|
Name |
Accession |
Description |
Interval |
E-value |
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
4-494 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 986.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 4 EELNDQFLVRREKMSNLRDQGIDPFGQRFERTHTSQQLISEYDELTKEQLEENEVPVSLAGRIMTKRGKGKAGFAHVQDL 83
Cdd:PRK00484 1 EELNEQIAVRREKLAELREQGIDPYPNKFERTHTAAELRAKYDDKEKEELEELEIEVSVAGRVMLKRVMGKASFATLQDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 84 TGQIQLYVRKDAIGEEQYEIFSSVDIGDLVGVEGVLFKTKVGELSIKVKDFTLLTKALRPLPDKYHGLKDIEQRYRQRYL 163
Cdd:PRK00484 81 SGRIQLYVSKDDVGEEALEAFKKLDLGDIIGVEGTLFKTKTGELSVKATELTLLTKSLRPLPDKFHGLTDVETRYRQRYV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 164 DLITNPESKQTFISRSRIIQSMRRYLDNHGYLEVETPMMHSIAGGAAARPFVTHHNALDMELYMRIAIELHLKRLIVGGL 243
Cdd:PRK00484 161 DLIVNPESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARPFITHHNALDIDLYLRIAPELYLKRLIVGGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 244 EKVYEIGRVFRNEGVSTRHNPEFTMIELYEAYADYKDIMALTENLIAHIAQEVLGTTKIQYGDQEVDLTPEWTRLHMVDA 323
Cdd:PRK00484 241 ERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTYQGTEIDFGPPFKRLTMVDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 324 IKQYTGVDFWgETSVEEARALAKEHGVEITEHMQYGHIVNEFFEQKVEEQLIQPTFIYGHPVEISPLAKKNAEDPRFTDR 403
Cdd:PRK00484 321 IKEYTGVDFD-DMTDEEARALAKELGIEVEKSWGLGKLINELFEEFVEPKLIQPTFITDYPVEISPLAKRHREDPGLTER 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 404 FELFIVAREHANAFTELNDPIDQRERFEAQLKEKEQGNDEAHEMDDDFIEALEYGMPPTGGLGIGIDRLVMLLTNAPSIR 483
Cdd:PRK00484 400 FELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIR 479
|
490
....*....|.
gi 502819918 484 DVLLFPHMRQR 494
Cdd:PRK00484 480 DVILFPLMRPE 490
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
1-492 |
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: 977.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 1 MS-HEELNDQFLVRREKMSNLRDQGIDPFGQRFERTHTSQQLISEYDELTKEqlEENEVPVSLAGRIMTKRGKGKAGFAH 79
Cdd:COG1190 1 MSeEEDLNEQIRVRREKLEELREAGIDPYPNKFPRTHTAAEIREKYDELEAE--EETGDEVSVAGRIMAKRDMGKASFAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 80 VQDLTGQIQLYVRKDAIGEEQYEIFSSVDIGDLVGVEGVLFKTKVGELSIKVKDFTLLTKALRPLPDKYHGLKDIEQRYR 159
Cdd:COG1190 79 LQDGSGRIQLYLRRDELGEEAYELFKLLDLGDIVGVEGTVFRTKTGELSVKVEELTLLSKSLRPLPEKFHGLTDPETRYR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 160 QRYLDLITNPESKQTFISRSRIIQSMRRYLDNHGYLEVETPMMHSIAGGAAARPFVTHHNALDMELYMRIAIELHLKRLI 239
Cdd:COG1190 159 QRYVDLIVNPEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 240 VGGLEKVYEIGRVFRNEGVSTRHNPEFTMIELYEAYADYKDIMALTENLIAHIAQEVLGTTKIQYGDQEVDLTPEWTRLH 319
Cdd:COG1190 239 VGGFERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGTTKVTYQGQEIDLSPPWRRIT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 320 MVDAIKQYTGVDFWGETSVEEARALAKEHGVEITEHMQYGHIVNEFFEQKVEEQLIQPTFIYGHPVEISPLAKKNAEDPR 399
Cdd:COG1190 319 MVEAIKEATGIDVTPLTDDEELRALAKELGIEVDPGWGRGKLIDELFEELVEPKLIQPTFVTDYPVEVSPLAKRHRDDPG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 400 FTDRFELFIVAREHANAFTELNDPIDQRERFEAQLKEKEQGNDEAHEMDDDFIEALEYGMPPTGGLGIGIDRLVMLLTNA 479
Cdd:COG1190 399 LTERFELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDS 478
|
490
....*....|...
