|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
1-557 |
0e+00 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 822.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 1 MSEPEAKLSKNEQKRLAKQAKKEQERLEKDAAKlNVAVADAPKVVREA------DPSDPQEYFNMRVRMIEARRAAGDNP 74
Cdd:PLN02502 1 AESNGEPLSKNALKKRLKAKQAEEEKAAKEEAK-AAAAAAAAKGRSRKsaaaddETMDPTQYRANRLKKVEALRAKGVEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 75 FPHKFNVTISLTDFITKYTPLEKEQVVE-EIVSVAGRIHSKRESGsKLVFYDIHGEGTHIQIMANAKFHTGDVD-FVTLH 152
Cdd:PLN02502 80 YPYKFDVTHTAPELQEKYGSLENGEELEdVSVSVAGRIMAKRAFG-KLAFYDLRDDGGKIQLYADKKRLDLDEEeFEKLH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 153 DRIKRGDIVGFTGRATRTKAGELSLIPNEILQLTPCLHMLPHSHFGLKDKELRFRKRYLDLILNPRVKDNFVIRSKIITF 232
Cdd:PLN02502 159 SLVDRGDIVGVTGTPGKTKKGELSIFPTSFEVLTKCLLMLPDKYHGLTDQETRYRQRYLDLIANPEVRDIFRTRAKIISY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 233 LRRYLDNLGFLEVETPIMNQIAGGATAKPFITHHNDLDMNLFLRVAPELYHKMLVVGGIDRVYEVGRLFRNEGIDLTHNP 312
Cdd:PLN02502 239 IRRFLDDRGFLEVETPMLNMIAGGAAARPFVTHHNDLNMDLYLRIATELHLKRLVVGGFERVYEIGRQFRNEGISTRHNP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 313 EFTTCEFYMAYADYEDVIQLTEDLLSSMVMSIKGTYKIEYHPngpntepvYEVDFTPPFKRVHMYDGLAEKLGatLPDPS 392
Cdd:PLN02502 319 EFTTCEFYQAYADYNDMMELTEEMVSGMVKELTGSYKIKYHG--------IEIDFTPPFRRISMISLVEEATG--IDFPA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 393 TLHTEEAREVFDKLCRDNNVDCSAPRTTARLLDKLVGEYLESTFISPTFLIGHPQIMSPLAKWHRSIPGLTERFELFAVT 472
Cdd:PLN02502 389 DLKSDEANAYLIAACEKFDVKCPPPQTTGRLLNELFEEFLEETLVQPTFVLDHPVEMSPLAKPHRSKPGLTERFELFING 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 473 REIANAYTELNDPITQRQRFEQQAKDKDAGDDEAQMIDETFCNALEYGLPPTGGWGMGIDRLSMILTDNNNIKEVLLFPA 552
Cdd:PLN02502 469 RELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFPA 548
|
....*
gi 300545151 553 MRPED 557
Cdd:PLN02502 549 MKPQD 553
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
59-558 |
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: 677.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 59 MRVRM--IEARRAAGDNPFPHKFNVTISLTDFITKYTPLEKEQVVEEIVSVAGRIHSKRESGsKLVFYDIHGEGTHIQIM 136
Cdd:COG1190 11 IRVRRekLEELREAGIDPYPNKFPRTHTAAEIREKYDELEAEEETGDEVSVAGRIMAKRDMG-KASFADLQDGSGRIQLY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 137 ANAKfHTGDVDFVTLHDrIKRGDIVGFTGRATRTKAGELSLIPNEILQLTPCLHMLPHSHFGLKDKELRFRKRYLDLILN 216
Cdd:COG1190 90 LRRD-ELGEEAYELFKL-LDLGDIVGVEGTVFRTKTGELSVKVEELTLLSKSLRPLPEKFHGLTDPETRYRQRYVDLIVN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 217 PRVKDNFVIRSKIITFLRRYLDNLGFLEVETPIMNQIAGGATAKPFITHHNDLDMNLFLRVAPELYHKMLVVGGIDRVYE 296
Cdd:COG1190 168 PEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVFE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 297 VGRLFRNEGIDLTHNPEFTTCEFYMAYADYEDVIQLTEDLLSSMVMSIKGTYKIEYhpNGpntepvYEVDFTPPFKRVHM 376
Cdd:COG1190 248 IGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGTTKVTY--QG------QEIDLSPPWRRITM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 377 YDGLAEKLGAtlpDPSTLHT-EEAREvfdkLCRDNNVDCSAPRTTARLLDKLVGEYLESTFISPTFLIGHPQIMSPLAKW 455
Cdd:COG1190 320 VEAIKEATGI---DVTPLTDdEELRA----LAKELGIEVDPGWGRGKLIDELFEELVEPKLIQPTFVTDYPVEVSPLAKR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 456 HRSIPGLTERFELFAVTREIANAYTELNDPITQRQRFEQQAKDKDAGDDEAQMIDETFCNALEYGLPPTGGWGMGIDRLS 535
Cdd:COG1190 393 HRDDPGLTERFELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGLGIGIDRLV 472
|
490 500
....*....|....*....|...
gi 300545151 536 MILTDNNNIKEVLLFPAMRPEDG 558
Cdd:COG1190 473 MLLTDSPSIRDVILFPLMRPEKK 495
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
59-557 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 669.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 59 MRVRM--IEARRAAGDNPFPHKFNVTISLTDFITKYTPLEKEQVVE--EIVSVAGRIHSKRESGsKLVFYDIHGEGTHIQ 134
Cdd:PRK00484 7 IAVRRekLAELREQGIDPYPNKFERTHTAAELRAKYDDKEKEELEEleIEVSVAGRVMLKRVMG-KASFATLQDGSGRIQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 135 IMANAKfHTGDvDFVTLHDRIKRGDIVGFTGRATRTKAGELSLIPNEILQLTPCLHMLPHSHFGLKDKELRFRKRYLDLI 214
Cdd:PRK00484 86 LYVSKD-DVGE-EALEAFKKLDLGDIIGVEGTLFKTKTGELSVKATELTLLTKSLRPLPDKFHGLTDVETRYRQRYVDLI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 215 LNPRVKDNFVIRSKIITFLRRYLDNLGFLEVETPIMNQIAGGATAKPFITHHNDLDMNLFLRVAPELYHKMLVVGGIDRV 294
Cdd:PRK00484 164 VNPESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARPFITHHNALDIDLYLRIAPELYLKRLIVGGFERV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 295 YEVGRLFRNEGIDLTHNPEFTTCEFYMAYADYEDVIQLTEDLLSSMVMSIKGTYKIEYhpNGpntepvYEVDFTPPFKRV 374
Cdd:PRK00484 244 YEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTY--QG------TEIDFGPPFKRL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 375 HMYDGLAEKLGAtlpDPSTLHTEEAREvfdkLCRDNNVDCSAPRTTARLLDKLVGEYLESTFISPTFLIGHPQIMSPLAK 454
Cdd:PRK00484 316 TMVDAIKEYTGV---DFDDMTDEEARA----LAKELGIEVEKSWGLGKLINELFEEFVEPKLIQPTFITDYPVEISPLAK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 455 WHRSIPGLTERFELFAVTREIANAYTELNDPITQRQRFEQQAKDKDAGDDEAQMIDETFCNALEYGLPPTGGWGMGIDRL 534
Cdd:PRK00484 389 RHREDPGLTERFELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIGIDRL 468
|
490 500
....*....|....*....|...
