|
Name |
Accession |
Description |
Interval |
E-value |
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
24-593 |
0e+00 |
|
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439943 [Multi-domain] Cd Length: 589 Bit Score: 584.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 24 RTHICDELSTSNKNEKVSVMGWLsHKRMD----RFFVLRDAYGSVQAKIS--ASSKLQSLLKDIPYESVVRVDGIVVDRG 97
Cdd:COG0173 3 RTHYCGELRESDVGQEVTLSGWV-HRRRDhgglIFIDLRDRYGITQVVFDpdDSAEAFEKAEKLRSEYVIAVTGKVRARP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 98 -DNRNSKMKTGDIEIDVEELTVLNKAtSNIPMLPD--ANANERTRLKYRYIDLRSDKLQKSLRLRSEFVHNVRRFLVEKs 174
Cdd:COG0173 82 eGTVNPKLPTGEIEVLASELEILNKA-KTPPFQIDddTDVSEELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDEN- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 175 GFVDVETPTLFRRTPGGAAEFVVPApSPNQGLAYSLPQSPQQFKQLLMVGAIDRYFQIARCYRDEGSKGDRQPEFTQVDV 254
Cdd:COG0173 160 GFLEIETPILTKSTPEGARDYLVPS-RVHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFRDEDLRADRQPEFTQLDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 255 EMSFTTQNGVMQLIEDMIISAWPESLNhIKPKSPFPRIPYSDAMRLYGIDKPDMRIPWQIDDVdNDIF---EF--LQKDI 329
Cdd:COG0173 239 EMSFVDQEDVFELMEGLIRHLFKEVLG-VELPTPFPRMTYAEAMERYGSDKPDLRFGLELVDV-TDIFkdsGFkvFAGAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 330 DDDTwRSRILVCRGAGKttISNSMKNEW---------KRL--IQMNENG------KNFaicHPSQKrwfkpfdnQKLIDQ 392
Cdd:COG0173 317 ENGG-RVKAINVPGGAS--LSRKQIDELtefakqygaKGLayIKVNEDGlkspiaKFL---SEEEL--------AAILER 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 393 FGLIDEDVLIVCWGNSEGVYWTL--------EVCGLRSKSNVTAHWIVDFPLFSF--EEGQLVSTHHPFTAPLEKDIDIL 462
Cdd:COG0173 383 LGAKPGDLIFFVADKPKVVNKALgalrlklgKELGLIDEDEFAFLWVVDFPLFEYdeEEGRWVAMHHPFTMPKDEDLDLL 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 463 YSNdidkLLQITGQHYDLVINGVEMGGGSIRIENSEIQRHVLKVLGEPTDEME----HLLNALSHGAPPHGGFALGLDRF 538
Cdd:COG0173 463 ETD----PGKVRAKAYDLVLNGYELGGGSIRIHDPELQEKVFELLGISEEEAEekfgFLLEAFKYGAPPHGGIAFGLDRL 538
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 32566633 539 VAMLTSDGNpltpVRDVIAFPKTKNGKDLMSDAPATLSQKQLERYGISLLPNAVE 593
Cdd:COG0173 539 VMLLAGEDS----IRDVIAFPKTQSAQDLMTGAPSEVDEKQLKELHIRLRPPEKK 589
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
24-591 |
0e+00 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 583.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 24 RTHICDELSTSNKNEKVSVMGWLsHKRMD----RFFVLRDAYGSVQAKISASSKLQSLLKDIPYESVVRVDGIVVDRGD- 98
Cdd:PRK00476 4 RTHYCGELRESHVGQTVTLCGWV-HRRRDhgglIFIDLRDREGIVQVVFDPDAEAFEVAESLRSEYVIQVTGTVRARPEg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 99 NRNSKMKTGDIEIDVEELTVLNKA-TSNIPMLPDANANERTRLKYRYIDLRSDKLQKSLRLRSEFVHNVRRFLvEKSGFV 177
Cdd:PRK00476 83 TVNPNLPTGEIEVLASELEVLNKSkTLPFPIDDEEDVSEELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFL-DDNGFL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 178 DVETPTLFRRTPGGAAEFVVPApSPNQGLAYSLPQSPQQFKQLLMVGAIDRYFQIARCYRDEGSKGDRQPEFTQVDVEMS 257
Cdd:PRK00476 162 EIETPILTKSTPEGARDYLVPS-RVHPGKFYALPQSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADRQPEFTQIDIEMS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 258 FTTQNGVMQLIEDMIISAWPESLNhIKPKSPFPRIPYSDAMRLYGIDKPDMRIPWQIDDVdNDIF---EFLQ-KDIDDDT 333
Cdd:PRK00476 241 FVTQEDVMALMEGLIRHVFKEVLG-VDLPTPFPRMTYAEAMRRYGSDKPDLRFGLELVDV-TDLFkdsGFKVfAGAANDG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 334 WRSRILVCRGAGkTTISNSMKNEW---------KRL--IQMNENG------KNFaicHPSQKrwfkpfdnQKLIDQFGLI 396
Cdd:PRK00476 319 GRVKAIRVPGGA-AQLSRKQIDELtefakiygaKGLayIKVNEDGlkgpiaKFL---SEEEL--------AALLERTGAK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 397 DEDVLIVCWGNSEGVYwtlEVCG-LRSKsnvTAH-------------WIVDFPLFSF--EEGQLVSTHHPFTAPLEKDID 460
Cdd:PRK00476 387 DGDLIFFGADKAKVVN---DALGaLRLK---LGKelglidedkfaflWVVDFPMFEYdeEEGRWVAAHHPFTMPKDEDLD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 461 ILYSNDidkLLQITGQHYDLVINGVEMGGGSIRIENSEIQRHVLKVLGEPTDEME----HLLNALSHGAPPHGGFALGLD 536
Cdd:PRK00476 461 ELETTD---PGKARAYAYDLVLNGYELGGGSIRIHRPEIQEKVFEILGISEEEAEekfgFLLDALKYGAPPHGGIAFGLD 537
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 32566633 537 RFVAMLTSDGNpltpVRDVIAFPKTKNGKDLMSDAPATLSQKQLERYGISLLPNA 591
Cdd:PRK00476 538 RLVMLLAGADS----IRDVIAFPKTQSAQDLLTGAPSPVDEKQLRELGIRLRKKE 588
|
|
| aspS_bact |
TIGR00459 |
aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be ... |
24-589 |
4.94e-166 |
|
aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be discriminating (6.1.1.12) or nondiscriminating (6.1.1.23). In a multiple sequence alignment of representative asparaginyl-tRNA synthetases (asnS), archaeal/eukaryotic type aspartyl-tRNA synthetases (aspS_arch), and bacterial type aspartyl-tRNA synthetases (aspS_bact), there is a striking similarity between asnS and aspS_arch in gap pattern and in sequence, and a striking divergence of aspS_bact. Consequently, a separate model was built for each of the three groups. This model, aspS_bact, represents aspartyl-tRNA synthetases from the Bacteria and from mitochondria. In some species, this enzyme aminoacylates tRNA for both Asp and Asn; Asp-tRNA(asn) is subsequently transamidated to Asn-tRNA(asn). This model generates very low scores for the archaeal type of aspS and for asnS; scores between the trusted and noise cutoffs represent fragmentary sequences. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 211576 [Multi-domain] Cd Length: 583 Bit Score: 485.39 E-value: 4.94e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 24 RTHICDELSTSNKNEKVSVMGWLsHKRMDR----FFVLRDAYGSVQAKISASSKLQSLLKDIPYESVVRVDGIVVDRGDN 99
Cdd:TIGR00459 2 RTHYCGQLRTEHLGQTVTLAGWV-NRRRDLggliFIDLRDRSGIVQVVCDPDADALKLAKGLRNEDVVQVKGKVSARPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 100 R-NSKMKTGDIEIDVEELTVLNKATSNIPMLPDANANERTRLKYRYIDLRSDKLQKSLRLRSEFVHNVRRFLVEKsGFVD 178
Cdd:TIGR00459 81 NiNRNLDTGEIEILAESITLLNKSKTPPLIIEKTDAEEEVRLKYRYLDLRRPEMQQRLKLRHKVTKAVRNFLDQQ-GFLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 179 VETPTLFRRTPGGAAEFVVPApSPNQGLAYSLPQSPQQFKQLLMVGAIDRYFQIARCYRDEGSKGDRQPEFTQVDVEMSF 258
Cdd:TIGR00459 160 IETPMLTKSTPEGARDYLVPS-RVHKGEFYALPQSPQLFKQLLMVSGVDRYYQIARCFRDEDLRADRQPEFTQIDMEMSF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 259 TTQNGVMQLIEDMIISAWPESLNhIKPKSPFPRIPYSDAMRLYGIDKPDMRIPWQIDDVdNDIF---EFLQ-KDIDDDTW 334
Cdd:TIGR00459 239 MTQEDVMELIEKLVSHVFLEVKG-IDLKKPFPVMTYAEAMERYGSDKPDLRFPLELIDV-TDLFkdsEFKVfSNLINDGG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 335 RSRILVCRGaGKTTISNSMKNEWKRL-----------IQMNENGKNFAIChpsqkrwfKPFDNQKLIDQFGLIDE---DV 400
Cdd:TIGR00459 317 RVKAIRVPG-GWAELSRKSIKELRKFakeygakglayLKVNEDGINSPIK--------KFLDEKKGKILLERTDAqngDI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 401 LIVCWGNSEGVyWT------LEV---CGLRSKSNVTAHWIVDFPLFSF-EEGQLVSTHHPFTAPLEKDIDILYSNDIDKL 470
Cdd:TIGR00459 388 LLFGAGSKKIV-LDalgalrLKLgkdLGLVDPDLFSFLWVVDFPMFEKdKEGRLCAAHHPFTMPKDEDLENLEAAPEEAL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 471 lqitGQHYDLVINGVEMGGGSIRIENSEIQRHVLKVLG----EPTDEMEHLLNALSHGAPPHGGFALGLDRFVAMLTSDG 546
Cdd:TIGR00459 467 ----AEAYDLVLNGVELGGGSIRIHDPEVQKKVFEILGidpeEAREKFGFLLEAFKYGTPPHAGFALGLDRLMMLLTGTD 542
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 32566633 547 NpltpVRDVIAFPKTKNGKDLMSDAPATLSQKQLERYGISLLP 589
Cdd:TIGR00459 543 N----IRDVIAFPKTTAAACLMTEAPSFIDEKQLEELSIKYVV 581
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
156-563 |
5.27e-141 |
|
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. AspRS is a homodimer, which attaches a specific amino acid to the 3' OH group of ribose of the appropriate tRNA. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. AspRS in this family differ from those found in the AsxRS family by a GAD insert in the core domain.
