|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
35-581 |
0e+00 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 816.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 35 REQKRLAKQAKKEQERLEKDAAKlNVAVADAPKVVREA------DPSDPQEYFNMRVRMIEARRAAGDNPFPHKFNVTIS 108
Cdd:PLN02502 11 NALKKRLKAKQAEEEKAAKEEAK-AAAAAAAAKGRSRKsaaaddETMDPTQYRANRLKKVEALRAKGVEPYPYKFDVTHT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 109 LTDFITKYTPLEKEQVVE-EIVSVAGRIHSKRESGsKLVFYDIHGEGTHIQIMANAKFHTGDVD-FVTLHDRIKRGDIVG 186
Cdd:PLN02502 90 APELQEKYGSLENGEELEdVSVSVAGRIMAKRAFG-KLAFYDLRDDGGKIQLYADKKRLDLDEEeFEKLHSLVDRGDIVG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 187 FTGRATRTKAGELSLIPNEILQLTPCLHMLPHSHFGLKDKELRFRKRYLDLILNPRVKDNFVIRSKIITFLRRYLDNLGF 266
Cdd:PLN02502 169 VTGTPGKTKKGELSIFPTSFEVLTKCLLMLPDKYHGLTDQETRYRQRYLDLIANPEVRDIFRTRAKIISYIRRFLDDRGF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 267 LEVETPIMNQIAGGATAKPFITHHNDLDMNLFLRVAPELYHKMLVVGGIDRVYEVGRLFRNEGIDLTHNPEFTTCEFYMA 346
Cdd:PLN02502 249 LEVETPMLNMIAGGAAARPFVTHHNDLNMDLYLRIATELHLKRLVVGGFERVYEIGRQFRNEGISTRHNPEFTTCEFYQA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 347 YADYEDVIQLTEDLLSSMVMSIKGTYKIEYHPngpntepvYEVDFTPPFKRVHMYDGLAEKLGatLPDPSTLHTEEAREV 426
Cdd:PLN02502 329 YADYNDMMELTEEMVSGMVKELTGSYKIKYHG--------IEIDFTPPFRRISMISLVEEATG--IDFPADLKSDEANAY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 427 FDKLCRDNNVDCSAPRTTARLLDKLVGEYLESTFISPTFLIGHPQIMSPLAKWHRSIPGLTERFELFAVTREIANAYTEL 506
Cdd:PLN02502 399 LIAACEKFDVKCPPPQTTGRLLNELFEEFLEETLVQPTFVLDHPVEMSPLAKPHRSKPGLTERFELFINGRELANAFSEL 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17535925 507 NDPITQRQRFEQQAKDKDAGDDEAQMIDETFCNALEYGLPPTGGWGMGIDRLSMILTDNNNIKEVLLFPAMRPED 581
Cdd:PLN02502 479 TDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFPAMKPQD 553
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
83-582 |
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: 679.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 83 MRVRM--IEARRAAGDNPFPHKFNVTISLTDFITKYTPLEKEQVVEEIVSVAGRIHSKRESGsKLVFYDIHGEGTHIQIM 160
Cdd:COG1190 11 IRVRRekLEELREAGIDPYPNKFPRTHTAAEIREKYDELEAEEETGDEVSVAGRIMAKRDMG-KASFADLQDGSGRIQLY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 161 ANAKfHTGDVDFVTLHDrIKRGDIVGFTGRATRTKAGELSLIPNEILQLTPCLHMLPHSHFGLKDKELRFRKRYLDLILN 240
Cdd:COG1190 90 LRRD-ELGEEAYELFKL-LDLGDIVGVEGTVFRTKTGELSVKVEELTLLSKSLRPLPEKFHGLTDPETRYRQRYVDLIVN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 241 PRVKDNFVIRSKIITFLRRYLDNLGFLEVETPIMNQIAGGATAKPFITHHNDLDMNLFLRVAPELYHKMLVVGGIDRVYE 320
Cdd:COG1190 168 PEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVFE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 321 VGRLFRNEGIDLTHNPEFTTCEFYMAYADYEDVIQLTEDLLSSMVMSIKGTYKIEYhpNGpntepvYEVDFTPPFKRVHM 400
Cdd:COG1190 248 IGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGTTKVTY--QG------QEIDLSPPWRRITM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 401 YDGLAEKLGAtlpDPSTLHT-EEAREvfdkLCRDNNVDCSAPRTTARLLDKLVGEYLESTFISPTFLIGHPQIMSPLAKW 479
Cdd:COG1190 320 VEAIKEATGI---DVTPLTDdEELRA----LAKELGIEVDPGWGRGKLIDELFEELVEPKLIQPTFVTDYPVEVSPLAKR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 480 HRSIPGLTERFELFAVTREIANAYTELNDPITQRQRFEQQAKDKDAGDDEAQMIDETFCNALEYGLPPTGGWGMGIDRLS 559
Cdd:COG1190 393 HRDDPGLTERFELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGLGIGIDRLV 472
|
490 500
....*....|....*....|...
gi 17535925 560 MILTDNNNIKEVLLFPAMRPEDG 582
Cdd:COG1190 473 MLLTDSPSIRDVILFPLMRPEKK 495
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
83-581 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 671.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 83 MRVRM--IEARRAAGDNPFPHKFNVTISLTDFITKYTPLEKEQVVE--EIVSVAGRIHSKRESGsKLVFYDIHGEGTHIQ 158
Cdd:PRK00484 7 IAVRRekLAELREQGIDPYPNKFERTHTAAELRAKYDDKEKEELEEleIEVSVAGRVMLKRVMG-KASFATLQDGSGRIQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 159 IMANAKfHTGDvDFVTLHDRIKRGDIVGFTGRATRTKAGELSLIPNEILQLTPCLHMLPHSHFGLKDKELRFRKRYLDLI 238
Cdd:PRK00484 86 LYVSKD-DVGE-EALEAFKKLDLGDIIGVEGTLFKTKTGELSVKATELTLLTKSLRPLPDKFHGLTDVETRYRQRYVDLI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 239 LNPRVKDNFVIRSKIITFLRRYLDNLGFLEVETPIMNQIAGGATAKPFITHHNDLDMNLFLRVAPELYHKMLVVGGIDRV 318
Cdd:PRK00484 164 VNPESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARPFITHHNALDIDLYLRIAPELYLKRLIVGGFERV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 319 YEVGRLFRNEGIDLTHNPEFTTCEFYMAYADYEDVIQLTEDLLSSMVMSIKGTYKIEYhpNGpntepvYEVDFTPPFKRV 398
Cdd:PRK00484 244 YEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTY--QG------TEIDFGPPFKRL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 399 HMYDGLAEKLGAtlpDPSTLHTEEAREvfdkLCRDNNVDCSAPRTTARLLDKLVGEYLESTFISPTFLIGHPQIMSPLAK 478
Cdd:PRK00484 316 TMVDAIKEYTGV---DFDDMTDEEARA----LAKELGIEVEKSWGLGKLINELFEEFVEPKLIQPTFITDYPVEISPLAK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 479 WHRSIPGLTERFELFAVTREIANAYTELNDPITQRQRFEQQAKDKDAGDDEAQMIDETFCNALEYGLPPTGGWGMGIDRL 558
Cdd:PRK00484 389 RHREDPGLTERFELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIGIDRL 468
|
490 500
....*....|....*....|...
