|
Name |
Accession |
Description |
Interval |
E-value |
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
4-595 |
0e+00 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 1026.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 4 HRYRSHTCGALTAGDAGNNVRLSGWVHRVRDHGGLLFIDLRDNYGITQCVIDPDSAAFSAAEKVRSEWVLRIDGEVKLRD 83
Cdd:PRK00476 1 HMMRTHYCGELRESHVGQTVTLCGWVHRRRDHGGLIFIDLRDREGIVQVVFDPDAEAFEVAESLRSEYVIQVTGTVRARP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 84 AAAVNPNIPTGTIEVFIREIEVLSEAKELPLPVFGDADYPEDIRLKYRFLDLRREKLHANILKRTKIISAMRAGMGGAGF 163
Cdd:PRK00476 81 EGTVNPNLPTGEIEVLASELEVLNKSKTLPFPIDDEEDVSEELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDDNGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 164 TEFSTPILTASSPEGARDFLVPSRIHPGTFFALPQAPQQYKQLLMVAGFDRYFQVAPCFRDEDPRADRLPgEFYQLDLEM 243
Cdd:PRK00476 161 LEIETPILTKSTPEGARDYLVPSRVHPGKFYALPQSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADRQP-EFTQIDIEM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 244 SFVTQEDVWNTVEPVITNVFEQFAdGKRVTKGWPRIPYDTAIRKYGSDKPDLRNPIEIQGVTEHFAGSGFKVFANQIEAD 323
Cdd:PRK00476 240 SFVTQEDVMALMEGLIRHVFKEVL-GVDLPTPFPRMTYAEAMRRYGSDKPDLRFGLELVDVTDLFKDSGFKVFAGAANDG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 324 SKVEVWAIPAknkpGAEPIGRAFCDRMNAWAQGEGQPGLGYIFFKDGQGSGPIAKNIGEERTAALKAQLGLDDGDAVFFV 403
Cdd:PRK00476 319 GRVKAIRVPG----GAAQLSRKQIDELTEFAKIYGAKGLAYIKVNEDGLKGPIAKFLSEEELAALLERTGAKDGDLIFFG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 404 AGRPDKFYKFAGEARTKVGTDLGLVDSEQFALCWIVDFPFYEWSEEEKRIDFAHNPFSMPQGG-IDGLNGDDPLSLKAYQ 482
Cdd:PRK00476 395 ADKAKVVNDALGALRLKLGKELGLIDEDKFAFLWVVDFPMFEYDEEEGRWVAAHHPFTMPKDEdLDELETTDPGKARAYA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 483 YDAVCNGFEIASGSIRNQEPETMIKAFELTGKSRSEVEEQFGGLYRAFQYGAPPHGGAAFGIDRIVMLLCGVANLREITA 562
Cdd:PRK00476 475 YDLVLNGYELGGGSIRIHRPEIQEKVFEILGISEEEAEEKFGFLLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIA 554
|
570 580 590
....*....|....*....|....*....|...
gi 1197219449 563 FPMNQQAQDLLMGAPSQASAKQLRELSIRLNVQ 595
Cdd:PRK00476 555 FPKTQSAQDLLTGAPSPVDEKQLRELGIRLRKK 587
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
5-595 |
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: 1007.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 5 RYRSHTCGALTAGDAGNNVRLSGWVHRVRDHGGLLFIDLRDNYGITQCVIDPD--SAAFSAAEKVRSEWVLRIDGEVKLR 82
Cdd:COG0173 1 MYRTHYCGELRESDVGQEVTLSGWVHRRRDHGGLIFIDLRDRYGITQVVFDPDdsAEAFEKAEKLRSEYVIAVTGKVRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 83 DAAAVNPNIPTGTIEVFIREIEVLSEAKELPLPVFGDADYPEDIRLKYRFLDLRREKLHANILKRTKIISAMRAGMGGAG 162
Cdd:COG0173 81 PEGTVNPKLPTGEIEVLASELEILNKAKTPPFQIDDDTDVSEELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDENG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 163 FTEFSTPILTASSPEGARDFLVPSRIHPGTFFALPQAPQQYKQLLMVAGFDRYFQVAPCFRDEDPRADRLPgEFYQLDLE 242
Cdd:COG0173 161 FLEIETPILTKSTPEGARDYLVPSRVHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFRDEDLRADRQP-EFTQLDIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 243 MSFVTQEDVWNTVEPVITNVFEQFAdGKRVTKGWPRIPYDTAIRKYGSDKPDLRNPIEIQGVTEHFAGSGFKVFANQIEA 322
Cdd:COG0173 240 MSFVDQEDVFELMEGLIRHLFKEVL-GVELPTPFPRMTYAEAMERYGSDKPDLRFGLELVDVTDIFKDSGFKVFAGAAEN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 323 DSKVEvwAIPAknkPGAEPIGRAFCDRMNAWAQGEGQPGLGYIFFKDGQGSGPIAKNIGEERTAALKAQLGLDDGDAVFF 402
Cdd:COG0173 319 GGRVK--AINV---PGGASLSRKQIDELTEFAKQYGAKGLAYIKVNEDGLKSPIAKFLSEEELAAILERLGAKPGDLIFF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 403 VAGRPDKFYKFAGEARTKVGTDLGLVDSEQFALCWIVDFPFYEWSEEEKRIDFAHNPFSMPQGGIDGLNGDDPLSLKAYQ 482
Cdd:COG0173 394 VADKPKVVNKALGALRLKLGKELGLIDEDEFAFLWVVDFPLFEYDEEEGRWVAMHHPFTMPKDEDLDLLETDPGKVRAKA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 483 YDAVCNGFEIASGSIRNQEPETMIKAFELTGKSRSEVEEQFGGLYRAFQYGAPPHGGAAFGIDRIVMLLCGVANLREITA 562
Cdd:COG0173 474 YDLVLNGYELGGGSIRIHDPELQEKVFELLGISEEEAEEKFGFLLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIA 553
|
570 580 590
....*....|....*....|....*....|...
gi 1197219449 563 FPMNQQAQDLLMGAPSQASAKQLRELSIRLNVQ 595
Cdd:COG0173 554 FPKTQSAQDLMTGAPSEVDEKQLKELHIRLRPP 586
|
|
| aspS_bact |
TIGR00459 |
aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be ... |
7-595 |
0e+00 |
|
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: 607.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 7 RSHTCGALTAGDAGNNVRLSGWVHRVRDHGGLLFIDLRDNYGITQCVIDPDSAAFSAAEKVRSEWVLRIDGEVKLRDAAA 86
Cdd:TIGR00459 2 RTHYCGQLRTEHLGQTVTLAGWVNRRRDLGGLIFIDLRDRSGIVQVVCDPDADALKLAKGLRNEDVVQVKGKVSARPEGN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 87 VNPNIPTGTIEVFIREIEVLSEAKELPLpVFGDADYPEDIRLKYRFLDLRREKLHANILKRTKIISAMRAGMGGAGFTEF 166
Cdd:TIGR00459 82 INRNLDTGEIEILAESITLLNKSKTPPL-IIEKTDAEEEVRLKYRYLDLRRPEMQQRLKLRHKVTKAVRNFLDQQGFLEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 167 STPILTASSPEGARDFLVPSRIHPGTFFALPQAPQQYKQLLMVAGFDRYFQVAPCFRDEDPRADRLPgEFYQLDLEMSFV 246
Cdd:TIGR00459 161 ETPMLTKSTPEGARDYLVPSRVHKGEFYALPQSPQLFKQLLMVSGVDRYYQIARCFRDEDLRADRQP-EFTQIDMEMSFM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 247 TQEDVWNTVEPVITNVFEQFAdGKRVTKGWPRIPYDTAIRKYGSDKPDLRNPIEIQGVTEHFAGSGFKVFANQIEADSKV 326
Cdd:TIGR00459 240 TQEDVMELIEKLVSHVFLEVK-GIDLKKPFPVMTYAEAMERYGSDKPDLRFPLELIDVTDLFKDSEFKVFSNLINDGGRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 327 EvwAIPAKNkpGAEPIGRAFCDRMNAWAQGEGQPGLGYIFFKDGQGSGPIAKNIGEERTAALKAQLGLDDGDAVFFVAGR 406
Cdd:TIGR00459 319 K--AIRVPG--GWAELSRKSIKELRKFAKEYGAKGLAYLKVNEDGINSPIKKFLDEKKGKILLERTDAQNGDILLFGAGS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 407 PDKFYKFAGEARTKVGTDLGLVDSEQFALCWIVDFPFYEWsEEEKRIDFAHNPFSMPQGGIDGLNGDDPLSLKAYQYDAV 486
Cdd:TIGR00459 395 KKIVLDALGALRLKLGKDLGLVDPDLFSFLWVVDFPMFEK-DKEGRLCAAHHPFTMPKDEDLENLEAAPEEALAEAYDLV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 487 CNGFEIASGSIRNQEPETMIKAFELTGKSRSEVEEQFGGLYRAFQYGAPPHGGAAFGIDRIVMLLCGVANLREITAFPMN 566
Cdd:TIGR00459 474 LNGVELGGGSIRIHDPEVQKKVFEILGIDPEEAREKFGFLLEAFKYGTPPHAGFALGLDRLMMLLTGTDNIRDVIAFPKT 553
|
570 580
....*....|....*....|....*....