Pssm-ID: 238400 [Multi-domain] Cd Length: 280 Bit Score: 410.04 E-value: 5.27e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 156 LRLRSEFVHNVRRFLVEKsGFVDVETPTLFRRTPGGAAEFVVPAPSpNQGLAYSLPQSPQQFKQLLMVGAIDRYFQIARC 235
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQ-GFVEIETPILTKSTPEGARDFLVPSRL-HPGKFYALPQSPQLFKQLLMVSGFDRYFQIARC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 236 YRDEGSKGDRQPEFTQVDVEMSFTTQNGVMQLIEDMIISAWPESLNhIKPKSPFPRIPYSDAMRLYGidkpdmripwqid 315
Cdd:cd00777 79 FRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG-VELTTPFPRMTYAEAMERYG------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 316 dvdndiFEFLqkdidddtwrsrilvcrgagkttisnsmknewkrliqmnengknfaichpsqkrwfkpfdnqklidqfgl 395
Cdd:cd00777 145 ------FKFL---------------------------------------------------------------------- 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 396 idedvlivcwgnsegvywtlevcglrsksnvtahWIVDFPLFSF--EEGQLVSTHHPFTAPLEKDIDILYSNDIDkllqI 473
Cdd:cd00777 149 ----------------------------------WIVDFPLFEWdeEEGRLVSAHHPFTAPKEEDLDLLEKDPED----A 190
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 474 TGQHYDLVINGVEMGGGSIRIENSEIQRHVLKVLG----EPTDEMEHLLNALSHGAPPHGGFALGLDRFVAMLTSdgnpL 549
Cdd:cd00777 191 RAQAYDLVLNGVELGGGSIRIHDPDIQEKVFEILGlseeEAEEKFGFLLEAFKYGAPPHGGIALGLDRLVMLLTG----S 266
|
410
....*....|....
gi 32566633 550 TPVRDVIAFPKTKN 563
Cdd:cd00777 267 ESIRDVIAFPKTQN 280
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
17-580 |
1.74e-133 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 404.17 E-value: 1.74e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 17 STSSYTVRTHICDELSTSNKNEKVSVMGWL-SHKRMD--RFFVLRDAYGSVQAKISASS--KLQSLLKDIPYESVVRVDG 91
Cdd:PLN02903 52 SQLTWPSRSHLCGALSVNDVGSRVTLCGWVdLHRDMGglTFLDVRDHTGIVQVVTLPDEfpEAHRTANRLRNEYVVAVEG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 92 IVVDRGDNR-NSKMKTGDIEIDVEELTVLNKATSNIPML------PDANANERTRLKYRYIDLRSDKLQKSLRLRSEFVH 164
Cdd:PLN02903 132 TVRSRPQESpNKKMKTGSVEVVAESVDILNVVTKSLPFLvttadeQKDSIKEEVRLRYRVLDLRRPQMNANLRLRHRVVK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 165 NVRRFLVEKSGFVDVETPTLFRRTPGGAAEFVVPapSPNQ-GLAYSLPQSPQQFKQLLMVGAIDRYFQIARCYRDEGSKG 243
Cdd:PLN02903 212 LIRRYLEDVHGFVEIETPILSRSTPEGARDYLVP--SRVQpGTFYALPQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 244 DRQPEFTQVDVEMSFTTQNGVMQLIEDMIISAWPESLNHIKPkSPFPRIPYSDAMRLYGIDKPDMRIPWQIDDVDnDIFE 323
Cdd:PLN02903 290 DRQPEFTQLDMELAFTPLEDMLKLNEDLIRQVFKEIKGVQLP-NPFPRLTYAEAMSKYGSDKPDLRYGLELVDVS-DVFA 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 324 FLQKDIDDDTWRSRILV---CRGAGKTTISNSMK------NEWKR-------LIQMNENGKNFAIchPSQKRWFKPFDNQ 387
Cdd:PLN02903 368 ESSFKVFAGALESGGVVkaiCVPDGKKISNNTALkkgdiyNEAIKsgakglaFLKVLDDGELEGI--KALVESLSPEQAE 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 388 KLIDQFGLIDEDVLIVCWGNSEGVYWTL--------EVCGLRSKSNVTAHWIVDFPLFSF--EEGQLVSTHHPFTAPLEK 457
Cdd:PLN02903 446 QLLAACGAGPGDLILFAAGPTSSVNKTLdrlrqfiaKTLDLIDPSRHSILWVTDFPMFEWneDEQRLEALHHPFTAPNPE 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 458 DIDilysnDIDKLLQITgqhYDLVINGVEMGGGSIRIENSEIQRHVLKVLGEPTDEME----HLLNALSHGAPPHGGFAL 533
Cdd:PLN02903 526 DMG-----DLSSARALA---YDMVYNGVEIGGGSLRIYRRDVQQKVLEAIGLSPEEAEskfgYLLEALDMGAPPHGGIAY 597
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 32566633 534 GLDRFVAMLTSDgnplTPVRDVIAFPKTKNGKDLMSDAPATLSQKQL 580
Cdd:PLN02903 598 GLDRLVMLLAGA----KSIRDVIAFPKTTTAQCALTRAPSEVDDKQL 640
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
28-591 |
1.40e-112 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 351.98 E-value: 1.40e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 28 CDELSTSNKNEKVSVMGWLSHKRmDR----FFVLRDAYGSVQAKIS---ASSKLQSLLKDIPYESVVRVDGIVVDR-GDN 99
Cdd:PRK12820 9 CGHLSLDDTGREVCLAGWVDAFR-DHgellFIHLRDRNGFIQAVFSpeaAPADVYELAASLRAEFCVALQGEVQKRlEET 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 100 RNSKMKTGDIEIDVEELTVLNK------ATSNIPMLPDANA------NERTRLKYRYIDLRSDKLQKSLRLRSEFVHNVR 167
Cdd:PRK12820 88 ENPHIETGDIEVFVRELSILAAsealpfAISDKAMTAGAGSagadavNEDLRLQYRYLDIRRPAMQDHLAKRHRIIKCAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 168 RFLvEKSGFVDVETPTLFRRTPGGAAEFVVPAPSPNQGLaYSLPQSPQQFKQLLMVGAIDRYFQIARCYRDEGSKGDRQP 247
Cdd:PRK12820 168 DFL-DSRGFLEIETPILTKSTPEGARDYLVPSRIHPKEF-YALPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 248 EFTQVDVEMSFTTQNGVMQLIEDMIISAWpeSLNHIKPKSPFPRIPYSDAMRLYGIDKPDMRIPWQIDDVdNDIFEFLQ- 326
Cdd:PRK12820 246 EFTQLDIEASFIDEEFIFELIEELTARMF--AIGGIALPRPFPRMPYAEAMDTTGSDRPDLRFDLKFADA-TDIFENTRy 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 327 ---KDIDDDTWRSRILVCRGAGKTTISNSMKNEWKRLIQMNENGKNFAICHPSQK-------RWFKPFDNQKLIDQFGLI 396
Cdd:PRK12820 323 gifKQILQRGGRIKGINIKGQSEKLSKNVLQNEYAKEIAPSFGAKGMTWMRAEAGgldsnivQFFSADEKEALKRRFHAE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 397 DEDVLIVCWGNSEGVYWTL---------EVCGLRSKSNVTAHWIVDFPLF-SFEEGQLVSTHHPFTAPLEKDIDILysnD 466
Cdd:PRK12820 403 DGDVIIMIADASCAIVLSAlgqlrlhlaDRLGLIPEGVFHPLWITDFPLFeATDDGGVTSSHHPFTAPDREDFDPG---D 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 467 IDKLLQITGQHYDLVINGVEMGGGSIRIENSEIQRHVLKVLGEPTDEMEH----LLNALSHGAPPHGGFALGLDRFVAML 542
Cdd:PRK12820 480 IEELLDLRSRAYDLVVNGEELGGGSIRINDKDIQLRIFAALGLSEEDIEDkfgfFLRAFDFAAPPHGGIALGLDRVVSMI 559
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 32566633 543 TSdgnplTP-VRDVIAFPKTKNGKDLMSDAPATLSQKQLERYGISLLPNA 591
