|
Name |
Accession |
Description |
Interval |
E-value |
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
16-510 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 891.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 16 QEENKLIAERRSKLDHIRKNcKANGHPNSFRRDSLAGDLQKKFGEKSKEELEALNHVVSIAGRVMAKRG----PFLVIQE 91
Cdd:PRK00484 1 EELNEQIAVRREKLAELREQ-GIDPYPNKFERTHTAAELRAKYDDKEKEELEELEIEVSVAGRVMLKRVmgkaSFATLQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 92 TSGRIQAYASK-EVQQELKDKYQGLDIGDIIGVQGALHKSGKGDLYVNMEQFQLLTKALRPLPEKFHGLTDQEMRYRQRY 170
Cdd:PRK00484 80 GSGRIQLYVSKdDVGEEALEAFKKLDLGDIIGVEGTLFKTKTGELSVKATELTLLTKSLRPLPDKFHGLTDVETRYRQRY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 171 VDLIVNENSRNAFIVRSKVMSAIRNFMISKQFMEVETPMMHVIPGGASARPFITHHNALDMPMYLRIAPELYLKRLVVGG 250
Cdd:PRK00484 160 VDLIVNPESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARPFITHHNALDIDLYLRIAPELYLKRLIVGG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 251 FDRVFEINRNFRNEGLSPRHNPEFTMMEFYMAYADYKDLMDLTEELLSSVALEVLGSTSMPYGEHTVEFGGKYARMSMFD 330
Cdd:PRK00484 240 FERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTYQGTEIDFGPPFKRLTMVD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 331 AIKHYnpnhaqiqalTEEDI--QNRDLMVSIAKSVHVDVEPFWTCGQLLEEIFGETAEPKLMQPTFITGYPADISPLARR 408
Cdd:PRK00484 320 AIKEY----------TGVDFddMTDEEARALAKELGIEVEKSWGLGKLINELFEEFVEPKLIQPTFITDYPVEISPLAKR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 409 SDDNPFFTDRFEFFIGGREVANGFSELNDAEDQDARFKAQVEAKESGDDEAMFYDADYITALEHGLPPTAGQGIGIDRLV 488
Cdd:PRK00484 390 HREDPGLTERFELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIGIDRLV 469
|
490 500
....*....|....*....|..
gi 446050909 489 MLLTNTHTIRDVILFPAMRPQQ 510
Cdd:PRK00484 470 MLLTDSPSIRDVILFPLMRPEK 491
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
15-510 |
0e+00 |
|
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: 826.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 15 AQEENKLIAERRSKLDHIRKNcKANGHPNSFRRDSLAGDLQKKFGEKSKEEleALNHVVSIAGRVMAKRG----PFLVIQ 90
Cdd:COG1190 4 EEDLNEQIRVRREKLEELREA-GIDPYPNKFPRTHTAAEIREKYDELEAEE--ETGDEVSVAGRIMAKRDmgkaSFADLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 91 ETSGRIQAYASK-EVQQELKDKYQGLDIGDIIGVQGALHKSGKGDLYVNMEQFQLLTKALRPLPEKFHGLTDQEMRYRQR 169
Cdd:COG1190 81 DGSGRIQLYLRRdELGEEAYELFKLLDLGDIVGVEGTVFRTKTGELSVKVEELTLLSKSLRPLPEKFHGLTDPETRYRQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 170 YVDLIVNENSRNAFIVRSKVMSAIRNFMISKQFMEVETPMMHVIPGGASARPFITHHNALDMPMYLRIAPELYLKRLVVG 249
Cdd:COG1190 161 YVDLIVNPEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 250 GFDRVFEINRNFRNEGLSPRHNPEFTMMEFYMAYADYKDLMDLTEELLSSVALEVLGSTSMPYGEHTVEFGGKYARMSMF 329
Cdd:COG1190 241 GFERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGTTKVTYQGQEIDLSPPWRRITMV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 330 DAIKHYNpnhaqiqALTEEDIQNRDLMVSIAKSVHVDVEPFWTCGQLLEEIFGETAEPKLMQPTFITGYPADISPLARRS 409
Cdd:COG1190 321 EAIKEAT-------GIDVTPLTDDEELRALAKELGIEVDPGWGRGKLIDELFEELVEPKLIQPTFVTDYPVEVSPLAKRH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 410 DDNPFFTDRFEFFIGGREVANGFSELNDAEDQDARFKAQVEAKESGDDEAMFYDADYITALEHGLPPTAGQGIGIDRLVM 489
Cdd:COG1190 394 RDDPGLTERFELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGLGIGIDRLVM 473
|
490 500
....*....|....*....|.
gi 446050909 490 LLTNTHTIRDVILFPAMRPQQ 510
Cdd:COG1190 474 LLTDSPSIRDVILFPLMRPEK 494
|
|
| lysS_bact |
TIGR00499 |
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ... |
17-509 |
0e+00 |
|
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the lysyl-tRNA synthetases that are class II amino-acyl tRNA synthetases. It includes all eukaryotic and most bacterial examples of the enzyme, but not archaeal or spirochete forms. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273107 [Multi-domain] Cd Length: 493 Bit Score: 632.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 17 EENKLIAERRSKLDHIRKNCKaNGHPNSFRRDSLAGDLQKKFGEKSKEELEALNHVVSIAGRVMAKRGP----FLVIQET 92
Cdd:TIGR00499 1 ELNDQAQQRLEKLNRLRQTGN-NPYLHKFERTHSAQEFQEKYADLSNEELKEKELKVSIAGRIKAIRSMgkatFITLQDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 93 SGRIQAYASKEVQQELKDKYQG--LDIGDIIGVQGALHKSGKGDLYVNMEQFQLLTKALRPLPEKFHGLTDQEMRYRQRY 170
Cdd:TIGR00499 80 SGQIQLYVNKNKLPEDFYEFDEylLDLGDIIGVTGYPFKTKTGELSVKVTELQILTKCLQPLPDKWHGLTDQETRYRQRY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 171 VDLIVNENSRNAFIVRSKVMSAIRNFMISKQFMEVETPMMHVIPGGASARPFITHHNALDMPMYLRIAPELYLKRLVVGG 250
Cdd:TIGR00499 160 LDLIVNPDVRQTFLKRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKPFITHHNALDMDLYLRIAPELYLKRLIVGG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 251 FDRVFEINRNFRNEGLSPRHNPEFTMMEFYMAYADYKDLMDLTEELLSSVALEVLGSTSMPYGEHTVEFGGKYARMSMFD 330
Cdd:TIGR00499 240 LEKVYEIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTFIINYNDLEIDLKPPWKRITMVD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 331 AIKhynpnhaQIQALTEEDIQNRDLMVSIAKSVHVDV-EPFWTCGQLLEEIFGETAEPKLMQPTFITGYPADISPLARRS 409
Cdd:TIGR00499 320 ALE-------MVTGIDFDILKDDETAKALAKEHGIEVaEDSLTLGHILNKFFEQFLEHTLIQPTFITHYPAEISPLAKRD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 410 DDNPFFTDRFEFFIGGREVANGFSELNDAEDQDARFKAQVEAKESGDDEAMFYDADYITALEHGLPPTAGQGIGIDRLVM 489
Cdd:TIGR00499 393 PSNPEFTERFELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGIGIDRLVM 472
|
490 500
....*....|....*....|
gi 446050909 490 LLTNTHTIRDVILFPAMRPQ 509
Cdd:TIGR00499 473 LLTDAPSIRDVLLFPQLRPQ 492
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
19-510 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 607.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 19 NKLIAERRSKLDHIRKNCKAngHPNSFRRDSLAGDLQKKFGEKSKEELEALNHVVSIAGRVMAKR----GPFLVIQETSG 94
Cdd:PRK12445 16 NDELRNRREKLAALRQQGVA--FPNDFRRDHTSDQLHEEFDAKDNQELESLNIEVSVAGRMMTRRimgkASFVTLQDVGG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 95 RIQAYASKEVQQE--LKDKYQGLDIGDIIGVQGALHKSGKGDLYVNMEQFQLLTKALRPLPEKFHGLTDQEMRYRQRYVD 172
Cdd:PRK12445 94 RIQLYVARDSLPEgvYNDQFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFHGLQDQEVRYRQRYLD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 173 LIVNENSRNAFIVRSKVMSAIRNFMISKQFMEVETPMMHVIPGGASARPFITHHNALDMPMYLRIAPELYLKRLVVGGFD 252
Cdd:PRK12445 174 LIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGFE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 253 RVFEINRNFRNEGLSPRHNPEFTMMEFYMAYADYKDLMDLTEELLSSVALEVLGSTSMPYGEHTVEFGGKYARMSMFDAI 332
Cdd:PRK12445 254 RVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFDFGKPFEKLTMREAI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 333 KHYNPNhaqiqaLTEEDIQNRDLMVSIAKSVHVDVEPFWTCGQLLEEIFGETAEPKLMQPTFITGYPADISPLARRSDDN 412
Cdd:PRK12445 334 KKYRPE------TDMADLDNFDAAKALAESIGITVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDVN 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 413 PFFTDRFEFFIGGREVANGFSELNDAEDQDARFKAQVEAKESGDDEAMFYDADYITALEHGLPPTAGQGIGIDRLVMLLT 492
Cdd:PRK12445 408 PEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFT 487
|
490
....*....|....*...