gi 300545151 535 SMILTDNNNIKEVLLFPAMRPED 557
Cdd:PRK00484 469 VMLLTDSPSIRDVILFPLMRPEK 491
|
|
| lysS_bact |
TIGR00499 |
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ... |
52-555 |
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: 612.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 52 DPQEYFNMRVRMIEARRAAGDNPFPHKFNVTISLTDFITKYTPLEKEQV--VEEIVSVAGRIHSKReSGSKLVFYDIHGE 129
Cdd:TIGR00499 1 ELNDQAQQRLEKLNRLRQTGNNPYLHKFERTHSAQEFQEKYADLSNEELkeKELKVSIAGRIKAIR-SMGKATFITLQDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 130 GTHIQIMANAKFHTGDVDFVTlHDRIKRGDIVGFTGRATRTKAGELSLIPNEILQLTPCLHMLPHSHFGLKDKELRFRKR 209
Cdd:TIGR00499 80 SGQIQLYVNKNKLPEDFYEFD-EYLLDLGDIIGVTGYPFKTKTGELSVKVTELQILTKCLQPLPDKWHGLTDQETRYRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 210 YLDLILNPRVKDNFVIRSKIITFLRRYLDNLGFLEVETPIMNQIAGGATAKPFITHHNDLDMNLFLRVAPELYHKMLVVG 289
Cdd:TIGR00499 159 YLDLIVNPDVRQTFLKRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKPFITHHNALDMDLYLRIAPELYLKRLIVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 290 GIDRVYEVGRLFRNEGIDLTHNPEFTTCEFYMAYADYEDVIQLTEDLLSSMVMSIKGTYKIEYhpngpNTEpvyEVDFTP 369
Cdd:TIGR00499 239 GLEKVYEIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTFIINY-----NDL---EIDLKP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 370 PFKRVHMYDGLAEKLGATLPDpstLHTEEAREVFDKLCRDNNVDCsaPRTTARLLDKLVGEYLESTFISPTFLIGHPQIM 449
Cdd:TIGR00499 311 PWKRITMVDALEMVTGIDFDI---LKDDETAKALAKEHGIEVAED--SLTLGHILNKFFEQFLEHTLIQPTFITHYPAEI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 450 SPLAKWHRSIPGLTERFELFAVTREIANAYTELNDPITQRQRFEQQAKDKDAGDDEAQMIDETFCNALEYGLPPTGGWGM 529
Cdd:TIGR00499 386 SPLAKRDPSNPEFTERFELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGI 465
|
490 500
....*....|....*....|....*.
gi 300545151 530 GIDRLSMILTDNNNIKEVLLFPAMRP 555
Cdd:TIGR00499 466 GIDRLVMLLTDAPSIRDVLLFPQLRP 491
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
1-555 |
0e+00 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 602.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 1 MSEPEAKLSKNEQKRLAKQAKKEQERLEkdaaklnvavadapkvvrEADpSDPQEYFNMRVRMIEARRAAGDNPFPHKFN 80
Cdd:PTZ00417 49 MSEKKEHVMEGEKKVRSVQASKDKKKEE------------------EAE-VDPRLYYENRSKFIQEQKAKGINPYPHKFE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 81 VTISLTDFITKYTPLEK-EQVVEEIVSVAGRIHSKRESGSKLVFYDIHGEGTHIQIMANAKFHTGD-VDFVTLHDRIKRG 158
Cdd:PTZ00417 110 RTITVPEFVEKYQDLASgEHLEDTILNVTGRIMRVSASGQKLRFFDLVGDGAKIQVLANFAFHDHTkSNFAECYDKIRRG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 159 DIVGFTGRATRTKAGELSLIPNEILQLTPCLHMLPHShFGLKDKELRFRKRYLDLILNPRVKDNFVIRSKIITFLRRYLD 238
Cdd:PTZ00417 190 DIVGIVGFPGKSKKGELSIFPKETIILSPCLHMLPMK-YGLKDTEIRYRQRYLDLMINESTRSTFITRTKIINYLRNFLN 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 239 NLGFLEVETPIMNQIAGGATAKPFITHHNDLDMNLFLRVAPELYHKMLVVGGIDRVYEVGRLFRNEGIDLTHNPEFTTCE 318
Cdd:PTZ00417 269 DRGFIEVETPTMNLVAGGANARPFITHHNDLDLDLYLRIATELPLKMLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 319 FYMAYADYEDVIQLTEDLLSSMVMSIKGTYKIEYHPNGPNTEPVyEVDFTPPFKRVHMYDGLAEKLGATLPDPstLHTEE 398
Cdd:PTZ00417 349 FYWAYADFYDLIKWSEDFFSQLVMHLFGTYKILYNKDGPEKDPI-EIDFTPPYPKVSIVEELEKLTNTKLEQP--FDSPE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 399 AREVFDKLCRDNNVDCSAPRTTARLLDKLVGEYLESTFIS-PTFLIGHPQIMSPLAKWHRSIPGLTERFELFAVTREIAN 477
Cdd:PTZ00417 426 TINKMINLIKENKIEMPNPPTAAKLLDQLASHFIENKYPNkPFFIIEHPQIMSPLAKYHRSKPGLTERLEMFICGKEVLN 505
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300545151 478 AYTELNDPITQRQRFEQQAKDKDAGDDEAQMIDETFCNALEYGLPPTGGWGMGIDRLSMILTDNNNIKEVLLFPAMRP 555
Cdd:PTZ00417 506 AYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFPTMRP 583
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
216-555 |
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: 596.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 216 NPRVKDNFVIRSKIITFLRRYLDNLGFLEVETPIMNQIAGGATAKPFITHHNDLDMNLFLRVAPELYHKMLVVGGIDRVY 295
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 296 EVGRLFRNEGIDLTHNPEFTTCEFYMAYADYEDVIQLTEDLLSSMVMSIKGTYKIEYhpngpntePVYEVDFTPPFKRVH 375
Cdd:cd00775 81 EIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIEY--------GGKELDFTPPFKRVT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 376 MYDGLAEKLGATLPDPSTLHTEEAREVFDKLCRDNNVDcsaPRTTARLLDKLVGEYLESTFISPTFLIGHPQIMSPLAKW 455
Cdd:cd00775 153 MVDALKEKTGIDFPELDLEQPEELAKLLAKLIKEKIEK---PRTLGKLLDKLFEEFVEPTLIQPTFIIDHPVEISPLAKR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 456 HRSIPGLTERFELFAVTREIANAYTELNDPITQRQRFEQQAKDKDAGDDEAQMIDETFCNALEYGLPPTGGWGMGIDRLS 535
Cdd:cd00775 230 HRSNPGLTERFELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLV 309
|
330 340
....*....|....*....|
gi 300545151 536 MILTDNNNIKEVLLFPAMRP 555
Cdd:cd00775 310 MLLTDSNSIRDVILFPAMRP 329
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
51-554 |