Cdd:PRK12820 560 LQ-----TPsIREVIAFPKNRSAACPLTGAPSEVAQEQLAELGLLDLGDA 604
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
135-562 |
1.09e-111 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 336.46 E-value: 1.09e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 135 NERTRLKYRYIDLRSDKLQKSLRLRSEFVHNVRRFLVEKsGFVDVETPTLFR-RTPGGAAEFVVPapSPNQGLAYSLPQS 213
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDEN-GFLEVETPILTKsATPEGARDFLVP--SRALGKFYALPQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 214 PQQFKQLLMVGAIDRYFQIARCYRDEGSKGDRQPEFTQVDVEMSFTTQNGVMQLIEDMIISAWPESLNH---------IK 284
Cdd:pfam00152 78 PQLYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIakeleggtlLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 285 PKSPFPRIPYSDAMR----------LYGIDKPDMRIPWQIdDVDNDIFEFLqkdidddtwrsrilvcrgagkttisnsmk 354
Cdd:pfam00152 158 LKKPFPRITYAEAIEklngkdveelGYGSDKPDLRFLLEL-VIDKNKFNPL----------------------------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 355 newkrliqmnengknfaichpsqkrwfkpfdnqklidqfglidedvlivcwgnsegvywtlevcglrsksnvtahWIVDF 434
Cdd:pfam00152 208 ---------------------------------------------------------------------------WVTDF 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 435 PlfsfeegqlvSTHHPFTAPLEKDIDILysndidkllqitGQHYDLVINGVEMGGGSIRIENSEIQRHVLKVLGEPTDEM 514
Cdd:pfam00152 213 P----------AEHHPFTMPKDEDDPAL------------AEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDPEEA 270
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 32566633 515 ----EHLLNALSHGAPPHGGFALGLDRFVAMLTSdgnpLTPVRDVIAFPKTK 562
Cdd:pfam00152 271 eekfGFYLDALKYGAPPHGGLGIGLDRLVMLLTG----LESIREVIAFPKTR 318
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
24-559 |
2.45e-60 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 206.96 E-value: 2.45e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 24 RTHICDELSTSNKNEKVSVMGWLsHKRMD----RFFVLRDAYGSVQAKISASS--KLQSLLKDIPYESVVRVDGIVVdrg 97
Cdd:PRK05159 3 KRHLTSELTPELDGEEVTLAGWV-HEIRDlggiAFLILRDRSGIIQVVVKKKVdeELFETIKKLKRESVVSVTGTVK--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 98 dnRNSKMKTGdIEIDVEELTVLNKATSNIPMLP--DANANERTRLKYRYIDLRSDKLQKSLRLRSEFVHNVRRFLVEKsG 175
Cdd:PRK05159 79 --ANPKAPGG-VEVIPEEIEVLNKAEEPLPLDIsgKVLAELDTRLDNRFLDLRRPRVRAIFKIRSEVLRAFREFLYEN-G 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 176 FVDVETPTLFRR-TPGGAAEFVV-----PapspnqglAYsLPQSPQQFKQLLMVGAIDRYFQIARCYRDEGSKGDRQ-PE 248
Cdd:PRK05159 155 FTEIFTPKIVASgTEGGAELFPIdyfekE--------AY-LAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSRHlNE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 249 FTQVDVEMSFTT-QNGVMQLIEDMIISAwpesLNHIK----------------PKSPFPRIPYSDAMRLygIDKPDMRIP 311
Cdd:PRK05159 226 YTSIDVEMGFIDdHEDVMDLLENLLRYM----YEDVAencekelellgielpvPETPIPRITYDEAIEI--LKSKGNEIS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 312 WqIDDVDNdifeflqkdidddtwrsrilvcrgAGKTTISNSMKNEWkrliqmneNGKNFAICH-PSQKRwfkPFdnqkli 390
Cdd:PRK05159 300 W-GDDLDT------------------------EGERLLGEYVKEEY--------GSDFYFITDyPSEKR---PF------ 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 391 dqfglidedvlivcwgnsegvywtlevcglrsksnvtahwivdfplfsfeegqlvsthhpFTAPLEKDIDILYSndidkl 470
Cdd:PRK05159 338 ------------------------------------------------------------YTMPDEDDPEISKS------ 351
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 471 lqitgqhYDLVINGVEMGGGSIRIENSEIQRHVLKVLGEPTDEMEHLLNALSHGAPPHGGFALGLDRFVAMLTSDGNplt 550
Cdd:PRK05159 352 -------FDLLFRGLEITSGGQRIHRYDMLVESIKEKGLNPESFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLEN--- 421
|
....*....
gi 32566633 551 pVRDVIAFP 559
Cdd:PRK05159 422 -IREAVLFP 429
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
156-562 |
7.82e-59 |
|
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of class II aminoacyl-tRNA synthetases of the subgroup containing aspartyl, lysyl, and asparaginyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. Nearly all class II tRNA synthetases are dimers and enzymes in this subgroup are homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.
Pssm-ID: 238358 [Multi-domain] Cd Length: 269 Bit Score: 197.70 E-value: 7.82e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 156 LRLRSEFVHNVRRFLVEKsGFVDVETPTLFRRTPGGAAE-FVVPAPSPnqGLAYSLPQSPQQFKQLLMVGAIDRYFQIAR 234
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDR-GFLEVETPMLQKITGGAGARpFLVKYNAL--GLDYYLRISPQLFKKRLMVGGLDRVFEINR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 235 CYRDEGSKGDRQPEFTQVDVEMSFTTQNGVMQLIEDMIISAWPESLNH---------IKPKSPFPRIPYSDAMRLYGidk 305
Cdd:cd00669 78 NFRNEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVtavtygfelEDFGLPFPRLTYREALERYG--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 306 pdmripwqiddvdndifeflqkdidddtwrsrilvcrgagkttisnsmknewkrliqmnengknfaichpsqkrwfKPFd 385
Cdd:cd00669 155 ----------------------------------------------------------------------------QPL- 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 386 nqklidqfglidedvlivcwgnsegvywtlevcglrsksnvtahWIVDFPLFSfeegqlvstHHPFTAPlekdidilysN 465
Cdd:cd00669 158 --------------------------------------------FLTDYPAEM---------HSPLASP----------H 174
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 466 DIDKLLqitGQHYDLVINGVEMGGGSIRIENSEIQRHVLKVLGEPTDEM----EHLLNALSHGAPPHGGFALGLDRFVAM 541
Cdd:cd00669 175 DVNPEI---ADAFDLFINGVEVGNGSSRLHDPDIQAEVFQEQGINKEAGmeyfEFYLKALEYGLPPHGGLGIGIDRLIML 251
|
410 420
....*....|....*....|.