gi 446050909 493 NTHTIRDVILFPAMRPQQ 510
Cdd:PRK12445 488 NSHTIRDVILFPAMRPQK 505
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
3-510 |
0e+00 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 604.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 3 DAVQNEINQEQIAQEENKLIAERRSKldhirkncKANGHPNSFRRDSLAGDLQKKFGE-KSKEELEalNHVVSIAGRVMA 81
Cdd:PLN02502 50 AADDETMDPTQYRANRLKKVEALRAK--------GVEPYPYKFDVTHTAPELQEKYGSlENGEELE--DVSVSVAGRIMA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 82 KRG----PFLVIQETSGRIQAYASK----EVQQELKDKYQGLDIGDIIGVQGALHKSGKGDLYVNMEQFQLLTKALRPLP 153
Cdd:PLN02502 120 KRAfgklAFYDLRDDGGKIQLYADKkrldLDEEEFEKLHSLVDRGDIVGVTGTPGKTKKGELSIFPTSFEVLTKCLLMLP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 154 EKFHGLTDQEMRYRQRYVDLIVNENSRNAFIVRSKVMSAIRNFMISKQFMEVETPMMHVIPGGASARPFITHHNALDMPM 233
Cdd:PLN02502 200 DKYHGLTDQETRYRQRYLDLIANPEVRDIFRTRAKIISYIRRFLDDRGFLEVETPMLNMIAGGAAARPFVTHHNDLNMDL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 234 YLRIAPELYLKRLVVGGFDRVFEINRNFRNEGLSPRHNPEFTMMEFYMAYADYKDLMDLTEELLSSVALEVLGSTSMPYG 313
Cdd:PLN02502 280 YLRIATELHLKRLVVGGFERVYEIGRQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKELTGSYKIKYH 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 314 EHTVEFGGKYARMSMFDAIKHYNPnhAQIQALTEEDIQNRDLMVSIAKSVhVDVEPFWTCGQLLEEIFGETAEPKLMQPT 393
Cdd:PLN02502 360 GIEIDFTPPFRRISMISLVEEATG--IDFPADLKSDEANAYLIAACEKFD-VKCPPPQTTGRLLNELFEEFLEETLVQPT 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 394 FITGYPADISPLARRSDDNPFFTDRFEFFIGGREVANGFSELNDAEDQDARFKAQVEAKESGDDEAMFYDADYITALEHG 473
Cdd:PLN02502 437 FVLDHPVEMSPLAKPHRSKPGLTERFELFINGRELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYG 516
|
490 500 510
....*....|....*....|....*....|....*..
gi 446050909 474 LPPTAGQGIGIDRLVMLLTNTHTIRDVILFPAMRPQQ 510
Cdd:PLN02502 517 LPPTGGWGLGIDRLVMLLTDSASIRDVIAFPAMKPQD 553
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
176-508 |
0e+00 |
|
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: 552.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 176 NENSRNAFIVRSKVMSAIRNFMISKQFMEVETPMMHVIPGGASARPFITHHNALDMPMYLRIAPELYLKRLVVGGFDRVF 255
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 256 EINRNFRNEGLSPRHNPEFTMMEFYMAYADYKDLMDLTEELLSSVALEVLGSTSMPYGEHTVEFGGKYARMSMFDAIKHY 335
Cdd:cd00775 81 EIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIEYGGKELDFTPPFKRVTMVDALKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 336 NPnhaqIQALTEEDIQNRDLMVSIAKSVHVDVEPFWTCGQLLEEIFGETAEPKLMQPTFITGYPADISPLARRSDDNPFF 415
Cdd:cd00775 161 TG----IDFPELDLEQPEELAKLLAKLIKEKIEKPRTLGKLLDKLFEEFVEPTLIQPTFIIDHPVEISPLAKRHRSNPGL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 416 TDRFEFFIGGREVANGFSELNDAEDQDARFKAQVEAKESGDDEAMFYDADYITALEHGLPPTAGQGIGIDRLVMLLTNTH 495
Cdd:cd00775 237 TERFELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLTDSN 316
|
330
....*....|...
gi 446050909 496 TIRDVILFPAMRP 508
Cdd:cd00775 317 SIRDVILFPAMRP 329
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
25-510 |
1.68e-146 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 447.49 E-value: 1.68e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 25 RRSKLDHIRknckANG---HPNSFRRDSLAGDlqkkfgekskeELEALN-HVVSIAGRVMAKR--GP--FLVIQETSGRI 96
Cdd:PRK02983 617 RLAKLEALR----AAGvdpYPVGVPPTHTVAE-----------ALDAPTgEEVSVSGRVLRIRdyGGvlFADLRDWSGEL 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 97 QAY--ASKEVQQELKDKYQGLDIGDIIGVQGALHKSGKGDLYVNMEQFQLLTKALRPLPEKFHGLTDQEMRYRQRYVDLI 174
Cdd:PRK02983 682 QVLldASRLEQGSLADFRAAVDLGDLVEVTGTMGTSRNGTLSLLVTSWRLAGKCLRPLPDKWKGLTDPEARVRQRYLDLA 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 175 VNENSRNAFIVRSKVMSAIRNFMISKQFMEVETPMMHVIPGGASARPFITHHNALDMPMYLRIAPELYLKRLVVGGFDRV 254
Cdd:PRK02983 762 VNPEARDLLRARSAVVRAVRETLVARGFLEVETPILQQVHGGANARPFVTHINAYDMDLYLRIAPELYLKRLCVGGVERV 841
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 255 FEINRNFRNEGLSPRHNPEFTMMEFYMAYADYKDLMDLTEELLSSVALEVLGSTSMP-----YGEHTVEFGGKYARMSMF 329
Cdd:PRK02983 842 FELGRNFRNEGVDATHNPEFTLLEAYQAHADYDTMRDLTRELIQNAAQAAHGAPVVMrpdgdGVLEPVDISGPWPVVTVH 921
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 330 DAIKhynpnhaqiQALTEE---DIQNRDLMvSIAKSVHVDVEPFWTCGQLLEEIFGETAEPKLMQPTFITGYPADISPLA 406
Cdd:PRK02983 922 DAVS---------EALGEEidpDTPLAELR-KLCDAAGIPYRTDWDAGAVVLELYEHLVEDRTTFPTFYTDFPTSVSPLT 991
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 407 RRSDDNPFFTDRFEFFIGGREVANGFSELNDAEDQDARFKAQVEAKESGDDEAMFYDADYITALEHGLPPTAGQGIGIDR 486
Cdd:PRK02983 992 RPHRSDPGLAERWDLVAWGVELGTAYSELTDPVEQRRRLTEQSLLAAGGDPEAMELDEDFLQALEYAMPPTGGLGMGVDR 1071
|
490 500
....*....|....*....|....