3.02e-144 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 431.38 E-value: 3.02e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 51 SDPQEYFNMRVRMIEARRAAGDNPFPHK-FNVTISLTDFITKYTPLEK-EQVVEEIVSVAGRIHSKRESGsKLVFYDIHG 128
Cdd:PTZ00385 54 SKASATKTVTQEASRAPRSKLDLPAAYSsFRGITPISEVRERYGYLASgDRAAQATVRVAGRVTSVRDIG-KIIFVTIRS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 129 EGTHIQIMANAKFHTGDVDFVTLHDRIKRGDIVGFTGRATRTKAGELSLIPNEILQLTP--------CLHMLPHSHfgLK 200
Cdd:PTZ00385 133 NGNELQVVGQVGEHFTREDLKKLKVSLRVGDIIGADGVPCRMQRGELSVAASRMLILSPyvctdqvvCPNLRGFTV--LQ 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 201 DKELRFRKRYLDLILNPRVKDNFVIRSKIITFLRRYLDNLGFLEVETPIMNQIAGGATAKPFITHHNDLDMNLFLRVAPE 280
Cdd:PTZ00385 211 DNDVKYRYRFTDMMTNPCVIETIKKRHVMLQALRDYFNERNFVEVETPVLHTVASGANAKSFVTHHNANAMDLFLRVAPE 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 281 LYHKMLVVGGIDRVYEVGRLFRNEGIDLTHNPEFTTCEFYMAYADYEDVIQLTEDLLSSMVMSIKGTYKIEYHPNGPNTE 360
Cdd:PTZ00385 291 LHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTSCEFYAAYHTYEDLMPMTEDIFRQLAMRVNGTTVVQIYPENAHGN 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 361 PVyEVDFTPPFKRVHMYDGLAEKLGATLPDPSTLHTEEAREVFDKLCRDNNVDCSAPRTTARLLDKLVGEYLESTFISPT 440
Cdd:PTZ00385 371 PV-TVDLGKPFRRVSVYDEIQRMSGVEFPPPNELNTPKGIAYMSVVMLRYNIPLPPVRTAAKMFEKLIDFFITDRVVEPT 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 441 FLIGHPQIMSPLAKWHRSIPGLTERFELFAVTREIANAYTELNDPITQRQRFEQQAKDKDAGDDEAQMIDETFCNALEYG 520
Cdd:PTZ00385 450 FVMDHPLFMSPLAKEQVSRPGLAERFELFVNGIEYCNAYSELNDPHEQYHRFQQQLVDRQGGDEEAMPLDETFLKSLQVG 529
|
490 500 510
....*....|....*....|....*....|....
gi 300545151 521 LPPTGGWGMGIDRLSMILTDNNNIKEVLLFPAMR 554
Cdd:PTZ00385 530 LPPTAGWGMGIDRALMLLTNSSNIRDGIIFPLLR 563
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
17-557 |
5.42e-138 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 427.84 E-value: 5.42e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 17 AKQAKKEQERLEKDAAKLNVAvADAPKVVReadPSDPQEyfnMRVRM--IEARRAAGDNPFPHKFNVTISLTDFItkytp 94
Cdd:PRK02983 579 VPERLAASGLLHHDGSAPDVA-ATAPDAPE---PRLPEQ---VRVRLakLEALRAAGVDPYPVGVPPTHTVAEAL----- 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 95 lekEQVVEEIVSVAGRIHSKRESGsKLVFYDIHGEGTHIQIMANAKfhTGDVDFVTLHDR-IKRGDIVGFTGRATRTKAG 173
Cdd:PRK02983 647 ---DAPTGEEVSVSGRVLRIRDYG-GVLFADLRDWSGELQVLLDAS--RLEQGSLADFRAaVDLGDLVEVTGTMGTSRNG 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 174 ELSLIPNEILQLTPCLHMLPHSHFGLKDKELRFRKRYLDLILNPRVKDNFVIRSKIITFLRRYLDNLGFLEVETPIMNQI 253
Cdd:PRK02983 721 TLSLLVTSWRLAGKCLRPLPDKWKGLTDPEARVRQRYLDLAVNPEARDLLRARSAVVRAVRETLVARGFLEVETPILQQV 800
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 254 AGGATAKPFITHHNDLDMNLFLRVAPELYHKMLVVGGIDRVYEVGRLFRNEGIDLTHNPEFTTCEFYMAYADYEDVIQLT 333
Cdd:PRK02983 801 HGGANARPFVTHINAYDMDLYLRIAPELYLKRLCVGGVERVFELGRNFRNEGVDATHNPEFTLLEAYQAHADYDTMRDLT 880
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 334 EDLLSSMVMSIKGTYKIEyhpnGPNTE-PVYEVDFTPPFKRVHMYDGLAEKLGATLpDPSTlHTEEARevfdKLCRDNNV 412
Cdd:PRK02983 881 RELIQNAAQAAHGAPVVM----RPDGDgVLEPVDISGPWPVVTVHDAVSEALGEEI-DPDT-PLAELR----KLCDAAGI 950
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 413 DCSAPRTTARLLDKLVGEYLESTFISPTFLIGHPQIMSPLAKWHRSIPGLTERFELFAVTREIANAYTELNDPITQRQRF 492
Cdd:PRK02983 951 PYRTDWDAGAVVLELYEHLVEDRTTFPTFYTDFPTSVSPLTRPHRSDPGLAERWDLVAWGVELGTAYSELTDPVEQRRRL 1030
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300545151 493 EQQAKDKDAGDDEAQMIDETFCNALEYGLPPTGGWGMGIDRLSMILTdNNNIKEVLLFPAMRPED 557
Cdd:PRK02983 1031 TEQSLLAAGGDPEAMELDEDFLQALEYAMPPTGGLGMGVDRLVMLLT-GRSIRETLPFPLVKPRQ 1094
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
105-556 |
1.26e-116 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 355.52 E-value: 1.26e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 105 VSVAGRIHSKRESGsKLVFYDIHGEGTHIQI-MANAKFHTGdvdfvTLHDRIKR---GDIVGFTGRATRTKAGELSLIPN 180
Cdd:PRK12445 68 VSVAGRMMTRRIMG-KASFVTLQDVGGRIQLyVARDSLPEG-----VYNDQFKKwdlGDIIGARGTLFKTQTGELSIHCT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 181 EILQLTPCLHMLPHSHFGLKDKELRFRKRYLDLILNPRVKDNFVIRSKIITFLRRYLDNLGFLEVETPIMNQIAGGATAK 260
Cdd:PRK12445 142 ELRLLTKALRPLPDKFHGLQDQEVRYRQRYLDLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASAR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 261 PFITHHNDLDMNLFLRVAPELYHKMLVVGGIDRVYEVGRLFRNEGIDLTHNPEFTTCEFYMAYADYEDVIQLTEDLLSSM 340
Cdd:PRK12445 222 PFITHHNALDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 341 VMSIKGTYKIEYhpngpnTEPVYevDFTPPFKRVHMYDGLAEKLGATlpDPSTLHTEEAREVfdkLCRDNNVDCSAPRTT 420
Cdd:PRK12445 302 AQEVLGTTKVTY------GEHVF--DFGKPFEKLTMREAIKKYRPET--DMADLDNFDAAKA---LAESIGITVEKSWGL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 421 ARLLDKLVGEYLESTFISPTFLIGHPQIMSPLAKWHRSIPGLTERFELFAVTREIANAYTELNDPITQRQRFEQQAKDKD 500
Cdd:PRK12445 369 GRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKA 448
