|
Name |
Accession |
Description |
Interval |
E-value |
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
41-644 |
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: 835.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 41 IPLENYRNFSIVAHVDHGKSTLSDRLLEITHVIDPNARNKQVLDKLEVERERGITIKAQTCSMFYKDKrTGKNYLLHLID 120
Cdd:COG0481 1 MDQKNIRNFSIIAHIDHGKSTLADRLLELTGTLSEREMKEQVLDSMDLERERGITIKAQAVRLNYKAK-DGETYQLNLID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 121 TPGHVDFRGEVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGLKLIPVINKIDLNFTDVKQVKDQIVNNFELPEED 200
Cdd:COG0481 80 TPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKQEIEDIIGIDASD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 201 IIGVSAKTGLNVEELLlPAIIDRIPPPTGRPDKPFRALLVDSWYDAYLGAVLLVNIVDGSVRKNDKVICAQTKEKYEVKD 280
Cdd:COG0481 160 AILVSAKTGIGIEEIL-EAIVERIPPPKGDPDAPLQALIFDSWYDSYRGVVVYVRVFDGTLKKGDKIKMMSTGKEYEVDE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 281 IGIMYPDRTSTGTLKTGQVGYLVLGMKDSKEAKIGDTIMHLSKvNETEVLPGFEEQKPMVFVGAFPADGIEFKAMDDDMS 360
Cdd:COG0481 239 VGVFTPKMTPVDELSAGEVGYIIAGIKDVRDARVGDTITLAKN-PAAEPLPGFKEVKPMVFAGLYPVDSDDYEDLRDALE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 361 RLVLNDRSVTLERETSNALGQGWRLGFLGSLHASVFRERLEKEYGSKLIITQPTVPYLVEFTDGKKKLITNPDEFPDgat 440
Cdd:COG0481 318 KLQLNDASLTYEPETSAALGFGFRCGFLGLLHMEIIQERLEREFDLDLITTAPSVVYEVTLTDGEVIEVDNPSDLPD--- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 441 kRVNVAAFHEPFIEAVMTLPQEYLGSVIRLCDSNRGEQIDITYLNTNgQVMLKYYLPLSHLVDDFFGKLKSVSRGFASLD 520
Cdd:COG0481 395 -PGKIEEIEEPIVKATIITPSEYVGAVMELCQEKRGVQKNMEYLGEN-RVELTYELPLAEIVFDFFDRLKSITRGYASLD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 521 YEDAGYRISDVVKLQLLVNGNAIDALSRVLHKSEVERVGREWVKKFKEYVKSQLYEVVIQARANNKIIARETIKARRKDV 600
Cdd:COG0481 473 YEFIGYRESDLVKLDILINGEPVDALSFIVHRDKAYSRGRALVEKLKELIPRQQFEVPIQAAIGGKIIARETIKALRKDV 552
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 6323320 601 LQKLHASDVSRRKKLLAKQKEGKKHMKTVGNIQINQEAYQAFLR 644
Cdd:COG0481 553 LAKCYGGDISRKRKLLEKQKEGKKRMKQVGNVEIPQEAFLAVLK 596
|
|
| lepA |
TIGR01393 |
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a ... |
44-644 |
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: 762.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 44 ENYRNFSIVAHVDHGKSTLSDRLLEITHVIDPNARNKQVLDKLEVERERGITIKAQTCSMFYKDKrTGKNYLLHLIDTPG 123
Cdd:TIGR01393 1 KNIRNFSIIAHIDHGKSTLADRLLEYTGAISEREMREQVLDSMDLERERGITIKAQAVRLNYKAK-DGETYVLNLIDTPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 124 HVDFRGEVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGLKLIPVINKIDLNFTDVKQVKDQIVNNFELPEEDIIG 203
Cdd:TIGR01393 80 HVDFSYEVSRSLAACEGALLLVDAAQGIEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKKEIEEVIGLDASEAIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 204 VSAKTGLNVEElLLPAIIDRIPPPTGRPDKPFRALLVDSWYDAYLGAVLLVNIVDGSVRKNDKVICAQTKEKYEVKDIGI 283
Cdd:TIGR01393 160 ASAKTGIGIEE-ILEAIVKRVPPPKGDPDAPLKALIFDSHYDNYRGVVALVRVFEGTIKPGDKIRFMSTGKEYEVDEVGV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 284 MYPDRTSTGTLKTGQVGYLVLGMKDSKEAKIGDTIMHlSKVNETEVLPGFEEQKPMVFVGAFPADGIEFKAMDDDMSRLV 363
Cdd:TIGR01393 239 FTPKLTKTDELSAGEVGYIIAGIKDVSDVRVGDTITH-VKNPAKEPLPGFKEVKPMVFAGLYPIDTEDYEDLRDALEKLK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 364 LNDRSVTLERETSNALGQGWRLGFLGSLHASVFRERLEKEYGSKLIITQPTVPYLVEFTDGKKKLITNPDEFPDgatkRV 443
Cdd:TIGR01393 318 LNDASLTYEPESSPALGFGFRCGFLGLLHMEIIQERLEREFNLDLITTAPSVIYRVYLTNGEVIEVDNPSDLPD----PG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 444 NVAAFHEPFIEAVMTLPQEYLGSVIRLCDSNRGEQIDITYLNTNgQVMLKYYLPLSHLVDDFFGKLKSVSRGFASLDYED 523
Cdd:TIGR01393 394 KIEHVEEPYVKATIITPTEYLGPIMTLCQEKRGVQTNMEYLDPN-RVELIYEMPLAEIVYDFFDKLKSISRGYASFDYEL 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 524 AGYRISDVVKLQLLVNGNAIDALSRVLHKSEVERVGREWVKKFKEYVKSQLYEVVIQARANNKIIARETIKARRKDVLQK 603
Cdd:TIGR01393 473 IGYRPSDLVKLDILINGEPVDALSFIVHRDKAYSRGREICEKLKELIPRQQFEIPIQAAIGGKIIARETIKALRKDVTAK 552
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 6323320 604 LHASDVSRRKKLLAKQKEGKKHMKTVGNIQINQEAYQAFLR 644
Cdd:TIGR01393 553 CYGGDITRKRKLLEKQKEGKKRMKQIGKVEVPQEAFLAVLK 593
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
47-227 |
1.86e-110 |
|
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: 329.49 E-value: 1.86e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 47 RNFSIVAHVDHGKSTLSDRLLEITHVIDPNARNKQVLDKLEVERERGITIKAQTCSMFYKDKrTGKNYLLHLIDTPGHVD 126
Cdd:cd01890 1 RNFSIIAHIDHGKSTLADRLLELTGTVSEREMKEQVLDSMDLERERGITIKAQAVRLFYKAK-DGEEYLLNLIDTPGHVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 127 FRGEVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGLKLIPVINKIDLNFTDVKQVKDQIVNNFELPEEDIIGVSA 206
Cdd:cd01890 80 FSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVKQEIEDVLGLDASEAILVSA 159
|
170 180
....*....|....*....|.
gi 6323320 207 KTGLNVEElLLPAIIDRIPPP 227
Cdd:cd01890 160 KTGLGVED-LLEAIVERIPPP 179
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
44-226 |
8.38e-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: 219.32 E-value: 8.38e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 44 ENYRNFSIVAHVDHGKSTLSDRLLEITHVIDPNARNKQ----VLDKLEVERERGITIKAQTCSMFYKDkrtgknYLLHLI 119
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGegeaGLDNLPEERERGITIKSAAVSFETKD------YLINLI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 120 DTPGHVDFRGEVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGLKLIPVINKIDL-NFTDVKQVKDQIVNNF--EL 196
Cdd:pfam00009 75 DTPGHVDFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRvDGAELEEVVEEVSRELleKY 154
|
170 180 190
....*....|....*....|....*....|....
gi 6323320 197 PEED----IIGVSAKTGLNVEElLLPAIIDRIPP 226
Cdd:pfam00009 155 GEDGefvpVVPGSALKGEGVQT-LLDALDEYLPS 187
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
46-515 |
2.51e-60 |
|
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, a GTP-binding protein, is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways, but the precise function is unknown. [Regulatory functions, Other, Cellular processes, Adaptations to atypical conditions, Protein synthesis, Translation factors]
Pssm-ID: 273597 [Multi-domain] Cd Length: 594 Bit Score: 211.78 E-value: 2.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 46 YRNFSIVAHVDHGKSTLSDRLLEITHVIDPN-ARNKQVLDKLEVERERGITIKAQTCSMFYKDkrtgknYLLHLIDTPGH 124
Cdd:TIGR01394 1 IRNIAIIAHVDHGKTTLVDALLKQSGTFRANeAVAERVMDSNDLERERGITILAKNTAIRYNG------TKINIVDTPGH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 125 VDFRGEVSRSYASCGGAILLVDASQGIQAQTvaNFYL--AFSLGLKLIPVINKIDLNFTDVKQVKDQIVNNF-ELPEED- 200
Cdd:TIGR01394 75 ADFGGEVERVLGMVDGVLLLVDASEGPMPQT--RFVLkkALELGLKPIVVINKIDRPSARPDEVVDEVFDLFaELGADDe 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 201 -----IIGVSAKTGLNVEEL---------LLPAIIDRIPPPTGRPDKPFRALLVDSWYDAYLGAVLLVNIVDGSVRKNDK 266
Cdd:TIGR01394 153 qldfpIVYASGRAGWASLDLddpsdnmapLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVHRGTVKKGQQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 267 VICA---QTKEKYEVKDI-GIMYPDRTSTGTLKTGQVgYLVLGMKDskeAKIGDTImhlSKVNETEVLPGFEEQKP---M 339
Cdd:TIGR01394 233 VALMkrdGTIENGRISKLlGFEGLERVEIDEAGAGDI-VAVAGLED---INIGETI---ADPEVPEALPTITVDEPtlsM 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 340 VF-VGAFPADGIEFKAMdddMSRLVlNDRsvtLERE--TSNAL-------GQGWRLGFLGSLHASVFRERLEKEyGSKLI 409
Cdd:TIGR01394 306 TFsVNDSPLAGKEGKKV---TSRHI-RDR---LMREleTNVALrvedtesADKFEVSGRGELHLSILIETMRRE-GFELQ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 410 ITQPTVPYLVEftDGKKklitnpdefpdgatkrvnvaafHEPFIEAVMTLPQEYLGSVIRLCDSNRGEQIDITYLNtNGQ 489
Cdd:TIGR01394 378 VGRPQVIYKEI--DGKK----------------------LEPIEELTIDVPEEHVGAVIEKLGKRKGEMVDMEPSG-NGR 432
|
490 500
....*....|....*....|....*.
gi 6323320 490 VMLKYYLPLSHLVdDFFGKLKSVSRG 515
Cdd:TIGR01394 433 TRLEFKIPSRGLI-GFRTEFLTDTRG 457
|
|
| LepA_C |
pfam06421 |
GTP-binding protein LepA C-terminus; This family consists of the C-terminal region of several ... |
538-644 |
3.86e-58 |
|
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: 190.69 E-value: 3.86e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 538 VNGNAIDALSRVLHKSEVERVGREWVKKFKEYVKSQLYEVVIQARANNKIIARETIKARRKDVLQKLHASDVSRRKKLLA 617
Cdd:pfam06421 1 INGEPVDALSFIVHRSKAYRRGRALVEKLKELIPRQQFEVPIQAAIGGKIIARETIKALRKDVTAKCYGGDISRKKKLLE 80
|
90 100
....*....|....*....|....*..