gi 446050909 487 LVMLLTNThTIRDVILFPAMRPQQ 510
Cdd:PRK02983 1072 LVMLLTGR-SIRETLPFPLVKPRQ 1094
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
11-508 |
2.36e-130 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 390.91 E-value: 2.36e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 11 QEQIAQEENKLIAERRSKLDHIRKNCKANGHPNSFRRDSLAGDLQKKFGE-KSKEELEalNHVVSIAGRVM-----AKRG 84
Cdd:PTZ00417 74 KEEEAEVDPRLYYENRSKFIQEQKAKGINPYPHKFERTITVPEFVEKYQDlASGEHLE--DTILNVTGRIMrvsasGQKL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 85 PFLVIQETSGRIQAYASKEVQQELK----DKYQGLDIGDIIGVQGALHKSGKGDLYVNMEQFQLLTKALRPLPEKFhGLT 160
Cdd:PTZ00417 152 RFFDLVGDGAKIQVLANFAFHDHTKsnfaECYDKIRRGDIVGIVGFPGKSKKGELSIFPKETIILSPCLHMLPMKY-GLK 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 161 DQEMRYRQRYVDLIVNENSRNAFIVRSKVMSAIRNFMISKQFMEVETPMMHVIPGGASARPFITHHNALDMPMYLRIAPE 240
Cdd:PTZ00417 231 DTEIRYRQRYLDLMINESTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLVAGGANARPFITHHNDLDLDLYLRIATE 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 241 LYLKRLVVGGFDRVFEINRNFRNEGLSPRHNPEFTMMEFYMAYADYKDLMDLTEELLSSVALEVLGSTSMPYGEH----- 315
Cdd:PTZ00417 311 LPLKMLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHLFGTYKILYNKDgpekd 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 316 --TVEFGGKYARMSMFDAIKHYNPNHAQIQALTEEDIQNrdlMVSIAKSVHVDVEPFWTCGQLLEEI---FGETAEPKlm 390
Cdd:PTZ00417 391 piEIDFTPPYPKVSIVEELEKLTNTKLEQPFDSPETINK---MINLIKENKIEMPNPPTAAKLLDQLashFIENKYPN-- 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 391 QPTFITGYPADISPLARRSDDNPFFTDRFEFFIGGREVANGFSELNDAEDQDARFKAQVEAKESGDDEAMFYDADYITAL 470
Cdd:PTZ00417 466 KPFFIIEHPQIMSPLAKYHRSKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCTSL 545
|
490 500 510
....*....|....*....|....*....|....*...
gi 446050909 471 EHGLPPTAGQGIGIDRLVMLLTNTHTIRDVILFPAMRP 508
Cdd:PTZ00417 546 EYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFPTMRP 583
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
161-507 |
8.43e-121 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 356.88 E-value: 8.43e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 161 DQEMRYRQRYVDLiVNENSRNAFIVRSKVMSAIRNFMISKQFMEVETPMMHVIPGGASARPFITHHNALDMPMYLRIAPE 240
Cdd:pfam00152 1 DEETRLKYRYLDL-RRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 241 LYLKRLVVGGFDRVFEINRNFRNEGLSPRHNPEFTMMEFYMAYADYKDLMDLTEELLSSVALEVLGSTSMPYGEHTVEFG 320
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 321 GKYARMSMFDAIKHYNPNHAQiqaLTEEDIQNRDLMVSIAKsvhvdvepfwtcgQLLEEIFgetaepklmQPTFITGYPA 400
Cdd:pfam00152 160 KPFPRITYAEAIEKLNGKDVE---ELGYGSDKPDLRFLLEL-------------VIDKNKF---------NPLWVTDFPA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 401 DISPLARRSD-DNPFFTDRFEFFIGGREVANGFSELNDAEDQDARFKAQVEAKEsgddEAMFYDADYITALEHGLPPTAG 479
Cdd:pfam00152 215 EHHPFTMPKDeDDPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDPE----EAEEKFGFYLDALKYGAPPHGG 290
|
330 340
....*....|....*....|....*...
gi 446050909 480 QGIGIDRLVMLLTNTHTIRDVILFPAMR 507
Cdd:pfam00152 291 LGIGLDRLVMLLTGLESIREVIAFPKTR 318
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
183-508 |
4.47e-118 |
|
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: 348.31 E-value: 4.47e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 183 FIVRSKVMSAIRNFMISKQFMEVETPMMHVIPGGASARPFITHHNALDMPMYLRIAPELYLKRLVVGGFDRVFEINRNFR 262
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 263 NEGLSPRHNPEFTMMEFYMAYADYKDLMDLTEELLSSVALEVLGSTSMPYGEHTVEFGGKYARMSMFDAIKhynpnhaqi 342
Cdd:cd00669 81 NEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYGFELEDFGLPFPRLTYREALE--------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 343 qalteediqnrdlmvsiaksvhvdvepfwtcgqlleeifgetaepKLMQPTFITGYPADI-SPLARRSDDNPFFTDRFEF 421
Cdd:cd00669 152 ---------------------------------------------RYGQPLFLTDYPAEMhSPLASPHDVNPEIADAFDL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 422 FIGGREVANGFSELNDAEDQDARFKAQVEAKESGddeaMFYDADYITALEHGLPPTAGQGIGIDRLVMLLTNTHTIRDVI 501
Cdd:cd00669 187 FINGVEVGNGSSRLHDPDIQAEVFQEQGINKEAG----MEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVI 262
|
....*..
gi 446050909 502 LFPAMRP 508
Cdd:cd00669 263 AFPKMRR 269
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
33-507 |
3.73e-104 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 325.83 E-value: 3.73e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 33 RKNCKANGHPNSFRRDSLAGDLQKKFGEKSKEELEAlNHVVSIAGRVMAKRGP----FLVIQETSGRIQAY---ASKEVQ 105
Cdd:PTZ00385 71 RSKLDLPAAYSSFRGITPISEVRERYGYLASGDRAA-QATVRVAGRVTSVRDIgkiiFVTIRSNGNELQVVgqvGEHFTR 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 106 QELKDKYQGLDIGDIIGVQGALHKSGKGDLYVNMEQFQLLT------KALRPLPEKFHGLTDQEMRYRQRYVDLIVNENS 179
Cdd:PTZ00385 150 EDLKKLKVSLRVGDIIGADGVPCRMQRGELSVAASRMLILSpyvctdQVVCPNLRGFTVLQDNDVKYRYRFTDMMTNPCV 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 180 RNAFIVRSKVMSAIRNFMISKQFMEVETPMMHVIPGGASARPFITHHNALDMPMYLRIAPELYLKRLVVGGFDRVFEINR 259
Cdd:PTZ00385 230 IETIKKRHVMLQALRDYFNERNFVEVETPVLHTVASGANAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERIYEIGK 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 260 NFRNEGLSPRHNPEFTMMEFYMAYADYKDLMDLTEELLSSVALEVLGSTSM---PYGEH----TVEFGGKYARMSMFDAI 332
Cdd:PTZ00385 310 VFRNEDADRSHNPEFTSCEFYAAYHTYEDLMPMTEDIFRQLAMRVNGTTVVqiyPENAHgnpvTVDLGKPFRRVSVYDEI 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 333 KHYN------PNHAQiqalTEEDIQnrdLMVSIAKSVHVDVEPFWTCGQLLEEIFGETAEPKLMQPTFITGYPADISPLA 406
Cdd:PTZ00385 390 QRMSgvefppPNELN----TPKGIA---YMSVVMLRYNIPLPPVRTAAKMFEKLIDFFITDRVVEPTFVMDHPLFMSPLA 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 407 RRSDDNPFFTDRFEFFIGGREVANGFSELNDAEDQDARFKAQVEAKESGDDEAMFYDADYITALEHGLPPTAGQGIGIDR 486
Cdd:PTZ00385 463 KEQVSRPGLAERFELFVNGIEYCNAYSELNDPHEQYHRFQQQLVDRQGGDEEAMPLDETFLKSLQVGLPPTAGWGMGIDR 542
|
490 500
....*....|....*....|.