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 300545151 501 AGDDEAQMIDETFCNALEYGLPPTGGWGMGIDRLSMILTDNNNIKEVLLFPAMRPE 556
Cdd:PRK12445 449 AGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFPAMRPQ 504
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
201-554 |
2.56e-115 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 345.32 E-value: 2.56e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 201 DKELRFRKRYLDLiLNPRVKDNFVIRSKIITFLRRYLDNLGFLEVETPIMNQIAGGATAKPFITHHNDLDMNLFLRVAPE 280
Cdd:pfam00152 1 DEETRLKYRYLDL-RRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 281 LYHKMLVVGGIDRVYEVGRLFRNEGIDLTHNPEFTTCEFYMAYADYEDVIQLTEDLLSSMVMSIKGTYKIEYHPngpnte 360
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGG------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 361 pvYEVDFTPPFKRVHMYDGLAEKLGatlpdpstlhteearevfdKLCRDNNVDCSAPRTtaRLLDKLVgeyLESTFISPT 440
Cdd:pfam00152 154 --TLLDLKKPFPRITYAEAIEKLNG-------------------KDVEELGYGSDKPDL--RFLLELV---IDKNKFNPL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 441 FLIGHPQIMSPLAKWHRS-IPGLTERFELFAVTREIANAYTELNDPITQRQRFEQQAKDKdagdDEAQMIDETFCNALEY 519
Cdd:pfam00152 208 WVTDFPAEHHPFTMPKDEdDPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDP----EEAEEKFGFYLDALKY 283
|
330 340 350
....*....|....*....|....*....|....*
gi 300545151 520 GLPPTGGWGMGIDRLSMILTDNNNIKEVLLFPAMR 554
Cdd:pfam00152 284 GAPPHGGLGIGLDRLVMLLTGLESIREVIAFPKTR 318
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
223-555 |
2.43e-90 |
|
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: 279.36 E-value: 2.43e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 223 FVIRSKIITFLRRYLDNLGFLEVETPIMNQIAGGATAKPFITHHNDLDMNLFLRVAPELYHKMLVVGGIDRVYEVGRLFR 302
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 303 NEGIDLTHNPEFTTCEFYMAYADYEDVIQLTEDLLSSMVMSIKGTYKIEYHpngpntepVYEVDFTPPFKRVHMYDGLaE 382
Cdd:cd00669 81 NEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYG--------FELEDFGLPFPRLTYREAL-E 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 383 KLGAtlpdpstlhteearevfdklcrdnnvdcsaprttarlldklvgeylestfisPTFLIGHP-QIMSPLAKWHRSIPG 461
Cdd:cd00669 152 RYGQ----------------------------------------------------PLFLTDYPaEMHSPLASPHDVNPE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 462 LTERFELFAVTREIANAYTELNDPITQRQRFEQQAKDKDAGDDEaqmiDETFCNALEYGLPPTGGWGMGIDRLSMILTDN 541
Cdd:cd00669 180 IADAFDLFINGVEVGNGSSRLHDPDIQAEVFQEQGINKEAGMEY----FEFYLKALEYGLPPHGGLGIGIDRLIMLMTNS 255
|
330
....*....|....
gi 300545151 542 NNIKEVLLFPAMRP 555
Cdd:cd00669 256 PTIREVIAFPKMRR 269
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
226-548 |
3.81e-52 |
|
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: 180.69 E-value: 3.81e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 226 RSKIITFLRRYLDNLGFLEVETPIMnQIAGGATA--KPFIT---HHNDLDMNLFLRVAPELYHKMLVVGGIDRVYEVGRL 300
Cdd:COG2269 9 RARLLAAIRAFFAERGVLEVETPAL-SVAPGTDPhlDSFATefiGPDGGGRPLYLHTSPEFAMKRLLAAGSGPIYQIAKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 301 FRNEGIDLTHNPEFTTCEFYMAYADYEDVIQLTEDLLSSmvmsikgtykieyhpngpntepVYEVDFTPPFKRVHMYDGL 380
Cdd:COG2269 88 FRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQL----------------------VLGAAGFAPAERLSYQEAF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 381 AEKLGatlPDPSTLHTEEAREVfdklCRDNNVDCSAPRTTARLLDKLVGEYLESTFI--SPTFLIGHPQIMSPLAKWHRS 458
Cdd:COG2269 146 LRYLG---IDPLTADLDELAAA----AAAAGLRVADDDDRDDLLDLLLSERVEPQLGrdRPTFLYDYPASQAALARISPD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 459 IPGLTERFELFAVTREIANAYTELNDPITQRQRFEQQAKDKDAGDDEAQMIDETFCNALEYGLPPTGGWGMGIDRLSMIL 538
Cdd:COG2269 219 DPRVAERFELYACGVELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLA 298
|
330
....*....|
gi 300545151 539 TDNNNIKEVL 548
Cdd:COG2269 299 LGAERIDDVL 308
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
236-548 |
9.08e-50 |
|
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: 173.51 E-value: 9.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 236 YLDNLGFLEVETPIMnqIAGGATA---KPFITH---HNDLDMNLFLRVAPELYHKMLVVGGIDRVYEVGRLFRNEGIDLT 309
Cdd:TIGR00462 1 FFAERGVLEVETPLL--SPAPVTDphlDAFATEfvgPDGQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 310 HNPEFTTCEFYMAYADYEDVIQLTEDLLSSMVMsikgtykieyhpngpntepvyevDFTPPFKRVHMYDGLAEKLGAtlp 389
Cdd:TIGR00462 79 HNPEFTMLEWYRPGFDYHDLMDEVEALLQELLG-----------------------DPFAPAERLSYQEAFLRYAGI--- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 390 DPSTlhteEAREVFDKLCRDNNVDCSAPRTTARLLDKLVGEYLEST--FISPTFLIGHPQIMSPLAKWHRSIPGLTERFE 467
Cdd:TIGR00462 133 DPLT----ASLAELQAAAAAHGIRASEEDDRDDLLDLLFSEKVEPHlgFGRPTFLYDYPASQAALARISPDDPRVAERFE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 468 LFAVTREIANAYTELNDPITQRQRFEQQAKDKDAGDDEAQMIDETFCNALEYGLPPTGGWGMGIDRLSMILTDNNNIKEV 547
Cdd:TIGR00462 209 LYIKGLELANGFHELTDAAEQRRRFEADNALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDV 288
|
.
