|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
15-569 |
0e+00 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 795.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 15 DEPTGEKVSKTELKKRLKSRAKEAEK------QKKAATAPTKIQKETSSEQDEANLSAHQYFEIRSNRINKLREtKNSYP 88
Cdd:PLN02502 1 AESNGEPLSKNALKKRLKAKQAEEEKaakeeaKAAAAAAAAKGRSRKSAAADDETMDPTQYRANRLKKVEALRA-KGVEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 89 YPHKFEVTNDLRDFLTVYKNLAKGEERTDVPIRIAGRIYTKRVSGnKLVFYDIRAEGVKVQVMCQAQNST---TGFEEQH 165
Cdd:PLN02502 80 YPYKFDVTHTAPELQEKYGSLENGEELEDVSVSVAGRIMAKRAFG-KLAFYDLRDDGGKIQLYADKKRLDldeEEFEKLH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 166 EVLRRGDIVGIVGFPGRTspktrDNGELSIFATQVVLLSPCLHALPSEHYGFQDKEQRFRQRYLDLIINDRPRQIFRTRA 245
Cdd:PLN02502 159 SLVDRGDIVGVTGTPGKT-----KKGELSIFPTSFEVLTKCLLMLPDKYHGLTDQETRYRQRYLDLIANPEVRDIFRTRA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 246 KIVSYLRSYLDSRDFTEVETPMMNAIAGGATASPFVTHHNDLKRDLFMRVAPELYLKMLVVGGLERVYEIGKQFRNEGID 325
Cdd:PLN02502 234 KIISYIRRFLDDRGFLEVETPMLNMIAGGAAARPFVTHHNDLNMDLYLRIATELHLKRLVVGGFERVYEIGRQFRNEGIS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 326 LTHSPEFTTCEFYQAYADYNDLMAMTEDLISSMVKHITGGYETTFesqtgQVYTINWQSPWKRIDMIPALEEACGDKFPP 405
Cdd:PLN02502 314 TRHNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKELTGSYKIKY-----HGIEIDFTPPFRRISMISLVEEATGIDFPA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 406 GdqLHTPEAGTFLKEMLKKMKVECTPPLTNARMLDKLVGEFVEDKCINPTFVTGHPQMMSPLAKAHRDTPGICERFEVFV 485
Cdd:PLN02502 389 D--LKSDEANAYLIAACEKFDVKCPPPQTTGRLLNELFEEFLEETLVQPTFVLDHPVEMSPLAKPHRSKPGLTERFELFI 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 486 TTKELLNAYTELNDPFDQRMRFEEQANQKAQGDDEAQMVDENFCQALEYGLPPTGGWGMGIDRLTMFLTNNYSIKEVLAF 565
Cdd:PLN02502 467 NGRELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRLVMLLTDSASIRDVIAF 546
|
....
gi 1064303005 566 PMMK 569
Cdd:PLN02502 547 PAMK 550
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
71-572 |
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: 682.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 71 EIRSNRINKLRETKNS--YPYPHKFEVTNDLRDFLTVYKNLAKGEErTDVPIRIAGRIYTKRVSGnKLVFYDIRAEGVKV 148
Cdd:COG1190 9 EQIRVRREKLEELREAgiDPYPNKFPRTHTAAEIREKYDELEAEEE-TGDEVSVAGRIMAKRDMG-KASFADLQDGSGRI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 149 QVMCQAqnSTTGfEEQHEVLR---RGDIVGIVGFPGRTspKTrdnGELSIFATQVVLLSPCLHALPSEHYGFQDKEQRFR 225
Cdd:COG1190 87 QLYLRR--DELG-EEAYELFKlldLGDIVGVEGTVFRT--KT---GELSVKVEELTLLSKSLRPLPEKFHGLTDPETRYR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 226 QRYLDLIINDRPRQIFRTRAKIVSYLRSYLDSRDFTEVETPMMNAIAGGATASPFVTHHNDLKRDLFMRVAPELYLKMLV 305
Cdd:COG1190 159 QRYVDLIVNPEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 306 VGGLERVYEIGKQFRNEGIDLTHSPEFTTCEFYQAYADYNDLMAMTEDLISSMVKHITGGYETTFesqtgQVYTINWQSP 385
Cdd:COG1190 239 VGGFERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGTTKVTY-----QGQEIDLSPP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 386 WKRIDMIPALEEACGDKFppgDQLHTPEAgtfLKEMLKKMKVECTPPLTNARMLDKLVGEFVEDKCINPTFVTGHPQMMS 465
Cdd:COG1190 314 WRRITMVEAIKEATGIDV---TPLTDDEE---LRALAKELGIEVDPGWGRGKLIDELFEELVEPKLIQPTFVTDYPVEVS 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 466 PLAKAHRDTPGICERFEVFVTTKELLNAYTELNDPFDQRMRFEEQANQKAQGDDEAQMVDENFCQALEYGLPPTGGWGMG 545
Cdd:COG1190 388 PLAKRHRDDPGLTERFELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGLGIG 467
|
490 500
....*....|....*....|....*..
gi 1064303005 546 IDRLTMFLTNNYSIKEVLAFPMMKDDK 572
Cdd:COG1190 468 IDRLVMLLTDSPSIRDVILFPLMRPEK 494
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
67-572 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 667.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 67 HQYFEIRSNRINKLRETKNSyPYPHKFEVTNDLRDFLTVYKNLAKGE-ERTDVPIRIAGRIYTKRVSGnKLVFYDIRAEG 145
Cdd:PRK00484 4 NEQIAVRREKLAELREQGID-PYPNKFERTHTAAELRAKYDDKEKEElEELEIEVSVAGRVMLKRVMG-KASFATLQDGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 146 VKVQVMCQAQNSTTGFEEQHEVLRRGDIVGIVGFPGRTspKTrdnGELSIFATQVVLLSPCLHALPSEHYGFQDKEQRFR 225
Cdd:PRK00484 82 GRIQLYVSKDDVGEEALEAFKKLDLGDIIGVEGTLFKT--KT---GELSVKATELTLLTKSLRPLPDKFHGLTDVETRYR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 226 QRYLDLIINDRPRQIFRTRAKIVSYLRSYLDSRDFTEVETPMMNAIAGGATASPFVTHHNDLKRDLFMRVAPELYLKMLV 305
Cdd:PRK00484 157 QRYVDLIVNPESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARPFITHHNALDIDLYLRIAPELYLKRLI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 306 VGGLERVYEIGKQFRNEGIDLTHSPEFTTCEFYQAYADYNDLMAMTEDLISSMVKHITGGYETTFesqtgQVYTINWQSP 385
Cdd:PRK00484 237 VGGFERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTY-----QGTEIDFGPP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 386 WKRIDMIPALEEACGDKFppgDQLHTPEAgtflKEMLKKMKVECTPPLTNARMLDKLVGEFVEDKCINPTFVTGHPQMMS 465
Cdd:PRK00484 312 FKRLTMVDAIKEYTGVDF---DDMTDEEA----RALAKELGIEVEKSWGLGKLINELFEEFVEPKLIQPTFITDYPVEIS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 466 PLAKAHRDTPGICERFEVFVTTKELLNAYTELNDPFDQRMRFEEQANQKAQGDDEAQMVDENFCQALEYGLPPTGGWGMG 545
Cdd:PRK00484 385 PLAKRHREDPGLTERFELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIG 464
|
490 500
....*....|....*....|....*..