gi 446050909 487 LVMLLTNTHTIRDVILFPAMR 507
Cdd:PTZ00385 543 ALMLLTNSSNIRDGIIFPLLR 563
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
179-501 |
2.29e-77 |
|
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441870 [Multi-domain] Cd Length: 309 Bit Score: 245.02 E-value: 2.29e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 179 SRNAFIVRSKVMSAIRNFMISKQFMEVETPMMHVIPGG-ASARPFIT---HHNALDMPMYLRIAPELYLKRLVVGGFDRV 254
Cdd:COG2269 2 SREALRARARLLAAIRAFFAERGVLEVETPALSVAPGTdPHLDSFATefiGPDGGGRPLYLHTSPEFAMKRLLAAGSGPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 255 FEINRNFRNEGLSPRHNPEFTMMEFYMAYADYKDLMDLTEELLSSVAlevlgstsMPYGEHTVEfggkyaRMSMFDAIKH 334
Cdd:COG2269 82 YQIAKVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVL--------GAAGFAPAE------RLSYQEAFLR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 335 ynpnHAQIQALTEediqNRDLMVSIAKSVHVDVEPFWTCGQLLEEIFGETAEPKLMQ--PTFITGYPADISPLARRSDDN 412
Cdd:COG2269 148 ----YLGIDPLTA----DLDELAAAAAAAGLRVADDDDRDDLLDLLLSERVEPQLGRdrPTFLYDYPASQAALARISPDD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 413 PFFTDRFEFFIGGREVANGFSELNDAEDQDARFKAQVEAKESGDDEAMFYDADYITALEHGLPPTAGQGIGIDRLVMLLT 492
Cdd:COG2269 220 PRVAERFELYACGVELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLAL 299
|
....*....
gi 446050909 493 NTHTIRDVI 501
Cdd:COG2269 300 GAERIDDVL 308
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
196-501 |
6.98e-71 |
|
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: 227.82 E-value: 6.98e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 196 FMISKQFMEVETPMMhvIPGGASA---RPFITH---HNALDMPMYLRIAPELYLKRLVVGGFDRVFEINRNFRNEGLSPR 269
Cdd:TIGR00462 1 FFAERGVLEVETPLL--SPAPVTDphlDAFATEfvgPDGQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 270 HNPEFTMMEFYMAYADYKDLMDLTEELLSsvalEVLGSTSMPygehtVEfggkyaRMSMFDAIKhynpNHAQIQALTEED 349
Cdd:TIGR00462 79 HNPEFTMLEWYRPGFDYHDLMDEVEALLQ----ELLGDPFAP-----AE------RLSYQEAFL----RYAGIDPLTASL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 350 IQNRDLMVsiAKSVHVDVEPFWTcgQLLEEIFGETAEPKLMQ--PTFITGYPADISPLARRSDDNPFFTDRFEFFIGGRE 427
Cdd:TIGR00462 140 AELQAAAA--AHGIRASEEDDRD--DLLDLLFSEKVEPHLGFgrPTFLYDYPASQAALARISPDDPRVAERFELYIKGLE 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446050909 428 VANGFSELNDAEDQDARFKAQVEAKESGDDEAMFYDADYITALEHGLPPTAGQGIGIDRLVMLLTNTHTIRDVI 501
Cdd:TIGR00462 216 LANGFHELTDAAEQRRRFEADNALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDVL 289
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
186-500 |
3.75e-57 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 192.45 E-value: 3.75e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 186 RSKVMSAIRNFMISKQFMEVETPMM--------HVIPggASARpFITHHNALDMPMYLRIAPELYLKRLVVGGFDRVFEI 257
Cdd:PRK09350 8 RAKIIAEIRRFFADRGVLEVETPILsqatvtdiHLVP--FETR-FVGPGASQGKTLWLMTSPEYHMKRLLAAGSGPIFQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 258 NRNFRNEGLSPRHNPEFTMMEFYMAYADYKDLMDLTEELLSsvalEVLGSTSmpygehtvefggkYARMSMFDAIKhynp 337
Cdd:PRK09350 85 CKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQ----QVLDCEP-------------AESLSYQQAFL---- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 338 NHAQIQALTEEDIQNRDLMVSIAKSVHVDVEPFWTcgQLLEEIFGETAEPKLMQ--PTFITGYPADISPLARRSDDNPFF 415
Cdd:PRK09350 144 RYLGIDPLSADKTQLREVAAKLGLSNIADEEEDRD--TLLQLLFTFGVEPNIGKekPTFVYHFPASQAALAKISTEDHRV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 416 TDRFEFFIGGREVANGFSELNDAEDQDARFKAQVEAKESGDDEAMFYDADYITALEHGLPPTAGQGIGIDRLVMLLTNTH 495
Cdd:PRK09350 222 AERFEVYFKGIELANGFHELTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCSGVALGVDRLIMLALGAE 301
|
....*
gi 446050909 496 TIRDV 500
Cdd:PRK09350 302 SISEV 306
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
73-173 |
8.43e-47 |
|
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: 158.02 E-value: 8.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 73 VSIAGRVMAKRGP----FLVIQETSGRIQAYASKEV--QQELKDKYQGLDIGDIIGVQGALHKSGKGDLYVNMEQFQLLT 146
Cdd:cd04322 2 VSVAGRIMSKRGSgklsFADLQDESGKIQVYVNKDDlgEEEFEDFKKLLDLGDIIGVTGTPFKTKTGELSIFVKEFTLLS 81
|
90 100
....*....|....*....|....*..