gi 300545151 548 L 548
Cdd:TIGR00462 289 L 289
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
104-213 |
2.37e-46 |
|
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: 2.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 104 IVSVAGRIHSKRESGsKLVFYDIHGEGTHIQIMANAKFHtGDVDFVTLHDRIKRGDIVGFTGRATRTKAGELSLIPNEIL 183
Cdd:cd04322 1 EVSVAGRIMSKRGSG-KLSFADLQDESGKIQVYVNKDDL-GEEEFEDFKKLLDLGDIIGVTGTPFKTKTGELSIFVKEFT 78
|
90 100 110
....*....|....*....|....*....|
gi 300545151 184 QLTPCLHMLPHSHFGLKDKELRFRKRYLDL 213
Cdd:cd04322 79 LLSKSLRPLPEKFHGLTDVETRYRQRYLDL 108
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
220-547 |
3.18e-42 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 153.93 E-value: 3.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 220 KDNFVIRSKIITFLRRYLDNLGFLEVETPIMNQiaggATA-----KPFITHHNDLD----MNLFLRVAPElYH-KMLVVG 289
Cdd:PRK09350 2 IPNLLKRAKIIAEIRRFFADRGVLEVETPILSQ----ATVtdihlVPFETRFVGPGasqgKTLWLMTSPE-YHmKRLLAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 290 GIDRVYEVGRLFRNEGIDLTHNPEFTTCEFYMAYADYEDVIQLTEDLLSsmvmsikgtykieyhpngpntepvyEVDFTP 369
Cdd:PRK09350 77 GSGPIFQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQ-------------------------QVLDCE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 370 PFKRVHMYDGLAEKLGAtlpDPSTLHTEEAREVFDKLCRDNNVDCSAPRTTarLLDKLVGEYLEST--FISPTFLIGHPQ 447
Cdd:PRK09350 132 PAESLSYQQAFLRYLGI---DPLSADKTQLREVAAKLGLSNIADEEEDRDT--LLQLLFTFGVEPNigKEKPTFVYHFPA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 448 IMSPLAKWHRSIPGLTERFELFAVTREIANAYTELNDPITQRQRFEQQAKDKDAGDDEAQMIDETFCNALEYGLPPTGGW 527
Cdd:PRK09350 207 SQAALAKISTEDHRVAERFEVYFKGIELANGFHELTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCSGV 286
|
330 340
....*....|....*....|
gi 300545151 528 GMGIDRLSMILTDNNNIKEV 547
Cdd:PRK09350 287 ALGVDRLIMLALGAESISEV 306
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
90-551 |
3.16e-37 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 143.41 E-value: 3.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 90 TKYTPLEKEQVVEEIVSVAGRIHSKRESGsKLVFYDIHG-EGThIQIMANAKFHTGDVDFVtlhDRIKRGDIVGFTGRAT 168
Cdd:PRK05159 4 RHLTSELTPELDGEEVTLAGWVHEIRDLG-GIAFLILRDrSGI-IQVVVKKKVDEELFETI---KKLKRESVVSVTGTVK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 169 ---RTKAGeLSLIPNEILQLTPCLHMLPHSHFGLKDKEL--RFRKRYLDLiLNPRVKDNFVIRSKIITFLRRYLDNLGFL 243
Cdd:PRK05159 79 anpKAPGG-VEVIPEEIEVLNKAEEPLPLDISGKVLAELdtRLDNRFLDL-RRPRVRAIFKIRSEVLRAFREFLYENGFT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 244 EVETP-IMNQIA-GGATAKPfithhndldMNLFLRVA-----PELYHKMLVVGGIDRVYEVGRLFRNEGIDLT-HNPEFT 315
Cdd:PRK05159 157 EIFTPkIVASGTeGGAELFP---------IDYFEKEAylaqsPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSrHLNEYT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 316 TCEFYMAYAD-YEDVIQLTEDLLSSMVMSIKGTYKIEYhpngpntepvyevdftppfkrvhmydglaEKLGATLPDPST- 393
Cdd:PRK05159 228 SIDVEMGFIDdHEDVMDLLENLLRYMYEDVAENCEKEL-----------------------------ELLGIELPVPETp 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 394 ---LHTEEAREVFDKLCRDNNVDCSAPRTTARLLDKLVGEYLESTFIsptFLIGHPQIMSPL-AKWHRSIPGLTERFELF 469
Cdd:PRK05159 279 iprITYDEAIEILKSKGNEISWGDDLDTEGERLLGEYVKEEYGSDFY---FITDYPSEKRPFyTMPDEDDPEISKSFDLL 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 470 AVTREIANAYTELNDPITQRQRFEQQAKDKDAGddeaqmidETFCNALEYGLPPTGGWGMGIDRLSMILTDNNNIKEVLL 549
Cdd:PRK05159 356 FRGLEITSGGQRIHRYDMLVESIKEKGLNPESF--------EFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVL 427
|
..
