|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
1-696 |
0e+00 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 838.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 1 MSSTLVINGKAPvvAYAELIAARLvndsksdASVTVEFVDDKKSAAA---------TFDGKSDN-ALEAIVAKFPEILGA 70
Cdd:PLN02907 1 MEAKLSFPPDSP--PLAVIAAAKV-------AGVPLTIDPSLKSGSAptllfssgeKLTGTNVLlRYIARSASLPGFYGQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 71 N----EESKPWIKLAAEELVIKNFQKLAqslEKLDAQLNFRTYING-GLKFdsADIACWGALRSNGMV-GSIIKNKVYVN 144
Cdd:PLN02907 72 DafesSQVDEWLDYAPTFSSGSEFENAC---EYVDGYLASRTFLVGySLTI--ADIAIWSGLAGSGQRwESLRKSKKYQN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 145 VSRWYLLLESNPSFGQSHE------------FLTKSLQElKKAANAGKKKESHKANFEIDLPDAKIGEVVTRFPPEPSGY 212
Cdd:PLN02907 147 LVRWFNSISAEYSDILNEVtaayvgkrgagkPAAAKSKE-KVADAGKADGAKDKGSFEVDLPGAEEGKVCTRFPPEPSGY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 213 LHIGHAKAALLNQYFAQAYKGKLIIRFDDTNPSKEKTEFQDSILEDLELLGIKGDRITYSSDYFQEMYELCVKLIKEGKA 292
Cdd:PLN02907 226 LHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTYTSDYFPQLMEMAEKLIKEGKA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 293 YCDDTPTEKMREERMDGIASARRERSVEENLKIFtEDMKNGTEEGLKNCVRAKIDYAALNKTLRDPVIYRCNLTPHHRTG 372
Cdd:PLN02907 306 YVDDTPREQMRKERMDGIESKCRNNSVEENLRLW-KEMIAGSERGLQCCVRGKLDMQDPNKSLRDPVYYRCNPTPHHRIG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 373 SEWKMYPTYDFCVPIVDSIEGVTHALRTIEYRDRNAQYDWFLDNLNLRKVHIWDFARVNFVRTLLSKRKLQWMVDKNLVS 452
Cdd:PLN02907 385 SKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLRKVHIWEFSRLNFVYTLLSKRKLQWFVDNGKVE 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 453 NWDDPRFPTVRGVRRRGMTVEGLRNFVLSQGPSRNVINLEWNLIWAFNKKVIDPVAPRHTAIVNP--VKIHIEGAPESPK 530
Cdd:PLN02907 465 GWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKKIIDPVCPRHTAVLKEgrVLLTLTDGPETPF 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 531 TEMKPKHKKNPAVGEKKVIYYQNVVIDKEDADSIEDNEEVTLMDWGNIIITK--KNADG---SMEAKLHLEGDFKKTKHK 605
Cdd:PLN02907 545 VRIIPRHKKYEGAGKKATTFTNRIWLDYADAEAISEGEEVTLMDWGNAIIKEitKDEGGavtALSGELHLEGSVKTTKLK 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 606 LTWLADTDDSVKVDLVDFDHLISKDKLEEDESFEDFLTPQTEFHTEAIADLNVKDMIVGDIIQFERKGYYRLDAE-AKDG 684
Cdd:PLN02907 625 LTWLPDTNELVPLSLVEFDYLITKKKLEEDDNFLDVLNPCTKKETAALGDSNMRNLKRGEIIQLERKGYYRCDAPfVRSS 704
|
730
....*....|..
gi 2130400838 685 KPYVFFTIPDGK 696
Cdd:PLN02907 705 KPIVLFAIPDGR 716
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
101-693 |
0e+00 |
|
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This model models just the eukaryotic cytosolic and archaeal forms of the enzyme. In some eukaryotes, the glutamyl-tRNA synthetase is part of a longer, multifunctional aminoacyl-tRNA ligase. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases, including all known archaeal enzymes (as of 2010) may act on both tRNA(gln) and tRNA(glu). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273091 [Multi-domain] Cd Length: 556 Bit Score: 767.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 101 DAQLNFRTYINGGLKFDsadiacwGALRSNGMVGSIIKNKVYVNVSRWYLLLESNPSFGQSHEFLTKSLQELKKAANAGK 180
Cdd:TIGR00463 1 MEELILRYALLNAVKYR-------GKANPKAVMGAVMSNNPELRKKAKEVLEAVEAAVEEVNSLSPEEQKELMKRLGLDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 181 KKESHKANFEIDLPDAKIGEVVTRFPPEPSGYLHIGHAKAALLNQYFAQAYKGKLIIRFDDTNPSKEKTEFQDSILEDLE 260
Cdd:TIGR00463 74 KKKEKKRKGLRELPGAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 261 LLGIKGDRITYSSDYFQEMYELCVKLIKEGKAYCDDTPTEKMREERMDGIASARRERSVEENLKIFtEDMKNGTEEGLKN 340
Cdd:TIGR00463 154 WLGVKWDEVVYQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNRGEACHCRDRSVEENLERW-EEMLEGKEEGGSV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 341 CVRAKIDYAALNKTLRDPVIYRCNLTPHHRTGSEWKMYPTYDFCVPIVDSIEGVTHALRTIEYRD--RNAQYDWFLDNLN 418
Cdd:TIGR00463 233 VVRVKTDLKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDnrRKQEYIYRYFGWE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 419 LRKVHIWDFARVNFVRTLLSKRKLQWMVDKNLvSNWDDPRFPTVRGVRRRGMTVEGLRNFVLSQGPSRNVINLEWNLIWA 498