gi 502819918 480 PSIRDVLLFPHMR 492
Cdd:COG1190 479 PSIRDVILFPLMR 491
|
|
| lysS_bact |
TIGR00499 |
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ... |
5-492 |
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: 792.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 5 ELNDQFLVRREKMSNLRDQGIDPFGQRFERTHTSQQLISEYDELTKEQLEENEVPVSLAGRIMTKRGKGKAGFAHVQDLT 84
Cdd:TIGR00499 1 ELNDQAQQRLEKLNRLRQTGNNPYLHKFERTHSAQEFQEKYADLSNEELKEKELKVSIAGRIKAIRSMGKATFITLQDES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 85 GQIQLYVRKDAIGEEQYEIFSSV-DIGDLVGVEGVLFKTKVGELSIKVKDFTLLTKALRPLPDKYHGLKDIEQRYRQRYL 163
Cdd:TIGR00499 81 GQIQLYVNKNKLPEDFYEFDEYLlDLGDIIGVTGYPFKTKTGELSVKVTELQILTKCLQPLPDKWHGLTDQETRYRQRYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 164 DLITNPESKQTFISRSRIIQSMRRYLDNHGYLEVETPMMHSIAGGAAARPFVTHHNALDMELYMRIAIELHLKRLIVGGL 243
Cdd:TIGR00499 161 DLIVNPDVRQTFLKRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKPFITHHNALDMDLYLRIAPELYLKRLIVGGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 244 EKVYEIGRVFRNEGVSTRHNPEFTMIELYEAYADYKDIMALTENLIAHIAQEVLGTTKIQYGDQEVDLTPEWTRLHMVDA 323
Cdd:TIGR00499 241 EKVYEIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTFIINYNDLEIDLKPPWKRITMVDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 324 IKQYTGVDFWGETSVEEARALAKEHGVEITEH-MQYGHIVNEFFEQKVEEQLIQPTFIYGHPVEISPLAKKNAEDPRFTD 402
Cdd:TIGR00499 321 LEMVTGIDFDILKDDETAKALAKEHGIEVAEDsLTLGHILNKFFEQFLEHTLIQPTFITHYPAEISPLAKRDPSNPEFTE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 403 RFELFIVAREHANAFTELNDPIDQRERFEAQLKEKEQGNDEAHEMDDDFIEALEYGMPPTGGLGIGIDRLVMLLTNAPSI 482
Cdd:TIGR00499 401 RFELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGIGIDRLVMLLTDAPSI 480
|
490
....*....|
gi 502819918 483 RDVLLFPHMR 492
Cdd:TIGR00499 481 RDVLLFPQLR 490
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
12-492 |
0e+00 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 702.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 12 VRREKMSNLRDQGIDPFGQRFERTHTSQQLISEYDELTKEQLEENEVpVSLAGRIMTKRGKGKAGFAHVQDLTGQIQLYV 91
Cdd:PLN02502 64 NRLKKVEALRAKGVEPYPYKFDVTHTAPELQEKYGSLENGEELEDVS-VSVAGRIMAKRAFGKLAFYDLRDDGGKIQLYA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 92 RKDAIGEEQYE---IFSSVDIGDLVGVEGVLFKTKVGELSIKVKDFTLLTKALRPLPDKYHGLKDIEQRYRQRYLDLITN 168
Cdd:PLN02502 143 DKKRLDLDEEEfekLHSLVDRGDIVGVTGTPGKTKKGELSIFPTSFEVLTKCLLMLPDKYHGLTDQETRYRQRYLDLIAN 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 169 PESKQTFISRSRIIQSMRRYLDNHGYLEVETPMMHSIAGGAAARPFVTHHNALDMELYMRIAIELHLKRLIVGGLEKVYE 248
Cdd:PLN02502 223 PEVRDIFRTRAKIISYIRRFLDDRGFLEVETPMLNMIAGGAAARPFVTHHNDLNMDLYLRIATELHLKRLVVGGFERVYE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 249 IGRVFRNEGVSTRHNPEFTMIELYEAYADYKDIMALTENLIAHIAQEVLGTTKIQYGDQEVDLTPEWTRLHMVDAIKQYT 328
Cdd:PLN02502 303 IGRQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKELTGSYKIKYHGIEIDFTPPFRRISMISLVEEAT 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 329 GVDFWGETSVEEARALAKE----HGVEITEHMQYGHIVNEFFEQKVEEQLIQPTFIYGHPVEISPLAKKNAEDPRFTDRF 404
Cdd:PLN02502 383 GIDFPADLKSDEANAYLIAacekFDVKCPPPQTTGRLLNELFEEFLEETLVQPTFVLDHPVEMSPLAKPHRSKPGLTERF 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 405 ELFIVAREHANAFTELNDPIDQRERFEAQLKEKEQGNDEAHEMDDDFIEALEYGMPPTGGLGIGIDRLVMLLTNAPSIRD 484
Cdd:PLN02502 463 ELFINGRELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRLVMLLTDSASIRD 542
|
....*...