gi 1064303005 546 IDRLTMFLTNNYSIKEVLAFPMMKDDK 572
Cdd:PRK00484 465 IDRLVMLLTDSPSIRDVILFPLMRPEK 491
|
|
| lysS_bact |
TIGR00499 |
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ... |
65-572 |
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: 622.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 65 SAHQYFEIRSNRINKLRETKNSyPYPHKFEVTNDLRDFLTVYKNLAKGE-ERTDVPIRIAGRIYTKRvSGNKLVFYDIRA 143
Cdd:TIGR00499 1 ELNDQAQQRLEKLNRLRQTGNN-PYLHKFERTHSAQEFQEKYADLSNEElKEKELKVSIAGRIKAIR-SMGKATFITLQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 144 EGVKVQVMCQAQNSTTGFEE-QHEVLRRGDIVGIVGFPGRTspKTrdnGELSIFATQVVLLSPCLHALPSEHYGFQDKEQ 222
Cdd:TIGR00499 79 ESGQIQLYVNKNKLPEDFYEfDEYLLDLGDIIGVTGYPFKT--KT---GELSVKVTELQILTKCLQPLPDKWHGLTDQET 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 223 RFRQRYLDLIINDRPRQIFRTRAKIVSYLRSYLDSRDFTEVETPMMNAIAGGATASPFVTHHNDLKRDLFMRVAPELYLK 302
Cdd:TIGR00499 154 RYRQRYLDLIVNPDVRQTFLKRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKPFITHHNALDMDLYLRIAPELYLK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 303 MLVVGGLERVYEIGKQFRNEGIDLTHSPEFTTCEFYQAYADYNDLMAMTEDLISSMVKHITGGYETTFESQtgqvyTINW 382
Cdd:TIGR00499 234 RLIVGGLEKVYEIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTFIINYNDL-----EIDL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 383 QSPWKRIDMIPALEEACGDKFppgDQLHTPEAGTFLKEMLKKMKVECtpPLTNARMLDKLVGEFVEDKCINPTFVTGHPQ 462
Cdd:TIGR00499 309 KPPWKRITMVDALEMVTGIDF---DILKDDETAKALAKEHGIEVAED--SLTLGHILNKFFEQFLEHTLIQPTFITHYPA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 463 MMSPLAKAHRDTPGICERFEVFVTTKELLNAYTELNDPFDQRMRFEEQANQKAQGDDEAQMVDENFCQALEYGLPPTGGW 542
Cdd:TIGR00499 384 EISPLAKRDPSNPEFTERFELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGL 463
|
490 500 510
....*....|....*....|....*....|
gi 1064303005 543 GMGIDRLTMFLTNNYSIKEVLAFPMMKDDK 572
Cdd:TIGR00499 464 GIGIDRLVMLLTDAPSIRDVLLFPQLRPQK 493
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
234-570 |
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: 574.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 234 NDRPRQIFRTRAKIVSYLRSYLDSRDFTEVETPMMNAIAGGATASPFVTHHNDLKRDLFMRVAPELYLKMLVVGGLERVY 313
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 314 EIGKQFRNEGIDLTHSPEFTTCEFYQAYADYNDLMAMTEDLISSMVKHITGGYETTFesqtgQVYTINWQSPWKRIDMIP 393
Cdd:cd00775 81 EIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIEY-----GGKELDFTPPFKRVTMVD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 394 ALEEACGDKFPPGDQLHTPEAgtfLKEMLKKMKVECTPPLTNARMLDKLVGEFVEDKCINPTFVTGHPQMMSPLAKAHRD 473
Cdd:cd00775 156 ALKEKTGIDFPELDLEQPEEL---AKLLAKLIKEKIEKPRTLGKLLDKLFEEFVEPTLIQPTFIIDHPVEISPLAKRHRS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 474 TPGICERFEVFVTTKELLNAYTELNDPFDQRMRFEEQANQKAQGDDEAQMVDENFCQALEYGLPPTGGWGMGIDRLTMFL 553
Cdd:cd00775 233 NPGLTERFELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLL 312
|
330
....*....|....*..
gi 1064303005 554 TNNYSIKEVLAFPMMKD 570
Cdd:cd00775 313 TDSNSIRDVILFPAMRP 329
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
4-569 |
0e+00 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 561.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 4 PGAVKETVLLLDEPTGEKVSKTELKKRlKSRAKEAEKqKKAATAPTKIQKEtsseQDEANLSAHQYFEIRSNRINKlRET 83
Cdd:PTZ00417 26 SKIILNKNKNIICPVHCKQCFVTMSEK-KEHVMEGEK-KVRSVQASKDKKK----EEEAEVDPRLYYENRSKFIQE-QKA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 84 KNSYPYPHKFEVTNDLRDFLTVYKNLAKGEERTDVPIRIAGRIYTKRVSGNKLVFYDIRAEGVKVQVMCQ---AQNSTTG 160
Cdd:PTZ00417 99 KGINPYPHKFERTITVPEFVEKYQDLASGEHLEDTILNVTGRIMRVSASGQKLRFFDLVGDGAKIQVLANfafHDHTKSN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 161 FEEQHEVLRRGDIVGIVGFPGRTSpktrdNGELSIFATQVVLLSPCLHALPSEhYGFQDKEQRFRQRYLDLIINDRPRQI 240
Cdd:PTZ00417 179 FAECYDKIRRGDIVGIVGFPGKSK-----KGELSIFPKETIILSPCLHMLPMK-YGLKDTEIRYRQRYLDLMINESTRST 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 241 FRTRAKIVSYLRSYLDSRDFTEVETPMMNAIAGGATASPFVTHHNDLKRDLFMRVAPELYLKMLVVGGLERVYEIGKQFR 320
Cdd:PTZ00417 253 FITRTKIINYLRNFLNDRGFIEVETPTMNLVAGGANARPFITHHNDLDLDLYLRIATELPLKMLIVGGIDKVYEIGKVFR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 321 NEGIDLTHSPEFTTCEFYQAYADYNDLMAMTEDLISSMVKHITGGYETTF--ESQTGQVYTINWQSPWKRIDMIPALEEA 398
Cdd:PTZ00417 333 NEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHLFGTYKILYnkDGPEKDPIEIDFTPPYPKVSIVEELEKL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 399 CGDKFP-PGDqlhTPEAGTFLKEMLKKMKVECTPPLTNARMLDKLVGEFVEDKCIN-PTFVTGHPQMMSPLAKAHRDTPG 476
Cdd:PTZ00417 413 TNTKLEqPFD---SPETINKMINLIKENKIEMPNPPTAAKLLDQLASHFIENKYPNkPFFIIEHPQIMSPLAKYHRSKPG 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 477 ICERFEVFVTTKELLNAYTELNDPFDQRMRFEEQANQKAQGDDEAQMVDENFCQALEYGLPPTGGWGMGIDRLTMFLTNN 556
Cdd:PTZ00417 490 LTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCTSLEYGLPPTGGLGLGIDRITMFLTNK 569
|
570
....*....|...