Cdd:TIGR00463 313 PPEFIHWGRLKIDDVRALSTSSARKGILRGEY-SGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 499 FNKKVIDPVAPRHTAIVNPVKIHIEGAPEsPKTEMKPKHKKNPAVGEKKVIYYQNVVIDKEDADsiEDNEEVTLMDWGNI 578
Cdd:TIGR00463 392 LNRKIIDEEARRYFFIWNPVKIEIVGLPE-PKRVERPLHPDHPEIGERVLILRGEIYVPKDDLE--EGVEPVRLMDAVNV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 579 IITKKNadgSMEAKLHLEGDFKKTKHKLTWLADtDDSVKVDLVDFDHLISKDKLEEDESFEDfltpqtefhteaiadlnv 658
Cdd:TIGR00463 469 IYSKKE---LRYHSEGLEGARKLGKSIIHWLPA-KDAVKVKVIMPDASIVEGVIEADASELE------------------ 526
|
570 580 590
....*....|....*....|....*....|....*
gi 2130400838 659 kdmiVGDIIQFERKGYYRLDAEAKDGKPYVfFTIP 693
Cdd:TIGR00463 527 ----VGDVVQFERFGFARLDSADKDGMVFV-YTHP 556
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
199-696 |
0e+00 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 586.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 199 GEVVTRFPPEPSGYLHIGHAKAALLNQYFAQAYKGKLIIRFDDTNPSKEKTEFQDSILEDLELLGIKGDRITYSSDYFQE 278
Cdd:PLN03233 10 GQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDYFEP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 279 MYELCVKLIKEGKAYCDDTPTEKMREERMDGIASARRERSVEENLKIFTEdMKNGTEEGLKNCVRAKIDYAALNKTLRDP 358
Cdd:PLN03233 90 IRCYAIILIEEGLAYMDDTPQEEMKKERADRAESKHRNQSPEEALEMFKE-MCSGKEEGGAWCLRAKIDMQSDNGTLRDP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 359 VIYRCNLTPHHRTGSEWKMYPTYDFCVPIVDSIEGVTHALRTIEYRDRNAQYDWFLDNLNLRKVHIWDFARVNFVRTLLS 438
Cdd:PLN03233 169 VLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPRIHAFARMNFMNTVLS 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 439 KRKLQWMVDKNLVSNWDDPRFPTVRGVRRRGMTVEGLRNFVLSQGPSRNVINLEWNLIWAFNKKVIDPVAPRHTAI--VN 516
Cdd:PLN03233 249 KRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRAKRFMAIdkAD 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 517 PVKIHIEGAPESPKTEMKPK--HKKNPAVGEKKVIYYQNVVIDKEDADSIEDNEEVTLMDWGNIIITKknADGSMEAKLH 594
Cdd:PLN03233 329 HTALTVTNADEEADFAFSETdcHPKDPGFGKRAMRICDEVLLEKADTEDIQLGEDIVLLRWGVIEISK--IDGDLEGHFI 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 595 LEGDFKKTKHKLTWLADTDDSVKVDLVDFDHLISKDKLEEDESFEDFLTPQTEFHTEAIADLNVKDMIVGDIIQFERKGY 674
Cdd:PLN03233 407 PDGDFKAAKKKISWIADVSDNIPVVLSEFDNLIIKEKLEEDDKFEDFINPDTLAETDVIGDAGLKTLKEHDIIQLERRGF 486
|
490 500
....*....|....*....|...
gi 2130400838 675 YRLDAE-AKDGKPYVFFTIPDGK 696
Cdd:PLN03233 487 YRVDRPyMGEEKPLILFMIPDGK 509
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
158-704 |
0e+00 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 580.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 158 FGQSHEFLTKSLQELKKAANAGKKKESHKA--NFEIDLPDAKIGEVVTRFPPEPSGYLHIGHAKAALLNQYFAQAYKGKL 235
Cdd:PTZ00402 8 FGPMIMLINILLKALTSFLSNTYFTAANANeeNDKLQLTNAEEGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 236 IIRFDDTNPSKEKTEFQDSILEDLELLGIKGDR-ITYSSDYFQEMYELCVKLIKEGKAYCDDTPTEKMREERMDGIASAR 314
Cdd:PTZ00402 88 VFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVgPTYSSDYMDLMYEKAEELIKKGLAYCDKTPREEMQKCRFDGVPTKY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 315 RERSVEENLKIFTEdMKNGTEEGLKNCVRAKIDYAALNKTLRDPVIYRCNLTPHHRTGSEWKMYPTYDFCVPIVDSIEGV 394
Cdd:PTZ00402 168 RDISVEETKRLWNE-MKKGSAEGQETCLRAKISVDNENKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 395 THALRTIEYRDRNAQYDWFLDNLNLRKVHIWDFARVNFVRTLLSKRKLQWMVDKNLVSNWDDPRFPTVRGVRRRGMTVEG 474
Cdd:PTZ00402 247 THALRTNEYHDRNDQYYWFCDALGIRKPIVEDFSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 475 LRNFVLSQGPSRNVINLEWNLIWAFNKKVIDPVAPRHTAIVNPVKIH--IEGAPESPKTEmKPKHKKNPAVGEKKviYYQ 552
Cdd:PTZ00402 327 LRQFVQEQGMSKTVNFMEWSKLWYFNTQILDPSVPRYTVVSNTLKVRctVEGQIHLEACE-KLLHKKVPDMGEKT--YYK 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 553 NVVI--DKEDADSIEDNEEVTLMDWGNII---ITKKNADGSM-EAK--LHLEGDFKKTKHKLTWLADTDDSVKVDLVDFD 624
Cdd:PTZ00402 404 SDVIflDAEDVALLKEGDEVTLMDWGNAYiknIRRSGEDALItDADivLHLEGDVKKTKFKLTWVPESPKAEVMELNEYD 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 625 HLISKDKLEEDESFEDFLTPQTEFHTEAIADLNVKDMIVGDIIQFERKGYYRLDaeaKDGKPYVFFTIPDGK-SVNKYGA 703
Cdd:PTZ00402 484 HLLTKKKPDPEESIDDIIAPVTKYTQEVYGEEALSVLKKGDIIQLERRGYYIVD---DVTPKKVLIAIPDGReKVNHLSA 560
|
.
