|
Name |
Accession |
Description |
Interval |
E-value |
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
10-610 |
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: 934.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 10 RTHTCGELRAAHAGETITIMGWVNRRRDHGNLIFLDLRDRYGITQVVLDKDLSAEAHAKAEQARPEYVICATGKVRARSQ 89
Cdd:COG0173 3 RTHYCGELRESDVGQEVTLSGWVHRRRDHGGLIFIDLRDRYGITQVVFDPDDSAEAFEKAEKLRSEYVIAVTGKVRARPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 90 EAINPKMPTGEIEIAATELLILNDSKVPPFSPAEEAIANEEVRLKYRYLDLRRPEMQHNFEVRHKVALAVRQYLSGQGFF 169
Cdd:COG0173 83 GTVNPKLPTGEIEVLASELEILNKAKTPPFQIDDDTDVSEELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDENGFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 170 EVETPFMTRSTPEGARDYLVPSRVHPGEFYALPQSPQLFKQILMISGMDRYFQIARCFRDEDLRADRQPEFTQIDLEMTF 249
Cdd:COG0173 163 EIETPILTKSTPEGARDYLVPSRVHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFRDEDLRADRQPEFTQLDIEMSF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 250 PQQETIFGVVEGFLAAAFEAV-GQQITVPFPRMTYDKAIELYGIDKPDLRLP-PMTDVRSVFSDEELQSLK--IEPGMPI 325
Cdd:COG0173 243 VDQEDVFELMEGLIRHLFKEVlGVELPTPFPRMTYAEAMERYGSDKPDLRFGlELVDVTDIFKDSGFKVFAgaAENGGRV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 326 VAIVIPNKSAMSNTQKKAFGKEVeEQVGAE-LAYLDV--ERLRtSPqfalLADRIdaaaaahcklervePDHRLVVISPR 402
Cdd:COG0173 323 KAINVPGGASLSRKQIDELTEFA-KQYGAKgLAYIKVneDGLK-SP----IAKFL--------------SEEELAAILER 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 403 LGAAA------VSRDTSWVYKRAGQLRLELGKRFaaehKAFEKKgtaaDYQFLWVTDFPFFEWDEQSHTWTFAHHPFTSP 476
Cdd:COG0173 383 LGAKPgdliffVADKPKVVNKALGALRLKLGKEL----GLIDED----EFAFLWVVDFPLFEYDEEEGRWVAMHHPFTMP 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 477 HQDDLiaGRLESDQAAVRALAYDVVLNGTELGSGSIRIHRQDVQQQIFRALGMSDDEAKERFGFFLEALQYGTPPHGGIA 556
Cdd:COG0173 455 KDEDL--DLLETDPGKVRAKAYDLVLNGYELGGGSIRIHDPELQEKVFELLGISEEEAEEKFGFLLEAFKYGAPPHGGIA 532
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 254781707 557 LGLDRIVMILAGASSLREVIAFPKTAKAIDLMVDAPTPVSDAQLRELHIRPTKQ 610
Cdd:COG0173 533 FGLDRLVMLLAGEDSIRDVIAFPKTQSAQDLMTGAPSEVDEKQLKELHIRLRPP 586
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
10-610 |
0e+00 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 921.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 10 RTHTCGELRAAHAGETITIMGWVNRRRDHGNLIFLDLRDRYGITQVVLDKDlsAEAHAKAEQARPEYVICATGKVRARSQ 89
Cdd:PRK00476 4 RTHYCGELRESHVGQTVTLCGWVHRRRDHGGLIFIDLRDREGIVQVVFDPD--AEAFEVAESLRSEYVIQVTGTVRARPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 90 EAINPKMPTGEIEIAATELLILNDSKVPPFSPAEEAIANEEVRLKYRYLDLRRPEMQHNFEVRHKVALAVRQYLSGQGFF 169
Cdd:PRK00476 82 GTVNPNLPTGEIEVLASELEVLNKSKTLPFPIDDEEDVSEELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDDNGFL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 170 EVETPFMTRSTPEGARDYLVPSRVHPGEFYALPQSPQLFKQILMISGMDRYFQIARCFRDEDLRADRQPEFTQIDLEMTF 249
Cdd:PRK00476 162 EIETPILTKSTPEGARDYLVPSRVHPGKFYALPQSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADRQPEFTQIDIEMSF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 250 PQQETIFGVVEGFLAAAFEAV-GQQITVPFPRMTYDKAIELYGIDKPDLRLP-PMTDVRSVFSDEELQSLK--IEPGMPI 325
Cdd:PRK00476 242 VTQEDVMALMEGLIRHVFKEVlGVDLPTPFPRMTYAEAMRRYGSDKPDLRFGlELVDVTDLFKDSGFKVFAgaANDGGRV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 326 VAIVIPNKSA-MSNTQKKAFGKEVeEQVGAE-LAYLDV-ERLRTSP--------QFALLADRIDaaaaahcklerVEPDH 394
Cdd:PRK00476 322 KAIRVPGGAAqLSRKQIDELTEFA-KIYGAKgLAYIKVnEDGLKGPiakflseeELAALLERTG-----------AKDGD 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 395 RLVVISprlGAAAVsrdtswVYKRAGQLRLELGKRFaaehKAFEKKgtaaDYQFLWVTDFPFFEWDEQSHTWTFAHHPFT 474
Cdd:PRK00476 390 LIFFGA---DKAKV------VNDALGALRLKLGKEL----GLIDED----KFAFLWVVDFPMFEYDEEEGRWVAAHHPFT 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 475 SPHQDDLIAgRLESDQAAVRALAYDVVLNGTELGSGSIRIHRQDVQQQIFRALGMSDDEAKERFGFFLEALQYGTPPHGG 554
Cdd:PRK00476 453 MPKDEDLDE-LETTDPGKARAYAYDLVLNGYELGGGSIRIHRPEIQEKVFEILGISEEEAEEKFGFLLDALKYGAPPHGG 531
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 254781707 555 IALGLDRIVMILAGASSLREVIAFPKTAKAIDLMVDAPTPVSDAQLRELHIRPTKQ 610
Cdd:PRK00476 532 IAFGLDRLVMLLAGADSIRDVIAFPKTQSAQDLLTGAPSPVDEKQLRELGIRLRKK 587
|
|
| aspS_bact |
TIGR00459 |
aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be ... |
10-606 |
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: 680.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 10 RTHTCGELRAAHAGETITIMGWVNRRRDHGNLIFLDLRDRYGITQVVLDKDlsAEAHAKAEQARPEYVICATGKVRARSQ 89
Cdd:TIGR00459 2 RTHYCGQLRTEHLGQTVTLAGWVNRRRDLGGLIFIDLRDRSGIVQVVCDPD--ADALKLAKGLRNEDVVQVKGKVSARPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 90 EAINPKMPTGEIEIAATELLILNDSKVPPFSpAEEAIANEEVRLKYRYLDLRRPEMQHNFEVRHKVALAVRQYLSGQGFF 169
Cdd:TIGR00459 80 GNINRNLDTGEIEILAESITLLNKSKTPPLI-IEKTDAEEEVRLKYRYLDLRRPEMQQRLKLRHKVTKAVRNFLDQQGFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 170 EVETPFMTRSTPEGARDYLVPSRVHPGEFYALPQSPQLFKQILMISGMDRYFQIARCFRDEDLRADRQPEFTQIDLEMTF 249
Cdd:TIGR00459 159 EIETPMLTKSTPEGARDYLVPSRVHKGEFYALPQSPQLFKQLLMVSGVDRYYQIARCFRDEDLRADRQPEFTQIDMEMSF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 250 PQQETIFGVVEGFLAAAFEAV-GQQITVPFPRMTYDKAIELYGIDKPDLRLP-PMTDVRSVFSDEELQ--SLKIEPGMPI 325
Cdd:TIGR00459 239 MTQEDVMELIEKLVSHVFLEVkGIDLKKPFPVMTYAEAMERYGSDKPDLRFPlELIDVTDLFKDSEFKvfSNLINDGGRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 326 VAIVIPNKSA-MSNTQKKAFGKEVEEQVGAELAYLDVERLRTSpqfALLADRIDAAAAAHCKLERVEPDHRLVVIsprlg 404
Cdd:TIGR00459 319 KAIRVPGGWAeLSRKSIKELRKFAKEYGAKGLAYLKVNEDGIN---SPIKKFLDEKKGKILLERTDAQNGDILLF----- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 405 aAAVSRDTSWVYkrAGQLRLELGKrfaaeHKAFEKKGTaadYQFLWVTDFPFFEWDEQSHtWTFAHHPFTSPHQDDLiaG 484
Cdd:TIGR00459 391 -GAGSKKIVLDA--LGALRLKLGK-----DLGLVDPDL---FSFLWVVDFPMFEKDKEGR-LCAAHHPFTMPKDEDL--E 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 485 RLESDQAAVRALAYDVVLNGTELGSGSIRIHRQDVQQQIFRALGMSDDEAKERFGFFLEALQYGTPPHGGIALGLDRIVM 564