gi 502819918 485 VLLFPHMR 492
Cdd:PLN02502 543 VIAFPAMK 550
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
168-493 |
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: 589.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 168 NPESKQTFISRSRIIQSMRRYLDNHGYLEVETPMMHSIAGGAAARPFVTHHNALDMELYMRIAIELHLKRLIVGGLEKVY 247
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 248 EIGRVFRNEGVSTRHNPEFTMIELYEAYADYKDIMALTENLIAHIAQEVLGTTKIQYGDQEVDLTPEWTRLHMVDAIKQY 327
Cdd:cd00775 81 EIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIEYGGKELDFTPPFKRVTMVDALKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 328 TGVDFWGET---SVEEARALAKEHGVEITEHMQYGHIVNEFFEQKVEEQLIQPTFIYGHPVEISPLAKKNAEDPRFTDRF 404
Cdd:cd00775 161 TGIDFPELDleqPEELAKLLAKLIKEKIEKPRTLGKLLDKLFEEFVEPTLIQPTFIIDHPVEISPLAKRHRSNPGLTERF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 405 ELFIVAREHANAFTELNDPIDQRERFEAQLKEKEQGNDEAHEMDDDFIEALEYGMPPTGGLGIGIDRLVMLLTNAPSIRD 484
Cdd:cd00775 241 ELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLTDSNSIRD 320
|
....*....
gi 502819918 485 VLLFPHMRQ 493
Cdd:cd00775 321 VILFPAMRP 329
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
5-492 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 528.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 5 ELNDQFLVRREKMSNLRDQGIdPFGQRFERTHTSQQLISEYDELTKEQLEENEVPVSLAGRIMTKRGKGKAGFAHVQDLT 84
Cdd:PRK12445 14 DFNDELRNRREKLAALRQQGV-AFPNDFRRDHTSDQLHEEFDAKDNQELESLNIEVSVAGRMMTRRIMGKASFVTLQDVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 85 GQIQLYVRKDAIGEEQY-EIFSSVDIGDLVGVEGVLFKTKVGELSIKVKDFTLLTKALRPLPDKYHGLKDIEQRYRQRYL 163
Cdd:PRK12445 93 GRIQLYVARDSLPEGVYnDQFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFHGLQDQEVRYRQRYL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 164 DLITNPESKQTFISRSRIIQSMRRYLDNHGYLEVETPMMHSIAGGAAARPFVTHHNALDMELYMRIAIELHLKRLIVGGL 243
Cdd:PRK12445 173 DLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 244 EKVYEIGRVFRNEGVSTRHNPEFTMIELYEAYADYKDIMALTENLIAHIAQEVLGTTKIQYGDQEVDLTPEWTRLHMVDA 323
Cdd:PRK12445 253 ERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFDFGKPFEKLTMREA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 324 IKQY-TGVDFWGETSVEEARALAKEHGVEITEHMQYGHIVNEFFEQKVEEQLIQPTFIYGHPVEISPLAKKNAEDPRFTD 402
Cdd:PRK12445 333 IKKYrPETDMADLDNFDAAKALAESIGITVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEITD 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 403 RFELFIVAREHANAFTELNDPIDQRERFEAQLKEKEQGNDEAHEMDDDFIEALEYGMPPTGGLGIGIDRLVMLLTNAPSI 482
Cdd:PRK12445 413 RFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTI 492
|
490
....*....|
gi 502819918 483 RDVLLFPHMR 492
Cdd:PRK12445 493 RDVILFPAMR 502
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
6-494 |