gi 2130400838 704 K 704
Cdd:PTZ00402 561 K 561
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
200-506 |
3.10e-152 |
|
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 395606 [Multi-domain] Cd Length: 314 Bit Score: 444.07 E-value: 3.10e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 200 EVVTRFPPEPSGYLHIGHAKAALLNQYFAQAYKGKLIIRFDDTNPSKEKTEFQDSILEDLELLGIKGD-RITYSSDYFQE 278
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDyGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 279 MYELCVKLIKEGKAYCDDTPTEKMREERMD--GIASARRERSVEENLKIFTEDMKNGTEEGLKNCVRAKIDYAAlNKTLR 356
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEqeALGSPSRDRYDEENLHLFEEEMKKGSAEGGPATVRAKIPMES-PYVFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 357 DPVIYRCNLTP---HHRTGSEWKMYPTYDFCVPIVDSIEGVTHALRTIEYRDRNAQYDWFLDNLNLR-KVHIWDFARVNF 432
Cdd:pfam00749 160 DPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEpPPFIHEYLRLNL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2130400838 433 VRTLLSKRKLQWMVDKNLVSNWDDPRFPTVRGVRRRGMTVEGLRNFVLSQGPSRNV-INLEWNLIWAFNKKVIDP 506
Cdd:pfam00749 240 DGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFdVNRLSKSLEAFDRKKLDW 314
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
183-689 |
6.00e-149 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 444.55 E-value: 6.00e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 183 ESHKANF-----EIDLPDAKIGEVVTRFPPEPSGYLHIGHAKAALLNQYFAQAYKGKLIIRFDDTNPSKEKTEFQDSILE 257
Cdd:PRK05347 7 EARPSNFirqiiDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSIKE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 258 DLELLGIK-GDRITYSSDYFQEMYELCVKLIKEGKAYCDDTPTEKMREERMD----GIASARRERSVEENLKIFtEDMKN 332
Cdd:PRK05347 87 DVRWLGFDwSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTltepGKNSPYRDRSVEENLDLF-ERMRA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 333 GT-EEGLKnCVRAKIDYAALNKTLRDPVIYRCNLTPHHRTGSEWKMYPTYDFCVPIVDSIEGVTHALRTIEYRDRNAQYD 411
Cdd:PRK05347 166 GEfPEGSA-VLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLYD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 412 WFLDNLNLRKV-HIWDFARVNFVRTLLSKRKLQWMVDKNLVSNWDDPRFPTVRGVRRRGMTVEGLRNFVLSQGPSR--NV 488
Cdd:PRK05347 245 WVLDNLPIPPHpRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKqdSV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 489 IN---LEwnliwAFNKKVIDPVAPRHTAIVNPVKIHIEGAPEsPKTEM--KPKHKKNPAVGEKKVIYYQNVVIDKED--- 560
Cdd:PRK05347 325 IDmsmLE-----SCIREDLNENAPRAMAVLDPLKLVITNYPE-GQVEEleAPNHPEDPEMGTREVPFSRELYIEREDfme 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 561 ------------------------ADSIEDNEEvtlmdwGNIII--------TK--KNADGsmeaklhlegdfKKTKHKL 606
Cdd:PRK05347 399 eppkkyfrlvpgkevrlrnayvikCEEVVKDAD------GNITEihctydpdTLsgNPADG------------RKVKGTI 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 607 TWLaDTDDSVKVDLVDFDHLISKDKLEEDESFEDFLTPQTEFHTEAIADLNVKDMIVGDIIQFERKGYYRLDAEAKDGKP 686
Cdd:PRK05347 461 HWV-SAAHAVPAEVRLYDRLFTVPNPAAGKDFLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCADKDSTPGKL 539
|
...
gi 2130400838 687 yVF 689
Cdd:PRK05347 540 -VF 541
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
200-510 |
4.60e-140 |
|
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Gln to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. GlnRS contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.
Pssm-ID: 185676 [Multi-domain] Cd Length: 238 Bit Score: 409.72 E-value: 4.60e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 200 EVVTRFPPEPSGYLHIGHAKAALLNQYFAQAYKGKLIIRFDDTNPSKEKTEFQDSILEDLELLGIKGDRITYSSDYFQEM 279
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 280 YELCVKLIKEGKAYCddtptekmreermdgiasarrersveenlkiftedmkngteeglkncvrakidyaalnktlrdpv 359
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 360 iyrcnltpHHRTGSEWKMYPTYDFCVPIVDSIEGVTHALRTIEYRDRNAQYDWFLDNLNLRKVHIWDFARVNFVRTLLSK 439
Cdd:cd00807 96 --------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSK 167
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2130400838 440 RKLQWMVDKNLVSNWDDPRFPTVRGVRRRGMTVEGLRNFVLSQGPSRNVINLEWNLIWAFNKKVIDPVAPR 510
Cdd:cd00807 168 RKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
201-689 |
2.91e-116 |
|
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found in the cytosolic compartment of eukaryotes, in E. coli and a number of other Gram-negative Bacteria, and in Deinococcus radiodurans. In contrast, the pathway to Gln-tRNA in mitochondria, Archaea, Gram-positive Bacteria, and a number of other lineages is by misacylation with Glu followed by transamidation to correct the aminoacylation to Gln. This enzyme is a class I tRNA synthetase (hit by the pfam model tRNA-synt_1c) and is quite closely related to glutamyl-tRNA synthetases. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273079 [Multi-domain] Cd Length: 522 Bit Score: 359.24 E-value: 2.91e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 201 VVTRFPPEPSGYLHIGHAKAALLNQYFAQAYKGKLIIRFDDTNPSKEKTEFQDSILEDLELLGIKGD-RITYSSDYFQEM 279