Cdd:TIGR00459 457 NLEAAPEEALAEAYDLVLNGVELGGGSIRIHDPEVQKKVFEILGIDPEEAREKFGFLLEAFKYGTPPHAGFALGLDRLMM 536
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 254781707 565 ILAGASSLREVIAFPKTAKAIDLMVDAPTPVSDAQLRELHIR 606
Cdd:TIGR00459 537 LLTGTDNIRDVIAFPKTTAAACLMTEAPSFIDEKQLEELSIK 578
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
10-610 |
0e+00 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 624.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 10 RTHTCGELRAAHAGETITIMGWVNRRRDHGNLIFLDLRDRYGITQVVLDKDLSAEAHAKAEQARPEYVICATGKVRARSQ 89
Cdd:PLN02903 59 RSHLCGALSVNDVGSRVTLCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDEFPEAHRTANRLRNEYVVAVEGTVRSRPQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 90 EAINPKMPTGEIEIAATELLILNDSKVP-PF--SPAEEA--IANEEVRLKYRYLDLRRPEMQHNFEVRHKVALAVRQYLS 164
Cdd:PLN02903 139 ESPNKKMKTGSVEVVAESVDILNVVTKSlPFlvTTADEQkdSIKEEVRLRYRVLDLRRPQMNANLRLRHRVVKLIRRYLE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 165 G-QGFFEVETPFMTRSTPEGARDYLVPSRVHPGEFYALPQSPQLFKQILMISGMDRYFQIARCFRDEDLRADRQPEFTQI 243
Cdd:PLN02903 219 DvHGFVEIETPILSRSTPEGARDYLVPSRVQPGTFYALPQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEFTQL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 244 DLEMTFPQQETIFGVVEGFLAAAF-EAVGQQITVPFPRMTYDKAIELYGIDKPDLRLP-PMTDVRSVFSDEELQ--SLKI 319
Cdd:PLN02903 299 DMELAFTPLEDMLKLNEDLIRQVFkEIKGVQLPNPFPRLTYAEAMSKYGSDKPDLRYGlELVDVSDVFAESSFKvfAGAL 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 320 EPGMPIVAIVIPNKSAMSNTQKKAFGKEVEEQV--GAE-LAYLDVerlrtspqfalLAD-RIDAAAAAhckLERVEPDHR 395
Cdd:PLN02903 379 ESGGVVKAICVPDGKKISNNTALKKGDIYNEAIksGAKgLAFLKV-----------LDDgELEGIKAL---VESLSPEQA 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 396 LVVISpRLGAAA------VSRDTSWVYKRAGQLRLelgkrFAAEHKAFEKKGtaaDYQFLWVTDFPFFEWDEQSHTWTFA 469
Cdd:PLN02903 445 EQLLA-ACGAGPgdlilfAAGPTSSVNKTLDRLRQ-----FIAKTLDLIDPS---RHSILWVTDFPMFEWNEDEQRLEAL 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 470 HHPFTSPHQDDLiagrleSDQAAVRALAYDVVLNGTELGSGSIRIHRQDVQQQIFRALGMSDDEAKERFGFFLEALQYGT 549
Cdd:PLN02903 516 HHPFTAPNPEDM------GDLSSARALAYDMVYNGVEIGGGSLRIYRRDVQQKVLEAIGLSPEEAESKFGYLLEALDMGA 589
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254781707 550 PPHGGIALGLDRIVMILAGASSLREVIAFPKTAKAIDLMVDAPTPVSDAQLRELHIRPTKQ 610
Cdd:PLN02903 590 PPHGGIAYGLDRLVMLLAGAKSIRDVIAFPKTTTAQCALTRAPSEVDDKQLQDLSIASTAP 650
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
14-603 |
1.00e-171 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 504.91 E-value: 1.00e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 14 CGELRAAHAGETITIMGWVNRRRDHGNLIFLDLRDRYGITQVVLDKD-LSAEAHAKAEQARPEYVICATGKVRARSQEAI 92
Cdd:PRK12820 9 CGHLSLDDTGREVCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFSPEaAPADVYELAASLRAEFCVALQGEVQKRLEETE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 93 NPKMPTGEIEIAATELLILNDSKVPPFSPAEEAIA-----------NEEVRLKYRYLDLRRPEMQHNFEVRHKVALAVRQ 161
Cdd:PRK12820 89 NPHIETGDIEVFVRELSILAASEALPFAISDKAMTagagsagadavNEDLRLQYRYLDIRRPAMQDHLAKRHRIIKCARD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 162 YLSGQGFFEVETPFMTRSTPEGARDYLVPSRVHPGEFYALPQSPQLFKQILMISGMDRYFQIARCFRDEDLRADRQPEFT 241
Cdd:PRK12820 169 FLDSRGFLEIETPILTKSTPEGARDYLVPSRIHPKEFYALPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEFT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 242 QIDLEMTFPQQETIFGVVEGFLAAAFEAVGQQITVPFPRMTYDKAIELYGIDKPDLRLP-PMTDVRSVFSDEELQSLK-- 318
Cdd:PRK12820 249 QLDIEASFIDEEFIFELIEELTARMFAIGGIALPRPFPRMPYAEAMDTTGSDRPDLRFDlKFADATDIFENTRYGIFKqi 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 319 IEPGMPIVAIVIPNKSAM--SNTQKKAFGKEVEEQVGAE-LAYLDVE--RLRTSPQFALLADRIDAAAaahcKLERVEPD 393
Cdd:PRK12820 329 LQRGGRIKGINIKGQSEKlsKNVLQNEYAKEIAPSFGAKgMTWMRAEagGLDSNIVQFFSADEKEALK----RRFHAEDG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 394 HRLVVIsprlgaAAVSRDTswVYKRAGQLRLELGKRFAAEHKAFekkgtaadYQFLWVTDFPFFEWDEQSHTwTFAHHPF 473
Cdd:PRK12820 405 DVIIMI------ADASCAI--VLSALGQLRLHLADRLGLIPEGV--------FHPLWITDFPLFEATDDGGV-TSSHHPF 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 474 TSPHQDDLIAGRLEsDQAAVRALAYDVVLNGTELGSGSIRIHRQDVQQQIFRALGMSDDEAKERFGFFLEALQYGTPPHG 553
Cdd:PRK12820 468 TAPDREDFDPGDIE-ELLDLRSRAYDLVVNGEELGGGSIRINDKDIQLRIFAALGLSEEDIEDKFGFFLRAFDFAAPPHG 546
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 254781707 554 GIALGLDRIVMILAGASSLREVIAFPKTAKAIDLMVDAPTPVSDAQLREL 603
Cdd:PRK12820 547 GIALGLDRVVSMILQTPSIREVIAFPKNRSAACPLTGAPSEVAQEQLAEL 596
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
149-583 |
3.87e-150 |
|
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: 433.93 E-value: 3.87e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 149 FEVRHKVALAVRQYLSGQGFFEVETPFMTRSTPEGARDYLVPSRVHPGEFYALPQSPQLFKQILMISGMDRYFQIARCFR 228
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTPEGARDFLVPSRLHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 229 DEDLRADRQPEFTQIDLEMTFPQQETIFGVVEGFLAAAF-EAVGQQITVPFPRMTYDKAIELYGidkpdlrlppmtdvrs 307
Cdd:cd00777 81 DEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFkEVLGVELTTPFPRMTYAEAMERYG---------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 308 vfsdeelqslkiepgmpivaivipnksamsntqkkafgkeveeqvgaelayldverlrtspqfalladridaaaaahckl 387
Cdd:cd00777 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 388 ervepdhrlvvisprlgaaavsrdtswvykragqlrlelgkrfaaehkafekkgtaadYQFLWVTDFPFFEWDEQSHTWT 467
Cdd:cd00777 145 ----------------------------------------------------------FKFLWIVDFPLFEWDEEEGRLV 166
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 468 FAHHPFTSPHQDDLIagRLESDQAAVRALAYDVVLNGTELGSGSIRIHRQDVQQQIFRALGMSDDEAKERFGFFLEALQY 547
Cdd:cd00777 167 SAHHPFTAPKEEDLD--LLEKDPEDARAQAYDLVLNGVELGGGSIRIHDPDIQEKVFEILGLSEEEAEEKFGFLLEAFKY 244
|
410 420 430
....*....|....*....|....*....|....*.
