------EVSRSLSACQGVLLVVDANEgIQAQTVANFFLAFEAQLSVIP---VINKIDLknADPER 187
Cdd:COG3596 89 GLVLLDTPGLGEVNErdreyrELRELLPEADLILWVVKADD-RALATDEEFLQALRAQYPDPPvlvVLTQVDR--LEPER 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 188 VG-------------------KQIEKVFDIPSEECIKISAKL---GTNVDSVLQAVIERIPPPKVHRenpLKALVFDSTF 245
Cdd:COG3596 166 EWdppynwpsppkeqnirralEAIAEQLGVPIDRVIPVSAAEdrtGYGLEELVDALAEALPEAKRSR---LARLLRAKAI 242
|
170
....*....|...
gi 27370038 246 DQYRGVIANIALF 258
Cdd:COG3596 243 DRYTLLAAAAALL 255
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
62-240 |
1.30e-03 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 41.57 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 62 GKSTLADRLleltgtidkTKKNKQVldklqVERERGIT--VKAQTASLfysfGGKQYLLnlIDTPGHV----DFSYEVSR 135
Cdd:PRK00093 13 GKSTLFNRL---------TGKRDAI-----VADTPGVTrdRIYGEAEW----LGREFIL--IDTGGIEpdddGFEKQIRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 136 -SLSA---CQGVLLVVDANEGIQAQ--TVANFFlaFEAQLSVIPVINKIDLKNADpervgkqiEKVFDIPS---EECIKI 206
Cdd:PRK00093 73 qAELAieeADVILFVVDGRAGLTPAdeEIAKIL--RKSNKPVILVVNKVDGPDEE--------ADAYEFYSlglGEPYPI 142
|
170 180 190
....*....|....*....|....*....|....*..
gi 27370038 207 SAKLGTNVDSVLQAVIERIPPPKV--HRENPLK-ALV 240
Cdd:PRK00093 143 SAEHGRGIGDLLDAILEELPEEEEedEEDEPIKiAII 179
|
|
| SR_beta |
cd04105 |
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ... |
99-194 |
1.36e-03 |
|
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: 40.38 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 99 TVKAQTAS--LFYSFGGKQYLLNLIDTPGHVDFSYEVSRSLS-ACQGVLLVVDANEGIQ-AQTVANF----FLAFEAQLS 170
Cdd:cd04105 28 TVTSIEPNvaSFYSNSSKGKKLTLVDVPGHEKLRDKLLEYLKaSLKAIVFVVDSATFQKnIRDVAEFlydiLTDLEKIKN 107
|
90 100
....*....|....*....|....*...
gi 27370038 171 VIPVI---NKIDLKNA-DPERVGKQIEK 194
Cdd:cd04105 108 KIPILiacNKQDLFTAkPAKKIKELLEK 135
|
|
| RF3_III |
cd16259 |
Domain III of bacterial Release Factor 3 (RF3); The class II RF3 is a member of one of two ... |
337-410 |
1.41e-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: 37.62 E-value: 1.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27370038 337 PMVFAGVYPIDQSEYNNLKSAIEKLTlNDSSVTVHRDSSlalGAGWRLGFLGLLHMEVFNQRLEQEYNASVILT 410
Cdd:cd16259 1 PEHFRRVRLKDPMKAKQLRKGLEQLA-EEGAVQVFRPMD---GSDPIVGAVGPLQFEVLQARLENEYGVEVVFE 70
|
|
| EFG_III |
pfam14492 |
Elongation Factor G, domain III; This domain is found in Elongation Factor G. It shares a ... |
336-409 |
1.68e-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: 37.46 E-value: 1.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27370038 336 KPMVFAGVYPIDQSEYNNLKSAIEKLTLNDSSVTVHRDSslalGAG-WRLGFLGLLHMEVFNQRLEQEYNASVIL 409
Cdd:pfam14492 3 EPVISVAIEPKTKGDEDKLSKALNRLLEEDPTLRVERDE----ETGeTILSGMGELHLEIVVDRLKRKYGVEVEL 73
|
|
| RalA_RalB |
cd04139 |
Ral (Ras-like) family containing highly homologous RalA and RalB; The Ral (Ras-like) subfamily ... |
110-225 |
2.67e-03 |
|
Ral (Ras-like) family containing highly homologous RalA and RalB; The Ral (Ras-like) subfamily consists of the highly homologous RalA and RalB. Ral proteins are believed to play a crucial role in tumorigenesis, metastasis, endocytosis, and actin cytoskeleton dynamics. Despite their high sequence similarity (>80% sequence identity), nonoverlapping and opposing functions have been assigned to RalA and RalBs in tumor migration. In human bladder and prostate cancer cells, RalB promotes migration while RalA inhibits it. A Ral-specific set of GEFs has been identified that are activated by Ras binding. This RalGEF activity is enhanced by Ras binding to another of its target proteins, phosphatidylinositol 3-kinase (PI3K). Ral effectors include RLIP76/RalBP1, a Rac/cdc42 GAP, and the exocyst (Sec6/8) complex, a heterooctomeric protein complex that is involved in tethering vesicles to specific sites on the plasma membrane prior to exocytosis. In rat kidney cells, RalB is required for functional assembly of the exocyst and for localizing the exocyst to the leading edge of migrating cells. In human cancer cells, RalA is required to support anchorage-independent proliferation and RalB is required to suppress apoptosis. RalA has been shown to localize to the plasma membrane while RalB is localized to the intracellular vesicles. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.