gi 17535925 559 SMILTDNNNIKEVLLFPAMRPED 581
Cdd:PRK00484 469 VMLLTDSPSIRDVILFPLMRPEK 491
|
|
| lysS_bact |
TIGR00499 |
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ... |
76-579 |
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: 616.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 76 DPQEYFNMRVRMIEARRAAGDNPFPHKFNVTISLTDFITKYTPLEKEQV--VEEIVSVAGRIHSKReSGSKLVFYDIHGE 153
Cdd:TIGR00499 1 ELNDQAQQRLEKLNRLRQTGNNPYLHKFERTHSAQEFQEKYADLSNEELkeKELKVSIAGRIKAIR-SMGKATFITLQDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 154 GTHIQIMANAKFHTGDVDFVTlHDRIKRGDIVGFTGRATRTKAGELSLIPNEILQLTPCLHMLPHSHFGLKDKELRFRKR 233
Cdd:TIGR00499 80 SGQIQLYVNKNKLPEDFYEFD-EYLLDLGDIIGVTGYPFKTKTGELSVKVTELQILTKCLQPLPDKWHGLTDQETRYRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 234 YLDLILNPRVKDNFVIRSKIITFLRRYLDNLGFLEVETPIMNQIAGGATAKPFITHHNDLDMNLFLRVAPELYHKMLVVG 313
Cdd:TIGR00499 159 YLDLIVNPDVRQTFLKRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKPFITHHNALDMDLYLRIAPELYLKRLIVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 314 GIDRVYEVGRLFRNEGIDLTHNPEFTTCEFYMAYADYEDVIQLTEDLLSSMVMSIKGTYKIEYhpngpNTEpvyEVDFTP 393
Cdd:TIGR00499 239 GLEKVYEIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTFIINY-----NDL---EIDLKP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 394 PFKRVHMYDGLAEKLGATLPDpstLHTEEAREVFDKLCRDNNVDCsaPRTTARLLDKLVGEYLESTFISPTFLIGHPQIM 473
Cdd:TIGR00499 311 PWKRITMVDALEMVTGIDFDI---LKDDETAKALAKEHGIEVAED--SLTLGHILNKFFEQFLEHTLIQPTFITHYPAEI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 474 SPLAKWHRSIPGLTERFELFAVTREIANAYTELNDPITQRQRFEQQAKDKDAGDDEAQMIDETFCNALEYGLPPTGGWGM 553
Cdd:TIGR00499 386 SPLAKRDPSNPEFTERFELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGI 465
|
490 500
....*....|....*....|....*.
gi 17535925 554 GIDRLSMILTDNNNIKEVLLFPAMRP 579
Cdd:TIGR00499 466 GIDRLVMLLTDAPSIRDVLLFPQLRP 491
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
37-579 |
0e+00 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 605.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 37 QKRLAKQAKKEQERLEKDAAKLNVAVADAPKVVREADpSDPQEYFNMRVRMIEARRAAGDNPFPHKFNVTISLTDFITKY 116
Cdd:PTZ00417 43 KQCFVTMSEKKEHVMEGEKKVRSVQASKDKKKEEEAE-VDPRLYYENRSKFIQEQKAKGINPYPHKFERTITVPEFVEKY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 117 TPLEK-EQVVEEIVSVAGRIHSKRESGSKLVFYDIHGEGTHIQIMANAKFHTGD-VDFVTLHDRIKRGDIVGFTGRATRT 194
Cdd:PTZ00417 122 QDLASgEHLEDTILNVTGRIMRVSASGQKLRFFDLVGDGAKIQVLANFAFHDHTkSNFAECYDKIRRGDIVGIVGFPGKS 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 195 KAGELSLIPNEILQLTPCLHMLPHShFGLKDKELRFRKRYLDLILNPRVKDNFVIRSKIITFLRRYLDNLGFLEVETPIM 274
Cdd:PTZ00417 202 KKGELSIFPKETIILSPCLHMLPMK-YGLKDTEIRYRQRYLDLMINESTRSTFITRTKIINYLRNFLNDRGFIEVETPTM 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 275 NQIAGGATAKPFITHHNDLDMNLFLRVAPELYHKMLVVGGIDRVYEVGRLFRNEGIDLTHNPEFTTCEFYMAYADYEDVI 354
Cdd:PTZ00417 281 NLVAGGANARPFITHHNDLDLDLYLRIATELPLKMLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLI 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 355 QLTEDLLSSMVMSIKGTYKIEYHPNGPNTEPVyEVDFTPPFKRVHMYDGLAEKLGATLPDPstLHTEEAREVFDKLCRDN 434
Cdd:PTZ00417 361 KWSEDFFSQLVMHLFGTYKILYNKDGPEKDPI-EIDFTPPYPKVSIVEELEKLTNTKLEQP--FDSPETINKMINLIKEN 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 435 NVDCSAPRTTARLLDKLVGEYLESTFIS-PTFLIGHPQIMSPLAKWHRSIPGLTERFELFAVTREIANAYTELNDPITQR 513
Cdd:PTZ00417 438 KIEMPNPPTAAKLLDQLASHFIENKYPNkPFFIIEHPQIMSPLAKYHRSKPGLTERLEMFICGKEVLNAYTELNDPFKQK 517
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17535925 514 QRFEQQAKDKDAGDDEAQMIDETFCNALEYGLPPTGGWGMGIDRLSMILTDNNNIKEVLLFPAMRP 579
Cdd:PTZ00417 518 ECFSAQQKDREKGDAEAFQFDAAFCTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFPTMRP 583
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
240-579 |
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: 599.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 240 NPRVKDNFVIRSKIITFLRRYLDNLGFLEVETPIMNQIAGGATAKPFITHHNDLDMNLFLRVAPELYHKMLVVGGIDRVY 319
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 320 EVGRLFRNEGIDLTHNPEFTTCEFYMAYADYEDVIQLTEDLLSSMVMSIKGTYKIEYhpngpntePVYEVDFTPPFKRVH 399
Cdd:cd00775 81 EIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIEY--------GGKELDFTPPFKRVT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 400 MYDGLAEKLGATLPDPSTLHTEEAREVFDKLCRDNNVDcsaPRTTARLLDKLVGEYLESTFISPTFLIGHPQIMSPLAKW 479
Cdd:cd00775 153 MVDALKEKTGIDFPELDLEQPEELAKLLAKLIKEKIEK---PRTLGKLLDKLFEEFVEPTLIQPTFIIDHPVEISPLAKR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 480 HRSIPGLTERFELFAVTREIANAYTELNDPITQRQRFEQQAKDKDAGDDEAQMIDETFCNALEYGLPPTGGWGMGIDRLS 559
Cdd:cd00775 230 HRSNPGLTERFELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLV 309
|
330 340
....*....|....*....|
gi 17535925 560 MILTDNNNIKEVLLFPAMRP 579
Cdd:cd00775 310 MLLTDSNSIRDVILFPAMRP 329
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
