|
Name |
Accession |
Description |
Interval |
E-value |
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
9-498 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 886.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 9 EENEQIAQRKLKLKKRREEGQA-YPNDFKRDSLAADLHAVYDQFDSGALTAKAIRVKMAGRMMTRRIMGKASFAHIQDMK 87
Cdd:PRK00484 2 ELNEQIAVRREKLAELREQGIDpYPNKFERTHTAAELRAKYDDKEKEELEELEIEVSVAGRVMLKRVMGKASFATLQDGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 88 GRMQIYVTRDSLPQGVYSDFKSWDLGDIVGIEGELFKTKTEELSVKVDQIRLLTKALRPMPDKFHGLHDQEQRFRQRYLD 167
Cdd:PRK00484 82 GRIQLYVSKDDVGEEALEAFKKLDLGDIIGVEGTLFKTKTGELSVKATELTLLTKSLRPLPDKFHGLTDVETRYRQRYVD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 168 LIVNESSRHLFQTRSQVIAQIRRFLDDRGYIEVETPMMHPLPGGAAARPFETHHNAMNMDLFLRIAPELYLKRLVVGGFE 247
Cdd:PRK00484 162 LIVNPESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARPFITHHNALDIDLYLRIAPELYLKRLIVGGFE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 248 KVYEINRNFRNEGISTRHNPEFTMLEFYQAYATYEDMMMLTESMIRHLAEKIFGVMEIKYQGVRIDLNKPFPRLSLRDAI 327
Cdd:PRK00484 242 RVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTYQGTEIDFGPPFKRLTMVDAI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 328 LQFnPGITPDQIDhLETARELAHKYEIATPAHYGLGKIQTELFEKLVEEKLQQPIFITHFPKEVSPLSRANEENDFITDR 407
Cdd:PRK00484 322 KEY-TGVDFDDMT-DEEARALAKELGIEVEKSWGLGKLINELFEEFVEPKLIQPTFITDYPVEISPLAKRHREDPGLTER 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 408 FEFYVGGREIANGFSELNDPEDQAARFREQLKARNAGDLEAMSFDEDYITALEYGLPPTAGEGIGIDRLVMLFTDNASIR 487
Cdd:PRK00484 400 FELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIR 479
|
490
....*....|.
gi 29653775 488 DVILFPLLRSK 498
Cdd:PRK00484 480 DVILFPLMRPE 490
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
9-498 |
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: 879.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 9 EENEQIAQRKLKLKKRREEG-QAYPNDFKRDSLAADLHAVYDQFDSGALTAKaiRVKMAGRMMTRRIMGKASFAHIQDMK 87
Cdd:COG1190 6 DLNEQIRVRREKLEELREAGiDPYPNKFPRTHTAAEIREKYDELEAEEETGD--EVSVAGRIMAKRDMGKASFADLQDGS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 88 GRMQIYVTRDSLPQGVYSDFKSWDLGDIVGIEGELFKTKTEELSVKVDQIRLLTKALRPMPDKFHGLHDQEQRFRQRYLD 167
Cdd:COG1190 84 GRIQLYLRRDELGEEAYELFKLLDLGDIVGVEGTVFRTKTGELSVKVEELTLLSKSLRPLPEKFHGLTDPETRYRQRYVD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 168 LIVNESSRHLFQTRSQVIAQIRRFLDDRGYIEVETPMMHPLPGGAAARPFETHHNAMNMDLFLRIAPELYLKRLVVGGFE 247
Cdd:COG1190 164 LIVNPEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 248 KVYEINRNFRNEGISTRHNPEFTMLEFYQAYATYEDMMMLTESMIRHLAEKIFGVMEIKYQGVRIDLNKPFPRLSLRDAI 327
Cdd:COG1190 244 RVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGTTKVTYQGQEIDLSPPWRRITMVEAI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 328 LQFNpGITPDQIDHLETARELAHKYEIATPAHYGLGKIQTELFEKLVEEKLQQPIFITHFPKEVSPLSRANEENDFITDR 407
Cdd:COG1190 324 KEAT-GIDVTPLTDDEELRALAKELGIEVDPGWGRGKLIDELFEELVEPKLIQPTFVTDYPVEVSPLAKRHRDDPGLTER 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 408 FEFYVGGREIANGFSELNDPEDQAARFREQLKARNAGDLEAMSFDEDYITALEYGLPPTAGEGIGIDRLVMLFTDNASIR 487
Cdd:COG1190 403 FELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIR 482
|
490
....*....|.
gi 29653775 488 DVILFPLLRSK 498
Cdd:COG1190 483 DVILFPLMRPE 493
|
|
| lysS_bact |
TIGR00499 |
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ... |
9-496 |
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: 649.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 9 EENEQIAQRKLKLKKRREEG-QAYPNDFKRDSLAADLHAVYDQFDSGALTAKAIRVKMAGRMMTRRIMGKASFAHIQDMK 87
Cdd:TIGR00499 1 ELNDQAQQRLEKLNRLRQTGnNPYLHKFERTHSAQEFQEKYADLSNEELKEKELKVSIAGRIKAIRSMGKATFITLQDES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 88 GRMQIYVTRDSLPQGVYSDFKS-WDLGDIVGIEGELFKTKTEELSVKVDQIRLLTKALRPMPDKFHGLHDQEQRFRQRYL 166
Cdd:TIGR00499 81 GQIQLYVNKNKLPEDFYEFDEYlLDLGDIIGVTGYPFKTKTGELSVKVTELQILTKCLQPLPDKWHGLTDQETRYRQRYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 167 DLIVNESSRHLFQTRSQVIAQIRRFLDDRGYIEVETPMMHPLPGGAAARPFETHHNAMNMDLFLRIAPELYLKRLVVGGF 246
Cdd:TIGR00499 161 DLIVNPDVRQTFLKRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKPFITHHNALDMDLYLRIAPELYLKRLIVGGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 247 EKVYEINRNFRNEGISTRHNPEFTMLEFYQAYATYEDMMMLTESMIRHLAEKIFGVMEIKYQGVRIDLNKPFPRLSLRDA 326
Cdd:TIGR00499 241 EKVYEIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTFIINYNDLEIDLKPPWKRITMVDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 327 ILQfNPGITPDQIDHLETARELAHKYEIATPAH-YGLGKIQTELFEKLVEEKLQQPIFITHFPKEVSPLSRANEENDFIT 405
Cdd:TIGR00499 321 LEM-VTGIDFDILKDDETAKALAKEHGIEVAEDsLTLGHILNKFFEQFLEHTLIQPTFITHYPAEISPLAKRDPSNPEFT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 406 DRFEFYVGGREIANGFSELNDPEDQAARFREQLKARNAGDLEAMSFDEDYITALEYGLPPTAGEGIGIDRLVMLFTDNAS 485
Cdd:TIGR00499 400 ERFELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGIGIDRLVMLLTDAPS 479
|
490
....*....|.