Pssm-ID: 206710 [Multi-domain] Cd Length: 163 Bit Score: 38.95 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 110 SFGGKQYLLNLIDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFF-----LAFEAQLSVIPVINKIDLKnaD 184
Cdd:cd04139 42 VLDGEEVQLNILDTAGQEDYAAIRDNYFRSGEGFLLVFSITDMESFTALAEFReqilrVKEDDNVPLLLVGNKCDLE--D 119
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 27370038 185 PERVGKQIEKVFdipSEEC----IKISAKLGTNVDSVLQAVIERI 225
Cdd:cd04139 120 KRQVSVEEAANL---AEQWgvnyVETSAKTRANVDKVFFDLVREI 161
|
|
| PRK09518 |
PRK09518 |
bifunctional cytidylate kinase/GTPase Der; Reviewed |
125-230 |
2.79e-03 |
|
bifunctional cytidylate kinase/GTPase Der; Reviewed
Pssm-ID: 236546 [Multi-domain] Cd Length: 712 Bit Score: 40.93 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 125 GHVDFSYEVSRS-LSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADP-ERVGKQIEKVFD-IPSE 201
Cdd:PRK09518 517 GAEYYSSLRTQAaIERSELALFLFDASQPISEQDLKVMSMAVDAGRALVLVFNKWDLMDEFRrQRLERLWKTEFDrVTWA 596
|
90 100 110
....*....|....*....|....*....|....*.
gi 27370038 202 ECIKISAKLGTNVDSVLQAVIE-------RIPPPKV 230
Cdd:PRK09518 597 RRVNLSAKTGWHTNRLAPAMQEaleswdqRIPTGKL 632
|
|
| Ras |
cd00876 |
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the ... |
109-225 |
3.21e-03 |
|
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the Ras superfamily includes classical N-Ras, H-Ras, and K-Ras, as well as R-Ras, Rap, Ral, Rheb, Rhes, ARHI, RERG, Rin/Rit, RSR1, RRP22, Ras2, Ras-dva, and RGK proteins. Ras proteins regulate cell growth, proliferation and differentiation. Ras is activated by guanine nucleotide exchange factors (GEFs) that release GDP and allow GTP binding. Many RasGEFs have been identified. These are sequestered in the cytosol until activation by growth factors triggers recruitment to the plasma membrane or Golgi, where the GEF colocalizes with Ras. Active GTP-bound Ras interacts with several effector proteins: among the best characterized are the Raf kinases, phosphatidylinositol 3-kinase (PI3K), RalGEFs and NORE/MST1. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.