gi 32566633 542 LTSDGNpltpVRDVIAFPKTK 562
Cdd:cd00669 252 MTNSPT----IREVIAFPKMR 268
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
24-563 |
3.71e-51 |
|
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl/asparaginyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439788 [Multi-domain] Cd Length: 430 Bit Score: 181.79 E-value: 3.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 24 RTHICDELSTSNKNEKVSVMGWLSHKRmD----RFFVLRDAYGSVQAKISASS-KLQSLLKDIPYESVVRVDGIVVDrgd 98
Cdd:COG0017 1 KRTYIKDLLPEHVGQEVTVAGWVRTKR-DsggiSFLILRDGSGFIQVVVKKDKlENFEEAKKLTTESSVEVTGTVVE--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 99 nrnSKMKTGDIEIDVEELTVLNKATSNIPMLPDaNANERTRLKYRYIDLRSDKLQKSLRLRSEFVHNVRRFLVEKsGFVD 178
Cdd:COG0017 77 ---SPRAPQGVELQAEEIEVLGEADEPYPLQPK-RHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQER-GFVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 179 VETPTLfrrTPG---GAAE-FVV-----PApspnqglaySLPQSPQQFKQLlMVGAIDRYFQIARCYRDEGSKGDRQ-PE 248
Cdd:COG0017 152 VHTPII---TASateGGGElFPVdyfgkEA---------YLTQSGQLYKEA-LAMALEKVYTFGPTFRAEKSNTRRHlAE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 249 FTQVDVEMSFTTQNGVMQLIEDMIISA-----------------WPESLNHIkPKSPFPRIPYSDAMRLYGidKPDMRIP 311
Cdd:COG0017 219 FWMIEPEMAFADLEDVMDLAEEMLKYIikyvlencpeeleflgrDVERLEKV-PESPFPRITYTEAIEILK--KSGEKVE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 312 WQIDdvdndifefLQKDidddtwRSRILVcrgagkttisnsmknEW--KRLIqmnengknFAICHPSQKrwfKPF----- 384
Cdd:COG0017 296 WGDD---------LGTE------HERYLG---------------EEffKKPV--------FVTDYPKEI---KAFymkpn 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 385 -DNQKLidqfglidedvlivcwgnsegvywtlevcglrSKSnvtahwivdfplfsfeegqlvsthhpftaplekdidily 463
Cdd:COG0017 335 pDDPKT--------------------------------VAA--------------------------------------- 343
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 464 sndidkllqitgqhYDLVINGV-EMGGGSIRIENSEIQRHVLKVLGEPTDEMEHLLNALSHGAPPHGGFALGLDRFVAML 542
Cdd:COG0017 344 --------------FDLLAPGIgEIIGGSQREHRYDVLVERIKEKGLDPEDYEWYLDLRRYGSVPHAGFGLGLERLVMWL 409
|
570 580
....*....|....*....|.
gi 32566633 543 TSDGNpltpVRDVIAFPKTKN 563
Cdd:COG0017 410 TGLEN----IREVIPFPRDPG 426
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
24-152 |
3.36e-44 |
|
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli aspartyl-tRNA synthetase (AspRS), the human mitochondrial (mt) AspRS-2, the discriminating (D) Thermus thermophilus AspRS-1, and the nondiscriminating (ND) Helicobacter pylori AspRS. These homodimeric enzymes are class2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. Human mtAspRS participates in mitochondrial biosynthesis; this enzyme been shown to charge E.coli native tRNAsp in addition to in vitro transcribed human mitochondrial tRNAsp. T. thermophilus is rare among bacteria in having both a D_AspRS and a ND_AspRS. H.pylori ND-AspRS can charge both tRNAASp and tRNAAsn, it is fractionally more efficient at aminoacylating tRNAAsp over tRNAAsn. The H.pylori genome does not contain AsnRS.
Pssm-ID: 239812 [Multi-domain] Cd Length: 135 Bit Score: 153.83 E-value: 3.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 24 RTHICDELSTSNKNEKVSVMGWLSHKRMD---RFFVLRDAYGSVQAKIS-ASSKLQSLLKDIPYESVVRVDGIVVDRG-D 98
Cdd:cd04317 1 RTHYCGELRESHVGQEVTLCGWVQRRRDHgglIFIDLRDRYGIVQVVFDpEEAPEFELAEKLRNESVIQVTGKVRARPeG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 32566633 99 NRNSKMKTGDIEIDVEELTVLNKATsNIPMLPD--ANANERTRLKYRYIDLRSDKL 152
Cdd:cd04317 81 TVNPKLPTGEIEVVASELEVLNKAK-TLPFEIDddVNVSEELRLKYRYLDLRRPKM 135
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
133-562 |
4.36e-31 |
|
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure and the presence of three characteristic sequence motifs in the core domain. This family includes AsnRS as well as a subgroup of AspRS. AsnRS and AspRS are homodimers, which attach either asparagine or aspartate to the 3'OH group of ribose of the appropriate tRNA. While archaea lack asnRS, they possess a non-discriminating aspRS, which can mischarge Asp-tRNA with Asn. Subsequently, a tRNA-dependent aspartate amidotransferase converts the bound aspartate to asparagine. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate.
Pssm-ID: 238399 [Multi-domain] Cd Length: 322 Bit Score: 123.45 E-value: 4.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 133 NANERTRLKYRYIDLRSDKLQKSLRLRSEFVHNVRRFLVEKsGFVDVETPTLFRR-TPGGAAEFVV-----Papspnqgl 206
Cdd:cd00776 1 DANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLREN-GFTEVHTPKITSTdTEGGAELFKVsyfgkP-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 207 AYsLPQSPQQFKQlLMVGAIDRYFQIARCYRDEGSKGDRQ-PEFTQVDVEMSF-TTQNGVMQLIEDMIISAW-------- 276
Cdd:cd00776 72 AY-LAQSPQLYKE-MLIAALERVYEIGPVFRAEKSNTRRHlSEFWMLEAEMAFiEDYNEVMDLIEELIKYIFkrvlerca 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 277 --PESLNHI-----KPKSPFPRIPYSDAmrlygidkpdmripwqiddvdndifeflqkdidddtwrsrilvcrgagktti 349
Cdd:cd00776 150 keLELVNQLnrellKPLEPFPRITYDEA---------------------------------------------------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 350 snsmknewkrlIQM-NENGKNFAIchpsqkRWFKPF--DNQKLIDQfgLIDEDVLIVcwgnsegvywtlevcglrsksnv 426
Cdd:cd00776 178 -----------IELlREKGVEEEV------KWGEDLstEHERLLGE--IVKGDPVFV----------------------- 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 427 tahwiVDFPLFSfeegqlvsthHPF-TAPLEKDIDILYSndidkllqitgqhYDLVINGV-EMGGGSIRIENSEIQRHVL 504
Cdd:cd00776 216 -----TDYPKEI----------KPFyMKPDDDNPETVES-------------FDLLMPGVgEIVGGSQRIHDYDELEERI 267
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 32566633 505 KVLGEPTDEMEHLLNALSHGAPPHGGFALGLDRFVAMLTSDGNpltpVRDVIAFPKTK 562
Cdd:cd00776 268 KEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDN----IREAILFPRDP 321
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
29-542 |
4.39e-25 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 109.41 E-value: 4.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 29 DELSTSNKNEKVSVMGWLSHKRM---DRFFVLRDAYGSVQAKISASSKLQS-----LLKDIPYESVVRVDGIVVDRGDNR 100
Cdd:PLN02850 73 SDLGEELAGSEVLIRGRVHTIRGkgkSAFLVLRQSGFTVQCVVFVSEVTVSkgmvkYAKQLSRESVVDVEGVVSVPKKPV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 101 NSKmkTGDIEIDVEELTVLNKATSNIPML-------------------PDANANERTRLKYRYIDLRSDKLQKSLRLRSE 161
Cdd:PLN02850 153 KGT--TQQVEIQVRKIYCVSKALATLPFNvedaarseseiekalqtgeQLVRVGQDTRLNNRVLDLRTPANQAIFRIQSQ 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 162 FVHNVRRFLVEKsGFVDVETPTLFR-RTPGGAAEFVVPApspnQGLAYSLPQSPQQFKQLLMVGAIDRYFQIARCYRDEG 240
Cdd:PLN02850 231 VCNLFREFLLSK-GFVEIHTPKLIAgASEGGSAVFRLDY----KGQPACLAQSPQLHKQMAICGDFRRVFEIGPVFRAED 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 241 SKGDRQ-PEFTQVDVEMSFTTQ-NGVMQLIEDMII-------SAWPESLNHIKPKSPFPRIPY-SDAMRLygidkpdmri 310