gi 446050909 147 KALRPLPEKFHGLTDQEMRYRQRYVDL 173
Cdd:cd04322 82 KSLRPLPEKFHGLTDVETRYRQRYLDL 108
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
86-504 |
6.25e-42 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 155.35 E-value: 6.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 86 FLVIQETSGRIQAYASKEVQQELKDKYQGLDIGDIIGVQGALHKSGK--GDLYVNMEQFQLLTKALRPLPEKFHGLTDQE 163
Cdd:PRK05159 36 FLILRDRSGIIQVVVKKKVDEELFETIKKLKRESVVSVTGTVKANPKapGGVEVIPEEIEVLNKAEEPLPLDISGKVLAE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 164 M--RYRQRYVDLiVNENSRNAFIVRSKVMSAIRNFMISKQFMEVETPmmHVIP----GGASARPfITHhnaLDMPMYLRI 237
Cdd:PRK05159 116 LdtRLDNRFLDL-RRPRVRAIFKIRSEVLRAFREFLYENGFTEIFTP--KIVAsgteGGAELFP-IDY---FEKEAYLAQ 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 238 APELYLKRLVVGGFDRVFEINRNFRNEGL-SPRHNPEFTMMEFYMAYAD-YKDLMDLTEELLSSV----------ALEVL 305
Cdd:PRK05159 189 SPQLYKQMMVGAGFERVFEIGPVFRAEEHnTSRHLNEYTSIDVEMGFIDdHEDVMDLLENLLRYMyedvaencekELELL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 306 GST-SMPYGEhtvefggkyarmsmFDAIKHynpnhaqiqaltEEDIQnrdlmvsIAKSVHVDVEP---FWTCGQ-LLEEI 380
Cdd:PRK05159 269 GIElPVPETP--------------IPRITY------------DEAIE-------ILKSKGNEISWgddLDTEGErLLGEY 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 381 FGETAEPKLMqptFITGYPADISPL-ARRSDDNPFFTDRFEFFIGGREVANGFSELNDAEDQDARFKAQveakesGDDEA 459
Cdd:PRK05159 316 VKEEYGSDFY---FITDYPSEKRPFyTMPDEDDPEISKSFDLLFRGLEITSGGQRIHRYDMLVESIKEK------GLNPE 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 446050909 460 MFydADYITALEHGLPPTAGQGIGIDRLVMLLTNTHTIRDVILFP 504
Cdd:PRK05159 387 SF--EFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFP 429
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
161-504 |
1.78e-41 |
|
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: 151.18 E-value: 1.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 161 DQEMRYRQRYVDLIVNENSRnAFIVRSKVMSAIRNFMISKQFMEVETPMMHVIP--GGASARPFithhNALDMPMYLRIA 238
Cdd:cd00776 3 NLETLLDNRHLDLRTPKVQA-IFRIRSEVLRAFREFLRENGFTEVHTPKITSTDteGGAELFKV----SYFGKPAYLAQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 239 PELYlKRLVVGGFDRVFEINRNFRNE-GLSPRHNPEFTMMEFYMAYA-DYKDLMDLTEELLSSVALEVL------GSTSM 310
Cdd:cd00776 78 PQLY-KEMLIAALERVYEIGPVFRAEkSNTRRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLercakeLELVN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 311 PYGEHTVEFGGKYARMSMFDAIKhynpnhaqiqalteediqnrdlmvsIAKSVHVDVEPFWtcgqllEEIFGETAEPKLM 390
Cdd:cd00776 157 QLNRELLKPLEPFPRITYDEAIE-------------------------LLREKGVEEEVKW------GEDLSTEHERLLG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 391 Q-----PTFITGYPADISPL-ARRSDDNPFFTDRFEFFI-GGREVANGFSELNDAEDQDARFKAQveakesGDDEAMFYD 463
Cdd:cd00776 206 EivkgdPVFVTDYPKEIKPFyMKPDDDNPETVESFDLLMpGVGEIVGGSQRIHDYDELEERIKEH------GLDPESFEW 279
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 446050909 464 adYITALEHGLPPTAGQGIGIDRLVMLLTNTHTIRDVILFP 504
Cdd:cd00776 280 --YLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
73-507 |
8.67e-38 |
|
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: 143.65 E-value: 8.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 73 VSIAGRVMAKRGP----FLVIQETSGRIQAYASKEVQqELKDKYQGLDIGDIIGVQGALHKSG--KGDLYVNMEQFQLLT 146
Cdd:COG0017 17 VTVAGWVRTKRDSggisFLILRDGSGFIQVVVKKDKL-ENFEEAKKLTTESSVEVTGTVVESPraPQGVELQAEEIEVLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 147 KALRPLP--EKFHGLtdqEMRYRQRYVDLIVNENsRNAFIVRSKVMSAIRNFMISKQFMEVETPMMhvIP----GGASAR 220
Cdd:COG0017 96 EADEPYPlqPKRHSL---EFLLDNRHLRLRTNRF-GAIFRIRSELARAIREFFQERGFVEVHTPII--TAsateGGGELF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 221 P---FithhnalDMPMYLRIAPELYlKRLVVGGFDRVFEINRNFRNEgLS--PRHNPEFTMMEFYMAYADYKDLMDLTEE 295
Cdd:COG0017 170 PvdyF-------GKEAYLTQSGQLY-KEALAMALEKVYTFGPTFRAE-KSntRRHLAEFWMIEPEMAFADLEDVMDLAEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 296 LLSSV----------ALEVLGSTSMPYgEHTVEfgGKYARMSMFDAIKhynpnhaqiqalteediqnrdlmvsIAKSVHV 365
Cdd:COG0017 241 MLKYIikyvlencpeELEFLGRDVERL-EKVPE--SPFPRITYTEAIE-------------------------ILKKSGE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 366 DVEpfWtcG---------QLLEEIFGEtaepklmqPTFITGYPADISPL-ARRSDDNPFFTDRF--------EFfIGG-- 425
Cdd:COG0017 293 KVE--W--GddlgteherYLGEEFFKK--------PVFVTDYPKEIKAFyMKPNPDDPKTVAAFdllapgigEI-IGGsq 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 426 REvangfselNDAEDQDARFKaqveakESGDDEAMFYDadYITALEHGLPPTAGQGIGIDRLVMLLTNTHTIRDVILFPA 505
Cdd:COG0017 360 RE--------HRYDVLVERIK------EKGLDPEDYEW--YLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPR 423
|
..
gi 446050909 506 MR 507
Cdd:COG0017 424 DP 425
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
183-504 |
4.11e-34 |
|
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: 130.00 E-value: 4.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 183 FIVRSKVMSAIRNFMISKQFMEVETPMM-HVIPGGAsaRPFI----THHN---ALDMpmylriAPELYLKRLVVGGFDRV 254
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILtKSTPEGA--RDFLvpsrLHPGkfyALPQ------SPQLFKQLLMVSGFDRY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 255 FEINRNFRNEGLSPRHNPEFTMMEFYMAYADYKDLMDLTEELLSSVALEVLGstsmpygehtVEFGGKYARMSMFDAIKH 334
Cdd:cd00777 73 FQIARCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG----------VELTTPFPRMTYAEAMER 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 335 YNPNHAQIQ--ALTEEDIQNRDLMvsiakSVHvdvEPFwtcgqlleeifgeTAePKLMQPTFITGYPADIspLARRSDdn 412
Cdd:cd00777 143 YGFKFLWIVdfPLFEWDEEEGRLV-----SAH---HPF-------------TA-PKEEDLDLLEKDPEDA--RAQAYD-- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 413 pfftdrfeFFIGGREVANGFSELNDAEDQDARFKAQVEAKESGDDEAMFydadYITALEHGLPPTAGQGIGIDRLVMLLT 492
Cdd:cd00777 197 --------LVLNGVELGGGSIRIHDPDIQEKVFEILGLSEEEAEEKFGF----LLEAFKYGAPPHGGIALGLDRLVMLLT 264
|
330
....*....|..