gi 1064303005 557 YSIKEVLAFPMMK 569
Cdd:PTZ00417 570 NCIKDVILFPTMR 582
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
44-571 |
6.17e-146 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 436.77 E-value: 6.17e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 44 AATAPTKIQKETSSEQDEANLSAHQYfeiRSNRINKLRETKNSYPyphKFEVTNDLRDFLTVYKNLAKGEERTDVPIRIA 123
Cdd:PTZ00385 40 LSSSRSPLELKKPISKASATKTVTQE---ASRAPRSKLDLPAAYS---SFRGITPISEVRERYGYLASGDRAAQATVRVA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 124 GRIYTKRVSGnKLVFYDIRAEGVKVQVMCQ-AQNSTTGFEEQHEV-LRRGDIVGIVGFPGRTSpktrdNGELSIFATQVV 201
Cdd:PTZ00385 114 GRVTSVRDIG-KIIFVTIRSNGNELQVVGQvGEHFTREDLKKLKVsLRVGDIIGADGVPCRMQ-----RGELSVAASRML 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 202 LLSPCL---HALPSEHYGF---QDKEQRFRQRYLDLIINDRPRQIFRTRAKIVSYLRSYLDSRDFTEVETPMMNAIAGGA 275
Cdd:PTZ00385 188 ILSPYVctdQVVCPNLRGFtvlQDNDVKYRYRFTDMMTNPCVIETIKKRHVMLQALRDYFNERNFVEVETPVLHTVASGA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 276 TASPFVTHHNDLKRDLFMRVAPELYLKMLVVGGLERVYEIGKQFRNEGIDLTHSPEFTTCEFYQAYADYNDLMAMTEDLI 355
Cdd:PTZ00385 268 NAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTSCEFYAAYHTYEDLMPMTEDIF 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 356 SSMVKHITGGYETTF--ESQTGQVYTINWQSPWKRIDMIPALEEACGDKFPPGDQLHTPEAGTFLKEMLKKMKVECTPPL 433
Cdd:PTZ00385 348 RQLAMRVNGTTVVQIypENAHGNPVTVDLGKPFRRVSVYDEIQRMSGVEFPPPNELNTPKGIAYMSVVMLRYNIPLPPVR 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 434 TNARMLDKLVGEFVEDKCINPTFVTGHPQMMSPLAKAHRDTPGICERFEVFVTTKELLNAYTELNDPFDQRMRFEEQANQ 513
Cdd:PTZ00385 428 TAAKMFEKLIDFFITDRVVEPTFVMDHPLFMSPLAKEQVSRPGLAERFELFVNGIEYCNAYSELNDPHEQYHRFQQQLVD 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1064303005 514 KAQGDDEAQMVDENFCQALEYGLPPTGGWGMGIDRLTMFLTNNYSIKEVLAFPMMKDD 571
Cdd:PTZ00385 508 RQGGDEEAMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFPLLRQD 565
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
76-569 |
8.58e-140 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 433.24 E-value: 8.58e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 76 RINKLRETKNS--YPYPHKFEVTNDLRDFLtvyknlakgEERTDVPIRIAGRIYTKRVSGnKLVFYDIRAEGVKVQVMcq 153
Cdd:PRK02983 617 RLAKLEALRAAgvDPYPVGVPPTHTVAEAL---------DAPTGEEVSVSGRVLRIRDYG-GVLFADLRDWSGELQVL-- 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 154 AQNSTTGFEEQHEVLR---RGDIVGIVGFPGRTspktrDNGELSIFATQVVLLSPCLHALPSEHYGFQDKEQRFRQRYLD 230
Cdd:PRK02983 685 LDASRLEQGSLADFRAavdLGDLVEVTGTMGTS-----RNGTLSLLVTSWRLAGKCLRPLPDKWKGLTDPEARVRQRYLD 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 231 LIINDRPRQIFRTRAKIVSYLRSYLDSRDFTEVETPMMNAIAGGATASPFVTHHNDLKRDLFMRVAPELYLKMLVVGGLE 310
Cdd:PRK02983 760 LAVNPEARDLLRARSAVVRAVRETLVARGFLEVETPILQQVHGGANARPFVTHINAYDMDLYLRIAPELYLKRLCVGGVE 839
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 311 RVYEIGKQFRNEGIDLTHSPEFTTCEFYQAYADYNDLMAMTEDLISSMVKHITGGYETTFESQTGQVYTINWQSPWKRID 390
Cdd:PRK02983 840 RVFELGRNFRNEGVDATHNPEFTLLEAYQAHADYDTMRDLTRELIQNAAQAAHGAPVVMRPDGDGVLEPVDISGPWPVVT 919
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 391 MIPALEEACGDKFPPGDQLHTpeagtfLKEMLKKMKVECTPPLTNARMLDKLVGEFVEDKCINPTFVTGHPQMMSPLAKA 470
Cdd:PRK02983 920 VHDAVSEALGEEIDPDTPLAE------LRKLCDAAGIPYRTDWDAGAVVLELYEHLVEDRTTFPTFYTDFPTSVSPLTRP 993
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 471 HRDTPGICERFEVFVTTKELLNAYTELNDPFDQRMRFEEQANQKAQGDDEAQMVDENFCQALEYGLPPTGGWGMGIDRLT 550
Cdd:PRK02983 994 HRSDPGLAERWDLVAWGVELGTAYSELTDPVEQRRRLTEQSLLAAGGDPEAMELDEDFLQALEYAMPPTGGLGMGVDRLV 1073
|
490
....*....|....*....
gi 1064303005 551 MFLTNNySIKEVLAFPMMK 569
Cdd:PRK02983 1074 MLLTGR-SIRETLPFPLVK 1091
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
73-572 |
8.04e-119 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 361.69 E-value: 8.04e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 73 RSNRINKLRETKNSYPYPHKFEVTND-LRDFLTVYKNlaKGEERTDVPIRIAGRIYTKRVSGnKLVFYDIRAEGVKVQVM 151
Cdd:PRK12445 22 RREKLAALRQQGVAFPNDFRRDHTSDqLHEEFDAKDN--QELESLNIEVSVAGRMMTRRIMG-KASFVTLQDVGGRIQLY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 152 CQAQNSTTG-FEEQHEVLRRGDIVGIVGFPGRTSpktrdNGELSIFATQVVLLSPCLHALPSEHYGFQDKEQRFRQRYLD 230
Cdd:PRK12445 99 VARDSLPEGvYNDQFKKWDLGDIIGARGTLFKTQ-----TGELSIHCTELRLLTKALRPLPDKFHGLQDQEVRYRQRYLD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 231 LIINDRPRQIFRTRAKIVSYLRSYLDSRDFTEVETPMMNAIAGGATASPFVTHHNDLKRDLFMRVAPELYLKMLVVGGLE 310
Cdd:PRK12445 174 LIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGFE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 311 RVYEIGKQFRNEGIDLTHSPEFTTCEFYQAYADYNDLMAMTEDLISSMVKHITGGYETTFESQtgqvyTINWQSPWKRID 390
Cdd:PRK12445 254 RVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEH-----VFDFGKPFEKLT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 391 MIPALEeacgdKFPPGDQLHTPEAGTFLKEMLKKMKVECTPPLTNARMLDKLVGEFVEDKCINPTFVTGHPQMMSPLAKA 470
Cdd:PRK12445 329 MREAIK-----KYRPETDMADLDNFDAAKALAESIGITVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARR 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 471 HRDTPGICERFEVFVTTKELLNAYTELNDPFDQRMRFEEQANQKAQGDDEAQMVDENFCQALEYGLPPTGGWGMGIDRLT 550
Cdd:PRK12445 404 NDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMI 483
|
490 500
....*....|....*....|..