gi 254781707 548 GTPPHGGIALGLDRIVMILAGASSLREVIAFPKTAK 583
Cdd:cd00777 245 GAPPHGGIALGLDRLVMLLTGSESIRDVIAFPKTQN 280
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
128-581 |
1.23e-130 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 385.77 E-value: 1.23e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 128 NEEVRLKYRYLDLRRPEMQHNFEVRHKVALAVRQYLSGQGFFEVETPFMTRS-TPEGARDYLVPSRVHpGEFYALPQSPQ 206
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSaTPEGARDFLVPSRAL-GKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 207 LFKQILMISGMDRYFQIARCFRDEDLRADRQPEFTQIDLEMTFPQQETIFGVVEGFLAAAFEAV-----------GQQIT 275
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVegiakeleggtLLDLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 276 VPFPRMTYDKAIE----------LYGIDKPDLRLPpmtdvrsvfsdeelqslkiepgmpivaivipnksamsntqkkafg 345
Cdd:pfam00152 160 KPFPRITYAEAIEklngkdveelGYGSDKPDLRFL--------------------------------------------- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 346 keveeqvgaelayldverlrtspqfalladridaaaaahcklervepdhrlvvisprlgaaavsrdtswvykragqlrle 425
Cdd:pfam00152 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 426 lgkrfaaehkaFEKKGTAADYQFLWVTDFPffewdeqshtwtFAHHPFTSPHQDDLiagrlesdqaAVRALAYDVVLNGT 505
Cdd:pfam00152 195 -----------LELVIDKNKFNPLWVTDFP------------AEHHPFTMPKDEDD----------PALAEAFDLVLNGV 241
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254781707 506 ELGSGSIRIHRQDVQQQIFRALGMSDDEAKERFGFFLEALQYGTPPHGGIALGLDRIVMILAGASSLREVIAFPKT 581
Cdd:pfam00152 242 EIGGGSIRIHDPELQEERFEEQGLDPEEAEEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAFPKT 317
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
9-579 |
6.00e-80 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 258.97 E-value: 6.00e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 9 QRTHTCGELRAAHAGETITIMGWVNRRRDHGNLIFLDLRDRYGITQVVLDKDLSAEAHAKAEQARPEYVICATGKVRArs 88
Cdd:PRK05159 2 MKRHLTSELTPELDGEEVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKVDEELFETIKKLKRESVVSVTGTVKA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 89 qeaiNPKMPTGeIEIAATELLILNDSKVP-PFSPAEEAIANEEVRLKYRYLDLRRPEMQHNFEVRHKVALAVRQYLSGQG 167
Cdd:PRK05159 80 ----NPKAPGG-VEVIPEEIEVLNKAEEPlPLDISGKVLAELDTRLDNRFLDLRRPRVRAIFKIRSEVLRAFREFLYENG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 168 FFEVETPFMTRSTPEGARDyLVPSRVHPGEFYaLPQSPQLFKQILMISGMDRYFQIARCFRDEDLRADRQ-PEFTQIDLE 246
Cdd:PRK05159 155 FTEIFTPKIVASGTEGGAE-LFPIDYFEKEAY-LAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSRHlNEYTSIDVE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 247 MTFPQQET-IFGVVEGFLAAAFEAVGQ--------------QITVPFPRMTYDKAIELygIDKPDLRLPPMTDvrsvFSD 311
Cdd:PRK05159 233 MGFIDDHEdVMDLLENLLRYMYEDVAEncekelellgielpVPETPIPRITYDEAIEI--LKSKGNEISWGDD----LDT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 312 EELqslkiepgmpivaivipnksamsntqkKAFGKEVEEQVGAElayldverlrtspqfalladridaaaaahcklerve 391
Cdd:PRK05159 307 EGE---------------------------RLLGEYVKEEYGSD------------------------------------ 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 392 pdhrlvvisprlgaaavsrdtswvykragqlrlelgkrfaaehkafekkgtaadyqFLWVTDFPffewdeqshtwtFAHH 471
Cdd:PRK05159 324 --------------------------------------------------------FYFITDYP------------SEKR 335
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 472 PF-TSPHQDDliagrlesdqaAVRALAYDVVLNGTELGSGSIRIHRQDVQQQIFRALGMSddeaKERFGFFLEALQYGTP 550
Cdd:PRK05159 336 PFyTMPDEDD-----------PEISKSFDLLFRGLEITSGGQRIHRYDMLVESIKEKGLN----PESFEFYLEAFKYGMP 400
|
570 580
....*....|....*....|....*....
gi 254781707 551 PHGGIALGLDRIVMILAGASSLREVIAFP 579
Cdd:PRK05159 401 PHGGFGLGLERLTMKLLGLENIREAVLFP 429
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
149-581 |
6.43e-76 |
|
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: 242.77 E-value: 6.43e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 149 FEVRHKVALAVRQYLSGQGFFEVETPFMTRSTP-EGARDYLVPSRvHPGEFYALPQSPQLFKQILMISGMDRYFQIARCF 227
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGgAGARPFLVKYN-ALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 228 RDEDLRADRQPEFTQIDLEMTFPQQETIFGVVEGFLAAAFEAVGQQITV-----------PFPRMTYDKAIELYGidkpd 296
Cdd:cd00669 80 RNEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVtygfeledfglPFPRLTYREALERYG----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 297 lrlppmtdvrsvfsdeelqslkiepgmpivaivipnksamsntqkkafgkeveeqvgaelayldverlrtspqfalladr 376
Cdd:cd00669 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 377 idaaaaahcklervepdhrlvvisprlgaaavsrdtswvykragqlrlelgkrfaaehkafekkgtaadyQFLWVTDFPf 456
Cdd:cd00669 155 ----------------------------------------------------------------------QPLFLTDYP- 163
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 457 fewdeqshtwTFAHHPFTSPHqddliagrlesDQAAVRALAYDVVLNGTELGSGSIRIHRQDVQQQIFRALGMSDDEAKE 536
Cdd:cd00669 164 ----------AEMHSPLASPH-----------DVNPEIADAFDLFINGVEVGNGSSRLHDPDIQAEVFQEQGINKEAGME 222
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 254781707 537 RFGFFLEALQYGTPPHGGIALGLDRIVMILAGASSLREVIAFPKT 581
Cdd:cd00669 223 YFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKM 267
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
10-145 |
6.86e-76 |
|
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: 237.80 E-value: 6.86e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 10 RTHTCGELRAAHAGETITIMGWVNRRRDHGNLIFLDLRDRYGITQVVLDKDlSAEAHAKAEQARPEYVICATGKVRARSQ 89
Cdd:cd04317 1 RTHYCGELRESHVGQEVTLCGWVQRRRDHGGLIFIDLRDRYGIVQVVFDPE-EAPEFELAEKLRNESVIQVTGKVRARPE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 254781707 90 EAINPKMPTGEIEIAATELLILNDSKVPPFSPAEEAIANEEVRLKYRYLDLRRPEM 145
Cdd:cd04317 80 GTVNPKLPTGEIEVVASELEVLNKAKTLPFEIDDDVNVSEELRLKYRYLDLRRPKM 135
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
10-581 |
1.45e-68 |
|
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: 228.78 E-value: 1.45e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 10 RTHTCGELRAAHAGETITIMGWVNRRRDHGNLIFLDLRDRYGITQVVLDKDlSAEAHAKAEQARPEYVICATGKVRArsq 89
Cdd:COG0017 1 KRTYIKDLLPEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKD-KLENFEEAKKLTTESSVEVTGTVVE--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 90 eaiNPKMPTGeIEIAATELLILNDSKVP-PFSPAEEAIaneEVRLKYRYLDLRRPEMQHNFEVRHKVALAVRQYLSGQGF 168
Cdd:COG0017 77 ---SPRAPQG-VELQAEEIEVLGEADEPyPLQPKRHSL---EFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 169 FEVETPFMTRSTPEGArdylvpsrvhpGEFYA---------LPQSPQLFKQILMISgMDRYFQIARCFRDEDLRADRQ-P 238
Cdd:COG0017 150 VEVHTPIITASATEGG-----------GELFPvdyfgkeayLTQSGQLYKEALAMA-LEKVYTFGPTFRAEKSNTRRHlA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 239 EFTQIDLEMTFPQQETIFGVVEGFLAAAFEAV-----------GQQITV-------PFPRMTYDKAIELYgidkpdlrlp 300
Cdd:COG0017 218 EFWMIEPEMAFADLEDVMDLAEEMLKYIIKYVlencpeeleflGRDVERlekvpesPFPRITYTEAIEIL---------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 301 pmtdvrsvfsdeelqslkiepgmpivaivipnksamsntqkKAFGKEVEEqvGAELAyldverlrtspqfalladridaa 380