1.47e-179 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 532.62 E-value: 1.47e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 6 LNDQFLVRREKMSNLRDQGIDPFGQRFERTHTSQQLIseyDELTKEQleenevpVSLAGRIMTKRGKGKAGFAHVQDLTG 85
Cdd:PRK02983 610 LPEQVRVRLAKLEALRAAGVDPYPVGVPPTHTVAEAL---DAPTGEE-------VSVSGRVLRIRDYGGVLFADLRDWSG 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 86 QIQLYVRKDAIGEEQYEIF-SSVDIGDLVGVEGVLFKTKVGELSIKVKDFTLLTKALRPLPDKYHGLKDIEQRYRQRYLD 164
Cdd:PRK02983 680 ELQVLLDASRLEQGSLADFrAAVDLGDLVEVTGTMGTSRNGTLSLLVTSWRLAGKCLRPLPDKWKGLTDPEARVRQRYLD 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 165 LITNPESKQTFISRSRIIQSMRRYLDNHGYLEVETPMMHSIAGGAAARPFVTHHNALDMELYMRIAIELHLKRLIVGGLE 244
Cdd:PRK02983 760 LAVNPEARDLLRARSAVVRAVRETLVARGFLEVETPILQQVHGGANARPFVTHINAYDMDLYLRIAPELYLKRLCVGGVE 839
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 245 KVYEIGRVFRNEGVSTRHNPEFTMIELYEAYADYKDIMALTENLIAHIAQEVLGTTKIQYGD-----QEVDLTPEWTRLH 319
Cdd:PRK02983 840 RVFELGRNFRNEGVDATHNPEFTLLEAYQAHADYDTMRDLTRELIQNAAQAAHGAPVVMRPDgdgvlEPVDISGPWPVVT 919
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 320 MVDAIKQYTGVDFWGETSVEEARALAKEHGVEITEHMQYGHIVNEFFEQKVEEQLIQPTFIYGHPVEISPLAKKNAEDPR 399
Cdd:PRK02983 920 VHDAVSEALGEEIDPDTPLAELRKLCDAAGIPYRTDWDAGAVVLELYEHLVEDRTTFPTFYTDFPTSVSPLTRPHRSDPG 999
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 400 FTDRFELFIVAREHANAFTELNDPIDQRERFEAQLKEKEQGNDEAHEMDDDFIEALEYGMPPTGGLGIGIDRLVMLLTNA 479
Cdd:PRK02983 1000 LAERWDLVAWGVELGTAYSELTDPVEQRRRLTEQSLLAAGGDPEAMELDEDFLQALEYAMPPTGGLGMGVDRLVMLLTGR 1079
|
490
....*....|....*
gi 502819918 480 pSIRDVLLFPHMRQR 494
Cdd:PRK02983 1080 -SIRETLPFPLVKPR 1093
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
13-492 |
1.12e-146 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 432.13 E-value: 1.12e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 13 RREKMSNLRDQGIDPFGQRFERTHTSQQLISEYDEL-TKEQLEENevPVSLAGRIMTKRGKGKAgfAHVQDLTG---QIQ 88
Cdd:PTZ00417 89 RSKFIQEQKAKGINPYPHKFERTITVPEFVEKYQDLaSGEHLEDT--ILNVTGRIMRVSASGQK--LRFFDLVGdgaKIQ 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 89 L---YVRKDAIGEEQYEIFSSVDIGDLVGVEGVLFKTKVGELSIKVKDFTLLTKALRPLPDKYhGLKDIEQRYRQRYLDL 165
Cdd:PTZ00417 165 VlanFAFHDHTKSNFAECYDKIRRGDIVGIVGFPGKSKKGELSIFPKETIILSPCLHMLPMKY-GLKDTEIRYRQRYLDL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 166 ITNPESKQTFISRSRIIQSMRRYLDNHGYLEVETPMMHSIAGGAAARPFVTHHNALDMELYMRIAIELHLKRLIVGGLEK 245
Cdd:PTZ00417 244 MINESTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLVAGGANARPFITHHNDLDLDLYLRIATELPLKMLIVGGIDK 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 246 VYEIGRVFRNEGVSTRHNPEFTMIELYEAYADYKDIMALTENLIAHIAQEVLGTTKIQYGDQ-------EVDLTPEWTRL 318