75-578 |
6.66e-144 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 431.38 E-value: 6.66e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 75 SDPQEYFNMRVRMIEARRAAGDNPFPHK-FNVTISLTDFITKYTPLEK-EQVVEEIVSVAGRIHSKRESGsKLVFYDIHG 152
Cdd:PTZ00385 54 SKASATKTVTQEASRAPRSKLDLPAAYSsFRGITPISEVRERYGYLASgDRAAQATVRVAGRVTSVRDIG-KIIFVTIRS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 153 EGTHIQIMANAKFHTGDVDFVTLHDRIKRGDIVGFTGRATRTKAGELSLIPNEILQLTP--------CLHMLPHSHfgLK 224
Cdd:PTZ00385 133 NGNELQVVGQVGEHFTREDLKKLKVSLRVGDIIGADGVPCRMQRGELSVAASRMLILSPyvctdqvvCPNLRGFTV--LQ 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 225 DKELRFRKRYLDLILNPRVKDNFVIRSKIITFLRRYLDNLGFLEVETPIMNQIAGGATAKPFITHHNDLDMNLFLRVAPE 304
Cdd:PTZ00385 211 DNDVKYRYRFTDMMTNPCVIETIKKRHVMLQALRDYFNERNFVEVETPVLHTVASGANAKSFVTHHNANAMDLFLRVAPE 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 305 LYHKMLVVGGIDRVYEVGRLFRNEGIDLTHNPEFTTCEFYMAYADYEDVIQLTEDLLSSMVMSIKGTYKIEYHPNGPNTE 384
Cdd:PTZ00385 291 LHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTSCEFYAAYHTYEDLMPMTEDIFRQLAMRVNGTTVVQIYPENAHGN 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 385 PVyEVDFTPPFKRVHMYDGLAEKLGATLPDPSTLHTEEAREVFDKLCRDNNVDCSAPRTTARLLDKLVGEYLESTFISPT 464
Cdd:PTZ00385 371 PV-TVDLGKPFRRVSVYDEIQRMSGVEFPPPNELNTPKGIAYMSVVMLRYNIPLPPVRTAAKMFEKLIDFFITDRVVEPT 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 465 FLIGHPQIMSPLAKWHRSIPGLTERFELFAVTREIANAYTELNDPITQRQRFEQQAKDKDAGDDEAQMIDETFCNALEYG 544
Cdd:PTZ00385 450 FVMDHPLFMSPLAKEQVSRPGLAERFELFVNGIEYCNAYSELNDPHEQYHRFQQQLVDRQGGDEEAMPLDETFLKSLQVG 529
|
490 500 510
....*....|....*....|....*....|....
gi 17535925 545 LPPTGGWGMGIDRLSMILTDNNNIKEVLLFPAMR 578
Cdd:PTZ00385 530 LPPTAGWGMGIDRALMLLTNSSNIRDGIIFPLLR 563
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
35-581 |
2.45e-137 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 427.07 E-value: 2.45e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 35 REQKRLAKQAKKEQERLEKDAAKLNVAvADAPKVVReadPSDPQEyfnMRVRM--IEARRAAGDNPFPHKFNVTISLTDF 112
Cdd:PRK02983 573 TGHHPAVPERLAASGLLHHDGSAPDVA-ATAPDAPE---PRLPEQ---VRVRLakLEALRAAGVDPYPVGVPPTHTVAEA 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 113 ItkytplekEQVVEEIVSVAGRIHSKRESGsKLVFYDIHGEGTHIQIMANAKfhTGDVDFVTLHDR-IKRGDIVGFTGRA 191
Cdd:PRK02983 646 L--------DAPTGEEVSVSGRVLRIRDYG-GVLFADLRDWSGELQVLLDAS--RLEQGSLADFRAaVDLGDLVEVTGTM 714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 192 TRTKAGELSLIPNEILQLTPCLHMLPHSHFGLKDKELRFRKRYLDLILNPRVKDNFVIRSKIITFLRRYLDNLGFLEVET 271
Cdd:PRK02983 715 GTSRNGTLSLLVTSWRLAGKCLRPLPDKWKGLTDPEARVRQRYLDLAVNPEARDLLRARSAVVRAVRETLVARGFLEVET 794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 272 PIMNQIAGGATAKPFITHHNDLDMNLFLRVAPELYHKMLVVGGIDRVYEVGRLFRNEGIDLTHNPEFTTCEFYMAYADYE 351
Cdd:PRK02983 795 PILQQVHGGANARPFVTHINAYDMDLYLRIAPELYLKRLCVGGVERVFELGRNFRNEGVDATHNPEFTLLEAYQAHADYD 874
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 352 DVIQLTEDLLSSMVMSIKGTYKIEyhpnGPNTE-PVYEVDFTPPFKRVHMYDGLAEKLGATLpDPSTlHTEEARevfdKL 430
Cdd:PRK02983 875 TMRDLTRELIQNAAQAAHGAPVVM----RPDGDgVLEPVDISGPWPVVTVHDAVSEALGEEI-DPDT-PLAELR----KL 944
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 431 CRDNNVDCSAPRTTARLLDKLVGEYLESTFISPTFLIGHPQIMSPLAKWHRSIPGLTERFELFAVTREIANAYTELNDPI 510
Cdd:PRK02983 945 CDAAGIPYRTDWDAGAVVLELYEHLVEDRTTFPTFYTDFPTSVSPLTRPHRSDPGLAERWDLVAWGVELGTAYSELTDPV 1024
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17535925 511 TQRQRFEQQAKDKDAGDDEAQMIDETFCNALEYGLPPTGGWGMGIDRLSMILTdNNNIKEVLLFPAMRPED 581
Cdd:PRK02983 1025 EQRRRLTEQSLLAAGGDPEAMELDEDFLQALEYAMPPTGGLGMGVDRLVMLLT-GRSIRETLPFPLVKPRQ 1094
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
129-580 |
9.51e-117 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 356.29 E-value: 9.51e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 129 VSVAGRIHSKRESGsKLVFYDIHGEGTHIQI-MANAKFHTGdvdfvTLHDRIKR---GDIVGFTGRATRTKAGELSLIPN 204
Cdd:PRK12445 68 VSVAGRMMTRRIMG-KASFVTLQDVGGRIQLyVARDSLPEG-----VYNDQFKKwdlGDIIGARGTLFKTQTGELSIHCT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 205 EILQLTPCLHMLPHSHFGLKDKELRFRKRYLDLILNPRVKDNFVIRSKIITFLRRYLDNLGFLEVETPIMNQIAGGATAK 284
Cdd:PRK12445 142 ELRLLTKALRPLPDKFHGLQDQEVRYRQRYLDLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASAR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 285 PFITHHNDLDMNLFLRVAPELYHKMLVVGGIDRVYEVGRLFRNEGIDLTHNPEFTTCEFYMAYADYEDVIQLTEDLLSSM 364
Cdd:PRK12445 222 PFITHHNALDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 365 VMSIKGTYKIEYhpngpnTEPVYevDFTPPFKRVHMYDGLAEKLGATlpDPSTLHTEEAREVfdkLCRDNNVDCSAPRTT 444
Cdd:PRK12445 302 AQEVLGTTKVTY------GEHVF--DFGKPFEKLTMREAIKKYRPET--DMADLDNFDAAKA---LAESIGITVEKSWGL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 445 ARLLDKLVGEYLESTFISPTFLIGHPQIMSPLAKWHRSIPGLTERFELFAVTREIANAYTELNDPITQRQRFEQQAKDKD 524