gi 1197219449 567 QQAQDLLMGAPSQASAKQLRELSIRLNVQ 595
Cdd:TIGR00459 554 TAAACLMTEAPSFIDEKQLEELSIKYVVK 582
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
7-591 |
0e+00 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 551.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 7 RSHTCGALTAGDAGNNVRLSGWVHRVRDHGGLLFIDLRDNYGITQCVIDPDSA--AFSAAEKVRSEWVLRIDGEVKLRDA 84
Cdd:PLN02903 59 RSHLCGALSVNDVGSRVTLCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDEFpeAHRTANRLRNEYVVAVEGTVRSRPQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 85 AAVNPNIPTGTIEVFIREIEVLSE-AKELPLPVFG----DADYPEDIRLKYRFLDLRREKLHANILKRTKIISAMRAGMG 159
Cdd:PLN02903 139 ESPNKKMKTGSVEVVAESVDILNVvTKSLPFLVTTadeqKDSIKEEVRLRYRVLDLRRPQMNANLRLRHRVVKLIRRYLE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 160 GA-GFTEFSTPILTASSPEGARDFLVPSRIHPGTFFALPQAPQQYKQLLMVAGFDRYFQVAPCFRDEDPRADRLPgEFYQ 238
Cdd:PLN02903 219 DVhGFVEIETPILSRSTPEGARDYLVPSRVQPGTFYALPQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQP-EFTQ 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 239 LDLEMSFVTQEDVWNTVEPVITNVFEQFAdGKRVTKGWPRIPYDTAIRKYGSDKPDLRNPIEIQGVTEHFAGSGFKVFAN 318
Cdd:PLN02903 298 LDMELAFTPLEDMLKLNEDLIRQVFKEIK-GVQLPNPFPRLTYAEAMSKYGSDKPDLRYGLELVDVSDVFAESSFKVFAG 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 319 QIEADSKVEVWAIPAKNK---PGAEPIGRAFCDRMNAwaqgeGQPGLGYIFFKDG---QGSGPIAKNIGEERTAALKAQL 392
Cdd:PLN02903 377 ALESGGVVKAICVPDGKKisnNTALKKGDIYNEAIKS-----GAKGLAFLKVLDDgelEGIKALVESLSPEQAEQLLAAC 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 393 GLDDGDAVFFVAGRPDKFYKFAGEARTKVGTDLGLVDSEQFALCWIVDFPFYEWSEEEKRIDFAHNPFSMPQGGidglNG 472
Cdd:PLN02903 452 GAGPGDLILFAAGPTSSVNKTLDRLRQFIAKTLDLIDPSRHSILWVTDFPMFEWNEDEQRLEALHHPFTAPNPE----DM 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 473 DDPLSLKAYQYDAVCNGFEIASGSIRNQEPETMIKAFELTGKSRSEVEEQFGGLYRAFQYGAPPHGGAAFGIDRIVMLLC 552
Cdd:PLN02903 528 GDLSSARALAYDMVYNGVEIGGGSLRIYRRDVQQKVLEAIGLSPEEAESKFGYLLEALDMGAPPHGGIAYGLDRLVMLLA 607
|
570 580 590
....*....|....*....|....*....|....*....
gi 1197219449 553 GVANLREITAFPMNQQAQDLLMGAPSQASAKQLRELSIR 591
Cdd:PLN02903 608 GAKSIRDVIAFPKTTTAQCALTRAPSEVDDKQLQDLSIA 646
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
11-590 |
8.43e-152 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 453.29 E-value: 8.43e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 11 CGALTAGDAGNNVRLSGWVHRVRDHGGLLFIDLRDNYGITQCVIDPDSAA---FSAAEKVRSEWVLRIDGEVKLRDAAAV 87
Cdd:PRK12820 9 CGHLSLDDTGREVCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFSPEAAPadvYELAASLRAEFCVALQGEVQKRLEETE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 88 NPNIPTGTIEVFIREIEVLSEAKELPLPVF----------GDADY-PEDIRLKYRFLDLRREKLHANILKRTKIISAMRA 156
Cdd:PRK12820 89 NPHIETGDIEVFVRELSILAASEALPFAISdkamtagagsAGADAvNEDLRLQYRYLDIRRPAMQDHLAKRHRIIKCARD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 157 GMGGAGFTEFSTPILTASSPEGARDFLVPSRIHPGTFFALPQAPQQYKQLLMVAGFDRYFQVAPCFRDEDPRADRLPgEF 236
Cdd:PRK12820 169 FLDSRGFLEIETPILTKSTPEGARDYLVPSRIHPKEFYALPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQP-EF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 237 YQLDLEMSFVTQEDVWNTVEPVITNVFEqfADGKRVTKGWPRIPYDTAIRKYGSDKPDLRNPIEIQGVTEHFAGSGFKVF 316
Cdd:PRK12820 248 TQLDIEASFIDEEFIFELIEELTARMFA--IGGIALPRPFPRMPYAEAMDTTGSDRPDLRFDLKFADATDIFENTRYGIF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 317 ANQIEADSKVEVWAIPAKNKPGAEPIgrafcdRMNAWAQ----GEGQPGLGYIFFKDGQGSGPIAKNIGEERTAALKAQL 392
Cdd:PRK12820 326 KQILQRGGRIKGINIKGQSEKLSKNV------LQNEYAKeiapSFGAKGMTWMRAEAGGLDSNIVQFFSADEKEALKRRF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 393 GLDDGDAVFFVAGRPDKFYKFA-GEARTKVGTDLGLVDSEQFALCWIVDFPFYEwSEEEKRIDFAHNPFSMP-QGGIDGL 470
Cdd:PRK12820 400 HAEDGDVIIMIADASCAIVLSAlGQLRLHLADRLGLIPEGVFHPLWITDFPLFE-ATDDGGVTSSHHPFTAPdREDFDPG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 471 NGDDPLSLKAYQYDAVCNGFEIASGSIRNQEPETMIKAFELTGKSRSEVEEQFGGLYRAFQYGAPPHGGAAFGIDRIVML 550
Cdd:PRK12820 479 DIEELLDLRSRAYDLVVNGEELGGGSIRINDKDIQLRIFAALGLSEEDIEDKFGFFLRAFDFAAPPHGGIALGLDRVVSM 558
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1197219449 551 LCGVANLREITAFPMNQQAQDLLMGAPSQASAKQLRELSI 590
Cdd:PRK12820 559 ILQTPSIREVIAFPKNRSAACPLTGAPSEVAQEQLAELGL 598
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
144-568 |
4.58e-138 |
|
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: 402.72 E-value: 4.58e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 144 ILKRTKIISAMRAGMGGAGFTEFSTPILTASSPEGARDFLVPSRIHPGTFFALPQAPQQYKQLLMVAGFDRYFQVAPCFR 223
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTPEGARDFLVPSRLHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 224 DEDPRADRLPgEFYQLDLEMSFVTQEDVWNTVEPVITNVFEQFAdGKRVTKGWPRIPYDTAIRKYGsdkpdlrnpieiqg 303
Cdd:cd00777 81 DEDLRADRQP-EFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVL-GVELTTPFPRMTYAEAMERYG-------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 304 vtehfagsgfkvfanqieadskvevwaipaknkpgaepigrafcdrmnawaqgegqpglgyiffkdgqgsgpiaknigee 383
Cdd:cd00777 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 384 rtaalkaqlglddgdavffvagrpdkfykfageartkvgtdlglvdseqFALCWIVDFPFYEWSEEEKRIDFAHNPFSMP 463
Cdd:cd00777 145 -------------------------------------------------FKFLWIVDFPLFEWDEEEGRLVSAHHPFTAP 175
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 464 QGGIDGLNGDDPLSLKAYQYDAVCNGFEIASGSIRNQEPETMIKAFELTGKSRSEVEEQFGGLYRAFQYGAPPHGGAAFG 543
Cdd:cd00777 176 KEEDLDLLEKDPEDARAQAYDLVLNGVELGGGSIRIHDPDIQEKVFEILGLSEEEAEEKFGFLLEAFKYGAPPHGGIALG 255
|
410 420
....*....|....*....|....*
gi 1197219449 544 IDRIVMLLCGVANLREITAFPMNQQ 568
Cdd:cd00777 256 LDRLVMLLTGSESIRDVIAFPKTQN 280
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
124-567 |
3.06e-114 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 343.01 E-value: 3.06e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 124 EDIRLKYRFLDLRREKLHANILKRTKIISAMRAGMGGAGFTEFSTPILTAS-SPEGARDFLVPSRIHpGTFFALPQAPQQ 202
Cdd:pfam00152 2 EETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSaTPEGARDFLVPSRAL-GKFYALPQSPQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 203 YKQLLMVAGFDRYFQVAPCFRDEDPRADRLPgEFYQLDLEMSFVTQEDVWNTVEPVITNVFEQFADGKR---------VT 273
Cdd:pfam00152 81 YKQLLMVAGFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKeleggtlldLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 274 KGWPRIPYDTAIRK----------YGSDKPDLRNPIEIQgvtehfagsgfkvfanqieadskvevwaipaknkpgaepig 343
