|
Name |
Accession |
Description |
Interval |
E-value |
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
6-596 |
0e+00 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 1009.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 6 YRTHHAVEVTEELVGQKVTIAGWVDRRRDHGGVAFVDVRDNTGLVQVVIYDE----ETARPLRSEFVVQVTGEVRLRPDG 81
Cdd:PRK00476 3 MRTHYCGELRESHVGQTVTLCGWVHRRRDHGGLIFIDLRDREGIVQVVFDPDaeafEVAESLRSEYVIQVTGTVRARPEG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 82 NENDHLATGKIEIVAQTVTILAKSDALPFQVSTALENesenklpSEDVRLKYRYLDLRRPSMQRNLKLRSNMAKAARHAL 161
Cdd:PRK00476 83 TVNPNLPTGEIEVLASELEVLNKSKTLPFPIDDEEDV-------SEELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 162 EDMDFTEVETPTFIKSTPEGARDFVVPARLVPGSWYALPQSPQLLKQLLMVSGVERYYQLARCYRDEDFRADRQPEFTQL 241
Cdd:PRK00476 156 DDNGFLEIETPILTKSTPEGARDYLVPSRVHPGKFYALPQSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADRQPEFTQI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 242 DMEMSFASQEDVMAMAERVIAAIWKEA-GHEITLPLPRITWQEAMDKYGSDKPDLRFGNPLIELTDFFKNTPFRVFQA-- 318
Cdd:PRK00476 236 DIEMSFVTQEDVMALMEGLIRHVFKEVlGVDLPTPFPRMTYAEAMRRYGSDKPDLRFGLELVDVTDLFKDSGFKVFAGaa 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 319 ---SYVGAVLFKGGAETP-RRQFDAWQDWAKQRGAKGLAYVVFGEDGeLKGPVAKNLSEEERAGLKEAVGAEDGDAVFFA 394
Cdd:PRK00476 316 ndgGRVKAIRVPGGAAQLsRKQIDELTEFAKIYGAKGLAYIKVNEDG-LKGPIAKFLSEEELAALLERTGAKDGDLIFFG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 395 AGSRESSQLLLGAVRVELASRAGLLHPDEFAFTWVVDFPLFKRTDdpddddvavGHSKWTSMHHPFTMPSADWIDKFDK- 473
Cdd:PRK00476 395 ADKAKVVNDALGALRLKLGKELGLIDEDKFAFLWVVDFPMFEYDE---------EEGRWVAAHHPFTMPKDEDLDELETt 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 474 DPEHAMSDSYDIVCNGNEMGGGSVRIHRDDIQDRVLNVLGIDKAEADEKFGFLLEAFKYGAPPHAGIALGWDRTAAILAG 553
Cdd:PRK00476 466 DPGKARAYAYDLVLNGYELGGGSIRIHRPEIQEKVFEILGISEEEAEEKFGFLLDALKYGAPPHGGIAFGLDRLVMLLAG 545
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 490236703 554 ASSIRDVIAFPKAGGGRDPLTGAPAPISDEQRAETGVDYDPEE 596
Cdd:PRK00476 546 ADSIRDVIAFPKTQSAQDLLTGAPSPVDEKQLRELGIRLRKKE 588
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
6-598 |
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: 1005.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 6 YRTHHAVEVTEELVGQKVTIAGWVDRRRDHGGVAFVDVRDNTGLVQVVIYDE------ETARPLRSEFVVQVTGEVRLRP 79
Cdd:COG0173 2 YRTHYCGELRESDVGQEVTLSGWVHRRRDHGGLIFIDLRDRYGITQVVFDPDdsaeafEKAEKLRSEYVIAVTGKVRARP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 80 DGNENDHLATGKIEIVAQTVTILAKSDALPFQVStalenesENKLPSEDVRLKYRYLDLRRPSMQRNLKLRSNMAKAARH 159
Cdd:COG0173 82 EGTVNPKLPTGEIEVLASELEILNKAKTPPFQID-------DDTDVSEELRLKYRYLDLRRPEMQKNLILRHKVTKAIRN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 160 ALEDMDFTEVETPTFIKSTPEGARDFVVPARLVPGSWYALPQSPQLLKQLLMVSGVERYYQLARCYRDEDFRADRQPEFT 239
Cdd:COG0173 155 YLDENGFLEIETPILTKSTPEGARDYLVPSRVHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFRDEDLRADRQPEFT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 240 QLDMEMSFASQEDVMAMAERVIAAIWKE-AGHEITLPLPRITWQEAMDKYGSDKPDLRFGNPLIELTDFFKNTPFRVFQA 318
Cdd:COG0173 235 QLDIEMSFVDQEDVFELMEGLIRHLFKEvLGVELPTPFPRMTYAEAMERYGSDKPDLRFGLELVDVTDIFKDSGFKVFAG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 319 -----SYVGAVLFKGGAETPRRQFDAWQDWAKQRGAKGLAYVVFGEDGeLKGPVAKNLSEEERAGLKEAVGAEDGDAVFF 393
Cdd:COG0173 315 aaengGRVKAINVPGGASLSRKQIDELTEFAKQYGAKGLAYIKVNEDG-LKSPIAKFLSEEELAAILERLGAKPGDLIFF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 394 AAGSRESSQLLLGAVRVELASRAGLLHPDEFAFTWVVDFPLFKRTDDPddddvavghSKWTSMHHPFTMPSADWIDKFDK 473
Cdd:COG0173 394 VADKPKVVNKALGALRLKLGKELGLIDEDEFAFLWVVDFPLFEYDEEE---------GRWVAMHHPFTMPKDEDLDLLET 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 474 DPEHAMSDSYDIVCNGNEMGGGSVRIHRDDIQDRVLNVLGIDKAEADEKFGFLLEAFKYGAPPHAGIALGWDRTAAILAG 553
Cdd:COG0173 465 DPGKVRAKAYDLVLNGYELGGGSIRIHDPELQEKVFELLGISEEEAEEKFGFLLEAFKYGAPPHGGIAFGLDRLVMLLAG 544
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 490236703 554 ASSIRDVIAFPKAGGGRDPLTGAPAPISDEQRAETGVDYDPEEDE 598
Cdd:COG0173 545 EDSIRDVIAFPKTQSAQDLMTGAPSEVDEKQLKELHIRLRPPEKK 589
|
|
| aspS_bact |
TIGR00459 |
aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be ... |
7-594 |
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: 729.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 7 RTHHAVEVTEELVGQKVTIAGWVDRRRDHGGVAFVDVRDNTGLVQVVIYDEETARP----LRSEFVVQVTGEVRLRPDGN 82
Cdd:TIGR00459 2 RTHYCGQLRTEHLGQTVTLAGWVNRRRDLGGLIFIDLRDRSGIVQVVCDPDADALKlakgLRNEDVVQVKGKVSARPEGN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 83 ENDHLATGKIEIVAQTVTILAKSDALPFQVStalENESEnklpsEDVRLKYRYLDLRRPSMQRNLKLRSNMAKAARHALE 162
Cdd:TIGR00459 82 INRNLDTGEIEILAESITLLNKSKTPPLIIE---KTDAE-----EEVRLKYRYLDLRRPEMQQRLKLRHKVTKAVRNFLD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 163 DMDFTEVETPTFIKSTPEGARDFVVPARLVPGSWYALPQSPQLLKQLLMVSGVERYYQLARCYRDEDFRADRQPEFTQLD 242
Cdd:TIGR00459 154 QQGFLEIETPMLTKSTPEGARDYLVPSRVHKGEFYALPQSPQLFKQLLMVSGVDRYYQIARCFRDEDLRADRQPEFTQID 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 243 MEMSFASQEDVMAMAERVIAAIWKE-AGHEITLPLPRITWQEAMDKYGSDKPDLRFGNPLIELTDFFKNTPFRVFQA--- 318
Cdd:TIGR00459 234 MEMSFMTQEDVMELIEKLVSHVFLEvKGIDLKKPFPVMTYAEAMERYGSDKPDLRFPLELIDVTDLFKDSEFKVFSNlin 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 319 --SYVGAVLFKGGAET-PRRQFDAWQDWAKQRGAKGLAYVVFGEDGeLKGPVAKNLSEEERAGLKEAVGAEDGDAVFFAA 395
Cdd:TIGR00459 314 dgGRVKAIRVPGGWAElSRKSIKELRKFAKEYGAKGLAYLKVNEDG-INSPIKKFLDEKKGKILLERTDAQNGDILLFGA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 396 GSRESSQLLLGAVRVELASRAGLLHPDEFAFTWVVDFPLFKRTddpddddvavGHSKWTSMHHPFTMPSADWIDKFDKDP 475
Cdd:TIGR00459 393 GSKKIVLDALGALRLKLGKDLGLVDPDLFSFLWVVDFPMFEKD----------KEGRLCAAHHPFTMPKDEDLENLEAAP 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 476 EHAMSDSYDIVCNGNEMGGGSVRIHRDDIQDRVLNVLGIDKAEADEKFGFLLEAFKYGAPPHAGIALGWDRTAAILAGAS 555
Cdd:TIGR00459 463 EEALAEAYDLVLNGVELGGGSIRIHDPEVQKKVFEILGIDPEEAREKFGFLLEAFKYGTPPHAGFALGLDRLMMLLTGTD 542
|
570 580 590
....*....|....*....|....*....|....*....