Cdd:PTZ00417 324 VYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHLFGTYKILYNKDgpekdpiEIDFTPPYPKV 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 319 HMVDAIKQYTGVD----FWGETSVEEARALAKEHGVEITEHMQYGHIVNEFFEQKVEEQLI-QPTFIYGHPVEISPLAKK 393
Cdd:PTZ00417 404 SIVEELEKLTNTKleqpFDSPETINKMINLIKENKIEMPNPPTAAKLLDQLASHFIENKYPnKPFFIIEHPQIMSPLAKY 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 394 NAEDPRFTDRFELFIVAREHANAFTELNDPIDQRERFEAQLKEKEQGNDEAHEMDDDFIEALEYGMPPTGGLGIGIDRLV 473
Cdd:PTZ00417 484 HRSKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCTSLEYGLPPTGGLGLGIDRIT 563
|
490
....*....|....*....
gi 502819918 474 MLLTNAPSIRDVLLFPHMR 492
Cdd:PTZ00417 564 MFLTNKNCIKDVILFPTMR 582
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
153-492 |
8.08e-127 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 371.90 E-value: 8.08e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 153 DIEQRYRQRYLDLiTNPESKQTFISRSRIIQSMRRYLDNHGYLEVETPMMHSIAGGAAARPFVTHHNALDMELYMRIAIE 232
Cdd:pfam00152 1 DEETRLKYRYLDL-RRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 233 LHLKRLIVGGLEKVYEIGRVFRNEGVSTRHNPEFTMIELYEAYADYKDIMALTENLIAHIAQEVLGTTKIQYGDQEVDLT 312
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 313 PEWTRLHMVDAIKQYTGVDfwgetsveearalAKEHGVEI-TEHMQYGhivnefFEQKVEEQLIQPTFIYGHPVEISPLA 391
Cdd:pfam00152 160 KPFPRITYAEAIEKLNGKD-------------VEELGYGSdKPDLRFL------LELVIDKNKFNPLWVTDFPAEHHPFT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 392 KKNAED-PRFTDRFELFIVAREHANAFTELNDPIDQRERFEAQLKEKEqgndEAHEMDDDFIEALEYGMPPTGGLGIGID 470
Cdd:pfam00152 221 MPKDEDdPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDPE----EAEEKFGFYLDALKYGAPPHGGLGIGLD 296
|
330 340
....*....|....*....|..
gi 502819918 471 RLVMLLTNAPSIRDVLLFPHMR 492
Cdd:pfam00152 297 RLVMLLTGLESIREVIAFPKTR 318
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
32-493 |
2.89e-122 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 372.06 E-value: 2.89e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 32 FERTHTSQQLISEYDELTKEQlEENEVPVSLAGRIMTKRGKGKAGFAHVQDLTGQIQL--YVRKDAIGEEQYEIFSSVDI 109
Cdd:PTZ00385 83 FRGITPISEVRERYGYLASGD-RAAQATVRVAGRVTSVRDIGKIIFVTIRSNGNELQVvgQVGEHFTREDLKKLKVSLRV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 110 GDLVGVEGVLFKTKVGELSIKVKDFTLLT------KALRPLPDKYHGLKDIEQRYRQRYLDLITNPESKQTFISRSRIIQ 183
Cdd:PTZ00385 162 GDIIGADGVPCRMQRGELSVAASRMLILSpyvctdQVVCPNLRGFTVLQDNDVKYRYRFTDMMTNPCVIETIKKRHVMLQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 184 SMRRYLDNHGYLEVETPMMHSIAGGAAARPFVTHHNALDMELYMRIAIELHLKRLIVGGLEKVYEIGRVFRNEGVSTRHN 263
Cdd:PTZ00385 242 ALRDYFNERNFVEVETPVLHTVASGANAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHN 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 264 PEFTMIELYEAYADYKDIMALTENLIAHIAQEVLGTTKIQ------YGD-QEVDLTPEWTRLHMVDAIKQYTGVDFWGET 336