Cdd:pfam00152 160 KPFPRITYAEAIEKlngkdveelgYGSDKPDLRFLLELV----------------------------------------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 344 rafcdrmnawaqgegqpglgyiffkdgqgsgpiaknigeertaalkaqlglddgdavffvagrpdkfykfageartkvgt 423
Cdd:pfam00152 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 424 dlglVDSEQFALCWIVDFPfyewseeekridFAHNPFSMPQggidglNGDDPlsLKAYQYDAVCNGFEIASGSIRNQEPE 503
Cdd:pfam00152 199 ----IDKNKFNPLWVTDFP------------AEHHPFTMPK------DEDDP--ALAEAFDLVLNGVEIGGGSIRIHDPE 254
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1197219449 504 TMIKAFELTGKSRSEVEEQFGGLYRAFQYGAPPHGGAAFGIDRIVMLLCGVANLREITAFPMNQ 567
Cdd:pfam00152 255 LQEERFEEQGLDPEEAEEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAFPKTR 318
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
6-564 |
1.59e-70 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 233.93 E-value: 1.59e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 6 YRSHTCGALTAGDAGNNVRLSGWVHRVRDHGGLLFIDLRDNYGITQCVIDPDSA--AFSAAEKVRSEWVLRIDGEVKLrd 83
Cdd:PRK05159 2 MKRHLTSELTPELDGEEVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKVDeeLFETIKKLKRESVVSVTGTVKA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 84 aaavNPNIPTGtIEVFIREIEVLSEAKE-LPLPVFGDADYPEDIRLKYRFLDLRREKLHAnILK-RTKIISAMRAGMGGA 161
Cdd:PRK05159 80 ----NPKAPGG-VEVIPEEIEVLNKAEEpLPLDISGKVLAELDTRLDNRFLDLRRPRVRA-IFKiRSEVLRAFREFLYEN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 162 GFTEFSTPILTASSPE-GARDFlvpsrihPGTFFA----LPQAPQQYKQLLMVAGFDRYFQVAPCFRDEDPRADRLPGEF 236
Cdd:PRK05159 154 GFTEIFTPKIVASGTEgGAELF-------PIDYFEkeayLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSRHLNEY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 237 YQLDLEMSFVT-QEDVWNTVEPVITNVFEQFA------------DGKRVTKGWPRIPYDTAI----RKYG--SDKPDLRN 297
Cdd:PRK05159 227 TSIDVEMGFIDdHEDVMDLLENLLRYMYEDVAencekelellgiELPVPETPIPRITYDEAIeilkSKGNeiSWGDDLDT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 298 PIEiqgvtehfagsgfkvfanqieadskvevwaipaknkpgaepigRAFCDRMnawaqgegqpglgyiffkdgqgsgpia 377
Cdd:PRK05159 307 EGE-------------------------------------------RLLGEYV--------------------------- 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 378 kniGEERtaalkaqlgldDGDAVFfvagrpdkfykfageartkvgtdlglvdseqfalcwIVDFPfyewseEEKRidfah 457
Cdd:PRK05159 317 ---KEEY-----------GSDFYF------------------------------------ITDYP------SEKR----- 335
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 458 nPF-SMPqggidglNGDDPLSLKAyqYDAVCNGFEIASGSIRNQEPETMIKAFeltgKSRSEVEEQFGGLYRAFQYGAPP 536
Cdd:PRK05159 336 -PFyTMP-------DEDDPEISKS--FDLLFRGLEITSGGQRIHRYDMLVESI----KEKGLNPESFEFYLEAFKYGMPP 401
|
570 580
....*....|....*....|....*...
gi 1197219449 537 HGGAAFGIDRIVMLLCGVANLREITAFP 564
Cdd:PRK05159 402 HGGFGLGLERLTMKLLGLENIREAVLFP 429
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
7-140 |
4.29e-69 |
|
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: 219.70 E-value: 4.29e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 7 RSHTCGALTAGDAGNNVRLSGWVHRVRDHGGLLFIDLRDNYGITQCVIDPDSA-AFSAAEKVRSEWVLRIDGEVKLRDAA 85
Cdd:cd04317 1 RTHYCGELRESHVGQEVTLCGWVQRRRDHGGLIFIDLRDRYGIVQVVFDPEEApEFELAEKLRNESVIQVTGKVRARPEG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1197219449 86 AVNPNIPTGTIEVFIREIEVLSEAKELPLPVFGDADYPEDIRLKYRFLDLRREKL 140
Cdd:cd04317 81 TVNPKLPTGEIEVVASELEVLNKAKTLPFEIDDDVNVSEELRLKYRYLDLRRPKM 135
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
7-564 |
4.48e-54 |
|
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: 189.88 E-value: 4.48e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 7 RSHTCGALTAGDAGNNVRLSGWVHRVRDHGGLLFIDLRDNYGITQCVIDPDS-AAFSAAEKVRSEWVLRIDGEVKLrdaa 85
Cdd:COG0017 1 KRTYIKDLLPEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKlENFEEAKKLTTESSVEVTGTVVE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 86 avNPNIPTGtIEVFIREIEVLSEAKE-LPLPVfGDADYpeDIRLKYRFLDLRREKLHAnILK-RTKIISAMRAGMGGAGF 163
Cdd:COG0017 77 --SPRAPQG-VELQAEEIEVLGEADEpYPLQP-KRHSL--EFLLDNRHLRLRTNRFGA-IFRiRSELARAIREFFQERGF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 164 TEFSTPILTASSPEGARD-FLVpsrihpgTFFA----LPQAPQQYKQlLMVAGFDRYFQVAPCFRDEDPRADRLPGEFYQ 238
Cdd:COG0017 150 VEVHTPIITASATEGGGElFPV-------DYFGkeayLTQSGQLYKE-ALAMALEKVYTFGPTFRAEKSNTRRHLAEFWM 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 239 LDLEMSFVTQEDVWNTVEPVITNVFEQFAD---------GKRVTK-------GWPRIPYDTAIRKYGSDKPDLRNPIEIQ 302
Cdd:COG0017 222 IEPEMAFADLEDVMDLAEEMLKYIIKYVLEncpeeleflGRDVERlekvpesPFPRITYTEAIEILKKSGEKVEWGDDLG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 303 gvTEHfagsgfkvfanqieadskvEVWaipaknkpgaepigrafcdrmnawaqgegqpglgyiffkdgqgsgpiaknIGE 382
Cdd:COG0017 302 --TEH-------------------ERY--------------------------------------------------LGE 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 383 ErtaalkaqlglddgdavFFvagrpDKFYkfageartkvgtdlglvdseqfalcWIVDFPfyewseEEKRidfahnPFSM 462
Cdd:COG0017 311 E-----------------FF-----KKPV-------------------------FVTDYP------KEIK------AFYM 331
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 463 PqggidgLNGDDPlslkayqydAVCNGF--------EIASGSIRNQEPETMIKAFELTGKSrsevEEQFGGLYRAFQYGA 534
Cdd:COG0017 332 K------PNPDDP---------KTVAAFdllapgigEIIGGSQREHRYDVLVERIKEKGLD----PEDYEWYLDLRRYGS 392
|
570 580 590
....*....|....*....|....*....|
gi 1197219449 535 PPHGGAAFGIDRIVMLLCGVANLREITAFP 564
Cdd:COG0017 393 VPHAGFGLGLERLVMWLTGLENIREVIPFP 422
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
147-566 |
1.41e-50 |
|
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: 175.74 E-value: 1.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 147 RTKIISAMRAGMGGAGFTEFSTPILTASSP-EGARDFLVPSRiHPGTFFALPQAPQQYKQLLMVAGFDRYFQVAPCFRDE 225
Cdd:cd00669 4 RSKIIKAIRDFMDDRGFLEVETPMLQKITGgAGARPFLVKYN-ALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFRNE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 226 DPRADRLPgEFYQLDLEMSFVTQEDVWNTVEPVITNVFEQFADGKRVTKG---------WPRIPYDTAIRKYGsdkpdlr 296
Cdd:cd00669 83 DLRARHQP-EFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYGfeledfglpFPRLTYREALERYG------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 297 NPIeiqgvtehfagsgfkvfanqieadskvevwaipaknkpgaepigrafcdrmnawaqgegqpglgyiffkdgqgsgpi 376