gi 490236703 556 SIRDVIAFPKAGGGRDPLTGAPAPISDEQRAETGVDYDP 594
Cdd:TIGR00459 543 NIRDVIAFPKTTAAACLMTEAPSFIDEKQLEELSIKYVV 581
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
7-587 |
0e+00 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 624.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 7 RTHHAVEVTEELVGQKVTIAGWVDRRRDHGGVAFVDVRDNTGLVQVVIYDEE------TARPLRSEFVVQVTGEVRLRPD 80
Cdd:PLN02903 59 RSHLCGALSVNDVGSRVTLCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDEfpeahrTANRLRNEYVVAVEGTVRSRPQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 81 GNENDHLATGKIEIVAQTVTIL-AKSDALPFQVSTALENESEnklPSEDVRLKYRYLDLRRPSMQRNLKLRSNMAKAARH 159
Cdd:PLN02903 139 ESPNKKMKTGSVEVVAESVDILnVVTKSLPFLVTTADEQKDS---IKEEVRLRYRVLDLRRPQMNANLRLRHRVVKLIRR 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 160 ALEDM-DFTEVETPTFIKSTPEGARDFVVPARLVPGSWYALPQSPQLLKQLLMVSGVERYYQLARCYRDEDFRADRQPEF 238
Cdd:PLN02903 216 YLEDVhGFVEIETPILSRSTPEGARDYLVPSRVQPGTFYALPQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEF 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 239 TQLDMEMSFASQEDVMAMAERVIAAIWKE-AGHEITLPLPRITWQEAMDKYGSDKPDLRFGNPLIELTDFFKNTPFRVFQ 317
Cdd:PLN02903 296 TQLDMELAFTPLEDMLKLNEDLIRQVFKEiKGVQLPNPFPRLTYAEAMSKYGSDKPDLRYGLELVDVSDVFAESSFKVFA 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 318 ASY-----VGAVLFKGGAE----TPRRQFDAWQDwAKQRGAKGLAYVVFGEDGELKGPVA--KNLSEEERAGLKEAVGAE 386
Cdd:PLN02903 376 GALesggvVKAICVPDGKKisnnTALKKGDIYNE-AIKSGAKGLAFLKVLDDGELEGIKAlvESLSPEQAEQLLAACGAG 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 387 DGDAVFFAAGSRESSQLLLGAVRVELASRAGLLHPDEFAFTWVVDFPLFKRTDDpddddvavgHSKWTSMHHPFTMPSAD 466
Cdd:PLN02903 455 PGDLILFAAGPTSSVNKTLDRLRQFIAKTLDLIDPSRHSILWVTDFPMFEWNED---------EQRLEALHHPFTAPNPE 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 467 WIDkfdkDPEHAMSDSYDIVCNGNEMGGGSVRIHRDDIQDRVLNVLGIDKAEADEKFGFLLEAFKYGAPPHAGIALGWDR 546
Cdd:PLN02903 526 DMG----DLSSARALAYDMVYNGVEIGGGSLRIYRRDVQQKVLEAIGLSPEEAESKFGYLLEALDMGAPPHGGIAYGLDR 601
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 490236703 547 TAAILAGASSIRDVIAFPKAGGGRDPLTGAPAPISDEQRAE 587
Cdd:PLN02903 602 LVMLLAGAKSIRDVIAFPKTTTAQCALTRAPSEVDDKQLQD 642
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
19-590 |
3.48e-179 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 523.78 E-value: 3.48e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 19 VGQKVTIAGWVDRRRDHGGVAFVDVRDNTGLVQVVIYDEETAR-------PLRSEFVVQVTGEVRLRPDGNENDHLATGK 91
Cdd:PRK12820 17 TGREVCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFSPEAAPAdvyelaaSLRAEFCVALQGEVQKRLEETENPHIETGD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 92 IEIVAQTVTILAKSDALPFQVS----TALENESENKLPSEDVRLKYRYLDLRRPSMQRNLKLRSNMAKAARHALEDMDFT 167
Cdd:PRK12820 97 IEVFVRELSILAASEALPFAISdkamTAGAGSAGADAVNEDLRLQYRYLDIRRPAMQDHLAKRHRIIKCARDFLDSRGFL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 168 EVETPTFIKSTPEGARDFVVPARLVPGSWYALPQSPQLLKQLLMVSGVERYYQLARCYRDEDFRADRQPEFTQLDMEMSF 247
Cdd:PRK12820 177 EIETPILTKSTPEGARDYLVPSRIHPKEFYALPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEFTQLDIEASF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 248 ASQEDVMAMAERVIAAIWKEAGHEITLPLPRITWQEAMDKYGSDKPDLRFGNPLIELTDFFKNTPFRVFQ-----ASYVG 322
Cdd:PRK12820 257 IDEEFIFELIEELTARMFAIGGIALPRPFPRMPYAEAMDTTGSDRPDLRFDLKFADATDIFENTRYGIFKqilqrGGRIK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 323 AVLFKGGAETPRR---QFDAWQDWAKQRGAKGLAYVVfGEDGELKGPVAKNLSEEERAGLKEAVGAEDGDAVFFAA-GSR 398
Cdd:PRK12820 337 GINIKGQSEKLSKnvlQNEYAKEIAPSFGAKGMTWMR-AEAGGLDSNIVQFFSADEKEALKRRFHAEDGDVIIMIAdASC 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 399 ESSQLLLGAVRVELASRAGLLHPDEFAFTWVVDFPLFKRTDDPDDddvavghskwTSMHHPFTMPsadwiDKFDKDPEHA 478
Cdd:PRK12820 416 AIVLSALGQLRLHLADRLGLIPEGVFHPLWITDFPLFEATDDGGV----------TSSHHPFTAP-----DREDFDPGDI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 479 M------SDSYDIVCNGNEMGGGSVRIHRDDIQDRVLNVLGIDKAEADEKFGFLLEAFKYGAPPHAGIALGWDRTAAILA 552
Cdd:PRK12820 481 EelldlrSRAYDLVVNGEELGGGSIRINDKDIQLRIFAALGLSEEDIEDKFGFFLRAFDFAAPPHGGIALGLDRVVSMIL 560
|
570 580 590
....*....|....*....|....*....|....*...