Cdd:PRK12445 369 GRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKA 448
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 17535925 525 AGDDEAQMIDETFCNALEYGLPPTGGWGMGIDRLSMILTDNNNIKEVLLFPAMRPE 580
Cdd:PRK12445 449 AGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFPAMRPQ 504
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
225-578 |
4.52e-115 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 345.32 E-value: 4.52e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 225 DKELRFRKRYLDLiLNPRVKDNFVIRSKIITFLRRYLDNLGFLEVETPIMNQIAGGATAKPFITHHNDLDMNLFLRVAPE 304
Cdd:pfam00152 1 DEETRLKYRYLDL-RRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 305 LYHKMLVVGGIDRVYEVGRLFRNEGIDLTHNPEFTTCEFYMAYADYEDVIQLTEDLLSSMVMSIKGTYKIEYHPngpnte 384
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGG------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 385 pvYEVDFTPPFKRVHMYDGLAEKLGatlpdpstlhteearevfdKLCRDNNVDCSAPRTtaRLLDKLVgeyLESTFISPT 464
Cdd:pfam00152 154 --TLLDLKKPFPRITYAEAIEKLNG-------------------KDVEELGYGSDKPDL--RFLLELV---IDKNKFNPL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 465 FLIGHPQIMSPLAKWHRS-IPGLTERFELFAVTREIANAYTELNDPITQRQRFEQQAKDKdagdDEAQMIDETFCNALEY 543
Cdd:pfam00152 208 WVTDFPAEHHPFTMPKDEdDPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDP----EEAEEKFGFYLDALKY 283
|
330 340 350
....*....|....*....|....*....|....*
gi 17535925 544 GLPPTGGWGMGIDRLSMILTDNNNIKEVLLFPAMR 578
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 ... |
247-579 |
3.29e-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: 3.29e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 247 FVIRSKIITFLRRYLDNLGFLEVETPIMNQIAGGATAKPFITHHNDLDMNLFLRVAPELYHKMLVVGGIDRVYEVGRLFR 326
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 327 NEGIDLTHNPEFTTCEFYMAYADYEDVIQLTEDLLSSMVMSIKGTYKIEYHpngpntepVYEVDFTPPFKRVHMYDGLaE 406
Cdd:cd00669 81 NEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYG--------FELEDFGLPFPRLTYREAL-E 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 407 KLGAtlpdpstlhteearevfdklcrdnnvdcsaprttarlldklvgeylestfisPTFLIGHP-QIMSPLAKWHRSIPG 485
Cdd:cd00669 152 RYGQ----------------------------------------------------PLFLTDYPaEMHSPLASPHDVNPE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 486 LTERFELFAVTREIANAYTELNDPITQRQRFEQQAKDKDAGDDEaqmiDETFCNALEYGLPPTGGWGMGIDRLSMILTDN 565
Cdd:cd00669 180 IADAFDLFINGVEVGNGSSRLHDPDIQAEVFQEQGINKEAGMEY----FEFYLKALEYGLPPHGGLGIGIDRLIMLMTNS 255
|
330
....*....|....
gi 17535925 566 NNIKEVLLFPAMRP 579
Cdd:cd00669 256 PTIREVIAFPKMRR 269
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
250-572 |
5.67e-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: 5.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 250 RSKIITFLRRYLDNLGFLEVETPIMnQIAGGATA--KPFIT---HHNDLDMNLFLRVAPELYHKMLVVGGIDRVYEVGRL 324
Cdd:COG2269 9 RARLLAAIRAFFAERGVLEVETPAL-SVAPGTDPhlDSFATefiGPDGGGRPLYLHTSPEFAMKRLLAAGSGPIYQIAKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 325 FRNEGIDLTHNPEFTTCEFYMAYADYEDVIQLTEDLLSSmvmsikgtykieyhpngpntepVYEVDFTPPFKRVHMYDGL 404
Cdd:COG2269 88 FRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQL----------------------VLGAAGFAPAERLSYQEAF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 405 AEKLGatlPDPSTLHTEEAREVfdklCRDNNVDCSAPRTTARLLDKLVGEYLESTFI--SPTFLIGHPQIMSPLAKWHRS 482
Cdd:COG2269 146 LRYLG---IDPLTADLDELAAA----AAAAGLRVADDDDRDDLLDLLLSERVEPQLGrdRPTFLYDYPASQAALARISPD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 483 IPGLTERFELFAVTREIANAYTELNDPITQRQRFEQQAKDKDAGDDEAQMIDETFCNALEYGLPPTGGWGMGIDRLSMIL 562
Cdd:COG2269 219 DPRVAERFELYACGVELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLA 298
|
330
....*....|
gi 17535925 563 TDNNNIKEVL 572
Cdd:COG2269 299 LGAERIDDVL 308
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
260-572 |
1.13e-49 |
|
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: 173.89 E-value: 1.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 260 YLDNLGFLEVETPIMnqIAGGATA---KPFITH---HNDLDMNLFLRVAPELYHKMLVVGGIDRVYEVGRLFRNEGIDLT 333
Cdd:TIGR00462 1 FFAERGVLEVETPLL--SPAPVTDphlDAFATEfvgPDGQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 334 HNPEFTTCEFYMAYADYEDVIQLTEDLLSSMVMsikgtykieyhpngpntepvyevDFTPPFKRVHMYDGLAEKLGAtlp 413
Cdd:TIGR00462 79 HNPEFTMLEWYRPGFDYHDLMDEVEALLQELLG-----------------------DPFAPAERLSYQEAFLRYAGI--- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 414 DPSTlhteEAREVFDKLCRDNNVDCSAPRTTARLLDKLVGEYLEST--FISPTFLIGHPQIMSPLAKWHRSIPGLTERFE 491
Cdd:TIGR00462 133 DPLT----ASLAELQAAAAAHGIRASEEDDRDDLLDLLFSEKVEPHlgFGRPTFLYDYPASQAALARISPDDPRVAERFE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 492 LFAVTREIANAYTELNDPITQRQRFEQQAKDKDAGDDEAQMIDETFCNALEYGLPPTGGWGMGIDRLSMILTDNNNIKEV 571
Cdd:TIGR00462 209 LYIKGLELANGFHELTDAAEQRRRFEADNALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDV 288
|
.