Cdd:cd00669 155 QPL----------------------------------------------------------------------------- 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 377 aknigeertaalkaqlglddgdavffvagrpdkfykfageartkvgtdlglvdseqfalcWIVDFPFyewseeekridFA 456
Cdd:cd00669 158 ------------------------------------------------------------FLTDYPA-----------EM 166
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 457 HNPFSMPQggidglngdDPLSLKAYQYDAVCNGFEIASGSIRNQEPETMIKAFELTGKSRSEVEEQFGGLYRAFQYGAPP 536
Cdd:cd00669 167 HSPLASPH---------DVNPEIADAFDLFINGVEVGNGSSRLHDPDIQAEVFQEQGINKEAGMEYFEFYLKALEYGLPP 237
|
410 420 430
....*....|....*....|....*....|
gi 1197219449 537 HGGAAFGIDRIVMLLCGVANLREITAFPMN 566
Cdd:cd00669 238 HGGLGIGIDRLIMLMTNSPTIREVIAFPKM 267
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
125-564 |
3.97e-32 |
|
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: 126.53 E-value: 3.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 125 DIRLKYRFLDLRREKLHAnILK-RTKIISAMRAGMGGAGFTEFSTPILTASSPE-GARDFlvpsrihPGTFFA----LPQ 198
Cdd:cd00776 5 ETLLDNRHLDLRTPKVQA-IFRiRSEVLRAFREFLRENGFTEVHTPKITSTDTEgGAELF-------KVSYFGkpayLAQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 199 APQQYKQLlMVAGFDRYFQVAPCFRDEDPRADRLPGEFYQLDLEMSFVTQ-EDVWNTVEPVITNVF----EQFADG---- 269
Cdd:cd00776 77 SPQLYKEM-LIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEDyNEVMDLIEELIKYIFkrvlERCAKElelv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 270 -------KRVTKGWPRIPYDTAIrkygsdkpDLRNpiEIQGVTEHFAGSGFkvfanqieadskvevwaipaknkpgaepi 342
Cdd:cd00776 156 nqlnrelLKPLEPFPRITYDEAI--------ELLR--EKGVEEEVKWGEDL----------------------------- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 343 grafcdrmnawaQGEGQPGLGYIFFKDgqgsgpiaknigeertaalkaqlglddgdaVFFVagrpdkfykfageartkvg 422
Cdd:cd00776 197 ------------STEHERLLGEIVKGD------------------------------PVFV------------------- 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 423 tdlglvdseqfalcwiVDFPfyewseEEKRidfahnPFSMPQggidglNGDDPLSLKAyqYDAVCNGF-EIASGSIRNQE 501
Cdd:cd00776 216 ----------------TDYP------KEIK------PFYMKP------DDDNPETVES--FDLLMPGVgEIVGGSQRIHD 259
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1197219449 502 PETMIKAFELTGKSRseveEQFGGLYRAFQYGAPPHGGAAFGIDRIVMLLCGVANLREITAFP 564
Cdd:cd00776 260 YDELEERIKEHGLDP----ESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
23-108 |
9.83e-31 |
|
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: 114.97 E-value: 9.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 23 VRLSGWVHRVRDHGGLLFIDLRDNYGITQCVIDPDSAA--FSAAEKVRSEWVLRIDGEVKLRDAaavnPNIPTGTIEVFI 100
Cdd:cd04100 2 VTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEELGefFEEAEKLRTESVVGVTGTVVKRPE----GNLATGEIELQA 77
|
....*...
gi 1197219449 101 REIEVLSE 108
Cdd:cd04100 78 EELEVLSK 85
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
12-564 |
2.82e-29 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 122.12 E-value: 2.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 12 GALTAGDAGNNVRLSGWVHRVRDHGGLLFIDLRDNYGITQCVIDPDSAAFSA-----AEKVRSEWVLRIDGEVklrdaaa 86
Cdd:PLN02850 73 SDLGEELAGSEVLIRGRVHTIRGKGKSAFLVLRQSGFTVQCVVFVSEVTVSKgmvkyAKQLSRESVVDVEGVV------- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 87 VNPNIP-TGT---IEVFIREIEVLSEAK-ELPLPVfGDADYPE------------------DIRLKYRFLDLRREKLHAN 143
Cdd:PLN02850 146 SVPKKPvKGTtqqVEIQVRKIYCVSKALaTLPFNV-EDAARSEseiekalqtgeqlvrvgqDTRLNNRVLDLRTPANQAI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 144 ILKRTKIISAMRAGMGGAGFTEFSTPILTASSPEGARDflVPSRIHPGTFFALPQAPQQYKQLLMVAGFDRYFQVAPCFR 223
Cdd:PLN02850 225 FRIQSQVCNLFREFLLSKGFVEIHTPKLIAGASEGGSA--VFRLDYKGQPACLAQSPQLHKQMAICGDFRRVFEIGPVFR 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 224 DEDPRADRLPGEFYQLDLEMsfvtqedvwntvepvitnvfeqfadgkrvtkgwpripydtAIRKYGSdkpdlrnpiEIQG 303
Cdd:PLN02850 303 AEDSFTHRHLCEFTGLDLEM----------------------------------------EIKEHYS---------EVLD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 304 VTEHFagsgFKVFANQIEADSKVEVWAIpAKNKPgAEPIgrAFCDRMNAWAQGEGQPGLgyiffkdgQGSGPIAKNIGEE 383
Cdd:PLN02850 334 VVDEL----FVAIFDGLNERCKKELEAI-REQYP-FEPL--KYLPKTLRLTFAEGIQML--------KEAGVEVDPLGDL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 384 RTAALKA--QLGLDDGDAVFFVagrpdkFYKFAGEARtkvgtdlglvdseqfalcwivdfPFYewseeekridfahnpfS 461
Cdd:PLN02850 398 NTESERKlgQLVKEKYGTDFYI------LHRYPLAVR-----------------------PFY----------------T 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 462 MPqggidglNGDDPLslkaY--QYDAVCNGFEIASGSIRNQEPETMIKAFELTGksrseVEEQFGGLY-RAFQYGAPPHG 538
Cdd:PLN02850 433 MP-------CPDDPK----YsnSFDVFIRGEEIISGAQRVHDPELLEKRAEECG-----IDVKTISTYiDSFRYGAPPHG 496
|
570 580
....*....|....*....|....*.
gi 1197219449 539 GAAFGIDRIVMLLCGVANLREITAFP 564
Cdd:PLN02850 497 GFGVGLERVVMLFCGLNNIRKTSLFP 522
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
13-285 |
1.41e-20 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 94.79 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 13 ALTAGDAGNNVRLSGWVHRVRDHGGLLFIDLRDNYGIT--QCVIDPDSAAFSAAEKVRSEWVLRIDGEVKLrdaaavNPN 90
Cdd:PRK03932 9 ILKGKYVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFKqlQVVKDNGEEYFEEIKKLTTGSSVIVTGTVVE------SPR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 91 IPTGtIEVFIREIEVLSEAkelplpvfgDADYPedIRLKYRFLDLRREklHANILKRTKIISAM---RAGMGGA------ 161
Cdd:PRK03932 83 AGQG-YELQATKIEVIGED---------PEDYP--IQKKRHSIEFLRE--IAHLRPRTNKFGAVmriRNTLAQAiheffn 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 162 --GFTEFSTPILTASSPEGARD-FLVPSRIHPGT--FFA----LPQAPQQYKQLLMVAgFDRYFQVAPCFRDEDPRADRL 232
Cdd:PRK03932 149 enGFVWVDTPIITASDCEGAGElFRVTTLDLDFSkdFFGkeayLTVSGQLYAEAYAMA-LGKVYTFGPTFRAENSNTRRH 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1197219449 233 PGEFYQLDLEMSFVTQEDVWNTVEP----VITNVFEQFAD-----GKRVTKG------------WPRIPYDTAI 285
Cdd:PRK03932 228 LAEFWMIEPEMAFADLEDNMDLAEEmlkyVVKYVLENCPDdleflNRRVDKGdierlenfiespFPRITYTEAI 301
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
15-119 |
6.21e-20 |
|
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: 85.06 E-value: 6.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 15 TAGDAGNNVRLSGWVHRVRDHGGLLFIDLRDNYGITQCVID---PDSAAFSAAEKVRSEWVLRIDGEVKLRDAAavnpni 91
Cdd:cd04316 7 TPELDGEEVTVAGWVHEIRDLGGIKFVILRDREGIVQVTAPkkkVDKELFKTVRKLSRESVISVTGTVKAEPKA------ 80
|
90 100
....*....|....*....|....*....
