|
Name |
Accession |
Description |
Interval |
E-value |
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
17-506 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 954.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 17 LHELLQVRHDKMNQIREWGFDPFGKKFEQTHHAADIVKAFGDKTKEELEAEENVVTIAGRLMAKRAMGKASFAQLLDRSG 96
Cdd:PRK00484 3 LNEQIAVRREKLAELREQGIDPYPNKFERTHTAAELRAKYDDKEKEELEELEIEVSVAGRVMLKRVMGKASFATLQDGSG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 97 QIQIYVRQDTIGDEAHKVFDISDIGDLIGIRGVVFKTKTGELSVKAKDFTYLSKSLRPLPEKYHGLKDIETRYRKRYVDL 176
Cdd:PRK00484 83 RIQLYVSKDDVGEEALEAFKKLDLGDIIGVEGTLFKTKTGELSVKATELTLLTKSLRPLPDKFHGLTDVETRYRQRYVDL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 177 IVNPEVRDTFITRSRILTSMRRYLDSLGYLEVETPTLHAIAGGASARPFITHHNALDMQLYMRIAIELHLKRLIVGGLEK 256
Cdd:PRK00484 163 IVNPESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARPFITHHNALDIDLYLRIAPELYLKRLIVGGFER 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 257 VYEIGRVYRNEGISTRHNPEFTMIELYEAYADYQDIMTLTEELIAHIAQEVLGTTKIEYQGNEIDLTPKWRRVHMVDLIK 336
Cdd:PRK00484 243 VYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTYQGTEIDFGPPFKRLTMVDAIK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 337 ENLGVDFWkEMSDDEARALAKEHGVAVEPHHTFGHVVNEFFEQKLEHTLIQPTFVYGHPVAISPLAKKNDEDPRFTDRFE 416
Cdd:PRK00484 323 EYTGVDFD-DMTDEEARALAKELGIEVEKSWGLGKLINELFEEFVEPKLIQPTFITDYPVEISPLAKRHREDPGLTERFE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 417 LFIVAREHANAFTELNDPIDQRERFEAQLLEKAAGNDEAHEMDDDFIEALEYGMPPTGGLGIGIDRLVMLLTNSPSIRDV 496
Cdd:PRK00484 402 LFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDV 481
|
490
....*....|
gi 1510971220 497 LLFPHMRARD 506
Cdd:PRK00484 482 ILFPLMRPEK 491
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
17-506 |
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: 944.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 17 LHELLQVRHDKMNQIREWGFDPFGKKFEQTHHAADIVKAFGDKTKEELEAEEnvVTIAGRLMAKRAMGKASFAQLLDRSG 96
Cdd:COG1190 7 LNEQIRVRREKLEELREAGIDPYPNKFPRTHTAAEIREKYDELEAEEETGDE--VSVAGRIMAKRDMGKASFADLQDGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 97 QIQIYVRQDTIGDEAHKVFDISDIGDLIGIRGVVFKTKTGELSVKAKDFTYLSKSLRPLPEKYHGLKDIETRYRKRYVDL 176
Cdd:COG1190 85 RIQLYLRRDELGEEAYELFKLLDLGDIVGVEGTVFRTKTGELSVKVEELTLLSKSLRPLPEKFHGLTDPETRYRQRYVDL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 177 IVNPEVRDTFITRSRILTSMRRYLDSLGYLEVETPTLHAIAGGASARPFITHHNALDMQLYMRIAIELHLKRLIVGGLEK 256
Cdd:COG1190 165 IVNPEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFER 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 257 VYEIGRVYRNEGISTRHNPEFTMIELYEAYADYQDIMTLTEELIAHIAQEVLGTTKIEYQGNEIDLTPKWRRVHMVDLIK 336
Cdd:COG1190 245 VFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGTTKVTYQGQEIDLSPPWRRITMVEAIK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 337 ENLGVDFWKEMSDDEARALAKEHGVAVEPHHTFGHVVNEFFEQKLEHTLIQPTFVYGHPVAISPLAKKNDEDPRFTDRFE 416
Cdd:COG1190 325 EATGIDVTPLTDDEELRALAKELGIEVDPGWGRGKLIDELFEELVEPKLIQPTFVTDYPVEVSPLAKRHRDDPGLTERFE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 417 LFIVAREHANAFTELNDPIDQRERFEAQLLEKAAGNDEAHEMDDDFIEALEYGMPPTGGLGIGIDRLVMLLTNSPSIRDV 496
Cdd:COG1190 405 LFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDV 484
|
490
....*....|
gi 1510971220 497 LLFPHMRARD 506
Cdd:COG1190 485 ILFPLMRPEK 494
|
|
| lysS_bact |
TIGR00499 |
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ... |
17-503 |
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: 752.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 17 LHELLQVRHDKMNQIREWGFDPFGKKFEQTHHAADIVKAFGDKTKEELEAEENVVTIAGRLMAKRAMGKASFAQLLDRSG 96
Cdd:TIGR00499 2 LNDQAQQRLEKLNRLRQTGNNPYLHKFERTHSAQEFQEKYADLSNEELKEKELKVSIAGRIKAIRSMGKATFITLQDESG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 97 QIQIYVRQDTIGDEAHKVF-DISDIGDLIGIRGVVFKTKTGELSVKAKDFTYLSKSLRPLPEKYHGLKDIETRYRKRYVD 175
Cdd:TIGR00499 82 QIQLYVNKNKLPEDFYEFDeYLLDLGDIIGVTGYPFKTKTGELSVKVTELQILTKCLQPLPDKWHGLTDQETRYRQRYLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 176 LIVNPEVRDTFITRSRILTSMRRYLDSLGYLEVETPTLHAIAGGASARPFITHHNALDMQLYMRIAIELHLKRLIVGGLE 255
Cdd:TIGR00499 162 LIVNPDVRQTFLKRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKPFITHHNALDMDLYLRIAPELYLKRLIVGGLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 256 KVYEIGRVYRNEGISTRHNPEFTMIELYEAYADYQDIMTLTEELIAHIAQEVLGTTKIEYQGNEIDLTPKWRRVHMVDLI 335
Cdd:TIGR00499 242 KVYEIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTFIINYNDLEIDLKPPWKRITMVDAL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 336 KENLGVDFWKEMSDDEARALAKEHGVAV-EPHHTFGHVVNEFFEQKLEHTLIQPTFVYGHPVAISPLAKKNDEDPRFTDR 414
Cdd:TIGR00499 322 EMVTGIDFDILKDDETAKALAKEHGIEVaEDSLTLGHILNKFFEQFLEHTLIQPTFITHYPAEISPLAKRDPSNPEFTER 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 415 FELFIVAREHANAFTELNDPIDQRERFEAQLLEKAAGNDEAHEMDDDFIEALEYGMPPTGGLGIGIDRLVMLLTNSPSIR 494
Cdd:TIGR00499 402 FELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGIGIDRLVMLLTDAPSIR 481
|
....*....