gi 446050909 493 NTHTIRDVILFP 504
Cdd:cd00777 265 GSESIRDVIAFP 276
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
8-504 |
5.79e-27 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 114.03 E-value: 5.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 8 EINQEQIAQEENKLIAERRSKLDHIRKNcKANGHPNSFRRDSLAG--------DLQKKFGEKSKEELEALNH-----VVS 74
Cdd:PLN02850 7 EESGEKISKKAAKKAAAKAEKLRREATA-KAAAASLEDEDDPLASnygdvpleELQSKVTGREWTDVSDLGEelagsEVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 75 IAGRVMAKRG----PFLVIQETSGRIQ--AYASKEVQQELKDKY-QGL---DIGDIIGVQGALHKSGKG---DLYVNMEQ 141
Cdd:PLN02850 86 IRGRVHTIRGkgksAFLVLRQSGFTVQcvVFVSEVTVSKGMVKYaKQLsreSVVDVEGVVSVPKKPVKGttqQVEIQVRK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 142 FQLLTKALRPLP-----------EKFHGLTD--------QEMRYRQRYVDLIVNENsrNA-FIVRSKVMSAIRNFMISKQ 201
Cdd:PLN02850 166 IYCVSKALATLPfnvedaarsesEIEKALQTgeqlvrvgQDTRLNNRVLDLRTPAN--QAiFRIQSQVCNLFREFLLSKG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 202 FMEVETPMmhvIPGGAS---ARPFITHHNAldMPMYLRIAPELYLKRLVVGGFDRVFEINRNFRNE-GLSPRHNPEFTMM 277
Cdd:PLN02850 244 FVEIHTPK---LIAGASeggSAVFRLDYKG--QPACLAQSPQLHKQMAICGDFRRVFEIGPVFRAEdSFTHRHLCEFTGL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 278 EFYMAYAD-YKDLMDLTEELLSSV----------ALEVLGSTsmpYGEHTVEFGGKYARMSMfdaikhynpnhaqiqalt 346
Cdd:PLN02850 319 DLEMEIKEhYSEVLDVVDELFVAIfdglnerckkELEAIREQ---YPFEPLKYLPKTLRLTF------------------ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 347 EEDIQnrdlmvsIAKSVHVDVEPFWTCGQLLEEIFGETAEPKLMQPTFI-TGYPADISPLARRSD-DNPFFTDRFEFFIG 424
Cdd:PLN02850 378 AEGIQ-------MLKEAGVEVDPLGDLNTESERKLGQLVKEKYGTDFYIlHRYPLAVRPFYTMPCpDDPKYSNSFDVFIR 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 425 GREVANGFSELNDAEDQDARfkaqveAKESGDDEAMFydADYITALEHGLPPTAGQGIGIDRLVMLLTNTHTIRDVILFP 504
Cdd:PLN02850 451 GEEIISGAQRVHDPELLEKR------AEECGIDVKTI--STYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFP 522
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
151-504 |
4.55e-24 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 105.53 E-value: 4.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 151 PLPEKFHGLTDQEMRYRQRYVDLIVNENSRNaFIVRSKVMSAIRNFMISKQFMEVETPMMhvipgGAS----ARPFI--- 223
Cdd:PRK00476 110 PFPIDDEEDVSEELRLKYRYLDLRRPEMQKN-LKLRSKVTSAIRNFLDDNGFLEIETPIL-----TKStpegARDYLvps 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 224 -THHN---ALdmPMylriAPELYLKRLVVGGFDRVFEINRNFRNEGLspRHN--PEFTMMEFYMAYADYKDLMDLTEELL 297
Cdd:PRK00476 184 rVHPGkfyAL--PQ----SPQLFKQLLMVAGFDRYYQIARCFRDEDL--RADrqPEFTQIDIEMSFVTQEDVMALMEGLI 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 298 SSVALEVLGstsmpygehtVEFGGKYARMSMFDAIKHY------------------------------------------ 335
Cdd:PRK00476 256 RHVFKEVLG----------VDLPTPFPRMTYAEAMRRYgsdkpdlrfglelvdvtdlfkdsgfkvfagaandggrvkair 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 336 ------NPNHAQIQALTEE------------DIQNRDLMVSIAKSVHVDVepfwtcgqlLEEIFGET-AEPK--LMqptF 394
Cdd:PRK00476 326 vpggaaQLSRKQIDELTEFakiygakglayiKVNEDGLKGPIAKFLSEEE---------LAALLERTgAKDGdlIF---F 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 395 ITGYPADISP--------LARRSD-------------DNPFF-----TDRFEF----F---IGGRE-------------- 427
Cdd:PRK00476 394 GADKAKVVNDalgalrlkLGKELGlidedkfaflwvvDFPMFeydeeEGRWVAahhpFtmpKDEDLdelettdpgkaray 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 428 ----VANGFsEL-------NDAEDQDARFKA----QVEAKES-GddeaMFYDadyitALEHGLPPTAGQGIGIDRLVMLL 491
Cdd:PRK00476 474 aydlVLNGY-ELgggsiriHRPEIQEKVFEIlgisEEEAEEKfG----FLLD-----ALKYGAPPHGGIAFGLDRLVMLL 543
|
490
....*....|...
gi 446050909 492 TNTHTIRDVILFP 504
Cdd:PRK00476 544 AGADSIRDVIAFP 556
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
62-504 |
1.15e-22 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 101.22 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 62 SKEELeaLNHVVSIAGRVMAKRG----PFLVIQETSGRIQAYA--SKEVQQELKDKYQGLDIGDIIGVQGALHK------ 129
Cdd:PTZ00401 72 SKPEL--VDKTVLIRARVSTTRKkgkmAFMVLRDGSDSVQAMAavEGDVPKEMIDFIGQIPTESIVDVEATVCKveqpit 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 130 -SGKGDLYVNMEQFQLLTKALRPLPEKFHGLTDQE----------MRYRQRYVDLiVNENSRNAFIVRSKVMSAIRNFMI 198
Cdd:PTZ00401 150 sTSHSDIELKVKKIHTVTESLRTLPFTLEDASRKEsdegakvnfdTRLNSRWMDL-RTPASGAIFRLQSRVCQYFRQFLI 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 199 SKQFMEVETPMMHVIPGGASARPFITHHnaLDMPMYLRIAPELYLKRLVVGGFDRVFEINRNFRNEGLSP-RHNPEFTMM 277
Cdd:PTZ00401 229 DSDFCEIHSPKIINAPSEGGANVFKLEY--FNRFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNThRHLTEFVGL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 278 EFYMAYAD-YKDLMDLTEELLSSVaLEVLGStsmpygeHTVEfggkyarmsmFDAIKHYNPNHAQIQALTEEDIqnRDLM 356
Cdd:PTZ00401 307 DVEMRINEhYYEVLDLAESLFNYI-FERLAT-------HTKE----------LKAVCQQYPFEPLVWKLTPERM--KELG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 357 VSIaksVHVDVEP-------------------FWTCGQLLEEIFGETAEP-------------KLMQPTFITG-YPADIS 403
Cdd:PTZ00401 367 VGV---ISEGVEPtdkyqarvhnmdsrmlrinYMHCIELLNTVLEEKMAPtddinttnekllgKLVKERYGTDfFISDRF 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 404 PLARRS------DDNPFFTDRFEFFIGGREVANGFSELNDAEDQDARfkaqveAKESGDDEAMFydADYITALEHGLPPT 477
Cdd:PTZ00401 444 PSSARPfytmecKDDERFTNSYDMFIRGEEISSGAQRIHDPDLLLAR------AKMLNVDLTPI--KEYVDSFRLGAWPH 515
|
490 500
....*....|....*....|....*..