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEgKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 280 YELCVKLIKEGKAYCDDTPTEKMREER----MDGIASARRERSVEENLKIFtEDMKNGTEEGLKNCVRAKIDYAALNKTL 355
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRgtltDPGKNSPYRDRSIEENLALF-EKMRDGKFKEGKAILRAKIDMASPFPVM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 356 RDPVIYRCNLTPHHRTGSEWKMYPTYDFCVPIVDSIEGVTHALRTIEYRDRNAQYDWFLDNLNL-RKVHIWDFARVNFVR 434
Cdd:TIGR00440 160 RDPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIfPRPAQYEFSRLNLEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 435 TLLSKRKLQWMVDKNLVSNWDDPRFPTVRGVRRRGMTVEGLRNFVLSQGPSRNVINLEWNLIWAFNKKVIDPVAPRHTAI 514
Cdd:TIGR00440 240 TVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 515 VNPVKIHIEGAPESPKTEMKPKHKKNPAVGEKKVIYYQNVVIDKED---------------------------ADSIEDN 567
Cdd:TIGR00440 320 IDPVEVVIENLSDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADfreeankqykrlvlgkevrlrnayvikAERVEKD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 568 EEvtlmdwGNIIITKKNADGSMEAKLHLEGdfKKTKHKLTWLADTdDSVKVDLVDFDHLISKDKLEEDESFEDFLTPQTE 647
Cdd:TIGR00440 400 AA------GKITTIFCTYDNKTLGKEPADG--RKVKGVIHWVSAS-SKYPTETRLYDRLFKVPNPGAPDDFLSVINPESL 470
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2130400838 648 FHTEAIADLNVKDMIVGDIIQFERKGYYRLDAEAKDGKPYVF 689
Cdd:TIGR00440 471 VIKQGFMEHSLGDAVANKRFQFEREGYFCLDSKESTTEKVVF 512
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
190-689 |
6.31e-113 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 358.27 E-value: 6.31e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 190 EIDLPDAKIGEVVTRFPPEPSGYLHIGHAKAALLNQYFAQAYKGKLIIRFDDTNPSKEKTEFQDSILEDLELLGIK-GDR 268
Cdd:PRK14703 21 EEDLEAGRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDwGEH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 269 ITYSSDYFQEMYELCVKLIKEGKAYCDDTPTEKMREERMD----GIASARRERSVEENLKIFtEDMKNGTEEGLKNCVRA 344
Cdd:PRK14703 101 LYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTvtepGTPSPYRDRSVEENLDLF-RRMRAGEFPDGAHVLRA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 345 KIDYAALNKTLRDPVIYRCNLTPHHRTGSEWKMYPTYDFCVPIVDSIEGVTHALRTIEYRDRNAQYDWFLDNLNLR--KV 422
Cdd:PRK14703 180 KIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLGPWppRP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 423 HIWDFARVNFVRTLLSKRKLQWMVDKNLVSNWDDPRFPTVRGVRRRGMTVEGLRNFVLSQGPSRN-----VINLEWNLIW 497
Cdd:PRK14703 260 RQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTnstvdIGVLEFAIRD 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 498 AFNKKvidpvAPRHTAIVNPVKIHIEGAPESPKTEMKPKH--KKNPAVGEKKVIYYQNVVIDKED--ADSIED------N 567
Cdd:PRK14703 340 DLNRR-----APRVMAVLDPLKVVIENLPAGKVEELDLPYwpHDVPKEGSRKVPFTRELYIERDDfsEDPPKGfkrltpG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 568 EEVTLMdwGNIIIT----KKNADGSM-EAKLHLEGDFK-------KTKHKLTWLaDTDDSVKVDLVDFDHLISKDKLE-E 634
Cdd:PRK14703 415 REVRLR--GAYIIRcdevVRDADGAVtELRCTYDPESAkgedtgrKAAGVIHWV-SAKHALPAEVRLYDRLFKVPQPEaA 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2130400838 635 DESFEDFLTPQTEFHTEAIADLNVKDMIVGDIIQFERKGYYRLDAEA-KDGKPyVF 689
Cdd:PRK14703 492 DEDFLEFLNPDSLRVAQGRVEPAVRDDPADTRYQFERQGYFWADPVDsRPDAL-VF 546
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
199-685 |
1.50e-104 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 336.73 E-value: 1.50e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 199 GEVVTRFPPEPSGYLHIGHAKAALLNQYFAQAYKGKLIIRFDDTNPSKEKTEFQDSILEDLELLGIKGDRITYSSDYFQE 278
Cdd:PLN02859 263 GKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMGWEPFKITYTSDYFQE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 279 MYELCVKLIKEGKAYCD-DTPTE--KMREERMDgiaSARRERSVEENLKIFtEDMKNG-TEEGlKNCVRAKIDYAALNKT 354
Cdd:PLN02859 343 LYELAVELIRRGHAYVDhQTPEEikEYREKKMN---SPWRDRPIEESLKLF-EDMRRGlIEEG-KATLRMKQDMQNDNFN 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 355 LRDPVIYRCNLTPHHRTGSEWKMYPTYDFCVPIVDSIEGVTHALRTIEYRDRNAQYDWFLDNLNLRKVHIWDFARVNFVR 434
Cdd:PLN02859 418 MYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSLGLYQPYVWEYSRLNVTN 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 435 TLLSKRKLQWMVDKNLVSNWDDPRFPTVRGVRRRGMTVEGLRNFVLSQGPSRN---VINLEwnLIWAFNKKVIDPVAPRH 511
Cdd:PLN02859 498 TVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSdnsLIRMD--RLEHHIREELNKTAPRT 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 512 TAIVNPVKIHIEGAPESPKTEMK----PKHKKNPAVGEKKVIYYQNVVIDKEDAdSIEDNEEV--------TLMDWG--- 576
Cdd:PLN02859 576 MVVLHPLKVVITNLESGEVIELDakrwPDAQNDDPSAFYKVPFSRVVYIERSDF-RLKDSKDYyglapgksVLLRYAfpi 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 577 ---NIIITKKNADGSmeaKLHLEGD-FKKTKHK--LTWLADTD---DSVKVDLVDFDHLI-SKDKLEEDESFEDFLTPQT 646
Cdd:PLN02859 655 kctDVVLADDNETVV---EIRAEYDpEKKTKPKgvLHWVAEPSpgvEPLKVEVRLFDKLFlSENPAELEDWLEDLNPQSK 731
|
490 500 510
....*....|....*....|....*....|....*....