gi 1510971220 495 DVLLFPHMR 503
Cdd:TIGR00499 482 DVLLFPQLR 490
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
19-506 |
0e+00 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 711.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 19 ELLQVRHDKMNQIREWGFDPFGKKFEQTHHAADIVKAFGDKTKEElEAEENVVTIAGRLMAKRAMGKASFAQLLDRSGQI 98
Cdd:PLN02502 60 QYRANRLKKVEALRAKGVEPYPYKFDVTHTAPELQEKYGSLENGE-ELEDVSVSVAGRIMAKRAFGKLAFYDLRDDGGKI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 99 QIYVRQDTIGDEAH---KVFDISDIGDLIGIRGVVFKTKTGELSVKAKDFTYLSKSLRPLPEKYHGLKDIETRYRKRYVD 175
Cdd:PLN02502 139 QLYADKKRLDLDEEefeKLHSLVDRGDIVGVTGTPGKTKKGELSIFPTSFEVLTKCLLMLPDKYHGLTDQETRYRQRYLD 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 176 LIVNPEVRDTFITRSRILTSMRRYLDSLGYLEVETPTLHAIAGGASARPFITHHNALDMQLYMRIAIELHLKRLIVGGLE 255
Cdd:PLN02502 219 LIANPEVRDIFRTRAKIISYIRRFLDDRGFLEVETPMLNMIAGGAAARPFVTHHNDLNMDLYLRIATELHLKRLVVGGFE 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 256 KVYEIGRVYRNEGISTRHNPEFTMIELYEAYADYQDIMTLTEELIAHIAQEVLGTTKIEYQGNEIDLTPKWRRVHMVDLI 335
Cdd:PLN02502 299 RVYEIGRQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKELTGSYKIKYHGIEIDFTPPFRRISMISLV 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 336 KENLGVDFWKEMSDDEARALAKE----HGVAVEPHHTFGHVVNEFFEQKLEHTLIQPTFVYGHPVAISPLAKKNDEDPRF 411
Cdd:PLN02502 379 EEATGIDFPADLKSDEANAYLIAacekFDVKCPPPQTTGRLLNELFEEFLEETLVQPTFVLDHPVEMSPLAKPHRSKPGL 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 412 TDRFELFIVAREHANAFTELNDPIDQRERFEAQLLEKAAGNDEAHEMDDDFIEALEYGMPPTGGLGIGIDRLVMLLTNSP 491
Cdd:PLN02502 459 TERFELFINGRELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRLVMLLTDSA 538
|
490
....*....|....*
gi 1510971220 492 SIRDVLLFPHMRARD 506
Cdd:PLN02502 539 SIRDVIAFPAMKPQD 553
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
179-503 |
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: 591.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 179 NPEVRDTFITRSRILTSMRRYLDSLGYLEVETPTLHAIAGGASARPFITHHNALDMQLYMRIAIELHLKRLIVGGLEKVY 258
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 259 EIGRVYRNEGISTRHNPEFTMIELYEAYADYQDIMTLTEELIAHIAQEVLGTTKIEYQGNEIDLTPKWRRVHMVDLIKEN 338
Cdd:cd00775 81 EIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIEYGGKELDFTPPFKRVTMVDALKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 339 LGVDFWK---EMSDDEARALAKEHGVAVEPHHTFGHVVNEFFEQKLEHTLIQPTFVYGHPVAISPLAKKNDEDPRFTDRF 415
Cdd:cd00775 161 TGIDFPEldlEQPEELAKLLAKLIKEKIEKPRTLGKLLDKLFEEFVEPTLIQPTFIIDHPVEISPLAKRHRSNPGLTERF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 416 ELFIVAREHANAFTELNDPIDQRERFEAQLLEKAAGNDEAHEMDDDFIEALEYGMPPTGGLGIGIDRLVMLLTNSPSIRD 495
Cdd:cd00775 241 ELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLTDSNSIRD 320
|
....*...
gi 1510971220 496 VLLFPHMR 503
Cdd:cd00775 321 VILFPAMR 328
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
17-506 |
4.13e-174 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 519.14 E-value: 4.13e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 17 LHELLQVRHDKMNQIREWGFDPFGKKFEQTHHAADIVKAfgdktkeeleAEENVVTIAGRLMAKRAMGKASFAQLLDRSG 96
Cdd:PRK02983 610 LPEQVRVRLAKLEALRAAGVDPYPVGVPPTHTVAEALDA----------PTGEEVSVSGRVLRIRDYGGVLFADLRDWSG 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 97 QIQIYVRQDTIGDEAHKVFDIS-DIGDLIGIRGVVFKTKTGELSVKAKDFTYLSKSLRPLPEKYHGLKDIETRYRKRYVD 175
Cdd:PRK02983 680 ELQVLLDASRLEQGSLADFRAAvDLGDLVEVTGTMGTSRNGTLSLLVTSWRLAGKCLRPLPDKWKGLTDPEARVRQRYLD 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 176 LIVNPEVRDTFITRSRILTSMRRYLDSLGYLEVETPTLHAIAGGASARPFITHHNALDMQLYMRIAIELHLKRLIVGGLE 255
Cdd:PRK02983 760 LAVNPEARDLLRARSAVVRAVRETLVARGFLEVETPILQQVHGGANARPFVTHINAYDMDLYLRIAPELYLKRLCVGGVE 839
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 256 KVYEIGRVYRNEGISTRHNPEFTMIELYEAYADYQDIMTLTEELIAHIAQEVLGTTKI-----EYQGNEIDLTPKWRRVH 330
Cdd:PRK02983 840 RVFELGRNFRNEGVDATHNPEFTLLEAYQAHADYDTMRDLTRELIQNAAQAAHGAPVVmrpdgDGVLEPVDISGPWPVVT 919
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 331 MVDLIKENLGVDFWKEMSDDEARALAKEHGVAVEPHHTFGHVVNEFFEQKLEHTLIQPTFVYGHPVAISPLAKKNDEDPR 410
Cdd:PRK02983 920 VHDAVSEALGEEIDPDTPLAELRKLCDAAGIPYRTDWDAGAVVLELYEHLVEDRTTFPTFYTDFPTSVSPLTRPHRSDPG 999
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 411 FTDRFELFIVAREHANAFTELNDPIDQRERFEAQLLEKAAGNDEAHEMDDDFIEALEYGMPPTGGLGIGIDRLVMLLTNS 490
Cdd:PRK02983 1000 LAERWDLVAWGVELGTAYSELTDPVEQRRRLTEQSLLAAGGDPEAMELDEDFLQALEYAMPPTGGLGMGVDRLVMLLTGR 1079
|
490
....*....|....*.
gi 1510971220 491 pSIRDVLLFPHMRARD 506
Cdd:PRK02983 1080 -SIRETLPFPLVKPRQ 1094
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
17-505 |
9.43e-170 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 488.80 E-value: 9.43e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 17 LHELLQVRHDKMNQIREWGFdPFGKKFEQTHHAADIVKAFGDKTKEELEAEENVVTIAGRLMAKRAMGKASFAQLLDRSG 96
Cdd:PRK12445 15 FNDELRNRREKLAALRQQGV-AFPNDFRRDHTSDQLHEEFDAKDNQELESLNIEVSVAGRMMTRRIMGKASFVTLQDVGG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 97 QIQIYVRQDTIGDEAH-KVFDISDIGDLIGIRGVVFKTKTGELSVKAKDFTYLSKSLRPLPEKYHGLKDIETRYRKRYVD 175
Cdd:PRK12445 94 RIQLYVARDSLPEGVYnDQFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFHGLQDQEVRYRQRYLD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 176 LIVNPEVRDTFITRSRILTSMRRYLDSLGYLEVETPTLHAIAGGASARPFITHHNALDMQLYMRIAIELHLKRLIVGGLE 255
Cdd:PRK12445 174 LIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGFE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 256 KVYEIGRVYRNEGISTRHNPEFTMIELYEAYADYQDIMTLTEELIAHIAQEVLGTTKIEYQGNEIDLTPKWRRVHMVDLI 335
Cdd:PRK12445 254 RVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFDFGKPFEKLTMREAI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 336 KENLGVDFWKEMSD-DEARALAKEHGVAVEPHHTFGHVVNEFFEQKLEHTLIQPTFVYGHPVAISPLAKKNDEDPRFTDR 414
Cdd:PRK12445 334 KKYRPETDMADLDNfDAAKALAESIGITVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEITDR 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 415 FELFIVAREHANAFTELNDPIDQRERFEAQLLEKAAGNDEAHEMDDDFIEALEYGMPPTGGLGIGIDRLVMLLTNSPSIR 494
Cdd:PRK12445 414 FEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIR 493
|
490
....*....|.
gi 1510971220 495 DVLLFPHMRAR 505
Cdd:PRK12445 494 DVILFPAMRPQ 504
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
35-503 |
1.14e-138 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 412.10 E-value: 1.14e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 35 GFDPFGKKFEQTHHAADIVKAFGDKTKEElEAEENVVTIAGRLMAKRAMG-KASFAQLLDRSGQIQI---YVRQDTIGDE 110
Cdd:PTZ00417 100 GINPYPHKFERTITVPEFVEKYQDLASGE-HLEDTILNVTGRIMRVSASGqKLRFFDLVGDGAKIQVlanFAFHDHTKSN 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 111 AHKVFDISDIGDLIGIRGVVFKTKTGELSVKAKDFTYLSKSLRPLPEKYhGLKDIETRYRKRYVDLIVNPEVRDTFITRS 190
Cdd:PTZ00417 179 FAECYDKIRRGDIVGIVGFPGKSKKGELSIFPKETIILSPCLHMLPMKY-GLKDTEIRYRQRYLDLMINESTRSTFITRT 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 191 RILTSMRRYLDSLGYLEVETPTLHAIAGGASARPFITHHNALDMQLYMRIAIELHLKRLIVGGLEKVYEIGRVYRNEGIS 270
Cdd:PTZ00417 258 KIINYLRNFLNDRGFIEVETPTMNLVAGGANARPFITHHNDLDLDLYLRIATELPLKMLIVGGIDKVYEIGKVFRNEGID 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 271 TRHNPEFTMIELYEAYADYQDIMTLTEELIAHIAQEVLGTTKIEYQGN-------EIDLTPKWRRVHMVDLIKENLGVDF 343
Cdd:PTZ00417 338 NTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHLFGTYKILYNKDgpekdpiEIDFTPPYPKVSIVEELEKLTNTKL 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 344 WKEMSDDEARA----LAKEHGVAVEPHHTFGHVVNE----FFEQKLEHtliQPTFVYGHPVAISPLAKKNDEDPRFTDRF 415
Cdd:PTZ00417 418 EQPFDSPETINkminLIKENKIEMPNPPTAAKLLDQlashFIENKYPN---KPFFIIEHPQIMSPLAKYHRSKPGLTERL 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 416 ELFIVAREHANAFTELNDPIDQRERFEAQLLEKAAGNDEAHEMDDDFIEALEYGMPPTGGLGIGIDRLVMLLTNSPSIRD 495
Cdd:PTZ00417 495 EMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKD 574
|
....*...