gi 6323320 618 KQKEGKKHMKTVGNIQINQEAYQAFLR 644
Cdd:pfam06421 81 KQKEGKKRMKQIGNVEIPQEAFLAVLK 107
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
44-497 |
6.11e-56 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 200.25 E-value: 6.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 44 ENYRNFSIVAHVDHGKSTLSDRLLEITHVIDPNAR-NKQVLDKLEVERERGITIKAQTCSMFYKDkrtgknYLLHLIDTP 122
Cdd:COG1217 4 EDIRNIAIIAHVDHGKTTLVDALLKQSGTFRENQEvAERVMDSNDLERERGITILAKNTAVRYKG------VKINIVDTP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 123 GHVDFRGEVSRSYASCGGAILLVDASQGIQAQTvaNFYL--AFSLGLKLIPVINKIDLNFTDVKQVKDQIvnnFEL---- 196
Cdd:COG1217 78 GHADFGGEVERVLSMVDGVLLLVDAFEGPMPQT--RFVLkkALELGLKPIVVINKIDRPDARPDEVVDEV---FDLfiel 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 197 --PEED----IIGVSAKTG---LNVEEL------LLPAIIDRIPPPTGRPDKPFRALLVDSWYDAYLGAVLLVNIVDGSV 261
Cdd:COG1217 153 gaTDEQldfpVVYASARNGwasLDLDDPgedltpLFDTILEHVPAPEVDPDGPLQMLVTNLDYSDYVGRIAIGRIFRGTI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 262 RKNDKVICAQtkekyevkdigimypdrtSTGTLKTGQV----GYLVLGMKDSKEAK--------------IGDTIMHlsk 323
Cdd:COG1217 233 KKGQQVALIK------------------RDGKVEKGKItklfGFEGLERVEVEEAEagdivaiagiedinIGDTICD--- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 324 VNETEVLPGFEEQKP---MVF-VGAFPADGIEFKAMdddMSRlVLNDRsvtLERET-SN-AL-------GQGWRLGFLGS 390
Cdd:COG1217 292 PENPEALPPIKIDEPtlsMTFsVNDSPFAGREGKFV---TSR-QIRER---LEKELeTNvALrveetdsPDAFKVSGRGE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 391 LHASVFRERLEKEyGSKLIITQPTVPYLVEftDGKKklitnpdefpdgatkrvnvaafHEPFIEAVMTLPQEYLGSVIRL 470
Cdd:COG1217 365 LHLSILIETMRRE-GYELQVSRPEVIFKEI--DGKK----------------------LEPIEELTIDVPEEYSGAVIEK 419
|
490 500
....*....|....*....|....*..
gi 6323320 471 CDSNRGEQIDITYlNTNGQVMLKYYLP 497
Cdd:COG1217 420 LGQRKGEMTNMEP-DGGGRVRLEFLIP 445
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
48-227 |
1.67e-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: 167.86 E-value: 1.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 48 NFSIVAHVDHGKSTLSDRLLEITHVIDPNARNKQ-VLDKLEVERERGITIKAQTCSMFYKDKRtgknylLHLIDTPGHVD 126
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKEtFLDTLKEERERGITIKTGVVEFEWPKRR------INFIDTPGHED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 127 FRGEVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGLKLIPVINKIDLN-FTDVKQVKDQIVNNFELPEED----- 200
Cdd:cd00881 75 FSKETVRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVgEEDFDEVLREIKELLKLIGFTflkgk 154
|
170 180 190
....*....|....*....|....*....|
gi 6323320 201 ---IIGVSAKTGLNVEElLLPAIIDRIPPP 227
Cdd:cd00881 155 dvpIIPISALTGEGIEE-LLDAIVEHLPPP 183
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
45-227 |
1.59e-42 |
|
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: 151.98 E-value: 1.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 45 NYRNFSIVAHVDHGKSTLSDRLLEITHVIDPNAR-NKQVLDKLEVERERGITIKAQTCSMFYKDKRtgknylLHLIDTPG 123
Cdd:cd01891 1 KIRNIAIIAHVDHGKTTLVDALLKQSGTFRENEEvGERVMDSNDLERERGITILAKNTAITYKDTK------INIIDTPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 124 HVDFRGEVSRSYASCGGAILLVDASQGIQAQTvaNFYL--AFSLGLKLIPVINKIDLNFTDVKQVKDQIVNNF-ELPEED 200
Cdd:cd01891 75 HADFGGEVERVLSMVDGVLLLVDASEGPMPQT--RFVLkkALEAGLKPIVVINKIDRPDARPEEVVDEVFDLFlELNATD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6323320 201 ------IIGVSAKTGLNVEEL---------LLPAIIDRIPPP 227
Cdd:cd01891 153 eqldfpIVYASAKNGWASLNLddpsedldpLFETIIEHVPAP 194
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
47-177 |
2.64e-42 |
|
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: 152.00 E-value: 2.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 47 RNFSIVAHVDHGKSTLSDRLLEITHVIDP-NARNKQVLDKLEVERERGITIKAQTCSMFYK---DKRTGKNYLLHLIDTP 122
Cdd:cd01885 1 RNICIIAHVDHGKTTLSDSLLASAGIISEkLAGKARYLDTREDEQERGITIKSSAISLYFEyeeEKMDGNDYLINLIDSP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 6323320 123 GHVDFRGEVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGLKLIPVINKID 177
Cdd:cd01885 81 GHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKID 135
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
43-502 |
1.73e-39 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 153.71 E-value: 1.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 43 LENYRNFSIVAHVDHGKSTLSDRLLEITHVIDPNARNKQ-VLDKLEVERERGITIKAQTCSMFYKDkrtgknYLLHLIDT 121
Cdd:PRK10218 2 IEKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQErVMDSNDLEKERGITILAKNTAIKWND------YRINIVDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 122 PGHVDFRGEVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGLKLIPVINKIDLNFTDVKQVKDQIVN---NFELPE 198
Cdd:PRK10218 76 PGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDlfvNLDATD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 199 ED----IIGVSAKTGL------NVEELLLP---AIIDRIPPPTGRPDKPFRALLVDSWYDAYLGAVLLVNIVDGSVRKND 265
Cdd:PRK10218 156 EQldfpIVYASALNGIagldheDMAEDMTPlyqAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 266 KVICAQTKEKYEVKDIGIMYP----DRTSTGTLKTGQvgylVLGMKDSKEAKIGDTIMHLSKVnetEVLPGFEEQKPMV- 340
Cdd:PRK10218 236 QVTIIDSEGKTRNAKVGKVLGhlglERIETDLAEAGD----IVAITGLGELNISDTVCDTQNV---EALPALSVDEPTVs 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 341 ---FVGAFPADGIEFKAMD-----DDMSRLVLNDRSVTLErETSNAlgQGWRLGFLGSLHASVFRERLEKEyGSKLIITQ 412
Cdd:PRK10218 309 mffCVNTSPFCGKEGKFVTsrqilDRLNKELVHNVALRVE-ETEDA--DAFRVSGRGELHLSVLIENMRRE-GFELAVSR 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 413 PTVpyLVEFTDGKKKlitnpdefpdgatkrvnvaafhEPFIEAVMTLPQEYLGSVIRLCDSNRGeqiDITYLNTNGQ--V 490
Cdd:PRK10218 385 PKV--IFREIDGRKQ----------------------EPYENVTLDVEEQHQGSVMQALGERKG---DLKNMNPDGKgrV 437
|
490
....*....|..
gi 6323320 491 MLKYYLPLSHLV 502
Cdd:PRK10218 438 RLDYVIPSRGLI 449
|
|
| EF4_II |
cd03699 |
Domain II of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly ... |
235-320 |
6.67e-39 |
|
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: 137.93 E-value: 6.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 235 FRALLVDSWYDAYLGAVLLVNIVDGSVRKNDKVICAQTKEKYEVKDIGIMYPDRTSTGTLKTGQVGYLVLGMKDSKEAKI 314
Cdd:cd03699 1 LRALIFDSWYDPYRGVVVLVRVFDGTLKKGDKIRFMATGKEYEVLEVGVFTPKMVPTDELSAGEVGYIIAGIKSVKDARV 80
|
....*.
gi 6323320 315 GDTIMH 320
Cdd:cd03699 81 GDTITL 86
|
|
| lepA_C |
cd03709 |
lepA_C: This family represents the C-terminal region of LepA, a GTP-binding protein localized ... |
450-530 |
8.69e-39 |
|
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: 137.62 E-value: 8.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 450 EPFIEAVMTLPQEYLGSVIRLCDSNRGEQIDITYLNTNgQVMLKYYLPLSHLVDDFFGKLKSVSRGFASLDYEDAGYRIS 529
Cdd:cd03709 1 EPFVKATIITPSEYLGAIMELCQERRGVQKDMEYLDAN-RVMLTYELPLAEIVYDFFDKLKSISKGYASLDYELIGYRES 79
|
.
gi 6323320 530 D 530
Cdd:cd03709 80 D 80
|
|
| EF4_III |
cd16260 |
Domain III of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly ... |
338-413 |
1.21e-37 |
|
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: 134.16 E-value: 1.21e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323320 338 PMVFVGAFPADGIEFKAMDDDMSRLVLNDRSVTLERETSNALGQGWRLGFLGSLHASVFRERLEKEYGSKLIITQP 413
Cdd:cd16260 1 PMVFAGLYPVDGSDYEELRDALEKLTLNDASVTFEPETSSALGFGFRCGFLGLLHMEVFQERLEREYGLDLIITAP 76
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
32-417 |
6.84e-36 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 143.85 E-value: 6.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 32 QKLQAQIEQIplenyRNFSIVAHVDHGKSTLSDRLLEITHVIDPNARNKQ-VLDKLEVERERGITIKAQTCSMFYKDKrt 110
Cdd:PRK07560 11 LELMKNPEQI-----RNIGIIAHIDHGKTTLSDNLLAGAGMISEELAGEQlALDFDEEEQARGITIKAANVSMVHEYE-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 111 GKNYLLHLIDTPGHVDFRGEVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGLKLIPVINKID-------LNFTDV 183
Cdd:PRK07560 84 GKEYLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKPVLFINKVDrlikelkLTPQEM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 184 KQVKDQIVNNF-EL-----PEEDI--------------------IGVS----AKTGL------------NVEEL------ 215
Cdd:PRK07560 164 QQRLLKIIKDVnKLikgmaPEEFKekwkvdvedgtvafgsalynWAISvpmmQKTGIkfkdiidyyekgKQKELaekapl 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 216 ---LLPAIIDRIPPP-------------------------TGRPDKPFRALLVDSWYDAYLGAVLLVNIVDGSVRKNDKV 267
Cdd:PRK07560 244 hevVLDMVVKHLPNPieaqkyripkiwkgdlnsevgkamlNCDPNGPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 268 ICAQTKEKYEVKDIGI-MYPDRTSTGTLKTGQVGYlVLGMKDskeAKIGDTIMHLSKVNETEVLPGFEEqkPMVFVgafp 346
Cdd:PRK07560 324 YLVGAKKKNRVQQVGIyMGPEREEVEEIPAGNIAA-VTGLKD---ARAGETVVSVEDMTPFESLKHISE--PVVTV---- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 347 adGIEFKAMdDDMSRLVLNDRSVTLE---------RETSNALGQGwrlgfLGSLHASVFRERLEKEYGSKLIITQPTVPY 417
Cdd:PRK07560 394 --AIEAKNP-KDLPKLIEVLRQLAKEdptlvvkinEETGEHLLSG-----MGELHLEVITYRIKRDYGIEVVTSEPIVVY 465
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
40-417 |
8.36e-36 |
|
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: 143.65 E-value: 8.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 40 QIPLENYRNFSIVAHVDHGKSTLSDRLLEITHVI-------DPNArnkqVLDKLEVERERGITIKAQTCSMFYKDKRtgk 112
Cdd:COG0480 3 EYPLEKIRNIGIVAHIDAGKTTLTERILFYTGAIhrigevhDGNT----VMDWMPEEQERGITITSAATTCEWKGHK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 113 nylLHLIDTPGHVDFRGEVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGLKLIPVINKID---LNFTD-VKQVKD 188
Cdd:COG0480 76 ---INIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDregADFDRvLEQLKE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 189 ---------QIV----NNF------------------------------------------------------------- 194
Cdd:COG0480 153 rlganpvplQLPigaeDDFkgvidlvtmkayvyddelgakyeeeeipaelkeeaeeareelieavaetddelmekylege 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 195 ELPEEDIIG----------------VSAKTGLNVEELL------LPAIIDRiPPPTGR-------------PDKPFRALL 239
Cdd:COG0480 233 ELTEEEIKAglrkatlagkivpvlcGSAFKNKGVQPLLdavvdyLPSPLDV-PAIKGVdpdtgeeverkpdDDEPFSALV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 240 VDSWYDAYLGAVLLVNIVDGSVRKNDKVICAQT--KEKyevkdIGIMY----PDRTSTGTLKTGQVGYLVlGMKDskeAK 313
Cdd:COG0480 312 FKTMTDPFVGKLSFFRVYSGTLKSGSTVYNSTKgkKER-----IGRLLrmhgNKREEVDEAGAGDIVAVV-KLKD---TT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 314 IGDTimhLSKVNETEVLPGFEEQKPMVFVGAFPADgiefKAMDDDMS----RLVLNDRSVTLER--ETsnalGQ----Gw 383
Cdd:COG0480 383 TGDT---LCDEDHPIVLEPIEFPEPVISVAIEPKT----KADEDKLStalaKLAEEDPTFRVETdeET----GQtiisG- 450
|
490 500 510
....*....|....*....|....*....|....