Cdd:PTZ00385 322 PEFTSCEFYAAYHTYEDLMPMTEDIFRQLAMRVNGTTVVQiypenaHGNpVTVDLGKPFRRVSVYDEIQRMSGVEFPPPN 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 337 SVEEARALAKEHGVEITEHMQYGHI--VNEFFEQKVE----EQLIQPTFIYGHPVEISPLAKKNAEDPRFTDRFELFIVA 410
Cdd:PTZ00385 402 ELNTPKGIAYMSVVMLRYNIPLPPVrtAAKMFEKLIDffitDRVVEPTFVMDHPLFMSPLAKEQVSRPGLAERFELFVNG 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 411 REHANAFTELNDPIDQRERFEAQLKEKEQGNDEAHEMDDDFIEALEYGMPPTGGLGIGIDRLVMLLTNAPSIRDVLLFPH 490
Cdd:PTZ00385 482 IEYCNAYSELNDPHEQYHRFQQQLVDRQGGDEEAMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFPL 561
|
...
gi 502819918 491 MRQ 493
Cdd:PTZ00385 562 LRQ 564
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
175-492 |
2.08e-102 |
|
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: 307.48 E-value: 2.08e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 175 FISRSRIIQSMRRYLDNHGYLEVETPMMHSIAGGAAARPFVTHHNALDMELYMRIAIELHLKRLIVGGLEKVYEIGRVFR 254
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 255 NEGVSTRHNPEFTMIELYEAYADYKDIMALTENLIAHIAQEVLGTTKIQYGDQEVDLTPEWTRLHMVDAIKQYTgvdfwg 334
Cdd:cd00669 81 NEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYGFELEDFGLPFPRLTYREALERYG------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 335 etsveearalakehgveitehmqyghivneffeqkveeqliQPTFIYGHPVEI-SPLAKKNAEDPRFTDRFELFIVAREH 413
Cdd:cd00669 155 -----------------------------------------QPLFLTDYPAEMhSPLASPHDVNPEIADAFDLFINGVEV 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502819918 414 ANAFTELNDPIDQRERFEAQLKEKEQGndeaHEMDDDFIEALEYGMPPTGGLGIGIDRLVMLLTNAPSIRDVLLFPHMR 492
Cdd:cd00669 194 GNGSSRLHDPDIQAEVFQEQGINKEAG----MEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKMR 268
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
178-486 |
3.67e-87 |
|
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: 270.05 E-value: 3.67e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 178 RSRIIQSMRRYLDNHGYLEVETPMMhSIAGGAAA--RPFVT---HHNALDMELYMRIAIELHLKRLIVGGLEKVYEIGRV 252
Cdd:COG2269 9 RARLLAAIRAFFAERGVLEVETPAL-SVAPGTDPhlDSFATefiGPDGGGRPLYLHTSPEFAMKRLLAAGSGPIYQIAKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 253 FRNEGVSTRHNPEFTMIELYEAYADYKDIMALTENLIAHIAQEVLgttkiqygdqevdlTPEWTRLHMVDAIKQYTGVDF 332
Cdd:COG2269 88 FRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAAG--------------FAPAERLSYQEAFLRYLGIDP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 333 WgETSVEEARALAKEHGVEITEHMQYGHIVNEFFEQKVEEQLIQ--PTFIYGHPVEISPLAKKNAEDPRFTDRFELFIVA 410
Cdd:COG2269 154 L-TADLDELAAAAAAAGLRVADDDDRDDLLDLLLSERVEPQLGRdrPTFLYDYPASQAALARISPDDPRVAERFELYACG 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502819918 411 REHANAFTELNDPIDQRERFEAQLKEKEQGNDEAHEMDDDFIEALEYGMPPTGGLGIGIDRLVMLLTNAPSIRDVL 486
Cdd:COG2269 233 VELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALGAERIDDVL 308