gi 446050909 478 AGQGIGIDRLVMLLTNTHTIRDVILFP 504
Cdd:PTZ00401 516 GGFGVGLERVVMLYLGLSNVRLASLFP 542
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
161-507 |
8.98e-22 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 98.91 E-value: 8.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 161 DQEMRYRQRYVDLIVNENSRNaFIVRSKVMSAIRNFMISKQFMEVETPMMHV-IPGGAsaRPFITHHNALDMPMY-LRIA 238
Cdd:PRK12820 135 NEDLRLQYRYLDIRRPAMQDH-LAKRHRIIKCARDFLDSRGFLEIETPILTKsTPEGA--RDYLVPSRIHPKEFYaLPQS 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 239 PELYLKRLVVGGFDRVFEINRNFRNEGLSPRHNPEFTMMEFYMAYADYKDLMDLTEELLSSVaLEVLGST------SMPY 312
Cdd:PRK12820 212 PQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEFTQLDIEASFIDEEFIFELIEELTARM-FAIGGIAlprpfpRMPY 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 313 GEHT---------VEFGGKYA---------RMSMFDAI-----------------------------KHYNPNHAQ---- 341
Cdd:PRK12820 291 AEAMdttgsdrpdLRFDLKFAdatdifentRYGIFKQIlqrggrikginikgqseklsknvlqneyaKEIAPSFGAkgmt 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 342 -------------IQALTEED---------IQNRDLMVSIAKSVHVDVEPfwTCGQL---LEEIFGeTAEPKLMQPTFIT 396
Cdd:PRK12820 371 wmraeaggldsniVQFFSADEkealkrrfhAEDGDVIIMIADASCAIVLS--ALGQLrlhLADRLG-LIPEGVFHPLWIT 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 397 GYP--ADISPLARRSDDNPFFT-DRFEF------------------FIGGREVANGFSELNDAEDQDARFKAQVEAKESG 455
Cdd:PRK12820 448 DFPlfEATDDGGVTSSHHPFTApDREDFdpgdieelldlrsraydlVVNGEELGGGSIRINDKDIQLRIFAALGLSEEDI 527
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 446050909 456 DDEAMFydadYITALEHGLPPTAGQGIGIDRLVMLLTNTHTIRDVILFPAMR 507
Cdd:PRK12820 528 EDKFGF----FLRAFDFAAPPHGGIALGLDRVVSMILQTPSIREVIAFPKNR 575
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
185-298 |
1.07e-21 |
|
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: 93.34 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 185 VRSKVMSAIRNFMISKQFMEVETPMMHVIPGGASAR----PFITHHNALDMPMYLRIAPELYLKRLVVG----GFDRVFE 256
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGhepkDLLPVGAENEEDLYLRPTLEPGLVRLFVShirkLPLRLAE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 446050909 257 INRNFRNEGLS--PRHNPEFTMMEFYMAYAD------YKDLMDLTEELLS 298
Cdd:cd00768 81 IGPAFRNEGGRrgLRRVREFTQLEGEVFGEDgeeaseFEELIELTEELLR 130
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
163-504 |
1.13e-21 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 95.86 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 163 EMRYRQRYVDL-------IVNENSRNAFIVRSKVMSAIRNFMISKQFMEVETPMMHVI-----PGGASARPFITHHNALD 230
Cdd:PRK06462 3 LERYPKEYEEFlrmswkhISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIISPStdplmGLGSDLPVKQISIDFYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 231 MPMYLRIAPELYlKRLVVGGFDRVFEINRNFRNEGLSP---RHNPEFTMMEFYMAYADYKDLMDLTEELLSSVALEVLgs 307
Cdd:PRK06462 83 VEYYLADSMILH-KQLALRMLGKIFYLSPNFRLEPVDKdtgRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELL-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 308 tsmPYGEHTVEFGGKyarmsmfdAIKHYNPNhaqIQALTEEDIqnrdlmVSIAKSVHVDVEPF----WTCGQLLEEIFGE 383
Cdd:PRK06462 160 ---EEHEDELEFFGR--------DLPHLKRP---FKRITHKEA------VEILNEEGCRGIDLeelgSEGEKSLSEHFEE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 384 taepklmqPTFITGYPADISPlarrsddnpfFTDRFEFFIGGREVA------NGFSELNDAEDQDARFKAQVEA-KESGD 456
Cdd:PRK06462 220 --------PFWIIDIPKGSRE----------FYDREDPERPGVLRNydlllpEGYGEAVSGGEREYEYEEIVERiREHGV 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 446050909 457 DEAMFydADYITALEHGLPPTAGQGIGIDRLVMLLTNTHTIRDVILFP 504
Cdd:PRK06462 282 DPEKY--KWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQPFP 327
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
160-504 |
6.24e-21 |
|
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: 96.22 E-value: 6.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 160 TDQEMRYRQRYVDLiVNENSRNAFIVRSKVMSAIRNFMISKQFMEVETPMMhvipgGAS----ARPFI----THHN---A 228
Cdd:COG0173 120 VSEELRLKYRYLDL-RRPEMQKNLILRHKVTKAIRNYLDENGFLEIETPIL-----TKStpegARDYLvpsrVHPGkfyA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 229 LdmPMylriAPELYLKRLVVGGFDRVFEINRNFRNEGLspRHN--PEFTM--MEfyMAYADYKDLMDLTEELLSSVALEV 304
Cdd:COG0173 194 L--PQ----SPQLFKQLLMVSGFDRYFQIARCFRDEDL--RADrqPEFTQldIE--MSFVDQEDVFELMEGLIRHLFKEV 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 305 LG---STSMP----------YG----------EHT--------VEF--------------------GGKYARmSMFDAIK 333
Cdd:COG0173 264 LGvelPTPFPrmtyaeamerYGsdkpdlrfglELVdvtdifkdSGFkvfagaaenggrvkainvpgGASLSR-KQIDELT 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 334 HYnpnhAQIQ--------ALTEEDIQNrdlmvSIAKSVHVDVepfwtcgqlLEEIFGET-AEPK--LMqptFITGYPADI 402
Cdd:COG0173 343 EF----AKQYgakglayiKVNEDGLKS-----PIAKFLSEEE---------LAAILERLgAKPGdlIF---FVADKPKVV 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 403 SP--------LARRSD-------------DNPFF-----TDRFEF----F---IGGRE-----------------VANGF 432
Cdd:COG0173 402 NKalgalrlkLGKELGlidedefaflwvvDFPLFeydeeEGRWVAmhhpFtmpKDEDLdlletdpgkvrakaydlVLNGY 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 433 sEL-------NDAEDQDARFKA----QVEAKES-GddeaMFYDadyitALEHGLPPTAGQGIGIDRLVMLLTNTHTIRDV 500
Cdd:COG0173 482 -ELgggsiriHDPELQEKVFELlgisEEEAEEKfG----FLLE-----AFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDV 551
|
....
gi 446050909 501 ILFP 504
Cdd:COG0173 552 IAFP 555
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
85-335 |
3.02e-20 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 94.08 E-value: 3.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 85 PFLVIQETSGRIQAYASKEVQQELKDKYQGLDIGDIIGVQGALHKSGKGDLYVNM---------EQFQLLTKALRPLPEK 155
Cdd:PLN02903 91 TFLDVRDHTGIVQVVTLPDEFPEAHRTANRLRNEYVVAVEGTVRSRPQESPNKKMktgsvevvaESVDILNVVTKSLPFL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 156 FHGLTDQ------EMRYRQRYVDLIVNENSRNaFIVRSKVMSAIRNFMISKQ-FMEVETPMMhvipggasARPfiTHHNA 228
Cdd:PLN02903 171 VTTADEQkdsikeEVRLRYRVLDLRRPQMNAN-LRLRHRVVKLIRRYLEDVHgFVEIETPIL--------SRS--TPEGA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 229 LDMPMYLRI----------APELYLKRLVVGGFDRVFEINRNFRNEGLSPRHNPEFTMMEFYMAYADYKDLMDLTEELLS 298
Cdd:PLN02903 240 RDYLVPSRVqpgtfyalpqSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEFTQLDMELAFTPLEDMLKLNEDLIR 319
|
250 260 270
....*....|....*....|....*....|....*..