gi 17535925 572 L 572
Cdd:TIGR00462 289 L 289
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
128-237 |
5.48e-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: 157.64 E-value: 5.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 128 IVSVAGRIHSKRESGsKLVFYDIHGEGTHIQIMANAKFHtGDVDFVTLHDRIKRGDIVGFTGRATRTKAGELSLIPNEIL 207
Cdd:cd04322 1 EVSVAGRIMSKRGSG-KLSFADLQDESGKIQVYVNKDDL-GEEEFEDFKKLLDLGDIIGVTGTPFKTKTGELSIFVKEFT 78
|
90 100 110
....*....|....*....|....*....|
gi 17535925 208 QLTPCLHMLPHSHFGLKDKELRFRKRYLDL 237
Cdd:cd04322 79 LLSKSLRPLPEKFHGLTDVETRYRQRYLDL 108
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
244-571 |
2.91e-42 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 154.32 E-value: 2.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 244 KDNFVIRSKIITFLRRYLDNLGFLEVETPIMNQiaggATA-----KPFITHHNDLD----MNLFLRVAPElYH-KMLVVG 313
Cdd:PRK09350 2 IPNLLKRAKIIAEIRRFFADRGVLEVETPILSQ----ATVtdihlVPFETRFVGPGasqgKTLWLMTSPE-YHmKRLLAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 314 GIDRVYEVGRLFRNEGIDLTHNPEFTTCEFYMAYADYEDVIQLTEDLLSsmvmsikgtykieyhpngpntepvyEVDFTP 393
Cdd:PRK09350 77 GSGPIFQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQ-------------------------QVLDCE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 394 PFKRVHMYDGLAEKLGAtlpDPSTLHTEEAREVFDKLCRDNNVDCSAPRTTarLLDKLVGEYLEST--FISPTFLIGHPQ 471
Cdd:PRK09350 132 PAESLSYQQAFLRYLGI---DPLSADKTQLREVAAKLGLSNIADEEEDRDT--LLQLLFTFGVEPNigKEKPTFVYHFPA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 472 IMSPLAKWHRSIPGLTERFELFAVTREIANAYTELNDPITQRQRFEQQAKDKDAGDDEAQMIDETFCNALEYGLPPTGGW 551
Cdd:PRK09350 207 SQAALAKISTEDHRVAERFEVYFKGIELANGFHELTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCSGV 286
|
330 340
....*....|....*....|
gi 17535925 552 GMGIDRLSMILTDNNNIKEV 571
Cdd:PRK09350 287 ALGVDRLIMLALGAESISEV 306
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
114-575 |
2.40e-37 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 143.79 E-value: 2.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 114 TKYTPLEKEQVVEEIVSVAGRIHSKRESGsKLVFYDIHG-EGThIQIMANAKFHTGDVDFVtlhDRIKRGDIVGFTGRAT 192
Cdd:PRK05159 4 RHLTSELTPELDGEEVTLAGWVHEIRDLG-GIAFLILRDrSGI-IQVVVKKKVDEELFETI---KKLKRESVVSVTGTVK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 193 ---RTKAGeLSLIPNEILQLTPCLHMLPHSHFGLKDKEL--RFRKRYLDLiLNPRVKDNFVIRSKIITFLRRYLDNLGFL 267
Cdd:PRK05159 79 anpKAPGG-VEVIPEEIEVLNKAEEPLPLDISGKVLAELdtRLDNRFLDL-RRPRVRAIFKIRSEVLRAFREFLYENGFT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 268 EVETP-IMNQIA-GGATAKPfithhndldMNLFLRVA-----PELYHKMLVVGGIDRVYEVGRLFRNEGIDLT-HNPEFT 339
Cdd:PRK05159 157 EIFTPkIVASGTeGGAELFP---------IDYFEKEAylaqsPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSrHLNEYT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 340 TCEFYMAYAD-YEDVIQLTEDLLSSMVMSIKGTYKIEYhpngpntepvyevdftppfkrvhmydglaEKLGATLPDPST- 417
Cdd:PRK05159 228 SIDVEMGFIDdHEDVMDLLENLLRYMYEDVAENCEKEL-----------------------------ELLGIELPVPETp 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 418 ---LHTEEAREVFDKLCRDNNVDCSAPRTTARLLDKLVGEYLESTFIsptFLIGHPQIMSPL-AKWHRSIPGLTERFELF 493
Cdd:PRK05159 279 iprITYDEAIEILKSKGNEISWGDDLDTEGERLLGEYVKEEYGSDFY---FITDYPSEKRPFyTMPDEDDPEISKSFDLL 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 494 AVTREIANAYTELNDPITQRQRFEQQAKDKDAGddeaqmidETFCNALEYGLPPTGGWGMGIDRLSMILTDNNNIKEVLL 573
Cdd:PRK05159 356 FRGLEITSGGQRIHRYDMLVESIKEKGLNPESF--------EFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVL 427
|
..