gi 1510971220 496 VLLFPHMR 503
Cdd:PTZ00417 575 VILFPTMR 582
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
164-503 |
1.46e-126 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 371.51 E-value: 1.46e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 164 DIETRYRKRYVDLiVNPEVRDTFITRSRILTSMRRYLDSLGYLEVETPTLHAIAGGASARPFITHHNALDMQLYMRIAIE 243
Cdd:pfam00152 1 DEETRLKYRYLDL-RRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 244 LHLKRLIVGGLEKVYEIGRVYRNEGISTRHNPEFTMIELYEAYADYQDIMTLTEELIAHIAQEVLGTTKIEYQGNEIDLT 323
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 324 PKWRRVHMVDLIKENLGVDF--WKEMSDdearalakehgvavEPHHTFGhvvnefFEQKLEHTLIQPTFVYGHPVAISPL 401
Cdd:pfam00152 160 KPFPRITYAEAIEKLNGKDVeeLGYGSD--------------KPDLRFL------LELVIDKNKFNPLWVTDFPAEHHPF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 402 AKKNDED-PRFTDRFELFIVAREHANAFTELNDPIDQRERFEAQLLEKaagnDEAHEMDDDFIEALEYGMPPTGGLGIGI 480
Cdd:pfam00152 220 TMPKDEDdPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDP----EEAEEKFGFYLDALKYGAPPHGGLGIGL 295
|
330 340
....*....|....*....|...
gi 1510971220 481 DRLVMLLTNSPSIRDVLLFPHMR 503
Cdd:pfam00152 296 DRLVMLLTGLESIREVIAFPKTR 318
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
71-503 |
1.29e-121 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 370.90 E-value: 1.29e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 71 VTIAGRLMAKRAMGKASFAQLLDRSGQIQI--YVRQDTIGDEAHKVFDISDIGDLIGIRGVVFKTKTGELSVKAKDFTYL 148
Cdd:PTZ00385 110 VRVAGRVTSVRDIGKIIFVTIRSNGNELQVvgQVGEHFTREDLKKLKVSLRVGDIIGADGVPCRMQRGELSVAASRMLIL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 149 S------KSLRPLPEKYHGLKDIETRYRKRYVDLIVNPEVRDTFITRSRILTSMRRYLDSLGYLEVETPTLHAIAGGASA 222
Cdd:PTZ00385 190 SpyvctdQVVCPNLRGFTVLQDNDVKYRYRFTDMMTNPCVIETIKKRHVMLQALRDYFNERNFVEVETPVLHTVASGANA 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 223 RPFITHHNALDMQLYMRIAIELHLKRLIVGGLEKVYEIGRVYRNEGISTRHNPEFTMIELYEAYADYQDIMTLTEELIAH 302
Cdd:PTZ00385 270 KSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTSCEFYAAYHTYEDLMPMTEDIFRQ 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 303 IAQEVLGTTKIEYQ-----GN--EIDLTPKWRRVHMVDLIKENLGVDFWKEMSDDEARALAK------EHGVAVEPHHTF 369
Cdd:PTZ00385 350 LAMRVNGTTVVQIYpenahGNpvTVDLGKPFRRVSVYDEIQRMSGVEFPPPNELNTPKGIAYmsvvmlRYNIPLPPVRTA 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 370 GHVVNEFFEQKLEHTLIQPTFVYGHPVAISPLAKKNDEDPRFTDRFELFIVAREHANAFTELNDPIDQRERFEAQLLEKA 449
Cdd:PTZ00385 430 AKMFEKLIDFFITDRVVEPTFVMDHPLFMSPLAKEQVSRPGLAERFELFVNGIEYCNAYSELNDPHEQYHRFQQQLVDRQ 509
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1510971220 450 AGNDEAHEMDDDFIEALEYGMPPTGGLGIGIDRLVMLLTNSPSIRDVLLFPHMR 503
Cdd:PTZ00385 510 GGDEEAMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFPLLR 563
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
186-504 |
4.15e-100 |
|
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: 302.09 E-value: 4.15e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 186 FITRSRILTSMRRYLDSLGYLEVETPTLHAIAGGASARPFITHHNALDMQLYMRIAIELHLKRLIVGGLEKVYEIGRVYR 265
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 266 NEGISTRHNPEFTMIELYEAYADYQDIMTLTEELIAHIAQEVLGTTKIEYQGNEIDLTPKWRRVHMVDLIKEnlgvdfwk 345
Cdd:cd00669 81 NEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYGFELEDFGLPFPRLTYREALER-------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 346 emsddearalakehgvavephhtfghvvneffeqklehtLIQPTFVYGHPV-AISPLAKKNDEDPRFTDRFELFIVAREH 424
Cdd:cd00669 153 ---------------------------------------YGQPLFLTDYPAeMHSPLASPHDVNPEIADAFDLFINGVEV 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 425 ANAFTELNDPIDQRERFEAQLLEKAAGndeaHEMDDDFIEALEYGMPPTGGLGIGIDRLVMLLTNSPSIRDVLLFPHMRA 504
Cdd:cd00669 194 GNGSSRLHDPDIQAEVFQEQGINKEAG----MEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKMRR 269
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
183-497 |
9.26e-80 |
|
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: 251.18 E-value: 9.26e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 183 RDTFITRSRILTSMRRYLDSLGYLEVETPTLhAIAGGASA--RPFIT---HHNALDMQLYMRIAIELHLKRLIVGGLEKV 257
Cdd:COG2269 3 REALRARARLLAAIRAFFAERGVLEVETPAL-SVAPGTDPhlDSFATefiGPDGGGRPLYLHTSPEFAMKRLLAAGSGPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 258 YEIGRVYRNEGISTRHNPEFTMIELYEAYADYQDIMTLTEELIAHIAQEVLgttkieyqgneidlTPKWRRVHMVDLIKE 337
Cdd:COG2269 82 YQIAKVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAAG--------------FAPAERLSYQEAFLR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 338 NLGVDFWkEMSDDEARALAKEHGVAVEPHHTFGHVVNEFFEQKLEHTLIQ--PTFVYGHPVAISPLAKKNDEDPRFTDRF 415
Cdd:COG2269 148 YLGIDPL-TADLDELAAAAAAAGLRVADDDDRDDLLDLLLSERVEPQLGRdrPTFLYDYPASQAALARISPDDPRVAERF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 416 ELFIVAREHANAFTELNDPIDQRERFEAQLLEKAAGNDEAHEMDDDFIEALEYGMPPTGGLGIGIDRLVMLLTNSPSIRD 495
Cdd:COG2269 227 ELYACGVELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALGAERIDD 306
|
..