Cdd:COG0017 288 -----------------------------------------KKSGEKVEW--GDDLG----------------------- 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 381 aaahcklervePDHrlvvisprlgaaavsrdtswvykragqlrlElgkRFAAEHkaFEKKgtaadyqFLWVTDFPffeWD 460
Cdd:COG0017 302 -----------TEH------------------------------E---RYLGEE--FFKK-------PVFVTDYP---KE 325
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 461 EQshtwtfahhPF-TSPHQDDliaGRLesdqaavrALAYDVVLNGT-ELGSGSIRIHRQDVQQQIFRALGMSddeaKERF 538
Cdd:COG0017 326 IK---------AFyMKPNPDD---PKT--------VAAFDLLAPGIgEIIGGSQREHRYDVLVERIKEKGLD----PEDY 381
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 254781707 539 GFFLEALQYGTPPHGGIALGLDRIVMILAGASSLREVIAFPKT 581
Cdd:COG0017 382 EWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRD 424
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
127-583 |
2.70e-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: 141.16 E-value: 2.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 127 ANEEVRLKYRYLDLRRPEMQHNFEVRHKVALAVRQYLSGQGFFEVETPFMTRSTPEGardylvPSRVHPGEFYA----LP 202
Cdd:cd00776 2 ANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEG------GAELFKVSYFGkpayLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 203 QSPQLFKQIlMISGMDRYFQIARCFRDEDLRADRQ-PEFTQIDLEMTFPQQET-IFGVVEGFLAAAFEAVGQ-------- 272
Cdd:cd00776 76 QSPQLYKEM-LIAALERVYEIGPVFRAEKSNTRRHlSEFWMLEAEMAFIEDYNeVMDLIEELIKYIFKRVLErcakelel 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 273 ---------QITVPFPRMTYDKAIELygidkpdLRlppmtdvrsvfsdEELQSLKIEPGMPivaivipnksamsntqkka 343
Cdd:cd00776 155 vnqlnrellKPLEPFPRITYDEAIEL-------LR-------------EKGVEEEVKWGED------------------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 344 FGKEVEEQVGAElayldverLRTSPQFalladridaaaaahcklervepdhrlvvisprlgaaavsrdtswvykragqlr 423
Cdd:cd00776 196 LSTEHERLLGEI--------VKGDPVF----------------------------------------------------- 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 424 lelgkrfaaehkafekkgtaadyqflwVTDFPffeWDEQshtwtfahhPF-TSPHQDDLiagrlesdqaaVRALAYDVVL 502
Cdd:cd00776 215 ---------------------------VTDYP---KEIK---------PFyMKPDDDNP-----------ETVESFDLLM 244
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 503 NGT-ELGSGSIRIHRQDVQQQIFRALGMSddeaKERFGFFLEALQYGTPPHGGIALGLDRIVMILAGASSLREVIAFPKT 581
Cdd:cd00776 245 PGVgEIVGGSQRIHDYDELEERIKEHGLD----PESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFPRD 320
|
..
gi 254781707 582 AK 583
Cdd:cd00776 321 PK 322
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
10-579 |
3.38e-33 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 133.29 E-value: 3.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 10 RTHTCGELRAAHAG----------ETITIMGWVNRRRDHGNLIFLDLRDRYGITQVVLDKD-LSAEAHAKAEQARPEYVI 78
Cdd:PRK00484 31 RTHTAAELRAKYDDkekeeleeleIEVSVAGRVMLKRVMGKASFATLQDGSGRIQLYVSKDdVGEEALEAFKKLDLGDII 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 79 CATGKVRaRSQeainpkmpTGEIEIAATELLILNDSKVPP---FSpaeeAIANEEVRLKYRYLDL-RRPEMQHNFEVRHK 154
Cdd:PRK00484 111 GVEGTLF-KTK--------TGELSVKATELTLLTKSLRPLpdkFH----GLTDVETRYRQRYVDLiVNPESRETFRKRSK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 155 VALAVRQYLSGQGFFEVETPFMtRSTPEG--AR---------D---YLvpsRVhpgefyalpqSPQLFKQILMISGMDRY 220
Cdd:PRK00484 178 IISAIRRFLDNRGFLEVETPML-QPIAGGaaARpfithhnalDidlYL---RI----------APELYLKRLIVGGFERV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 221 FQIARCFRDEDLRADRQPEFTQIDLEMTFPQQETIFGVVEGFLAAAFEAVGQQITVPFPRMTYDkaielygIDKPDLRLp 300
Cdd:PRK00484 244 YEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTYQGTEID-------FGPPFKRL- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 301 PMTDvrsvfsdeelqslkiepgmpivaivipnksamsntqkkafgkEVEEQVGAELAYLDVERLRTspqfalLADRIdaa 380
Cdd:PRK00484 316 TMVD------------------------------------------AIKEYTGVDFDDMTDEEARA------LAKEL--- 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 381 aaahcKLErVEPDHRLvvisprlgaaavsrdtswvykraGQLRLELgkrFaaEHKAfEKKgtaadyqfLW----VTDFPF 456
Cdd:PRK00484 345 -----GIE-VEKSWGL-----------------------GKLINEL---F--EEFV-EPK--------LIqptfITDYPV 381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 457 fewdEQShtwtfahhPFTSPHQDD---------LIAGRlEsdqaavRALAYdvvlngTELgsgsirihrQD--------V 519
Cdd:PRK00484 382 ----EIS--------PLAKRHREDpglterfelFIGGR-E------IANAF------SEL---------NDpidqrerfE 427
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254781707 520 QQQIFRALGmsDDEA----KErfgfFLEALQYGTPPHGGIALGLDRIVMILAGASSLREVIAFP 579
Cdd:PRK00484 428 AQVEAKEAG--DDEAmfmdED----FLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
25-112 |
4.95e-33 |
|
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: 121.52 E-value: 4.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 25 TITIMGWVNRRRDHGNLIFLDLRDRYGITQVVLDKDLSAEAHAKAEQARPEYVICATGKVRARSQeainPKMPTGEIEIA 104
Cdd:cd04100 1 EVTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEELGEFFEEAEKLRTESVVGVTGTVVKRPE----GNLATGEIELQ 76
|
....*...
gi 254781707 105 ATELLILN 112
Cdd:cd04100 77 AEELEVLS 84
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
10-579 |
2.84e-32 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 133.17 E-value: 2.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 10 RTHTCGELRAAHAGETITIMGWVNRRRDHGNLIFLDLRDRYGITQVVLDKdlSAEAHAKAEQARPEY----VICATGKV- 84
Cdd:PRK02983 638 PTHTVAEALDAPTGEEVSVSGRVLRIRDYGGVLFADLRDWSGELQVLLDA--SRLEQGSLADFRAAVdlgdLVEVTGTMg 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 85 RARsqeainpkmpTGEIEIAATELLILNDSKVPPFSPaEEAIANEEVRLKYRYLDLR-RPEMQHNFEVRHKVALAVRQYL 163
Cdd:PRK02983 716 TSR----------NGTLSLLVTSWRLAGKCLRPLPDK-WKGLTDPEARVRQRYLDLAvNPEARDLLRARSAVVRAVRETL 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 164 SGQGFFEVETP-------------FMTRSTPEGARDYLvpsRVhpgefyalpqSPQLFKQILMISGMDRYFQIARCFRDE 230
Cdd:PRK02983 785 VARGFLEVETPilqqvhgganarpFVTHINAYDMDLYL---RI----------APELYLKRLCVGGVERVFELGRNFRNE 851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 231 DLRADRQPEFTQIDLEMTFPQQET-IFGVVEGFLAAAFEAVGQQITVpfprmtydkaielygidKPDlrlppmtdvrsvf 309
Cdd:PRK02983 852 GVDATHNPEFTLLEAYQAHADYDTmRDLTRELIQNAAQAAHGAPVVM-----------------RPD------------- 901
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 310 SDEELQSLKIEPGMPivaiVIPNKSAMSntqkKAFGKEVEEQvgaelayLDVERLRTspqfalLADRidaaaaahckler 389
Cdd:PRK02983 902 GDGVLEPVDISGPWP----VVTVHDAVS----EALGEEIDPD-------TPLAELRK------LCDA------------- 947
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 390 vepdhrlvvisprlgaAAVSRDTSWvykRAGQLRLELGKRFAAEHKAFEKkgtaadyqflWVTDFPFfewdEQShtwtfa 469
Cdd:PRK02983 948 ----------------AGIPYRTDW---DAGAVVLELYEHLVEDRTTFPT----------FYTDFPT----SVS------ 988
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 470 hhPFTSPHQDDL-IAGRlesdqaavralaYDVVLNGTELGSGSIRI-----HRQDVQQQIFRALGmSDDEAKERFGFFLE 543
Cdd:PRK02983 989 --PLTRPHRSDPgLAER------------WDLVAWGVELGTAYSELtdpveQRRRLTEQSLLAAG-GDPEAMELDEDFLQ 1053
|
570 580 590
....*....|....*....|....*....|....*.