gi 6323320 384 rlgfLGSLHASVFRERLEKEYGSKLIITQPTVPY 417
Cdd:COG0480 451 ----MGELHLEIIVDRLKREFGVEVNVGKPQVAY 480
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
42-526 |
2.43e-32 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 132.77 E-value: 2.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 42 PLENYRNFSIVAHVDHGKSTLSDRLLEITHVI-------DPNArnkqVLDKLEVERERGITIKAQTCSMFYKdkrtgkNY 114
Cdd:PRK13351 4 PLMQIRNIGILAHIDAGKTTLTERILFYTGKIhkmgeveDGTT----VTDWMPQEQERGITIESAATSCDWD------NH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 115 LLHLIDTPGHVDFRGEVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGLKLIPVINKIDLNFTDVKQVKDQIVNNF 194
Cdd:PRK13351 74 RINLIDTPGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLFKVLEDIEERF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 195 -------ELP---EEDIIGV------------------------------------------------------------ 204
Cdd:PRK13351 154 gkrplplQLPigsEDGFEGVvdlitepelhfsegdggstveegpipeelleeveearekliealaefddellelylegee 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 205 -------------------------SAKTGLNVEElLLPAIID------RIPPPTGR------------PDKPFRALLVD 241
Cdd:PRK13351 234 lsaeqlraplregtrsghlvpvlfgSALKNIGIEP-LLDAVVDylpsplEVPPPRGSkdngkpvkvdpdPEKPLLALVFK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 242 SWYDAYLGAVLLVNIVDGSVRKNDKVICAQTKEKYEVKDIGIMYPD-RTSTGTLKTGQVGyLVLGMkdsKEAKIGDTimh 320
Cdd:PRK13351 313 VQYDPYAGKLTYLRVYSGTLRAGSQLYNGTGGKREKVGRLFRLQGNkREEVDRAKAGDIV-AVAGL---KELETGDT--- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 321 LSKVNETEVLPGFEEQKPMVFVgafpadGIEFKAMDDD------MSRLVLNDRSVTLER--ETSNALGQGwrlgfLGSLH 392
Cdd:PRK13351 386 LHDSADPVLLELLTFPEPVVSL------AVEPERRGDEqklaeaLEKLVWEDPSLRVEEdeETGQTILSG-----MGELH 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 393 ASVFRERLEKEYGSKLIITQPTVPYL---------VEF----TDGKK-----KLITNPDE-------------------- 434
Cdd:PRK13351 455 LEVALERLRREFKLEVNTGKPQVAYRetirkmaegVYRhkkqFGGKGqfgevHLRVEPLErgagfifvskvvggaipeel 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 435 -------------------FP---------DGATKRVN----------VAAFHEPFIEAVMTL-----------PQEYLG 465
Cdd:PRK13351 535 ipavekgirealasgplagYPvtdlrvtvlDGKYHPVDssesafkaaaRKAFLEAFRKANPVLlepimeleitvPTEHVG 614
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323320 466 SVIRLCDSNRGeQIDITYLNTNGQVMLKYYLPLSHLvDDFFGKLKSVSRGFASLDYEDAGY 526
Cdd:PRK13351 615 DVLGDLSQRRG-RIEGTEPRGDGEVLVKAEAPLAEL-FGYATRLRSMTKGRGSFTMEFSHF 673
|
|
| EF-G |
TIGR00484 |
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ... |
41-467 |
4.72e-32 |
|
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: 132.24 E-value: 4.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 41 IPLENYRNFSIVAHVDHGKSTLSDRLLEIT---HVIDPNARNKQVLDKLEVERERGITIKAQTCSMFYKDKRtgknylLH 117
Cdd:TIGR00484 5 TDLNRFRNIGISAHIDAGKTTTTERILFYTgriHKIGEVHDGAATMDWMEQEKERGITITSAATTVFWKGHR------IN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 118 LIDTPGHVDFRGEVSRSYASCGGAILLVDASQGIQAQTV------------------------ANFY-----LAFSLGLK 168
Cdd:TIGR00484 79 IIDTPGHVDFTVEVERSLRVLDGAVAVLDAVGGVQPQSEtvwrqanryevpriafvnkmdktgANFLrvvnqIKQRLGAN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 169 LIPV----------INKIDL------NF-------TDVKQVKDQIV-------NNF-------------------ELPEE 199
Cdd:TIGR00484 159 AVPIqlpigaednfIGVIDLvemkayFFngdkgtkAIEKEIPSDLLeqakelrENLveavaefdeelmekylegeELTIE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 200 DIIGVSAKTGLNVE---------------ELLLPAIIDRIPPPTGRP-------------------DKPFRALLVDSWYD 245
Cdd:TIGR00484 239 EIKNAIRKGVLNCEffpvlcgsafknkgvQLLLDAVVDYLPSPTDVPaikgidpdtekeierkasdDEPFSALAFKVATD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 246 AYLGAVLLVNIVDGSVRKNDKVICAQTKEKYEVKDIGIMYPDRTStgTLKTGQVGYLV--LGMKDskeAKIGDTimhLSK 323
Cdd:TIGR00484 319 PFVGQLTFVRVYSGVLKSGSYVKNSRKNKKERVGRLVKMHANNRE--EIKEVRAGDICaaIGLKD---TTTGDT---LCD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 324 VNETEVLPGFEEQKPMVFVGAFPADGIEFKAMDDDMSRLVLNDRS--VTLERETSNALGQGwrlgfLGSLHASVFRERLE 401
Cdd:TIGR00484 391 PKIDVILERMEFPEPVISLAVEPKTKADQEKMGIALGKLAEEDPTfrTFTDPETGQTIIAG-----MGELHLDIIVDRMK 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323320 402 KEYGSKLIITQPTVPYLVEFTDGKKKLITNPDEfPDGATKRVNVAAFHEP-------FIEAVM--TLPQEYLGSV 467
Cdd:TIGR00484 466 REFKVEANVGAPQVAYRETIRSKVEVEGKHAKQ-SGGRGQYGHVKIRFEPlepkgyeFVNEIKggVIPREYIPAV 539
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
47-493 |
1.70e-31 |
|
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: 130.40 E-value: 1.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 47 RNFSIVAHVDHGKSTLSDRLLEITHVIDPNARNKQV-LDKLEVERERGITIKAQTCSMFYKDKrtGKNYLLHLIDTPGHV 125
Cdd:TIGR00490 20 RNIGIVAHIDHGKTTLSDNLLAGAGMISEELAGQQLyLDFDEQEQERGITINAANVSMVHEYE--GNEYLINLIDTPGHV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 126 DFRGEVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGLKLIPVINKIDLNFTDVKQVKDQ-------IVNNFE--- 195
Cdd:TIGR00490 98 DFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKPVLFINKVDRLINELKLTPQElqerfikIITEVNkli 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 196 ---LPEE-------DIIGVSA-----------------KTGLN---------------------VEELLLPAIIDRIPPP 227
Cdd:TIGR00490 178 kamAPEEfrdkwkvRVEDGSVafgsayynwaisvpsmkKTGIGfkdiykyckedkqkelakkspLHQVVLDMVIRHLPSP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 228 -------------------TGR------PDKPFRALLVDSWYDAYLGAVLLVNIVDGSVRKNDKVICAQTKEKYEVKDIG 282
Cdd:TIGR00490 258 ieaqkyripviwkgdlnseVGKamlncdPKGPLALMITKIVVDKHAGEVAVGRLYSGTIRPGMEVYIVDRKAKARIQQVG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 283 I-MYPDRTSTGTLKTGQVGYLVlGMKDskeAKIGDTImhlskVNETEVLPGFEEQK----PMVFVGAFPADGIEFKAMDD 357
Cdd:TIGR00490 338 VyMGPERVEVDEIPAGNIVAVI-GLKD---AVAGETI-----CTTVENITPFESIKhisePVVTVAIEAKNTKDLPKLIE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 358 DMSRLVLNDRS--VTLERETSNALGQGwrlgfLGSLHASVFRERLEKEYGSKLIITQPTVPY---------LVEFTDGKK 426
Cdd:TIGR00490 409 VLRQVAKEDPTvhVEINEETGEHLISG-----MGELHLEIIVEKIREDYGLDVETSPPIVVYretvtgtspVVEGKSPNK 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 427 K----LITNPDE-----------FPDGATKRVNVAafhEPFIEAVMTlPQE-------YLGSVirLCDSNRGeqidITYL 484
Cdd:TIGR00490 484 HnrfyIVVEPLEesviqafkegkIVDMKMKKKERR---RLLIEAGMD-SEEaarveeyYEGNL--FINMTRG----IQYL 553
|
....*....
gi 6323320 485 NTNGQVMLK 493
Cdd:TIGR00490 554 DETKELILE 562
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
48-193 |
1.90e-31 |
|
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: 122.34 E-value: 1.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 48 NFSIVAHVDHGKSTLSDRLLEITHVIDP-------NARnkqvLDKLEVERERGITIKAQTCSMFYKDKRtgknylLHLID 120
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIRElgsvdkgTTR----TDSMELERQRGITIFSAVASFQWEDTK------VNIID 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323320 121 TPGHVDFRGEVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGLKLIPVINKIDLNFTDVKQVKDQIVNN 193
Cdd:cd04168 71 TPGHMDFIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTIIFVNKIDRAGADLEKVYQEIKEK 143
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
52-417 |
1.63e-29 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 124.08 E-value: 1.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 52 VAHVDHGKSTLSDRLLEITHVI-------DPNArnkqVLDKLEVERERGITIKAQTCSMFYKDKRtgknylLHLIDTPGH 124
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIhrigeveDGTT----TMDFMPEERERGISITSAATTCEWKGHK------INLIDTPGH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 125 VDFRGEVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGLKLIPVINKID---LNFTDV-KQVKD---------QI- 190
Cdd:PRK12740 71 VDFTGEVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDragADFFRVlAQLQEklgapvvplQLp 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 191 ---VNNF-----------------------------------------------------------ELPEEDIIG----- 203
Cdd:PRK12740 151 igeGDDFtgvvdllsmkayrydeggpseeieipaelldraeeareellealaefddelmekylegeELSEEEIKAglrka 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 204 -----------VSAKTGLNVEELL------LPAIIDRIPPPTGR----------PDKPFRALLVDSWYDAYLGAVLLVNI 256
Cdd:PRK12740 231 tlageivpvfcGSALKNKGVQRLLdavvdyLPSPLEVPPVDGEDgeegaelapdPDGPLVALVFKTMDDPFVGKLSLVRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 257 VDGSVRKNDKVICAQTKEKyeVKdIGIMY----PDRTSTGTLKTGQVGYLVlGMKDskeAKIGDTimhLSKVNETEVLPG 332
Cdd:PRK12740 311 YSGTLKKGDTLYNSGTGKK--ER-VGRLYrmhgKQREEVDEAVAGDIVAVA-KLKD---AATGDT---LCDKGDPILLEP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 333 FEEQKPMVFVGAFPADgiefKAMDDDMS----RLVLNDRSVTLER--ETSNALGQGwrlgfLGSLHASVFRERLEKEYGS 406
Cdd:PRK12740 381 MEFPEPVISLAIEPKD----KGDEEKLSealgKLAEEDPTLRVERdeETGQTILSG-----MGELHLDVALERLKREYGV 451
|
490
....*....|.
gi 6323320 407 KLIITQPTVPY 417
Cdd:PRK12740 452 EVETGPPQVPY 462
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
37-194 |
2.65e-29 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 124.01 E-value: 2.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 37 QIEQI------PlENYRNFSIVAHVDHGKSTLSDRLLEITHVI-DPNARNKQVLDKLEVERERGITIKAQTCSMFY---- 105
Cdd:PTZ00416 5 TVDQIreimdnP-DQIRNMSVIAHVDHGKSTLTDSLVCKAGIIsSKNAGDARFTDTRADEQERGITIKSTGISLYYehdl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 106 KDKRTGKNYLLHLIDTPGHVDFRGEVSRSYASCGGAILLVDASQG--IQAQTVanfyLAFSLGLKLIPV--INKIDLNFT 181
Cdd:PTZ00416 84 EDGDDKQPFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGvcVQTETV----LRQALQERIRPVlfINKVDRAIL 159
|
170
....*....|...