gi 1510971220 496 VL 497
Cdd:COG2269 307 VL 308
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
204-497 |
2.00e-70 |
|
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: 226.28 E-value: 2.00e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 204 GYLEVETPTLhAIAGGASA--RPFITH---HNALDMQLYMRIAIELHLKRLIVGGLEKVYEIGRVYRNEGISTRHNPEFT 278
Cdd:TIGR00462 6 GVLEVETPLL-SPAPVTDPhlDAFATEfvgPDGQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRHNPEFT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 279 MIELYEAYADYQDIMTLTEELIAHIAQevlgttkieyqgneiDLTPKWRRVHMVDLIKENLGVDFWKEmSDDEARALAKE 358
Cdd:TIGR00462 85 MLEWYRPGFDYHDLMDEVEALLQELLG---------------DPFAPAERLSYQEAFLRYAGIDPLTA-SLAELQAAAAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 359 HGVAVEPHHTFGHVVNEFFEQKLEHTLIQ--PTFVYGHPVAISPLAKKNDEDPRFTDRFELFIVAREHANAFTELNDPID 436
Cdd:TIGR00462 149 HGIRASEEDDRDDLLDLLFSEKVEPHLGFgrPTFLYDYPASQAALARISPDDPRVAERFELYIKGLELANGFHELTDAAE 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1510971220 437 QRERFEAQLLEKAAGNDEAHEMDDDFIEALEYGMPPTGGLGIGIDRLVMLLTNSPSIRDVL 497
Cdd:TIGR00462 229 QRRRFEADNALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDVL 289
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
185-496 |
5.63e-57 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 191.68 E-value: 5.63e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 185 TFITRSRILTSMRRYLDSLGYLEVETPTL-HAIAGGASARPFITHHNALD----MQLYMRIAIELHLKRLIVGGLEKVYE 259
Cdd:PRK09350 4 NLLKRAKIIAEIRRFFADRGVLEVETPILsQATVTDIHLVPFETRFVGPGasqgKTLWLMTSPEYHMKRLLAAGSGPIFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 260 IGRVYRNEGISTRHNPEFTMIELYEAYADYQDIMTLTEELIahiaQEVLGTTKIE---YQgneidltpkwrrvhmvDLIK 336
Cdd:PRK09350 84 ICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLL----QQVLDCEPAEslsYQ----------------QAFL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 337 ENLGVDfwkEMSDDEA--RALAKEHGVAvephhtfghvvNEFFEQKLEHTLIQ---------------PTFVYGHPVAIS 399
Cdd:PRK09350 144 RYLGID---PLSADKTqlREVAAKLGLS-----------NIADEEEDRDTLLQllftfgvepnigkekPTFVYHFPASQA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 400 PLAKKNDEDPRFTDRFELFIVAREHANAFTELNDPIDQRERFEAQLLEKAAGNDEAHEMDDDFIEALEYGMPPTGGLGIG 479
Cdd:PRK09350 210 ALAKISTEDHRVAERFEVYFKGIELANGFHELTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCSGVALG 289
|
330
....*....|....*..
gi 1510971220 480 IDRLVMLLTNSPSIRDV 496
Cdd:PRK09350 290 VDRLIMLALGAESISEV 306
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
71-176 |
8.19e-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: 179.21 E-value: 8.19e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 71 VTIAGRLMAKRAMGKASFAQLLDRSGQIQIYVRQDTIGDEAHKVF-DISDIGDLIGIRGVVFKTKTGELSVKAKDFTYLS 149
Cdd:cd04322 2 VSVAGRIMSKRGSGKLSFADLQDESGKIQVYVNKDDLGEEEFEDFkKLLDLGDIIGVTGTPFKTKTGELSIFVKEFTLLS 81
|
90 100
....*....|....*....|....*..
gi 1510971220 150 KSLRPLPEKYHGLKDIETRYRKRYVDL 176
Cdd:cd04322 82 KSLRPLPEKFHGLTDVETRYRQRYLDL 108
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
45-505 |
2.95e-51 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 180.39 E-value: 2.95e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 45 QTHHAADIvkafgdktKEELEAEEnvVTIAGRLMAKRAMGKASFAQLLDRSGQIQIYVRQDTIGDEAHKVFDISdIGDLI 124
Cdd:PRK05159 3 KRHLTSEL--------TPELDGEE--VTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKVDEELFETIKKLK-RESVV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 125 GIRGVVF---KTKTGeLSVKAKDFTYLSKSLRPLPEKYHG--LKDIETRYRKRYVDLiVNPEVRDTFITRSRILTSMRRY 199
Cdd:PRK05159 72 SVTGTVKanpKAPGG-VEVIPEEIEVLNKAEEPLPLDISGkvLAELDTRLDNRFLDL-RRPRVRAIFKIRSEVLRAFREF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 200 LDSLGYLEVETPTLHAIA--GGASARPfITHHN-----ALDMQLYmriaielhlKRLIVG-GLEKVYEIGRVYRNEGIST 271
Cdd:PRK05159 150 LYENGFTEIFTPKIVASGteGGAELFP-IDYFEkeaylAQSPQLY---------KQMMVGaGFERVFEIGPVFRAEEHNT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 272 -RHNPEFTMIELYEAYAD-YQDIMTLTEELIAHIAQEVlgttkIEYQGNEIDLtpkwrrvhmvdlikenLGVDF------ 343
Cdd:PRK05159 220 sRHLNEYTSIDVEMGFIDdHEDVMDLLENLLRYMYEDV-----AENCEKELEL----------------LGIELpvpetp 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 344 WKEMSDDEARALAKEHGVAVEPHHTFG----HVVNEFFEQKLEHTLIqptFVYGHPVAISPL-AKKNDEDPRFTDRFELF 418
Cdd:PRK05159 279 IPRITYDEAIEILKSKGNEISWGDDLDtegeRLLGEYVKEEYGSDFY---FITDYPSEKRPFyTMPDEDDPEISKSFDLL 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 419 -----IVA---REHanaftelndpidQRERFEAQLLEKaaGND-EAHEmddDFIEALEYGMPPTGGLGIGIDRLVMLLTN 489
Cdd:PRK05159 356 frgleITSggqRIH------------RYDMLVESIKEK--GLNpESFE---FYLEAFKYGMPPHGGFGLGLERLTMKLLG 418
|
490
....*....|....*.
gi 1510971220 490 SPSIRDVLLFPHMRAR 505
Cdd:PRK05159 419 LENIREAVLFPRDRHR 434
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
45-505 |
1.38e-50 |
|
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: 178.32 E-value: 1.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 45 QTHHAADIVKAFGDKTkeeleaeenvVTIAGRLMAKRAMGKASFAQLLDRSGQIQIyvrqdTIGDEAHKVFD-ISDI--G 121
Cdd:COG0017 1 KRTYIKDLLPEHVGQE----------VTVAGWVRTKRDSGGISFLILRDGSGFIQV-----VVKKDKLENFEeAKKLttE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 122 DLIGIRGVVFKTKT--GELSVKAKDFTYLSKSLRPLP--EKYHGLkdiETRYRKRYVDLiVNPEVRDTFITRSRILTSMR 197
Cdd:COG0017 66 SSVEVTGTVVESPRapQGVELQAEEIEVLGEADEPYPlqPKRHSL---EFLLDNRHLRL-RTNRFGAIFRIRSELARAIR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 198 RYLDSLGYLEVETPTLHAIA--GGAsarpfithhnalDM----------------QLYMRIAielhlkrliVGGLEKVYE 259
Cdd:COG0017 142 EFFQERGFVEVHTPIITASAteGGG------------ELfpvdyfgkeayltqsgQLYKEAL---------AMALEKVYT 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 260 IGRVYRNEGIST-RHNPEFTMIELYEAYADYQDIMTLTEELIAHIAQEVLgttkiEYQGNEIDLTPKWrrvhmVDLIKEN 338
Cdd:COG0017 201 FGPTFRAEKSNTrRHLAEFWMIEPEMAFADLEDVMDLAEEMLKYIIKYVL-----ENCPEELEFLGRD-----VERLEKV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 339 LGVDFwKEMSDDEARALAKEHGVAVE-------PHHTFghVVNEFFEqklehtliQPTFVYGHPVAISPL-AKKNDEDPR 410
Cdd:COG0017 271 PESPF-PRITYTEAIEILKKSGEKVEwgddlgtEHERY--LGEEFFK--------KPVFVTDYPKEIKAFyMKPNPDDPK 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 411 FTDRFELFivarehANAFTELndpI--DQRE-RFEaQLLEKAagndEAHEMD-DDF---IEALEYGMPPTGGLGIGIDRL 483
Cdd:COG0017 340 TVAAFDLL------APGIGEI---IggSQREhRYD-VLVERI----KEKGLDpEDYewyLDLRRYGSVPHAGFGLGLERL 405
|
490 500
....*....|....*....|..