gi 29653775 486 IRDVILFPLLR 496
Cdd:TIGR00499 480 IRDVLLFPQLR 490
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
5-498 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 605.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 5 DQIKEENEQIAQRKLKLKKRREEGQAYPNDFKRDSLAADLHAVYDQFDSGALTAKAIRVKMAGRMMTRRIMGKASFAHIQ 84
Cdd:PRK12445 10 NEAIDFNDELRNRREKLAALRQQGVAFPNDFRRDHTSDQLHEEFDAKDNQELESLNIEVSVAGRMMTRRIMGKASFVTLQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 85 DMKGRMQIYVTRDSLPQGVYSD-FKSWDLGDIVGIEGELFKTKTEELSVKVDQIRLLTKALRPMPDKFHGLHDQEQRFRQ 163
Cdd:PRK12445 90 DVGGRIQLYVARDSLPEGVYNDqFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFHGLQDQEVRYRQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 164 RYLDLIVNESSRHLFQTRSQVIAQIRRFLDDRGYIEVETPMMHPLPGGAAARPFETHHNAMNMDLFLRIAPELYLKRLVV 243
Cdd:PRK12445 170 RYLDLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 244 GGFEKVYEINRNFRNEGISTRHNPEFTMLEFYQAYATYEDMMMLTESMIRHLAEKIFGVMEIKYQGVRIDLNKPFPRLSL 323
Cdd:PRK12445 250 GGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFDFGKPFEKLTM 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 324 RDAILQFNPGITPDQIDHLETARELAHKYEIATPAHYGLGKIQTELFEKLVEEKLQQPIFITHFPKEVSPLSRANEENDF 403
Cdd:PRK12445 330 REAIKKYRPETDMADLDNFDAAKALAESIGITVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDVNPE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 404 ITDRFEFYVGGREIANGFSELNDPEDQAARFREQLKARNAGDLEAMSFDEDYITALEYGLPPTAGEGIGIDRLVMLFTDN 483
Cdd:PRK12445 410 ITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNS 489
|
490
....*....|....*
gi 29653775 484 ASIRDVILFPLLRSK 498
Cdd:PRK12445 490 HTIRDVILFPAMRPQ 504
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
12-497 |
0e+00 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 600.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 12 EQI-AQRKLKLKKRREEGQ-AYPNDFKRDSLAADLHAVYDQFDSGALTAKAIrVKMAGRMMTRRIMGKASFAHIQDMKGR 89
Cdd:PLN02502 59 TQYrANRLKKVEALRAKGVePYPYKFDVTHTAPELQEKYGSLENGEELEDVS-VSVAGRIMAKRAFGKLAFYDLRDDGGK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 90 MQIYV--TRDSLPQGVYSDFKSW-DLGDIVGIEGELFKTKTEELSVKVDQIRLLTKALRPMPDKFHGLHDQEQRFRQRYL 166
Cdd:PLN02502 138 IQLYAdkKRLDLDEEEFEKLHSLvDRGDIVGVTGTPGKTKKGELSIFPTSFEVLTKCLLMLPDKYHGLTDQETRYRQRYL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 167 DLIVNESSRHLFQTRSQVIAQIRRFLDDRGYIEVETPMMHPLPGGAAARPFETHHNAMNMDLFLRIAPELYLKRLVVGGF 246
Cdd:PLN02502 218 DLIANPEVRDIFRTRAKIISYIRRFLDDRGFLEVETPMLNMIAGGAAARPFVTHHNDLNMDLYLRIATELHLKRLVVGGF 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 247 EKVYEINRNFRNEGISTRHNPEFTMLEFYQAYATYEDMMMLTESMIRHLAEKIFGVMEIKYQGVRIDLNKPFPRLSLRDA 326
Cdd:PLN02502 298 ERVYEIGRQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKELTGSYKIKYHGIEIDFTPPFRRISMISL 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 327 I-----LQFNPGITPDQIDHLetARELAHKYEIATPAHYGLGKIQTELFEKLVEEKLQQPIFITHFPKEVSPLSRANEEN 401
Cdd:PLN02502 378 VeeatgIDFPADLKSDEANAY--LIAACEKFDVKCPPPQTTGRLLNELFEEFLEETLVQPTFVLDHPVEMSPLAKPHRSK 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 402 DFITDRFEFYVGGREIANGFSELNDPEDQAARFREQLKARNAGDLEAMSFDEDYITALEYGLPPTAGEGIGIDRLVMLFT 481
Cdd:PLN02502 456 PGLTERFELFINGRELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRLVMLLT 535
|
490
....*....|....*.
gi 29653775 482 DNASIRDVILFPLLRS 497
Cdd:PLN02502 536 DSASIRDVIAFPAMKP 551
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
171-496 |
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: 524.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 171 NESSRHLFQTRSQVIAQIRRFLDDRGYIEVETPMMHPLPGGAAARPFETHHNAMNMDLFLRIAPELYLKRLVVGGFEKVY 250
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 251 EINRNFRNEGISTRHNPEFTMLEFYQAYATYEDMMMLTESMIRHLAEKIFGVMEIKYQGVRIDLNKPFPRLSLRDAILQF 330
Cdd:cd00775 81 EIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIEYGGKELDFTPPFKRVTMVDALKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 331 NPGITP--DQIDHLETARELAHKYEIATPAHYGLGKIQTELFEKLVEEKLQQPIFITHFPKEVSPLSRANEENDFITDRF 408
Cdd:cd00775 161 TGIDFPelDLEQPEELAKLLAKLIKEKIEKPRTLGKLLDKLFEEFVEPTLIQPTFIIDHPVEISPLAKRHRSNPGLTERF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 409 EFYVGGREIANGFSELNDPEDQAARFREQLKARNAGDLEAMSFDEDYITALEYGLPPTAGEGIGIDRLVMLFTDNASIRD 488
Cdd:cd00775 241 ELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLTDSNSIRD 320
|
....*...
gi 29653775 489 VILFPLLR 496
Cdd:cd00775 321 VILFPAMR 328
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
12-496 |
5.39e-170 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 508.35 E-value: 5.39e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 12 EQIAQRKLKLKKRREEG-QAYPNDFKRDSLAADlhAVydqfdsGALTAKAIRVkmAGRMMTRRIMGKASFAHIQDMKGRM 90
Cdd:PRK02983 612 EQVRVRLAKLEALRAAGvDPYPVGVPPTHTVAE--AL------DAPTGEEVSV--SGRVLRIRDYGGVLFADLRDWSGEL 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 91 QIYVTRDSLPQGVYSDFKSW-DLGDIVGIEGELFKTKTEELSVKVDQIRLLTKALRPMPDKFHGLHDQEQRFRQRYLDLI 169
Cdd:PRK02983 682 QVLLDASRLEQGSLADFRAAvDLGDLVEVTGTMGTSRNGTLSLLVTSWRLAGKCLRPLPDKWKGLTDPEARVRQRYLDLA 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 170 VNESSRHLFQTRSQVIAQIRRFLDDRGYIEVETPMMHPLPGGAAARPFETHHNAMNMDLFLRIAPELYLKRLVVGGFEKV 249
Cdd:PRK02983 762 VNPEARDLLRARSAVVRAVRETLVARGFLEVETPILQQVHGGANARPFVTHINAYDMDLYLRIAPELYLKRLCVGGVERV 841
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 250 YEINRNFRNEGISTRHNPEFTMLEFYQAYATYEDMMMLTESMIRHLAEKIFGVMEI-----KYQGVRIDLNKPFPRLSLR 324
Cdd:PRK02983 842 FELGRNFRNEGVDATHNPEFTLLEAYQAHADYDTMRDLTRELIQNAAQAAHGAPVVmrpdgDGVLEPVDISGPWPVVTVH 921
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 325 DAILQ-FNPGITPDQidHLETARELAHKYEIATPAHYGLGKIQTELFEKLVEEKLQQPIFITHFPKEVSPLSRANEENDF 403
Cdd:PRK02983 922 DAVSEaLGEEIDPDT--PLAELRKLCDAAGIPYRTDWDAGAVVLELYEHLVEDRTTFPTFYTDFPTSVSPLTRPHRSDPG 999
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 404 ITDRFEFYVGGREIANGFSELNDPEDQAARFREQ-LKARnAGDLEAMSFDEDYITALEYGLPPTAGEGIGIDRLVMLFTd 482
Cdd:PRK02983 1000 LAERWDLVAWGVELGTAYSELTDPVEQRRRLTEQsLLAA-GGDPEAMELDEDFLQALEYAMPPTGGLGMGVDRLVMLLT- 1077
|
490
....*....|....