gi 490236703 553 GASSIRDVIAFPKAGGGRDPLTGAPAPISDEQRAETGV 590
Cdd:PRK12820 561 QTPSIREVIAFPKNRSAACPLTGAPSEVAQEQLAELGL 598
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
147-565 |
3.57e-151 |
|
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: 436.24 E-value: 3.57e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 147 LKLRSNMAKAARHALEDMDFTEVETPTFIKSTPEGARDFVVPARLVPGSWYALPQSPQLLKQLLMVSGVERYYQLARCYR 226
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTPEGARDFLVPSRLHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 227 DEDFRADRQPEFTQLDMEMSFASQEDVMAMAERVIAAIWKEA-GHEITLPLPRITWQEAMDKYGsdkpdlrfgnplielt 305
Cdd:cd00777 81 DEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVlGVELTTPFPRMTYAEAMERYG---------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 306 dffkntpfrvfqasyvgavlfkggaetprrqfdawqdwakqrgakglayvvfgedgelkgpvaknlseeeraglkeavga 385
Cdd:cd00777 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 386 edgdavffaagsressqlllgavrvelasragllhpdeFAFTWVVDFPLFKRTDDpddddvavgHSKWTSMHHPFTMPSA 465
Cdd:cd00777 145 --------------------------------------FKFLWIVDFPLFEWDEE---------EGRLVSAHHPFTAPKE 177
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 466 DWIDKFDKDPEHAMSDSYDIVCNGNEMGGGSVRIHRDDIQDRVLNVLGIDKAEADEKFGFLLEAFKYGAPPHAGIALGWD 545
Cdd:cd00777 178 EDLDLLEKDPEDARAQAYDLVLNGVELGGGSIRIHDPDIQEKVFEILGLSEEEAEEKFGFLLEAFKYGAPPHGGIALGLD 257
|
410 420
....*....|....*....|
gi 490236703 546 RTAAILAGASSIRDVIAFPK 565
Cdd:cd00777 258 RLVMLLTGSESIRDVIAFPK 277
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
126-565 |
2.43e-132 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 389.62 E-value: 2.43e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 126 SEDVRLKYRYLDLRRPSMQRNLKLRSNMAKAARHALEDMDFTEVETPTFIKS-TPEGARDFVVPARLVpGSWYALPQSPQ 204
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSaTPEGARDFLVPSRAL-GKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 205 LLKQLLMVSGVERYYQLARCYRDEDFRADRQPEFTQLDMEMSFASQEDVMAMAERVIAAIWKEAGH-----------EIT 273
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGiakeleggtllDLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 274 LPLPRITWQEAMDK----------YGSDKPDLRFGNPLIeltdffkntpfrvfqasyvgavlfkggaetprrqfdawqdw 343
Cdd:pfam00152 160 KPFPRITYAEAIEKlngkdveelgYGSDKPDLRFLLELV----------------------------------------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 344 akqrgakglayvvfgedgelkgpvaknlseeeraglkeavgaedgdavffaagsressqlllgavrvelasraglLHPDE 423
Cdd:pfam00152 199 ---------------------------------------------------------------------------IDKNK 203
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 424 FAFTWVVDFPlfkrtddpddddvavghskwtSMHHPFTMPSADWIDkfdkdpehAMSDSYDIVCNGNEMGGGSVRIHRDD 503
Cdd:pfam00152 204 FNPLWVTDFP---------------------AEHHPFTMPKDEDDP--------ALAEAFDLVLNGVEIGGGSIRIHDPE 254
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490236703 504 IQDRVLNVLGIDKAEADEKFGFLLEAFKYGAPPHAGIALGWDRTAAILAGASSIRDVIAFPK 565
Cdd:pfam00152 255 LQEERFEEQGLDPEEAEEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAFPK 316
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
6-572 |
3.59e-84 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 269.75 E-value: 3.59e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 6 YRTHHAVEVTEELVGQKVTIAGWVDRRRDHGGVAFVDVRDNTGLVQVVIYDE------ETARPLRSEFVVQVTGEVRlrp 79
Cdd:PRK05159 2 MKRHLTSELTPELDGEEVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKvdeelfETIKKLKRESVVSVTGTVK--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 80 dgnENDHlATGKIEIVAQTVTILAKSDA-LPFQVStaleneseNKLPSE-DVRLKYRYLDLRRPSMQRNLKLRSNMAKAA 157
Cdd:PRK05159 79 ---ANPK-APGGVEVIPEEIEVLNKAEEpLPLDIS--------GKVLAElDTRLDNRFLDLRRPRVRAIFKIRSEVLRAF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 158 RHALEDMDFTEVETPTFIKSTPEGArdfvvpARLVPGSWYA----LPQSPQLLKQLLMVSGVERYYQLARCYRDEDFRAD 233
Cdd:PRK05159 147 REFLYENGFTEIFTPKIVASGTEGG------AELFPIDYFEkeayLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 234 RQ-PEFTQLDMEMSFA-SQEDVMAMAERVIAAIWKEAgheitlplpRITWQEAMDKYGSDKPDLrfgnplieltdffkNT 311
Cdd:PRK05159 221 RHlNEYTSIDVEMGFIdDHEDVMDLLENLLRYMYEDV---------AENCEKELELLGIELPVP--------------ET 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 312 PFrvfqasyvgavlfkggaetPRRQFDAWQDWAKQRGAKglayVVFGEDgelkgpvaknLS-EEERAgLKEAVGAEDGDA 390
Cdd:PRK05159 278 PI-------------------PRITYDEAIEILKSKGNE----ISWGDD----------LDtEGERL-LGEYVKEEYGSD 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 391 VFFaagsressqlllgavrvelasragllhpdefaftwVVDFPLFKRtddpddddvavghskwtsmhhPF-TMPsadwid 469
Cdd:PRK05159 324 FYF-----------------------------------ITDYPSEKR---------------------PFyTMP------ 341
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 470 kFDKDPEhaMSDSYDIVCNGNEMGGGSVRIHRDD-----IQDRVLNVlgidkaeadEKFGFLLEAFKYGAPPHAGIALGW 544
Cdd:PRK05159 342 -DEDDPE--ISKSFDLLFRGLEITSGGQRIHRYDmlvesIKEKGLNP---------ESFEFYLEAFKYGMPPHGGFGLGL 409
|
570 580
....*....|....*....|....*...
gi 490236703 545 DRTAAILAGASSIRDVIAFPkagggRDP 572
Cdd:PRK05159 410 ERLTMKLLGLENIREAVLFP-----RDR 432
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
7-572 |
1.46e-69 |
|
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: 231.09 E-value: 1.46e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 7 RTHHAVEVTEELVGQKVTIAGWVDRRRDHGGVAFVDVRDNTGLVQVVIYDE-----ETARPLRSEFVVQVTGEVRLRPDg 81
Cdd:COG0017 1 KRTYIKDLLPEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDklenfEEAKKLTTESSVEVTGTVVESPR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 82 nendhlATGKIEIVAQTVTILAKSDA-LPFQVSTAlenesenklpSEDVRLKYRYLDLRRPSMQRNLKLRSNMAKAARHA 160
Cdd:COG0017 80 ------APQGVELQAEEIEVLGEADEpYPLQPKRH----------SLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 161 LEDMDFTEVETPTFIKSTPEGARD-FVV-----PArlvpgswYaLPQSPQLLKQlLMVSGVERYYQLARCYRDEDFRADR 234
Cdd:COG0017 144 FQERGFVEVHTPIITASATEGGGElFPVdyfgkEA-------Y-LTQSGQLYKE-ALAMALEKVYTFGPTFRAEKSNTRR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 235 Q-PEFTQLDMEMSFASQEDVMAMAERVIAAIWKeagheitlplpritwqEAMDKYgsdKPDLRFGNPLIELTDFFKNTPF 313
Cdd:COG0017 215 HlAEFWMIEPEMAFADLEDVMDLAEEMLKYIIK----------------YVLENC---PEELEFLGRDVERLEKVPESPF 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 314 rvfqasyvgavlfkggaetPRRQFDAWQDWAKQRGAKglayVVFGEDgelkgpvaknL-SEEERAgLKEAVGaedGDAVF 392
Cdd:COG0017 276 -------------------PRITYTEAIEILKKSGEK----VEWGDD----------LgTEHERY-LGEEFF---KKPVF 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 393 faagsressqlllgavrvelasragllhpdefaftwVVDFPLFKRtddpddddvavghskwtsmhhPF-TMPSADwidkf 471
Cdd:COG0017 319 ------------------------------------VTDYPKEIK---------------------AFyMKPNPD----- 336
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 472 dkDPEhaMSDSYDIVCNG-NEMGGGSVRIHRDDIQDRVLNVLGIDKaeadEKFGFLLEAFKYGAPPHAGIALGWDRTAAI 550
Cdd:COG0017 337 --DPK--TVAAFDLLAPGiGEIIGGSQREHRYDVLVERIKEKGLDP----EDYEWYLDLRRYGSVPHAGFGLGLERLVMW 408
|
570 580
....*....|....*....|..
gi 490236703 551 LAGASSIRDVIAFPkagggRDP 572
Cdd:COG0017 409 LTGLENIREVIPFP-----RDP 425
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
147-565 |
4.76e-69 |
|
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: 224.66 E-value: 4.76e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 147 LKLRSNMAKAARHALEDMDFTEVETPTFIKSTP-EGARDFVVPARlVPGSWYALPQSPQLLKQLLMVSGVERYYQLARCY 225
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGgAGARPFLVKYN-ALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 226 RDEDFRADRQPEFTQLDMEMSFASQEDVMAMAERVIAAIWKEA-GH----------EITLPLPRITWQEAMDKYGsdkpd 294
Cdd:cd00669 80 RNEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVlGVtavtygfeleDFGLPFPRLTYREALERYG----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 295 lrfgnplieltdffkntpfrvfqasyvgavlfkggaetprrqfdawqdwakqrgakglayvvfgedgelkgpvaknlsee 374
Cdd:cd00669 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 375 eraglkeavgaedgdavffaagsressqlllgavrvelasragllhpdefAFTWVVDFPLFkrtddpddddvavghskwt 454
Cdd:cd00669 155 --------------------------------------------------QPLFLTDYPAE------------------- 165
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 455 sMHHPFTMPsadwidkFDKDPEHAmsDSYDIVCNGNEMGGGSVRIHRDDIQDRVLNVLGIDKAEADEKFGFLLEAFKYGA 534
Cdd:cd00669 166 -MHSPLASP-------HDVNPEIA--DAFDLFINGVEVGNGSSRLHDPDIQAEVFQEQGINKEAGMEYFEFYLKALEYGL 235
|
410 420 430
....*....|....*....|....*....|.