gi 2130400838 647 EFHTEAIADLNVKDMIVGDIIQFERKGYYRLDAEAKDGK 685
Cdd:PLN02859 732 EVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEK 770
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
204-685 |
2.42e-102 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 324.63 E-value: 2.42e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 204 RFPPEPSGYLHIGHAKAALLNQYFAQAYKGKLIIRFDDTNPSKEKTEFQDSILEDLELLGIKGDRITYSSDYFQEMYELC 283
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKPDWVTFSSDYFDQLHEFA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 284 VKLIKEGKAYCDDTPTEKMREERMDGIASARRERSVEENLKIFtEDMKNGTEEGLKNCVRAKIDYAALNKTLRDPVIYRC 363
Cdd:PTZ00437 135 VQLIKDGKAYVDHSTPDELKQQREQREDSPWRNRSVEENLLLF-EHMRQGRYAEGEATLRVKADMKSDNPNMRDFIAYRV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 364 NLTPHHRTGSEWKMYPTYDFCVPIVDSIEGVTHALRTIEYRDRNAQYDWFLDNLNLRKVHIWDFARVNFVRTLLSKRKLQ 443
Cdd:PTZ00437 214 KYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNLWRPHVWEFSRLNVTGSLLSKRKIN 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 444 WMVDKNLVSNWDDPRFPTVRGVRRRGMTVEGLRNFVLSQGPSRNVINLEWNLIWAFNKKVIDPVAPRHTAIVNPVKIHIE 523
Cdd:PTZ00437 294 VLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCERRLMVIDPIKVVVD 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 524 GApESPKTEMKPKHKKNPAVGEKKVIYYQNVVIDKEDAdSIEDNEE-----------VTLMDWGNIIITKKNADGSMEAK 592
Cdd:PTZ00437 374 NW-KGEREFECPNHPRKPELGSRKVMFTDTFYVDRSDF-RTEDNNSkfyglapgprvVGLKYSGNVVCKGFEVDAAGQPS 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 593 L-HLEGDFKKT---KHKLTWLADTdDSVKVDLVDFDHLISKDKLEEDESFEDFLTPQTEFHTEAIADLNVKDMIVGDIIQ 668
Cdd:PTZ00437 452 ViHVDIDFERKdkpKTNISWVSAT-ACTPVEVRLYNALLKDDRAAIDPEFLKFIDEDSEVVSHGYAEKGIENAKHFESVQ 530
|
490
....*....|....*..
gi 2130400838 669 FERKGYYRLDAEAKDGK 685
Cdd:PTZ00437 531 AERFGYFVVDPDTRPDH 547
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
192-691 |
3.27e-101 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 321.42 E-value: 3.27e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 192 DLPDAKIGEVVTRFPPEPSGYLHIGHAKAALLNQYFAQAYKGKLIIRFDDTNPsKEKT---EFQDSILEDLELLGIKGDR 268
Cdd:PRK04156 93 PLPNAEKGKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDP-RTKRpdpEAYDMILEDLKWLGVKWDE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 269 ITYSSDYFQEMYELCVKLIKEGKAYCDDTPTEKMREERMDGIASARRERSVEENLKIFtEDMKNGT-EEGlKNCVRAKID 347
Cdd:PRK04156 172 VVIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELRDAGKPCPHRDKSPEENLELW-EKMLDGEyKEG-EAVVRVKTD 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 348 YAALNKTLRDPVIYRCNLTPHHRTGSEWKMYPTYDFCVPIVDSIEGVTHALRTIEYRDrNAQ-----YDWFLdnlnlrkv 422
Cdd:PRK04156 250 LEHPNPSVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHID-NTEkqryiYDYFG-------- 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 423 hiWD------FARVNFVRTLLSKRKLQWMVDKNLVSNWDDPRFPTVRGVRRRGMTVEGLRNFVLSQGPSRNVINLEWNLI 496
Cdd:PRK04156 321 --WEypetihYGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENL 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 497 WAFNKKVIDPVAPRHTAIVNPVKIHIEGAPEspkTEMK-PKHKKNPAVGEKKVIYYQNVVIDKEDADsiEDNEEVTLMDW 575
Cdd:PRK04156 399 YAINRKLIDPIANRYFFVRDPVELEIEGAEP---LEAKiPLHPDRPERGEREIPVGGKVYVSSDDLE--AEGKMVRLMDL 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 576 GNIIITKKNADgsmEAKLHLEG--DFKKTKHKLT-WLADtDDSVKVDLvdfdhliskdkleedesfedfLTPQTEfHTEA 652
Cdd:PRK04156 474 FNVEITGVSVD---KARYHSDDleEARKNKAPIIqWVPE-DESVPVRV---------------------LKPDGG-DIEG 527
|
490 500 510
....*....|....*....|....*....|....*....