gi 29653775 483 NASIRDVILFPLLR 496
Cdd:PRK02983 1078 GRSIRETLPFPLVK 1091
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
4-496 |
1.57e-123 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 373.19 E-value: 1.57e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 4 KDQIKEENEQIAQR-------KLKLKKRREEGQAYPNDFKRDSLAADLHAVYDQFDSGALTAKAIrVKMAGRMMTRRIMG 76
Cdd:PTZ00417 70 KDKKKEEEAEVDPRlyyenrsKFIQEQKAKGINPYPHKFERTITVPEFVEKYQDLASGEHLEDTI-LNVTGRIMRVSASG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 77 -KASFAHIQDMKGRMQI---YVTRDSLPQGVYSDFKSWDLGDIVGIEGELFKTKTEELSVKVDQIRLLTKALRPMPDKFh 152
Cdd:PTZ00417 149 qKLRFFDLVGDGAKIQVlanFAFHDHTKSNFAECYDKIRRGDIVGIVGFPGKSKKGELSIFPKETIILSPCLHMLPMKY- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 153 GLHDQEQRFRQRYLDLIVNESSRHLFQTRSQVIAQIRRFLDDRGYIEVETPMMHPLPGGAAARPFETHHNAMNMDLFLRI 232
Cdd:PTZ00417 228 GLKDTEIRYRQRYLDLMINESTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLVAGGANARPFITHHNDLDLDLYLRI 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 233 APELYLKRLVVGGFEKVYEINRNFRNEGISTRHNPEFTMLEFYQAYATYEDMMMLTESMIRHLAEKIFGVMEIKY----- 307
Cdd:PTZ00417 308 ATELPLKMLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHLFGTYKILYnkdgp 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 308 --QGVRIDLNKPFPRLSLRDAILQFNPGITPDQIDHLETAREL-----AHKYEIATPAhyGLGKIQTELFEKLVEEKL-Q 379
Cdd:PTZ00417 388 ekDPIEIDFTPPYPKVSIVEELEKLTNTKLEQPFDSPETINKMinlikENKIEMPNPP--TAAKLLDQLASHFIENKYpN 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 380 QPIFITHFPKEVSPLSRANEENDFITDRFEFYVGGREIANGFSELNDPEDQAARFREQLKARNAGDLEAMSFDEDYITAL 459
Cdd:PTZ00417 466 KPFFIIEHPQIMSPLAKYHRSKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCTSL 545
|
490 500 510
....*....|....*....|....*....|....*..
gi 29653775 460 EYGLPPTAGEGIGIDRLVMLFTDNASIRDVILFPLLR 496
Cdd:PTZ00417 546 EYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFPTMR 582
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
156-496 |
6.29e-120 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 354.18 E-value: 6.29e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 156 DQEQRFRQRYLDLiVNESSRHLFQTRSQVIAQIRRFLDDRGYIEVETPMMHPLPGGAAARPFETHHNAMNMDLFLRIAPE 235
Cdd:pfam00152 1 DEETRLKYRYLDL-RRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 236 LYLKRLVVGGFEKVYEINRNFRNEGISTRHNPEFTMLEFYQAYATYEDMMMLTESMIRHLAEKIFGVMEIKYQGVRIDLN 315
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 316 KPFPRLSLRDAILQFNPGITPDQIdhletarelahkyeiatpahYGLGKIQTE-LFEKLVEEKLQQPIFITHFPKEVSPL 394
Cdd:pfam00152 160 KPFPRITYAEAIEKLNGKDVEELG--------------------YGSDKPDLRfLLELVIDKNKFNPLWVTDFPAEHHPF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 395 SRANEEND-FITDRFEFYVGGREIANGFSELNDPEDQAARFREQLKARNagdlEAMSFDEDYITALEYGLPPTAGEGIGI 473
Cdd:pfam00152 220 TMPKDEDDpALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDPE----EAEEKFGFYLDALKYGAPPHGGLGIGL 295
|
330 340
....*....|....*....|...
gi 29653775 474 DRLVMLFTDNASIRDVILFPLLR 496
Cdd:pfam00152 296 DRLVMLLTGLESIREVIAFPKTR 318
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
22-496 |
1.11e-118 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 362.81 E-value: 1.11e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 22 KKRREEGQAYpNDFKRDSLAADLHAVYDQFDSGALTAKAIrVKMAGRMMTRRIMGKASFAHIQDMKGRMQIYV------T 95
Cdd:PTZ00385 71 RSKLDLPAAY-SSFRGITPISEVRERYGYLASGDRAAQAT-VRVAGRVTSVRDIGKIIFVTIRSNGNELQVVGqvgehfT 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 96 RDSLPQgvysdFK-SWDLGDIVGIEGELFKTKTEELSVKVDQIRLLT------KALRPMPDKFHGLHDQEQRFRQRYLDL 168
Cdd:PTZ00385 149 REDLKK-----LKvSLRVGDIIGADGVPCRMQRGELSVAASRMLILSpyvctdQVVCPNLRGFTVLQDNDVKYRYRFTDM 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 169 IVNESSRHLFQTRSQVIAQIRRFLDDRGYIEVETPMMHPLPGGAAARPFETHHNAMNMDLFLRIAPELYLKRLVVGGFEK 248
Cdd:PTZ00385 224 MTNPCVIETIKKRHVMLQALRDYFNERNFVEVETPVLHTVASGANAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMER 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 249 VYEINRNFRNEGISTRHNPEFTMLEFYQAYATYEDMMMLTESMIRHLAEKIFGVMEIKYQ-------GVRIDLNKPFPRL 321
Cdd:PTZ00385 304 IYEIGKVFRNEDADRSHNPEFTSCEFYAAYHTYEDLMPMTEDIFRQLAMRVNGTTVVQIYpenahgnPVTVDLGKPFRRV 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 322 SLRDAIlQFNPGITPDQIDHLETARELAH------KYEIATPAHYGLGKIQTELFEKLVEEKLQQPIFITHFPKEVSPLS 395
Cdd:PTZ00385 384 SVYDEI-QRMSGVEFPPPNELNTPKGIAYmsvvmlRYNIPLPPVRTAAKMFEKLIDFFITDRVVEPTFVMDHPLFMSPLA 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 396 RANEENDFITDRFEFYVGGREIANGFSELNDPEDQAARFREQLKARNAGDLEAMSFDEDYITALEYGLPPTAGEGIGIDR 475
Cdd:PTZ00385 463 KEQVSRPGLAERFELFVNGIEYCNAYSELNDPHEQYHRFQQQLVDRQGGDEEAMPLDETFLKSLQVGLPPTAGWGMGIDR 542
|
490 500
....*....|....*....|.
gi 29653775 476 LVMLFTDNASIRDVILFPLLR 496
Cdd:PTZ00385 543 ALMLLTNSSNIRDGIIFPLLR 563
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
178-496 |
1.42e-107 |
|
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: 320.96 E-value: 1.42e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 178 FQTRSQVIAQIRRFLDDRGYIEVETPMMHPLPGGAAARPFETHHNAMNMDLFLRIAPELYLKRLVVGGFEKVYEINRNFR 257
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 258 NEGISTRHNPEFTMLEFYQAYATYEDMMMLTESMIRHLAEKIFGVMEIKYQGVRIDLNKPFPRLSLRDAIlqfnpgitpd 337
Cdd:cd00669 81 NEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYGFELEDFGLPFPRLTYREAL---------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 338 qidhletarelahkyeiatpahyglgkiqtelfeklveEKLQQPIFITHFPKE-VSPLSRANEENDFITDRFEFYVGGRE 416
Cdd:cd00669 151 --------------------------------------ERYGQPLFLTDYPAEmHSPLASPHDVNPEIADAFDLFINGVE 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 417 IANGFSELNDPEDQAARFREQLKARNAGdleaMSFDEDYITALEYGLPPTAGEGIGIDRLVMLFTDNASIRDVILFPLLR 496
Cdd:cd00669 193 VGNGSSRLHDPDIQAEVFQEQGINKEAG----MEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKMR 268
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
191-490 |
1.10e-78 |
|
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: 247.46 E-value: 1.10e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 191 FLDDRGYIEVETPMMHPLPGGAAA-RPFETH---HNAMNMDLFLRIAPELYLKRLVVGGFEKVYEINRNFRNEGISTRHN 266
Cdd:TIGR00462 1 FFAERGVLEVETPLLSPAPVTDPHlDAFATEfvgPDGQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 267 PEFTMLEFYQAYATYEDMMMLTESMIRHLAEkifgvmeikyqgvriDLNKPFPRLSLRDAILQFNpGITPDQIDhLETAR 346
Cdd:TIGR00462 81 PEFTMLEWYRPGFDYHDLMDEVEALLQELLG---------------DPFAPAERLSYQEAFLRYA-GIDPLTAS-LAELQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 347 ELAHKYEIATPAHYGLGKIQTELFEKLVEEKLQQ--PIFITHFPKEVSPLSRANEENDFITDRFEFYVGGREIANGFSEL 424
Cdd:TIGR00462 144 AAAAAHGIRASEEDDRDDLLDLLFSEKVEPHLGFgrPTFLYDYPASQAALARISPDDPRVAERFELYIKGLELANGFHEL 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29653775 425 NDPEDQAARFREQLKARNAGDLEAMSFDEDYITALEYGLPPTAGEGIGIDRLVMLFTDNASIRDVI 490
Cdd:TIGR00462 224 TDAAEQRRRFEADNALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDVL 289
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
174-490 |
2.86e-77 |
|
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441870 [Multi-domain] Cd Length: 309 Bit Score: 244.63 E-value: 2.86e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 174 SRHLFQTRSQVIAQIRRFLDDRGYIEVETPMMHPLPGGAAA-RPFET---HHNAMNMDLFLRIAPELYLKRLVVGGFEKV 249
Cdd:COG2269 2 SREALRARARLLAAIRAFFAERGVLEVETPALSVAPGTDPHlDSFATefiGPDGGGRPLYLHTSPEFAMKRLLAAGSGPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 250 YEINRNFRNEGISTRHNPEFTMLEFYQAYATYEDMMMLTESMIRHLAEkifgvmeikyqgvrIDLNKPFPRLSLRDAILQ 329
Cdd:COG2269 82 YQIAKVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLG--------------AAGFAPAERLSYQEAFLR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 330 FnPGITPDQIDhLETARELAHKYEIATPAhyGLGKiqTELFEKL----VEEKL--QQPIFITHFPKEVSPLSRANEENDF 403
Cdd:COG2269 148 Y-LGIDPLTAD-LDELAAAAAAAGLRVAD--DDDR--DDLLDLLlserVEPQLgrDRPTFLYDYPASQAALARISPDDPR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 404 ITDRFEFYVGGREIANGFSELNDPEDQAARFREQLKARNAGDLEAMSFDEDYITALEYGLPPTAGEGIGIDRLVMLFTDN 483
Cdd:COG2269 222 VAERFELYACGVELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALGA 301
|
....*..