gi 490236703 535 PPHAGIALGWDRTAAILAGASSIRDVIAFPK 565
Cdd:cd00669 236 PPHGGLGIGIDRLIMLMTNSPTIREVIAFPK 266
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
7-143 |
2.05e-63 |
|
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: 204.68 E-value: 2.05e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 7 RTHHAVEVTEELVGQKVTIAGWVDRRRDHGGVAFVDVRDNTGLVQVVIYDE-----ETARPLRSEFVVQVTGEVRLRPDG 81
Cdd:cd04317 1 RTHYCGELRESHVGQEVTLCGWVQRRRDHGGLIFIDLRDRYGIVQVVFDPEeapefELAEKLRNESVIQVTGKVRARPEG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490236703 82 NENDHLATGKIEIVAQTVTILAKSDALPFQVSTALENesenklpSEDVRLKYRYLDLRRPSM 143
Cdd:cd04317 81 TVNPKLPTGEIEVVASELEVLNKAKTLPFEIDDDVNV-------SEELRLKYRYLDLRRPKM 135
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
126-572 |
4.60e-37 |
|
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: 140.39 E-value: 4.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 126 SEDVRLKYRYLDLRRPSMQRNLKLRSNMAKAARHALEDMDFTEVETPTFIKSTPEGardfvvPARLVPGSWYA----LPQ 201
Cdd:cd00776 3 NLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEG------GAELFKVSYFGkpayLAQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 202 SPQLLKQlLMVSGVERYYQLARCYRDEDFRADRQ-PEFTQLDMEMSFA-SQEDVMAMAERVIAAIWK----EAGHEItlp 275
Cdd:cd00776 77 SPQLYKE-MLIAALERVYEIGPVFRAEKSNTRRHlSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKrvleRCAKEL--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 276 lpritwqEAMDKYGSDkpdlrfgnplieltDFFKNTPFrvfqasyvgavlfkggaetPRRQFDAWQDWAKQRGAKglAYV 355
Cdd:cd00776 153 -------ELVNQLNRE--------------LLKPLEPF-------------------PRITYDEAIELLREKGVE--EEV 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 356 VFGEDgelkgpvaknLSEEEraglkeavgaedgdavffaagsressQLLLGAvrvelasraglLHPDEFAFtwVVDFPLF 435
Cdd:cd00776 191 KWGED----------LSTEH--------------------------ERLLGE-----------IVKGDPVF--VTDYPKE 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 436 KRtddpddddvavghskwtsmhhPF-TMPSADwidkfdkDPEhaMSDSYD-IVCNGNEMGGGSVRIHRDDIQDRVLNVLG 513
Cdd:cd00776 222 IK---------------------PFyMKPDDD-------NPE--TVESFDlLMPGVGEIVGGSQRIHDYDELEERIKEHG 271
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 490236703 514 IDKaeadEKFGFLLEAFKYGAPPHAGIALGWDRTAAILAGASSIRDVIAFPkagggRDP 572
Cdd:cd00776 272 LDP----ESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP-----RDP 321
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
13-577 |
2.91e-35 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 139.46 E-value: 2.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 13 EVTEELVGQKVTIAGWVDRRRDHGGVAFVDVRDNTGLVQVVIYDEET---------ARPLRSEFVVQVTGEVRLRPDGNE 83
Cdd:PLN02850 74 DLGEELAGSEVLIRGRVHTIRGKGKSAFLVLRQSGFTVQCVVFVSEVtvskgmvkyAKQLSRESVVDVEGVVSVPKKPVK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 84 NdhlATGKIEIVAQTVTILAKSDA-LPFQVSTALENESENKLPSE----------DVRLKYRYLDLRRPSMQRNLKLRSN 152
Cdd:PLN02850 154 G---TTQQVEIQVRKIYCVSKALAtLPFNVEDAARSESEIEKALQtgeqlvrvgqDTRLNNRVLDLRTPANQAIFRIQSQ 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 153 MAKAARHALEDMDFTEVETPTFIKSTPEGARD------FVVPArlvpgswyALPQSPQLLKQLLMVSGVERYYQLARCYR 226
Cdd:PLN02850 231 VCNLFREFLLSKGFVEIHTPKLIAGASEGGSAvfrldyKGQPA--------CLAQSPQLHKQMAICGDFRRVFEIGPVFR 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 227 DEDFRADRQ-PEFTQLDMEMSFASQED-VMAMAERVIAAIWKEAGHEITLPLPRITWQeamdkYGSDkpDLRFGNPLIEL 304
Cdd:PLN02850 303 AEDSFTHRHlCEFTGLDLEMEIKEHYSeVLDVVDELFVAIFDGLNERCKKELEAIREQ-----YPFE--PLKYLPKTLRL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 305 TdffkntpfrvfqasyvgavlFKGGAETPRrqfdawqdwakqrgakglayvvfgEDGELKGPVAKNLSEEERA-G--LKE 381
Cdd:PLN02850 376 T--------------------FAEGIQMLK------------------------EAGVEVDPLGDLNTESERKlGqlVKE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 382 AVGAEdgdavFFaagsressqlllgavrvelasragLLHpdefaftwvvDFPLFKRtddpddddvavghskwtsmhhPF- 460
Cdd:PLN02850 412 KYGTD-----FY------------------------ILH----------RYPLAVR---------------------PFy 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 461 TMPSADwidkfdkDPehAMSDSYDIVCNGNEMGGGSVRIHRDDIQDRVLNVLGIDKaeadEKFGFLLEAFKYGAPPHAGI 540
Cdd:PLN02850 432 TMPCPD-------DP--KYSNSFDVFIRGEEIISGAQRVHDPELLEKRAEECGIDV----KTISTYIDSFRYGAPPHGGF 498
|
570 580 590
....*....|....*....|....*....|....*..
gi 490236703 541 ALGWDRTAAILAGASSIRDVIAFPkagggRDPLTGAP 577
Cdd:PLN02850 499 GVGLERVVMLFCGLNNIRKTSLFP-----RDPQRLAP 530
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
7-564 |
4.23e-28 |
|
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: 117.83 E-value: 4.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 7 RTHHAVEV--------TEELVGQKVTIAGWVDRRRDHGGVAFVDVRDNTGLVQVVIYDEETARPLRSEF-------VVQV 71
Cdd:COG1190 35 RTHTAAEIrekydeleAEEETGDEVSVAGRIMAKRDMGKASFADLQDGSGRIQLYLRRDELGEEAYELFklldlgdIVGV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 72 TGEV-RLRpdgnendhlaTGKIEIVAQTVTILAKSdALPfqvstalenesenkLPS-----EDVRLKYR--YLDL-RRPS 142
Cdd:COG1190 115 EGTVfRTK----------TGELSVKVEELTLLSKS-LRP--------------LPEkfhglTDPETRYRqrYVDLiVNPE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 143 MQRNLKLRSNMAKAARHALEDMDFTEVETPTfIKSTPEGA--RDFVVparlvpgswY--ALPQ------SPQL-LKQLLm 211
Cdd:COG1190 170 VRETFRKRSKIIRAIRRFLDERGFLEVETPM-LQPIAGGAaaRPFIT---------HhnALDMdlylriAPELyLKRLI- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 212 VSGVERYYQLARCYRDEDfrADRQ--PEFTQLDMEMSFASQEDVMAMAERVIAAIWKEAGHEitlplPRITWQEAMdkyg 289
Cdd:COG1190 239 VGGFERVFEIGRNFRNEG--IDTThnPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGT-----TKVTYQGQE---- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 290 sdkpdlrfgnplIELTdffknTPFRVfqASYVGAVLFKGGAE-TPRRQFDAWQDWAKQRGakglayvvfgedgelkgpva 368
Cdd:COG1190 308 ------------IDLS-----PPWRR--ITMVEAIKEATGIDvTPLTDDEELRALAKELG-------------------- 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 369 knLSEEERAGLKEAVgaedgDAVFfaagsressqlllgavrvELASRAGLLHPdefafTWVVDFPLFkrtddpddddvav 448
Cdd:COG1190 349 --IEVDPGWGRGKLI-----DELF------------------EELVEPKLIQP-----TFVTDYPVE------------- 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 449 ghskwTSmhhPFTMPSadwidkfDKDPEhaMSDSYDIVCNGNEMGGG-S----VRIHRDDIQDRVLnvlgiDKA----EA 519
Cdd:COG1190 386 -----VS---PLAKRH-------RDDPG--LTERFELFIAGREIANAfSelndPIDQRERFEEQLE-----LKAagddEA 443
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 490236703 520 ---DEKFgflLEAFKYGAPPHAGIALGWDRTAAILAGASSIRDVIAFP 564
Cdd:COG1190 444 mpmDEDF---LRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 488
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
22-104 |
5.67e-28 |
|
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: 107.27 E-value: 5.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 22 KVTIAGWVDRRRDHGGVAFVDVRDNTGLVQVVIYDE------ETARPLRSEFVVQVTGEVRLRPDGNendhLATGKIEIV 95
Cdd:cd04100 1 EVTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEelgeffEEAEKLRTESVVGVTGTVVKRPEGN----LATGEIELQ 76
|
....*....