gi 1064303005 551 MFLTNNYSIKEVLAFPMMKDDK 572
Cdd:PRK12445 484 MLFTNSHTIRDVILFPAMRPQK 505
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
219-569 |
1.00e-110 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 334.15 E-value: 1.00e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 219 DKEQRFRQRYLDLIiNDRPRQIFRTRAKIVSYLRSYLDSRDFTEVETPMMNAIAGGATASPFVTHHNDLKRDLFMRVAPE 298
Cdd:pfam00152 1 DEETRLKYRYLDLR-RPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 299 LYLKMLVVGGLERVYEIGKQFRNEGIDLTHSPEFTTCEFYQAYADYNDLMAMTEDLISSMVKHITGGYETTFESQTGQVy 378
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDL- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 379 tinwQSPWKRIDMIPALEEACG-DKFPPGDQLHTPEagtflkemlkkmkvectppltnarmlDKLVGEFVEDKCI-NPTF 456
Cdd:pfam00152 159 ----KKPFPRITYAEAIEKLNGkDVEELGYGSDKPD--------------------------LRFLLELVIDKNKfNPLW 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 457 VTGHPQMMSPLAKAHR-DTPGICERFEVFVTTKELLNAYTELNDPFDQRMRFEEQANQKaqgdDEAQMVDENFCQALEYG 535
Cdd:pfam00152 209 VTDFPAEHHPFTMPKDeDDPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDP----EEAEEKFGFYLDALKYG 284
|
330 340 350
....*....|....*....|....*....|....
gi 1064303005 536 LPPTGGWGMGIDRLTMFLTNNYSIKEVLAFPMMK 569
Cdd:pfam00152 285 APPHGGLGIGLDRLVMLLTGLESIREVIAFPKTR 318
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
241-569 |
6.44e-86 |
|
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: 268.58 E-value: 6.44e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 241 FRTRAKIVSYLRSYLDSRDFTEVETPMMNAIAGGATASPFVTHHNDLKRDLFMRVAPELYLKMLVVGGLERVYEIGKQFR 320
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 321 NEGIDLTHSPEFTTCEFYQAYADYNDLMAMTEDLISSMVKHITGGYETTFESqtgqvYTINWQSPWKRIDMIPALEeacg 400
Cdd:cd00669 81 NEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYGF-----ELEDFGLPFPRLTYREALE---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 401 dkfppgdqlhtpeagtflkemlkkmkvectppltnarmldklvgefvedKCINPTFVTGHP-QMMSPLAKAHRDTPGICE 479
Cdd:cd00669 152 -------------------------------------------------RYGQPLFLTDYPaEMHSPLASPHDVNPEIAD 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 480 RFEVFVTTKELLNAYTELNDPFDQRMRFEEQANQKaqgddEAQMV-DENFCQALEYGLPPTGGWGMGIDRLTMFLTNNYS 558
Cdd:cd00669 183 AFDLFINGVEVGNGSSRLHDPDIQAEVFQEQGINK-----EAGMEyFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPT 257
|
330
....*....|.
gi 1064303005 559 IKEVLAFPMMK 569
Cdd:cd00669 258 IREVIAFPKMR 268
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
258-564 |
4.40e-56 |
|
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: 190.84 E-value: 4.40e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 258 RDFTEVETPMMnaIAGGATAS---PFVTH---HNDLKRDLFMRVAPELYLKMLVVGGLERVYEIGKQFRNEGIDLTHSPE 331
Cdd:TIGR00462 5 RGVLEVETPLL--SPAPVTDPhldAFATEfvgPDGQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRHNPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 332 FTTCEFYQAYADYNDLMAMTEDLISSMVKHITGgyettfesqtgqvytinwqsPWKRIDMIPALEEACGDkfppgDQLHT 411
Cdd:TIGR00462 83 FTMLEWYRPGFDYHDLMDEVEALLQELLGDPFA--------------------PAERLSYQEAFLRYAGI-----DPLTA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 412 PEAGtfLKEMLKKMKVECTPPLTNARMLDKLVGEFVEDK--CINPTFVTGHPQMMSPLAKAHRDTPGICERFEVFVTTKE 489
Cdd:TIGR00462 138 SLAE--LQAAAAAHGIRASEEDDRDDLLDLLFSEKVEPHlgFGRPTFLYDYPASQAALARISPDDPRVAERFELYIKGLE 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1064303005 490 LLNAYTELNDPFDQRMRFEEQANQKAQGDDEAQMVDENFCQALEYGLPPTGGWGMGIDRLTMFLTNNYSIKEVLA 564
Cdd:TIGR00462 216 LANGFHELTDAAEQRRRFEADNALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDVLA 290
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
237-564 |
9.87e-55 |
|
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: 188.01 E-value: 9.87e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 237 PRQIFRTRAKIVSYLRSYLDSRDFTEVETPMMnAIAGGATA--SPFVT---HHNDLKRDLFMRVAPELYLKMLVVGGLER 311
Cdd:COG2269 2 SREALRARARLLAAIRAFFAERGVLEVETPAL-SVAPGTDPhlDSFATefiGPDGGGRPLYLHTSPEFAMKRLLAAGSGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 312 VYEIGKQFRNEGIDLTHSPEFTTCEFYQAYADYNDLMAMTEDLISsmvkhitggyettfesqtgQVYTINWQSPWKRIDM 391
Cdd:COG2269 81 IYQIAKVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQ-------------------LVLGAAGFAPAERLSY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 392 IPALEEACGdkFPPgdqLHTPEAGtfLKEMLKKMKVECTPPLTNARMLDKLVGEFVE-----DKcinPTFVTGHPQMMSP 466
Cdd:COG2269 142 QEAFLRYLG--IDP---LTADLDE--LAAAAAAAGLRVADDDDRDDLLDLLLSERVEpqlgrDR---PTFLYDYPASQAA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 467 LAKAHRDTPGICERFEVFVTTKELLNAYTELNDPFDQRMRFEEQANQKAQGDDEAQMVDENFCQALEYGLPPTGGWGMGI 546
Cdd:COG2269 212 LARISPDDPRVAERFELYACGVELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGF 291
|
330
....*....|....*...
gi 1064303005 547 DRLTMFLTNNYSIKEVLA 564
Cdd:COG2269 292 DRLLMLALGAERIDDVLA 309
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
120-231 |
1.75e-44 |
|
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: 153.40 E-value: 1.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 120 IRIAGRIYTKRVSGnKLVFYDIRAEGVKVQVMCQAQNSTTG-FEEQHEVLRRGDIVGIVGFPGRTspKTrdnGELSIFAT 198
Cdd:cd04322 2 VSVAGRIMSKRGSG-KLSFADLQDESGKIQVYVNKDDLGEEeFEDFKKLLDLGDIIGVTGTPFKT--KT---GELSIFVK 75
|
90 100 110
....*....|....*....|....*....|...