gi 29653775 484 ASIRDVI 490
Cdd:COG2269 302 ERIDDVL 308
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
178-489 |
4.50e-60 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 199.77 E-value: 4.50e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 178 FQTRSQVIAQIRRFLDDRGYIEVETPMMHPLPG-GAAARPFETH----HNAMNMDLFLRIAPELYLKRLVVGGFEKVYEI 252
Cdd:PRK09350 5 LLKRAKIIAEIRRFFADRGVLEVETPILSQATVtDIHLVPFETRfvgpGASQGKTLWLMTSPEYHMKRLLAAGSGPIFQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 253 NRNFRNEGISTRHNPEFTMLEFYQAYATYEDMMMLTESMIRHLAEkifgvmeikyqgvridlNKPFPRLSLRDAILQFnP 332
Cdd:PRK09350 85 CKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLD-----------------CEPAESLSYQQAFLRY-L 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 333 GITPDQIDHLETaRELAHKYEIATPAHyglgkiqTE---------LFEKLVEEKLQQ--PIFITHFPKEVSPLSRANEEN 401
Cdd:PRK09350 147 GIDPLSADKTQL-REVAAKLGLSNIAD-------EEedrdtllqlLFTFGVEPNIGKekPTFVYHFPASQAALAKISTED 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 402 DFITDRFEFYVGGREIANGFSELNDPEDQAARFREQLKARNAGDLEAMSFDEDYITALEYGLPPTAGEGIGIDRLVMLFT 481
Cdd:PRK09350 219 HRVAERFEVYFKGIELANGFHELTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCSGVALGVDRLIMLAL 298
|
....*...
gi 29653775 482 DNASIRDV 489
Cdd:PRK09350 299 GAESISEV 306
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
62-168 |
1.13e-55 |
|
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: 181.14 E-value: 1.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 62 RVKMAGRMMTRRIMGKASFAHIQDMKGRMQIYVTRDSLPQGVYSDFKS-WDLGDIVGIEGELFKTKTEELSVKVDQIRLL 140
Cdd:cd04322 1 EVSVAGRIMSKRGSGKLSFADLQDESGKIQVYVNKDDLGEEEFEDFKKlLDLGDIIGVTGTPFKTKTGELSIFVKEFTLL 80
|
90 100
....*....|....*....|....*...
gi 29653775 141 TKALRPMPDKFHGLHDQEQRFRQRYLDL 168
Cdd:cd04322 81 SKSLRPLPEKFHGLTDVETRYRQRYLDL 108
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
62-493 |
4.92e-46 |
|
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: 166.00 E-value: 4.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 62 RVKMAGRMMTRRIMGKASFAHIQDMKGRMQIYVTRDSLPqgVYSDFKSWDLGDIVGIEGELFKTKTEELSV--KVDQIRL 139
Cdd:COG0017 16 EVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKLE--NFEEAKKLTTESSVEVTGTVVESPRAPQGVelQAEEIEV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 140 LTKALRPMP-DKFHglHDQEQRFRQRYLDLIVNESsRHLFQTRSQVIAQIRRFLDDRGYIEVETPMMHPLP--GGAAArp 216
Cdd:COG0017 94 LGEADEPYPlQPKR--HSLEFLLDNRHLRLRTNRF-GAIFRIRSELARAIREFFQERGFVEVHTPIITASAteGGGEL-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 217 FEThhnamnmDLFLRIA-----PELYlKRLVVGGFEKVYEINRNFRNEGIST-RHNPEFTMLEFYQAYATYEDMMMLTES 290
Cdd:COG0017 169 FPV-------DYFGKEAyltqsGQLY-KEALAMALEKVYTFGPTFRAEKSNTrRHLAEFWMIEPEMAFADLEDVMDLAEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 291 MIRHLAEKifgVME-----IKYQGVRID-----LNKPFPRLSLRDA--ILQfNPGITPDQIDHLETARElahKYeiatpa 358
Cdd:COG0017 241 MLKYIIKY---VLEncpeeLEFLGRDVErlekvPESPFPRITYTEAieILK-KSGEKVEWGDDLGTEHE---RY------ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 359 hyglgkiqtelfekLVEEKLQQPIFITHFPKEVSPL-SRANEENDFITDRFEFYVGG-REIANGFSELNDPEDQAARFRE 436
Cdd:COG0017 308 --------------LGEEFFKKPVFVTDYPKEIKAFyMKPNPDDPKTVAAFDLLAPGiGEIIGGSQREHRYDVLVERIKE 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 29653775 437 QlkarnaG-DLEAMSFdedYITALEYGLPPTAGEGIGIDRLVMLFTDNASIRDVILFP 493
Cdd:COG0017 374 K------GlDPEDYEW---YLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFP 422
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
62-493 |
2.35e-44 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 161.51 E-value: 2.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 62 RVKMAGRMMTRRIMGKASFAHIQDMKGRMQIYVTRDSLPQgVYSDFKSWDLGDIVGIEGELFKTKTEELSVKV--DQIRL 139
Cdd:PRK05159 18 EVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKVDEE-LFETIKKLKRESVVSVTGTVKANPKAPGGVEVipEEIEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 140 LTKALRPMPDKFHG--LHDQEQRFRQRYLDLiVNESSRHLFQTRSQVIAQIRRFLDDRGYIEVETPMM--HPLPGGAAAR 215
Cdd:PRK05159 97 LNKAEEPLPLDISGkvLAELDTRLDNRFLDL-RRPRVRAIFKIRSEVLRAFREFLYENGFTEIFTPKIvaSGTEGGAELF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 216 P---FEthHNAmnmdlFLRIAPELYLKRLVVGGFEKVYEINRNFRNEGIST-RHNPEFTMLEFYQAYAT-YEDMMMLTES 290
Cdd:PRK05159 176 PidyFE--KEA-----YLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTsRHLNEYTSIDVEMGFIDdHEDVMDLLEN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 291 MIRHLAEKIF--GVMEIKYQGVRIDLNK-PFPRLSLRDAI-LQFNPGITPDQIDHLETARELAhkyeiatpahygLGKIq 366
Cdd:PRK05159 249 LLRYMYEDVAenCEKELELLGIELPVPEtPIPRITYDEAIeILKSKGNEISWGDDLDTEGERL------------LGEY- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 367 telfekLVEEKLQQPIFITHFPKEVSPL-SRANEENDFITDRFEFYVGGREIANGFSELNDPEDQAARFREQlkarnagD 445
Cdd:PRK05159 316 ------VKEEYGSDFYFITDYPSEKRPFyTMPDEDDPEISKSFDLLFRGLEITSGGQRIHRYDMLVESIKEK-------G 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 29653775 446 LEAMSFdEDYITALEYGLPPTAGEGIGIDRLVMLFTDNASIRDVILFP 493
Cdd:PRK05159 383 LNPESF-EFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFP 429
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
155-493 |
2.03e-42 |
|
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: 153.49 E-value: 2.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 155 HDQEQRFRQRYLDLIVNESSRhLFQTRSQVIAQIRRFLDDRGYIEVETPMMhplpggaAARPFETHHNAMNMDLFLRIA- 233
Cdd:cd00776 2 ANLETLLDNRHLDLRTPKVQA-IFRIRSEVLRAFREFLRENGFTEVHTPKI-------TSTDTEGGAELFKVSYFGKPAy 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 234 ----PELYlKRLVVGGFEKVYEINRNFRNEGIST-RHNPEFTMLEFYQAYA-TYEDMMMLTESMIRH----LAEKIFGVM 303
Cdd:cd00776 74 laqsPQLY-KEMLIAALERVYEIGPVFRAEKSNTrRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYifkrVLERCAKEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 304 EIKYQGVRIDL--NKPFPRLSLRDAIlqfnpgitpdqidhlETARELAHKYEIAtpahYGLGkIQTELFEKLVEEKLQQP 381
Cdd:cd00776 153 ELVNQLNRELLkpLEPFPRITYDEAI---------------ELLREKGVEEEVK----WGED-LSTEHERLLGEIVKGDP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 382 IFITHFPKEVSPL-SRANEENDFITDRFEFYV-GGREIANGFSELNDPEDQAARFREQlkarnagDLEAMSFdEDYITAL 459
Cdd:cd00776 213 VFVTDYPKEIKPFyMKPDDDNPETVESFDLLMpGVGEIVGGSQRIHDYDELEERIKEH-------GLDPESF-EWYLDLR 284
|
330 340 350
....*....|....*....|....*....|....