gi 254781707 544 ALQYGTPPHGGIALGLDRIVMILAGAsSLREVIAFP 579
Cdd:PRK02983 1054 ALEYAMPPTGGLGMGVDRLVMLLTGR-SIRETLPFP 1088
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
18-579 |
1.07e-26 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 115.13 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 18 RAAHAgeTITIMGWVNRRRDHGNLIFLDLRDRYGITQVVLdkdlSAEAHAKAEQARPEYVICATGKVRArsQEAINPKMP 97
Cdd:PTZ00385 104 RAAQA--TVRVAGRVTSVRDIGKIIFVTIRSNGNELQVVG----QVGEHFTREDLKKLKVSLRVGDIIG--ADGVPCRMQ 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 98 TGEIEIAATELLIL-----NDSKVPPFSPAEEAIANEEVRLKYRYLDL-RRPEMQHNFEVRHKVALAVRQYLSGQGFFEV 171
Cdd:PTZ00385 176 RGELSVAASRMLILspyvcTDQVVCPNLRGFTVLQDNDVKYRYRFTDMmTNPCVIETIKKRHVMLQALRDYFNERNFVEV 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 172 ETPFM-TRSTPEGARDYLVPSRVHPGEFYaLPQSPQLFKQILMISGMDRYFQIARCFRDEDLRADRQPEFTQIDLEMTFP 250
Cdd:PTZ00385 256 ETPVLhTVASGANAKSFVTHHNANAMDLF-LRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTSCEFYAAYH 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 251 QQETIFGVVEG-FLAAAFEAVGQQITVPFPRMTYDKAIELygidkpDLRLPpmtdVRSVFSDEELQSlkiepgMPIVAIV 329
Cdd:PTZ00385 335 TYEDLMPMTEDiFRQLAMRVNGTTVVQIYPENAHGNPVTV------DLGKP----FRRVSVYDEIQR------MSGVEFP 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 330 IPNKsamSNTQKKafgkeveeqvgaeLAYLDVERLRTSPQFalladridaaaaahcklervepdhrlvvisPRLGAAAvs 409
Cdd:PTZ00385 399 PPNE---LNTPKG-------------IAYMSVVMLRYNIPL------------------------------PPVRTAA-- 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 410 rdtswvykragqlrlelgkrfaaehKAFEKkgtaadyqflwVTDFpFFEWDEQSHTWTFAHHPFTSPhqddliagrLESD 489
Cdd:PTZ00385 431 -------------------------KMFEK-----------LIDF-FITDRVVEPTFVMDHPLFMSP---------LAKE 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 490 QAAVRALA--YDVVLNG-------TELGSGSIRIHRqdVQQQIFRALGmSDDEAKERFGFFLEALQYGTPPHGGIALGLD 560
Cdd:PTZ00385 465 QVSRPGLAerFELFVNGieycnaySELNDPHEQYHR--FQQQLVDRQG-GDEEAMPLDETFLKSLQVGLPPTAGWGMGID 541
|
570
....*....|....*....
gi 254781707 561 RIVMILAGASSLREVIAFP 579
Cdd:PTZ00385 542 RALMLLTNSSNIRDGIIFP 560
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
15-580 |
5.63e-26 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 112.11 E-value: 5.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 15 GELRAAHAGETITIMGWVNRRRDHGNLIFLDLRDRYGITQVVL---DKDLSAEAHAKAEQARPEYVICATGKVrarsqea 91
Cdd:PLN02850 73 SDLGEELAGSEVLIRGRVHTIRGKGKSAFLVLRQSGFTVQCVVfvsEVTVSKGMVKYAKQLSRESVVDVEGVV------- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 92 INPKMP----TGEIEIAATELLILNDSKVP-PF-----SPAEEAI------------ANEEVRLKYRYLDLRRPEMQHNF 149
Cdd:PLN02850 146 SVPKKPvkgtTQQVEIQVRKIYCVSKALATlPFnvedaARSESEIekalqtgeqlvrVGQDTRLNNRVLDLRTPANQAIF 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 150 EVRHKVALAVRQYLSGQGFFEVETPFMTRSTPEGAR-----DYLvpsrvhpGEFYALPQSPQLFKQILMISGMDRYFQIA 224
Cdd:PLN02850 226 RIQSQVCNLFREFLLSKGFVEIHTPKLIAGASEGGSavfrlDYK-------GQPACLAQSPQLHKQMAICGDFRRVFEIG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 225 RCFRDEDLRADRQ-PEFTQIDLEMTFPQQET-IFGVVEGFLAAAF-----------EAVGQQitVPFPRMTYdkaielyg 291
Cdd:PLN02850 299 PVFRAEDSFTHRHlCEFTGLDLEMEIKEHYSeVLDVVDELFVAIFdglnerckkelEAIREQ--YPFEPLKY-------- 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 292 IDKPdLRLPpmtdvrsvFSdEELQSLKIEpgmpivaivipnksamsntqkkafGKEVEeqvgaELAYLDVErlrtspqfa 371
Cdd:PLN02850 369 LPKT-LRLT--------FA-EGIQMLKEA------------------------GVEVD-----PLGDLNTE--------- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 372 lladridaaaaahckLERvepdhrlvvisprlgaaavsrdtswvykRAGQLRLelgkrfaaehkafEKKGTaaDYQFLwv 451
Cdd:PLN02850 401 ---------------SER----------------------------KLGQLVK-------------EKYGT--DFYIL-- 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 452 tdfpffewdeqsHTWTFAHHPF-TSPHQDDliaGRLESdqaavralAYDVVLNGTELGSGSIRIHRQDVQQQIFRALGMS 530
Cdd:PLN02850 421 ------------HRYPLAVRPFyTMPCPDD---PKYSN--------SFDVFIRGEEIISGAQRVHDPELLEKRAEECGID 477
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 254781707 531 DDEAKErfgfFLEALQYGTPPHGGIALGLDRIVMILAGASSLREVIAFPK 580
Cdd:PLN02850 478 VKTIST----YIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPR 523
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
17-289 |
4.63e-25 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 108.27 E-value: 4.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 17 LRAAHAGETITIMGWVNRRRDHGNLIFLDLRDRYGITQVVLDKDLSAEAHAKAEQARPEYVICATGKVRArsqeaiNPKM 96
Cdd:PRK03932 10 LKGKYVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDNGEEYFEEIKKLTTGSSVIVTGTVVE------SPRA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 97 PTGeIEIAATELLIL-NDSKVPPFSPAEEAIaneEVRLKYRYLDLRRPEMQHNFEVRHKVALAVRQYLSGQGFFEVETPF 175
Cdd:PRK03932 84 GQG-YELQATKIEVIgEDPEDYPIQKKRHSI---EFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVDTPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 176 MTRSTPEGA----------RDYlvpsrvhPGEFYA----LPQSPQLFKQIlMISGMDRYFQIARCFRDEDLRADRQ-PEF 240
Cdd:PRK03932 160 ITASDCEGAgelfrvttldLDF-------SKDFFGkeayLTVSGQLYAEA-YAMALGKVYTFGPTFRAENSNTRRHlAEF 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254781707 241 TQIDLEMTFPQQETIFGVVEGFLAAAFEAV-----------GQQ------------ITVPFPRMTYDKAIEL 289
Cdd:PRK03932 232 WMIEPEMAFADLEDNMDLAEEMLKYVVKYVlencpddleflNRRvdkgdierlenfIESPFPRITYTEAIEI 303
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
9-579 |
8.36e-25 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 108.54 E-value: 8.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 9 QRTHTCGELRAAHA---------GETITIMGWVNRRRDHGNLIFLDLRDRYGITQVVLDKDLSAEAHAKAEQARPEY--- 76
Cdd:PLN02502 85 DVTHTAPELQEKYGslengeeleDVSVSVAGRIMAKRAFGKLAFYDLRDDGGKIQLYADKKRLDLDEEEFEKLHSLVdrg 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 77 -VICATGKVRarsqeainpKMPTGEIEIAATELLILNDSKVPPfsPAEEA-IANEEVRLKYRYLDL-RRPEMQHNFEVRH 153
Cdd:PLN02502 165 dIVGVTGTPG---------KTKKGELSIFPTSFEVLTKCLLML--PDKYHgLTDQETRYRQRYLDLiANPEVRDIFRTRA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 154 KVALAVRQYLSGQGFFEVETPFMtRSTPEGA--RdylvPSRVHPGE----FYaLPQSPQLFKQILMISGMDRYFQIARCF 227
Cdd:PLN02502 234 KIISYIRRFLDDRGFLEVETPML-NMIAGGAaaR----PFVTHHNDlnmdLY-LRIATELHLKRLVVGGFERVYEIGRQF 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 228 RDEDLRADRQPEFTQID-----------LEMTfpqQETIFGVVE---GFLAAAFEAVGQQITVPFPRMTYDKAIELY-GI 292
Cdd:PLN02502 308 RNEGISTRHNPEFTTCEfyqayadyndmMELT---EEMVSGMVKeltGSYKIKYHGIEIDFTPPFRRISMISLVEEAtGI 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 293 DKPdlrlppmtdvrSVFSDEELQSLKIEPGMPIvAIVIPNKSAMSNTQKKAFGKEVEEQVgaelayldverlrTSPQFAL 372
Cdd:PLN02502 385 DFP-----------ADLKSDEANAYLIAACEKF-DVKCPPPQTTGRLLNELFEEFLEETL-------------VQPTFVL 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 373 ladridaaaaahcklervepDHRlVVISP-----RLGAAAVSRDTSWVYKRagqlrlELGKRFAAehkafekkgtaadyq 447