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
188-486 |
4.30e-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: 245.92 E-value: 4.30e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 188 YLDNHGYLEVETPMMhSIAGGAAA--RPFVTH---HNALDMELYMRIAIELHLKRLIVGGLEKVYEIGRVFRNEGVSTRH 262
Cdd:TIGR00462 1 FFAERGVLEVETPLL-SPAPVTDPhlDAFATEfvgPDGQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 263 NPEFTMIELYEAYADYKDIMALTENLIAHIAQevlgttkiqygdqevDLTPEWTRLHMVDAIKQYTGVDFWgETSVEEAR 342
Cdd:TIGR00462 80 NPEFTMLEWYRPGFDYHDLMDEVEALLQELLG---------------DPFAPAERLSYQEAFLRYAGIDPL-TASLAELQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 343 ALAKEHGVEITEHMQYGHIVNEFFEQKVEEQLIQ--PTFIYGHPVEISPLAKKNAEDPRFTDRFELFIVAREHANAFTEL 420
Cdd:TIGR00462 144 AAAAAHGIRASEEDDRDDLLDLLFSEKVEPHLGFgrPTFLYDYPASQAALARISPDDPRVAERFELYIKGLELANGFHEL 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502819918 421 NDPIDQRERFEAQLKEKEQGNDEAHEMDDDFIEALEYGMPPTGGLGIGIDRLVMLLTNAPSIRDVL 486
Cdd:TIGR00462 224 TDAAEQRRRFEADNALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDVL 289
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
171-485 |
1.92e-63 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 208.63 E-value: 1.92e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 171 SKQTFISRSRIIQSMRRYLDNHGYLEVETPMM-HSIAGGAAARPFVTHHNALDME----LYMRIAIELHLKRLIVGGLEK 245
Cdd:PRK09350 1 SIPNLLKRAKIIAEIRRFFADRGVLEVETPILsQATVTDIHLVPFETRFVGPGASqgktLWLMTSPEYHMKRLLAAGSGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 246 VYEIGRVFRNEGVSTRHNPEFTMIELYEAYADYKDIMALTENLIahiaqevlgttkiqygdQEVDLTPEWTRLHMVDAIK 325
Cdd:PRK09350 81 IFQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLL-----------------QQVLDCEPAESLSYQQAFL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 326 QYTGVDFWgETSVEEARALAKEHGveitehmqYGHIVNE----------FFEQKVEEQLIQ--PTFIYGHPVEISPLAKK 393
Cdd:PRK09350 144 RYLGIDPL-SADKTQLREVAAKLG--------LSNIADEeedrdtllqlLFTFGVEPNIGKekPTFVYHFPASQAALAKI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 394 NAEDPRFTDRFELFIVAREHANAFTELNDPIDQRERFEAQLKEKEQGNDEAHEMDDDFIEALEYGMPPTGGLGIGIDRLV 473
Cdd:PRK09350 215 STEDHRVAERFEVYFKGIELANGFHELTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCSGVALGVDRLI 294
|
330
....*....|..
gi 502819918 474 MLLTNAPSIRDV 485
Cdd:PRK09350 295 MLALGAESISEV 306
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
60-165 |
4.59e-59 |
|
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: 190.00 E-value: 4.59e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 60 VSLAGRIMTKRGKGKAGFAHVQDLTGQIQLYVRKDAIGEEQYEIFSS-VDIGDLVGVEGVLFKTKVGELSIKVKDFTLLT 138
Cdd:cd04322 2 VSVAGRIMSKRGSGKLSFADLQDESGKIQVYVNKDDLGEEEFEDFKKlLDLGDIIGVTGTPFKTKTGELSIFVKEFTLLS 81
|
90 100
....*....|....*....|....*..