gi 6323320 182 DVKQVKDQIVNNF 194
Cdd:PTZ00416 160 ELQLDPEEIYQNF 172
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
47-177 |
2.70e-29 |
|
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: 115.44 E-value: 2.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 47 RNFSIVAHVDHGKSTLSDRLLEITHVIDPNARNKQV----LDKLEVERERGITIKAQTCSMFYKDKRtGKNYLLHLIDTP 122
Cdd:cd04167 1 RNVCIAGHLHHGKTSLLDMLIEQTHKRTPSVKLGWKplryTDTRKDEQERGISIKSNPISLVLEDSK-GKSYLINIIDTP 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 6323320 123 GHVDFRGEVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGLKLIPVINKID 177
Cdd:cd04167 80 GHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKID 134
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
45-194 |
2.03e-28 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 121.37 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 45 NYRNFSIVAHVDHGKSTLSDRLLEITHVID-PNARNKQVLDKLEVERERGITIKAQTCSMFY----------KDKRTGKN 113
Cdd:PLN00116 18 NIRNMSVIAHVDHGKSTLTDSLVAAAGIIAqEVAGDVRMTDTRADEAERGITIKSTGISLYYemtdeslkdfKGERDGNE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 114 YLLHLIDTPGHVDFRGEVSRSYASCGGAILLVDASQG--IQAQTVanfyLAFSLGLKLIPV--INKIDLNFTDVKQVKDQ 189
Cdd:PLN00116 98 YLINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGvcVQTETV----LRQALGERIRPVltVNKMDRCFLELQVDGEE 173
|
....*
gi 6323320 190 IVNNF 194
Cdd:PLN00116 174 AYQTF 178
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
48-281 |
5.23e-27 |
|
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: 113.87 E-value: 5.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 48 NFSIVAHVDHGKSTLSDRLLEITHVIDPN----------ARNKQ------VLDKLEVERERGITIkaqtcSMFYKDKRTG 111
Cdd:COG5256 9 NLVVIGHVDHGKSTLVGRLLYETGAIDEHiiekyeeeaeKKGKEsfkfawVMDRLKEERERGVTI-----DLAHKKFETD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 112 KNYLLhLIDTPGHVDFRGE--VSRSYASCggAILLVDASQGIQAQTVANFYLAFSLGLK-LIPVINKIDL-NFTD--VKQ 185
Cdd:COG5256 84 KYYFT-IIDAPGHRDFVKNmiTGASQADA--AILVVSAKDGVMGQTREHAFLARTLGINqLIVAVNKMDAvNYSEkrYEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 186 VKDQIVN-----NFELPEEDIIGVSAKTGLNVEEL-----------LLPAiIDRIPPPTGRPDKPFRALLVDSWYDAYLG 249
Cdd:COG5256 161 VKEEVSKllkmvGYKVDKIPFIPVSAWKGDNVVKKsdnmpwyngptLLEA-LDNLKEPEKPVDKPLRIPIQDVYSISGIG 239
|
250 260 270
....*....|....*....|....*....|..
gi 6323320 250 AVLLVNIVDGSVRKNDKVICAQTKEKYEVKDI 281
Cdd:COG5256 240 TVPVGRVETGVLKVGDKVVFMPAGVVGEVKSI 271
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
48-194 |
4.24e-26 |
|
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: 107.96 E-value: 4.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 48 NFSIVAHVDHGKSTLSDRLL-------EITHVIDPNArnkqVLDKLEVERERGITIKAQTCSMFYKDKRtgknylLHLID 120
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILyytgrihKIGEVHGGGA----TMDWMEQERERGITIQSAATTCFWKDHR------INIID 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323320 121 TPGHVDFRGEVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGLKLIPVINKIDLNFTDVKQVKDQIVNNF 194
Cdd:cd01886 71 TPGHVDFTIEVERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQIREKL 144
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
48-281 |
5.67e-23 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 101.93 E-value: 5.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 48 NFSIVAHVDHGKSTLSDRLLEITHVIDPN--------ARNKQ--------VLDKLEVERERGITIkaqtcSMFYKDKRTG 111
Cdd:PRK12317 8 NLAVIGHVDHGKSTLVGRLLYETGAIDEHiieelreeAKEKGkesfkfawVMDRLKEERERGVTI-----DLAHKKFETD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 112 KnYLLHLIDTPGHVDFRGEVSRSYASCGGAILLVDA--SQGIQAQTVANFYLAFSLGLK-LIPVINKIDL-NFT--DVKQ 185
Cdd:PRK12317 83 K-YYFTIVDCPGHRDFVKNMITGASQADAAVLVVAAddAGGVMPQTREHVFLARTLGINqLIVAINKMDAvNYDekRYEE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 186 VKDQIVN-----NFELPEEDIIGVSAKTGLNVEEL-----------LLPAiIDRIPPPTGRPDKPFRALLVDSWYDAYLG 249
Cdd:PRK12317 162 VKEEVSKllkmvGYKPDDIPFIPVSAFEGDNVVKKsenmpwyngptLLEA-LDNLKPPEKPTDKPLRIPIQDVYSISGVG 240
|
250 260 270
....*....|....*....|....*....|..
gi 6323320 250 AVLLVNIVDGSVRKNDKVICAQTKEKYEVKDI 281
Cdd:PRK12317 241 TVPVGRVETGVLKVGDKVVFMPAGVVGEVKSI 272
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
48-212 |
3.16e-22 |
|
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: 95.33 E-value: 3.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 48 NFSIVAHVDHGKSTLSDRLLEITHVI-----------DPNARNKQ------VLDKLEVERERGITIKAqTCSMFYKDKRT 110
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSIfedqlaalersKSSGTQGEkldlalLVDGLQAEREQGITIDV-AYRYFSTPKRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 111 gknYLLhlIDTPGHVDF-RGEVSRSyASCGGAILLVDASQGIQAQTVANFYLAFSLGLK-LIPVINKIDLN------FTD 182
Cdd:cd04166 80 ---FII--ADTPGHEQYtRNMVTGA-STADLAILLVDARKGVLEQTRRHSYIASLLGIRhVVVAVNKMDLVdydeevFEE 153
|
170 180 190
....*....|....*....|....*....|
gi 6323320 183 VKQVKDQIVNNFELPEEDIIGVSAKTGLNV 212
Cdd:cd04166 154 IKADYLAFAASLGIEDITFIPISALEGDNV 183
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
51-216 |
1.25e-20 |
|
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: 89.45 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 51 IVAHVDHGKSTLSDRLleithvidpnaRNKQVldkleVERE-RGIT--IKAQTCSMFYKDKRtgknylLHLIDTPGHVDF 127
Cdd:cd01887 5 VMGHVDHGKTTLLDKI-----------RKTNV-----AAGEaGGITqhIGAYQVPIDVKIPG------ITFIDTPGHEAF 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 128 -----RGevsrsyASCGG-AILLVDASQGIQAQTVANFYLAFSLGLKLIPVINKIDLNFT---DVKQVKDQIVNNFELPE 198
Cdd:cd01887 63 tnmraRG------ASVTDiAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKPYGteaDPERVKNELSELGLVGE 136
|
170 180
....*....|....*....|...
gi 6323320 199 E---DIIGV--SAKTGLNVEELL 216
Cdd:cd01887 137 EwggDVSIVpiSAKTGEGIDDLL 159
|
|
| Elongation_Factor_C |
cd01514 |
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ... |
450-530 |
7.23e-20 |
|
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of elongation factors (EFs) bacterial EF-G, eukaryotic and archeal EF-2 and eukaryotic mitochondrial mtEFG1s and mtEFG2s. This group also includes proteins similar to the ribosomal protection proteins Tet(M) and Tet(O), BipA, LepA and, spliceosomal proteins: human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and yeast counterpart Snu114p. This domain adopts a ferredoxin-like fold consisting of an alpha-beta sandwich with anti-parallel beta-sheets, resembling the topology of domain III found in the elongation factors EF-G and eukaryotic EF-2, with which it forms the C-terminal block. The two domains however are not superimposable and domain III lacks some of the characteristics of this domain. EF-2/EF-G in complex with GTP, promotes the translocation step of translation. During translocation the peptidyl-tRNA is moved from the A site to the P site, the uncharged tRNA from the P site to the E-site and, the mRNA is shifted one codon relative to the ribosome. Tet(M) and Tet(O) mediate Tc resistance. Typical Tcs bind to the ribosome and inhibit the elongation phase of protein synthesis, by inhibiting the occupation of site A by aminoacyl-tRNA. Tet(M) and Tet(O) catalyze the release of tetracycline (Tc) from the ribosome in a GTP-dependent manner. BipA is a highly conserved protein with global regulatory properties in Escherichia coli. Yeast Snu114p is essential for cell viability and for splicing in vivo. Experiments suggest that GTP binding and probably GTP hydrolysis is important for the function of the U5-116 kD/Snu114p. The function of LepA proteins is unknown.
Pssm-ID: 238772 [Multi-domain] Cd Length: 79 Bit Score: 84.07 E-value: 7.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 450 EPFIEAVMTLPQEYLGSVIRLCDSNRGEQIDITYLNTnGQVMLKYYLPLSHLVdDFFGKLKSVSRGFASLDYEDAGYRIS 529
Cdd:cd01514 1 EPIMKVEITVPEEYLGAVIGDLSKRRGEILGMEPRGT-GRVVIKAELPLAEMF-GFATDLRSLTQGRASFSMEFSHYEPV 78
|
.
gi 6323320 530 D 530
Cdd:cd01514 79 P 79
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
54-228 |
3.04e-19 |
|
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: 85.35 E-value: 3.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 54 HVDHGKSTLSDRLleithvidpnarNKQVLDKLEVERERGITIKaqtCSMFYKDKRTGKNylLHLIDTPGHVDFrgeVSR 133
Cdd:cd04171 7 HIDHGKTTLIKAL------------TGIETDRLPEEKKRGITID---LGFAYLDLPDGKR--LGFIDVPGHEKF---VKN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 134 SYASCGG---AILLVDASQGIQAQTVANFYLAFSLGLK-LIPVINKIDLNFTD-VKQVKDQIVNNFE---LPEEDIIGVS 205
Cdd:cd04171 67 MLAGAGGidaVLLVVAADEGIMPQTREHLEILELLGIKkGLVVLTKADLVDEDrLELVEEEILELLAgtfLADAPIFPVS 146
|
170 180
....*....|....*....|...
gi 6323320 206 AKTGLNVEELLlpAIIDRIPPPT 228
Cdd:cd04171 147 SVTGEGIEELK--NYLDELAEPQ 167
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
48-236 |
5.52e-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: 89.76 E-value: 5.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 48 NFSIVAHVDHGKSTLSDRLLEITHVI----------DPNARNKQ------VLDKLEVERERGITIK-AQTcsMFYKDKRT 110
Cdd:COG2895 19 RFITCGSVDDGKSTLIGRLLYDTKSIfedqlaalerDSKKRGTQeidlalLTDGLQAEREQGITIDvAYR--YFSTPKRK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 111 gknYLlhLIDTPGHVDF-R----GevsrsyAS-CGGAILLVDASQGIQAQTVANFYLAFSLGLK-LIPVINKIDL-NFTd 182
Cdd:COG2895 97 ---FI--IADTPGHEQYtRnmvtG------AStADLAILLIDARKGVLEQTRRHSYIASLLGIRhVVVAVNKMDLvDYS- 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323320 183 vKQVKDQIVNNF-----ELPEEDI--IGVSAKTGLNVEE------------LLlpAIIDRIPPPTGRPDKPFR 236
Cdd:COG2895 165 -EEVFEEIVADYrafaaKLGLEDItfIPISALKGDNVVErsenmpwydgptLL--EHLETVEVAEDRNDAPFR 234
|
|
| EFG_C |
pfam00679 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
449-535 |
7.36e-19 |
|
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of Elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopt a ferredoxin-like fold.