gi 490236703 96 AQTVTILAK 104
Cdd:cd04100 77 AEELEVLSK 85
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
1-577 |
3.50e-25 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 109.70 E-value: 3.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 1 MSQTAYRTHHAVEVT----EELVGQKVTIAGWVDRRRDHGGVAFVDVRDNTGLVQVVIYDEETARPLRSEFVVQVTGEVR 76
Cdd:PTZ00401 55 VQSTTYKSRTFIPVAvlskPELVDKTVLIRARVSTTRKKGKMAFMVLRDGSDSVQAMAAVEGDVPKEMIDFIGQIPTESI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 77 LRPDGN----ENDHLATGKIEIVAQTVTILAKSDAL---PFQVSTALENESENKLPSE-DVRLKYRYLDLRRPSMQRNLK 148
Cdd:PTZ00401 135 VDVEATvckvEQPITSTSHSDIELKVKKIHTVTESLrtlPFTLEDASRKESDEGAKVNfDTRLNSRWMDLRTPASGAIFR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 149 LRSNMAKAARHALEDMDFTEVETPTFIKSTPEGARDfVVPARLVPGSWYaLPQSPQLLKQLLMVSGVERYYQLARCYRDE 228
Cdd:PTZ00401 215 LQSRVCQYFRQFLIDSDFCEIHSPKIINAPSEGGAN-VFKLEYFNRFAY-LAQSPQLYKQMVLQGDVPRVFEVGPVFRSE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 229 DFRADRQ-PEFTQLDMEMSFASQ-EDVMAMAERVIAAIWKE-AGHEITL-------PLPRITWQ---EAMDKYG----SD 291
Cdd:PTZ00401 293 NSNTHRHlTEFVGLDVEMRINEHyYEVLDLAESLFNYIFERlATHTKELkavcqqyPFEPLVWKltpERMKELGvgviSE 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 292 KpdlrfgnplIELTDFFK----NTPFRVFQASYVGAVlfkggaetprrqfdawqdwakqrgakglayvvfgedgELKGPV 367
Cdd:PTZ00401 373 G---------VEPTDKYQarvhNMDSRMLRINYMHCI-------------------------------------ELLNTV 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 368 AknlseEERAGLKEAVGAedgdavffaagsreSSQLLLGAVRVElasRAGllhpdefaftwvVDFPLFKRtddpddddva 447
Cdd:PTZ00401 407 L-----EEKMAPTDDINT--------------TNEKLLGKLVKE---RYG------------TDFFISDR---------- 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 448 vghskWTSMHHPF-TMPSADwidkfdkdpEHAMSDSYDIVCNGNEMGGGSVRIHRDDIQDRVLNVLGIDKAEADEkfgfL 526
Cdd:PTZ00401 443 -----FPSSARPFyTMECKD---------DERFTNSYDMFIRGEEISSGAQRIHDPDLLLARAKMLNVDLTPIKE----Y 504
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 490236703 527 LEAFKYGAPPHAGIALGWDRTAAILAGASSIRDVIAFPkagggRDPLTGAP 577
Cdd:PTZ00401 505 VDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFP-----RDPQRTTP 550
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
7-564 |
1.11e-24 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 107.48 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 7 RTHHAVEV--------TEELV--GQKVTIAGWVDRRRDHGGVAFVDVRDNTGLVQVVIYDEETARPLRSEF-------VV 69
Cdd:PRK00484 31 RTHTAAELrakyddkeKEELEelEIEVSVAGRVMLKRVMGKASFATLQDGSGRIQLYVSKDDVGEEALEAFkkldlgdII 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 70 QVTGEV-RLRpdgnendhlaTGKIEIVAQTVTILAKS-DALPfqvstalenESENKLPSEDVRLKYRYLDL-RRPSMQRN 146
Cdd:PRK00484 111 GVEGTLfKTK----------TGELSVKATELTLLTKSlRPLP---------DKFHGLTDVETRYRQRYVDLiVNPESRET 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 147 LKLRSNMAKAARHALEDMDFTEVETPTfIKSTPEG--ARDFV-------VParlvpgsWYaLPQSPQL-LKQLLmVSGVE 216
Cdd:PRK00484 172 FRKRSKIISAIRRFLDNRGFLEVETPM-LQPIAGGaaARPFIthhnaldID-------LY-LRIAPELyLKRLI-VGGFE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 217 RYYQLARCYRDEDfrADRQ--PEFTQLDMEMSFASQEDVMAMAERVIAAIwkeagheitlplpritwqeAMDKYGSDKpd 294
Cdd:PRK00484 242 RVYEIGRNFRNEG--IDTRhnPEFTMLEFYQAYADYNDMMDLTEELIRHL-------------------AQAVLGTTK-- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 295 LRFGNPLIELTdffknTPFRvfQASYVGAVLFKGGAETPRRQFDAWQDWAKQRGAKglayvvfgedgelkgpvaknlsEE 374
Cdd:PRK00484 299 VTYQGTEIDFG-----PPFK--RLTMVDAIKEYTGVDFDDMTDEEARALAKELGIE----------------------VE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 375 ERAGLKEAVgaedgDAVFfaagsressqlllgavrvELASRAGLLHPdefafTWVVDFPlfkrtddpddddVAVghskwt 454
Cdd:PRK00484 350 KSWGLGKLI-----NELF------------------EEFVEPKLIQP-----TFITDYP------------VEI------ 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 455 SmhhPFTMPSadwidkfDKDPEhaMSDSYDIVCNGNEMGGG-SVRIhrDDIQDRVLNVLGIDKAEA--------DEKFgf 525
Cdd:PRK00484 384 S---PLAKRH-------REDPG--LTERFELFIGGREIANAfSELN--DPIDQRERFEAQVEAKEAgddeamfmDEDF-- 447
|
570 580 590
....*....|....*....|....*....|....*....
gi 490236703 526 lLEAFKYGAPPHAGIALGWDRTAAILAGASSIRDVIAFP 564
Cdd:PRK00484 448 -LRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
15-564 |
2.15e-24 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 106.35 E-value: 2.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 15 TEELVGQKVTIAGWVDRRRDHGGVAFVDVRDNTGLVQ-VVIYDE-----ETARPLRSEFVVQVTGEVRLRPDgnendhlA 88
Cdd:PRK03932 11 KGKYVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFKQlQVVKDNgeeyfEEIKKLTTGSSVIVTGTVVESPR-------A 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 89 TGKIEIVAQTVTILAKSDA-LPFQvstaleneseNKLPSEDVRLKYRYLDLRRPSMQRNLKLRSNMAKAARHALEDMDFT 167
Cdd:PRK03932 84 GQGYELQATKIEVIGEDPEdYPIQ----------KKRHSIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 168 EVETPTFIKSTPEGARD-FVVPARLVPGSW-------YaLPQSPQLlkQL-LMVSGVERYYQLARCYRDEDFRADRQ-PE 237
Cdd:PRK03932 154 WVDTPIITASDCEGAGElFRVTTLDLDFSKdffgkeaY-LTVSGQL--YAeAYAMALGKVYTFGPTFRAENSNTRRHlAE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 238 FTQLDMEMSFASQEDVMAMAER----VIAAIWKEAGHEItlplpritwqEAMDKygsdkpdlRFGNPLIELTDFFKNTPF 313
Cdd:PRK03932 231 FWMIEPEMAFADLEDNMDLAEEmlkyVVKYVLENCPDDL----------EFLNR--------RVDKGDIERLENFIESPF 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 314 -RVfqaSYVGAVlfkggaetprrqfdawqDWAKQRGAKGLAYVVFGEDgeLKgpvaknlSEEERAGLKEAVGAedgdAVF 392
Cdd:PRK03932 293 pRI---TYTEAI-----------------EILQKSGKKFEFPVEWGDD--LG-------SEHERYLAEEHFKK----PVF 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 393 faagsressqlllgavrvelasragllhpdefaftwVVDFPL-FKrtddpddddvavghskwtsmhhPFTMPsadwidkf 471
Cdd:PRK03932 340 ------------------------------------VTNYPKdIK----------------------AFYMR-------- 353
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 472 dKDPEH----AMsdsyDIVCNG-NEMGGGSVRIHRDDIQDRVLNVLGIDKaeadEKFGFLLEAFKYGAPPHAGIALGWDR 546
Cdd:PRK03932 354 -LNPDGktvaAM----DLLAPGiGEIIGGSQREERLDVLEARIKELGLNK----EDYWWYLDLRRYGSVPHSGFGLGFER 424
|
570
....*....|....*...