Cdd:PLN02850 306 SFTHRHlCEFTGLDLEMEIKEHySEVLDVVDELFVaifdglnERCKKELEAIREQYPFEPLKYlPKTLRL---------- 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 311 pwqiddvdndifeflqkdidddTWRSRILVCRGAGKTT-----ISNSMKNEWKRLIQmNENGKNFAICH--PSQKRwfkP 383
Cdd:PLN02850 376 ----------------------TFAEGIQMLKEAGVEVdplgdLNTESERKLGQLVK-EKYGTDFYILHryPLAVR---P 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 384 FdnqklidqfglidedvlivcwgnsegvywtlevcglrsksnvtahwivdfplfsfeegqlvsthhpFTAPLEKdiDILY 463
Cdd:PLN02850 430 F------------------------------------------------------------------YTMPCPD--DPKY 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32566633 464 SNDidkllqitgqhYDLVINGVEMGGGSIRIENSEIQRHVLKVLGEPTDEMEHLLNALSHGAPPHGGFALGLDRfVAML 542
Cdd:PLN02850 442 SNS-----------FDVFIRGEEIISGAQRVHDPELLEKRAEECGIDVKTISTYIDSFRYGAPPHGGFGVGLER-VVML 508
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
54-560 |
7.12e-24 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 105.85 E-value: 7.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 54 FFVLRDAYGSVQAKISASSKLQSLLKD----IPYESVVRVDGIVVDRGDNRNSKMKTgDIEIDVEELTVLNKATSNIPM- 128
Cdd:PTZ00401 98 FMVLRDGSDSVQAMAAVEGDVPKEMIDfigqIPTESIVDVEATVCKVEQPITSTSHS-DIELKVKKIHTVTESLRTLPFt 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 129 LPDANANER---------TRLKYRYIDLRSDKLQKSLRLRSEFVHNVRRFLVEkSGFVDVETPTLFRR-TPGGAAEFVVP 198
Cdd:PTZ00401 177 LEDASRKESdegakvnfdTRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLID-SDFCEIHSPKIINApSEGGANVFKLE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 199 APSPNqglAYsLPQSPQQFKQLLMVGAIDRYFQIARCYRDEGSKGDRQ-PEFTQVDVEMSFTTQ-NGVMQLIEDMI---- 272
Cdd:PTZ00401 256 YFNRF---AY-LAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNTHRHlTEFVGLDVEMRINEHyYEVLDLAESLFnyif 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 273 --ISAWPESLNHIKPKSPFPRIPY---SDAMRLYGIDKPDmripwqiDDVDndifeflqkdiDDDTWRSRIlvcrgagkt 347
Cdd:PTZ00401 332 erLATHTKELKAVCQQYPFEPLVWkltPERMKELGVGVIS-------EGVE-----------PTDKYQARV--------- 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 348 tisnsmKNEWKRLIQMNENgKNFAICHPSQKRWFKPFD-----NQKLIDQFglidedvlivcwgnsegvywtlevcglrs 422
Cdd:PTZ00401 385 ------HNMDSRMLRINYM-HCIELLNTVLEEKMAPTDdinttNEKLLGKL----------------------------- 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 423 ksnVTAHWIVDFplfsFEEGQLVSTHHPF-TAPLEKDIDILYSndidkllqitgqhYDLVINGVEMGGGSIRIENSEIQR 501
Cdd:PTZ00401 429 ---VKERYGTDF----FISDRFPSSARPFyTMECKDDERFTNS-------------YDMFIRGEEISSGAQRIHDPDLLL 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 32566633 502 HVLKVLGEPTDEMEHLLNALSHGAPPHGGFALGLDRFVAMLTSDGNpltpVRDVIAFPK 560
Cdd:PTZ00401 489 ARAKMLNVDLTPIKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSN----VRLASLFPR 543
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
24-559 |
1.14e-22 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 101.32 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 24 RTHICDEL----------STSNKNEKVSVMGWLSHKR-MDR--FFVLRDAYGSVQAKISassklqslLKDIP---YESVV 87
Cdd:PRK00484 31 RTHTAAELrakyddkekeELEELEIEVSVAGRVMLKRvMGKasFATLQDGSGRIQLYVS--------KDDVGeeaLEAFK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 88 RVD-G-IVVDRGDNRnsKMKTGDIEIDVEELTVLNKATsnIPmLPD---ANANERTRLKYRYIDL-RSDKLQKSLRLRSE 161
Cdd:PRK00484 103 KLDlGdIIGVEGTLF--KTKTGELSVKATELTLLTKSL--RP-LPDkfhGLTDVETRYRQRYVDLiVNPESRETFRKRSK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 162 FVHNVRRFLVEKsGFVDVETPTLfRRTPGGAAE--FV-------VP-----APspnqglaySLPqspqqFKQLLmVGAID 227
Cdd:PRK00484 178 IISAIRRFLDNR-GFLEVETPML-QPIAGGAAArpFIthhnaldIDlylriAP--------ELY-----LKRLI-VGGFE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 228 RYFQIARCYRDEGSkgDRQ--PEFTQVDVEMSFTTQNGVMQLIEDMIISAwpeslnhikpkspfpripysdAMRLYGIDK 305
Cdd:PRK00484 242 RVYEIGRNFRNEGI--DTRhnPEFTMLEFYQAYADYNDMMDLTEELIRHL---------------------AQAVLGTTK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 306 pdmrIPWQIDDVDndifeflqkdidddtwrsrilvcrgagkttisnsMKNEWKRlIQMNE-----NGKNFAICHPSQKRw 380
Cdd:PRK00484 299 ----VTYQGTEID----------------------------------FGPPFKR-LTMVDaikeyTGVDFDDMTDEEAR- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 381 fkpfdnqKLIDQFGLIDEDvlivcwgnsegvYWTLevcglrsksnvtAHWIVDFplfsFE---EGQLVS----THHPF-T 452
Cdd:PRK00484 339 -------ALAKELGIEVEK------------SWGL------------GKLINEL----FEefvEPKLIQptfiTDYPVeI 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 453 APLEKdidilySNDIDKllQITgQHYDLVINGVEMGggsirieN--SE-----IQRH------VLKVLGEptDEMEHL-- 517
Cdd:PRK00484 384 SPLAK------RHREDP--GLT-ERFELFIGGREIA-------NafSElndpiDQRErfeaqvEAKEAGD--DEAMFMde 445
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 32566633 518 --LNALSHGAPPHGGFALGLDRFVAMLTsdGNPltPVRDVIAFP 559
Cdd:PRK00484 446 dfLRALEYGMPPTGGLGIGIDRLVMLLT--DSP--SIRDVILFP 485
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
24-562 |
1.26e-22 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 101.99 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 24 RTHICDEL-----STSN----KNEKVSVMGWLSHKRMD---RFFVLRDAYGSVQAKISASSklqSLLKDIPYESVVRVdg 91
Cdd:PLN02502 86 VTHTAPELqekygSLENgeelEDVSVSVAGRIMAKRAFgklAFYDLRDDGGKIQLYADKKR---LDLDEEEFEKLHSL-- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 92 ivVDRGD-----NRNSKMKTGDIEIDVEELTVLNKAtsnIPMLPDANA---NERTRLKYRYIDLRSD-KLQKSLRLRSEF 162
Cdd:PLN02502 161 --VDRGDivgvtGTPGKTKKGELSIFPTSFEVLTKC---LLMLPDKYHgltDQETRYRQRYLDLIANpEVRDIFRTRAKI 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 163 VHNVRRFLvEKSGFVDVETPTLfRRTPGGAAE--FVVPAPSPNQGLaySLPQSPQQFKQLLMVGAIDRYFQIARCYRDEG 240
Cdd:PLN02502 236 ISYIRRFL-DDRGFLEVETPML-NMIAGGAAArpFVTHHNDLNMDL--YLRIATELHLKRLVVGGFERVYEIGRQFRNEG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 241 SKGDRQPEFTQVDVEMSFTTQNGVMQLIEDMIISAwpeslnhikpkspfpripysdAMRLYGidkpDMRIPWQIDDVDnd 320
Cdd:PLN02502 312 ISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGM---------------------VKELTG----SYKIKYHGIEID-- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 321 iFEflqkdiddDTWRsRIlvcrgagkttisnSMKNEWKRL--IQMNENGKNFAIchpsqkrwfkpfdNQKLIDQFGLIDE 398
Cdd:PLN02502 365 -FT--------PPFR-RI-------------SMISLVEEAtgIDFPADLKSDEA-------------NAYLIAACEKFDV 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 399 DVlivcwgnsegvywtlevcglrSKSNVTAHwIVDFPLFSFEEGQLVS----THHP-FTAPLEKdidilYSNDIDKLLqi 473
Cdd:PLN02502 409 KC---------------------PPPQTTGR-LLNELFEEFLEETLVQptfvLDHPvEMSPLAK-----PHRSKPGLT-- 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 474 tgQHYDLVINGVEMGGGSIRIENSEIQRHV----LKVLGEPTDEM----EHLLNALSHGAPPHGGFALGLDRFVAMLTSD 545
Cdd:PLN02502 460 --ERFELFINGRELANAFSELTDPVDQRERfeeqVKQHNAGDDEAmaldEDFCTALEYGLPPTGGWGLGIDRLVMLLTDS 537
|
570
....*....|....*..