Pssm-ID: 425814 [Multi-domain] Cd Length: 88 Bit Score: 81.44 E-value: 7.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 449 HEPFIEAVMTLPQEYLGSVIRLCDSNRGEQIDITYlNTNGQVMLKYYLPLSHLVdDFFGKLKSVSRGFASLDYEDAGYRI 528
Cdd:pfam00679 3 LEPIEKVTIDVPEEYVGDVISDLNSRRGEILDMDP-DDGGRVVIEAEVPLAELF-GFATELRSLTKGRGSFSMEFSGYQP 80
|
....*..
gi 6323320 529 SDVVKLQ 535
Cdd:pfam00679 81 VPGDILD 87
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
48-281 |
7.65e-19 |
|
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: 90.32 E-value: 7.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 48 NFSIVAHVDHGKSTLSDRLLEIThvidpnarnkqvLDKLEVERERGITIKAQTCSMFYKDKRTGknyllhLIDTPGHVDF 127
Cdd:TIGR00475 2 IIATAGHVDHGKTTLLKALTGIA------------ADRLPEEKKRGMTIDLGFAYFPLPDYRLG------FIDVPGHEKF 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 128 RGEVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGLK-LIPVINKID-LNFTDVKQVKD---QIVNNFE-LPEEDI 201
Cdd:TIGR00475 64 ISNAIAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPhTIVVITKADrVNEEEIKRTEMfmkQILNSYIfLKNAKI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 202 IGVSAKTGLNVEEL--LLPAIIDRIppPTGRPDKPFRaLLVDSWYDAY-LGAVLLVNIVDGSVRKNDKVICAQTKEKYEV 278
Cdd:TIGR00475 144 FKTSAKTGQGIGELkkELKNLLESL--DIKRIQKPLR-MAIDRAFKVKgAGTVVTGTAFSGEVKVGDNLRLLPINHEVRV 220
|
...
gi 6323320 279 KDI 281
Cdd:TIGR00475 221 KAI 223
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
48-227 |
1.14e-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: 85.24 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 48 NFSIVAHVDHGKSTLSDRLLEITHVIDP--------NARNKQ--------VLDKLEVERERGITIKAQTCSMFYKDKRtg 111
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKrtiekyekEAKEMGkesfkyawVLDKLKEERERGVTIDVGLAKFETEKYR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 112 knylLHLIDTPGHVDFrgeVSR-----SYASCggAILLVDASQG-------IQAQTVANFYLAFSLGLK-LIPVINKIDL 178
Cdd:cd01883 79 ----FTIIDAPGHRDF---VKNmitgaSQADV--AVLVVSARKGefeagfeKGGQTREHALLARTLGVKqLIVAVNKMDD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 179 NFTDVKQVK-DQIVNNFEL-------PEEDI--IGVSAKTGLNVEEL-----------LLPAiIDRIPPP 227
Cdd:cd01883 150 VTVNWSQERyDEIKKKVSPflkkvgyNPKDVpfIPISGFTGDNLIEKsenmpwykgptLLEA-LDSLEPP 218
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
48-281 |
1.23e-17 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 85.95 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 48 NFSIVAHVDHGKSTLSDRLLEITHVIDPNARNK----------------QVLDKLEVERERGITIKAQTCsmfykdKRTG 111
Cdd:PTZ00141 9 NLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKfekeaaemgkgsfkyaWVLDKLKAERERGITIDIALW------KFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 112 KNYLLHLIDTPGHVDFRGEVSRSYASCGGAILLVDASQGI-------QAQTVANFYLAFSLGLK-LIPVINKID---LNF 180
Cdd:PTZ00141 83 PKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEfeagiskDGQTREHALLAFTLGVKqMIVCINKMDdktVNY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 181 TD------VKQVKDQIVNNFELPEE-DIIGVSAKTGLNVEE-----------LLLPAiIDRIPPPTgRP-DKPFRALLVD 241
Cdd:PTZ00141 163 SQerydeiKKEVSAYLKKVGYNPEKvPFIPISGWQGDNMIEksdnmpwykgpTLLEA-LDTLEPPK-RPvDKPLRLPLQD 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 6323320 242 SWYDAYLGAVLLVNIVDGSVRKNDKVICAQTKEKYEVKDI 281
Cdd:PTZ00141 241 VYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSV 280
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
50-314 |
8.57e-17 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 84.50 E-value: 8.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 50 SIVAHVDHGKSTLSDRLleithvidpnaRNKQVLDKlEVErerGIT--IKAQTCSMFYKDKrtgkNYLLHLIDTPGHVDF 127
Cdd:CHL00189 248 TILGHVDHGKTTLLDKI-----------RKTQIAQK-EAG---GITqkIGAYEVEFEYKDE----NQKIVFLDTPGHEAF 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 128 RGEVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGLKLIPVINKIDLNFTDVKQVKDQIVNNFELPEE-----DII 202
Cdd:CHL00189 309 SSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANTERIKQQLAKYNLIPEKwggdtPMI 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 203 GVSAKTGLNVEELL-----LPAIIDRIPPPTgrpdKPFRALLVDSWYDAYLGAVLLVNIVDGSVRKNDKVICAQTKEKYE 277
Cdd:CHL00189 389 PISASQGTNIDKLLetillLAEIEDLKADPT----QLAQGIILEAHLDKTKGPVATILVQNGTLHIGDIIVIGTSYAKIR 464
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 6323320 278 V------KDIGIMYPDRTST--GTLKTGQVGYLVLGMKDSKEAKI 314
Cdd:CHL00189 465 GminslgNKINLATPSSVVEiwGLSSVPATGEHFQVFNSEKEAKL 509
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
51-216 |
1.80e-16 |
|
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: 77.11 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 51 IVAHVDHGKSTLSDRLLEITHVIdpnarnkqvldkleVERERGITIKAQTCSMFYKDKrtgkNYLLHLIDTPGHVDFRG- 129
Cdd:cd00882 2 VVGRGGVGKSSLLNALLGGEVGE--------------VSDVPGTTRDPDVYVKELDKG----KVKLVLVDTPGLDEFGGl 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 130 ----EVSRSYASCGGAILLVDASQGIQAQTVANFYLA--FSLGLKLIPVINKIDLNFTDVKQVKDQIVNNFELPEEDIIG 203
Cdd:cd00882 64 greeLARLLLRGADLILLVVDSTDRESEEDAKLLILRrlRKEGIPIILVGNKIDLLEEREVEELLRLEELAKILGVPVFE 143
|
170
....*....|...
gi 6323320 204 VSAKTGLNVEELL 216
Cdd:cd00882 144 VSAKTGEGVDELF 156
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
48-307 |
2.73e-15 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 78.71 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 48 NFSIVAHVDHGKSTLSDrllEITHVIDPNARNKQV----LDKLEVERERGITIkaQTCSMFYKdkrTGKNYLLHlIDTPG 123
Cdd:PLN03127 63 NVGTIGHVDHGKTTLTA---AITKVLAEEGKAKAVafdeIDKAPEEKARGITI--ATAHVEYE---TAKRHYAH-VDCPG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 124 HVDFRGEVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGL-KLIPVINKIDLnfTDVKQVKD-------QIVNNFE 195
Cdd:PLN03127 134 HADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVpSLVVFLNKVDV--VDDEELLElvemelrELLSFYK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 196 LPEEDI-----IGVSAKTGLNvEEL-------LLPAIIDRIPPPTGRPDKPFRALLVDSWYDAYLGAVLLVNIVDGSVRK 263
Cdd:PLN03127 212 FPGDEIpiirgSALSALQGTN-DEIgknailkLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKV 290
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 6323320 264 NDKVicaqtkekyEVKDIGIMYPDRTS-TG------TLKTGQ----VGYLVLGMK 307
Cdd:PLN03127 291 GEEV---------EIVGLRPGGPLKTTvTGvemfkkILDQGQagdnVGLLLRGLK 336
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
48-190 |
2.83e-15 |
|
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: 76.48 E-value: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 48 NFSIVAHVDHGKSTLSDRLLEITHVIDPNARNKQ---VLDKLEVERERGITIKAQTCSMFYKDKRtgknylLHLIDTPGH 124
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRLGRVEDgntVSDYDPEEKKRKMSIETSVAPLEWNGHK------INLIDTPGY 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323320 125 VDFRGEVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGLKLIPVINKIDLNFTDVKQVKDQI 190
Cdd:cd04170 75 ADFVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRARADFDKTLAAL 140
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
48-209 |
3.47e-15 |
|
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: 74.32 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 48 NFSIVAHVDHGKSTLSDRLLEIThvidpnarNKQVLDKLEVERERGITIKAQTcSMFYKDKRTG---------KNYLLHL 118
Cdd:cd01889 2 NVGLLGHVDSGKTSLAKALSEIA--------STAAFDKNPQSQERGITLDLGF-SSFEVDKPKHlednenpqiENYQITL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 119 IDTPGHVDF-RGEVsrsyascGGA------ILLVDASQGIQAQTVANFYLAFSLGLKLIPVINKIDLNFTDVKQVKDQIV 191
Cdd:cd01889 73 VDCPGHASLiRTII-------GGAqiidlmLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDLIPEEERKRKIEKM 145
|
170 180
....*....|....*....|....*.
gi 6323320 192 --------NNFELPEEDIIGVSAKTG 209
Cdd:cd01889 146 kkrlqktlEKTRLKDSPIIPVSAKPG 171
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
54-241 |
4.16e-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: 78.80 E-value: 4.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 54 HVDHGKSTLSDRLLEIthviDPnarnkqvlDKLEVERERGITIK---AQTcsmfykdkRTGKNYLLHLIDTPGHVDFrge 130
Cdd:COG3276 8 HIDHGKTTLVKALTGI----DT--------DRLKEEKKRGITIDlgfAYL--------PLPDGRRLGFVDVPGHEKF--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 131 VSRSYASCGG---AILLVDASQGIQAQT-----VANFylafsLGLK-LIPVINKIDLnfTD---VKQVKDQI---VNNFE 195
Cdd:COG3276 65 IKNMLAGAGGidlVLLVVAADEGVMPQTrehlaILDL-----LGIKrGIVVLTKADL--VDeewLELVEEEIrelLAGTF 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6323320 196 LPEEDIIGVSAKTGLNVEELL--LPAIIDRIPPPtgRPDKPFRaLLVD 241
Cdd:COG3276 138 LEDAPIVPVSAVTGEGIDELRaaLDALAAAVPAR--DADGPFR-LPID 182
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
50-313 |
1.82e-14 |
|
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: 76.73 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 50 SIVAHVDHGKSTLSDRLleithvidpnaRNKQVldkleVERER-GIT--IKAQTCSMFYKDKRTgknyllhLIDTPGHVD 126
Cdd:TIGR00487 91 TIMGHVDHGKTSLLDSI-----------RKTKV-----AQGEAgGITqhIGAYHVENEDGKMIT-------FLDTPGHEA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 127 FRGEVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGLKLIPVINKIDLNFTDVKQVKDQIVNNFELPEE-----DI 201
Cdd:TIGR00487 148 FTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVPIIVAINKIDKPEANPDRVKQELSEYGLVPEDwggdtIF 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 202 IGVSAKTGLNVEELL-LPAIIDRIPPPTGRPDKPFRALLVDSWYDAYLGAVLLVNIVDGSVRKNDKVIC--------AQT 272
Cdd:TIGR00487 228 VPVSALTGDGIDELLdMILLQSEVEELKANPNGQASGVVIEAQLDKGRGPVATVLVQSGTLRVGDIVVVgaaygrvrAMI 307
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 6323320 273 KEK-YEVKDIGIMYPDRTsTGTLKTGQVGYLVLGMKDSKEAK 313
Cdd:TIGR00487 308 DENgKSVKEAGPSKPVEI-LGLSDVPAAGDEFIVFKDEKDAR 348
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
48-307 |
8.80e-14 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 74.27 E-value: 8.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 48 NFSIVAHVDHGKSTLSDRL-LEITHVIDPNARNKQVLDKLEVERERGITIKAQTCsmfykDKRTGKNYLLHlIDTPGHVD 126
Cdd:PLN03126 83 NIGTIGHVDHGKTTLTAALtMALASMGGSAPKKYDEIDAAPEERARGITINTATV-----EYETENRHYAH-VDCPGHAD 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 127 FRGEVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGL-KLIPVINKIDlnftdvkQVKD------------QIVNN 193
Cdd:PLN03126 157 YVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVpNMVVFLNKQD-------QVDDeellelvelevrELLSS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 194 FELPEEDIIGVSAKTGLNVEEL-------------------LLPAIIDRIPPPTGRPDKPFRALLVDSWYDAYLGAVLLV 254
Cdd:PLN03126 230 YEFPGDDIPIISGSALLALEALmenpnikrgdnkwvdkiyeLMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATG 309
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 6323320 255 NIVDGSVRKNDKVICAQTKEKYEVKDIGIMYPDRTSTGTLKTGQVGYLVLGMK 307
Cdd:PLN03126 310 RVERGTVKVGETVDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQ 362
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
48-267 |
8.95e-14 |
|
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: 73.66 E-value: 8.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 48 NFSIVAHVDHGKSTLSdrlLEITHVI----DPNARNKQVLDKLEVERERGITIKAQTCsmfykDKRTGKNYLLHlIDTPG 123
Cdd:TIGR00485 14 NVGTIGHVDHGKTTLT---AAITTVLakegGAAARAYDQIDNAPEEKARGITINTAHV-----EYETETRHYAH-VDCPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 124 HVDFRGEVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGLKLIPV-INKIDLnfTDVKQVKD-------QIVNNFE 195
Cdd:TIGR00485 85 HADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKCDM--VDDEELLElvemevrELLSQYD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 196 LPEED--IIGVSAKTGLNVEEL-------LLPAIIDRIPPPTGRPDKPFRALLVDSWYDAYLGAVLLVNIVDGSVRKNDK 266
Cdd:TIGR00485 163 FPGDDtpIIRGSALKALEGDAEweakileLMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEE 242
|
.