gi 29653775 460 EYGLPPTAGEGIGIDRLVMLFTDNASIRDVILFP 493
Cdd:cd00776 285 KYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
178-493 |
2.31e-34 |
|
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. AspRS is a homodimer, which attaches a specific amino acid to the 3' OH group of ribose of the appropriate tRNA. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. AspRS in this family differ from those found in the AsxRS family by a GAD insert in the core domain.
Pssm-ID: 238400 [Multi-domain] Cd Length: 280 Bit Score: 130.39 E-value: 2.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 178 FQTRSQVIAQIRRFLDDRGYIEVETPMM-HPLPGGAaaR----PFETHHNamnmdLF--LRIAPELYLKRLVVGGFEKVY 250
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILtKSTPEGA--RdflvPSRLHPG-----KFyaLPQSPQLFKQLLMVSGFDRYF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 251 EINRNFRNEGISTRHNPEFTMLEFYQAYATYEDMMMLTESMIRHLAEKIFGVmeikyqgvriDLNKPFPRLSLRDAILQF 330
Cdd:cd00777 74 QIARCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLGV----------ELTTPFPRMTYAEAMERY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 331 npGITPDQIdhletarelahkyeiatpahyglgkIQTELFEKLVEEKlqqPIFITHFP-----KEVSPLSRANEEnDFIT 405
Cdd:cd00777 144 --GFKFLWI-------------------------VDFPLFEWDEEEG---RLVSAHHPftapkEEDLDLLEKDPE-DARA 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 406 DRFEFYVGGREIANGFSELNDPEDQAARFrEQLKARNAGDLEAMSFdedYITALEYGLPPTAGEGIGIDRLVMLFTDNAS 485
Cdd:cd00777 193 QAYDLVLNGVELGGGSIRIHDPDIQEKVF-EILGLSEEEAEEKFGF---LLEAFKYGAPPHGGIALGLDRLVMLLTGSES 268
|
....*...
gi 29653775 486 IRDVILFP 493
Cdd:cd00777 269 IRDVIAFP 276
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
169-493 |
2.35e-27 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 112.42 E-value: 2.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 169 IVNESSRHLFQTRSQVIAQIRRFLDDRGYIEVETPMMHPL-----PGGAAARPFETHHNAMNMDLFLRIAPELYlKRLVV 243
Cdd:PRK06462 21 ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIISPStdplmGLGSDLPVKQISIDFYGVEYYLADSMILH-KQLAL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 244 GGFEKVYEINRNFRNEG---ISTRHNPEFTMLEFYQAYATYEDMMMLTESMIRHLAEKIFGVM--EIKYQGVRI-DLNKP 317
Cdd:PRK06462 100 RMLGKIFYLSPNFRLEPvdkDTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHedELEFFGRDLpHLKRP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 318 FPRLSLRDAILQFNpgitpdqidhlETARELAHKYEIatpahyglgkiqTELFEKLVEEKLQQPIFITHFPKEVSPL-SR 396
Cdd:PRK06462 180 FKRITHKEAVEILN-----------EEGCRGIDLEEL------------GSEGEKSLSEHFEEPFWIIDIPKGSREFyDR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 397 ANEENDFITDRFEFYV--GGREIANGFSELNDPEDQAARFREqlkarnaGDLEAMSFdEDYITALEYGLPPTAGEGIGID 474
Cdd:PRK06462 237 EDPERPGVLRNYDLLLpeGYGEAVSGGEREYEYEEIVERIRE-------HGVDPEKY-KWYLEMAKEGPLPSAGFGIGVE 308
|
330
....*....|....*....
gi 29653775 475 RLVMLFTDNASIRDVILFP 493
Cdd:PRK06462 309 RLTRYICGLRHIREVQPFP 327
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
126-493 |
2.40e-27 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 115.55 E-value: 2.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 126 KTEELSVKVDQIRLLTKA--LrPMPDKFHGLHDQEQRFRQRYLDLIVNESSRHLfQTRSQVIAQIRRFLDDRGYIEVETP 203
Cdd:PRK00476 89 PTGEIEVLASELEVLNKSktL-PFPIDDEEDVSEELRLKYRYLDLRRPEMQKNL-KLRSKVTSAIRNFLDDNGFLEIETP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 204 MM-HPLPGGaaARpfethhnamnmDlFL---RI----------APELYLKRLVVGGFEKVYEINRNFRNEGISTRHNPEF 269
Cdd:PRK00476 167 ILtKSTPEG--AR-----------D-YLvpsRVhpgkfyalpqSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADRQPEF 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 270 TMLEFYQAYATYEDMMMLTESMIRHLAEKIFGVmeikyqgvriDLNKPFPRLSLRDAILQF------------------- 330
Cdd:PRK00476 233 TQIDIEMSFVTQEDVMALMEGLIRHVFKEVLGV----------DLPTPFPRMTYAEAMRRYgsdkpdlrfglelvdvtdl 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 331 -------------------------NPGITPD--QIDHL-ETARELAHKyeiatpahyGLGKIqtelfeKLVEEKLQQPI 382
Cdd:PRK00476 303 fkdsgfkvfagaandggrvkairvpGGAAQLSrkQIDELtEFAKIYGAK---------GLAYI------KVNEDGLKGPI 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 383 --FIThfPKEVSPLSRAN--EENDFItdrfeFYVGG-REIANGF---------SELN------------------DPEDQ 430
Cdd:PRK00476 368 akFLS--EEELAALLERTgaKDGDLI-----FFGADkAKVVNDAlgalrlklgKELGlidedkfaflwvvdfpmfEYDEE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 431 AARF--------------------REQLKAR-NAGDL------------------------EAMSFDEDY--------IT 457
Cdd:PRK00476 441 EGRWvaahhpftmpkdedldeletTDPGKARaYAYDLvlngyelgggsirihrpeiqekvfEILGISEEEaeekfgflLD 520
|
490 500 510
....*....|....*....|....*....|....*.