gi 1510971220 484 VMLLTNSPSIRDVLLFPHMRAR 505
Cdd:COG0017 406 VMWLTGLENIREVIPFPRDPGR 427
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
47-505 |
9.22e-40 |
|
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative asparaginyl-tRNA synthetases (asnS), archaeal/eukaryotic type aspartyl-tRNA synthetases (aspS_arch), and bacterial type aspartyl-tRNA synthetases (aspS_bact), there is a striking similarity between asnS and aspS_arch in gap pattern and in sequence, and a striking divergence of aspS_bact. Consequently, a separate model was built for each of the three groups. This model, aspS_arch, represents aspartyl-tRNA synthetases from the eukaryotic cytosol and from the Archaea. In some species, this enzyme aminoacylates tRNA for both Asp and Asn; Asp-tRNA(asn) is subsequently transamidated to Asn-tRNA(asn). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273087 [Multi-domain] Cd Length: 428 Bit Score: 149.20 E-value: 9.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 47 HHAADIvkafgdktKEELEAEEnvVTIAGRLMAKRAMGKASFAQLLDRSGQIQIYVRQDTIGDEAHKVFDISDIGDLIGI 126
Cdd:TIGR00458 1 VYSADI--------KPEMDGQE--VTFMGWVHEIRDLGGLIFVLLRDREGLIQITAPAKKVSKNLFKWAKKLNLESVVAV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 127 RGVV-FKTKT-GELSVKAKDFTYLSKSLRPLP----EKYHGlkDIETRYRKRYVDLiVNPEVRDTFITRSRILTSMRRYL 200
Cdd:TIGR00458 71 RGIVkIKEKApGGFEIIPTKIEVINEAKEPLPldptEKVPA--ELDTRLDYRFLDL-RRPTVQAIFRIRSGVLESVREFL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 201 DSLGYLEVETPTLHAIA--GGASARPfITHhnaLDMQLYMRIAIELHLKRLIVGGLEKVYEIGRVYRNEGIST-RHNPEF 277
Cdd:TIGR00458 148 AEEGFIEVHTPKLVASAteGGTELFP-ITY---FEREAFLGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNThRHLNEA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 278 TMIELYEAYADYQDIMTLTEELIAHIAQEVLGTTKIEYQGNEIDLTpkwrrvhmvdliKENLGVDfwkEMSDDEARALAK 357
Cdd:TIGR00458 224 TSIDIEMAFEDHHDVMDILEELVVRVFEDVPERCAHQLETLEFKLE------------KPEGKFV---RLTYDEAIEMAN 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 358 EHGVAVEPHHTFGHVVNEFFEQKLEHTLiqptFVYGHPVAISPLAKKNDED-PRFTDRFELFIVAREHANAFTELNDPID 436
Cdd:TIGR00458 289 AKGVEIGWGEDLSTEAEKALGEEMDGLY----FITDWPTEIRPFYTMPDEDnPEISKSFDLMYRDLEISSGAQRIHLHDL 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1510971220 437 QRERFEAQLLEKaagndeahEMDDDFIEALEYGMPPTGGLGIGIDRLVMLLTNSPSIRDVLLFPHMRAR 505
Cdd:TIGR00458 365 LVERIKAKGLNP--------EGFKDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFPRDRKR 425
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
164-500 |
9.13e-39 |
|
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: 143.86 E-value: 9.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 164 DIETRYRKRYVDLiVNPEVRDTFITRSRILTSMRRYLDSLGYLEVETPTLHAIA--GGASARPFithhNALDMQLYMRIA 241
Cdd:cd00776 3 NLETLLDNRHLDL-RTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDteGGAELFKV----SYFGKPAYLAQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 242 IELHLKRLIvGGLEKVYEIGRVYRNEGIST-RHNPEFTMIELYEAYA-DYQDIMTLTEELIAHIAQEVLgttkiEYQGNE 319
Cdd:cd00776 78 PQLYKEMLI-AALERVYEIGPVFRAEKSNTrRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVL-----ERCAKE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 320 IdltpKWRRVHMVDLIKENLGvdfWKEMSDDEARALAKEHGVAVEPhhTFGHVVNEFFEQKL-EHTLIQPTFVYGHPVAI 398
Cdd:cd00776 152 L----ELVNQLNRELLKPLEP---FPRITYDEAIELLREKGVEEEV--KWGEDLSTEHERLLgEIVKGDPVFVTDYPKEI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 399 SPL-AKKNDEDPRFTDRFELF------IVA---REHanaftelnDPIDQRERFEAQLLEkaagndeaHEMDDDFIEALEY 468
Cdd:cd00776 223 KPFyMKPDDDNPETVESFDLLmpgvgeIVGgsqRIH--------DYDELEERIKEHGLD--------PESFEWYLDLRKY 286
|
330 340 350
....*....|....*....|....*....|..
gi 1510971220 469 GMPPTGGLGIGIDRLVMLLTNSPSIRDVLLFP 500
Cdd:cd00776 287 GMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
67-500 |
8.05e-36 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 140.59 E-value: 8.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 67 EENV---VTIAGRLMAKRAMGKASFAQLLDRSGQIQIYVRQDTigdEAHKVfdISDIG--DLIGIRGVVF---------K 132
Cdd:PRK00476 13 ESHVgqtVTLCGWVHRRRDHGGLIFIDLRDREGIVQVVFDPDA---EAFEV--AESLRseYVIQVTGTVRarpegtvnpN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 133 TKTGELSVKAKDFTYLSKSlRPLPEKYHGLKDI--ETRYRKRYVDLiVNPEVRDTFITRSRILTSMRRYLDSLGYLEVET 210
Cdd:PRK00476 88 LPTGEIEVLASELEVLNKS-KTLPFPIDDEEDVseELRLKYRYLDL-RRPEMQKNLKLRSKVTSAIRNFLDDNGFLEIET 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 211 PTLhaiagGAS----ARPFI----THHN---ALDM------QLYMriaielhlkrliVGGLEKVYEIGRVYRNEGISTRH 273
Cdd:PRK00476 166 PIL-----TKStpegARDYLvpsrVHPGkfyALPQspqlfkQLLM------------VAGFDRYYQIARCFRDEDLRADR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 274 NPEFTMIELYEAYADYQDIMTLTEELIAHIAQEVLGttkieyqgneIDLTPKWRR--------------------VHMVD 333
Cdd:PRK00476 229 QPEFTQIDIEMSFVTQEDVMALMEGLIRHVFKEVLG----------VDLPTPFPRmtyaeamrrygsdkpdlrfgLELVD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 334 LIKENLGVDFW--------------------------KEMsdDEARALAKEHG------VAVEPHHTFGHVVNEFFEQKL 381
Cdd:PRK00476 299 VTDLFKDSGFKvfagaandggrvkairvpggaaqlsrKQI--DELTEFAKIYGakglayIKVNEDGLKGPIAKFLSEEEL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 382 EhTLIQPT---------FVYGHPVAIS------------------------------PLAKKNDEDPR-------FT--- 412
Cdd:PRK00476 377 A-ALLERTgakdgdlifFGADKAKVVNdalgalrlklgkelglidedkfaflwvvdfPMFEYDEEEGRwvaahhpFTmpk 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 413 --DRFELFIVAREHANAF--------TEL-------NDPIDQRERFEaqllekAAGNDEAhEMDDDF---IEALEYGMPP 472
Cdd:PRK00476 456 deDLDELETTDPGKARAYaydlvlngYELgggsiriHRPEIQEKVFE------ILGISEE-EAEEKFgflLDALKYGAPP 528
|
570 580
....*....|....*....|....*...
gi 1510971220 473 TGGLGIGIDRLVMLLTNSPSIRDVLLFP 500
Cdd:PRK00476 529 HGGIAFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
186-500 |
1.68e-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: 130.77 E-value: 1.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 186 FITRSRILTSMRRYLDSLGYLEVETPTLhaiagGAS----ARPFI----THHN---ALDM--QLYMRIaielhlkrLIVG 252
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPIL-----TKStpegARDFLvpsrLHPGkfyALPQspQLFKQL--------LMVS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 253 GLEKVYEIGRVYRNEGISTRHNPEFTMIELYEAYADYQDIMTLTEELIAHIAQEVLGttkieyqgneIDLTPKWRRVHMV 332
Cdd:cd00777 68 GFDRYFQIARCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG----------VELTTPFPRMTYA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 333 DLIkENLGVDF-----WKEMSDDEaralakEHGVAVEPHHTFGHVvneffEQKLEHTLiqptfvyghpvaisplaKKNDE 407
Cdd:cd00777 138 EAM-ERYGFKFlwivdFPLFEWDE------EEGRLVSAHHPFTAP-----KEEDLDLL-----------------EKDPE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 408 DPRfTDRFELFIVAREHANAFTELNDPIDQRERFEAQLLEKAagndEAHEMDDDFIEALEYGMPPTGGLGIGIDRLVMLL 487
Cdd:cd00777 189 DAR-AQAYDLVLNGVELGGGSIRIHDPDIQEKVFEILGLSEE----EAEEKFGFLLEAFKYGAPPHGGIALGLDRLVMLL 263
|
330
....*....|...