gi 2130400838 653 IADLNVKDMIVGDIIQFERKGYYRLDaEAKDGKPYVFFT 691
Cdd:PRK04156 528 LAEPDVADLEVDDIVQFERFGFVRID-SVEDDEVVAYFA 565
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
199-526 |
2.31e-76 |
|
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 252.79 E-value: 2.31e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 199 GEVVTRFPPEPSGYLHIGHAKAALLNQYFAQAYKGKLIIRFDDTNPSKEKTEFQDSILEDLELLGIKGD-RITYSSDYFQ 277
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDeGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 278 EMYELCVKLIKEGKAY-CDDTPTE--KMREERM--------DGIAsarRERSVEEnlkifTEDMKngtEEGLKNCVRAKI 346
Cdd:COG0008 83 IYYEYAEKLIEKGKAYvCFCTPEEleALRETQTapgkppryDGRC---RDLSPEE-----LERML---AAGEPPVLRFKI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 347 DYAAL-------------NKTLRDPVIYRcnltphhRTGsewkmYPTYDFCVPIVDSIEGVTHALRTIEYRDRNAQYDWF 413
Cdd:COG0008 152 PEEGVvfddlvrgeitfpNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 414 LDNLNLRKVHiwdFARVNFV----RTLLSKRklqwmvdKNLVsnwddprfpTVRGVRRRGMTVEGLRNFVL----SQGPS 485
Cdd:COG0008 220 YEALGWEPPE---FAHLPLIlgpdGTKLSKR-------KGAV---------TVSGLRRRGYLPEAIRNYLAllgwSKSDD 280
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2130400838 486 RNVINLEwNLIWAFNkkvIDPVaPRHTAIVNPVKIHIEGAP 526
Cdd:COG0008 281 QEIFSLE-ELIEAFD---LDRV-SRSPAVFDPVKLVWLNGP 316
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
200-510 |
5.30e-57 |
|
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating Glutamyl-tRNA synthetase (GluRS) cataytic core domain. These enzymes attach Glu to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.
Pssm-ID: 185682 [Multi-domain] Cd Length: 240 Bit Score: 193.72 E-value: 5.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 200 EVVTRFPPEPSGYLHIGHAKAALLNQYFAQAYKGKLIIRFDDTNPsKEKT---EFQDSILEDLELLGIKGDRITYSSDYF 276
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDP-RTKRpdpEAYDMIPEDLEWLGVKWDEVVIASDRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 277 QEMYELCVKLIKEGKAYCddtptekmreermdgiasarrersveenlkiftedmkngteeglkncvrakidyaalnktlr 356
Cdd:cd09287 80 ELYYEYARKLIEMGGAYV-------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 357 dpviyrcnltpHHRTGSEWKMYPTYDFCVPIVDSIEGVTHALRTIEYRDRNAQYDWFLDNLNLRKVHIWDFARVNFVRTL 436
Cdd:cd09287 98 -----------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPETIHWGRLKIEGGK 166
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2130400838 437 LSKRKLQWMVDKNLVSNWDDPRFPTVRGVRRRGMTVEGLRNFVLSQGPSRNVINLEWNLIWAFNKKVIDPVAPR 510
Cdd:cd09287 167 LSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDPRANR 240
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
508-678 |
3.42e-44 |
|
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 427609 [Multi-domain] Cd Length: 175 Bit Score: 156.28 E-value: 3.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 508 APRHTAIVNPVKIHIEGAPESPKTEMK-PKHKKNPAVGEKKVIYYQNVVIDKEDADSIEDNEEVTLMDWGNIIITK--KN 584
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEvPNHPKNPELGTRKVPFSREIYIEREDFKRLAPGEEVRLMDAYNIKVTEvvKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 585 ADGS-MEAKLHLEGD-----FKKTKHKLTWLAdTDDSVKVDLVDFDHLISkdkleEDESFEDFLTPQTEF-HTEAIADLN 657
Cdd:pfam03950 81 EDGNvTELHCTYDGDdlggaRKVKGKIIHWVS-ASDAVPAEVRLYDRLFK-----DEDDADFLLNPDSLKvLTEGLAEPA 154
|
170 180
....*....|....*....|.
gi 2130400838 658 VKDMIVGDIIQFERKGYYRLD 678
Cdd:pfam03950 155 LANLKPGDIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
201-486 |
7.92e-42 |
|
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA synthetase(GluRS)/Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Glu or Gln, respectively, to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea, cellular organelles, and some bacteria lack GlnRS. In these cases, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme. The discriminating form of GluRS differs from GlnRS and the non-discriminating form of GluRS in their C-terminal anti-codon binding domains.
Pssm-ID: 185672 [Multi-domain] Cd Length: 230 Bit Score: 151.86 E-value: 7.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 201 VVTRFPPEPSGYLHIGHAKAALLNQYFAQAYKGKLIIRFDDTNPSKEKTEFQDSILEDLELLGIKGDR-ITYSSDYFQEM 279
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEgPYRQSDRFDLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 280 YELCVKLIKEGkaycddtptekmreermdgiasarrersveenlkiftedmkngteeglkncvrakidyaalnktlrdpv 359
Cdd:cd00418 82 RAYAEELIKKG--------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 360 iyrcnltphhrtgsewkMYPTYDFCVPIVDSIEGVTHALRTIEYRDRNAQYDWFLDNLNLRKVHIWDFARVNF-VRTLLS 438
Cdd:cd00418 93 -----------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLeDGTKLS 155
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2130400838 439 KRKLQwmvdknlvsnwddprfPTVRGVRRRGMTVEGLRNFVLSQGPSR 486
Cdd:cd00418 156 KRKLN----------------TTLRALRRRGYLPEALRNYLALIGWSK 187
|
|
| GST_C_GluRS_N |
cd10306 |
Glutathione S-transferase C-terminal-like, alpha helical domain of Glutamyl-tRNA synthetase; ... |
71-154 |
3.26e-31 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of Glutamyl-tRNA synthetase; Glutathione S-transferase (GST) C-terminal domain family, Glutamyl-tRNA synthetase (GluRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of GluRS from lower eukaryotes. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. The GST_C-like domain of GluRS is involved in protein-protein interactions. This domain mediates the formation of the MetRS-Arc1p-GluRS ternary complex found in lower eukaryotes, which is considered an evolutionary intermediate between prokaryotic aaRS and the multi-aaRS complex found in higher eukaryotes. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.