gi 1064303005 199 QVVLLSPCLHALPSEHYGFQDKEQRFRQRYLDL 231
Cdd:cd04322 76 EFTLLSKSLRPLPEKFHGLTDVETRYRQRYLDL 108
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
237-562 |
2.79e-41 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 151.62 E-value: 2.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 237 PRQIFRTRAKIVSYLRSYLDSRDFTEVETPMM-NAIAGGATASPFVTH----HNDLKRDLFMRVAPELYLKMLVVGGLER 311
Cdd:PRK09350 1 SIPNLLKRAKIIAEIRRFFADRGVLEVETPILsQATVTDIHLVPFETRfvgpGASQGKTLWLMTSPEYHMKRLLAAGSGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 312 VYEIGKQFRNEGIDLTHSPEFTTCEFYQAYADYNDLMAMTEDL-----ISSMVKHITggYETTFESQTGqvytinwqspw 386
Cdd:PRK09350 81 IFQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLlqqvlDCEPAESLS--YQQAFLRYLG----------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 387 krIDMIPALEE---ACGDKFPPGDQLHTPEAGTFLKEMLKKMKVEctPPLTNARmldklvgefvedkcinPTFVTGHPQM 463
Cdd:PRK09350 148 --IDPLSADKTqlrEVAAKLGLSNIADEEEDRDTLLQLLFTFGVE--PNIGKEK----------------PTFVYHFPAS 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 464 MSPLAKAHRDTPGICERFEVFVTTKELLNAYTELNDPFDQRMRFEEQANQKAQGDDEAQMVDENFCQALEYGLPPTGGWG 543
Cdd:PRK09350 208 QAALAKISTEDHRVAERFEVYFKGIELANGFHELTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCSGVA 287
|
330
....*....|....*....
gi 1064303005 544 MGIDRLTMFLTNNYSIKEV 562
Cdd:PRK09350 288 LGVDRLIMLALGAESISEV 306
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
120-566 |
7.85e-39 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 148.03 E-value: 7.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 120 IRIAGRIYTKRVSGnKLVFYDIR-AEGVkVQVMCQAQNSTTGFEeQHEVLRRGDIVGIVGFPgRTSPKTRdNGeLSIFAT 198
Cdd:PRK05159 19 VTLAGWVHEIRDLG-GIAFLILRdRSGI-IQVVVKKKVDEELFE-TIKKLKRESVVSVTGTV-KANPKAP-GG-VEVIPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 199 QVVLLSPCLHALPSEHYGFQDKE--QRFRQRYLDLIiNDRPRQIFRTRAKIVSYLRSYLDSRDFTEVETPMMNAIA--GG 274
Cdd:PRK05159 93 EIEVLNKAEEPLPLDISGKVLAEldTRLDNRFLDLR-RPRVRAIFKIRSEVLRAFREFLYENGFTEIFTPKIVASGteGG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 275 ATASPfVTHHNdlkRDLFMRVAPELYLKMLVVGGLERVYEIGKQFRNEGIDLT-HSPEFTTCEFYQAYAD-YNDLMAMTE 352
Cdd:PRK05159 172 AELFP-IDYFE---KEAYLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSrHLNEYTSIDVEMGFIDdHEDVMDLLE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 353 DLISSMVKHITGGYETTFEsqtgqVYTINWQSPWKRIDMIP---ALE--EACGDKFPPGDQLHTPEagtflkemlkkmkv 427
Cdd:PRK05159 248 NLLRYMYEDVAENCEKELE-----LLGIELPVPETPIPRITydeAIEilKSKGNEISWGDDLDTEG-------------- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 428 ectppltnarmlDKLVGEFV-EDKCINPTFVTGHPQMMSPL-AKAHRDTPGICERFEVFVTTKELLNAytelndpfDQRM 505
Cdd:PRK05159 309 ------------ERLLGEYVkEEYGSDFYFITDYPSEKRPFyTMPDEDDPEISKSFDLLFRGLEITSG--------GQRI 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1064303005 506 -RFEEQANQ-KAQGDDEAQMvdENFCQALEYGLPPTGGWGMGIDRLTMFLTNNYSIKEVLAFP 566
Cdd:PRK05159 369 hRYDMLVESiKEKGLNPESF--EFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFP 429
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
221-566 |
1.79e-33 |
|
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: 130.38 E-value: 1.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 221 EQRFRQRYLDLIiNDRPRQIFRTRAKIVSYLRSYLDSRDFTEVETPMM--NAIAGGATASPFvthhNDLKRDLFMRVAPE 298
Cdd:cd00776 5 ETLLDNRHLDLR-TPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKItsTDTEGGAELFKV----SYFGKPAYLAQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 299 LYLKMLVvGGLERVYEIGKQFRNEGIDLT-HSPEFTTCEFYQAYA-DYNDLMAMTEDLISSMVKHITGGYETtfESQTGQ 376
Cdd:cd00776 80 LYKEMLI-AALERVYEIGPVFRAEKSNTRrHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAK--ELELVN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 377 VYTINW---QSPWKRIDMIPALE--EACGDKFPP--GDQLHTPEagtflkemlkkmkvectppltnarmlDKLVGEFVED 449
Cdd:cd00776 157 QLNRELlkpLEPFPRITYDEAIEllREKGVEEEVkwGEDLSTEH--------------------------ERLLGEIVKG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 450 KcinPTFVTGHPQMMSPL-AKAHRDTPGICERFEVFVT-TKELLNAytelndpfDQRM-RFEE-QANQKAQGDDEAQMvd 525
Cdd:cd00776 211 D---PVFVTDYPKEIKPFyMKPDDDNPETVESFDLLMPgVGEIVGG--------SQRIhDYDElEERIKEHGLDPESF-- 277
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1064303005 526 ENFCQALEYGLPPTGGWGMGIDRLTMFLTNNYSIKEVLAFP 566
Cdd:cd00776 278 EWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
120-566 |
5.39e-32 |
|
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: 128.25 E-value: 5.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 120 IRIAGRIYTKRVSGnKLVFYDIR-AEGVkVQVMCQAqNSTTGFEEQHEvLRRGDIV---GIVgfpgRTSPKTrdNGELSI 195
Cdd:COG0017 17 VTVAGWVRTKRDSG-GISFLILRdGSGF-IQVVVKK-DKLENFEEAKK-LTTESSVevtGTV----VESPRA--PQGVEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 196 FATQVVLLSPCLHALP---SEHygfqDKEQRFRQRYLDLIiNDRPRQIFRTRAKIVSYLRSYLDSRDFTEVETPMMNAIA 272
Cdd:COG0017 87 QAEEIEVLGEADEPYPlqpKRH----SLEFLLDNRHLRLR-TNRFGAIFRIRSELARAIREFFQERGFVEVHTPIITASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 273 --GGATASPfVTHHNdlkRDLFMRVAPELYLKMLVvGGLERVYEIGKQFRNEGIDLT-HSPEFTTCEFYQAYADYNDLMA 349