gi 1510971220 488 TNSPSIRDVLLFP 500
Cdd:cd00777 264 TGSESIRDVIAFP 276
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
46-500 |
1.27e-30 |
|
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: 125.50 E-value: 1.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 46 THHAADIVKAFGDKTkeeleaeenvVTIAGRLMAKRAMGKASFAQLLDRSGQIQIYVRQDTiGDEAHKVFDisdigDL-- 123
Cdd:COG0173 4 THYCGELRESDVGQE----------VTLSGWVHRRRDHGGLIFIDLRDRYGITQVVFDPDD-SAEAFEKAE-----KLrs 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 124 ---IGIRGVVF---------KTKTGELSVKAKDFTYLSKSlRPLPEKYHGLKDI--ETRYRKRYVDLiVNPEVRDTFITR 189
Cdd:COG0173 68 eyvIAVTGKVRarpegtvnpKLPTGEIEVLASELEILNKA-KTPPFQIDDDTDVseELRLKYRYLDL-RRPEMQKNLILR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 190 SRILTSMRRYLDSLGYLEVETPTLhaiagGAS----ARPFI----THHN---ALDM--QLYmriaielhlKRLI-VGGLE 255
Cdd:COG0173 146 HKVTKAIRNYLDENGFLEIETPIL-----TKStpegARDYLvpsrVHPGkfyALPQspQLF---------KQLLmVSGFD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 256 KVYEIGRVYRNEgiSTRHN--PEFTMIELYEAYADYQDIMTLTEELIAHIAQEVLGttkieyqgneIDLTPKWRR----- 328
Cdd:COG0173 212 RYFQIARCFRDE--DLRADrqPEFTQLDIEMSFVDQEDVFELMEGLIRHLFKEVLG----------VELPTPFPRmtyae 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 329 ---------------VHMVDLIKENLGVDF--WKEMSD---------------------DEARALAKEHG------VAVE 364
Cdd:COG0173 280 amerygsdkpdlrfgLELVDVTDIFKDSGFkvFAGAAEnggrvkainvpggaslsrkqiDELTEFAKQYGakglayIKVN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 365 PHHTFGHVVNeFFEQKLEHTLIQPT---------FVYGHPVAISP--------LAKKN---DEDP-RF---TDrFELF-- 418
Cdd:COG0173 360 EDGLKSPIAK-FLSEEELAAILERLgakpgdlifFVADKPKVVNKalgalrlkLGKELgliDEDEfAFlwvVD-FPLFey 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 419 ------IVArEHaNAFT---------ELNDPIDQRER------------------FEAQLLEK---AAGNDEAhEMDDDF 462
Cdd:COG0173 438 deeegrWVA-MH-HPFTmpkdedldlLETDPGKVRAKaydlvlngyelgggsiriHDPELQEKvfeLLGISEE-EAEEKF 514
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1510971220 463 ---IEALEYGMPPTGGLGIGIDRLVMLLTNSPSIRDVLLFP 500
Cdd:COG0173 515 gflLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
61-506 |
3.99e-26 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 111.72 E-value: 3.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 61 KEELEAEEnvVTIAGRLMAKRAMGKASFAQLLDRSGQIQIYVRQDTIGDEAHKVFDISDIG--DLIGIRGVV------FK 132
Cdd:PLN02850 76 GEELAGSE--VLIRGRVHTIRGKGKSAFLVLRQSGFTVQCVVFVSEVTVSKGMVKYAKQLSreSVVDVEGVVsvpkkpVK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 133 TKTGELSVKAKDFTYLSKSLRPLP-----------EKYHGLKD--------IETRYRKRYVDLIVnPEVRDTFITRSRIL 193
Cdd:PLN02850 154 GTTQQVEIQVRKIYCVSKALATLPfnvedaarsesEIEKALQTgeqlvrvgQDTRLNNRVLDLRT-PANQAIFRIQSQVC 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 194 TSMRRYLDSLGYLEVETPTLHAIA--GGASArpFITHHN------ALDMQLYMRIAIElhlkrlivGGLEKVYEIGRVYR 265
Cdd:PLN02850 233 NLFREFLLSKGFVEIHTPKLIAGAseGGSAV--FRLDYKgqpaclAQSPQLHKQMAIC--------GDFRRVFEIGPVFR 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 266 NEGIST-RHNPEFTMIEL-YEAYADYQDIMTLTEELIAHI--------AQEvLGTTKIEYQGNEIDLTPKWRRVHMvdli 335
Cdd:PLN02850 303 AEDSFThRHLCEFTGLDLeMEIKEHYSEVLDVVDELFVAIfdglnercKKE-LEAIREQYPFEPLKYLPKTLRLTF---- 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 336 kenlgvdfwkemsdDEARALAKEHGVAVEP--------HHTFGHVVNE-----FFeqklehtliqptFVYGHPVAISPLA 402
Cdd:PLN02850 378 --------------AEGIQMLKEAGVEVDPlgdlntesERKLGQLVKEkygtdFY------------ILHRYPLAVRPFY 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 403 KKND-EDPRFTDRFELFIVAREHANAFTELNDPidqrerfeaQLLEKAAgndEAHEMD----DDFIEALEYGMPPTGGLG 477
Cdd:PLN02850 432 TMPCpDDPKYSNSFDVFIRGEEIISGAQRVHDP---------ELLEKRA---EECGIDvktiSTYIDSFRYGAPPHGGFG 499
|
490 500
....*....|....*....|....*....
gi 1510971220 478 IGIDRLVMLLTNSPSIRDVLLFPhmraRD 506
Cdd:PLN02850 500 VGLERVVMLFCGLNNIRKTSLFP----RD 524
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
71-500 |
8.94e-24 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 104.87 E-value: 8.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 71 VTIAGRLMAKRAMGKASFAQLLDRSGQIQIYVRQDTIgDEAHKVFDISDIGDLIGIRGVVF---------KTKTGELSVK 141
Cdd:PLN02903 75 VTLCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDEF-PEAHRTANRLRNEYVVAVEGTVRsrpqespnkKMKTGSVEVV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 142 AKDFTYLSKSLRPLP-------EKYHGLKDiETRYRKRYVDLiVNPEVRDTFITRSRILTSMRRYL-DSLGYLEVETPTL 213
Cdd:PLN02903 154 AESVDILNVVTKSLPflvttadEQKDSIKE-EVRLRYRVLDL-RRPQMNANLRLRHRVVKLIRRYLeDVHGFVEIETPIL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 214 haiaggasARPfiTHHNALDMQLYMRI----------AIELHLKRLIVGGLEKVYEIGRVYRNEGISTRHNPEFTMIELY 283
Cdd:PLN02903 232 --------SRS--TPEGARDYLVPSRVqpgtfyalpqSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEFTQLDME 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 284 EAYADYQDIMTLTEELIAHIAQEVLGttkieyqgneIDLTPKWRRV--------------------HMVDLIK------- 336
Cdd:PLN02903 302 LAFTPLEDMLKLNEDLIRQVFKEIKG----------VQLPNPFPRLtyaeamskygsdkpdlryglELVDVSDvfaessf 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 337 -------ENLGV---------------------DFWKE-----------------------------MSDDEARALAKEH 359
Cdd:PLN02903 372 kvfagalESGGVvkaicvpdgkkisnntalkkgDIYNEaiksgakglaflkvlddgelegikalvesLSPEQAEQLLAAC 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 360 GV--------AVEPHHTfghvVNEFFE---QKLEHT--LIQPTfvyGHP---VAISPLAKKNDEDPR-------FT---- 412
Cdd:PLN02903 452 GAgpgdlilfAAGPTSS----VNKTLDrlrQFIAKTldLIDPS---RHSilwVTDFPMFEWNEDEQRlealhhpFTapnp 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 413 DRFELFIVARehANAFTELNDPID-------------QRERFEAQLLEKAagndEAHEMDDDFIEALEYGMPPTGGLGIG 479
Cdd:PLN02903 525 EDMGDLSSAR--ALAYDMVYNGVEigggslriyrrdvQQKVLEAIGLSPE----EAESKFGYLLEALDMGAPPHGGIAYG 598
|
570 580
....*....|....*....|.
gi 1510971220 480 IDRLVMLLTNSPSIRDVLLFP 500
Cdd:PLN02903 599 LDRLVMLLAGAKSIRDVIAFP 619
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
71-504 |
5.98e-22 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 99.68 E-value: 5.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 71 VTIAGRLMAKRAMGKASFAQLLDRSGQIQIYVRQDTIGDEAHKVFDISDIGDLIGIRGVVFK---------TKTGELSVK 141
Cdd:PRK12820 21 VCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFSPEAAPADVYELAASLRAEFCVALQGEVQKrleetenphIETGDIEVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 142 AKDFTYLSKSLR---PLPEKY-----------HGLKDIETRYRkrYVDlIVNPEVRDTFITRSRILTSMRRYLDSLGYLE 207
Cdd:PRK12820 101 VRELSILAASEAlpfAISDKAmtagagsagadAVNEDLRLQYR--YLD-IRRPAMQDHLAKRHRIIKCARDFLDSRGFLE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 208 VETPTLhAIAGGASARPFITHHNALDMQLY-MRIAIELHLKRLIVGGLEKVYEIGRVYRNEGISTRHNPEFTMIELYEAY 286
Cdd:PRK12820 178 IETPIL-TKSTPEGARDYLVPSRIHPKEFYaLPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEFTQLDIEASF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 287 ADYQDIMTLTEELIAHI-------------------AQEVLGTTK--IEYQGNEIDLTPKWRRVHMvDLIKENL------ 339
Cdd:PRK12820 257 IDEEFIFELIEELTARMfaiggialprpfprmpyaeAMDTTGSDRpdLRFDLKFADATDIFENTRY-GIFKQILqrggri 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 340 -GVDFWKEMSDDEARALAKEHGVAVEPhhTFG----------------HVVNEFFEQKLE-------------------- 382
Cdd:PRK12820 336 kGINIKGQSEKLSKNVLQNEYAKEIAP--SFGakgmtwmraeaggldsNIVQFFSADEKEalkrrfhaedgdviimiada 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 383 -HTLIQ-----------------PTFVYgHPVAIS--PLAKKNDED-------PrFT--DR------------------F 415
Cdd:PRK12820 414 sCAIVLsalgqlrlhladrlgliPEGVF-HPLWITdfPLFEATDDGgvtsshhP-FTapDRedfdpgdieelldlrsraY 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 416 ELFIVAREHANAFTELNDPIDQRERFEAQLLEKaagndeaHEMDDD---FIEALEYGMPPTGGLGIGIDRLVMLLTNSPS 492
Cdd:PRK12820 492 DLVVNGEELGGGSIRINDKDIQLRIFAALGLSE-------EDIEDKfgfFLRAFDFAAPPHGGIALGLDRVVSMILQTPS 564
|
570
....*....|..