gi 446050909 299 SVALEVLGstsmpygehtVEFGGKYARMSMFDAIKHY 335
Cdd:PLN02903 320 QVFKEIKG----------VQLPNPFPRLTYAEAMSKY 346
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
73-504 |
1.61e-12 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 69.37 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 73 VSIAGRVMAKRGP----FLVIQETSGRIQAYASKEVQQELKDKYQGLDIGDIIGVQGALHKS-GKGDLY-VNMEQFQLLT 146
Cdd:PRK03932 19 VTVRGWVRTKRDSgkiaFLQLRDGSCFKQLQVVKDNGEEYFEEIKKLTTGSSVIVTGTVVESpRAGQGYeLQATKIEVIG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 147 KALR--PLPEKFHGL-TDQEMRY-RQRyvdlivnENSRNA-FIVRSKVMSAIRNFMISKQFMEVETPMM-HVIPGGASAR 220
Cdd:PRK03932 99 EDPEdyPIQKKRHSIeFLREIAHlRPR-------TNKFGAvMRIRNTLAQAIHEFFNENGFVWVDTPIItASDCEGAGEL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 221 pFITHHNALDM-------PMYLRIAPELYLKRLVVGgFDRVFEINRNFRNEGlS--PRHNPEFTMMEFYMAYADYKDLMD 291
Cdd:PRK03932 172 -FRVTTLDLDFskdffgkEAYLTVSGQLYAEAYAMA-LGKVYTFGPTFRAEN-SntRRHLAEFWMIEPEMAFADLEDNMD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 292 LTEELLSSV----------ALEVLGSTSMPYG----EHTVEfgGKYARMSMFDAIKHYNPNHAQIQALTE--EDIQnrdl 355
Cdd:PRK03932 249 LAEEMLKYVvkyvlencpdDLEFLNRRVDKGDierlENFIE--SPFPRITYTEAIEILQKSGKKFEFPVEwgDDLG---- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 356 mvsiakSVHvdvEPFwtcgqLLEEIFGetaepklmQPTFITGYPADISPLARRSDDNpfftdrfeffigGREVAN----- 430
Cdd:PRK03932 323 ------SEH---ERY-----LAEEHFK--------KPVFVTNYPKDIKAFYMRLNPD------------GKTVAAmdlla 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 431 -GFSEL-------NDAEDQDARFKaqveakesgddeamfydadyitalEHGLP----------------PTAGQGIGIDR 486
Cdd:PRK03932 369 pGIGEIiggsqreERLDVLEARIK------------------------ELGLNkedywwyldlrrygsvPHSGFGLGFER 424
|
490
....*....|....*...
gi 446050909 487 LVMLLTNTHTIRDVILFP 504
Cdd:PRK03932 425 LVAYITGLDNIRDVIPFP 442
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
73-147 |
5.72e-11 |
|
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: 58.73 E-value: 5.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 73 VSIAGRVMAKRGP----FLVIQETSGRIQAYASKEVQQELKDKYQGLDIGDIIGVQGALHKS-----GKGDLYVNMEQFQ 143
Cdd:cd04100 2 VTLAGWVHSRRDHggliFIDLRDGSGIVQVVVNKEELGEFFEEAEKLRTESVVGVTGTVVKRpegnlATGEIELQAEELE 81
|
....
gi 446050909 144 LLTK 147
Cdd:cd04100 82 VLSK 85
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
73-145 |
6.02e-11 |
|
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: 58.40 E-value: 6.02e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446050909 73 VSIAGRVMAKRGP-----FLVIQETSGRIQAYASKEVQQELKDKyqgLDIGDIIGVQGALHKSGKGDLYVNMEQFQLL 145
Cdd:pfam01336 1 VTVAGRVTSIRRSggkllFLTLRDGTGSIQVVVFKEEAEKLAKK---LKEGDVVRVTGKVKKRKGGELELVVEEIELL 75
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
234-504 |
1.55e-08 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 56.96 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 234 YLRIAPELYLKRLVVGGFDrVFEINRNFRNEGL-SPRHNPEFTMMEFYMAYADYKDLMDLTEELLSSVALEVLGST--SM 310
Cdd:PTZ00425 327 FLTVSGQLSLENLCSSMGD-VYTFGPTFRAENShTSRHLAEFWMIEPEIAFADLYDNMELAESYIKYCIGYVLNNNfdDI 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 311 PYGEHTVEFGgkyarmsMFDAIKH-YNPNHAQIqalTEEDIQnrDLMVSIAKSVHVDVEpfWTCG-QLLEEIFgeTAEPK 388
Cdd:PTZ00425 406 YYFEENVETG-------LISRLKNiLDEDFAKI---TYTNVI--DLLQPYSDSFEVPVK--WGMDlQSEHERF--VAEQI 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 389 LMQPTFITGYPADISPL-ARRSDDNPFFT--DRFEFFIGgrEVANGfselNDAEDQDARFKAQVEAKESGDDEAMFYDad 465
Cdd:PTZ00425 470 FKKPVIVYNYPKDLKAFyMKLNEDQKTVAamDVLVPKIG--EVIGG----SQREDNLERLDKMIKEKKLNMESYWWYR-- 541
|
250 260 270
....*....|....*....|....*....|....*....
gi 446050909 466 yiTALEHGLPPTAGQGIGIDRLVMLLTNTHTIRDVILFP 504
Cdd:PTZ00425 542 --QLRKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFP 578
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
254-504 |
2.38e-06 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 49.97 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 254 VFEINRNFRNEGL-SPRHNPEFTMMEFYMAYADYKDLMDLTEELLSSVALEVLGSTS--MPYGEHTVEFG---------- 320
Cdd:PLN02603 324 VYTFGPTFRAENSnTSRHLAEFWMIEPELAFADLNDDMACATAYLQYVVKYILENCKedMEFFNTWIEKGiidrlsdvve 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 321 GKYARMSMFDAIkhynpnhaqiqalteediqnrDLMVSIAKSVHVDVEpfWTCG-------QLLEEIFGEtaepklmQPT 393
Cdd:PLN02603 404 KNFVQLSYTDAI---------------------ELLLKAKKKFEFPVK--WGLDlqseherYITEEAFGG-------RPV 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 394 FITGYPADISPLARRSDDN-------PFFTDRFEFFIGGREVANGFSELndaedqDARFKAQVEAKESgddeamFYDadY 466
Cdd:PLN02603 454 IIRDYPKEIKAFYMRENDDgktvaamDMLVPRVGELIGGSQREERLEYL------EARLDELKLNKES------YWW--Y 519
|
250 260 270
....*....|....*....|....*....|....*...
gi 446050909 467 ITALEHGLPPTAGQGIGIDRLVMLLTNTHTIRDVILFP 504
Cdd:PLN02603 520 LDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFP 557
|
|
| pylS |
PRK09537 |
pyrrolysine--tRNA(Pyl) ligase; |
177-314 |
4.57e-06 |
|
pyrrolysine--tRNA(Pyl) ligase;
Pssm-ID: 236555 [Multi-domain] Cd Length: 417 Bit Score: 49.07 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 177 ENSRNAFIvrSKVMSAIRNFMISKQFMEVETPMMhvIPGGASARPFITHHNAL-------DMPMYLR--IAPELY--LKR 245
Cdd:PRK09537 199 EEDREDYL--GKLERDITKFFVDRGFLEIKSPIL--IPAEYIERMGIDNDTELskqifrvDKNFCLRpmLAPGLYnyLRK 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446050909 246 lvvggFDRV-------FEINRNFRNEGLSPRHNPEFTMMEFYM--AYADYKDLMDLTEELLS--SVALEVLGSTSMPYGE 314
Cdd:PRK09537 275 -----LDRIlpdpikiFEIGPCYRKESDGKEHLEEFTMVNFCQmgSGCTRENLENIIDDFLKhlGIDYEIIGDNCMVYGD 349
|
|
| |