gi 29653775 458 ALEYGLPPTAGEGIGIDRLVMLFTDNASIRDVILFP 493
Cdd:PRK00476 521 ALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
54-327 |
3.29e-27 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 115.27 E-value: 3.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 54 GALTAKAI--RVKMAGRMMTRRIMGKASFAHIQDMKGRMQIYVTRDSLPQgVYSDFKSWDLGDIVGIEGELF-------- 123
Cdd:PLN02903 64 GALSVNDVgsRVTLCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDEFPE-AHRTANRLRNEYVVAVEGTVRsrpqespn 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 124 -KTKTEELSVKVDQIRLLTKALRPMPDKFHGLHDQ------EQRFRQRYLDLIVNESSRHLfQTRSQVIAQIRRFLDDR- 195
Cdd:PLN02903 143 kKMKTGSVEVVAESVDILNVVTKSLPFLVTTADEQkdsikeEVRLRYRVLDLRRPQMNANL-RLRHRVVKLIRRYLEDVh 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 196 GYIEVETPMM-HPLPGGAaaRPFETHHNAMNMDLF-LRIAPELYLKRLVVGGFEKVYEINRNFRNEGISTRHNPEFTMLE 273
Cdd:PLN02903 222 GFVEIETPILsRSTPEGA--RDYLVPSRVQPGTFYaLPQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEFTQLD 299
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 29653775 274 FYQAYATYEDMMMLTESMIRHLAEKIFGVmeikyqgvriDLNKPFPRLSLRDAI 327
Cdd:PLN02903 300 MELAFTPLEDMLKLNEDLIRQVFKEIKGV----------QLPNPFPRLTYAEAM 343
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
126-493 |
1.19e-24 |
|
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: 107.39 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 126 KTEELSVKVDQIRLLTKALR-PMPDKFHGLHDQEQRFRQRYLDLIVNESSRHLfQTRSQVIAQIRRFLDDRGYIEVETPM 204
Cdd:COG0173 90 PTGEIEVLASELEILNKAKTpPFQIDDDTDVSEELRLKYRYLDLRRPEMQKNL-ILRHKVTKAIRNYLDENGFLEIETPI 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 205 mhpL----PGGAaaRpfethhnamnmDlFL---RI----------APELYLKRLVVGGFEKVYEINRNFRNEgiSTRHN- 266
Cdd:COG0173 169 ---LtkstPEGA--R-----------D-YLvpsRVhpgkfyalpqSPQLFKQLLMVSGFDRYFQIARCFRDE--DLRADr 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 267 -PEFTMLEFYQAYATYEDMMMLTESMIRHLAEKIFGvmeikyqgvrIDLNKPFPRLSLRDAILQF--------------- 330
Cdd:COG0173 230 qPEFTQLDIEMSFVDQEDVFELMEGLIRHLFKEVLG----------VELPTPFPRMTYAEAMERYgsdkpdlrfglelvd 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 331 -----------------NPG-------------ITPDQIDHL-ETARELAHKyeiatpahyGLGKIqtelfeKLVEEKLQ 379
Cdd:COG0173 300 vtdifkdsgfkvfagaaENGgrvkainvpggasLSRKQIDELtEFAKQYGAK---------GLAYI------KVNEDGLK 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 380 QPI--FIThfPKEVSPL-SRAN-EENDFItdrfeFYVGG-------------REIA--------NGFS----------EL 424
Cdd:COG0173 365 SPIakFLS--EEELAAIlERLGaKPGDLI-----FFVADkpkvvnkalgalrLKLGkelglideDEFAflwvvdfplfEY 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 425 ND----------------PEDQAARFREQLKAR-NAGDL------------------------EAMSFDEDY-------- 455
Cdd:COG0173 438 DEeegrwvamhhpftmpkDEDLDLLETDPGKVRaKAYDLvlngyelgggsirihdpelqekvfELLGISEEEaeekfgfl 517
|
490 500 510
....*....|....*....|....*....|....*...
gi 29653775 456 ITALEYGLPPTAGEGIGIDRLVMLFTDNASIRDVILFP 493
Cdd:COG0173 518 LEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
62-493 |
1.45e-23 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 103.63 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 62 RVKMAGRMMTRRIMGKASFAHIQDMKGRMQ--IYVTRDSLPQGVYSDFKSWDLGDIVGIEGEL------FKTKTEELSVK 133
Cdd:PLN02850 83 EVLIRGRVHTIRGKGKSAFLVLRQSGFTVQcvVFVSEVTVSKGMVKYAKQLSRESVVDVEGVVsvpkkpVKGTTQQVEIQ 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 134 VDQIRLLTKALRPMP-----------DKFHGLHD--------QEQRFRQRYLDLIV--NESsrhLFQTRSQVIAQIRRFL 192
Cdd:PLN02850 163 VRKIYCVSKALATLPfnvedaarsesEIEKALQTgeqlvrvgQDTRLNNRVLDLRTpaNQA---IFRIQSQVCNLFREFL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 193 DDRGYIEVETP--MMHPLPGGAAArpFETHHnaMNMDLFLRIAPELYLKRLVVGGFEKVYEINRNFRNEGIST-RHNPEF 269
Cdd:PLN02850 240 LSKGFVEIHTPklIAGASEGGSAV--FRLDY--KGQPACLAQSPQLHKQMAICGDFRRVFEIGPVFRAEDSFThRHLCEF 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 270 TMLEFYQAYAT-YEDMMMLTESMIRHlaekIFGVMEIKYQGVRIDLNKPFP-----------RLSLRDAI--LQfNPGIT 335
Cdd:PLN02850 316 TGLDLEMEIKEhYSEVLDVVDELFVA----IFDGLNERCKKELEAIREQYPfeplkylpktlRLTFAEGIqmLK-EAGVE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 336 PDQIDHLETARELAhkyeiatpahygLGKiqtelfekLVEEKLQQPIFITH-FPKEVSPL-SRANEENDFITDRFEFYVG 413
Cdd:PLN02850 391 VDPLGDLNTESERK------------LGQ--------LVKEKYGTDFYILHrYPLAVRPFyTMPCPDDPKYSNSFDVFIR 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 414 GREIANGFSELNDPEDQAARfreqlkARNAG-DLEAMSfdeDYITALEYGLPPTAGEGIGIDRLVMLFTDNASIRDVILF 492
Cdd:PLN02850 451 GEEIISGAQRVHDPELLEKR------AEECGiDVKTIS---TYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLF 521
|
.
gi 29653775 493 P 493
Cdd:PLN02850 522 P 522
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
62-497 |
2.55e-23 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 103.53 E-value: 2.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 62 RVKMAGRMMTRRIMGKASFAHIQDMKGRMQIYVTRDSLPQGVYSDFKSWDLGDIVGIEGELFK---------TKTEELSV 132
Cdd:PRK12820 20 EVCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFSPEAAPADVYELAASLRAEFCVALQGEVQKrleetenphIETGDIEV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 133 KVDQIRLLTKALR---PMPDKF------HGLHD---QEQRFRQRYLDLIVNESSRHLFQtRSQVIAQIRRFLDDRGYIEV 200
Cdd:PRK12820 100 FVRELSILAASEAlpfAISDKAmtagagSAGADavnEDLRLQYRYLDIRRPAMQDHLAK-RHRIIKCARDFLDSRGFLEI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 201 ETPMM-HPLPGGAAAR--PFETHHNAMNMdlfLRIAPELYLKRLVVGGFEKVYEINRNFRNEGISTRHNPEFTMLEFYQA 277
Cdd:PRK12820 179 ETPILtKSTPEGARDYlvPSRIHPKEFYA---LPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEFTQLDIEAS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 278 YATYEDMMMLTESMIRHLAEkIFGvmeikyqgvrIDLNKPFPRLSLRDA------------------------------- 326
Cdd:PRK12820 256 FIDEEFIFELIEELTARMFA-IGG----------IALPRPFPRMPYAEAmdttgsdrpdlrfdlkfadatdifentrygi 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 327 ---ILQFNPGI----TPDQIDHL-------ETARELAHKY---------------------------------------- 352
Cdd:PRK12820 325 fkqILQRGGRIkginIKGQSEKLsknvlqnEYAKEIAPSFgakgmtwmraeaggldsnivqffsadekealkrrfhaedg 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 353 ----EIATPAH----YGLGKIQTELFEK--LVEEKLQQPIFITHFP-----------KEVSPLSRANEEN---------- 401
Cdd:PRK12820 405 dviiMIADASCaivlSALGQLRLHLADRlgLIPEGVFHPLWITDFPlfeatddggvtSSHHPFTAPDREDfdpgdieell 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 402 DFITDRFEFYVGGREIANGFSELNDPEDQAARFReqlkarnagdleAMSFDED--------YITALEYGLPPTAGEGIGI 473
Cdd:PRK12820 485 DLRSRAYDLVVNGEELGGGSIRINDKDIQLRIFA------------ALGLSEEdiedkfgfFLRAFDFAAPPHGGIALGL 552
|
570 580
....*....|....*....|....