gi 6323320 267 V 267
Cdd:TIGR00485 243 V 243
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
46-215 |
2.43e-13 |
|
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: 68.17 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 46 YRNFSIVAHVDHGKSTLSDRLLeithvidpnaRNKQVldklEVERERGITIKAQTCSMFYKdkrtGKNYLLHLIDTPGHV 125
Cdd:TIGR00231 1 DIKIVIVGHPNVGKSTLLNSLL----------GNKGS----ITEYYPGTTRNYVTTVIEED----GKTYKFNLLDTAGQE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 126 DFRG-------EVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSlGLKLIPVINKIDLNFTDVKQVKDQIVNNfeLPE 198
Cdd:TIGR00231 63 DYDAirrlyypQVERSLRVFDIVILVLDVEEILEKQTKEIIHHADS-GVPIILVGNKIDLKDADLKTHVASEFAK--LNG 139
|
170
....*....|....*..
gi 6323320 199 EDIIGVSAKTGLNVEEL 215
Cdd:TIGR00231 140 EPIIPLSAETGKNIDSA 156
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
48-235 |
3.19e-13 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 71.90 E-value: 3.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 48 NFSIVAHVDHGKSTLSdrlLEITHVIDPNARNKQV----LDKLEVERERGITIkaQTCSMFYKdkrTGKNYLLHlIDTPG 123
Cdd:PRK12736 14 NIGTIGHVDHGKTTLT---AAITKVLAERGLNQAKdydsIDAAPEEKERGITI--NTAHVEYE---TEKRHYAH-VDCPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 124 HVDFRGEVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGLKLIPV-INKIDLnfTDVKQVKD-------QIVNNFE 195
Cdd:PRK12736 85 HADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVfLNKVDL--VDDEELLElvemevrELLSEYD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6323320 196 LPEED--IIGVSAKTGLN--------VEElLLPAIIDRIPPPTGRPDKPF 235
Cdd:PRK12736 163 FPGDDipVIRGSALKALEgdpkwedaIME-LMDAVDEYIPTPERDTDKPF 211
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
55-212 |
2.42e-12 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 69.56 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 55 VDHGKSTLSDRLLEITHVI----------DPNARNKQ--------VLDKLEVERERGITIKAQTcSMFYKDKRTgknyll 116
Cdd:PRK05124 36 VDDGKSTLIGRLLHDTKQIyedqlaslhnDSKRHGTQgekldlalLVDGLQAEREQGITIDVAY-RYFSTEKRK------ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 117 hLI--DTPGHVDFrgevSRSYAS----CGGAILLVDASQGIQAQTVANFYLAFSLGLK-LIPVINKIDL-NFTdvKQVKD 188
Cdd:PRK05124 109 -FIiaDTPGHEQY----TRNMATgastCDLAILLIDARKGVLDQTRRHSFIATLLGIKhLVVAVNKMDLvDYS--EEVFE 181
|
170 180 190
....*....|....*....|....*....|..
gi 6323320 189 QIVNNF-----ELPEE-DI--IGVSAKTGLNV 212
Cdd:PRK05124 182 RIREDYltfaeQLPGNlDIrfVPLSALEGDNV 213
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
54-178 |
4.60e-12 |
|
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: 65.30 E-value: 4.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 54 HVDHGKSTLSDrllEITHVI----DPNARNKQVLDKLEVERERGITIkaQTCSMFYKdkrTGKNYLLHlIDTPGHVDFRG 129
Cdd:cd01884 10 HVDHGKTTLTA---AITKVLakkgGAKAKKYDEIDKAPEEKARGITI--NTAHVEYE---TANRHYAH-VDCPGHADYIK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 6323320 130 EVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGLKLIPV-INKIDL 178
Cdd:cd01884 81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVfLNKADM 130
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
55-212 |
4.67e-12 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 69.19 E-value: 4.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 55 VDHGKSTLSDRLLEITHVI----------DPNARNKQ--------VLDKLEVERERGITIKAQTcSMFYKDKRTgknyll 116
Cdd:PRK05506 33 VDDGKSTLIGRLLYDSKMIfedqlaalerDSKKVGTQgdeidlalLVDGLAAEREQGITIDVAY-RYFATPKRK------ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 117 hLI--DTPGHVDFRGEVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGLKLIPV-INKIDLNFTDvKQVKDQIVNN 193
Cdd:PRK05506 106 -FIvaDTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLaVNKMDLVDYD-QEVFDEIVAD 183
|
170 180
....*....|....*....|....*.
gi 6323320 194 F-----ELPEEDI--IGVSAKTGLNV 212
Cdd:PRK05506 184 YrafaaKLGLHDVtfIPISALKGDNV 209
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
48-242 |
9.22e-12 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 67.18 E-value: 9.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 48 NFSIVAHVDHGKSTLSDRLleiTHVIdpnarnkqvLDKLEVERERGITIK---AQTcsMFYKDKRTGKN--Y-------- 114
Cdd:PRK04000 11 NIGMVGHVDHGKTTLVQAL---TGVW---------TDRHSEELKRGITIRlgyADA--TIRKCPDCEEPeaYttepkcpn 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 115 ------LLH---LIDTPGHvdfrgEVSRSYASCG-----GAILLVDASQGI-QAQTVANFYLAFSLGLK-LIPVINKIDL 178
Cdd:PRK04000 77 cgseteLLRrvsFVDAPGH-----ETLMATMLSGaalmdGAILVIAANEPCpQPQTKEHLMALDIIGIKnIVIVQNKIDL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323320 179 --------NFTDVKQ-VKDQIVNNFElpeedIIGVSAKTGLNVEeLLLPAIIDRIPPPTGRPDKPFRALLVDS 242
Cdd:PRK04000 152 vskeraleNYEQIKEfVKGTVAENAP-----IIPVSALHKVNID-ALIEAIEEEIPTPERDLDKPPRMYVARS 218
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
48-281 |
1.00e-11 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 67.42 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 48 NFSIVAHVDHGKSTLSDRLLEITHVIDPNA----------RNKQ------VLDKLEVERERGITIKAQtcsmFYKDKRTg 111
Cdd:PLN00043 9 NIVVIGHVDSGKSTTTGHLIYKLGGIDKRVierfekeaaeMNKRsfkyawVLDKLKAERERGITIDIA----LWKFETT- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 112 kNYLLHLIDTPGHVDFRGEVSRSYASCGGAILLVDASQG-------IQAQTVANFYLAFSLGLK-LIPVINKIDLNFTDV 183
Cdd:PLN00043 84 -KYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGgfeagisKDGQTREHALLAFTLGVKqMICCCNKMDATTPKY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 184 KQVK-DQIV------------NNFELPEEDIIGVSA----KTGLNVEELLLPAI---IDRIPPPTGRPDKPFRALLVDSW 243
Cdd:PLN00043 163 SKARyDEIVkevssylkkvgyNPDKIPFVPISGFEGdnmiERSTNLDWYKGPTLleaLDQINEPKRPSDKPLRLPLQDVY 242
|
250 260 270
....*....|....*....|....*....|....*...
gi 6323320 244 YDAYLGAVLLVNIVDGSVRKNDKVICAQTKEKYEVKDI 281
Cdd:PLN00043 243 KIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSV 280
|
|
| tufA |
CHL00071 |
elongation factor Tu |
48-267 |
1.38e-11 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 66.90 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 48 NFSIVAHVDHGKSTLSdrlLEITHVI----DPNARNKQVLDKLEVERERGITIKaqTCSMFYKdkrTGKNYLLHlIDTPG 123
Cdd:CHL00071 14 NIGTIGHVDHGKTTLT---AAITMTLaakgGAKAKKYDEIDSAPEEKARGITIN--TAHVEYE---TENRHYAH-VDCPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 124 HVDFRGEVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGLKLIPV-INKIDlnftdvkQVKD------------QI 190
Cdd:CHL00071 85 HADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVfLNKED-------QVDDeellelvelevrEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 191 VNNFELPEEDIIGVSAKTGLNVEELLLPAIIDR-------------------IPPPTGRPDKPFRALLVDSWYDAYLGAV 251
Cdd:CHL00071 158 LSKYDFPGDDIPIVSGSALLALEALTENPKIKRgenkwvdkiynlmdavdsyIPTPERDTDKPFLMAIEDVFSITGRGTV 237
|
250
....*....|....*.
gi 6323320 252 LLVNIVDGSVRKNDKV 267
Cdd:CHL00071 238 ATGRIERGTVKVGDTV 253
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
54-235 |
2.77e-11 |
|
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: 65.94 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 54 HVDHGKSTLSdrlLEITHVIDPNARNKQV----LDKLEVERERGITIkaQTCSMFYKdkrTGKNYLLHlIDTPGHVDFRG 129
Cdd:COG0050 20 HVDHGKTTLT---AAITKVLAKKGGAKAKaydqIDKAPEEKERGITI--NTSHVEYE---TEKRHYAH-VDCPGHADYVK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 130 EVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGLKLIPV-INKIDLnftdvkqVKDQ------------IVNNFEL 196
Cdd:COG0050 91 NMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKCDM-------VDDEellelvemevreLLSKYGF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6323320 197 PEED--IIGVSAKTGLNVEEL---------LLPAIIDRIPPPTGRPDKPF 235
Cdd:COG0050 164 PGDDtpIIRGSALKALEGDPDpewekkileLMDAVDSYIPEPERDTDKPF 213
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
58-215 |
6.58e-11 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 61.54 E-value: 6.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 58 GKSTLSDRLLEithvidpnarnkqvlDKLEVERE---RGITIKAQTCSMFYKDKRtgknylLHLIDTPGHVDFRgEVSRS 134
Cdd:COG1100 15 GKTSLVNRLVG---------------DIFSLEKYlstNGVTIDKKELKLDGLDVD------LVIWDTPGQDEFR-ETRQF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 135 YAS----CGGAILLVDASqgIQAQTVANFYLA---FSLGLK--LIPVINKIDLnFTDVKQVKDQIVNNF--ELPEEDIIG 203
Cdd:COG1100 73 YARqltgASLYLFVVDGT--REETLQSLYELLeslRRLGKKspIILVLNKIDL-YDEEEIEDEERLKEAlsEDNIVEVVA 149
|
170
....*....|..