gi 1510971220 493 IRDVLLFPHMRA 504
Cdd:PRK12820 565 IREVIAFPKNRS 576
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
42-500 |
3.66e-20 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 93.52 E-value: 3.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 42 KFEQTHHAADIV--KAFGDKTKEEL------EAEENVVTIAGRLMAKRAMGKASFAQLLDRSGQIQIYVRQDtiGDEAHK 113
Cdd:PTZ00401 44 KYKDVFGAAPMVqsTTYKSRTFIPVavlskpELVDKTVLIRARVSTTRKKGKMAFMVLRDGSDSVQAMAAVE--GDVPKE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 114 VFD---------ISDI-GDLIGIRGVVFKTKTGELSVKAKDFTYLSKSLRPLP---------EKYHGLK-DIETRYRKRY 173
Cdd:PTZ00401 122 MIDfigqiptesIVDVeATVCKVEQPITSTSHSDIELKVKKIHTVTESLRTLPftledasrkESDEGAKvNFDTRLNSRW 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 174 VDLiVNPEVRDTFITRSRILTSMRRYLDSLGYLEVETPTLHAIAGGASARPF-ITHHN-----ALDMQLYMRIAIElhlk 247
Cdd:PTZ00401 202 MDL-RTPASGAIFRLQSRVCQYFRQFLIDSDFCEIHSPKIINAPSEGGANVFkLEYFNrfaylAQSPQLYKQMVLQ---- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 248 rlivGGLEKVYEIGRVYRNEGIST-RHNPEFTMIELyEAYAD--YQDIMTLTEELIAHIAQEVLGTTK------IEYQGN 318
Cdd:PTZ00401 277 ----GDVPRVFEVGPVFRSENSNThRHLTEFVGLDV-EMRINehYYEVLDLAESLFNYIFERLATHTKelkavcQQYPFE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 319 EI--DLTPKWRRVHMVDLIKENL-GVDFWK-EMSDDEARALAKEHGVAVEphhtfghVVNEFFEQKLEHT---------- 384
Cdd:PTZ00401 352 PLvwKLTPERMKELGVGVISEGVePTDKYQaRVHNMDSRMLRINYMHCIE-------LLNTVLEEKMAPTddinttnekl 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 385 ---LIQPTfvYG--------HPVAISP---LAKKNDEdpRFTDRFELFIVAREHANAFTELNDPidqrerfeAQLLEKAA 450
Cdd:PTZ00401 425 lgkLVKER--YGtdffisdrFPSSARPfytMECKDDE--RFTNSYDMFIRGEEISSGAQRIHDP--------DLLLARAK 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1510971220 451 GNDEAHEMDDDFIEALEYGMPPTGGLGIGIDRLVMLLTNSPSIRDVLLFP 500
Cdd:PTZ00401 493 MLNVDLTPIKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFP 542
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
168-500 |
3.69e-19 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 88.54 E-value: 3.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 168 RYRKRYVDL-------IVNPEVRDTFITRSRILTSMRRYLDSLGYLEVETPTLHAI----AGGASARP-FITHHNALDMQ 235
Cdd:PRK06462 5 RYPKEYEEFlrmswkhISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIISPStdplMGLGSDLPvKQISIDFYGVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 236 LYMRIAIELHlKRLIVGGLEKVYEIGRVYRNEG---ISTRHNPEFTMIELYEAYADYQDIMTLTEELIAHIAQEVLGTTK 312
Cdd:PRK06462 85 YYLADSMILH-KQLALRMLGKIFYLSPNFRLEPvdkDTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 313 --IEYQGNEidlTPKWRRvhmvdlikenlgvDFwKEMSDDEARALAKEHGVAVEPHHTFGHVvnefFEQKLEHTLIQPTF 390
Cdd:PRK06462 164 deLEFFGRD---LPHLKR-------------PF-KRITHKEAVEILNEEGCRGIDLEELGSE----GEKSLSEHFEEPFW 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 391 VYGHPVAISPLAKKNDED-PRFTDRFELFIVARehanaFTELndpIDQRER-FE-AQLLE--KAAGNDEAHEmdDDFIEA 465
Cdd:PRK06462 223 IIDIPKGSREFYDREDPErPGVLRNYDLLLPEG-----YGEA---VSGGEReYEyEEIVEriREHGVDPEKY--KWYLEM 292
|
330 340 350
....*....|....*....|....*....|....*
gi 1510971220 466 LEYGMPPTGGLGIGIDRLVMLLTNSPSIRDVLLFP 500
Cdd:PRK06462 293 AKEGPLPSAGFGIGVERLTRYICGLRHIREVQPFP 327
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
71-505 |
2.88e-18 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 87.09 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 71 VTIAGRLMAKRAMGKASFAQLLDRSGQIQIYVrqdtIGDEAHKVFDISD---IGDLIGIRGVVFKT--KTGELSVKAKDF 145
Cdd:PRK03932 19 VTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQV----VKDNGEEYFEEIKkltTGSSVIVTGTVVESprAGQGYELQATKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 146 TYLSKSLR--PLPEKYHG---LKDIetRY-RKRyvdlivNPEVRDTFITRSRILTSMRRYLDSLGYLEVETPTLHAIAGG 219
Cdd:PRK03932 95 EVIGEDPEdyPIQKKRHSiefLREI--AHlRPR------TNKFGAVMRIRNTLAQAIHEFFNENGFVWVDTPIITASDCE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 220 ASARPFITHHNALDM---------------QLYMRIAIElhlkrlivgGLEKVYEIGRVYRNEGIST-RHNPEFTMIELY 283
Cdd:PRK03932 167 GAGELFRVTTLDLDFskdffgkeayltvsgQLYAEAYAM---------ALGKVYTFGPTFRAENSNTrRHLAEFWMIEPE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 284 EAYADYQDIMTLTEELIAHIAQEVLgttkiEYQGNEIDLTPKWRRVHMVDLIKENLGVDFwKEMSDDEARALAKEHGVAV 363
Cdd:PRK03932 238 MAFADLEDNMDLAEEMLKYVVKYVL-----ENCPDDLEFLNRRVDKGDIERLENFIESPF-PRITYTEAIEILQKSGKKF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 364 E-----------PHHTFghVVNEFFEqklehtliQPTFVYGHPVAISPLAKKNDEDPRftdrfelfIVArehanAFteln 432
Cdd:PRK03932 312 EfpvewgddlgsEHERY--LAEEHFK--------KPVFVTNYPKDIKAFYMRLNPDGK--------TVA-----AM---- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 433 dpiD-------------QRE-RFEaQLLEKAagndEAHEMDddfIEALE-------YGMPPTGGLGIGIDRLVMLLTNSP 491
Cdd:PRK03932 365 ---DllapgigeiiggsQREeRLD-VLEARI----KELGLN---KEDYWwyldlrrYGSVPHSGFGLGFERLVAYITGLD 433
|
490
....*....|....