gi 1197219449 92 PTGtIEVFIREIEVLSEAK-ELPLPVFGD 119
Cdd:cd04316 81 PNG-VEIIPEEIEVLSEAKtPLPLDPTGK 108
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
7-565 |
1.76e-18 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 89.64 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 7 RSHTCGALTAGDAGNNVRLSGWVHRVRDHGGLLFIDLRDNYGITQCVIDpdsaafsaAEKVRSEWVLRIDGEVKLRDAAA 86
Cdd:PRK02983 638 PTHTVAEALDAPTGEEVSVSGRVLRIRDYGGVLFADLRDWSGELQVLLD--------ASRLEQGSLADFRAAVDLGDLVE 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 87 VNPNIPT---GTIEVFIREIEVlsEAKEL-PLPV----FGDadyPEdIRLKYRFLDLRREKLHANIL-KRTKIISAMRAG 157
Cdd:PRK02983 710 VTGTMGTsrnGTLSLLVTSWRL--AGKCLrPLPDkwkgLTD---PE-ARVRQRYLDLAVNPEARDLLrARSAVVRAVRET 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 158 MGGAGFTEFSTPIL-TASSPEGARDFlvpsRIHPGTF---FALPQAPQQYKQLLMVAGFDRYFQVAPCFRDEDPRADRLP 233
Cdd:PRK02983 784 LVARGFLEVETPILqQVHGGANARPF----VTHINAYdmdLYLRIAPELYLKRLCVGGVERVFELGRNFRNEGVDATHNP 859
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 234 gEFYQLD--------LEMSFVTQEDVWNTV-----EPVIT----NVFEQFADgkrVTKGWPRIPYDTAIRkygsdkpdlr 296
Cdd:PRK02983 860 -EFTLLEayqahadyDTMRDLTRELIQNAAqaahgAPVVMrpdgDGVLEPVD---ISGPWPVVTVHDAVS---------- 925
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 297 npieiQGVTEHfagsgfkvfanqIEADSKVEVWaipaknkpgaepigRAFCDRmnawaqgegqpglgyiffkdgqgsgpi 376
Cdd:PRK02983 926 -----EALGEE------------IDPDTPLAEL--------------RKLCDA--------------------------- 947
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 377 aknigeertAALKAQLGLDDGDAVFfvagrpdKFYKFAGEARTKVGTdlglvdseqfalcWIVDFPFyEWSeeekridfa 456
Cdd:PRK02983 948 ---------AGIPYRTDWDAGAVVL-------ELYEHLVEDRTTFPT-------------FYTDFPT-SVS--------- 988
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 457 hnPFSMPQGGIDGLngddplslkAYQYDAVCNGFEI------------------------ASGsirnqEPETMikafelt 512
Cdd:PRK02983 989 --PLTRPHRSDPGL---------AERWDLVAWGVELgtayseltdpveqrrrlteqsllaAGG-----DPEAM------- 1045
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1197219449 513 gksrsEVEEQFgglYRAFQYGAPPHGGAAFGIDRIVMLLCGvANLREITAFPM 565
Cdd:PRK02983 1046 -----ELDEDF---LQALEYAMPPTGGLGMGVDRLVMLLTG-RSIRETLPFPL 1089
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
7-565 |
5.00e-17 |
|
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA synthetase (class II) is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440803 [Multi-domain] Cd Length: 495 Bit Score: 83.93 E-value: 5.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 7 RSHTC-------GALTAGDA-GNNVRLSGWVHRVRDHGGLLFIDLRDNYGITQCVIDPDS---AAFSAAEKV-RSEWVLr 74
Cdd:COG1190 35 RTHTAaeirekyDELEAEEEtGDEVSVAGRIMAKRDMGKASFADLQDGSGRIQLYLRRDElgeEAYELFKLLdLGDIVG- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 75 IDGEV-KLRdaaavnpnipTGTIEVFIREIEVLSeaKEL-PLPV--FGDADyPEdIRLKYRFLDL-RREKLHANILKRTK 149
Cdd:COG1190 114 VEGTVfRTK----------TGELSVKVEELTLLS--KSLrPLPEkfHGLTD-PE-TRYRQRYVDLiVNPEVRETFRKRSK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 150 IISAMRAGMGGAGFTEFSTPILTaSSPEGA--RDF------------LvpsRIhpgtffalpqAPQQY-KQLLmVAGFDR 214
Cdd:COG1190 180 IIRAIRRFLDERGFLEVETPMLQ-PIAGGAaaRPFithhnaldmdlyL---RI----------APELYlKRLI-VGGFER 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 215 YFQVAPCFRDEDprADR--LPgEFYQLDLEMSFVTQEDVWNTVEPVITNVFEQfADGKRV----------TKGWPRIPYD 282
Cdd:COG1190 245 VFEIGRNFRNEG--IDTthNP-EFTMLELYQAYADYNDMMDLTEELIREAAEA-VLGTTKvtyqgqeidlSPPWRRITMV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 283 TAIRKY-GSDKPDLRNPIEIqgvtehfagsgfkvfanqieadskvevwaipaknkpgaepigRAFCDRMNawaqgegqpg 361
Cdd:COG1190 321 EAIKEAtGIDVTPLTDDEEL------------------------------------------RALAKELG---------- 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 362 lgyIFFKDGQGSGpiaknigeertaalKAQLGLddgdavffvagrpdkFYKFAGEArtkvgtdlgLVDSeqfalCWIVDF 441
Cdd:COG1190 349 ---IEVDPGWGRG--------------KLIDEL---------------FEELVEPK---------LIQP-----TFVTDY 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 442 PFyEWSeeekridfahnPFSMPqggidglNGDDPLslKAYQYDAVCNGFEIAsgsirnqepetmiKAF-ELT-------- 512
Cdd:COG1190 383 PV-EVS-----------PLAKR-------HRDDPG--LTERFELFIAGREIA-------------NAFsELNdpidqrer 428
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1197219449 513 ------GKSRSEVE-----EQFgglYRAFQYGAPPHGGAAFGIDRIVMLLCGVANLREITAFPM 565
Cdd:COG1190 429 feeqleLKAAGDDEampmdEDF---LRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFPL 489
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
6-568 |
1.20e-16 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 83.12 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 6 YRSHT---CGALTAGD-AGNNVRLSGWVHRVRDHGGLLFIDLRDNygitqcvIDPDSAAFSAAEKVRSEWVLRIdGEVKL 81
Cdd:PTZ00401 60 YKSRTfipVAVLSKPElVDKTVLIRARVSTTRKKGKMAFMVLRDG-------SDSVQAMAAVEGDVPKEMIDFI-GQIPT 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 82 RDAAAVNPNI------PTGT----IEVFIREIEVLSEA-KELPLpVFGDADYPE---------DIRLKYRFLDLRREKLH 141
Cdd:PTZ00401 132 ESIVDVEATVckveqpITSTshsdIELKVKKIHTVTESlRTLPF-TLEDASRKEsdegakvnfDTRLNSRWMDLRTPASG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 142 ANILKRTKIISAMRAGMGGAGFTEFSTP-ILTASSPEGARDFLVPsriHPGTFFALPQAPQQYKQLLMVAGFDRYFQVAP 220
Cdd:PTZ00401 211 AIFRLQSRVCQYFRQFLIDSDFCEIHSPkIINAPSEGGANVFKLE---YFNRFAYLAQSPQLYKQMVLQGDVPRVFEVGP 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 221 CFRDEDPRADRLPGEFYQLDLEMSFVTQ-EDVWNTVEPVITNVFEQFADGKRVTKGWPR-IPYDtairkygsdkpdlrnP 298
Cdd:PTZ00401 288 VFRSENSNTHRHLTEFVGLDVEMRINEHyYEVLDLAESLFNYIFERLATHTKELKAVCQqYPFE---------------P 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 299 IEIQGVTEHFAGSGFKVFANQIEADSKVEVWAipaknkpgaepigRAFCDRMNAWAQGEGQPGLGYIFFKDGQGSGPIak 378
Cdd:PTZ00401 353 LVWKLTPERMKELGVGVISEGVEPTDKYQARV-------------HNMDSRMLRINYMHCIELLNTVLEEKMAPTDDI-- 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 379 NIGEERTAA--LKAQLGLDdgdavFFVAGRpdkfykFAGEARtkvgtdlglvdseqfalcwivdfPFY--EWSEEEKrid 454
Cdd:PTZ00401 418 NTTNEKLLGklVKERYGTD-----FFISDR------FPSSAR-----------------------PFYtmECKDDER--- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 455 FAHNpfsmpqggidglngddplslkayqYDAVCNGFEIASGSIRNQEPETMIKAFELTGKSRSEVEEQFGglyrAFQYGA 534
Cdd:PTZ00401 461 FTNS------------------------YDMFIRGEEISSGAQRIHDPDLLLARAKMLNVDLTPIKEYVD----SFRLGA 512
|
570 580 590
....*....|....*....|....*....|....