gi 490236703 547 TAAILAGASSIRDVIAFP 564
Cdd:PRK03932 425 LVAYITGLDNIRDVIPFP 442
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
7-264 |
2.06e-23 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 105.43 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 7 RTHHAVEVTEELVGQKVTIAGWVDRRRDHGGVAFVDVRDNTGLVQVVIYDEETARPLRSEF--------VVQVTGEV-RL 77
Cdd:PRK02983 638 PTHTVAEALDAPTGEEVSVSGRVLRIRDYGGVLFADLRDWSGELQVLLDASRLEQGSLADFraavdlgdLVEVTGTMgTS 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 78 RpdgnendhlaTGKIEIVAQTVTILAKS-DALPFQVSTALENESenklpsedvRLKYRYLDLR-RPSMQRNLKLRSNMAK 155
Cdd:PRK02983 718 R----------NGTLSLLVTSWRLAGKClRPLPDKWKGLTDPEA---------RVRQRYLDLAvNPEARDLLRARSAVVR 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 156 AARHALEDMDFTEVETPtfIKSTPEG---ARDFVVPARLVPGSWYaLPQSPQL-LKQLlMVSGVERYYQLARCYRDEDFR 231
Cdd:PRK02983 779 AVRETLVARGFLEVETP--ILQQVHGganARPFVTHINAYDMDLY-LRIAPELyLKRL-CVGGVERVFELGRNFRNEGVD 854
|
250 260 270
....*....|....*....|....*....|....*
gi 490236703 232 ADRQPEFTQLDMEMSFASQEDVMAMAERVI--AAI 264
Cdd:PRK02983 855 ATHNPEFTLLEAYQAHADYDTMRDLTRELIqnAAQ 889
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
9-113 |
1.41e-21 |
|
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: 90.07 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 9 HHAVEVTEELVGQKVTIAGWVDRRRDHGGVAFVDVRDNTGLVQVVIYDE-------ETARPLRSEFVVQVTGEVRLRPDg 81
Cdd:cd04316 1 HYSAEITPELDGEEVTVAGWVHEIRDLGGIKFVILRDREGIVQVTAPKKkvdkelfKTVRKLSRESVISVTGTVKAEPK- 79
|
90 100 110
....*....|....*....|....*....|...
gi 490236703 82 nendhlATGKIEIVAQTVTILAKSDA-LPFQVS 113
Cdd:cd04316 80 ------APNGVEIIPEEIEVLSEAKTpLPLDPT 106
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
23-564 |
7.09e-20 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 93.56 E-value: 7.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 23 VTIAGWVDRRRDHGGVAFVDVRDNTGLVQVVI-----YDEETARPLRSEFVVqvtGEVrLRPDGNENdHLATGKIEIVAQ 97
Cdd:PTZ00385 110 VRVAGRVTSVRDIGKIIFVTIRSNGNELQVVGqvgehFTREDLKKLKVSLRV---GDI-IGADGVPC-RMQRGELSVAAS 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 98 TVTILAKSDALPFQVSTALENESEnkLPSEDVRLKYRYLDL-RRPSMQRNLKLRSNMAKAARHALEDMDFTEVETPTF-I 175
Cdd:PTZ00385 185 RMLILSPYVCTDQVVCPNLRGFTV--LQDNDVKYRYRFTDMmTNPCVIETIKKRHVMLQALRDYFNERNFVEVETPVLhT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 176 KSTPEGARDFVVPARLVPGSWYaLPQSPQLLKQLLMVSGVERYYQLARCYRDEDFRADRQPEFTQLDMEMSFASQEDVMA 255
Cdd:PTZ00385 263 VASGANAKSFVTHHNANAMDLF-LRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTSCEFYAAYHTYEDLMP 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 256 MAERVIAAIWKEAGHEITLPLpritwqeamdkygsdKPDLRFGNPL-IELtdffkNTPFRvfQASYVGAVLFKGGAETPR 334
Cdd:PTZ00385 342 MTEDIFRQLAMRVNGTTVVQI---------------YPENAHGNPVtVDL-----GKPFR--RVSVYDEIQRMSGVEFPP 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 335 RQfdawqdwaKQRGAKGLAY---VVFGEDGELKgPVaknlseeeraglkeavgaedgdavffaagsRESSQLLLGAVRVE 411
Cdd:PTZ00385 400 PN--------ELNTPKGIAYmsvVMLRYNIPLP-PV------------------------------RTAAKMFEKLIDFF 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 412 LASRagLLHPdefafTWVVDFPLFkrtddpdDDDVAVGHSKWTSMHHPFTMpsadwidkFDKDPEHamsdsydivCNG-N 490
Cdd:PTZ00385 441 ITDR--VVEP-----TFVMDHPLF-------MSPLAKEQVSRPGLAERFEL--------FVNGIEY---------CNAyS 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490236703 491 EMGGGSVRIHRddIQDRVLNVLGIDKaEA---DEKFgflLEAFKYGAPPHAGIALGWDRTAAILAGASSIRDVIAFP 564
Cdd:PTZ00385 490 ELNDPHEQYHR--FQQQLVDRQGGDE-EAmplDETF---LKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFP 560
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
9-280 |
1.92e-19 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 91.98 E-value: 1.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 9 HHAVEVTEELVGQKVTIAGWVDRRRDHGGVAFVDVRDNTGLVQvVIYDEETARPLRSEF-----------VVQVTGEVRl 77
Cdd:PLN02502 97 YGSLENGEELEDVSVSVAGRIMAKRAFGKLAFYDLRDDGGKIQ-LYADKKRLDLDEEEFeklhslvdrgdIVGVTGTPG- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 78 RPDgnendhlaTGKIEIVAQTVTILAKS-DALPFQVStalenesenKLPSEDVRLKYRYLDL-RRPSMQRNLKLRSNMAK 155
Cdd:PLN02502 175 KTK--------KGELSIFPTSFEVLTKClLMLPDKYH---------GLTDQETRYRQRYLDLiANPEVRDIFRTRAKIIS 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 156 AARHALEDMDFTEVETPTfIKSTPEG--ARDFV-----VPARLVpgswyaLPQSPQL-LKQLLmVSGVERYYQLARCYRD 227
Cdd:PLN02502 238 YIRRFLDDRGFLEVETPM-LNMIAGGaaARPFVthhndLNMDLY------LRIATELhLKRLV-VGGFERVYEIGRQFRN 309
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490236703 228 EDFRADRQPEFTQLDMEMSFASQEDVMAMAERVIAAIWKEA---------GHEITL--PLPRIT 280
Cdd:PLN02502 310 EGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKELtgsykikyhGIEIDFtpPFRRIS 373
|
|
| GAD |
pfam02938 |
GAD domain; This domain is found in some members of the GatB and aspartyl tRNA synthetases. |
321-400 |
2.38e-18 |
|
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: 80.39 E-value: 2.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 321 VGAVLFKGGAETPRRQFDAWQDWAKQRGAKGLAYVVFGEDGElKGPVAKNLSEEERAGLKEAVGAEDGDAVFFAAGSRES 400
Cdd:pfam02938 11 VKALRVPGAAGLSRKEIDELERFAKEYGAKGLAWIKVEGGGH-TGPIAKFLTEEEVEKLLEAVGAEDGDALLFVADKKKT 89
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
23-102 |
1.18e-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: 74.58 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 23 VTIAGWV-DRRRDHGGVAFVDVRDNTGLVQVVIYDEE---TARPLRSEFVVQVTGEVRLRPdgnendhlaTGKIEIVAQT 98
Cdd:pfam01336 1 VTVAGRVtSIRRSGGKLLFLTLRDGTGSIQVVVFKEEaekLAKKLKEGDVVRVTGKVKKRK---------GGELELVVEE 71
|
....