Cdd:COG0017 162 teGGGELFP-VDYFG---KEAYLTQSGQLYKEALA-MALEKVYTFGPTFRAEKSNTRrHLAEFWMIEPEMAFADLEDVMD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 350 MTEDLISSMVKHITGGYET---TFESQTG--QVYTinwQSPWKRIDMIPALE--EACGDKFPPGDQLHTPEagtflkeml 422
Cdd:COG0017 237 LAEEMLKYIIKYVLENCPEeleFLGRDVErlEKVP---ESPFPRITYTEAIEilKKSGEKVEWGDDLGTEH--------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 423 kkmkvEctppltnarmldKLVGEFVEDKcinPTFVTGHPQMMSPL-AKAHRDTPGICERFEVfvttkeLLNAYTELndpf 501
Cdd:COG0017 305 -----E------------RYLGEEFFKK---PVFVTDYPKEIKAFyMKPNPDDPKTVAAFDL------LAPGIGEIig-g 357
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1064303005 502 dQRM-RFEEQANQ-KAQGDDEAQMvdENFCQALEYGLPPTGGWGMGIDRLTMFLTNNYSIKEVLAFP 566
Cdd:COG0017 358 sQREhRYDVLVERiKEKGLDPEDY--EWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFP 422
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
15-566 |
8.05e-22 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 99.40 E-value: 8.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 15 DEPTGEKVSKtelkKRLKSRAKEAEKQKKAATAPTkiqkETSSEQDEANLSAHQYFEIRSNRINKLRETKnsypyphKFE 94
Cdd:PLN02850 6 VEESGEKISK----KAAKKAAAKAEKLRREATAKA----AAASLEDEDDPLASNYGDVPLEELQSKVTGR-------EWT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 95 VTNDLrdfltvyknlakGEERTDVPIRIAGRIYTKRVSGnKLVFYDIRAEGVKVQVMCQAQNSTTG-----FEEQHEVLR 169
Cdd:PLN02850 71 DVSDL------------GEELAGSEVLIRGRVHTIRGKG-KSAFLVLRQSGFTVQCVVFVSEVTVSkgmvkYAKQLSRES 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 170 RGDIVGIVGFPGRTSPKTRDNGELSIfaTQVVLLSPCLHALP--------SE---HYGFQDKEQ--------RFRQRYLD 230
Cdd:PLN02850 138 VVDVEGVVSVPKKPVKGTTQQVEIQV--RKIYCVSKALATLPfnvedaarSEseiEKALQTGEQlvrvgqdtRLNNRVLD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 231 LIIndrP--RQIFRTRAKIVSYLRSYLDSRDFTEVETPMMNAIAGGATASPFVTHHNDLKRDLFMrvAPELYLKMLVVGG 308
Cdd:PLN02850 216 LRT---PanQAIFRIQSQVCNLFREFLLSKGFVEIHTPKLIAGASEGGSAVFRLDYKGQPACLAQ--SPQLHKQMAICGD 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 309 LERVYEIGKQFRNEGiDLTHSP--EFTTCEFYQAYAD-YNDLMamteDLISSMVKHITGGYETTFESQTGqvyTINWQSP 385
Cdd:PLN02850 291 FRRVFEIGPVFRAED-SFTHRHlcEFTGLDLEMEIKEhYSEVL----DVVDELFVAIFDGLNERCKKELE---AIREQYP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 386 WKRIdmipaleeacgdKF-PPGDQLHTPEAgtflKEMLKKMKVECTP--PLT--NARMLDKLVGE------FVEDK---C 451
Cdd:PLN02850 363 FEPL------------KYlPKTLRLTFAEG----IQMLKEAGVEVDPlgDLNteSERKLGQLVKEkygtdfYILHRyplA 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 452 INPtFVTghpqMMSPlakahrDTPGICERFEVFVTTKELLNAYTELNDPfdqrMRFEEQAnqKAQGDDEAQMvdENFCQA 531
Cdd:PLN02850 427 VRP-FYT----MPCP------DDPKYSNSFDVFIRGEEIISGAQRVHDP----ELLEKRA--EECGIDVKTI--STYIDS 487
|
570 580 590
....*....|....*....|....*....|....*
gi 1064303005 532 LEYGLPPTGGWGMGIDRLTMFLTNNYSIKEVLAFP 566
Cdd:PLN02850 488 FRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFP 522
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
136-364 |
3.80e-21 |
|
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439943 [Multi-domain] Cd Length: 589 Bit Score: 97.38 E-value: 3.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 136 LVFYDIR-AEGVkVQVMCQAQNSTTGFEEQHEvLRRGDIVGIVG-----FPGRTSPK--TrdnGELSIFATQVVLLSPCl 207
Cdd:COG0173 34 LIFIDLRdRYGI-TQVVFDPDDSAEAFEKAEK-LRSEYVIAVTGkvrarPEGTVNPKlpT---GEIEVLASELEILNKA- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 208 HALPsehygFQ-------DKEQRFRQRYLDLiinDRPR--QIFRTRAKIVSYLRSYLDSRDFTEVETPMMNAiaggAT-- 276
Cdd:COG0173 108 KTPP-----FQidddtdvSEELRLKYRYLDL---RRPEmqKNLILRHKVTKAIRNYLDENGFLEIETPILTK----STpe 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 277 -AspfvthhndlkRDlFM---RV----------APELYLKMLVVGGLERVYEIGKQFRNEgiDL--THSPEFTT--CEFy 338
Cdd:COG0173 176 gA-----------RD-YLvpsRVhpgkfyalpqSPQLFKQLLMVSGFDRYFQIARCFRDE--DLraDRQPEFTQldIEM- 240
|
250 260
....*....|....*....|....*.
gi 1064303005 339 qAYADYNDLMAMTEDLISSMVKHITG 364
Cdd:COG0173 241 -SFVDQEDVFELMEGLIRHLFKEVLG 265
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
120-364 |
5.49e-21 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 97.17 E-value: 5.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 120 IRIAGRIYTKRVSGNkLVFYDIRAEGVKVQVMCQAQNsttgFEEQHEVLRRGDIVGIVGFPG--RTSPKTRDN-----GE 192
Cdd:PLN02903 75 VTLCGWVDLHRDMGG-LTFLDVRDHTGIVQVVTLPDE----FPEAHRTANRLRNEYVVAVEGtvRSRPQESPNkkmktGS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 193 LSIFATQVVLLSPCLHALP---SEHYGFQD---KEQRFRQRYLDLiinDRPRQIF--RTRAKIVSYLRSYL-DSRDFTEV 263
Cdd:PLN02903 150 VEVVAESVDILNVVTKSLPflvTTADEQKDsikEEVRLRYRVLDL---RRPQMNAnlRLRHRVVKLIRRYLeDVHGFVEI 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 264 ETPMMN-AIAGGAtaspfvthhndlkRDLFM--RV----------APELYLKMLVVGGLERVYEIGKQFRNEGIDLTHSP 330
Cdd:PLN02903 227 ETPILSrSTPEGA-------------RDYLVpsRVqpgtfyalpqSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQP 293
|
250 260 270
....*....|....*....|....*....|....