Pssm-ID: 198339 [Multi-domain] Cd Length: 87 Bit Score: 116.68 E-value: 3.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 71 NEESKPWIKLAAEELVIKNFQKLAQSLEKLDAQLNFRTYINGGlKFDSADIACWGALRSNGMVGSIIKNKVYVNVSRWYL 150
Cdd:cd10306 4 KEQVAEWIDFATTLLVLKDFKALSQALEELDSHLTLRTFIVGY-SLSLADIAVWGALRGNGVAGSLIKNKVYVNLSRWFS 82
|
....
gi 2130400838 151 LLES 154
Cdd:cd10306 83 FLES 86
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
194-440 |
1.64e-22 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 102.13 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 194 PDAKIGEVVTRFPPEPSGYLHIGHAKAALLNQYFAQAYKGKLIIRFDDTNPSKEKTEFQDSILEDLELLGIK-------- 265
Cdd:PLN02627 39 GESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDwdegpdvg 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 266 GDRITYSSDYFQEMY-ELCVKLIKEGKAY---CDDTPTEKMREE--------RMDGIASARRERSVEENL---KIFTEDM 330
Cdd:PLN02627 119 GEYGPYRQSERNAIYkQYAEKLLESGHVYpcfCTDEELEAMKEEaelkklppRYTGKWATASDEEVQAELakgTPYTYRF 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 331 KNGTEEGLK--NCVRAKIDYAAlnKTLRDPVIYRCNltphhrtGSewkmyPTYDFCVPIVDSIEGVTHALRTIEYrdrna 408
Cdd:PLN02627 199 RVPKEGSVKidDLIRGEVSWNT--DTLGDFVLLRSN-------GQ-----PVYNFCVAVDDATMGITHVIRAEEH----- 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2130400838 409 qydwfLDNlNLRKVHIWD--------FARVNFV----RTLLSKR 440
Cdd:PLN02627 260 -----LPN-TLRQALIYKalgfpmprFAHVSLIlapdRSKLSKR 297
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
200-299 |
2.59e-20 |
|
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA synthetase (GluRS) catalytic core domain . The discriminating form of GluRS is only found in bacteria and cellular organelles. GluRS is a monomer that attaches Glu to the appropriate tRNA. Like other class I tRNA synthetases, GluRS aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173905 [Multi-domain] Cd Length: 239 Bit Score: 90.72 E-value: 2.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 200 EVVTRFPPEPSGYLHIGHAKAALLNQYFAQAYKGKLIIRFDDTNPSKEKTEFQDSILEDLELLGIKGDRITYSSD----Y 275
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGpygpY 80
|
90 100
....*....|....*....|....*....
gi 2130400838 276 FQ----EMY-ELCVKLIKEGkaycDDTPT 299
Cdd:cd00808 81 RQserlEIYrKYAEKLLEKG----DGFPT 105
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
202-293 |
2.67e-14 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 74.12 E-value: 2.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 202 VTRFPPEPSGYLHIGHAKAALLNQYFAQAYKGKLIIRFDDTNPSKEKTEFQDSILEDLELLGIKGD-RITYSSDYFQEmY 280
Cdd:PRK05710 7 IGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDgPVLYQSQRHDA-Y 85
|
90
....*....|....*
gi 2130400838 281 E--LCvKLIKEGKAY 293
Cdd:PRK05710 86 RaaLD-RLRAQGLVY 99
|
|
| GST_C_AaRS_like |
cd10289 |
Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA ... |
77-154 |
2.02e-11 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA synthetases and similar domains; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl-tRNA synthetase (AaRS)-like subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of some eukaryotic AaRSs, as well as similar domains found in proteins involved in protein synthesis including Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 2 (AIMP2), AIMP3, and eukaryotic translation Elongation Factor 1 beta (eEF1b). AaRSs comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. AaRSs in this subfamily include GluRS from lower eukaryotes, as well as GluProRS, MetRS, and CysRS from higher eukaryotes. AIMPs are non-enzymatic cofactors that play critical roles in the assembly and formation of a macromolecular multi-tRNA synthetase protein complex found in higher eukaryotes. The GST_C-like domain is involved in protein-protein interactions, mediating the formation of aaRS complexes such as the MetRS-Arc1p-GluRS ternary complex in lower eukaryotes and the multi-aaRS complex in higher eukaryotes, that act as molecular hubs for protein synthesis. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.
Pssm-ID: 198322 [Multi-domain] Cd Length: 82 Bit Score: 60.40 E-value: 2.02e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2130400838 77 WIKLAAEELVIKNFQklaQSLEKLDAQLNFRTYInGGLKFDSADIACWGALRSNGMVGSIIKNKVYVNVSRWYLLLES 154
Cdd:cd10289 8 WLDLAGSLLKGKELE---ALLKSLNSYLASRTFL-VGYSLTLADVAVFSALYPSGQKLSDKEKKKFPHVTRWFNHIQN 81
|
|
| GluRS_N |
pfam18466 |
Glutamate--tRNA ligase N-terminal domain; This is an N-terminal domain of Glutamate--tRNA ... |
23-65 |
3.27e-09 |
|
Glutamate--tRNA ligase N-terminal domain; This is an N-terminal domain of Glutamate--tRNA ligase (GluRS, EC:6.1.1.17). The domain adopts a classical glutathione S-transferase (GST)-like fold and it interacts with tRNA-aminoacylation cofactor ARC1 (Arc1p) N-terminal domain for the formation of aminoacyl-tRNA synthetase (aaRS) complex in yeast.