gi 32566633 546 GNpltpVRDVIAFPKTK 562
Cdd:PLN02502 538 AS----IRDVIAFPAMK 550
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
29-565 |
8.87e-20 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 92.82 E-value: 8.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 29 DELSTSNKneKVSVMGWLSHKRM---DRFFVLRDAYGSVQAKISASSklqsLLKDIPYESVVRVD--GIVVDRGdnRNSK 103
Cdd:PRK12445 59 QELESLNI--EVSVAGRMMTRRImgkASFVTLQDVGGRIQLYVARDS----LPEGVYNDQFKKWDlgDIIGARG--TLFK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 104 MKTGDIEIDVEELTVLNKATSNIPMLPDANANERTRLKYRYIDL-RSDKLQKSLRLRSEFVHNVRRFLVEKsGFVDVETP 182
Cdd:PRK12445 131 TQTGELSIHCTELRLLTKALRPLPDKFHGLQDQEVRYRQRYLDLiANDKSRQTFVVRSKILAAIRQFMVAR-GFMEVETP 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 183 tLFRRTPGGAAEFVVPAPSPNQGLAYSLPQSPQQFKQLLMVGAIDRYFQIARCYRDEGSKGDRQPEFTQVDVEMSFTTQN 262
Cdd:PRK12445 210 -MMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYH 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 263 GVMQLIEDMIISAWPESLNHIKpkspfprIPYSDAMRLYGidKPdmripwqiddvdndiFEflqkdidddtwrsrilvcr 342
Cdd:PRK12445 289 DLIELTESLFRTLAQEVLGTTK-------VTYGEHVFDFG--KP---------------FE------------------- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 343 gagKTTISNSMKNewkrliqmnengknfaichpsqkrwFKPFDNQKLIDQFglidedvlivcwgnsEGVYWTLEVCGLRS 422
Cdd:PRK12445 326 ---KLTMREAIKK-------------------------YRPETDMADLDNF---------------DAAKALAESIGITV 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 423 KSNVTAHWIVDFPLFSFEEGQLVS----THHPF-TAPLEKdidilySNDIDKllQITGQhYDLVINGVEMGGGSIRIENS 497
Cdd:PRK12445 363 EKSWGLGRIVTEIFDEVAEAHLIQptfiTEYPAeVSPLAR------RNDVNP--EITDR-FEFFIGGREIGNGFSELNDA 433
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32566633 498 EIQRHVL------KVLGEptDEM----EHLLNALSHGAPPHGGFALGLDRFVAMLTSDGNpltpVRDVIAFPKTKNGK 565
Cdd:PRK12445 434 EDQAERFqeqvnaKAAGD--DEAmfydEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHT----IRDVILFPAMRPQK 505
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
39-121 |
1.00e-18 |
|
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. Class 2b aaRSs include the homodimeric aspartyl-, asparaginyl-, and lysyl-tRNA synthetases (AspRS, AsnRS, and LysRS). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Included in this group are archeal and archeal-like AspRSs which are non-discriminating and can charge both tRNAAsp and tRNAAsn. E. coli cells have two isoforms of LysRSs (LysS and LysU) encoded by two distinct genes, which are differentially regulated. The cytoplasmic and the mitochondrial isoforms of human LysRS are encoded by a single gene. Yeast cytoplasmic and mitochondrial LysRSs participate in mitochondrial import of cytoplasmic tRNAlysCUU. In addition to their housekeeping role, human LysRS may function as a signaling molecule that activates immune cells. Tomato LysRS may participate in a process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging. AsnRS is immunodominant antigen of the filarial nematode Brugia malayai and is of interest as a target for anti-parasitic drug design. Human AsnRS has been shown to be a pro-inflammatory chemokine which interacts with CCR3 chemokine receptors on T cells, immature dendritic cells and macrophages.
Pssm-ID: 239766 [Multi-domain] Cd Length: 85 Bit Score: 81.07 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 39 KVSVMGWLSHKRMD---RFFVLRDAYGSVQAKISASSK--LQSLLKDIPYESVVRVDGIVVDRgdnRNSKMKTGDIEIDV 113
Cdd:cd04100 1 EVTLAGWVHSRRDHgglIFIDLRDGSGIVQVVVNKEELgeFFEEAEKLRTESVVGVTGTVVKR---PEGNLATGEIELQA 77
|
....*...
gi 32566633 114 EELTVLNK 121
Cdd:cd04100 78 EELEVLSK 85
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
24-561 |
2.20e-18 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 87.86 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 24 RTHICDELSTSNKNEKVSVMGWLSHKRmD----RFFVLRDayGS----VQAKISASSKLQSLLKDIPYESVVRVDGIVVd 95
Cdd:PRK03932 3 RVSIKDILKGKYVGQEVTVRGWVRTKR-DsgkiAFLQLRD--GScfkqLQVVKDNGEEYFEEIKKLTTGSSVIVTGTVV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 96 rgdnrNSKMKTGDIEIDVEELTVLNKATSNIPMLPDANANERTRlKYRYIDLRSDKLQKSLRLRSEFVHNVRRFLVEKsG 175
Cdd:PRK03932 79 -----ESPRAGQGYELQATKIEVIGEDPEDYPIQKKRHSIEFLR-EIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNEN-G 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 176 FVDVETPTLfrrTPG---GAAE-FVVPAPSPNQGLAY-----SLPQSpqqfKQL---LMVGAIDRYFQIARCYRDEGSKG 243
Cdd:PRK03932 152 FVWVDTPII---TASdceGAGElFRVTTLDLDFSKDFfgkeaYLTVS----GQLyaeAYAMALGKVYTFGPTFRAENSNT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 244 DRQ-PEFTQVDVEMSFTTQNGVMQLIEDM---IISA-------------------WPESLNHIKpKSPFPRIPYSDAMrl 300
Cdd:PRK03932 225 RRHlAEFWMIEPEMAFADLEDNMDLAEEMlkyVVKYvlencpddleflnrrvdkgDIERLENFI-ESPFPRITYTEAI-- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 301 ygidkpdmripwqiddvdndifEFLQKdidddtwrsrilvcrgagkttisnsmknewkrliqmneNGKNFAIchpsqkrw 380
Cdd:PRK03932 302 ----------------------EILQK--------------------------------------SGKKFEF-------- 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 381 fkpfdnqklidqfglidedvlIVCWGnsegvywtlevcglrsksnvtahwiVDfpLFSFEEGQLVSTHhpFTAPL----- 455
Cdd:PRK03932 314 ---------------------PVEWG-------------------------DD--LGSEHERYLAEEH--FKKPVfvtny 343
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 456 EKDIDILY--SNDIDKllqiTGQHYDLVINGV-EMGGGSIRIENSEI--QRhvLKVLGEPTDEMEHLLNALSHGAPPHGG 530
Cdd:PRK03932 344 PKDIKAFYmrLNPDGK----TVAAMDLLAPGIgEIIGGSQREERLDVleAR--IKELGLNKEDYWWYLDLRRYGSVPHSG 417
|
570 580 590
....*....|....*....|....*....|.
gi 32566633 531 FALGLDRFVAMLTSDGNpltpVRDVIAFPKT 561
Cdd:PRK03932 418 FGLGFERLVAYITGLDN----IRDVIPFPRT 444
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
156-559 |
8.16e-18 |
|
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a lysine to the 3' OH group of ribose of the appropriate tRNA. Its assignment to class II aaRS is based upon its structure and the presence of three characteristic sequence motifs in the core domain. It is found in eukaryotes as well as some prokaryotes and archaea. However, LysRS belongs to class I aaRS's in some prokaryotes and archaea. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate.
Pssm-ID: 238398 [Multi-domain] Cd Length: 329 Bit Score: 84.94 E-value: 8.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 156 LRLRSEFVHNVRRFLVEKsGFVDVETPTLfRRTPGGAAE--FVVPAPSPNQGLaYsLPQSPQQFKQLLMVGAIDRYFQIA 233
Cdd:cd00775 8 FIVRSKIISYIRKFLDDR-GFLEVETPML-QPIAGGAAArpFITHHNALDMDL-Y-LRIAPELYLKRLIVGGFERVYEIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 234 RCYRDEGSKGDRQPEFTQVDVEMSFTTQNGVMQLIEDMiISAWPESLN----------HIKPKSPFPRIPYSDAMRLY-G 302
Cdd:cd00775 84 RNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDL-FSGLVKKINgktkieyggkELDFTPPFKRVTMVDALKEKtG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 303 IDKPDMripwqiddVDNDIFEfLQKDIDDDtwrsrilvcrgagkttisnsmknewkrliqmnengknfaichpSQKRWFK 382
Cdd:cd00775 163 IDFPEL--------DLEQPEE-LAKLLAKL-------------------------------------------IKEKIEK 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 383 PFDNQKLIDQ-FGLIDEDVLIvcwgnsegvywtlevcglrsksNVTahWIVDFPlfsfeegQLVSthhpftaPLEKdidi 461
Cdd:cd00775 191 PRTLGKLLDKlFEEFVEPTLI----------------------QPT--FIIDHP-------VEIS-------PLAK---- 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 462 lySNDIDKllQITgQHYDLVINGVEMGGGSIRIENSEIQRHVLK---VLGEPTDEMEHL-----LNALSHGAPPHGGFAL 533
Cdd:cd00775 229 --RHRSNP--GLT-ERFELFICGKEIANAYTELNDPFDQRERFEeqaKQKEAGDDEAMMmdedfVTALEYGMPPTGGLGI 303
|
410 420
....*....|....*....|....*.