gi 1197219449 535 PPHGGAAFGIDRIVMLLCGVANLREITAFPMNQQ 568
Cdd:PTZ00401 513 WPHGGFGVGLERVVMLYLGLSNVRLASLFPRDPQ 546
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
12-568 |
2.36e-16 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 82.39 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 12 GALTAGD--AGNNVRLSGWVHRVRDHGGLLFIDLRDNYGITQCVIdpdsaafSAAEKVRSEWVLRIDGEVKLRD---AAA 86
Cdd:PTZ00385 97 GYLASGDraAQATVRVAGRVTSVRDIGKIIFVTIRSNGNELQVVG-------QVGEHFTREDLKKLKVSLRVGDiigADG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 87 VNPNIPTGTIEVFIREIEVLSE---AKELPLP-VFGDADYPE-DIRLKYRFLDLRREK-LHANILKRTKIISAMRAGMGG 160
Cdd:PTZ00385 170 VPCRMQRGELSVAASRMLILSPyvcTDQVVCPnLRGFTVLQDnDVKYRYRFTDMMTNPcVIETIKKRHVMLQALRDYFNE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 161 AGFTEFSTPIL-TASSPEGARDFLVPSRIHPGTFFaLPQAPQQYKQLLMVAGFDRYFQVAPCFRDEDprADRLPG-EFYQ 238
Cdd:PTZ00385 250 RNFVEVETPVLhTVASGANAKSFVTHHNANAMDLF-LRVAPELHLKQCIVGGMERIYEIGKVFRNED--ADRSHNpEFTS 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 239 LDLEMSFVTQEDVWntvePVITNVFEQFA---DGKRVTKGWPRipydtaiRKYGsdkpdlrNPIEIQgvtehfAGSGFKV 315
Cdd:PTZ00385 327 CEFYAAYHTYEDLM----PMTEDIFRQLAmrvNGTTVVQIYPE-------NAHG-------NPVTVD------LGKPFRR 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 316 FA--NQIEADSKVEvwaIPAKNKPGAePIGRAFcdrMNAwaqgegqpglgyIFFKDGQGSGPIaknigeeRTAALKAQLG 393
Cdd:PTZ00385 383 VSvyDEIQRMSGVE---FPPPNELNT-PKGIAY---MSV------------VMLRYNIPLPPV-------RTAAKMFEKL 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 394 LDdgdavFFVAGRpdkfykfageartkvgtdlgLVDSeqfalCWIVDFPFYewseeekridfaHNPFSMPQGGIDGLngd 473
Cdd:PTZ00385 437 ID-----FFITDR--------------------VVEP-----TFVMDHPLF------------MSPLAKEQVSRPGL--- 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 474 dplslkAYQYDAVCNGFEIASGSIRNQEPETMIKAFELTGKSRSEVEEQFGGLYRAF----QYGAPPHGGAAFGIDRIVM 549
Cdd:PTZ00385 472 ------AERFELFVNGIEYCNAYSELNDPHEQYHRFQQQLVDRQGGDEEAMPLDETFlkslQVGLPPTAGWGMGIDRALM 545
|
570
....*....|....*....
gi 1197219449 550 LLCGVANLREITAFPMNQQ 568
Cdd:PTZ00385 546 LLTNSSNIRDGIIFPLLRQ 564
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
23-106 |
2.67e-16 |
|
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: 73.81 E-value: 2.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 23 VRLSGWVHRV-RDHGGLLFIDLRDNYGITQCVIDPDsAAFSAAEKVRSEWVLRIDGEVKLRdaaavnpniPTGTIEVFIR 101
Cdd:pfam01336 1 VTVAGRVTSIrRSGGKLLFLTLRDGTGSIQVVVFKE-EAEKLAKKLKEGDVVRVTGKVKKR---------KGGELELVVE 70
|
....*
gi 1197219449 102 EIEVL 106
Cdd:pfam01336 71 EIELL 75
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
7-289 |
1.12e-15 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 79.75 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 7 RSHTCGALTA----------GDAGNNVRLSGWVHRVRDHGGLLFIDLRDNYGITQCVIDPDS---AAFSAAEKV-RSEWV 72
Cdd:PRK00484 31 RTHTAAELRAkyddkekeelEELEIEVSVAGRVMLKRVMGKASFATLQDGSGRIQLYVSKDDvgeEALEAFKKLdLGDII 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 73 LrIDGEV-KLRdaaavnpnipTGTIEVFIREIEVLSeaKEL-PLPV--FGDADypEDIRLKYRFLDL-RREKLHANILKR 147
Cdd:PRK00484 111 G-VEGTLfKTK----------TGELSVKATELTLLT--KSLrPLPDkfHGLTD--VETRYRQRYVDLiVNPESRETFRKR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 148 TKIISAMRAGMGGAGFTEFSTPILtASSPEG--ARDF------------LvpsRIhpgtffalpqAPQQY-KQLLmVAGF 212
Cdd:PRK00484 176 SKIISAIRRFLDNRGFLEVETPML-QPIAGGaaARPFithhnaldidlyL---RI----------APELYlKRLI-VGGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 213 DRYFQVAPCFRDEDprADRL--PgEFYQLDLEMSFVTQEDVWNTVEPVITNVFEQFADGKRVTKG---------WPRIPY 281
Cdd:PRK00484 241 ERVYEIGRNFRNEG--IDTRhnP-EFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTYQgteidfgppFKRLTM 317
|
....*...
gi 1197219449 282 DTAIRKYG 289
Cdd:PRK00484 318 VDAIKEYT 325
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
147-250 |
1.76e-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: 66.76 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 147 RTKIISAMRAGMGGAGFTEFSTPILTASSPEGARD----FLVPSRIHPGTFFALPQAPQQYKQLLMV----AGFDRYFQV 218
Cdd:cd00768 2 RSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGhepkDLLPVGAENEEDLYLRPTLEPGLVRLFVshirKLPLRLAEI 81
|
90 100 110
....*....|....*....|....*....|....
gi 1197219449 219 APCFRDEDPRAD--RLPgEFYQLDLEMSFVTQED 250
Cdd:cd00768 82 GPAFRNEGGRRGlrRVR-EFTQLEGEVFGEDGEE 114
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
23-108 |
1.80e-12 |
|
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and Saccharomyces cerevisiae cytoplasmic asparaginyl-tRNA synthetase (AsnRS), in Brugia malayai AsnRs and, in various putative bacterial AsnRSs. 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 synthesis, whereas the other exclusively with mitochondrial protein synthesis. AsnRS is immunodominant antigen of the filarial nematode B. malayai and 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: 239818 [Multi-domain] Cd Length: 84 Bit Score: 63.02 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 23 VRLSGWVHRVRDHGGLLFIDLRDNYGITQCVI-DPDSAAFSAAEKVRSEWVLRIDGEVKLRDAAAVNPniptGTIEVFIR 101
Cdd:cd04323 2 VKVFGWVHRLRSQKKLMFLVLRDGTGFLQCVLsKKLVTEFYDAKSLTQESSVEVTGEVKEDPRAKQAP----GGYELQVD 77
|
....*..