Cdd:PLN02502 440 --------------------DHP-VEMSPlakphRSKPGLTERFELFINGR------ELANAFSE--------------- 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 448 flwVTDfPFfewdEQSHtwtfahhpftsphqddliagRLEsDQAAVRALAYDvvlngtelgsgsirihrqdvqqqifRAL 527
Cdd:PLN02502 478 ---LTD-PV----DQRE--------------------RFE-EQVKQHNAGDD-------------------------EAM 503
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 254781707 528 GMSDDeakerfgfFLEALQYGTPPHGGIALGLDRIVMILAGASSLREVIAFP 579
Cdd:PLN02502 504 ALDED--------FCTALEYGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFP 547
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
26-579 |
1.27e-23 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 104.76 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 26 ITIMGWVNRRRDHGNLIFLDLRDRYGITQVVLDKDLSAEAHAKAEQARPEY--VICATGKVRarsqeainpKMPTGEIEI 103
Cdd:PRK12445 68 VSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEGVYNDQFKKWDLgdIIGARGTLF---------KTQTGELSI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 104 AATELLILNDSkVPPFSPAEEAIANEEVRLKYRYLDL-RRPEMQHNFEVRHKVALAVRQYLSGQGFFEVETPFMtRSTPE 182
Cdd:PRK12445 139 HCTELRLLTKA-LRPLPDKFHGLQDQEVRYRQRYLDLiANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMM-QVIPG 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 183 GA--RDYLVPSRVHPGEFYaLPQSPQLFKQILMISGMDRYFQIARCFRDEDLRADRQPEFTQIDLEMTFPQQETIFGVVE 260
Cdd:PRK12445 217 GAsaRPFITHHNALDLDMY-LRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTE 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 261 GFLAAAFEAVGQQITVPFPRMTYDkaielygIDKPDLRLppmtdvrsvfsdeelqslkiepgmpivaivipnksamsnTQ 340
Cdd:PRK12445 296 SLFRTLAQEVLGTTKVTYGEHVFD-------FGKPFEKL---------------------------------------TM 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 341 KKAFGKEVEEQVGAELAYLDVERlrtspqfaLLADRIdaaaaahcklervepdhrlvvisprlgaaAVSRDTSWvykRAG 420
Cdd:PRK12445 330 REAIKKYRPETDMADLDNFDAAK--------ALAESI-----------------------------GITVEKSW---GLG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 421 QLRLELgkrfaaehkaFEKKGTAADYQFLWVTDFPffewdeqSHTWTFAHHPFTSPHQDDliagrlesdqaavralAYDV 500
Cdd:PRK12445 370 RIVTEI----------FDEVAEAHLIQPTFITEYP-------AEVSPLARRNDVNPEITD----------------RFEF 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 501 VLNGTELGSGSIRIHRQDVQQQIFR----ALGMSDDEAKERFGFFLEALQYGTPPHGGIALGLDRIVMILAGASSLREVI 576
Cdd:PRK12445 417 FIGGREIGNGFSELNDAEDQAERFQeqvnAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVI 496
|
...
gi 254781707 577 AFP 579
Cdd:PRK12445 497 LFP 499
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
143-579 |
9.00e-23 |
|
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: 99.58 E-value: 9.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 143 PEMQHNFEVRHKVALAVRQYLSGQGFFEVETPFMtRSTPEGA--RDYLVPSRVHPGEFYaLPQSPQLFKQILMISGMDRY 220
Cdd:cd00775 2 EEVRQTFIVRSKIISYIRKFLDDRGFLEVETPML-QPIAGGAaaRPFITHHNALDMDLY-LRIAPELYLKRLIVGGFERV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 221 FQIARCFRDEDLRADRQPEFTQIDLEMTFPQQETIFGVVEGFLAAAFEAV---------GQQI--TVPFPRMTYDKAIEL 289
Cdd:cd00775 80 YEIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKIngktkieygGKELdfTPPFKRVTMVDALKE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 290 Y-GIDKPDLRLPPMTDVRSVFsdEELQSLKIEPGMPIVAIVIpnksamsntqkKAFGKEVEEQVgaelayldverlrTSP 368
Cdd:cd00775 160 KtGIDFPELDLEQPEELAKLL--AKLIKEKIEKPRTLGKLLD-----------KLFEEFVEPTL-------------IQP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 369 QFALladridaaaaahcklervepDHRlVVISPrlgaaavsrdtswvykragqlrlelgkrFAAEHKafEKKGtaadyqf 448
Cdd:cd00775 214 TFII--------------------DHP-VEISP----------------------------LAKRHR--SNPG------- 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 449 lwVTD-FPFFewdeqshtwtfahhpftsphqddlIAGRlEsdqaavralaydvVLNG-TELGSgsIRIHRQDVQQQIfRA 526
Cdd:cd00775 236 --LTErFELF------------------------ICGK-E-------------IANAyTELND--PFDQRERFEEQA-KQ 272
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 254781707 527 LGMSDDEAKERFGFFLEALQYGTPPHGGIALGLDRIVMILAGASSLREVIAFP 579
Cdd:cd00775 273 KEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLTDSNSIRDVILFP 325
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
18-580 |
5.16e-20 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 93.90 E-value: 5.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 18 RAAHAGETITIMGWVNRRRDHGNLIFLDLRDryGITqvvldkdlSAEAHAKAEQARPEYVICATGKVRARS---QEAI-- 92
Cdd:PTZ00401 73 KPELVDKTVLIRARVSTTRKKGKMAFMVLRD--GSD--------SVQAMAAVEGDVPKEMIDFIGQIPTESivdVEATvc 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 93 ---NPKMPTG--EIEIAATELLILNDS-KVPPFSPA--------EEAIANEEVRLKYRYLDLRRPEMQHNFEVRHKVALA 158
Cdd:PTZ00401 143 kveQPITSTShsDIELKVKKIHTVTESlRTLPFTLEdasrkesdEGAKVNFDTRLNSRWMDLRTPASGAIFRLQSRVCQY 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 159 VRQYLSGQGFFEVETPFMTRSTPEGARDylVPSRVHPGEFYALPQSPQLFKQILMISGMDRYFQIARCFRDEDLRADRQ- 237
Cdd:PTZ00401 223 FRQFLIDSDFCEIHSPKIINAPSEGGAN--VFKLEYFNRFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNTHRHl 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 238 PEFTQIDLEMTFPQQ--------ETIFGVVEGFLA---AAFEAVGQQitVPFP----RMTYDKAIELyGIDKPDLRLPPM 302
Cdd:PTZ00401 301 TEFVGLDVEMRINEHyyevldlaESLFNYIFERLAthtKELKAVCQQ--YPFEplvwKLTPERMKEL-GVGVISEGVEPT 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 303 TDVRSVFSDEELQSLKIE--PGMPIVAIVIPNKSAMSN----TQKKAFGKEVEEQVGAELayldverlrtspqfalladr 376
Cdd:PTZ00401 378 DKYQARVHNMDSRMLRINymHCIELLNTVLEEKMAPTDdintTNEKLLGKLVKERYGTDF-------------------- 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 377 idaaaaahcklervepdhrlvVISPRLGAAAVsrdtswvykragqlrlelgkrfaaehkafekkgtaadyqflwvtdfPF 456
Cdd:PTZ00401 438 ---------------------FISDRFPSSAR----------------------------------------------PF 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 457 fewdeqshtwtfahhpFTSPHQDDLiagRLESdqaavralAYDVVLNGTELGSGSIRIHRQDVQQQIFRALGMSDDEAKE 536
Cdd:PTZ00401 451 ----------------YTMECKDDE---RFTN--------SYDMFIRGEEISSGAQRIHDPDLLLARAKMLNVDLTPIKE 503
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 254781707 537 rfgfFLEALQYGTPPHGGIALGLDRIVMILAGASSLREVIAFPK 580
Cdd:PTZ00401 504 ----YVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFPR 543
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
12-123 |
1.11e-19 |
|
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: 84.67 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 12 HTCGELRAAHAGETITIMGWVNRRRDHGNLIFLDLRDRYGITQVVLDKDL-SAEAHAKAEQARPEYVICATGKVRArsqe 90
Cdd:cd04316 1 HYSAEITPELDGEEVTVAGWVHEIRDLGGIKFVILRDREGIVQVTAPKKKvDKELFKTVRKLSRESVISVTGTVKA---- 76
|
90 100 110
....*....|....*....|....*....|....