Pssm-ID: 408259 Cd Length: 55 Bit Score: 53.25 E-value: 3.27e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2130400838 23 RLVNDSKSDASVTVEFVDDKKSAAATFDG------------KSDNALEAIVAKFP 65
Cdd:pfam18466 1 RFVNASKSDVSITIEFVDDKKVDPADFDSsvkltpggktiyGSEDVLNKLAEKFP 55
|
|
| GST_C_GluProRS_N |
cd10309 |
Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional ... |
77-154 |
1.53e-08 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional Glutamyl-Prolyl-tRNA synthetase; Glutathione S-transferase (GST) C-terminal domain family, bifunctional GluRS-Prolyl-tRNA synthetase (GluProRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of GluProRS from higher eukaryotes. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. The GST_C-like domain of GluProRS may be involved in protein-protein interactions, mediating the formation of the multi-aaRS complex in higher eukaryotes. The multi-aaRS complex acts as a molecular hub for protein synthesis. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.
Pssm-ID: 198342 [Multi-domain] Cd Length: 81 Bit Score: 51.94 E-value: 1.53e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2130400838 77 WIKLAAEELviKNFQKLAQSLEKLDAQLNFRTYINGGlKFDSADIACWGALRSNGMVGSiiKNKVYVNVSRWYLLLES 154
Cdd:cd10309 8 WISFSAGRL--SCDQDFSSALSYLDKALSLRTYLVGN-SLTLADFAVWAALRGNGEWLA--SKEKYVNVTRWFKFISS 80
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
202-248 |
8.77e-07 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 49.02 E-value: 8.77e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2130400838 202 VTRFPPEPSGYLHIGHAKAALLNQYFAQA-----YKGKLIIRFDDTNPSKEK 248
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAyrklgYKVRCIALIDDAGGLIGD 52
|
|
| GST_C_YfcG_like |
cd10291 |
C-terminal, alpha helical domain of Escherichia coli YfcG Glutathione S-transferases and ... |
87-158 |
8.39e-05 |
|
C-terminal, alpha helical domain of Escherichia coli YfcG Glutathione S-transferases and related uncharacterized proteins; Glutathione S-transferase (GST) C-terminal domain family, YfcG-like subfamily; composed of the Escherichia coli YfcG and related proteins. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST active site is located in a cleft between the N- and C-terminal domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. YfcG is one of nine GST homologs in Escherichia coli. It is expressed predominantly during the late stationary phase where the predominant form of GSH is glutathionylspermidine (GspSH), suggesting that YfcG might interact with GspSH. It has very low or no GSH transferase or peroxidase activity, but displays a unique disulfide bond reductase activity that is comparable to thioredoxins (TRXs) and glutaredoxins (GRXs). However, unlike TRXs and GRXs, YfcG does not contain a redox active cysteine residue and may use a bound thiol disulfide couple such as 2GSH/GSSG for activity. The crystal structure of YcfG reveals a bound GSSG molecule in its active site. The actual physiological substrates for YfcG are yet to be identified.
Pssm-ID: 198324 [Multi-domain] Cd Length: 110 Bit Score: 42.25 E-value: 8.39e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2130400838 87 IKNFQKLAQSLEK-LDAQLNFRTYInGGLKFDSADIACWGALRSNGMVGSIIKNkvYVNVSRWYLLLESNPSF 158
Cdd:cd10291 38 IKRYTNETKRLYGvLDRRLAKSKYL-AGDEYSIADIAIWPWVARHEWQGIDLAD--FPNLKRWFERLAARPAV 107
|
|
| GST_C_Ure2p_like |
cd03178 |
C-terminal, alpha helical domain of Ure2p and related Glutathione S-transferase-like proteins; ... |
77-160 |
1.16e-04 |
|
C-terminal, alpha helical domain of Ure2p and related Glutathione S-transferase-like proteins; Glutathione S-transferase (GST) C-terminal domain family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p, YfcG and YghU from Escherichia coli, and related GST-like proteins. Ure2p is a regulator for nitrogen catabolism in yeast. It represses the expression of several gene products involved in the use of poor nitrogen sources when rich sources are available. A transmissible conformational change of Ure2p results in a prion called [Ure3], an inactive, self-propagating and infectious amyloid. Ure2p displays a GST fold containing an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. The N-terminal thioredoxin-fold domain is sufficient to induce the [Ure3] phenotype and is also called the prion domain of Ure2p. In addition to its role in nitrogen regulation, Ure2p confers protection to cells against heavy metal ion and oxidant toxicity, and shows glutathione (GSH) peroxidase activity. YfcG and YghU are two of the nine GST homologs in the genome of Escherichia coli. They display very low or no GSH transferase, but show very good disulfide bond oxidoreductase activity. YghU also shows modest organic hydroperoxide reductase activity. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of GSH with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST active site is located in a cleft between the N- and C-terminal domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain.
Pssm-ID: 198288 [Multi-domain] Cd Length: 110 Bit Score: 41.85 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 77 WIKLAAEELV---IKNFQKLAQSLEK-LDAQLNFRTYINGGlKFDSADIACWGALRSNGMVGSIIKNKvYVNVSRWYLLL 152
Cdd:cd03178 25 HFLYFAPEKIpyaIERYTDEVKRLYGvLDKRLSDRPYLAGE-EYSIADIALYPWTHYADLGGFADLSE-YPNVKRWLERI 102
|
....*...
gi 2130400838 153 ESNPSFGQ 160
Cdd:cd03178 103 AARPAVQK 110
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
202-268 |
1.05e-03 |
|
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.
Pssm-ID: 173912 [Multi-domain] Cd Length: 105 Bit Score: 39.06 E-value: 1.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130400838 202 VTRFPPEPsGYLHIGHAKaaLLNQYFAQAYkgKLIIRFDDTNPSKEKT---EFQDSILEDLELLGIKGDR 268
Cdd:cd02156 1 KARFPGEP-GYLHIGHAK--LICRAKGIAD--QCVVRIDDNPPVKVWQdphELEERKESIEEDISVCGED 65
|
|
| |