gi 300545151 550 FP 551
Cdd:PRK05159 428 FP 429
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
105-551 |
1.80e-36 |
|
nondiscriminating aspartyl-tRNA synthetase; 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_arch, represents aspartyl-tRNA synthetases from the eukaryotic cytosol and from the Archaea. In some species, this enzyme aminoacylates tRNA for both Asp and Asn; Asp-tRNA(asn) is subsequently transamidated to Asn-tRNA(asn). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273087 [Multi-domain] Cd Length: 428 Bit Score: 141.11 E-value: 1.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 105 VSVAGRIHSKRESGsKLVFYDIHGEGTHIQIMANAKFhTGDvDFVTLHDRIKRGDIVGFTGRATRTKA--GELSLIPNEI 182
Cdd:TIGR00458 15 VTFMGWVHEIRDLG-GLIFVLLRDREGLIQITAPAKK-VSK-NLFKWAKKLNLESVVAVRGIVKIKEKapGGFEIIPTKI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 183 LQLTPCLHMLPhshFGLKDK-----ELRFRKRYLDLiLNPRVKDNFVIRSKIITFLRRYLDNLGFLEVETP-IMNQIAGG 256
Cdd:TIGR00458 92 EVINEAKEPLP---LDPTEKvpaelDTRLDYRFLDL-RRPTVQAIFRIRSGVLESVREFLAEEGFIEVHTPkLVASATEG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 257 ATAKPFITHhndLDMNLFLRVAPELYHKMLVVGGIDRVYEVGRLFRNEGIDLT-HNPEFTTCEFYMAYADYEDVIqlteD 335
Cdd:TIGR00458 168 GTELFPITY---FEREAFLGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNTHrHLNEATSIDIEMAFEDHHDVM----D 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 336 LLSSMVMSIkgtykieyhpngpnTEPVYEvdftppfKRVHMYdglaEKLGATLPDPST----LHTEEAREvfdkLCRDNN 411
Cdd:TIGR00458 241 ILEELVVRV--------------FEDVPE-------RCAHQL----ETLEFKLEKPEGkfvrLTYDEAIE----MANAKG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 412 VDCSAPRTTARLLDKLVGEYLESTFisptFLIGHPQIMSPL-AKWHRSIPGLTERFELFAVTREIANAYTELNDPITQRQ 490
Cdd:TIGR00458 292 VEIGWGEDLSTEAEKALGEEMDGLY----FITDWPTEIRPFyTMPDEDNPEISKSFDLMYRDLEISSGAQRIHLHDLLVE 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300545151 491 RFEQQAKDKDAGDDeaqmidetFCNALEYGLPPTGGWGMGIDRLSMILTDNNNIKEVLLFP 551
Cdd:TIGR00458 368 RIKAKGLNPEGFKD--------YLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFP 420
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
101-554 |
9.79e-31 |
|
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: 124.39 E-value: 9.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 101 VEEIVSVAGRIHSKRESGsKLVFYDIH-GEGThIQIMANAKfhtgDVDFVTLHDRIKRGDIVGFTG--RATRTKAGELSL 177
Cdd:COG0017 13 VGQEVTVAGWVRTKRDSG-GISFLILRdGSGF-IQVVVKKD----KLENFEEAKKLTTESSVEVTGtvVESPRAPQGVEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 178 IPNEILQLTPCLHMLPhshFGLKDKELRFR--KRYLDLiLNPRVKDNFVIRSKIITFLRRYLDNLGFLEVETPIMnqIA- 254
Cdd:COG0017 87 QAEEIEVLGEADEPYP---LQPKRHSLEFLldNRHLRL-RTNRFGAIFRIRSELARAIREFFQERGFVEVHTPII--TAs 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 255 ---GGAtakpfithhndldmNLF----------LRVAPELYHKMLVvGGIDRVYEVGRLFRNEGIDLT-HNPEFTTCEFY 320
Cdd:COG0017 161 ateGGG--------------ELFpvdyfgkeayLTQSGQLYKEALA-MALEKVYTFGPTFRAEKSNTRrHLAEFWMIEPE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 321 MAYADYEDVIQLTEDLLSSMVMSIKGTYKIEYHPNGPNTEPVyEVDFTPPFKRVHMYDG--LAEKLGATLPDPSTLHTEE 398
Cdd:COG0017 226 MAFADLEDVMDLAEEMLKYIIKYVLENCPEELEFLGRDVERL-EKVPESPFPRITYTEAieILKKSGEKVEWGDDLGTEH 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 399 ARevfdklcrdnnvdcsaprttarlldkLVGEYLESTFIsptFLIGHP-QIMSPLAKWHRSIPGLTERFELfavtreIAN 477
Cdd:COG0017 305 ER--------------------------YLGEEFFKKPV---FVTDYPkEIKAFYMKPNPDDPKTVAAFDL------LAP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 478 AYTELndpIT--QRQ-RFEQ-QAKDKDAGDDEAQMidETFCNALEYGLPPTGGWGMGIDRLSMILTDNNNIKEVLLFPAM 553
Cdd:COG0017 350 GIGEI---IGgsQREhRYDVlVERIKEKGLDPEDY--EWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRD 424
|
.
gi 300545151 554 R 554
Cdd:COG0017 425 P 425
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
203-551 |
9.77e-28 |
|
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: 113.82 E-value: 9.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 203 ELRFRKRYLDLiLNPRVKDNFVIRSKIITFLRRYLDNLGFLEVETPIM--NQIAGGATAKPFithhNDLDMNLFLRVAPE 280
Cdd:cd00776 5 ETLLDNRHLDL-RTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKItsTDTEGGAELFKV----SYFGKPAYLAQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 281 LYHKMLvVGGIDRVYEVGRLFRNEGIDLT-HNPEFTTCEFYMAYA-DYEDVIQLTEDLLSSMVMSIKGTYK--IEYHPNG 356
Cdd:cd00776 80 LYKEML-IAALERVYEIGPVFRAEKSNTRrHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAkeLELVNQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 357 PNTEPVYEvdftPPFKRVHMYDG--LAEKLGATLPDPST--LHTEEarevfdklcrdnnvdcsaprttarllDKLVGEYL 432
Cdd:cd00776 159 NRELLKPL----EPFPRITYDEAieLLREKGVEEEVKWGedLSTEH--------------------------ERLLGEIV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 433 ESTFIsptFLIGHPQIMSPL-AKWHRSIPGLTERFELFAvtR---EIANAYTELNDPITQRQRFEQQAKDKDAgddeaqm 508
Cdd:cd00776 209 KGDPV---FVTDYPKEIKPFyMKPDDDNPETVESFDLLM--PgvgEIVGGSQRIHDYDELEERIKEHGLDPES------- 276
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 300545151 509 iDETFCNALEYGLPPTGGWGMGIDRLSMILTDNNNIKEVLLFP 551
Cdd:cd00776 277 -FEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
203-551 |
5.74e-24 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 105.92 E-value: 5.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 203 ELRFRKRYLDLiLNPRVKDNFVIRSKIITFLRRYLDNLGFLEVETPIMnqiaGGAT---AKPFI----THHNDldmnlF- 274
Cdd:PRK00476 122 ELRLKYRYLDL-RRPEMQKNLKLRSKVTSAIRNFLDDNGFLEIETPIL----TKSTpegARDYLvpsrVHPGK-----Fy 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 275 -LRVAPELYHKMLVVGGIDRVYEVGRLFRNEgiDLTHN--PEFTT--CEfyMAYADYEDVIQLTEDLLSSMVMSIKGtyk 349
Cdd:PRK00476 192 aLPQSPQLFKQLLMVAGFDRYYQIARCFRDE--DLRADrqPEFTQidIE--MSFVTQEDVMALMEGLIRHVFKEVLG--- 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 350 ieyhpngpntepvyeVDFTPPFKRvhM-YDGLAEKLGATLPD---PSTLH--TEEARE----VFDKLCRDN------NVD 413
Cdd:PRK00476 265 ---------------VDLPTPFPR--MtYAEAMRRYGSDKPDlrfGLELVdvTDLFKDsgfkVFAGAANDGgrvkaiRVP 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 414 CSAPRTTARLLDKL---VGEY--------------LEST---FISPT------------------FLIGHPQIMS----- 450
Cdd:PRK00476 328 GGAAQLSRKQIDELtefAKIYgakglayikvnedgLKGPiakFLSEEelaallertgakdgdlifFGADKAKVVNdalga 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 451 -------------------------PLAKW----------H----RSIPGLTERFELFAVTREIANAY------TEL--- 482
Cdd:PRK00476 408 lrlklgkelglidedkfaflwvvdfPMFEYdeeegrwvaaHhpftMPKDEDLDELETTDPGKARAYAYdlvlngYELggg 487
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300545151 483 ----NDPITQRQRF------EQQAKDKDAGddeaqMIDetfcnALEYGLPPTGGWGMGIDRLSMILTDNNNIKEVLLFP 551
Cdd:PRK00476 488 siriHRPEIQEKVFeilgisEEEAEEKFGF-----LLD-----ALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
203-373 |
1.39e-22 |
|
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: 101.61 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 203 ELRFRKRYLDLiLNPRVKDNFVIRSKIITFLRRYLDNLGFLEVETPIMnqIA---GGAtakpfithhNDldmnlFL---R 276
Cdd:COG0173 123 ELRLKYRYLDL-RRPEMQKNLILRHKVTKAIRNYLDENGFLEIETPIL--TKstpEGA---------RD-----YLvpsR 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 277 V----------APELYHKMLVVGGIDRVYEVGRLFRNEgiDLTHN--PEFTT--CEfyMAYADYEDVIQLTEDLLSSMVM 342
Cdd:COG0173 186 VhpgkfyalpqSPQLFKQLLMVSGFDRYFQIARCFRDE--DLRADrqPEFTQldIE--MSFVDQEDVFELMEGLIRHLFK 261
|
170 180 190
....*....|....*....|....*....|.