gi 254781707 91 aiNPKMPTGeIEIAATELLILNDSK-VPPFSPAE 123
Cdd:cd04316 77 --EPKAPNG-VEIIPEEIEVLSEAKtPLPLDPTG 107
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
95-579 |
3.74e-16 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 81.98 E-value: 3.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 95 KMPTGEIEIAATELLILndSKVPPFSPAEEAIANEEVRLKYRYLDLRRPE-MQHNFEVRHKVALAVRQYLSGQGFFEVET 173
Cdd:PTZ00417 200 KSKKGELSIFPKETIIL--SPCLHMLPMKYGLKDTEIRYRQRYLDLMINEsTRSTFITRTKIINYLRNFLNDRGFIEVET 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 174 PFMTR-STPEGARDYLVPSRVHPGEFYaLPQSPQLFKQILMISGMDRYFQIARCFRDEDLRADRQPEFTQIDLEMTFPQQ 252
Cdd:PTZ00417 278 PTMNLvAGGANARPFITHHNDLDLDLY-LRIATELPLKMLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADF 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 253 ETIFGVVEGFLAA-AFEAVGqqitvpfprmTYDKaieLYGIDKPdlrlppmtdvrsvfsDEELQSLKIEPGMPIVAIVip 331
Cdd:PTZ00417 357 YDLIKWSEDFFSQlVMHLFG----------TYKI---LYNKDGP---------------EKDPIEIDFTPPYPKVSIV-- 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 332 nksamsntqkkafgKEVEEQVGAELayldvERLRTSPQfalladRIDaaaaahcKLERVEPDHRLVVISPrlgaaavsrd 411
Cdd:PTZ00417 407 --------------EELEKLTNTKL-----EQPFDSPE------TIN-------KMINLIKENKIEMPNP---------- 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 412 tswvyKRAGQLRLELGKRFaAEHKAFEKkgtaadyqflwvtdfPFFEWDEQSHTWTFAHHPFTSPHqddlIAGRLEsdqa 491
Cdd:PTZ00417 445 -----PTAAKLLDQLASHF-IENKYPNK---------------PFFIIEHPQIMSPLAKYHRSKPG----LTERLE---- 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 492 avralaydVVLNGTELGSGSIRIHRQDVQQQIFRALGMS----DDEAKERFGFFLEALQYGTPPHGGIALGLDRIVMILA 567
Cdd:PTZ00417 496 --------MFICGKEVLNAYTELNDPFKQKECFSAQQKDrekgDAEAFQFDAAFCTSLEYGLPPTGGLGLGIDRITMFLT 567
|
490
....*....|..
gi 254781707 568 GASSLREVIAFP 579
Cdd:PTZ00417 568 NKNCIKDVILFP 579
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
151-274 |
4.94e-16 |
|
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: 77.16 E-value: 4.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 151 VRHKVALAVRQYLSGQGFFEVETPFMTRSTPEGARD----YLVPSRVHPGEFYALPQSPQLFKQILMIS----GMDRYFQ 222
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGhepkDLLPVGAENEEDLYLRPTLEPGLVRLFVShirkLPLRLAE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 254781707 223 IARCFRDEDLRAD--RQPEFTQIDLEM---TFPQQETIFGVVEgFLAAAFEAVGQQI 274
Cdd:cd00768 81 IGPAFRNEGGRRGlrRVREFTQLEGEVfgeDGEEASEFEELIE-LTEELLRALGIKL 136
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
26-111 |
1.71e-15 |
|
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: 71.50 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 26 ITIMGWV-NRRRDHGNLIFLDLRDRYGITQVVLDKDlsaEAHAKAEQARPEYVICATGKVRARsqeainpkmPTGEIEIA 104
Cdd:pfam01336 1 VTVAGRVtSIRRSGGKLLFLTLRDGTGSIQVVVFKE---EAEKLAKKLKEGDVVRVTGKVKKR---------KGGELELV 68
|
....*..
gi 254781707 105 ATELLIL 111
Cdd:pfam01336 69 VEEIELL 75
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
128-334 |
1.35e-13 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 72.36 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 128 NEEVRLKYRYLDLRRPEMQHNFEVRHKVALAVRQYLSGQGFFEVETPFMTRSTPEGARD-----YLVPSRVHPGEFYALP 202
Cdd:PRK06462 9 EYEEFLRMSWKHISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIISPSTDPLMGLgsdlpVKQISIDFYGVEYYLA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 203 QSPQLFKQiLMISGMDRYFQIARCFRDEDLRADRQP---EFTQIDLEMTFPQQETIFGVVEGFL-----------AAAFE 268
Cdd:PRK06462 89 DSMILHKQ-LALRMLGKIFYLSPNFRLEPVDKDTGRhlyEFTQLDIEIEGADLDEVMDLIEDLIkylvkelleehEDELE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254781707 269 AVGQQ---ITVPFPRMTYDKAIELYGidkpdlRLPPMTDVRSVFSDEELQSLKIEPGMPIVAIVIPNKS 334
Cdd:PRK06462 168 FFGRDlphLKRPFKRITHKEAVEILN------EEGCRGIDLEELGSEGEKSLSEHFEEPFWIIDIPKGS 230
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
26-138 |
1.08e-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: 58.69 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 26 ITIMGWVNRRRDHGNLIFLDLRDRYGITQVVLDKDLSAEAHAKAEQARPEYVICATGKVRArsqeaiNPKMPTGeIEIAA 105
Cdd:cd04319 2 VTLAGWVYRKREVGKKAFIVLRDSTGIVQAVFSKDLNEEAYREAKKVGIESSVIVEGAVKA------DPRAPGG-AEVHG 74
|
90 100 110
....*....|....*....|....*....|...