gi 6323320 204 VSAKTGLNVEEL 215
Cdd:COG1100 150 TSAKTGEGVEEL 161
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
54-235 |
7.98e-11 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 64.44 E-value: 7.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 54 HVDHGKSTLSdrlLEITHVIDPNARNKQV----LDKLEVERERGITIkaQTCSMFYKdkrTGKNYLLHlIDTPGHVDFRG 129
Cdd:PRK00049 20 HVDHGKTTLT---AAITKVLAKKGGAEAKaydqIDKAPEEKARGITI--NTAHVEYE---TEKRHYAH-VDCPGHADYVK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 130 EVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGLKLIPV-INKIDlnftdvkQVKD------------QIVNNFEL 196
Cdd:PRK00049 91 NMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVfLNKCD-------MVDDeellelvemevrELLSKYDF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6323320 197 PEED--IIGVSAKTGLN----------VEElLLPAIIDRIPPPTGRPDKPF 235
Cdd:PRK00049 164 PGDDtpIIRGSALKALEgdddeewekkILE-LMDAVDSYIPTPERAIDKPF 213
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
48-235 |
2.62e-10 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 62.55 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 48 NFSIVAHVDHGKSTLSdrlLEITHVIDP----NARNKQVLDKLEVERERGITIkaQTCSMFYKdkrTGKNYLLHlIDTPG 123
Cdd:PRK12735 14 NVGTIGHVDHGKTTLT---AAITKVLAKkgggEAKAYDQIDNAPEEKARGITI--NTSHVEYE---TANRHYAH-VDCPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 124 HVDFRGEVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGLKLIPV-INKIDlnftdvkQVKD------------QI 190
Cdd:PRK12735 85 HADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVfLNKCD-------MVDDeellelvemevrEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6323320 191 VNNFELPEED--IIGVSAKTGLN----------VEElLLPAIIDRIPPPTGRPDKPF 235
Cdd:PRK12735 158 LSKYDFPGDDtpIIRGSALKALEgdddeeweakILE-LMDAVDSYIPEPERAIDKPF 213
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
58-216 |
6.70e-10 |
|
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: 58.03 E-value: 6.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 58 GKSTLSDRLLeithvidpnarNKQVLdklEVERERGITIKAQTCSMFYKDKRTgknylLHLIDTPGHVD------FRGEV 131
Cdd:cd00880 9 GKSSLLNALL-----------GQNVG---IVSPIPGTTRDPVRKEWELLPLGP-----VVLIDTPGLDEegglgrERVEE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 132 SRS-YASCGGAILLVDASQGIQAQtVANFYLAFSLGLKLIPVINKIDL-NFTDVKQVKDQIVNNFeLPEEDIIGVSAKTG 209
Cdd:cd00880 70 ARQvADRADLVLLVVDSDLTPVEE-EAKLGLLRERGKPVLLVLNKIDLvPESEEEELLRERKLEL-LPDLPVIAVSALPG 147
|
....*..
gi 6323320 210 LNVEELL 216
Cdd:cd00880 148 EGIDELR 154
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
54-272 |
8.03e-10 |
|
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: 61.57 E-value: 8.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 54 HVDHGKSTLSDRLleithvidpnaRNKQVldkleVERE-RGIT--IKAqtcsmfYKDKRTGKNylLHLIDTPGHVDF--- 127
Cdd:COG0532 12 HVDHGKTSLLDAI-----------RKTNV-----AAGEaGGITqhIGA------YQVETNGGK--ITFLDTPGHEAFtam 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 128 RgevSRsyascgGA------ILLVDASQGIQAQTV--------AnfylafslGLKLIPVINKIDLNFTDVKQVKDQIVNn 193
Cdd:COG0532 68 R---AR------GAqvtdivILVVAADDGVMPQTIeainhakaA--------GVPIIVAINKIDKPGANPDRVKQELAE- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 194 FEL-PEE---DII--GVSAKTGLNVEELL-----------LPAIidrippptgrPDKPFRALLVDSWYDAYLGAV--LLV 254
Cdd:COG0532 130 HGLvPEEwggDTIfvPVSAKTGEGIDELLemillqaevleLKAN----------PDRPARGTVIEAKLDKGRGPVatVLV 199
|
250
....*....|....*...
gi 6323320 255 NivDGSVRKNDKVICAQT 272
Cdd:COG0532 200 Q--NGTLKVGDIVVAGTA 215
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
112-216 |
1.94e-09 |
|
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: 56.73 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 112 KNYLLHLIDTPGhvdFRGE--------VSRSYASCGGA---ILLVDASQGIQAQTVANfyLAFSLGLKLIPVINKIDLnf 180
Cdd:cd04164 49 GGIPVRLIDTAG---LRETedeiekigIERAREAIEEAdlvLLVVDASEGLDEEDLEI--LELPAKKPVIVVLNKSDL-- 121
|
90 100 110
....*....|....*....|....*....|....*.
gi 6323320 181 tdvkqvKDQIVNNFELPEEDIIGVSAKTGLNVEELL 216
Cdd:cd04164 122 ------LSDAEGISELNGKPIIAISAKTGEGIDELK 151
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
47-177 |
2.67e-09 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 60.15 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 47 RNFSIVAHVDHGKSTLSDRLLEITHVIDP----NAR---NKQVLDKLEVERERGITIkaqTCS---MFYKDKRtgknylL 116
Cdd:PRK00741 11 RTFAIISHPDAGKTTLTEKLLLFGGAIQEagtvKGRksgRHATSDWMEMEKQRGISV---TSSvmqFPYRDCL------I 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323320 117 HLIDTPGHVDFRGEVSRSYASCGGAILLVDASQGIQAQTvanfylafslgLKLIPV-----------INKID 177
Cdd:PRK00741 82 NLLDTPGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQT-----------RKLMEVcrlrdtpiftfINKLD 142
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
249-318 |
3.96e-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: 3.96e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323320 249 GAVLLVNIVDGSVRKNDKV--ICAQTKEKYEVKDIGIMYPDRTSTGTLKTGQVGYLVLGMKDSKEAKIGDTI 318
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVriLPNGTGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTL 72
|
|
| EFG_III-like |
cd16257 |
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G ... |
338-411 |
6.25e-08 |
|
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: 50.04 E-value: 6.25e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323320 338 PMVFVGAFPADGIEFKAMDDDMSRLVLNDRSVTLERETSNalgQGWRLGFLGSLHASVFRERLEKEYGSKLIIT 411
Cdd:cd16257 1 PVVFVTVEVKNPLDQEKLLEGLERLSEEDPALQVYREEST---GEFILSGLGELHLEIIVARLEREYGVELVVS 71
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
54-241 |
3.12e-07 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 53.52 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 54 HVDHGKSTLsdrLLEITHVidpNArnkqvlDKLEVERERGITIKAQTCSMFYKDKRtgknyLLHLIDTPGHVDFrgeVSR 133
Cdd:PRK10512 8 HVDHGKTTL---LQAITGV---NA------DRLPEEKKRGMTIDLGYAYWPQPDGR-----VLGFIDVPGHEKF---LSN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 134 SYASCGG---AILLVDASQGIQAQT---VANFYLAFSLGLKLipVINKIDL-NFTDVKQVKDQI---VNNFELPEEDIIG 203
Cdd:PRK10512 68 MLAGVGGidhALLVVACDDGVMAQTrehLAILQLTGNPMLTV--ALTKADRvDEARIAEVRRQVkavLREYGFAEAKLFV 145
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6323320 204 VSAKTGLNVEEL---LLpaiidRIPPPTGRPDKPFRaLLVD 241
Cdd:PRK10512 146 TAATEGRGIDALrehLL-----QLPEREHAAQHRFR-LAID 180
|
|
| MnmE_helical |
pfam12631 |
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ... |
112-216 |
4.19e-07 |
|
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: 52.48 E-value: 4.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 112 KNYLLHLIDTPGhvdFRGE--------VSRSYASCGGA---ILLVDASQGIQAQTvANFYLAFSLGLKLIPVINKIDLnf 180
Cdd:pfam12631 140 GGIPLRLIDTAG---IRETddevekigIERAREAIEEAdlvLLVLDASRPLDEED-LEILELLKDKKPIIVVLNKSDL-- 213
|
90 100 110
....*....|....*....|....*....|....*.
gi 6323320 181 tdvkqvKDQIVNNFELPEEDIIGVSAKTGLNVEELL 216
Cdd:pfam12631 214 ------LGEIDELEELKGKPVLAISAKTGEGLDELE 243
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
50-274 |
1.93e-06 |
|
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: 50.97 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 50 SIVAHVDHGKSTLSDRLL----------EITHVIDPNARNKQVLDKLEVERERGITIKAQTCSMFYkdkrtgknyllhlI 119
Cdd:TIGR00491 8 VVLGHVDHGKTTLLDKIRgtavvkkeagGITQHIGASEVPTDVIEKICGDLLKSFKIKLKIPGLLF-------------I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 120 DTPGHVDFRGEVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGLKLIPVINKID-------------LNFTD---- 182
Cdd:TIGR00491 75 DTPGHEAFTNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTPFVVAANKIDripgwkshegypfLESINkqeq 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 183 -VKQVKDQIVNNF--ELPEED-----------------IIGVSAKTGLNVEELL--LPAIIDRIPPPTGR--PDKPFRAL 238
Cdd:TIGR00491 155 rVRQNLDKQVYNLviQLAEQGfnaerfdrirdftktvaIIPVSAKTGEGIPELLaiLAGLAQNYLENKLKlaIEGPAKGT 234
|
250 260 270
....*....|....*....|....*....|....*.
gi 6323320 239 LVDSWYDAYLGAVLLVNIVDGSVRKNDKVICAQTKE 274
Cdd:TIGR00491 235 ILEVKEEQGLGYTIDAVIYDGILRKGDIIVLAGIDD 270
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
45-222 |
2.78e-06 |
|
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: 47.81 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 45 NYRNFSIVAHVDHGKSTLSDRLLEITHVIdpnarnkqvldkleVERERGITIKAQTCSMFYKdkrtGKNYLLhlIDTPG- 123
Cdd:cd01895 1 DPIKIAIIGRPNVGKSSLLNALLGEERVI--------------VSDIAGTTRDSIDVPFEYD----GQKYTL--IDTAGi 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 124 --------HVDFRGeVSRSYASCGGA---ILLVDASQGI--QAQTVANFylAFSLGLKLIPVINKIDL---NFTDVKQVK 187
Cdd:cd01895 61 rkkgkvteGIEKYS-VLRTLKAIERAdvvLLVLDASEGIteQDLRIAGL--ILEEGKALIIVVNKWDLvekDEKTMKEFE 137
|
170 180 190
....*....|....*....|....*....|....*...
gi 6323320 188 DQIvnNFELPEED---IIGVSAKTGLNVEElLLPAIID 222
Cdd:cd01895 138 KEL--RRKLPFLDyapIVFISALTGQGVDK-LFDAIKE 172
|
|
| MnmE |
COG0486 |
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
114-216 |
3.18e-06 |
|
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: 50.06 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 114 YLLHLIDTPG------HVDFRGeVSRSYASCGGA---ILLVDASQGIQAQTVAnfYLAFSLGLKLIPVINKIDLnftdvk 184
Cdd:COG0486 261 IPVRLIDTAGlretedEVEKIG-IERAREAIEEAdlvLLLLDASEPLTEEDEE--ILEKLKDKPVIVVLNKIDL------ 331
|
90 100 110
....*....|....*....|....*....|..
gi 6323320 185 qVKDQIVNNFELPEEDIIGVSAKTGLNVEELL 216
Cdd:COG0486 332 -PSEADGELKSLPGEPVIAISAKTGEGIDELK 362
|
|
| trmE |
PRK05291 |
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; |
112-216 |
3.66e-06 |
|
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
Pssm-ID: 235392 [Multi-domain] Cd Length: 449 Bit Score: 49.72 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 112 KNYLLHLIDTPG------HVdfrgE---VSRSYASCGGA---ILLVDASQGIQAQTVANFYLafSLGLKLIPVINKIDLN 179
Cdd:PRK05291 261 DGIPLRLIDTAGiretddEV----EkigIERSREAIEEAdlvLLVLDASEPLTEEDDEILEE--LKDKPVIVVLNKADLT 334
|
90 100 110
....*....|....*....|....*....|....*..
gi 6323320 180 ftdvkqvkdQIVNNFELPEEDIIGVSAKTGLNVEELL 216
Cdd:PRK05291 335 ---------GEIDLEEENGKPVIRISAKTGEGIDELR 362
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
108-230 |
7.39e-06 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 48.87 E-value: 7.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 108 KRTGKNYLLhlIDTPG-----HVDFRGE---VSRSYAS---CGGAILLVDASQGIQAQ--TVANfyLAFSLGLKLIPVIN 174
Cdd:COG1160 219 ERDGKKYTL--IDTAGirrkgKVDEGIEkysVLRTLRAierADVVLLVIDATEGITEQdlKIAG--LALEAGKALVIVVN 294
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323320 175 KIDLnFTDVKQVKDQIVNNFE-----LPEEDIIGVSAKTGLNVEElLLPAIID-------RIppPTGR 230
Cdd:COG1160 295 KWDL-VEKDRKTREELEKEIRrrlpfLDYAPIVFISALTGQGVDK-LLEAVDEvyesankRI--STSK 358
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
118-216 |
1.36e-05 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 47.35 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 118 LIDTPG-H----------VDFrgeVSRSYASCGGAILLVDASQGI--QAQTVANfyLAFSLGLKLIPVINKIDLnFTDVK 184
Cdd:PRK00089 57 FVDTPGiHkpkralnramNKA---AWSSLKDVDLVLFVVDADEKIgpGDEFILE--KLKKVKTPVILVLNKIDL-VKDKE 130
|
90 100 110
....*....|....*....|....*....|...