gi 32566633 534 GLDRFVAMLTSDGNpltpVRDVIAFP 559
Cdd:cd00775 304 GIDRLVMLLTDSNS----IRDVILFP 325
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
24-562 |
1.35e-14 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 77.31 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 24 RTHICDELSTSNKNEKVSVMGWLSHKRmDR----FFVLRDAYGSVQAKISASSKLQSLLKDIPYEsvvrvdgivVDRGD- 98
Cdd:PRK02983 638 PTHTVAEALDAPTGEEVSVSGRVLRIR-DYggvlFADLRDWSGELQVLLDASRLEQGSLADFRAA---------VDLGDl 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 99 ----NRNSKMKTGDIEIDVEELTVLNKATSNIPMLPDANANERTRLKYRYIDLRSDKLQKS-LRLRSEFVHNVRRFLVEK 173
Cdd:PRK02983 708 vevtGTMGTSRNGTLSLLVTSWRLAGKCLRPLPDKWKGLTDPEARVRQRYLDLAVNPEARDlLRARSAVVRAVRETLVAR 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 174 sGFVDVETPTLfRRTPGGAAE--FVVPAPSPNQGLaYsLPQSPQQFKQLLMVGAIDRYFQIARCYRDEGSKGDRQPEFTQ 251
Cdd:PRK02983 788 -GFLEVETPIL-QQVHGGANArpFVTHINAYDMDL-Y-LRIAPELYLKRLCVGGVERVFELGRNFRNEGVDATHNPEFTL 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 252 VDVEMSFTTQNGVMQLIEDMIISAwpeslnhikpkspfpripysdAMRLYG---IDKPDMRIPWQIDDVDNDifeflqkd 328
Cdd:PRK02983 864 LEAYQAHADYDTMRDLTRELIQNA---------------------AQAAHGapvVMRPDGDGVLEPVDISGP-------- 914
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 329 idddtWRSRIL---VCRGAGKTTISNSMKNEWKRLIQmnengknfaichpsqkRWFKPFDNQklidqfglidedvlivcW 405
Cdd:PRK02983 915 -----WPVVTVhdaVSEALGEEIDPDTPLAELRKLCD----------------AAGIPYRTD-----------------W 956
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 406 GNSEGVywtLEVCG-LRSKSNVTAHWIVDFPlfsfeegqlVSThHPFTAPLEKDIDIlysndidkllqitGQHYDLVING 484
Cdd:PRK02983 957 DAGAVV---LELYEhLVEDRTTFPTFYTDFP---------TSV-SPLTRPHRSDPGL-------------AERWDLVAWG 1010
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 485 VEMGGGSirienSEI-----QRH------VLKVLGEPtDEM---EHLLNALSHGAPPHGGFALGLDRFVAMLTSdgnplT 550
Cdd:PRK02983 1011 VELGTAY-----SELtdpveQRRrlteqsLLAAGGDP-EAMeldEDFLQALEYAMPPTGGLGMGVDRLVMLLTG-----R 1079
|
570
....*....|..
gi 32566633 551 PVRDVIAFPKTK 562
Cdd:PRK02983 1080 SIRETLPFPLVK 1091
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
135-300 |
7.78e-14 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 72.74 E-value: 7.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 135 NERTRLKYRYIDLRSDKLQKSLRLRSEFVHNVRRFLVEKsGFVDVETPTLFRRT----PGGAAEFVVPAPSPNQGLAYSL 210
Cdd:PRK06462 9 EYEEFLRMSWKHISSEKYRKVLKVQSSILRYTREFLDGR-GFVEVLPPIISPSTdplmGLGSDLPVKQISIDFYGVEYYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 211 PQSPQQFKQLlMVGAIDRYFQIARCYRDEG---SKGDRQPEFTQVDVEMSFTTQNGVMQLIEDMIIS-------AWPESL 280
Cdd:PRK06462 88 ADSMILHKQL-ALRMLGKIFYLSPNFRLEPvdkDTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYlvkelleEHEDEL 166
|
170 180
....*....|....*....|....*
gi 32566633 281 NHI-----KPKSPFPRIPYSDAMRL 300
Cdd:PRK06462 167 EFFgrdlpHLKRPFKRITHKEAVEI 191
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
139-559 |
2.71e-13 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 72.76 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 139 RLKYRYIDLRSDK-LQKSLRLRSEFVHNVRRFLVEKSgFVDVETPTLFRRTPGGAAEFVVPAPSPNQGLAYsLPQSPQQF 217
Cdd:PTZ00385 215 KYRYRFTDMMTNPcVIETIKKRHVMLQALRDYFNERN-FVEVETPVLHTVASGANAKSFVTHHNANAMDLF-LRVAPELH 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 218 KQLLMVGAIDRYFQIARCYRDEGSKGDRQPEFTQVDVEMSFTTQNGVMQLIEDM------------IISAWPESLN---- 281
Cdd:PTZ00385 293 LKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTSCEFYAAYHTYEDLMPMTEDIfrqlamrvngttVVQIYPENAHgnpv 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 282 HIKPKSPFPRIP-YSDAMRLYGIDKPDmripwqiddvDNDIfeflqkdidddtwrsrilvcrgagkttisnsmkNEWKRL 360
Cdd:PTZ00385 373 TVDLGKPFRRVSvYDEIQRMSGVEFPP----------PNEL---------------------------------NTPKGI 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 361 IQMNENGKNFAICHPSQKRWFKPFDnqKLIDQFglidedvlivcwgnsegvywtlevcglrsksnVTAHwIVDfPLFsfe 440
Cdd:PTZ00385 410 AYMSVVMLRYNIPLPPVRTAAKMFE--KLIDFF--------------------------------ITDR-VVE-PTF--- 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 441 egqlVSTHHPFTAPLEKDidilysndidkllQIT----GQHYDLVINGVEMGGGSIRIENSEIQRH-----VLKVLGEPT 511
Cdd:PTZ00385 451 ----VMDHPLFMSPLAKE-------------QVSrpglAERFELFVNGIEYCNAYSELNDPHEQYHrfqqqLVDRQGGDE 513
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 32566633 512 DEM---EHLLNALSHGAPPHGGFALGLDRFVAMLTSDGNpltpVRDVIAFP 559
Cdd:PTZ00385 514 EAMpldETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSN----IRDGIIFP 560
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
166-303 |
1.42e-12 |
|
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.
Pssm-ID: 238391 [Multi-domain] Cd Length: 211 Bit Score: 67.14 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 166 VRRFLVEKsGFVDVETP-----TLFRRTPGGAAEFVVPAPSPnqGLAYSLPQSPQQFKQLLMVGAI----DRYFQIARCY 236
Cdd:cd00768 9 LRRFMAEL-GFQEVETPiverePLLEKAGHEPKDLLPVGAEN--EEDLYLRPTLEPGLVRLFVSHIrklpLRLAEIGPAF 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32566633 237 RDEGSKGD--RQPEFTQVDVEMSFTT---QNGVMQLIEdmIISAWPESLnhIKPKSPFPRIPYSDAMRLYGI 303
Cdd:cd00768 86 RNEGGRRGlrRVREFTQLEGEVFGEDgeeASEFEELIE--LTEELLRAL--GIKLDIVFVEKTPGEFSPGGA 153
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
83-562 |
4.55e-12 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 68.88 E-value: 4.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 83 YESVVRVD--GIVVDRGdnrnsKMKTGDIEIDVEELTVLNKATSNIPMLPDANANErTRLKYRYIDLRSDKLQKSLRL-R 159
Cdd:PTZ00417 183 YDKIRRGDivGIVGFPG-----KSKKGELSIFPKETIILSPCLHMLPMKYGLKDTE-IRYRQRYLDLMINESTRSTFItR 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 160 SEFVHNVRRFLVEKsGFVDVETPTLfRRTPGGAAEFVVPAPSPNQGLAYSLPQSPQQFKQLLMVGAIDRYFQIARCYRDE 239
Cdd:PTZ00417 257 TKIINYLRNFLNDR-GFIEVETPTM-NLVAGGANARPFITHHNDLDLDLYLRIATELPLKMLIVGGIDKVYEIGKVFRNE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 240 GSKGDRQPEFTQVDVEMSFTTQNGVMQLIEDMIISAwpeslnhikpkspfpripysdAMRLYGIDKpdmrIPWQIDDVDN 319
Cdd:PTZ00417 335 GIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQL---------------------VMHLFGTYK----ILYNKDGPEK 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 320 DIFEflqkdIDDDTWRSRILVCRGAGKTT--------ISNSMKNEWKRLIQMNEngknfaICHPSqkrwfkPFDNQKLID 391
Cdd:PTZ00417 390 DPIE-----IDFTPPYPKVSIVEELEKLTntkleqpfDSPETINKMINLIKENK------IEMPN------PPTAAKLLD 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 392 QFGlidedvlivcwgnsegvywtlevcglrskSNVTAHWIVDFPLFSFEEGQLVSthhpftaPLEKdidilYSNDIDKLL 471
Cdd:PTZ00417 453 QLA-----------------------------SHFIENKYPNKPFFIIEHPQIMS-------PLAK-----YHRSKPGLT 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 472 qitgQHYDLVINGVEMGGGSIRIENSEIQRHVLKVLG---EPTDEMEHLLNA-----LSHGAPPHGGFALGLDRFVAMLT 543
Cdd:PTZ00417 492 ----ERLEMFICGKEVLNAYTELNDPFKQKECFSAQQkdrEKGDAEAFQFDAafctsLEYGLPPTGGLGLGIDRITMFLT 567
|
490
....*....|....*....