gi 490236703 99 VTIL 102
Cdd:pfam01336 72 IELL 75
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
142-564 |
2.06e-15 |
|
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: 77.63 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 142 SMQRnLKLRSNMAKAARHALEDMDFTEVETPTfIKSTPEGA--RDFVVPARLVPGSWYaLPQSPQL-LKQLLmVSGVERY 218
Cdd:cd00775 4 VRQT-FIVRSKIISYIRKFLDDRGFLEVETPM-LQPIAGGAaaRPFITHHNALDMDLY-LRIAPELyLKRLI-VGGFERV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 219 YQLARCYRDEDFRADRQPEFTQLDMEMSFASQEDVMAMAERVIAAIwkeagheitlplpritwqeAMDKYGSDKPDlrFG 298
Cdd:cd00775 80 YEIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGL-------------------VKKINGKTKIE--YG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 299 NPLIELTdffknTPFRVfqASYVGAVLFKGGAETPRRQFDAWQDWAKQRGAKGlayVVFGEDGELKGPVAKNLSEEErag 378
Cdd:cd00775 139 GKELDFT-----PPFKR--VTMVDALKEKTGIDFPELDLEQPEELAKLLAKLI---KEKIEKPRTLGKLLDKLFEEF--- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 379 lkeavgaedgdavffaagsressqlllgavrVElasrAGLLHPdefafTWVVDFP-----LFKRtddpddddvavghskw 453
Cdd:cd00775 206 -------------------------------VE----PTLIQP-----TFIIDHPveispLAKR---------------- 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 454 tsmhHPftmpsadwidkfdKDPEhaMSDSYDIVCNGNEMGGGSVRIhrDDIQDR--------VLNVLGIDKA-EADEKFg 524
Cdd:cd00775 230 ----HR-------------SNPG--LTERFELFICGKEIANAYTEL--NDPFDQrerfeeqaKQKEAGDDEAmMMDEDF- 287
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 490236703 525 flLEAFKYGAPPHAGIALGWDRTAAILAGASSIRDVIAFP 564
Cdd:cd00775 288 --VTALEYGMPPTGGLGIGIDRLVMLLTDSNSIRDVILFP 325
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
22-564 |
1.37e-13 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 73.56 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 22 KVTIAGWVDRRRDHGGVAFVDVRDNTGLVQVVIYDEETARPLRSE-FVVQVTGEVrLRPDGNENDhLATGKIEIVAQTVT 100
Cdd:PRK12445 67 EVSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEGVYNDqFKKWDLGDI-IGARGTLFK-TQTGELSIHCTELR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 101 ILAKS-DALPfqvstalenESENKLPSEDVRLKYRYLDLRRPSMQRN-LKLRSNMAKAARHALEDMDFTEVETPtFIKST 178
Cdd:PRK12445 145 LLTKAlRPLP---------DKFHGLQDQEVRYRQRYLDLIANDKSRQtFVVRSKILAAIRQFMVARGFMEVETP-MMQVI 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 179 PEGA--RDFVVPARLVPGSWYaLPQSPQLLKQLLMVSGVERYYQLARCYRDEDFRADRQPEFTQLDMEMSFASQEDVMAM 256
Cdd:PRK12445 215 PGGAsaRPFITHHNALDLDMY-LRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIEL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 257 AERVIAAIWKEAGHEITLPlpritwqeamdkYGSDKPDlrFGNPLIELTdffkntpfrvfqasyVGAVLFKGGAETPRRQ 336
Cdd:PRK12445 294 TESLFRTLAQEVLGTTKVT------------YGEHVFD--FGKPFEKLT---------------MREAIKKYRPETDMAD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 337 FDAWQdwakqrGAKGLAYVVfgedgelkgpvakNLSEEERAGLKEAVgAEDGDAVffaagsressqlllgavrvelaSRA 416
Cdd:PRK12445 345 LDNFD------AAKALAESI-------------GITVEKSWGLGRIV-TEIFDEV----------------------AEA 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 417 GLLHPdefafTWVVDFPlfkrtddpddddvavghskwtsmhhpftMPSADWIDKFDKDPEhaMSDSYDIVCNGNEMGGGS 496
Cdd:PRK12445 383 HLIQP-----TFITEYP----------------------------AEVSPLARRNDVNPE--ITDRFEFFIGGREIGNGF 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490236703 497 VRIHRDDIQDRVLNVLGIDKAEADEKFGFLLE----AFKYGAPPHAGIALGWDRTAAILAGASSIRDVIAFP 564
Cdd:PRK12445 428 SELNDAEDQAERFQEQVNAKAAGDDEAMFYDEdyvtALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
22-104 |
4.22e-11 |
|
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: 59.17 E-value: 4.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 22 KVTIAGWVDRRRDHGGVAFVDVRDNTGLVQVVIYDEETARP-----LRSEFVVQVTGEVRLRPDGNEndhlATGKIEIVA 96
Cdd:cd04323 1 RVKVFGWVHRLRSQKKLMFLVLRDGTGFLQCVLSKKLVTEFydaksLTQESSVEVTGEVKEDPRAKQ----APGGYELQV 76
|
....*...
gi 490236703 97 QTVTILAK 104
Cdd:cd04323 77 DYLEIIGE 84
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
149-272 |
5.58e-11 |
|
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: 62.52 E-value: 5.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 149 LRSNMAKAARHALEDMDFTEVETPTFIKSTPEGARDFVVPARLVPGSW----YALPQSPQLLKQLLMVSGV----ERYYQ 220
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHEPKDLLPVGAEneedLYLRPTLEPGLVRLFVSHIrklpLRLAE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 490236703 221 LARCYRDEDFRAD--RQPEFTQLDMEMSFASQEDVMAMAE--RVIAAIWKEAGHEI 272
Cdd:cd00768 81 IGPAFRNEGGRRGlrRVREFTQLEGEVFGEDGEEASEFEEliELTEELLRALGIKL 136
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
120-306 |
2.98e-10 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 61.96 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 120 SENKLPSEDVRLKYRYLDLRRPSMQRNLKLRSNMAKAARHALEDMDFTEVETPTFIKST----PEGARDFVVPARL-VPG 194
Cdd:PRK06462 3 LERYPKEYEEFLRMSWKHISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIISPSTdplmGLGSDLPVKQISIdFYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 195 SWYALPQSPQLLKQLlMVSGVERYYQLARCYRDEDFRADRQP---EFTQLDMEMSFASQEDVMAMAERVIAAIWKEA--- 268
Cdd:PRK06462 83 VEYYLADSMILHKQL-ALRMLGKIFYLSPNFRLEPVDKDTGRhlyEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELlee 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490236703 269 -GHEI----------TLPLPRITWQEAMDKYGSDKPDlrfGNPLIELTD 306
Cdd:PRK06462 162 hEDELeffgrdlphlKRPFKRITHKEAVEILNEEGCR---GIDLEELGS 207
|
|
| ScAspRS_mt_like_N |
cd04321 |
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
22-102 |
4.63e-10 |
|
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: 56.17 E-value: 4.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 22 KVTIAGWVDRRRD-HGGVAFVDVRDNTG-LVQVVIYDEETA----RPLRSEFVVQVTGEVRLRPdgnENDHLATGKIEIV 95
Cdd:cd04321 1 KVTLNGWIDRKPRiVKKLSFADLRDPNGdIIQLVSTAKKDAfsllKSITAESPVQVRGKLQLKE---AKSSEKNDEWELV 77
|
....*..
gi 490236703 96 AQTVTIL 102
Cdd:cd04321 78 VDDIQTL 84
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
124-300 |
3.73e-09 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 59.64 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 124 LPSEDVRLKYRYLDLR-RPSMQRNLKLRSNMAKAARHALEDMDFTEVETPTF-IKSTPEGARDFVVPARLVPGSWYaLPQ 201
Cdd:PTZ00417 229 LKDTEIRYRQRYLDLMiNESTRSTFITRTKIINYLRNFLNDRGFIEVETPTMnLVAGGANARPFITHHNDLDLDLY-LRI 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 202 SPQLLKQLLMVSGVERYYQLARCYRDEDFRADRQPEFTQLDMEMSFASQEDVMAMAERVIAAI-----------WKEAGH 270
Cdd:PTZ00417 308 ATELPLKMLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLvmhlfgtykilYNKDGP 387
|
170 180 190
....*....|....*....|....*....|....*..