gi 254781707 106 TELLILNDskVPPFSPAEEaiANEEVRLKYRYL 138
Cdd:cd04319 75 EKLEIIQN--VEFFPITED--ASDEFLLDVRHL 103
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
25-111 |
5.52e-09 |
|
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: 53.39 E-value: 5.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 25 TITIMGWVNRRRDHGNLIFLDLRDRYGITQVVLDKDLSAEAHAkAEQARPEYVICATGKVRA--RSQEAinpkmPTGeIE 102
Cdd:cd04323 1 RVKVFGWVHRLRSQKKLMFLVLRDGTGFLQCVLSKKLVTEFYD-AKSLTQESSVEVTGEVKEdpRAKQA-----PGG-YE 73
|
....*....
gi 254781707 103 IAATELLIL 111
Cdd:cd04323 74 LQVDYLEII 82
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
485-587 |
3.74e-08 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 56.16 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 485 RLESDQAAVRALayDVVLNGT-ELGSGSIRIHRQDVQQQIFRALGMSddeaKERFGFFLEALQYGTPPHGGIALGLDRIV 563
Cdd:PLN02221 475 RLNDDEKTVAAM--DVLVPKVgELIGGSQREERYDVIKQRIEEMGLP----IEPYEWYLDLRRYGTVKHCGFGLGFERMI 548
|
90 100
....*....|....*....|....
gi 254781707 564 MILAGASSLREVIAFPKTAKAIDL 587
Cdd:PLN02221 549 LFATGIDNIRDVIPFPRYPGKADL 572
|
|
| ScAspRS_mt_like_N |
cd04321 |
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
26-113 |
6.88e-08 |
|
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: 50.39 E-value: 6.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 26 ITIMGWVNRRRD-HGNLIFLDLRDRYG-ITQVVLDKdlSAEAHAKAEQARPEYVICATGKVRARSQeaiNPKMPTGEIEI 103
Cdd:cd04321 2 VTLNGWIDRKPRiVKKLSFADLRDPNGdIIQLVSTA--KKDAFSLLKSITAESPVQVRGKLQLKEA---KSSEKNDEWEL 76
|
90
....*....|
gi 254781707 104 AATELLILND 113
Cdd:cd04321 77 VVDDIQTLNA 86
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
503-575 |
9.96e-08 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 54.16 E-value: 9.96e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254781707 503 NG-TELGSGSIRIHR--QDVQQQifRALGMSDDEAKERFgffLEALQYGTPPHGGIALGLDRIVMILAGASSLREV 575
Cdd:PRK09350 236 NGfHELTDAREQRQRfeQDNRKR--AARGLPQQPIDENL---IAALEAGLPDCSGVALGVDRLIMLALGAESISEV 306
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
25-140 |
1.36e-07 |
|
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: 50.17 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 25 TITIMGWVNRRRDHGNLIFLDLRDRYGITQVVLDKDLSAEAHAKAEQarpEYV-----ICATGKVRaRSQeainpkmpTG 99
Cdd:cd04322 1 EVSVAGRIMSKRGSGKLSFADLQDESGKIQVYVNKDDLGEEEFEDFK---KLLdlgdiIGVTGTPF-KTK--------TG 68
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 254781707 100 EIEIAATELLILNDSKVPPFSPAEEaIANEEVRLKYRYLDL 140
Cdd:cd04322 69 ELSIFVKEFTLLSKSLRPLPEKFHG-LTDVETRYRQRYLDL 108
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
506-581 |
7.69e-07 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 51.90 E-value: 7.69e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254781707 506 ELGSGSIRIHRQDVQQQIFRALGMSddeaKERFGFFLEALQYGTPPHGGIALGLDRIVMILAGASSLREVIAFPKT 581
Cdd:PLN02603 488 ELIGGSQREERLEYLEARLDELKLN----KESYWWYLDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFPRV 559
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
162-577 |
1.35e-06 |
|
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: 50.24 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 162 YLSGQGFFEVETPFMTRST-PEGARDYLVPSRVHPG----EFYaLPQSPQLFKQILMISGMDRYFQIARCFRDEDLRADR 236
Cdd:TIGR00462 1 FFAERGVLEVETPLLSPAPvTDPHLDAFATEFVGPDgqgrPLY-LQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 237 QPEFT-----QIDLEMTFPQQETifgvvegflAAAFEAVGQQITVPFPRMTYDKAIELY-GIDkpdlrlpPMTDvrsvfS 310
Cdd:TIGR00462 80 NPEFTmlewyRPGFDYHDLMDEV---------EALLQELLGDPFAPAERLSYQEAFLRYaGID-------PLTA-----S 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 311 DEELQSLkiepgmpivaivipnksamsntqkkafGKEVEEQVGAELAYLDVErlrtspqFALLadridaaaaahckLERV 390
Cdd:TIGR00462 139 LAELQAA---------------------------AAAHGIRASEEDDRDDLL-------DLLF-------------SEKV 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 391 EpdhrlvvisPRLGAaavsrdtswvykragqlrlelgkrfaaehkafekkgtaadYQFLWVTDFPffewdeqshtwtfah 470
Cdd:TIGR00462 172 E---------PHLGF----------------------------------------GRPTFLYDYP--------------- 187
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 471 hpftsPHQDDLiaGRLESDQAAVrALAYDVVLNGTELGSGSIRIhrQDVQQQIFRAlgMSDDEAKERFG--------FFL 542
Cdd:TIGR00462 188 -----ASQAAL--ARISPDDPRV-AERFELYIKGLELANGFHEL--TDAAEQRRRF--EADNALRKALGlprypldeRFL 255
|
410 420 430
....*....|....*....|....*....|....*
gi 254781707 543 EALQYGTPPHGGIALGLDRIVMILAGASSLREVIA 577
Cdd:TIGR00462 256 AALEAGLPECSGVALGVDRLLMLALGADSIDDVLA 290
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
25-111 |
3.12e-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: 42.55 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 25 TITIMGWVNRRRDHGNLIFLDLRDryGIT----QVVLDKDLSAEahAKAEQARPEYVICATGKVRArSQEAINPkmptge 100
Cdd:cd04318 1 EVTVNGWVRSVRDSKKISFIELND--GSClknlQVVVDKELTNF--KEILKLSTGSSIRVEGVLVK-SPGAKQP------ 69
|
90
....*....|.
gi 254781707 101 IEIAATELLIL 111
Cdd:cd04318 70 FELQAEKIEVL 80
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
458-580 |
7.57e-05 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 45.78 E-value: 7.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 458 EW--DEQS-HTWTFAHHPFTSP-----HQDDLIA--GRLESDQAAVRALAYDVVLNGTELGsGSIR---IHRQDvQQQIF 524
Cdd:PTZ00425 452 KWgmDLQSeHERFVAEQIFKKPvivynYPKDLKAfyMKLNEDQKTVAAMDVLVPKIGEVIG-GSQRednLERLD-KMIKE 529
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 254781707 525 RALGMsddeakERFGFFLEALQYGTPPHGGIALGLDRIVMILAGASSLREVIAFPK 580
Cdd:PTZ00425 530 KKLNM------ESYWWYRQLRKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFPR 579
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
485-581 |
2.37e-04 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 44.09 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 485 RLESDQAAVRAlaYDVVL-NGTELGSGSIRIHRQDVQQQIFRALGMSddeaKERFGFFLEALQYGTPPHGGIALGLDRIV 563
Cdd:PLN02532 536 RLNDDGKTVAA--FDLVVpKVGTVITGSQNEERMDILNARIEELGLP----REQYEWYLDLRRHGTVKHSGFSLGFELMV 609
|
90
....*....|....*...
gi 254781707 564 MILAGASSLREVIAFPKT 581
Cdd:PLN02532 610 LFATGLPDVRDAIPFPRS 627
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
19-184 |
3.31e-04 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 43.81 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 19 AAHAGETITIMGWVNRRRDHGNLIFLDLRDRYGIT--QVVLDKDlsAEAHAKAEQArpeyvICATGKVRARSQEAINPKM 96
Cdd:PLN02603 103 LARVGKTLNVMGWVRTLRAQSSVTFIEVNDGSCLSnmQCVMTPD--AEGYDQVESG-----LITTGASVLVQGTVVSSQG 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254781707 97 PTGEIEIAATELLILNDSKvPPFSPAEEAIANEEVRLKyRYLDLRRPEMQHNFEVRHKVALAVRQYLSGQGFFEVETPFM 176
Cdd:PLN02603 176 GKQKVELKVSKIVVVGKSD-PSYPIQKKRVSREFLRTK-AHLRPRTNTFGAVARVRNALAYATHKFFQENGFVWVSSPII 253
|
....*...
gi 254781707 177 TRSTPEGA 184
Cdd:PLN02603 254 TASDCEGA 261
|
|
| |