gi 300545151 343 SIKGtykieyhpngpntepvyeVDFTPPFKR 373
Cdd:COG0173 262 EVLG------------------VELPTPFPR 274
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
137-390 |
2.04e-22 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 101.40 E-value: 2.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 137 ANAKFHTGDVDFVTLHD----------RIKRGDIVGFTGRA---------TRTKAGELSLIPNEILQLTPCLHMLPHSHF 197
Cdd:PLN02903 93 LDVRDHTGIVQVVTLPDefpeahrtanRLRNEYVVAVEGTVrsrpqespnKKMKTGSVEVVAESVDILNVVTKSLPFLVT 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 198 GLKD------KELRFRKRYLDLILnPRVKDNFVIRSKIITFLRRYL-DNLGFLEVETPIMNQiaggatakpfITHHNDLD 270
Cdd:PLN02903 173 TADEqkdsikEEVRLRYRVLDLRR-PQMNANLRLRHRVVKLIRRYLeDVHGFVEIETPILSR----------STPEGARD 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 271 MNLFLRV----------APELYHKMLVVGGIDRVYEVGRLFRNEGIDLTHNPEFTTCEFYMAYADYEDVIQLTEDLLSSM 340
Cdd:PLN02903 242 YLVPSRVqpgtfyalpqSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEFTQLDMELAFTPLEDMLKLNEDLIRQV 321
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 300545151 341 VMSIKGtykieyhpngpntepvyeVDFTPPFKRVhMYDGLAEKLGATLPD 390
Cdd:PLN02903 322 FKEIKG------------------VQLPNPFPRL-TYAEAMSKYGSDKPD 352
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
201-340 |
2.36e-18 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 88.89 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 201 DKELRFRKRYLDlILNPRVKDNFVIRSKIITFLRRYLDNLGFLEVETPIMNQiAGGATAKPFITHHNDLDMNLF-LRVAP 279
Cdd:PRK12820 135 NEDLRLQYRYLD-IRRPAMQDHLAKRHRIIKCARDFLDSRGFLEIETPILTK-STPEGARDYLVPSRIHPKEFYaLPQSP 212
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300545151 280 ELYHKMLVVGGIDRVYEVGRLFRNEGIDLTHNPEFTTCEFYMAYADYEDVIQLTEDLLSSM 340
Cdd:PRK12820 213 QLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEFTQLDIEASFIDEEFIFELIEELTARM 273
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
225-364 |
3.26e-18 |
|
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: 83.32 E-value: 3.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 225 IRSKIITFLRRYLDNLGFLEVETPIMNQIAGGATA----KPFITHHNDLDMNLFLRVAPELYHKMLVVGGI----DRVYE 296
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAghepKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIrklpLRLAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 297 VGRLFRNEGI--DLTHNPEFTTCEFYMAYADYED------VIQLTEDLLSSMVMSIKGTYKIEY------HPNGPNTEPV 362
Cdd:cd00768 81 IGPAFRNEGGrrGLRRVREFTQLEGEVFGEDGEEasefeeLIELTEELLRALGIKLDIVFVEKTpgefspGGAGPGFEIE 160
|
..
gi 300545151 363 YE 364
Cdd:cd00768 161 VD 162
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
91-551 |
4.15e-18 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 87.74 E-value: 4.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 91 KYTP---LEKEQVVEEIVSVAGRIHSKRESGsKLVFYDIHgEGTH-IQIMANAKfhtGDV--DFVTLHDRIKRGDIVGFT 164
Cdd:PTZ00401 64 TFIPvavLSKPELVDKTVLIRARVSTTRKKG-KMAFMVLR-DGSDsVQAMAAVE---GDVpkEMIDFIGQIPTESIVDVE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 165 GRA-------TRTKAGELSLIPNEILQLTPCLHMLPhshFGLKDK-------------ELRFRKRYLDLiLNPRVKDNFV 224
Cdd:PTZ00401 139 ATVckveqpiTSTSHSDIELKVKKIHTVTESLRTLP---FTLEDAsrkesdegakvnfDTRLNSRWMDL-RTPASGAIFR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 225 IRSKIITFLRRYLDNLGFLEVETPIMNQIAGGATAKPFITHHNDLDMnlFLRVAPELYHKMLVVGGIDRVYEVGRLFRNE 304
Cdd:PTZ00401 215 LQSRVCQYFRQFLIDSDFCEIHSPKIINAPSEGGANVFKLEYFNRFA--YLAQSPQLYKQMVLQGDVPRVFEVGPVFRSE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 305 GIDL-THNPEFTTCEFYMAYAD-YEDVIQLTEDLLSSMVMSIKGtykieyhpngpNTEPVYEVDFTPPFKRVhMYDGLAE 382
Cdd:PTZ00401 293 NSNThRHLTEFVGLDVEMRINEhYYEVLDLAESLFNYIFERLAT-----------HTKELKAVCQQYPFEPL-VWKLTPE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 383 KL-----GATLPD--PSTLHTEEAREVFDKLCRDNNVDCSA----------------PRTTARLLDKLVGE-YLESTFIS 438
Cdd:PTZ00401 361 RMkelgvGVISEGvePTDKYQARVHNMDSRMLRINYMHCIEllntvleekmaptddiNTTNEKLLGKLVKErYGTDFFIS 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 439 PTFlighPQIMSPLakWHRSIPG---LTERFELFAVTREIANAYTELNDPITQRQRFEQQAKDKDAGDDeaqmidetFCN 515
Cdd:PTZ00401 441 DRF----PSSARPF--YTMECKDderFTNSYDMFIRGEEISSGAQRIHDPDLLLARAKMLNVDLTPIKE--------YVD 506
|
490 500 510
....*....|....*....|....*....|....*.