gi 29653775 474 DRLVMLFTDNASIRDVILFPLLRS 497
Cdd:PRK12820 553 DRVVSMILQTPSIREVIAFPKNRS 576
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
63-493 |
4.01e-23 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 102.76 E-value: 4.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 63 VKMAGRMMTRRIMGKASFAHIQDMKGRMQIYVT-RDSLPQGVYSDFKSWDLGDIVGIEGELFK-------TKTEELSVKV 134
Cdd:PTZ00401 81 VLIRARVSTTRKKGKMAFMVLRDGSDSVQAMAAvEGDVPKEMIDFIGQIPTESIVDVEATVCKveqpitsTSHSDIELKV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 135 DQIRLLTKALRPMPDKFHGLHDQEQ----------RFRQRYLDLiVNESSRHLFQTRSQVIAQIRRFLDDRGYIEVETPM 204
Cdd:PTZ00401 161 KKIHTVTESLRTLPFTLEDASRKESdegakvnfdtRLNSRWMDL-RTPASGAIFRLQSRVCQYFRQFLIDSDFCEIHSPK 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 205 MHPLPGGAAARPFETHHnaMNMDLFLRIAPELYLKRLVVGGFEKVYEINRNFRNEGIST-RHNPEFTMLE--------FY 275
Cdd:PTZ00401 240 IINAPSEGGANVFKLEY--FNRFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNThRHLTEFVGLDvemrinehYY 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 276 QAYATYEDMM-MLTESMIRHLAE----------------------KIFGVMEIKYQGVRIDLNKPFPRlSLRDAILQFNp 332
Cdd:PTZ00401 318 EVLDLAESLFnYIFERLATHTKElkavcqqypfeplvwkltpermKELGVGVISEGVEPTDKYQARVH-NMDSRMLRIN- 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 333 giTPDQIDHLETARE--LAHKYEIATPAHYGLGkiqtelfeKLVEEKLQQPIFIT-HFPKEVSPLSRANEENDF-ITDRF 408
Cdd:PTZ00401 396 --YMHCIELLNTVLEekMAPTDDINTTNEKLLG--------KLVKERYGTDFFISdRFPSSARPFYTMECKDDErFTNSY 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 409 EFYVGGREIANGFSELNDPEDQAARfreqlkARNAG-DLEAMSfdeDYITALEYGLPPTAGEGIGIDRLVMLFTDNASIR 487
Cdd:PTZ00401 466 DMFIRGEEISSGAQRIHDPDLLLAR------AKMLNvDLTPIK---EYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVR 536
|
....*.
gi 29653775 488 DVILFP 493
Cdd:PTZ00401 537 LASLFP 542
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
63-493 |
8.58e-23 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 100.57 E-value: 8.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 63 VKMAGRMMTRRIMGKASFAHIQDMKGRMQIYVTRDSLPQgVYSDFKSWDLGDIVGIEGELFKTKTEELSV--KVDQIRLL 140
Cdd:PRK03932 19 VTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDNGEE-YFEEIKKLTTGSSVIVTGTVVESPRAGQGYelQATKIEVI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 141 TKALR--PMPDKFHG---LHDQeqrfrqryldlivnessRHL----------FQTRSQVIAQIRRFLDDRGYIEVETPMM 205
Cdd:PRK03932 98 GEDPEdyPIQKKRHSiefLREI-----------------AHLrprtnkfgavMRIRNTLAQAIHEFFNENGFVWVDTPII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 206 HPLPGGAAARPFETHHNAMNM--DLFLRIApelYLKrlVVG---------GFEKVYEINRNFRNEGIST-RHNPEFTMLE 273
Cdd:PRK03932 161 TASDCEGAGELFRVTTLDLDFskDFFGKEA---YLT--VSGqlyaeayamALGKVYTFGPTFRAENSNTrRHLAEFWMIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 274 FYQAYATYEDMMMLTESMIRHLAEKifgVME-----IKYQGVRID----------LNKPFPRLSLRDAIlqfnpgitpdq 338
Cdd:PRK03932 236 PEMAFADLEDNMDLAEEMLKYVVKY---VLEncpddLEFLNRRVDkgdierlenfIESPFPRITYTEAI----------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 339 iDHLETArelAHKYEIatPAHYGLgKIQTElFEK-LVEEKLQQPIFITHFPKEVSPL-SRANEEN------DFITDRfef 410
Cdd:PRK03932 302 -EILQKS---GKKFEF--PVEWGD-DLGSE-HERyLAEEHFKKPVFVTNYPKDIKAFyMRLNPDGktvaamDLLAPG--- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 411 yVGgrEIANGfSElndpedqaarfRE----QLKARnagdLEAMSFD-EDYITALE---YGLPPTAGEGIGIDRLVMLFTD 482
Cdd:PRK03932 371 -IG--EIIGG-SQ-----------REerldVLEAR----IKELGLNkEDYWWYLDlrrYGSVPHSGFGLGFERLVAYITG 431
|
490
....*....|.
gi 29653775 483 NASIRDVILFP 493
Cdd:PRK03932 432 LDNIRDVIPFP 442
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
180-309 |
8.20e-20 |
|
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: 87.94 E-value: 8.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 180 TRSQVIAQIRRFLDDRGYIEVETPMMHPLPGGAAARPFE----THHNAMNMDLFLRIAPELYLKRLVVG----GFEKVYE 251
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHEPkdllPVGAENEEDLYLRPTLEPGLVRLFVShirkLPLRLAE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29653775 252 INRNFRNEGIS--TRHNPEFTMLEFYQAYATYED------MMMLTESMIRHLAEKIFGVMEIKYQG 309
Cdd:cd00768 81 IGPAFRNEGGRrgLRRVREFTQLEGEVFGEDGEEasefeeLIELTEELLRALGIKLDIVFVEKTPG 146
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
63-140 |
6.57e-15 |
|
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic acids. The family includes the anti-codon binding domain of lysyl, aspartyl, and asparaginyl -tRNA synthetases (See pfam00152). Aminoacyl-tRNA synthetases catalyze the addition of an amino acid to the appropriate tRNA molecule EC:6.1.1.-. This family also includes part of RecG helicase involved in DNA repair. Replication factor A is a hetero-trimeric complex, that contains a subunit in this family. This domain is also found at the C-terminus of bacterial DNA polymerase III alpha chain.
Pssm-ID: 460164 [Multi-domain] Cd Length: 75 Bit Score: 69.57 E-value: 6.57e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29653775 63 VKMAGRMMT-RRIMGKASFAHIQDMKGRMQIYVTRDSlpqgVYSDFKSWDLGDIVGIEGELFKTKTEELSVKVDQIRLL 140
Cdd:pfam01336 1 VTVAGRVTSiRRSGGKLLFLTLRDGTGSIQVVVFKEE----AEKLAKKLKEGDVVRVTGKVKKRKGGELELVVEEIELL 75
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
62-142 |
1.15e-13 |
|
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: 66.44 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 62 RVKMAGRMMTRRIMGKASFAHIQDMKGRMQIYVTRDSLPqGVYSDFKSWDLGDIVGIEGELFKT-----KTEELSVKVDQ 136
Cdd:cd04100 1 EVTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEELG-EFFEEAEKLRTESVVGVTGTVVKRpegnlATGEIELQAEE 79
|
....*.