gi 17535925 574 FP 575
Cdd:PRK05159 428 FP 429
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
129-575 |
9.88e-37 |
|
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: 141.89 E-value: 9.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 129 VSVAGRIHSKRESGsKLVFYDIHGEGTHIQIMANAKFhTGDvDFVTLHDRIKRGDIVGFTGRATRTKA--GELSLIPNEI 206
Cdd:TIGR00458 15 VTFMGWVHEIRDLG-GLIFVLLRDREGLIQITAPAKK-VSK-NLFKWAKKLNLESVVAVRGIVKIKEKapGGFEIIPTKI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 207 LQLTPCLHMLPhshFGLKDK-----ELRFRKRYLDLiLNPRVKDNFVIRSKIITFLRRYLDNLGFLEVETP-IMNQIAGG 280
Cdd:TIGR00458 92 EVINEAKEPLP---LDPTEKvpaelDTRLDYRFLDL-RRPTVQAIFRIRSGVLESVREFLAEEGFIEVHTPkLVASATEG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 281 ATAKPFITHhndLDMNLFLRVAPELYHKMLVVGGIDRVYEVGRLFRNEGIDLT-HNPEFTTCEFYMAYADYEDVIqlteD 359
Cdd:TIGR00458 168 GTELFPITY---FEREAFLGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNTHrHLNEATSIDIEMAFEDHHDVM----D 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 360 LLSSMVMSIkgtykieyhpngpnTEPVYEvdftppfKRVHMYdglaEKLGATLPDPST----LHTEEAREvfdkLCRDNN 435
Cdd:TIGR00458 241 ILEELVVRV--------------FEDVPE-------RCAHQL----ETLEFKLEKPEGkfvrLTYDEAIE----MANAKG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 436 VDCSAPRTTARLLDKLVGEYLESTFisptFLIGHPQIMSPL-AKWHRSIPGLTERFELFAVTREIANAYTELNDPITQRQ 514
Cdd:TIGR00458 292 VEIGWGEDLSTEAEKALGEEMDGLY----FITDWPTEIRPFyTMPDEDNPEISKSFDLMYRDLEISSGAQRIHLHDLLVE 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17535925 515 RFEQQAKDKDAGDDeaqmidetFCNALEYGLPPTGGWGMGIDRLSMILTDNNNIKEVLLFP 575
Cdd:TIGR00458 368 RIKAKGLNPEGFKD--------YLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFP 420
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
125-578 |
1.07e-30 |
|
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: 124.78 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 125 VEEIVSVAGRIHSKRESGsKLVFYDIH-GEGThIQIMANAKfhtgDVDFVTLHDRIKRGDIVGFTG--RATRTKAGELSL 201
Cdd:COG0017 13 VGQEVTVAGWVRTKRDSG-GISFLILRdGSGF-IQVVVKKD----KLENFEEAKKLTTESSVEVTGtvVESPRAPQGVEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 202 IPNEILQLTPCLHMLPhshFGLKDKELRFR--KRYLDLiLNPRVKDNFVIRSKIITFLRRYLDNLGFLEVETPIMnqIA- 278
Cdd:COG0017 87 QAEEIEVLGEADEPYP---LQPKRHSLEFLldNRHLRL-RTNRFGAIFRIRSELARAIREFFQERGFVEVHTPII--TAs 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 279 ---GGAtakpfithhndldmNLF----------LRVAPELYHKMLVvGGIDRVYEVGRLFRNEGIDLT-HNPEFTTCEFY 344
Cdd:COG0017 161 ateGGG--------------ELFpvdyfgkeayLTQSGQLYKEALA-MALEKVYTFGPTFRAEKSNTRrHLAEFWMIEPE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 345 MAYADYEDVIQLTEDLLSSMVMSIKGTYKIEYHPNGPNTEPVyEVDFTPPFKRVHMYDG--LAEKLGATLPDPSTLHTEE 422
Cdd:COG0017 226 MAFADLEDVMDLAEEMLKYIIKYVLENCPEELEFLGRDVERL-EKVPESPFPRITYTEAieILKKSGEKVEWGDDLGTEH 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 423 ARevfdklcrdnnvdcsaprttarlldkLVGEYLESTFIsptFLIGHP-QIMSPLAKWHRSIPGLTERFELfavtreIAN 501
Cdd:COG0017 305 ER--------------------------YLGEEFFKKPV---FVTDYPkEIKAFYMKPNPDDPKTVAAFDL------LAP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 502 AYTELndpIT--QRQ-RFEQ-QAKDKDAGDDEAQMidETFCNALEYGLPPTGGWGMGIDRLSMILTDNNNIKEVLLFPAM 577
Cdd:COG0017 350 GIGEI---IGgsQREhRYDVlVERIKEKGLDPEDY--EWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRD 424
|
.
gi 17535925 578 R 578
Cdd:COG0017 425 P 425
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
227-575 |
9.57e-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: 9.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 227 ELRFRKRYLDLiLNPRVKDNFVIRSKIITFLRRYLDNLGFLEVETPIM--NQIAGGATAKPFithhNDLDMNLFLRVAPE 304
Cdd:cd00776 5 ETLLDNRHLDL-RTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKItsTDTEGGAELFKV----SYFGKPAYLAQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 305 LYHKMLvVGGIDRVYEVGRLFRNEGIDLT-HNPEFTTCEFYMAYA-DYEDVIQLTEDLLSSMVMSIKGTYK--IEYHPNG 380
Cdd:cd00776 80 LYKEML-IAALERVYEIGPVFRAEKSNTRrHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAkeLELVNQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 381 PNTEPVYEvdftPPFKRVHMYDG--LAEKLGATLPDPST--LHTEEarevfdklcrdnnvdcsaprttarllDKLVGEYL 456
Cdd:cd00776 159 NRELLKPL----EPFPRITYDEAieLLREKGVEEEVKWGedLSTEH--------------------------ERLLGEIV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 457 ESTFIsptFLIGHPQIMSPL-AKWHRSIPGLTERFELFAvtR---EIANAYTELNDPITQRQRFEQQAKDKDAgddeaqm 532
Cdd:cd00776 209 KGDPV---FVTDYPKEIKPFyMKPDDDNPETVESFDLLM--PgvgEIVGGSQRIHDYDELEERIKEHGLDPES------- 276
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 17535925 533 iDETFCNALEYGLPPTGGWGMGIDRLSMILTDNNNIKEVLLFP 575
Cdd:cd00776 277 -FEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
227-575 |
5.21e-24 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 106.30 E-value: 5.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 227 ELRFRKRYLDLiLNPRVKDNFVIRSKIITFLRRYLDNLGFLEVETPIMnqiaGGAT---AKPFI----THHNDldmnlF- 298
Cdd:PRK00476 122 ELRLKYRYLDL-RRPEMQKNLKLRSKVTSAIRNFLDDNGFLEIETPIL----TKSTpegARDYLvpsrVHPGK-----Fy 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 299 -LRVAPELYHKMLVVGGIDRVYEVGRLFRNEgiDLTHN--PEFTT--CEfyMAYADYEDVIQLTEDLLSSMVMSIKGtyk 373
Cdd:PRK00476 192 aLPQSPQLFKQLLMVAGFDRYYQIARCFRDE--DLRADrqPEFTQidIE--MSFVTQEDVMALMEGLIRHVFKEVLG--- 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 374 ieyhpngpntepvyeVDFTPPFKRvhM-YDGLAEKLGATLPD---PSTLH--TEEARE----VFDKLCRDN------NVD 437
Cdd:PRK00476 265 ---------------VDLPTPFPR--MtYAEAMRRYGSDKPDlrfGLELVdvTDLFKDsgfkVFAGAANDGgrvkaiRVP 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 438 CSAPRTTARLLDKL---VGEY--------------LEST---FISPT------------------FLIGHPQIMS----- 474
Cdd:PRK00476 328 GGAAQLSRKQIDELtefAKIYgakglayikvnedgLKGPiakFLSEEelaallertgakdgdlifFGADKAKVVNdalga 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 475 -------------------------PLAKW----------H----RSIPGLTERFELFAVTREIANAY------TEL--- 506
Cdd:PRK00476 408 lrlklgkelglidedkfaflwvvdfPMFEYdeeegrwvaaHhpftMPKDEDLDELETTDPGKARAYAYdlvlngYELggg 487
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17535925 507 ----NDPITQRQRF------EQQAKDKDAGddeaqMIDetfcnALEYGLPPTGGWGMGIDRLSMILTDNNNIKEVLLFP 575
Cdd:PRK00476 488 siriHRPEIQEKVFeilgisEEEAEEKFGF-----LLD-----ALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
227-397 |
1.31e-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: 102.00 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 227 ELRFRKRYLDLiLNPRVKDNFVIRSKIITFLRRYLDNLGFLEVETPIMnqIA---GGAtakpfithhNDldmnlFL---R 300
Cdd:COG0173 123 ELRLKYRYLDL-RRPEMQKNLILRHKVTKAIRNYLDENGFLEIETPIL--TKstpEGA---------RD-----YLvpsR 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 301 V----------APELYHKMLVVGGIDRVYEVGRLFRNEgiDLTHN--PEFTT--CEfyMAYADYEDVIQLTEDLLSSMVM 366
Cdd:COG0173 186 VhpgkfyalpqSPQLFKQLLMVSGFDRYFQIARCFRDE--DLRADrqPEFTQldIE--MSFVDQEDVFELMEGLIRHLFK 261
|
170 180 190
....*....|....*....|....*....|.