gi 300545151 516 ALEYGLPPTGGWGMGIDRLSMILTDNNNIKEVLLFP 551
Cdd:PTZ00401 507 SFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFP 542
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
3-551 |
1.27e-15 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 79.75 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 3 EPEAKLSKneqkrlaKQAKKEQERLEKDAAKLNVAVADAPkvvrEADPSDPQEYFNMRVRMIEARRAAGDNpfphkfnvt 82
Cdd:PLN02850 8 ESGEKISK-------KAAKKAAAKAEKLRREATAKAAAAS----LEDEDDPLASNYGDVPLEELQSKVTGR--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 83 isltdfitKYTPLE--KEQVVEEIVSVAGRIHSKRESGsKLVFYDIHGEGTHIQIMANAKFHTGDVDFVTLHDRIKRGDI 160
Cdd:PLN02850 68 --------EWTDVSdlGEELAGSEVLIRGRVHTIRGKG-KSAFLVLRQSGFTVQCVVFVSEVTVSKGMVKYAKQLSRESV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 161 VGFTGRATRTKAG------ELSLIPNEILQLTPCLHMLPhshFGLKD----------------------KELRFRKRYLD 212
Cdd:PLN02850 139 VDVEGVVSVPKKPvkgttqQVEIQVRKIYCVSKALATLP---FNVEDaarseseiekalqtgeqlvrvgQDTRLNNRVLD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 213 LilnpRVKDN---FVIRSKIITFLRRYLDNLGFLEVETPIMnqIAGGAT--AKPFithhnDLDMN---LFLRVAPELYHK 284
Cdd:PLN02850 216 L----RTPANqaiFRIQSQVCNLFREFLLSKGFVEIHTPKL--IAGASEggSAVF-----RLDYKgqpACLAQSPQLHKQ 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 285 MLVVGGIDRVYEVGRLFRNEGiDLTHNP--EFTTCEFYMAYAD-YEDVIQLTEDLLSSMVMSIKGTYKIEY------HPN 355
Cdd:PLN02850 285 MAICGDFRRVFEIGPVFRAED-SFTHRHlcEFTGLDLEMEIKEhYSEVLDVVDELFVAIFDGLNERCKKELeaireqYPF 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 356 GPntepvyeVDFTPPFKRVHMYDGLAE-KLGATLPDP-STLHTEearevfdklcrdnnvdcsaprtTARLLDKLVGEYLE 433
Cdd:PLN02850 364 EP-------LKYLPKTLRLTFAEGIQMlKEAGVEVDPlGDLNTE----------------------SERKLGQLVKEKYG 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 434 STFIsptFLIGHPQIMSP---LAKWHRsiPGLTERFELFAVTREIANAYTELNDP--ITQRQRfeqqAKDKDAGDdeaqm 508
Cdd:PLN02850 415 TDFY---ILHRYPLAVRPfytMPCPDD--PKYSNSFDVFIRGEEIISGAQRVHDPelLEKRAE----ECGIDVKT----- 480
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 300545151 509 iDETFCNALEYGLPPTGGWGMGIDRLSMILTDNNNIKEVLLFP 551
Cdd:PLN02850 481 -ISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFP 522
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
105-182 |
4.04e-14 |
|
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: 67.65 E-value: 4.04e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300545151 105 VSVAGRIHSKRESGSKLVFYDIHGEGTHIQIMANAKfhtgdvDFVTLHDRIKRGDIVGFTGRATRTKAGELSLIPNEI 182
Cdd:pfam01336 1 VTVAGRVTSIRRSGGKLLFLTLRDGTGSIQVVVFKE------EAEKLAKKLKEGDVVRVTGKVKKRKGGELELVVEEI 72
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
214-551 |
5.14e-14 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 73.52 E-value: 5.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 214 ILNPRVKDNFVIRSKIITFLRRYLDNLGFLEVETPIMNQI----AGGATAKPFithhNDLDMNLF---LRVAPEL-YHKM 285
Cdd:PRK06462 21 ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIISPStdplMGLGSDLPV----KQISIDFYgveYYLADSMiLHKQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 286 LVVGGIDRVYEVGRLFRNEG---IDLTHNPEFTTCEFYMAYADYEDVIQLTEDLLSSMVMSIKGTYKIEYHPNGPNTEpv 362
Cdd:PRK06462 97 LALRMLGKIFYLSPNFRLEPvdkDTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHEDELEFFGRDLP-- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 363 yevDFTPPFKRVHMydglaeklgatlpdpstlhtEEAREVFDKLCRDNNVDcsaprttARLLDKlvGE-YLESTFISPTF 441
Cdd:PRK06462 175 ---HLKRPFKRITH--------------------KEAVEILNEEGCRGIDL-------EELGSE--GEkSLSEHFEEPFW 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 442 LIGHPQIMSPLakWHRSIPGLTERfeLFAVTREIANAYTELndpITQRQR---FEQ-QAKDKDAGDDEAQMidETFCNAL 517
Cdd:PRK06462 223 IIDIPKGSREF--YDREDPERPGV--LRNYDLLLPEGYGEA---VSGGEReyeYEEiVERIREHGVDPEKY--KWYLEMA 293
|
330 340 350
....*....|....*....|....*....|....
gi 300545151 518 EYGLPPTGGWGMGIDRLSMILTDNNNIKEVLLFP 551
Cdd:PRK06462 294 KEGPLPSAGFGIGVERLTRYICGLRHIREVQPFP 327
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
105-182 |
1.26e-10 |
|
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: 57.96 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545151 105 VSVAGRIHSKRESGsKLVFYDIHGEGTHIQIMANAKfhtGDVDFVTLHDRIKRGDIVGFTGRATRTKA-----GELSLIP 179
Cdd:cd04100 2 VTLAGWVHSRRDHG-GLIFIDLRDGSGIVQVVVNKE---ELGEFFEEAEKLRTESVVGVTGTVVKRPEgnlatGEIELQA 77
|
...
gi 300545151 180 NEI 182
Cdd:cd04100 78 EEL 80
|
|
| PheRS_alpha_core |
cd00496 |
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ... |
292-366 |
1.45e-04 |
|
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure and the presence of three characteristic sequence motifs. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. While class II aaRSs generally aminoacylate the 3'-OH 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. PheRS is an alpha-2/ beta-2 tetramer.
Pssm-ID: 238277 [Multi-domain] Cd Length: 218 Bit Score: 43.30 E-value: 1.45e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300545151 292 DRVYEVGRLFRNEGIDLTHNPEFTTCEFYMAYAD--YEDVIQLTEDLLSSMVMSIKgtyKIEYHPN-GPNTEPVYEVD 366
Cdd:cd00496 81 IRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKGltFADLKGTLEEFAKELFGPIT---KVRFRPSyFPFTEPSFEVD 155
|
|
| |