gi 29653775 137 IRLLTK 142
Cdd:cd04100 80 LEVLSK 85
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
229-493 |
2.11e-11 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 66.20 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 229 FLRIAPELYLKRLVvGGFEKVYEINRNFRNEGIST-RHNPEFTMLEFYQAYATYEDMMMLTESMIRHLAEKIFG--VMEI 305
Cdd:PTZ00425 327 FLTVSGQLSLENLC-SSMGDVYTFGPTFRAENSHTsRHLAEFWMIEPEIAFADLYDNMELAESYIKYCIGYVLNnnFDDI 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 306 KY----------QGVRIDLNKPFPRLSLRDAIlqfnpgitpdqidhlETARELAHKYEIatPAHYGLgKIQTElFEKLVE 375
Cdd:PTZ00425 406 YYfeenvetgliSRLKNILDEDFAKITYTNVI---------------DLLQPYSDSFEV--PVKWGM-DLQSE-HERFVA 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 376 EKL-QQPIFITHFPKEVSPL-SRANEEN------DFITDRFEFYVGGREiangfselndPEDQAARFREQLKARNAgDLE 447
Cdd:PTZ00425 467 EQIfKKPVIVYNYPKDLKAFyMKLNEDQktvaamDVLVPKIGEVIGGSQ----------REDNLERLDKMIKEKKL-NME 535
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 29653775 448 AMSFdedYITALEYGLPPTAGEGIGIDRLVMLFTDNASIRDVILFP 493
Cdd:PTZ00425 536 SYWW---YRQLRKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFP 578
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
249-493 |
4.40e-09 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 58.83 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 249 VYEINRNFRNEGIST-RHNPEFTMLEFYQAYATYEDMMMLT----ESMIRHLAEKIFGVMEI----KYQGVRIDLN---- 315
Cdd:PLN02603 324 VYTFGPTFRAENSNTsRHLAEFWMIEPELAFADLNDDMACAtaylQYVVKYILENCKEDMEFfntwIEKGIIDRLSdvve 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 316 KPFPRLSLRDAIlqfnpgitpdqidhlETARELAHKYEIatPAHYGLgKIQTELFEKLVEEKLQ-QPIFITHFPKEVSPL 394
Cdd:PLN02603 404 KNFVQLSYTDAI---------------ELLLKAKKKFEF--PVKWGL-DLQSEHERYITEEAFGgRPVIIRDYPKEIKAF 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 395 -SRANEEN------DFITDRFEFYVGGreiangfselndpeDQAARFREQLKARnagdLEAMSFDED----YITALEYGL 463
Cdd:PLN02603 466 yMRENDDGktvaamDMLVPRVGELIGG--------------SQREERLEYLEAR----LDELKLNKEsywwYLDLRRYGS 527
|
250 260 270
....*....|....*....|....*....|
gi 29653775 464 PPTAGEGIGIDRLVMLFTDNASIRDVILFP 493
Cdd:PLN02603 528 VPHAGFGLGFERLVQFATGIDNIRDAIPFP 557
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
249-493 |
5.43e-09 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 58.47 E-value: 5.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 249 VYEINRNFRNEGIST-RHNPEFTMLEFYQAYATYEDMMMLTESMIRH----LAEKIFGVMEIKYQGV------RIDL--N 315
Cdd:PLN02221 329 VYTFGPTFRAENSHTsRHLAEFWMVEPEIAFADLEDDMNCAEAYVKYmckwLLDKCFDDMELMAKNFdsgcidRLRMvaS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 316 KPFPRLSLRDAilqfnpgitpdqIDHLETAreLAHKYEIATPAHYGLgKIQTELFEKLVEEKLQQPIFITHFPKEVSPL- 394
Cdd:PLN02221 409 TPFGRITYTEA------------IELLEEA--VAKGKEFDNNVEWGI-DLASEHERYLTEVLFQKPLIVYNYPKGIKAFy 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 395 SRANEEN------DFITDRFEFYVGGREiangfselndpedQAARFrEQLKARnagdLEAMSFD----EDYITALEYGLP 464
Cdd:PLN02221 474 MRLNDDEktvaamDVLVPKVGELIGGSQ-------------REERY-DVIKQR----IEEMGLPiepyEWYLDLRRYGTV 535
|
250 260
....*....|....*....|....*....
gi 29653775 465 PTAGEGIGIDRLVMLFTDNASIRDVILFP 493
Cdd:PLN02221 536 KHCGFGLGFERMILFATGIDNIRDVIPFP 564
|
|
| pylS |
PRK09537 |
pyrrolysine--tRNA(Pyl) ligase; |
188-295 |
1.35e-05 |
|
pyrrolysine--tRNA(Pyl) ligase;
Pssm-ID: 236555 [Multi-domain] Cd Length: 417 Bit Score: 47.53 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 188 IRRFLDDRGYIEVETPMMhpLPGGAAARPFETHHNAMNMDLF-------LR--IAPELY--LKRL--VVGGFEKVYEINR 254
Cdd:PRK09537 213 ITKFFVDRGFLEIKSPIL--IPAEYIERMGIDNDTELSKQIFrvdknfcLRpmLAPGLYnyLRKLdrILPDPIKIFEIGP 290
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 29653775 255 NFRNEGISTRHNPEFTMLEFYQ--AYATYEDMMMLTESMIRHL 295
Cdd:PRK09537 291 CYRKESDGKEHLEEFTMVNFCQmgSGCTRENLENIIDDFLKHL 333
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
248-498 |
1.55e-05 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 47.56 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 248 KVYEINRNFRNEGI-STRHNPEFTMLEFYQAYATYEDMMMLTESMIRHLAEKIFG--VMEIKYQGVRID----------L 314
Cdd:PLN02532 391 NVYTFGPRFRADRIdSARHLAEMWMVEVEMAFSELEDAMNCAEDYFKFLCKWVLEncSEDMKFVSKRIDktistrleaiI 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 315 NKPFPRLSLRDAIlqfnpgitpdqiDHLETAreLAHKYEiaTPAHYGLGkIQTELFEKLVEEKLQQPIFITHFPKEVSPL 394
Cdd:PLN02532 471 SSSLQRISYTEAV------------DLLKQA--TDKKFE--TKPEWGIA-LTTEHLSYLADEIYKKPVIIYNYPKELKPF 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 395 -SRANEEN------DFITDRFEFYVGGREIANGFSELNDPEDQAARFREQLkarnagdleamsfdEDYITALEYGLPPTA 467
Cdd:PLN02532 534 yVRLNDDGktvaafDLVVPKVGTVITGSQNEERMDILNARIEELGLPREQY--------------EWYLDLRRHGTVKHS 599
|
250 260 270
....*....|....*....|....*....|.
gi 29653775 468 GEGIGIDRLVMLFTDNASIRDVILFPllRSK 498
Cdd:PLN02532 600 GFSLGFELMVLFATGLPDVRDAIPFP--RSW 628
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
54-168 |
3.16e-03 |
|
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli aspartyl-tRNA synthetase (AspRS), the human mitochondrial (mt) AspRS-2, the discriminating (D) Thermus thermophilus AspRS-1, and the nondiscriminating (ND) Helicobacter pylori AspRS. These homodimeric enzymes are class2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. Human mtAspRS participates in mitochondrial biosynthesis; this enzyme been shown to charge E.coli native tRNAsp in addition to in vitro transcribed human mitochondrial tRNAsp. T. thermophilus is rare among bacteria in having both a D_AspRS and a ND_AspRS. H.pylori ND-AspRS can charge both tRNAASp and tRNAAsn, it is fractionally more efficient at aminoacylating tRNAAsp over tRNAAsn. The H.pylori genome does not contain AsnRS.
Pssm-ID: 239812 [Multi-domain] Cd Length: 135 Bit Score: 37.89 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653775 54 GALTAKAI--RVKMAGRMMTRRIMGKASFAHIQDMKGRMQIYVTRDSLPqgVYSDFKSWDLGDIVGIEGELF-------- 123
Cdd:cd04317 6 GELRESHVgqEVTLCGWVQRRRDHGGLIFIDLRDRYGIVQVVFDPEEAP--EFELAEKLRNESVIQVTGKVRarpegtvn 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 29653775 124 -KTKTEELSVKVDQIRLLTKALRP---MPDKFHGlhDQEQRFRQRYLDL 168
Cdd:cd04317 84 pKLPTGEIEVVASELEVLNKAKTLpfeIDDDVNV--SEELRLKYRYLDL 130
|
|
| |