gi 6323320 185 QVKDQIVN-NFELPEEDIIGVSAKTGLNVEELL 216
Cdd:PRK00089 131 ELLPLLEElSELMDFAEIVPISALKGDNVDELL 163
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
141-227 |
2.35e-05 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 47.35 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 141 AILLVDASQGI--QAQTVANFylAFSLGLKLIPVINKIDLNFTDV-KQVKDQIVNNFE-LPEEDIIGVSAKTGLNVEElL 216
Cdd:PRK00093 259 VLLVIDATEGIteQDLRIAGL--ALEAGRALVIVVNKWDLVDEKTmEEFKKELRRRLPfLDYAPIVFISALTGQGVDK-L 335
|
90
....*....|....*...
gi 6323320 217 LPAIID-------RIPPP 227
Cdd:PRK00093 336 LEAIDEayenanrRISTS 353
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
51-156 |
3.78e-05 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 46.71 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 51 IVA---HVDHGKSTLSDRLleithvidpnaRNKQVldkleVERERG-IT------------IKAQTCSMfyKDKRTGKNY 114
Cdd:PRK04004 8 IVVvlgHVDHGKTTLLDKI-----------RGTAV-----AAKEAGgITqhigatevpidvIEKIAGPL--KKPLPIKLK 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 6323320 115 L--LHLIDTPGHVDFRGEVSRsyascGG-----AILLVDASQGIQAQTV 156
Cdd:PRK04004 70 IpgLLFIDTPGHEAFTNLRKR-----GGaladiAILVVDINEGFQPQTI 113
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
118-226 |
6.06e-05 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 45.36 E-value: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 118 LIDTPG-H----------VDFrgeVSRSYASCGGAILLVDASQGIQA--QTVANfyLAFSLGLKLIPVINKIDLnftdVK 184
Cdd:COG1159 55 FVDTPGiHkpkrklgrrmNKA---AWSALEDVDVILFVVDATEKIGEgdEFILE--LLKKLKTPVILVINKIDL----VK 125
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 6323320 185 qvKDQIVNNFE-----LPEEDIIGVSAKTGLNVEElLLPAIIDRIPP 226
Cdd:COG1159 126 --KEELLPLLAeyselLDFAEIVPISALKGDNVDE-LLDEIAKLLPE 169
|
|
| YihA_EngB |
cd01876 |
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
140-215 |
1.51e-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: 1.51e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323320 140 GAILLVDASQGIQAQTVANFYLAFSLGLKLIPVINKID-LNFTDVKQVKDQIVNNFELPEED--IIGVSAKTGLNVEEL 215
Cdd:cd01876 84 GVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADkLKKSELAKVLKKIKEELNLFNILppVILFSSKKGTGIDEL 162
|
|
| EFG_mtEFG_C |
cd03713 |
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational ... |
450-527 |
1.94e-04 |
|
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational elongation factor (EF) EF-G. Included in this group is the C-terminus of mitochondrial Elongation factor G1 (mtEFG1) and G2 (mtEFG2) proteins. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. In bacteria this translocation step is catalyzed by EF-G_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. No clear phenotype has been found for mutants in the yeast homologue of mtEFG2, MEF2.
Pssm-ID: 239683 [Multi-domain] Cd Length: 78 Bit Score: 40.20 E-value: 1.94e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323320 450 EPFIEAVMTLPQEYLGSVIRLCDSNRGEQIDitYLNTNGQVMLKYYLPLSHLvDDFFGKLKSVSRGFASLDYEDAGYR 527
Cdd:cd03713 1 EPIMKVEVTVPEEYMGDVIGDLSSRRGQILG--TESRGGWKVIKAEVPLAEM-FGYSTDLRSLTQGRGSFTMEFSHYE 75
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
115-226 |
2.98e-04 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 43.22 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 115 LLHLIDTPGHvdfrGEVSRS---------YASCGGAILLVDASQGIQAQTVANFY---LAFSLGLKLIPVINKIDL---- 178
Cdd:COG3596 89 GLVLLDTPGL----GEVNERdreyrelreLLPEADLILWVVKADDRALATDEEFLqalRAQYPDPPVLVVLTQVDRlepe 164
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323320 179 -------------NFTDVKQVKDQIVNNFELPEEDIIGVSAK---TGLNVEElLLPAIIDRIPP 226
Cdd:COG3596 165 rewdppynwpsppKEQNIRRALEAIAEQLGVPIDRVIPVSAAedrTGYGLEE-LVDALAEALPE 227
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
58-216 |
3.35e-04 |
|
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: 41.68 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 58 GKSTLSDRLLE-----ITHVidPNA-RNkqvldkleveRERGItikaqtcsmfykdkRTGKNYLLHLIDTPG-HVDFRG- 129
Cdd:cd04163 15 GKSTLLNALVGqkisiVSPK--PQTtRN----------RIRGI--------------YTDDDAQIIFVDTPGiHKPKKKl 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 130 ------EVSRSYASCGGAILLVDASQGI--QAQTVANfyLAFSLGLKLIPVINKIDL--NFTDVKQVKDQIvnNFELPEE 199
Cdd:cd04163 69 germvkAAWSALKDVDLVLFVVDASEWIgeGDEFILE--LLKKSKTPVILVLNKIDLvkDKEDLLPLLEKL--KELHPFA 144
|
170
....*....|....*..
gi 6323320 200 DIIGVSAKTGLNVEELL 216
Cdd:cd04163 145 EIFPISALKGENVDELL 161
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
235-318 |
4.57e-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: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 235 FRALLVDSWYDAYLGAVLLVNIVDGSVRKNDKVICAQTKEKYEVKDIGIMypdRTSTGTLKTGQVGYLVLgmKDSKEAKI 314
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERF---HEEVDEAKAGDIVGIGI--LGVKDILT 75
|
....
gi 6323320 315 GDTI 318
Cdd:cd01342 76 GDTL 79
|
|
| HflX |
cd01878 |
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
142-224 |
9.03e-04 |
|
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: 40.91 E-value: 9.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 142 ILLVDASQ---GIQAQTVANFyLAfSLGLKLIPVI---NKIDLNFtdvkqvKDQIVNNFELPEEDIIGVSAKTGLNVEEL 215
Cdd:cd01878 125 LHVVDASDpdrEEQIETVEEV-LK-ELGADDIPIIlvlNKIDLLD------DEELEERLRAGRPDAVFISAKTGEGLDLL 196
|
....*....
gi 6323320 216 LLpAIIDRI 224
Cdd:cd01878 197 KE-AIEELL 204
|
|
| PRK13768 |
PRK13768 |
GTPase; Provisional |
109-215 |
2.94e-03 |
|
GTPase; Provisional
Pssm-ID: 237498 [Multi-domain] Cd Length: 253 Bit Score: 39.85 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 109 RTGKNYLLhlIDTPGHVD---FR--GEV-----SRSYASCggAILLVDASQgiqAQTVANF----YLA----FSLGLKLI 170
Cdd:PRK13768 94 SLDADYVL--VDTPGQMElfaFResGRKlverlSGSSKSV--VVFLIDAVL---AKTPSDFvsllLLAlsvqLRLGLPQI 166
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323320 171 PVINKIDL-NFTDVKQVKD---------------------------QIVNNFELPEEdIIGVSAKTGLNVEEL 215
Cdd:PRK13768 167 PVLNKADLlSEEELERILKwledpeylleelklekglqgllslellRALEETGLPVR-VIPVSAKTGEGFDEL 238
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
48-211 |
3.84e-03 |
|
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.
Pssm-ID: 206739 [Multi-domain] Cd Length: 180 Bit Score: 38.68 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 48 NFSIVAHVDHGKSTLSDRLLE-------ITHVIDpnarnkqVLDKLEVERERGITIkaqtcsmfykdkrtgknyllhlID 120
Cdd:cd09912 2 LLAVVGEFSAGKSTLLNALLGeevlptgVTPTTA-------VITVLRYGLLKGVVL----------------------VD 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 121 TPG---HVDFRGEVSRSY-ASCGGAILLVDASqgiQAQTVANFYLAFSLGLKLIP----VINKIDL------NFTDVKQV 186
Cdd:cd09912 53 TPGlnsTIEHHTEITESFlPRADAVIFVLSAD---QPLTESEREFLKEILKWSGKkiffVLNKIDLlseeelEEVLEYSR 129
|
170 180
....*....|....*....|....*
gi 6323320 187 KDQIVNNFELPEEDIIGVSAKTGLN 211
Cdd:cd09912 130 EELGVLELGGGEPRIFPVSAKEALE 154
|
|
| Rab |
cd00154 |
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ... |
111-215 |
4.58e-03 |
|
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases form the largest family within the Ras superfamily. There are at least 60 Rab genes in the human genome, and a number of Rab GTPases are conserved from yeast to humans. Rab GTPases are small, monomeric proteins that function as molecular switches to regulate vesicle trafficking pathways. The different Rab GTPases are localized to the cytosolic face of specific intracellular membranes, where they regulate distinct steps in membrane traffic pathways. In the GTP-bound form, Rab GTPases recruit specific sets of effector proteins onto membranes. Through their effectors, Rab GTPases regulate vesicle formation, actin- and tubulin-dependent vesicle movement, and membrane fusion. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which mask C-terminal lipid binding and promote cytosolic localization. While most unicellular organisms possess 5-20 Rab members, several have been found to possess 60 or more Rabs; for many of these Rab isoforms, homologous proteins are not found in other organisms. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Since crystal structures often lack C-terminal residues, the lipid modification site is not available for annotation in many of the CDs in the hierarchy, but is included where possible.
Pssm-ID: 206640 [Multi-domain] Cd Length: 159 Bit Score: 38.21 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 111 GKNYLLHLIDTPGHVDFRGEVSRSYASCGGAILLVDASQgiqAQT---VANFY-LAFSLGLKLIPVI---NKIDLNftDV 183
Cdd:cd00154 46 GKKVKLQIWDTAGQERFRSITSSYYRGAHGAILVYDVTN---RESfenLDKWLnELKEYAPPNIPIIlvgNKSDLE--DE 120
|
90 100 110
....*....|....*....|....*....|....*
gi 6323320 184 KQVKDQIVNNFElpEEDIIG---VSAKTGLNVEEL 215
Cdd:cd00154 121 RQVSTEEAQQFA--KENGLLffeTSAKTGENVDEA 153
|
|
| BipA_TypA_C |
cd03710 |
BipA_TypA_C: a C-terminal portion of BipA or TypA having homology to the C terminal domains of ... |
450-527 |
4.75e-03 |
|
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: 36.33 E-value: 4.75e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323320 450 EPFIEAVMTLPQEYLGSVIRLCDSNRGEQIDITyLNTNGQVMLKYYLPLSHLVdDFFGKLKSVSRGFASLDYEDAGYR 527
Cdd:cd03710 1 EPIEELTIDVPEEYSGAVIEKLGKRKGEMVDME-PDGNGRTRLEFKIPSRGLI-GFRSEFLTDTRGTGIMNHVFDGYE 76
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
58-175 |
6.88e-03 |
|
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: 36.83 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323320 58 GKSTLSDRLLEithvidpnarnkqvlDKLEVERERGITIKAQTCSMFYKDKRtgknylLHLIDTPGHVDFRGE---VSRS 134
Cdd:pfam01926 11 GKSTLINALTG---------------AKAIVSDYPGTTRDPNEGRLELKGKQ------IILVDTPGLIEGASEgegLGRA 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 6323320 135 YAS---CGGAILLVDASQGIQAQTVANFYLAFSLGLKLIPVINK 175
Cdd:pfam01926 70 FLAiieADLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
|
|
| Obg |
cd01898 |
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ... |
172-216 |
8.89e-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: 37.40 E-value: 8.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 6323320 172 VINKIDL-NFTDVKQVKDQIVNnfELPEEDIIGVSAKTGLNVEELL 216
Cdd:cd01898 120 VLNKIDLlDAEERFEKLKELLK--ELKGKKVFPISALTGEGLDELL 163
|
|
| |