Pssm-ID: 206642 [Multi-domain] Cd Length: 160 Bit Score: 38.66 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 109 YSFGGKQYLLNLIDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFlafeAQL------SVIPVI---NKID 179
Cdd:cd00876 40 IVVDGETYTLDILDTAGQEEFSAMRDQYIRNGDGFILVYSITSRESFEEIKNIR----EQIlrvkdkEDVPIVlvgNKCD 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 27370038 180 LKNadpERV-----GKQIEKVFDIPSEECikiSAKLGTNVDSVLQAVIERI 225
Cdd:cd00876 116 LEN---ERQvsteeGEALAEEWGCPFLET---SAKTNINIDELFNTLVREI 160
|
|
| Arf_Arl |
cd00878 |
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ... |
62-224 |
3.48e-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: 38.71 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 62 GKSTLADRLLelTGTIDKTKKNKQVldklQVErergiTVKAQTASL-FYSFGGKQYLLNLIDtpghvdfSYEVSrslsaC 140
Cdd:cd00878 11 GKTTILYKLK--LGEVVTTIPTIGF----NVE-----TVEYKNVKFtVWDVGGQDKIRPLWK-------HYYEN-----T 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 141 QGVLLVVDANEGIQAQTVANFFLAF--EAQLSVIPVI---NKIDLKNADPERvgkQIEKVFDIPSE-----ECIKISAKL 210
Cdd:cd00878 68 DGLIFVVDSSDRERIEEAKNELHKLlnEEELKGAPLLilaNKQDLPGALTES---ELIELLGLESIkgrrwHIQPCSAVT 144
|
170
....*....|....
gi 27370038 211 GTNVDSVLQAVIER 224
Cdd:cd00878 145 GDGLDEGLDWLIEQ 158
|
|
| Obg |
cd01898 |
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ... |
140-225 |
5.08e-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: 38.17 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 140 CQGVLLVVDANEGIQAqtVANFFL------AFEAQLS---VIPVINKIDLkNADPERVGKQIEKVFDIPSEECIKISAKL 210
Cdd:cd01898 79 TRVLLHVIDLSGEDDP--VEDYETirneleAYNPGLAekpRIVVLNKIDL-LDAEERFEKLKELLKELKGKKVFPISALT 155
|
90
....*....|....*
gi 27370038 211 GTNVDSVLQAVIERI 225
Cdd:cd01898 156 GEGLDELLKKLAKLL 170
|
|
| RAS |
smart00173 |
Ras subfamily of RAS small GTPases; Similar in fold and function to the bacterial EF-Tu GTPase. ... |
113-225 |
6.27e-03 |
|
Ras subfamily of RAS small GTPases; Similar in fold and function to the bacterial EF-Tu GTPase. p21Ras couples receptor Tyr kinases and G protein receptors to protein kinase cascades
Pssm-ID: 214541 [Multi-domain] Cd Length: 164 Bit Score: 37.92 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 113 GKQYLLNLIDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFlafEAQLSV-----IPVI---NKIDLKNad 184
Cdd:smart00173 45 GEVCLLDILDTAGQEEFSAMRDQYMRTGEGFLLVYSITDRQSFEEIKKFR---EQILRVkdrddVPIVlvgNKCDLES-- 119
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 27370038 185 pERV-----GKQIEKVFDIPSEECikiSAKLGTNVDSVLQAVIERI 225
Cdd:smart00173 120 -ERVvsteeGKELARQWGCPFLET---SAKERVNVDEAFYDLVREI 161
|
|
| small_GTPase |
smart00010 |
Small GTPase of the Ras superfamily; ill-defined subfamily; SMART predicts Ras-like small ... |
113-225 |
7.04e-03 |
|
Small GTPase of the Ras superfamily; ill-defined subfamily; SMART predicts Ras-like small GTPases of the ARF, RAB, RAN, RAS, and SAR subfamilies. Others that could not be classified in this way are predicted to be members of the small GTPase superfamily without predictions of the subfamily.
Pssm-ID: 197466 [Multi-domain] Cd Length: 166 Bit Score: 37.92 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370038 113 GKQYLLNLIDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFlafEAQLSV-----IPVI---NKIDLKNad 184
Cdd:smart00010 47 GEVCLLDILDTAGQEEFSAMRDQYMRTGEGFLLVYSITDRQSFEEIAKFR---EQILRVkdrddVPIVlvgNKCDLEN-- 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 27370038 185 pERV-----GKQIEKVFDIPSEECikiSAKLGTNVDSVLQAVIERI 225
Cdd:smart00010 122 -ERVvsteeGKELARQWGCPFLET---SAKERINVDEAFYDLVREI 163
|
|
| |