gi 1197219449 102 EIEVLSE 108
Cdd:cd04323 78 YLEIIGE 84
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
7-297 |
3.53e-11 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 65.85 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 7 RSHTCGALTAG-DAGNN---------VRLSGWVHRVRDHGGLLFIDLRDNYGITQCVIDPDSAAFSAAEKVRSEWVLrid 76
Cdd:PRK12445 42 RDHTSDQLHEEfDAKDNqeleslnieVSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEGVYNDQFKKWDL--- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 77 GEVKlrDAAAVNPNIPTGTIEVFIREIEVLSEA-KELPLPVFGDADypEDIRLKYRFLDL-RREKLHANILKRTKIISAM 154
Cdd:PRK12445 119 GDII--GARGTLFKTQTGELSIHCTELRLLTKAlRPLPDKFHGLQD--QEVRYRQRYLDLiANDKSRQTFVVRSKILAAI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 155 RAGMGGAGFTEFSTPILTASsPEGA--RDFLVPSRIHPGTFFaLPQAPQQYKQLLMVAGFDRYFQVAPCFRDEDPRADRL 232
Cdd:PRK12445 195 RQFMVARGFMEVETPMMQVI-PGGAsaRPFITHHNALDLDMY-LRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHN 272
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1197219449 233 PgEFYQLDLEMSFVTQEDVWNTVEPVITNVFEQFADGKRVTKG---------WPRIPYDTAIRKY--GSDKPDLRN 297
Cdd:PRK12445 273 P-EFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGehvfdfgkpFEKLTMREAIKKYrpETDMADLDN 347
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
4-260 |
1.06e-10 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 64.24 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 4 HRY-RSHTC-------GALTAG--DAGNNVRLSGWVHRVRDHGGLLFIDLRDNYGITQCVIDPDSAAFSAAEkvrsewVL 73
Cdd:PLN02502 82 YKFdVTHTApelqekyGSLENGeeLEDVSVSVAGRIMAKRAFGKLAFYDLRDDGGKIQLYADKKRLDLDEEE------FE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 74 RIDGEVKLRDAAAVNPNI---PTGTIEVFIREIEVLSEAKeLPLP--VFGDADypEDIRLKYRFLDLRREKLHANILK-R 147
Cdd:PLN02502 156 KLHSLVDRGDIVGVTGTPgktKKGELSIFPTSFEVLTKCL-LMLPdkYHGLTD--QETRYRQRYLDLIANPEVRDIFRtR 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 148 TKIISAMRAGMGGAGFTEFSTPIL-TASSPEGARDFLvpsrihpgTF-------FALPQAPQQYKQLLMVAGFDRYFQVA 219
Cdd:PLN02502 233 AKIISYIRRFLDDRGFLEVETPMLnMIAGGAAARPFV--------THhndlnmdLYLRIATELHLKRLVVGGFERVYEIG 304
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1197219449 220 PCFRDE--DPRADrlPgEFYQLDLEMSFVTQEDVWNTVEPVIT 260
Cdd:PLN02502 305 RQFRNEgiSTRHN--P-EFTTCEFYQAYADYNDMMELTEEMVS 344
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
142-301 |
4.03e-10 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 61.57 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 142 ANILK-RTKIISAMRAGMGGAGFTEFSTPILTASSPEGARDFL-----VPSRIHPGTFFALPQAPQQYKQLlMVAGFDRY 215
Cdd:PRK06462 27 RKVLKvQSSILRYTREFLDGRGFVEVLPPIISPSTDPLMGLGSdlpvkQISIDFYGVEYYLADSMILHKQL-ALRMLGKI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 216 FQVAPCFRDE--DPRADRLPGEFYQLDLEMSFVTQEDVWNTVEPVITNVFeqfadgKRVTKgwpriPYDTAIRKYGSDKP 293
Cdd:PRK06462 106 FYLSPNFRLEpvDKDTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLV------KELLE-----EHEDELEFFGRDLP 174
|
....*...
gi 1197219449 294 DLRNPIEI 301
Cdd:PRK06462 175 HLKRPFKR 182
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
23-127 |
5.21e-10 |
|
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: 56.76 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 23 VRLSGWVHRVRDHGGLLFIDLRDNYGITQCVI--DPDSAAFSAAEKVRSEWVLRIDGEVKlrdaaaVNPNIPTGtIEVFI 100
Cdd:cd04319 2 VTLAGWVYRKREVGKKAFIVLRDSTGIVQAVFskDLNEEAYREAKKVGIESSVIVEGAVK------ADPRAPGG-AEVHG 74
|
90 100
....*....|....*....|....*..
gi 1197219449 101 REIEVLSEAKELPLPVFGDADYPEDIR 127
Cdd:cd04319 75 EKLEIIQNVEFFPITEDASDEFLLDVR 101
|
|
| GAD |
pfam02938 |
GAD domain; This domain is found in some members of the GatB and aspartyl tRNA synthetases. |
316-412 |
1.67e-08 |
|
GAD domain; This domain is found in some members of the GatB and aspartyl tRNA synthetases.
Pssm-ID: 397199 [Multi-domain] Cd Length: 94 Bit Score: 52.27 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 316 FANQIEADSKVEvwAIPAknkPGAEPIGRAFCDRMNAWAQGEGQPGLGYIFFKDGQGSGPIAKNIGEERTAALKAQLGLD 395
Cdd:pfam02938 1 FSEALKSGGSVK--ALRV---PGAAGLSRKEIDELERFAKEYGAKGLAWIKVEGGGHTGPIAKFLTEEEVEKLLEAVGAE 75
|
90
....*....|....*..
gi 1197219449 396 DGDAVFFVAGRPDKFYK 412
Cdd:pfam02938 76 DGDALLFVADKKKTVNK 92
|
|
| ScAspRS_mt_like_N |
cd04321 |
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
22-108 |
1.93e-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: 48.85 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 22 NVRLSGWVHRVRD-HGGLLFIDLRDNYG-ITQCVIDPDSAAFSAAEKVRSEWVLRIDGEVKLRDAAAVNPNIPtgtIEVF 99
Cdd:cd04321 1 KVTLNGWIDRKPRiVKKLSFADLRDPNGdIIQLVSTAKKDAFSLLKSITAESPVQVRGKLQLKEAKSSEKNDE---WELV 77
|
....*....
gi 1197219449 100 IREIEVLSE 108
Cdd:cd04321 78 VDDIQTLNA 86
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
145-295 |
2.17e-07 |
|
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: 52.97 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 145 LKRTKIISAMRAGMGGAGFTEFSTPILTaSSPEG--ARDFLvpsrihpgTF-------FALPQAPQQYKQLLMVAGFDRY 215
Cdd:cd00775 9 IVRSKIISYIRKFLDDRGFLEVETPMLQ-PIAGGaaARPFI--------THhnaldmdLYLRIAPELYLKRLIVGGFERV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 216 FQVAPCFRDE--DPRADrlPgEFYQLDLEMSFVTQEDVWNTVEPVITNVFEQFADGKRV---------TKGWPRIPYDTA 284
Cdd:cd00775 80 YEIGRNFRNEgiDLTHN--P-EFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIeyggkeldfTPPFKRVTMVDA 156
|
170
....*....|..
gi 1197219449 285 IRKY-GSDKPDL 295
Cdd:cd00775 157 LKEKtGIDFPEL 168
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
487-564 |
5.15e-07 |
|
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: 51.82 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 487 CNGFEIASGSIRNQEP-------ETMIKAFELTGKSRSEVEEQFgglYRAFQYGAPPHGGAAFGIDRIVMLLCGVANLRE 559
Cdd:cd00775 244 ICGKEIANAYTELNDPfdqrerfEEQAKQKEAGDDEAMMMDEDF---VTALEYGMPPTGGLGIGIDRLVMLLTDSNSIRD 320
|
....*
gi 1197219449 560 ITAFP 564
Cdd:cd00775 321 VILFP 325
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
23-135 |
1.25e-06 |
|
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These enzymes are homodimeric class 2b 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. Included in this group are E. coli LysS and LysU. These two isoforms of LysRS are encoded by distinct genes which are differently regulated. Eukaryotes contain 2 sets of aaRSs, both of which encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Saccharomyces cerevisiae cytoplasmic and mitochondrial LysRSs have been shown to participate in the mitochondrial import of the only nuclear-encoded tRNA of S. cerevisiae (tRNAlysCUU). The gene for human LysRS encodes both the cytoplasmic and the mitochondrial isoforms of LysRS. In addition to their housekeeping role, human lysRS may function as a signaling molecule that activates immune cells and tomato LysRS may participate in a root-specific 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.