gi 1510971220 492 SIRDVLLFPHMRAR 505
Cdd:PRK03932 434 NIRDVIPFPRTPGR 447
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
71-150 |
5.53e-16 |
|
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: 72.98 E-value: 5.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 71 VTIAGRLMAKRAMGKASFAQLLDRSGQIQIYVRQDTiGDEAHKVFDISDIGDLIGIRGVVFKT-----KTGELSVKAKDF 145
Cdd:cd04100 2 VTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEE-LGEFFEEAEKLRTESVVGVTGTVVKRpegnlATGEIELQAEEL 80
|
....*
gi 1510971220 146 TYLSK 150
Cdd:cd04100 81 EVLSK 85
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
188-400 |
4.14e-15 |
|
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: 74.08 E-value: 4.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 188 TRSRILTSMRRYLDSLGYLEVETPTLHAIAGGASAR----PFITHHNALDMQLYMRIAIELHLKRLIVGGL----EKVYE 259
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGhepkDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIrklpLRLAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 260 IGRVYRNEGIS--TRHNPEFTMIELYEAYADYQDI------MTLTEELIAHIAQEVLGTTKIEYQGnEIDLTPKWRrvhm 331
Cdd:cd00768 81 IGPAFRNEGGRrgLRRVREFTQLEGEVFGEDGEEAsefeelIELTEELLRALGIKLDIVFVEKTPG-EFSPGGAGP---- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1510971220 332 vdlikenlGVDFWKEMSDDEARALakehgvavephhTFGHVVNEFFEQKLEHTLIQPTFVYGHPVAISP 400
Cdd:cd00768 156 --------GFEIEVDHPEGRGLEI------------GSGGYRQDEQARAADLYFLDEALEYRYPPTIGF 204
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
71-146 |
3.80e-14 |
|
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic acids. The family includes the anti-codon binding domain of lysyl, aspartyl, and asparaginyl -tRNA synthetases (See pfam00152). Aminoacyl-tRNA synthetases catalyze the addition of an amino acid to the appropriate tRNA molecule EC:6.1.1.-. This family also includes part of RecG helicase involved in DNA repair. Replication factor A is a hetero-trimeric complex, that contains a subunit in this family. This domain is also found at the C-terminus of bacterial DNA polymerase III alpha chain.
Pssm-ID: 460164 [Multi-domain] Cd Length: 75 Bit Score: 67.26 E-value: 3.80e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1510971220 71 VTIAGRLMAK-RAMGKASFAQLLDRSGQIQIYVRqdtiGDEAHKVFDISDIGDLIGIRGVVFKTKTGELSVKAKDFT 146
Cdd:pfam01336 1 VTVAGRVTSIrRSGGKLLFLTLRDGTGSIQVVVF----KEEAEKLAKKLKEGDVVRVTGKVKKRKGGELELVVEEIE 73
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
235-500 |
3.11e-10 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 62.35 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 235 QLYMRIAIELHLKRLiVGGLEKVYEIGRVYRNEGIST-RHNPEFTMIELYEAYADYQDIMTLTEELIAHIAQEVLGTT-- 311
Cdd:PTZ00425 325 QAFLTVSGQLSLENL-CSSMGDVYTFGPTFRAENSHTsRHLAEFWMIEPEIAFADLYDNMELAESYIKYCIGYVLNNNfd 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 312 KIEY--QGNEIDLTPKWRRVHMVDLIKENL--GVDFWKEMSDdeARALAKEHGVAVEPHHtfghvvNEFFEQKLehtLIQ 387
Cdd:PTZ00425 404 DIYYfeENVETGLISRLKNILDEDFAKITYtnVIDLLQPYSD--SFEVPVKWGMDLQSEH------ERFVAEQI---FKK 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 388 PTFVYGHPVAISPLAKKNDEDPRFTDRFELFIVAREHANAFTELNDPIdqrERFEAQLLEKAAgNDEAHEMdddFIEALE 467
Cdd:PTZ00425 473 PVIVYNYPKDLKAFYMKLNEDQKTVAAMDVLVPKIGEVIGGSQREDNL---ERLDKMIKEKKL-NMESYWW---YRQLRK 545
|
250 260 270
....*....|....*....|....*....|...
gi 1510971220 468 YGMPPTGGLGIGIDRLVMLLTNSPSIRDVLLFP 500
Cdd:PTZ00425 546 FGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFP 578
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
67-176 |
1.58e-09 |
|
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: 55.99 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 67 EENV---VTIAGRLMAKRAMGKASFAQLLDRSGQIQIYVRQDTigDEAHKVFDisdigDL-----IGIRGVVF------- 131
Cdd:cd04317 10 ESHVgqeVTLCGWVQRRRDHGGLIFIDLRDRYGIVQVVFDPEE--APEFELAE-----KLrnesvIQVTGKVRarpegtv 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1510971220 132 --KTKTGELSVKAKDFTYLSKSLR-PLPEKYHGLKDIETRYRKRYVDL 176
Cdd:cd04317 83 npKLPTGEIEVVASELEVLNKAKTlPFEIDDDVNVSEELRLKYRYLDL 130
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
235-505 |
1.27e-08 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 57.57 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 235 QLYMRIAIELHLKRLiVGGLEKVYEIGRVYRNEGI-STRHNPEFTMIELYEAYADYQDIMTLTEELIAHIAQEVLG--TT 311
Cdd:PLN02532 371 PTYLTVSGRLHLESY-ACALGNVYTFGPRFRADRIdSARHLAEMWMVEVEMAFSELEDAMNCAEDYFKFLCKWVLEncSE 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 312 KIEYQGNEIDLTPKWRRVHMV----DLIKENLGVDFWKEMSDDEARaLAKEHGVAVEPHHtFGHVVNEFFEqklehtliQ 387
Cdd:PLN02532 450 DMKFVSKRIDKTISTRLEAIIssslQRISYTEAVDLLKQATDKKFE-TKPEWGIALTTEH-LSYLADEIYK--------K 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 388 PTFVYGHPVAISPLAKKNDEDPRFTDRFEL-------FIVAREHANAFTELNDPID----QRERFEAqllekaagndeah 456
Cdd:PLN02532 520 PVIIYNYPKELKPFYVRLNDDGKTVAAFDLvvpkvgtVITGSQNEERMDILNARIEelglPREQYEW------------- 586
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1510971220 457 emdddFIEALEYGMPPTGGLGIGIDRLVMLLTNSPSIRDVLLFPHMRAR 505
Cdd:PLN02532 587 -----YLDLRRHGTVKHSGFSLGFELMVLFATGLPDVRDAIPFPRSWGK 630
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
254-500 |
1.35e-08 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 57.31 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 254 LEKVYEIGRVYRNEGIST-RHNPEFTMIELYEAYADYQDIMTLTEELIAHIAQEVLgttkiEYQGNEIDLTPK------W 326
Cdd:PLN02221 326 LSSVYTFGPTFRAENSHTsRHLAEFWMVEPEIAFADLEDDMNCAEAYVKYMCKWLL-----DKCFDDMELMAKnfdsgcI 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 327 RRVHMVDliKENLGVDFWKEMSD--DEARALAKEHGVAVEphhtFGHVVNEFFEQKLEHTLIQ-PTFVYGHPVAISPLAK 403
Cdd:PLN02221 401 DRLRMVA--STPFGRITYTEAIEllEEAVAKGKEFDNNVE----WGIDLASEHERYLTEVLFQkPLIVYNYPKGIKAFYM 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 404 KNDEDPRFTDRFELFIvarehaNAFTELNDPIDQRERFEA--QLLEKAAGNDEAHEMdddFIEALEYGMPPTGGLGIGID 481
Cdd:PLN02221 475 RLNDDEKTVAAMDVLV------PKVGELIGGSQREERYDVikQRIEEMGLPIEPYEW---YLDLRRYGTVKHCGFGLGFE 545
|
250
....*....|....*....
gi 1510971220 482 RLVMLLTNSPSIRDVLLFP 500
Cdd:PLN02221 546 RMILFATGIDNIRDVIPFP 564
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
47-156 |
1.51e-05 |
|
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the homodimeric non-discriminating (ND) Pyrococcus kodakaraensis aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. P. kodakaraensis AspRS is a class 2b aaRS. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation 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. P. kodakaraensis ND-AspRS can charge both tRNAAsp and tRNAAsn. Some of the enzymes in this group may be discriminating, based on the presence of homologs of asparaginyl-tRNA synthetase (AsnRS) in their completed genomes.
Pssm-ID: 239811 [Multi-domain] Cd Length: 108 Bit Score: 43.84 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971220 47 HHAADIvkafgdktKEELEAEEnvVTIAGRLMAKRAMGKASFAQLLDRSGQIQIYVRQDTIGDEAHKVFDISDIGDLIGI 126
Cdd:cd04316 1 HYSAEI--------TPELDGEE--VTVAGWVHEIRDLGGIKFVILRDREGIVQVTAPKKKVDKELFKTVRKLSRESVISV 70
|
90 100 110
....*....|....*....|....*....|...
gi 1510971220 127 RGVVF---KTKTGeLSVKAKDFTYLSKSLRPLP 156
Cdd:cd04316 71 TGTVKaepKAPNG-VEIIPEEIEVLSEAKTPLP 102
|
|
| |