gi 1064303005 331 EFTTCEFYQAYADYNDLMAMTEDLISSMVKHITG 364
Cdd:PLN02903 294 EFTQLDMELAFTPLEDMLKLNEDLIRQVFKEIKG 327
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
120-364 |
1.95e-20 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 95.13 E-value: 1.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 120 IRIAGRIYTKRVSGNkLVFYDIR-AEGVkVQVMCqaqNSTTGFEEQHEVLRRGDIVGIVG-----FPGRTSPKTRdNGEL 193
Cdd:PRK00476 20 VTLCGWVHRRRDHGG-LIFIDLRdREGI-VQVVF---DPDAEAFEVAESLRSEYVIQVTGtvrarPEGTVNPNLP-TGEI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 194 SIFATQVVLLSPClHALP-----SEHYGfqdKEQRFRQRYLDLiinDRPR--QIFRTRAKIVSYLRSYLDSRDFTEVETP 266
Cdd:PRK00476 94 EVLASELEVLNKS-KTLPfpiddEEDVS---EELRLKYRYLDL---RRPEmqKNLKLRSKVTSAIRNFLDDNGFLEIETP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 267 MM-NAIAGGAtaspfvthhndlkRDlFM---RV----------APELYLKMLVVGGLERVYEIGKQFRNEgiDL--THSP 330
Cdd:PRK00476 167 ILtKSTPEGA-------------RD-YLvpsRVhpgkfyalpqSPQLFKQLLMVAGFDRYYQIARCFRDE--DLraDRQP 230
|
250 260 270
....*....|....*....|....*....|....*.
gi 1064303005 331 EFTT--CEFyqAYADYNDLMAMTEDLISSMVKHITG 364
Cdd:PRK00476 231 EFTQidIEM--SFVTQEDVMALMEGLIRHVFKEVLG 264
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
241-567 |
8.68e-18 |
|
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. AspRS is a homodimer, which attaches a specific amino acid to the 3' OH group of ribose of the appropriate tRNA. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. AspRS in this family differ from those found in the AsxRS family by a GAD insert in the core domain.
Pssm-ID: 238400 [Multi-domain] Cd Length: 280 Bit Score: 83.78 E-value: 8.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 241 FRTRAKIVSYLRSYLDSRDFTEVETPMMNA-IAGGAtaspfvthhndlkRDLFM--RV----------APELYLKMLVVG 307
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKsTPEGA-------------RDFLVpsRLhpgkfyalpqSPQLFKQLLMVS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 308 GLERVYEIGKQFRNEGIDLTHSPEFTTCEFYQAYADYNDLMAMTEDLISSMVKHITGgyettfesqtgqvytINWQSPWK 387
Cdd:cd00777 68 GFDRYFQIARCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG---------------VELTTPFP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 388 RIDMIPALEEAcGDK------FPPGDqlHTPEAGTFlkemlkkmkvectppltnarmldklvgEFVEdkciNPtFVTGHP 461
Cdd:cd00777 133 RMTYAEAMERY-GFKflwivdFPLFE--WDEEEGRL---------------------------VSAH----HP-FTAPKE 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 462 QMMSPLAKAHRDTPGicERFEVFVTTKELLNAYTELNDPFDQRMRFEeqanqkAQGDDEAQMVDE--NFCQALEYGLPPT 539
Cdd:cd00777 178 EDLDLLEKDPEDARA--QAYDLVLNGVELGGGSIRIHDPDIQEKVFE------ILGLSEEEAEEKfgFLLEAFKYGAPPH 249
|
330 340
....*....|....*....|....*...
gi 1064303005 540 GGWGMGIDRLTMFLTNNYSIKEVLAFPM 567
Cdd:cd00777 250 GGIALGLDRLVMLLTGSESIRDVIAFPK 277
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
120-205 |
3.01e-17 |
|
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: 76.84 E-value: 3.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 120 IRIAGRIYTKRVSGnKLVFYDIRAEGVKVQVMCQAQNSTTGFEEqHEVLRRGDIVGIVGFPGRTSPKTRDNGELSIFATQ 199
Cdd:cd04100 2 VTLAGWVHSRRDHG-GLIFIDLRDGSGIVQVVVNKEELGEFFEE-AEKLRTESVVGVTGTVVKRPEGNLATGEIELQAEE 79
|
....*.
gi 1064303005 200 VVLLSP 205
Cdd:cd04100 80 LEVLSK 85
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
136-367 |
2.30e-14 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 76.18 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 136 LVFYDIRAEGVKVQVMCQAQNSTTGFEEQHEVLRRGDIVGIVGFPGRTSPKTR----DNGELSIFATQVVLLSPCLhALP 211
Cdd:PRK12820 36 LLFIHLRDRNGFIQAVFSPEAAPADVYELAASLRAEFCVALQGEVQKRLEETEnphiETGDIEVFVRELSILAASE-ALP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 212 sehYGFQDK----------------EQRFRQRYLDLiinDRP--RQIFRTRAKIVSYLRSYLDSRDFTEVETPMMNAIAG 273
Cdd:PRK12820 115 ---FAISDKamtagagsagadavneDLRLQYRYLDI---RRPamQDHLAKRHRIIKCARDFLDSRGFLEIETPILTKSTP 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 274 GATASPFVTHHNDLKRDLFMRVAPELYLKMLVVGGLERVYEIGKQFRNEGIDLTHSPEFTTCEFYQAYADYNDLMAMTED 353
Cdd:PRK12820 189 EGARDYLVPSRIHPKEFYALPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEFTQLDIEASFIDEEFIFELIEE 268
|
250
....*....|....
gi 1064303005 354 LISSMVKhiTGGYE 367
Cdd:PRK12820 269 LTARMFA--IGGIA 280
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
232-566 |
5.46e-14 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 73.52 E-value: 5.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 232 IINDRPRQIFRTRAKIVSYLRSYLDSRDFTEVETPMMnaiaggataSPFVTHHNDLKRDLFMRVAP------ELYL---- 301
Cdd:PRK06462 21 ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPII---------SPSTDPLMGLGSDLPVKQISidfygvEYYLadsm 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 302 ---KMLVVGGLERVYEIGKQFRNEGID---LTHSPEFTTCEFYQAYADYNDLMAMTEDLISSMVKHITGGYETTFESQTG 375
Cdd:PRK06462 92 ilhKQLALRMLGKIFYLSPNFRLEPVDkdtGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHEDELEFFGR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 376 QVYTINwqSPWKRIDMipalEEACgdKFPPGDQLHTPEAGTFLKEMLKKMkvectppltnaRMLDKlvgefvedkciNPT 455
Cdd:PRK06462 172 DLPHLK--RPFKRITH----KEAV--EILNEEGCRGIDLEELGSEGEKSL-----------SEHFE-----------EPF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 456 FVTGHPQMMSPL-AKAHRDTPGICERFEVFvttkeLLNAYTELNDPFDQRMRFEE-QANQKAQGDDEAQMvdENFCQALE 533
Cdd:PRK06462 222 WIIDIPKGSREFyDREDPERPGVLRNYDLL-----LPEGYGEAVSGGEREYEYEEiVERIREHGVDPEKY--KWYLEMAK 294
|
330 340 350
....*....|....*....|....*....|...