Pssm-ID: 239817 [Multi-domain] Cd Length: 108 Bit Score: 47.09 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 23 VRLSGWVHRVRDHGGLLFIDLRDNYGITQCVIDPDSAAFSAAEKVRSEW----VLRIDGEVKLRDaaavnpnipTGTIEV 98
Cdd:cd04322 2 VSVAGRIMSKRGSGKLSFADLQDESGKIQVYVNKDDLGEEEFEDFKKLLdlgdIIGVTGTPFKTK---------TGELSI 72
|
90 100 110
....*....|....*....|....*....|....*...
gi 1197219449 99 FIREIEVLSEA-KELPLPVFGDADypEDIRLKYRFLDL 135
Cdd:cd04322 73 FVKEFTLLSKSlRPLPEKFHGLTD--VETRYRQRYLDL 108
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
94-225 |
2.31e-06 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 50.39 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 94 GTIEVFIREIEVLSEAKELpLPV-FGDADypEDIRLKYRFLDLR-REKLHANILKRTKIISAMRAGMGGAGFTEFSTPIL 171
Cdd:PTZ00417 204 GELSIFPKETIILSPCLHM-LPMkYGLKD--TEIRYRQRYLDLMiNESTRSTFITRTKIINYLRNFLNDRGFIEVETPTM 280
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1197219449 172 T-ASSPEGARDFLVPSRIHPGTFFaLPQAPQQYKQLLMVAGFDRYFQVAPCFRDE 225
Cdd:PTZ00417 281 NlVAGGANARPFITHHNDLDLDLY-LRIATELPLKMLIVGGIDKVYEIGKVFRNE 334
|
|
| GatE |
COG2511 |
Archaeal Glu-tRNAGln amidotransferase subunit E, contains GAD domain [Translation, ribosomal ... |
297-409 |
3.68e-06 |
|
Archaeal Glu-tRNAGln amidotransferase subunit E, contains GAD domain [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442001 [Multi-domain] Cd Length: 630 Bit Score: 49.79 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 297 NPIEIQGVTEHFAGSGFKVFANQIEADSKVevWAIPAKN---KPGAEP-----IGRAFCDRMNAWaqgegqpGLGYIFFK 368
Cdd:COG2511 278 EDIEIVDVTDVFKDTKSKVIKKALKKGGKV--LAVKLPGfagLLGREIqpgrrLGTELADYAKFW-------GVGGIFHT 348
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1197219449 369 D---GQGsgpiaknIGEERTAALKAQLGLDDGDAVFFVAGRPDK 409
Cdd:COG2511 349 DelpNYG-------ITEEEVEALREALGAGEEDAFVIVADEEEK 385
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
22-116 |
1.20e-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: 44.09 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 22 NVRLSGWVHRVRDHGG-LLFIDLRDNYGITQCVIDPDSAAFSA-----AEKVRSEWVLRIDGEVKLrdaaavnPNIP-TG 94
Cdd:cd04320 1 EVLIRARVHTSRAQGAkLAFLVLRQQGYTIQGVLAASAEGVSKqmvkwAGSLSKESIVDVEGTVKK-------PEEPiKS 73
|
90 100
....*....|....*....|....*..
gi 1197219449 95 T----IEVFIREIEVLSEAKE-LPLPV 116
Cdd:cd04320 74 CtqqdVELHIEKIYVVSEAAEpLPFQL 100
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
23-81 |
1.83e-05 |
|
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli asparaginyl-tRNA synthetase (AsnRS) and, in Arabidopsis thaliana and Saccharomyces cerevisiae mitochondrial (mt) AsnRS. 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. S. cerevisiae mtAsnRS can charge E.coli tRNA with asparagines. Mutations in the gene for S. cerevisiae mtAsnRS has been found to induce a "petite" phenotype typical for a mutation in a nuclear gene that results in a non-functioning mitochondrial protein synthesis system.
Pssm-ID: 239813 [Multi-domain] Cd Length: 82 Bit Score: 43.32 E-value: 1.83e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1197219449 23 VRLSGWVHRVRDHGGLLFIDLRDnyGIT----QCVIDPDSAAFSAAEKVRSEWVLRIDGEVKL 81
Cdd:cd04318 2 VTVNGWVRSVRDSKKISFIELND--GSClknlQVVVDKELTNFKEILKLSTGSSIRVEGVLVK 62
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
20-250 |
1.91e-05 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 47.66 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 20 GNNVRLSGWVHRVRDHGGLLFIDLRDNYGIT--QCVIDPDSAAFsaaEKVRSEWVLriDGEVKLRDAAAVNPNIPTGTIE 97
Cdd:PLN02603 107 GKTLNVMGWVRTLRAQSSVTFIEVNDGSCLSnmQCVMTPDAEGY---DQVESGLIT--TGASVLVQGTVVSSQGGKQKVE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 98 VFIREIEVLSEAkelplpvfgDADYP-EDIRLKYRFLdlrREKLHanILKRTKIISAM---RAGMGGA--------GFTE 165
Cdd:PLN02603 182 LKVSKIVVVGKS---------DPSYPiQKKRVSREFL---RTKAH--LRPRTNTFGAVarvRNALAYAthkffqenGFVW 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 166 FSTPILTASSPEGA-RDFLVPSRIH-------------PGT----------FFALPQAPQQYKQL---LMVAGFDRYFQV 218
Cdd:PLN02603 248 VSSPIITASDCEGAgEQFCVTTLIPnsaenggslvddiPKTkdglidwsqdFFGKPAFLTVSGQLngeTYATALSDVYTF 327
|
250 260 270
....*....|....*....|....*....|..
gi 1197219449 219 APCFRDEDPRADRLPGEFYQLDLEMSFVTQED 250
Cdd:PLN02603 328 GPTFRAENSNTSRHLAEFWMIEPELAFADLND 359
|
|
| PRK04028 |
PRK04028 |
Glu-tRNA(Gln) amidotransferase subunit GatE; |
300-409 |
4.45e-05 |
|
Glu-tRNA(Gln) amidotransferase subunit GatE;
Pssm-ID: 235205 [Multi-domain] Cd Length: 630 Bit Score: 46.35 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 300 EIQGVTEHFAGSGFKVFANQIEADSKVevWAIPAKN---------KPGAEpIGRAFCDRMNAWaqgegqpGLGYIFFKD- 369
Cdd:PRK04028 280 EIVDVTELFKDTKSKIIKKALKKGGKV--LAIKLPGfkgllgreiQPGRR-LGTELADYAKAW-------GVGGIFHTDe 349
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1197219449 370 --GQGsgpiaknIGEERTAALKAQLGLDDGDAVFFVAGRPDK 409
Cdd:PRK04028 350 lpAYG-------ITEEEVEALREALGAGENDAFILVADEEEK 384
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
16-179 |
1.67e-04 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 44.60 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 16 AGDAGNNVRLSGWVHRVRDHG--GLLFIDLRDNYGITQCVIDPDSAAFSAAEKVRSEWVLRIDGEVKLrdaaavnPNIPT 93
Cdd:PLN02221 46 AGLAGQKVRIGGWVKTGREQGkgTFAFLEVNDGSCPANLQVMVDSSLYDLSTLVATGTCVTVDGVLKV-------PPEGK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 94 GTIEvfirEIEvLSEAKELPLPVFGDADYP-EDIRLKYRFLdlrREKLHanILKRTKIISA---MRAGMGGA-------- 161
Cdd:PLN02221 119 GTKQ----KIE-LSVEKVIDVGTVDPTKYPlPKTKLTLEFL---RDVLH--LRSRTNSISAvarIRNALAFAthsffqeh 188
|
170
....*....|....*...
gi 1197219449 162 GFTEFSTPILTASSPEGA 179
Cdd:PLN02221 189 SFLYIHTPIITTSDCEGA 206
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
527-564 |
5.50e-04 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 42.70 E-value: 5.50e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1197219449 527 YRAF-QYGAPPHGGAAFGIDRIVMLLCGVANLREITAFP 564
Cdd:PTZ00425 540 YRQLrKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFP 578
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
488-560 |
6.80e-03 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 38.76 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197219449 488 NGFEIASGSIRNQEPETMIKAFELTGKSRSE-------VEEQFgglYRAFQYGAPPHGGAAFGIDRIVMLLCGVANLREI 560
Cdd:PRK09350 230 KGIELANGFHELTDAREQRQRFEQDNRKRAArglpqqpIDENL---IAALEAGLPDCSGVALGVDRLIMLALGAESISEV 306
|
|
| |