gi 17535925 367 SIKGtykieyhpngpntepvyeVDFTPPFKR 397
Cdd:COG0173 262 EVLG------------------VELPTPFPR 274
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
161-414 |
2.32e-22 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 101.40 E-value: 2.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 161 ANAKFHTGDVDFVTLHD----------RIKRGDIVGFTGRA---------TRTKAGELSLIPNEILQLTPCLHMLPHSHF 221
Cdd:PLN02903 93 LDVRDHTGIVQVVTLPDefpeahrtanRLRNEYVVAVEGTVrsrpqespnKKMKTGSVEVVAESVDILNVVTKSLPFLVT 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 222 GLKD------KELRFRKRYLDLILnPRVKDNFVIRSKIITFLRRYL-DNLGFLEVETPIMNQiaggatakpfITHHNDLD 294
Cdd:PLN02903 173 TADEqkdsikEEVRLRYRVLDLRR-PQMNANLRLRHRVVKLIRRYLeDVHGFVEIETPILSR----------STPEGARD 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 295 MNLFLRV----------APELYHKMLVVGGIDRVYEVGRLFRNEGIDLTHNPEFTTCEFYMAYADYEDVIQLTEDLLSSM 364
Cdd:PLN02903 242 YLVPSRVqpgtfyalpqSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEFTQLDMELAFTPLEDMLKLNEDLIRQV 321
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 17535925 365 VMSIKGtykieyhpngpntepvyeVDFTPPFKRVhMYDGLAEKLGATLPD 414
Cdd:PLN02903 322 FKEIKG------------------VQLPNPFPRL-TYAEAMSKYGSDKPD 352
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
225-364 |
2.78e-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: 2.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 225 DKELRFRKRYLDlILNPRVKDNFVIRSKIITFLRRYLDNLGFLEVETPIMNQiAGGATAKPFITHHNDLDMNLF-LRVAP 303
Cdd:PRK12820 135 NEDLRLQYRYLD-IRRPAMQDHLAKRHRIIKCARDFLDSRGFLEIETPILTK-STPEGARDYLVPSRIHPKEFYaLPQSP 212
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17535925 304 ELYHKMLVVGGIDRVYEVGRLFRNEGIDLTHNPEFTTCEFYMAYADYEDVIQLTEDLLSSM 364
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 ... |
249-388 |
3.65e-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: 3.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 249 IRSKIITFLRRYLDNLGFLEVETPIMNQIAGGATA----KPFITHHNDLDMNLFLRVAPELYHKMLVVGGI----DRVYE 320
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAghepKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIrklpLRLAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 321 VGRLFRNEGI--DLTHNPEFTTCEFYMAYADYED------VIQLTEDLLSSMVMSIKGTYKIEY------HPNGPNTEPV 386
Cdd:cd00768 81 IGPAFRNEGGrrGLRRVREFTQLEGEVFGEDGEEasefeeLIELTEELLRALGIKLDIVFVEKTpgefspGGAGPGFEIE 160
|
..
gi 17535925 387 YE 388
Cdd:cd00768 161 VD 162
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
115-575 |
3.70e-18 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 88.13 E-value: 3.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 115 KYTP---LEKEQVVEEIVSVAGRIHSKRESGsKLVFYDIHgEGTH-IQIMANAKfhtGDV--DFVTLHDRIKRGDIVGFT 188
Cdd:PTZ00401 64 TFIPvavLSKPELVDKTVLIRARVSTTRKKG-KMAFMVLR-DGSDsVQAMAAVE---GDVpkEMIDFIGQIPTESIVDVE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 189 GRA-------TRTKAGELSLIPNEILQLTPCLHMLPhshFGLKDK-------------ELRFRKRYLDLiLNPRVKDNFV 248
Cdd:PTZ00401 139 ATVckveqpiTSTSHSDIELKVKKIHTVTESLRTLP---FTLEDAsrkesdegakvnfDTRLNSRWMDL-RTPASGAIFR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 249 IRSKIITFLRRYLDNLGFLEVETPIMNQIAGGATAKPFITHHNDLDMnlFLRVAPELYHKMLVVGGIDRVYEVGRLFRNE 328
Cdd:PTZ00401 215 LQSRVCQYFRQFLIDSDFCEIHSPKIINAPSEGGANVFKLEYFNRFA--YLAQSPQLYKQMVLQGDVPRVFEVGPVFRSE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 329 GIDL-THNPEFTTCEFYMAYAD-YEDVIQLTEDLLSSMVMSIKGtykieyhpngpNTEPVYEVDFTPPFKRVhMYDGLAE 406
Cdd:PTZ00401 293 NSNThRHLTEFVGLDVEMRINEhYYEVLDLAESLFNYIFERLAT-----------HTKELKAVCQQYPFEPL-VWKLTPE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 407 KL-----GATLPD--PSTLHTEEAREVFDKLCRDNNVDCSA----------------PRTTARLLDKLVGE-YLESTFIS 462
Cdd:PTZ00401 361 RMkelgvGVISEGvePTDKYQARVHNMDSRMLRINYMHCIEllntvleekmaptddiNTTNEKLLGKLVKErYGTDFFIS 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 463 PTFlighPQIMSPLakWHRSIPG---LTERFELFAVTREIANAYTELNDPITQRQRFEQQAKDKDAGDDeaqmidetFCN 539
Cdd:PTZ00401 441 DRF----PSSARPF--YTMECKDderFTNSYDMFIRGEEISSGAQRIHDPDLLLARAKMLNVDLTPIKE--------YVD 506
|
490 500 510
....*....|....*....|....*....|....*.