gi 32566633 544 SDGNpltpVRDVIAFPKTK 562
Cdd:PTZ00417 568 NKNC----IKDVILFPTMR 582
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
38-130 |
3.31e-10 |
|
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the homodimeric non-discriminating (ND) Pyrococcus kodakaraensis aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. P. kodakaraensis AspRS is a class 2b aaRS. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. P. kodakaraensis ND-AspRS can charge both tRNAAsp and tRNAAsn. Some of the enzymes in this group may be discriminating, based on the presence of homologs of asparaginyl-tRNA synthetase (AsnRS) in their completed genomes.
Pssm-ID: 239811 [Multi-domain] Cd Length: 108 Bit Score: 57.32 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 38 EKVSVMGWLSHKRmD----RFFVLRDAYGSVQA---KISASSKLQSLLKDIPYESVVRVDGIVvdrgdNRNSKMKTGdIE 110
Cdd:cd04316 13 EEVTVAGWVHEIR-DlggiKFVILRDREGIVQVtapKKKVDKELFKTVRKLSRESVISVTGTV-----KAEPKAPNG-VE 85
|
90 100
....*....|....*....|
gi 32566633 111 IDVEELTVLNKATSNIPMLP 130
Cdd:cd04316 86 IIPEEIEVLSEAKTPLPLDP 105
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
40-119 |
9.77e-10 |
|
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic acids. The family includes the anti-codon binding domain of lysyl, aspartyl, and asparaginyl -tRNA synthetases (See pfam00152). Aminoacyl-tRNA synthetases catalyze the addition of an amino acid to the appropriate tRNA molecule EC:6.1.1.-. This family also includes part of RecG helicase involved in DNA repair. Replication factor A is a hetero-trimeric complex, that contains a subunit in this family. This domain is also found at the C-terminus of bacterial DNA polymerase III alpha chain.
Pssm-ID: 460164 [Multi-domain] Cd Length: 75 Bit Score: 54.93 E-value: 9.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 40 VSVMGWLSHKRMDR----FFVLRDAYGSVQAKISaSSKLQSLLKDIPYESVVRVDGIVVDRgdnrnskmKTGDIEIDVEE 115
Cdd:pfam01336 1 VTVAGRVTSIRRSGgkllFLTLRDGTGSIQVVVF-KEEAEKLAKKLKEGDVVRVTGKVKKR--------KGGELELVVEE 71
|
....
gi 32566633 116 LTVL 119
Cdd:pfam01336 72 IELL 75
|
|
| ScAspRS_mt_like_N |
cd04321 |
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
39-120 |
2.38e-07 |
|
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces cerevisiae mitochondrial (mt) aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this fungal group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Mutations in the gene for S. cerevisiae mtAspRS result in a "petite" phenotype typical for a mutation in a nuclear gene that results in a non-functioning mitochondrial protein synthesis system.
Pssm-ID: 239816 [Multi-domain] Cd Length: 86 Bit Score: 48.47 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 39 KVSVMGWLsHKRMDR-----FFVLRDAYG-SVQAKISASSKLQSLLKDIPYESVVRVDGIVVDRgdNRNSKMKTGDIEID 112
Cdd:cd04321 1 KVTLNGWI-DRKPRIvkklsFADLRDPNGdIIQLVSTAKKDAFSLLKSITAESPVQVRGKLQLK--EAKSSEKNDEWELV 77
|
....*...
gi 32566633 113 VEELTVLN 120
Cdd:cd04321 78 VDDIQTLN 85
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
486-567 |
9.52e-06 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 48.45 E-value: 9.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 486 EMGGGSIRIENSEIQRHVLKVLGEPTDEMEHLLNALSHGAPPHGGFALGLDRFVAMLTSDGNpltpVRDVIAFPKTKNGK 565
Cdd:PLN02221 495 ELIGGSQREERYDVIKQRIEEMGLPIEPYEWYLDLRRYGTVKHCGFGLGFERMILFATGIDN----IRDVIPFPRYPGKA 570
|
..
gi 32566633 566 DL 567
Cdd:PLN02221 571 DL 572
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
39-131 |
2.25e-05 |
|
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces cerevisiae and human cytoplasmic aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis.
Pssm-ID: 239815 [Multi-domain] Cd Length: 102 Bit Score: 43.32 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 39 KVSVMGWLSHKRMDR----FFVLRDAYGSVQAKISASSKLQS-----LLKDIPYESVVRVDGIVVdrgdnRNSKMKTG-- 107
Cdd:cd04320 1 EVLIRARVHTSRAQGaklaFLVLRQQGYTIQGVLAASAEGVSkqmvkWAGSLSKESIVDVEGTVK-----KPEEPIKSct 75
|
90 100
....*....|....*....|....*.
gi 32566633 108 --DIEIDVEELTVLNKATSNIPMLPD 131
Cdd:cd04320 76 qqDVELHIEKIYVVSEAAEPLPFQLE 101
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
478-565 |
2.53e-04 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 44.09 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 478 YDLVingVEMGG----GSIRIENSEIQRHVLKVLGEPTDEMEHLLNALSHGAPPHGGFALGLDRFVAMLTSdgnpLTPVR 553
Cdd:PLN02532 547 FDLV---VPKVGtvitGSQNEERMDILNARIEELGLPREQYEWYLDLRRHGTVKHSGFSLGFELMVLFATG----LPDVR 619
|
90
....*....|..
gi 32566633 554 DVIAFPKTKnGK 565
Cdd:PLN02532 620 DAIPFPRSW-GK 630
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
482-542 |
2.60e-04 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 43.38 E-value: 2.60e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32566633 482 INGVEMGGGSIRIENSEIQRHVL-------KVLGEPTDEM-EHLLNALSHGAPPHGGFALGLDRFVaML 542
Cdd:PRK09350 229 FKGIELANGFHELTDAREQRQRFeqdnrkrAARGLPQQPIdENLIAALEAGLPDCSGVALGVDRLI-ML 296
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
154-250 |
5.51e-04 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 42.22 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 154 KSLRLRSEFVHNVRRFLVEKsGFVDVETPTLFRRTPGGA------AEFVVPAPSpnQGLAYSLPQSPQ-QFKQLLMVGAI 226
Cdd:PRK09350 3 PNLLKRAKIIAEIRRFFADR-GVLEVETPILSQATVTDIhlvpfeTRFVGPGAS--QGKTLWLMTSPEyHMKRLLAAGSG 79
|
90 100
....*....|....*....|....
gi 32566633 227 DrYFQIARCYRDEGSKGDRQPEFT 250
Cdd:PRK09350 80 P-IFQICKSFRNEEAGRYHNPEFT 102
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
39-133 |
2.30e-03 |
|
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus horikoshii AsnRS asparaginyl-tRNA synthetase (AsnRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The archeal enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose.
Pssm-ID: 239814 [Multi-domain] Cd Length: 103 Bit Score: 37.89 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566633 39 KVSVMGWLSHKRM---DRFFVLRDAYGSVQAKISASSKLQSL--LKDIPYESVVRVDGIVvdRGDNRnskmKTGDIEIDV 113
Cdd:cd04319 1 KVTLAGWVYRKREvgkKAFIVLRDSTGIVQAVFSKDLNEEAYreAKKVGIESSVIVEGAV--KADPR----APGGAEVHG 74
|
90 100
....*....|....*....|
gi 32566633 114 EELTVLnKATSNIPMLPDAN 133
Cdd:cd04319 75 EKLEII-QNVEFFPITEDAS 93
|
|
| |