gi 490236703 271 E-------ITLPLPRITWQEAMDKYGSDKPDLRFGNP 300
Cdd:PTZ00417 388 EkdpieidFTPPYPKVSIVEELEKLTNTKLEQPFDSP 424
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
19-568 |
9.61e-09 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 58.06 E-value: 9.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 19 VGQKVTIAGWVDRRRDHGGVAFVDVRDNTGL--VQVVI------YDEETARPLRSEFVVQVTGEVRLRPDGNEndhlatg 90
Cdd:PLN02603 106 VGKTLNVMGWVRTLRAQSSVTFIEVNDGSCLsnMQCVMtpdaegYDQVESGLITTGASVLVQGTVVSSQGGKQ------- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 91 KIEIVAQTVTILAKSD-ALPFQvstalenesENKLPSEDVRLKyRYLDLRRPSMQRNLKLRSNMAKAARHALEDMDFTEV 169
Cdd:PLN02603 179 KVELKVSKIVVVGKSDpSYPIQ---------KKRVSREFLRTK-AHLRPRTNTFGAVARVRNALAYATHKFFQENGFVWV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 170 ETPTFIKSTPEGARDFVVPARLVPGSWYA-------LPQSPQLL----------KQLLMVSG---VERY-------YQLA 222
Cdd:PLN02603 249 SSPIITASDCEGAGEQFCVTTLIPNSAENggslvddIPKTKDGLidwsqdffgkPAFLTVSGqlnGETYatalsdvYTFG 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 223 RCYRDEDFRADRQ-PEFTQLDMEMSFASQEDVMAMAERVIAAIWKEAGHEItlplpritwqeamdkygsdKPDLRFGNPL 301
Cdd:PLN02603 329 PTFRAENSNTSRHlAEFWMIEPELAFADLNDDMACATAYLQYVVKYILENC-------------------KEDMEFFNTW 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 302 IE--LTDFFKNTPFRVF-QASYVGAVLFKGGAetpRRQFDAWQDWakqrgakglayvvfGEDGElkgpvaknlSEEERAG 378
Cdd:PLN02603 390 IEkgIIDRLSDVVEKNFvQLSYTDAIELLLKA---KKKFEFPVKW--------------GLDLQ---------SEHERYI 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 379 LKEAVGaedGDAVFfaagsressqlllgavrvelasragllhpdefaftwVVDFPLFKRTddpddddvavghskwtsmhh 458
Cdd:PLN02603 444 TEEAFG---GRPVI------------------------------------IRDYPKEIKA-------------------- 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 459 pFTMPSADwidkfDKDPEHAMSDsydIVCNGNEMGGGSVRIHRDDIQDRVLNVLGIDKaeadEKFGFLLEAFKYGAPPHA 538
Cdd:PLN02603 465 -FYMREND-----DGKTVAAMDM---LVPRVGELIGGSQREERLEYLEARLDELKLNK----ESYWWYLDLRRYGSVPHA 531
|
570 580 590
....*....|....*....|....*....|
gi 490236703 539 GIALGWDRTAAILAGASSIRDVIAFPKAGG 568
Cdd:PLN02603 532 GFGLGFERLVQFATGIDNIRDAIPFPRVPG 561
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
22-138 |
1.07e-08 |
|
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: 53.25 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 22 KVTIAGWVDRRRDHGGVAFVDVRDNTGLVQVVI----YDEETARPLRSEF----VVQVTGEVRLRPdgnendhlaTGKIE 93
Cdd:cd04322 1 EVSVAGRIMSKRGSGKLSFADLQDESGKIQVYVnkddLGEEEFEDFKKLLdlgdIIGVTGTPFKTK---------TGELS 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 490236703 94 IVAQTVTILAKSdaLpfqvstaleneseNKLPS-----EDVRLKYR--YLDL 138
Cdd:cd04322 72 IFVKEFTLLSKS--L-------------RPLPEkfhglTDVETRYRqrYLDL 108
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
22-136 |
1.11e-08 |
|
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: 52.91 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 22 KVTIAGWVDRRRDHGGVAFVDVRDNTGLVQVVI---YDEET---ARPLRSEFVVQVTGEVRLRPDgnendhlATGKIEIV 95
Cdd:cd04319 1 KVTLAGWVYRKREVGKKAFIVLRDSTGIVQAVFskdLNEEAyreAKKVGIESSVIVEGAVKADPR-------APGGAEVH 73
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 490236703 96 AQTVTILAKSDALPFqvstaleneseNKLPSEDVRLKYRYL 136
Cdd:cd04319 74 GEKLEIIQNVEFFPI-----------TEDASDEFLLDVRHL 103
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
165-288 |
1.87e-07 |
|
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous to the C-terminal region of lysyl-tRNA synthetase (LysS). Multiple sequence alignment of these proteins with the homologous regions of collected LysS proteins shows that these proteins form a distinct set rather than just similar truncations of LysS. The protein is termed GenX after its designation in E. coli. Interestingly, genX often is located near a homolog of lysine-2,3-aminomutase. Its function is unknown. [Unknown function, General]
Pssm-ID: 273090 [Multi-domain] Cd Length: 290 Bit Score: 52.94 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 165 DFTEVETPTFIKSTPEGARDFVVPARLVPGS-----WYaLPQSPQL-LKQLLmVSGVERYYQLARCYRDEDFRADRQPEF 238
Cdd:TIGR00462 6 GVLEVETPLLSPAPVTDPHLDAFATEFVGPDgqgrpLY-LQTSPEYaMKRLL-AAGSGPIFQICKVFRNGERGRRHNPEF 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 490236703 239 TQLDMEMSFASQEDVMAMAERVIAaiwkEAGHEITLPLPRITWQEAMDKY 288
Cdd:TIGR00462 84 TMLEWYRPGFDYHDLMDEVEALLQ----ELLGDPFAPAERLSYQEAFLRY 129
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
22-104 |
9.66e-07 |
|
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: 46.79 E-value: 9.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 22 KVTIAGWVDRRRDHGGVAFVDVRDNTGL--VQVVIYDEETARPLRSEF----VVQVTGEVRLRPDGNEndhlatgKIEIV 95
Cdd:cd04318 1 EVTVNGWVRSVRDSKKISFIELNDGSCLknLQVVVDKELTNFKEILKLstgsSIRVEGVLVKSPGAKQ-------PFELQ 73
|
....*....
gi 490236703 96 AQTVTILAK 104
Cdd:cd04318 74 AEKIEVLGE 82
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
491-571 |
2.04e-05 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 47.30 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 491 EMGGGSVRIHRDDIQDRVLNVLGIDKaeadEKFGFLLEAFKYGAPPHAGIALGWDRTAAILAGASSIRDVIAFPKAGGGR 570
Cdd:PLN02221 495 ELIGGSQREERYDVIKQRIEEMGLPI----EPYEWYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPRYPGKA 570
|
.
gi 490236703 571 D 571
Cdd:PLN02221 571 D 571
|
|
| GatE |
COG2511 |
Archaeal Glu-tRNAGln amidotransferase subunit E, contains GAD domain [Translation, ribosomal ... |
302-413 |
3.30e-05 |
|
Archaeal Glu-tRNAGln amidotransferase subunit E, contains GAD domain [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442001 [Multi-domain] Cd Length: 630 Bit Score: 46.71 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 302 IELTDFFKNTPFRVFQASY-----VGAVLFKG-----GAE-TPRRQFDA-WQDWAKQRGAKGLayvvFGEDgELkgPvAK 369
Cdd:COG2511 283 VDVTDVFKDTKSKVIKKALkkggkVLAVKLPGfagllGREiQPGRRLGTeLADYAKFWGVGGI----FHTD-EL--P-NY 354
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 490236703 370 NLSEEERAGLKEAVGAEDGDAVFFAAGSRESSQLLLGAV--RVELA 413
Cdd:COG2511 355 GITEEEVEALREALGAGEEDAFVIVADEEEKAKKALEAVieRAKEA 400
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
491-568 |
3.39e-05 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 46.94 E-value: 3.39e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490236703 491 EMGGGSvriHRDDIQDRvLNVLGIDKAEADEKFGFLLEAFKYGAPPHAGIALGWDRTAAILAGASSIRDVIAFPKAGG 568
Cdd:PTZ00425 509 EVIGGS---QREDNLER-LDKMIKEKKLNMESYWWYRQLRKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFPRYPG 582
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
18-182 |
7.13e-05 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 45.76 E-value: 7.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 18 LVGQKVTIAGWVDRRRDHG--GVAFVDVRDNT--GLVQVVIYD--EETARPLRSEFVVQVTGEVRLRPDGNENDHlatgK 91
Cdd:PLN02221 48 LAGQKVRIGGWVKTGREQGkgTFAFLEVNDGScpANLQVMVDSslYDLSTLVATGTCVTVDGVLKVPPEGKGTKQ----K 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 92 IEIVAQTVTILAKSDALPFQVstaleneSENKLPSEDVRlKYRYLDLRRPSMQRNLKLRSNMAKAARHALEDMDFTEVET 171
Cdd:PLN02221 124 IELSVEKVIDVGTVDPTKYPL-------PKTKLTLEFLR-DVLHLRSRTNSISAVARIRNALAFATHSFFQEHSFLYIHT 195
|
170
....*....|.
gi 490236703 172 PTFIKSTPEGA 182
Cdd:PLN02221 196 PIITTSDCEGA 206
|
|
| PRK04028 |
PRK04028 |
Glu-tRNA(Gln) amidotransferase subunit GatE; |
298-413 |
7.32e-04 |
|
Glu-tRNA(Gln) amidotransferase subunit GatE;
Pssm-ID: 235205 [Multi-domain] Cd Length: 630 Bit Score: 42.50 E-value: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 298 GNPLIELTDFFKNTPFRVFQASY-----VGAVLFKG-----GAET-PRRQFDA-WQDWAKQRGAKGLayvvFGEDgELkg 365
Cdd:PRK04028 278 EDEIVDVTELFKDTKSKIIKKALkkggkVLAIKLPGfkgllGREIqPGRRLGTeLADYAKAWGVGGI----FHTD-EL-- 350
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 490236703 366 PvAKNLSEEERAGLKEAVGAEDGDAVFFAAGSRESSQLLLGAV--RVELA 413
Cdd:PRK04028 351 P-AYGITEEEVEALREALGAGENDAFILVADEEEKAEKALEAVieRAKEA 399
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
525-560 |
1.16e-03 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 41.45 E-value: 1.16e-03
10 20 30
....*....|....*....|....*....|....*.
gi 490236703 525 FLLEAFKYGAPPHAGIALGWDRTAAILAGASSIRDV 560
Cdd:PRK09350 271 NLIAALEAGLPDCSGVALGVDRLIMLALGAESISEV 306
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
22-112 |
6.81e-03 |
|
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: 36.39 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490236703 22 KVTIAGWVDRRRDHGG-VAFVDVRDNTGLVQVVIYDEET---------ARPLRSEFVVQVTGEVRLRPdgNENDHLATGK 91
Cdd:cd04320 1 EVLIRARVHTSRAQGAkLAFLVLRQQGYTIQGVLAASAEgvskqmvkwAGSLSKESIVDVEGTVKKPE--EPIKSCTQQD 78
|
90 100
....*....|....*....|..
gi 490236703 92 IEIVAQTVTILAKSDA-LPFQV 112
Cdd:cd04320 79 VELHIEKIYVVSEAAEpLPFQL 100
|
|
| |