gi 1064303005 534 YGLPPTGGWGMGIDRLTMFLTNNYSIKEVLAFP 566
Cdd:PRK06462 295 EGPLPSAGFGIGVERLTRYICGLRHIREVQPFP 327
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
221-566 |
2.32e-13 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 72.72 E-value: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 221 EQRFRQRYLDLIiNDRPRQIFRTRAKIVSYLRSYLDSRDFTEVETPMMNAIAGGATASPFVTHHndLKRDLFMRVAPELY 300
Cdd:PTZ00401 194 DTRLNSRWMDLR-TPASGAIFRLQSRVCQYFRQFLIDSDFCEIHSPKIINAPSEGGANVFKLEY--FNRFAYLAQSPQLY 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 301 LKMLVVGGLERVYEIGKQFRNEGIDL-THSPEFTTCEFYQAYAD-YNDLMAMTEDLISSMVKHITGgyettfesQTGQVY 378
Cdd:PTZ00401 271 KQMVLQGDVPRVFEVGPVFRSENSNThRHLTEFVGLDVEMRINEhYYEVLDLAESLFNYIFERLAT--------HTKELK 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 379 TINWQSPWKRI--DMIPALEEACG-----DKFPPGD--------------QLHTPEAGTFLKEMLK-KMKVECTPPLTNA 436
Cdd:PTZ00401 343 AVCQQYPFEPLvwKLTPERMKELGvgvisEGVEPTDkyqarvhnmdsrmlRINYMHCIELLNTVLEeKMAPTDDINTTNE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 437 RMLDKLVGE------FVEDKCinPTFVTGHPQMMSPlakahrDTPGICERFEVFVTTKELLNAYTELNDPFDQRMRfeeq 510
Cdd:PTZ00401 423 KLLGKLVKErygtdfFISDRF--PSSARPFYTMECK------DDERFTNSYDMFIRGEEISSGAQRIHDPDLLLAR---- 490
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1064303005 511 anqkaqgddeAQMVDENFCQALEY------GLPPTGGWGMGIDRLTMFLTNNYSIKEVLAFP 566
Cdd:PTZ00401 491 ----------AKMLNVDLTPIKEYvdsfrlGAWPHGGFGVGLERVVMLYLGLSNVRLASLFP 542
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
243-358 |
1.96e-11 |
|
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.
Pssm-ID: 238391 [Multi-domain] Cd Length: 211 Bit Score: 63.68 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 243 TRAKIVSYLRSYLDSRDFTEVETPMMNAIAGGATA----SPFVTHHNDLKRDLFMRVAPELYLKMLVVGGL----ERVYE 314
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAghepKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIrklpLRLAE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1064303005 315 IGKQFRNEGI--DLTHSPEFTTCEFYQAYAD------YNDLMAMTEDLISSM 358
Cdd:cd00768 81 IGPAFRNEGGrrGLRRVREFTQLEGEVFGEDgeeaseFEELIELTEELLRAL 132
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
120-203 |
6.35e-11 |
|
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic acids. The family includes the anti-codon binding domain of lysyl, aspartyl, and asparaginyl -tRNA synthetases (See pfam00152). Aminoacyl-tRNA synthetases catalyze the addition of an amino acid to the appropriate tRNA molecule EC:6.1.1.-. This family also includes part of RecG helicase involved in DNA repair. Replication factor A is a hetero-trimeric complex, that contains a subunit in this family. This domain is also found at the C-terminus of bacterial DNA polymerase III alpha chain.
Pssm-ID: 460164 [Multi-domain] Cd Length: 75 Bit Score: 58.40 E-value: 6.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 120 IRIAGRIYTKRVSGNKLVFYDIRAEGVKVQVMCQAQNsttgFEEQHEVLRRGDIVGIVGfpgrtSPKTRDNGELSIFATQ 199
Cdd:pfam01336 1 VTVAGRVTSIRRSGGKLLFLTLRDGTGSIQVVVFKEE----AEKLAKKLKEGDVVRVTG-----KVKKRKGGELELVVEE 71
|
....
gi 1064303005 200 VVLL 203
Cdd:pfam01336 72 IELL 75
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
120-362 |
5.33e-07 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 52.42 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 120 IRIAGRIYTKRVSGnKLVFYDIRAEGVKVQVMCQAQNSTTGFEE-QHevLRRG---DIVGIVgfpgRTSPKTRDNGELSi 195
Cdd:PRK03932 19 VTVRGWVRTKRDSG-KIAFLQLRDGSCFKQLQVVKDNGEEYFEEiKK--LTTGssvIVTGTV----VESPRAGQGYELQ- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 196 fATQVVLLSpclhaLPSEHYGFQDKEQRFR----QRYLdliindRPRQ-----IFRTRAKIVSYLRSYLDSRDFTEVETP 266
Cdd:PRK03932 91 -ATKIEVIG-----EDPEDYPIQKKRHSIEflreIAHL------RPRTnkfgaVMRIRNTLAQAIHEFFNENGFVWVDTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 267 MM--NAIAGGATASPFVTHHNDLKRDLFMR-----VAPELYLKMLVVGgLERVYEIGKQFRNEGIDLT-HSPEFTTCEFY 338
Cdd:PRK03932 159 IItaSDCEGAGELFRVTTLDLDFSKDFFGKeayltVSGQLYAEAYAMA-LGKVYTFGPTFRAENSNTRrHLAEFWMIEPE 237
|
250 260
....*....|....*....|....
gi 1064303005 339 QAYADYNDLMAMTEDLISSMVKHI 362
Cdd:PRK03932 238 MAFADLEDNMDLAEEMLKYVVKYV 261
|
|
| pheS |
TIGR00468 |
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ... |
311-370 |
1.52e-04 |
|
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are heterodimeric, with 2 alpha (pheS) and 2 beta (pheT) subunits. This model describes the alpha subunit, which shows some similarity to class II aminoacyl-tRNA ligases. Mitochondrial phenylalanyl-tRNA synthetase is a single polypeptide chain, active as a monomer, and similar to this chain rather than to the beta chain, but excluded from this model. An interesting feature of the alignment of all sequences captured by this model is a deep split between non-spirochete bacterial examples and all other examples; supporting this split is a relative deletion of about 50 residues in the former set between two motifs well conserved throughout the alignment. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273095 [Multi-domain] Cd Length: 293 Bit Score: 43.84 E-value: 1.52e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303005 311 RVYEIGKQFRNEGIDLTHSPEFTTCEFyqAYADYNDLMAMTEDLISSMVKHITGGYETTF 370
Cdd:TIGR00468 152 RIFSPGRVFRNDTVDATHLPEFHQVEG--LVIDKNISFTNLKGFLEEFLKKMFGETEIRF 209
|
|
| PheRS_alpha_core |
cd00496 |
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ... |
311-363 |
7.56e-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: 41.38 E-value: 7.56e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1064303005 311 RVYEIGKQFRNEGIDLTHSPEFTTCEFyqAYADYN----DLMAMTEDLISSMVKHIT 363
Cdd:cd00496 82 RIFSIGRVYRNDEIDATHLPEFHQIEG--LVVDKGltfaDLKGTLEEFAKELFGPIT 136
|
|
| tRNA-synt_2d |
pfam01409 |
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ... |
311-358 |
4.08e-03 |
|
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only phenylalanyl-tRNA synthetases. This is the core catalytic domain.
Pssm-ID: 396130 [Multi-domain] Cd Length: 245 Bit Score: 39.10 E-value: 4.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1064303005 311 RVYEIGKQFRNEGIDLTHSPEFTTCEFYqaYADYN----DLMAMTEDLISSM 358
Cdd:pfam01409 104 KIFSIGRVFRRDQVDATHLPEFHQVEGL--VVDENvtfaDLKGVLEEFLRKF 153
|
|
| |