gi 17535925 540 ALEYGLPPTGGWGMGIDRLSMILTDNNNIKEVLLFP 575
Cdd:PTZ00401 507 SFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFP 542
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
42-575 |
4.54e-15 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 78.21 E-value: 4.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 42 KQAKKEQERLEKDAAKLNVAVADAPkvvrEADPSDPQEYFNMRVRMIEARRAAGDNpfphkfnvtisltdfitKYTPLE- 120
Cdd:PLN02850 16 KAAKKAAAKAEKLRREATAKAAAAS----LEDEDDPLASNYGDVPLEELQSKVTGR-----------------EWTDVSd 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 121 -KEQVVEEIVSVAGRIHSKRESGsKLVFYDIHGEGTHIQIMANAKFHTGDVDFVTLHDRIKRGDIVGFTGRATRTKAG-- 197
Cdd:PLN02850 75 lGEELAGSEVLIRGRVHTIRGKG-KSAFLVLRQSGFTVQCVVFVSEVTVSKGMVKYAKQLSRESVVDVEGVVSVPKKPvk 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 198 ----ELSLIPNEILQLTPCLHMLPhshFGLKD----------------------KELRFRKRYLDLilnpRVKDN---FV 248
Cdd:PLN02850 154 gttqQVEIQVRKIYCVSKALATLP---FNVEDaarseseiekalqtgeqlvrvgQDTRLNNRVLDL----RTPANqaiFR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 249 IRSKIITFLRRYLDNLGFLEVETPIMnqIAGGAT--AKPFithhnDLDMN---LFLRVAPELYHKMLVVGGIDRVYEVGR 323
Cdd:PLN02850 227 IQSQVCNLFREFLLSKGFVEIHTPKL--IAGASEggSAVF-----RLDYKgqpACLAQSPQLHKQMAICGDFRRVFEIGP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 324 LFRNEGiDLTHNP--EFTTCEFYMAYAD-YEDVIQLTEDLLSSMVMSIKGTYKIEY------HPNGPntepvyeVDFTPP 394
Cdd:PLN02850 300 VFRAED-SFTHRHlcEFTGLDLEMEIKEhYSEVLDVVDELFVAIFDGLNERCKKELeaireqYPFEP-------LKYLPK 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 395 FKRVHMYDGLAE-KLGATLPDP-STLHTEearevfdklcrdnnvdcsaprtTARLLDKLVGEYLESTFIsptFLIGHPQI 472
Cdd:PLN02850 372 TLRLTFAEGIQMlKEAGVEVDPlGDLNTE----------------------SERKLGQLVKEKYGTDFY---ILHRYPLA 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 473 MSP---LAKWHRsiPGLTERFELFAVTREIANAYTELNDP--ITQRQRfeqqAKDKDAGDdeaqmiDETFCNALEYGLPP 547
Cdd:PLN02850 427 VRPfytMPCPDD--PKYSNSFDVFIRGEEIISGAQRVHDPelLEKRAE----ECGIDVKT------ISTYIDSFRYGAPP 494
|
570 580
....*....|....*....|....*...
gi 17535925 548 TGGWGMGIDRLSMILTDNNNIKEVLLFP 575
Cdd:PLN02850 495 HGGFGVGLERVVMLFCGLNNIRKTSLFP 522
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
238-575 |
3.45e-14 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 73.90 E-value: 3.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 238 ILNPRVKDNFVIRSKIITFLRRYLDNLGFLEVETPIMNQI----AGGATAKPFithhNDLDMNLF---LRVAPEL-YHKM 309
Cdd:PRK06462 21 ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIISPStdplMGLGSDLPV----KQISIDFYgveYYLADSMiLHKQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 310 LVVGGIDRVYEVGRLFRNEGID---LTHNPEFTTCEFYMAYADYEDVIQLTEDLLSSMVMSIKGTYKIEYHPNGPNTEpv 386
Cdd:PRK06462 97 LALRMLGKIFYLSPNFRLEPVDkdtGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHEDELEFFGRDLP-- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 387 yevDFTPPFKRVHMydglaeklgatlpdpstlhtEEAREVFDKLCRDNNVDcsaprttARLLDKlvGE-YLESTFISPTF 465
Cdd:PRK06462 175 ---HLKRPFKRITH--------------------KEAVEILNEEGCRGIDL-------EELGSE--GEkSLSEHFEEPFW 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 466 LIGHPQIMSPLakWHRSIPGLTERfeLFAVTREIANAYTELndpITQRQR---FEQ-QAKDKDAGDDEAQMidETFCNAL 541
Cdd:PRK06462 223 IIDIPKGSREF--YDREDPERPGV--LRNYDLLLPEGYGEA---VSGGEReyeYEEiVERIREHGVDPEKY--KWYLEMA 293
|
330 340 350
....*....|....*....|....*....|....
gi 17535925 542 EYGLPPTGGWGMGIDRLSMILTDNNNIKEVLLFP 575
Cdd:PRK06462 294 KEGPLPSAGFGIGVERLTRYICGLRHIREVQPFP 327
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
129-206 |
4.65e-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: 67.26 E-value: 4.65e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17535925 129 VSVAGRIHSKRESGSKLVFYDIHGEGTHIQIMANAKfhtgdvDFVTLHDRIKRGDIVGFTGRATRTKAGELSLIPNEI 206
Cdd:pfam01336 1 VTVAGRVTSIRRSGGKLLFLTLRDGTGSIQVVVFKE------EAEKLAKKLKEGDVVRVTGKVKKRKGGELELVVEEI 72
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
129-206 |
1.31e-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: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535925 129 VSVAGRIHSKRESGsKLVFYDIHGEGTHIQIMANAKfhtGDVDFVTLHDRIKRGDIVGFTGRATRTKA-----GELSLIP 203
Cdd:cd04100 2 VTLAGWVHSRRDHG-GLIFIDLRDGSGIVQVVVNKE---ELGEFFEEAEKLRTESVVGVTGTVVKRPEgnlatGEIELQA 77
|
...
gi 17535925 204 NEI 206
Cdd:cd04100 78 EEL 80
|
|
| PheRS_alpha_core |
cd00496 |
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ... |
316-390 |
1.56e-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: 1.56e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17535925 316 DRVYEVGRLFRNEGIDLTHNPEFTTCEFYMAYAD--YEDVIQLTEDLLSSMVMSIKgtyKIEYHPN-GPNTEPVYEVD 390
Cdd:cd00496 81 IRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKGltFADLKGTLEEFAKELFGPIT---KVRFRPSyFPFTEPSFEVD 155
|
|
| |