gi 502819918 139 KALRPLPDKYHGLKDIEQRYRQRYLDL 165
Cdd:cd04322 82 KSLRPLPEKFHGLTDVETRYRQRYLDL 108
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
47-494 |
1.28e-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: 1.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 47 ELTKEQLEENevpVSLAGRIMTKRGKGKAGFAHVQDLTGQIQLYVRKDAIgeEQYEIFSSVDIGDLVGVEGVLFKT--KV 124
Cdd:COG0017 7 DLLPEHVGQE---VTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKL--ENFEEAKKLTTESSVEVTGTVVESprAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 125 GELSIKVKDFTLLTKALRPLP-DKY-HGLkdiEQRYRQRYLDLITNpesKQTFIS--RSRIIQSMRRYLDNHGYLEVETP 200
Cdd:COG0017 82 QGVELQAEEIEVLGEADEPYPlQPKrHSL---EFLLDNRHLRLRTN---RFGAIFriRSELARAIREFFQERGFVEVHTP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 201 MM-HSIAGGAAA--------RP-FVTHHNALDMELYMriaielhlkrlivGGLEKVYEIGRVFRNEGVST-RHNPEFTMI 269
Cdd:COG0017 156 IItASATEGGGElfpvdyfgKEaYLTQSGQLYKEALA-------------MALEKVYTFGPTFRAEKSNTrRHLAEFWMI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 270 ELYEAYADYKDIMALTENLIAHIAQEVLgttkIQYGDQ-----------EVDLTPEWTRLHMVDAIKqytgvdfwgetsv 338
Cdd:COG0017 223 EPEMAFADLEDVMDLAEEMLKYIIKYVL----ENCPEEleflgrdverlEKVPESPFPRITYTEAIE------------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 339 eearaLAKEHGVEI-------TEHMQYghIVNEFFEqkveeqliQPTFIYGHPVEISPL-AKKNAEDPRFTDRFELF--- 407
Cdd:COG0017 286 -----ILKKSGEKVewgddlgTEHERY--LGEEFFK--------KPVFVTDYPKEIKAFyMKPNPDDPKTVAAFDLLapg 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 408 ---IVA---REHanaftelndpidQRERFEAQLKEkeqgndeaHEMD-DDF---IEALEYGMPPTGGLGIGIDRLVMLLT 477
Cdd:COG0017 351 igeIIGgsqREH------------RYDVLVERIKE--------KGLDpEDYewyLDLRRYGSVPHAGFGLGLERLVMWLT 410
|
490
....*....|....*..
gi 502819918 478 NAPSIRDVLLFPHMRQR 494
Cdd:COG0017 411 GLENIREVIPFPRDPGR 427
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
47-494 |
4.86e-46 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 166.13 E-value: 4.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 47 ELTKEQLEENevpVSLAGRIMTKRGKGKAGFAHVQDLTGQIQLYVRKDAIgEEQYEIFSSVDIGDLVGVEGVLFKTKV-- 124
Cdd:PRK05159 9 ELTPELDGEE---VTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKVD-EELFETIKKLKRESVVSVTGTVKANPKap 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 125 GELSIKVKDFTLLTKALRPLPDKYHG--LKDIEQRYRQRYLDLiTNPESKQTFISRSRIIQSMRRYLDNHGYLEVETPMM 202
Cdd:PRK05159 85 GGVEVIPEEIEVLNKAEEPLPLDISGkvLAELDTRLDNRFLDL-RRPRVRAIFKIRSEVLRAFREFLYENGFTEIFTPKI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 203 HSIA--GGAAARPfVTHhnaLDMELYMRIAIELHlKRLIVG-GLEKVYEIGRVFRNEGVST-RHNPEFTMIELYEAYAD- 277
Cdd:PRK05159 164 VASGteGGAELFP-IDY---FEKEAYLAQSPQLY-KQMMVGaGFERVFEIGPVFRAEEHNTsRHLNEYTSIDVEMGFIDd 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 278 YKDIMALTENLIAHIAQEVLGTTKIQYGDQEVDL---TPEWTRLHMvdaikqytgvdfwgetsvEEARALAKEHGVEI-- 352
Cdd:PRK05159 239 HEDVMDLLENLLRYMYEDVAENCEKELELLGIELpvpETPIPRITY------------------DEAIEILKSKGNEIsw 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 353 -----TEHMqygHIVNEFFEQKVEEQLIqptFIYGHPVEISPL-AKKNAEDPRFTDRFELF-----IVA---REHanaft 418
Cdd:PRK05159 301 gddldTEGE---RLLGEYVKEEYGSDFY---FITDYPSEKRPFyTMPDEDDPEISKSFDLLfrgleITSggqRIH----- 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502819918 419 elndpidQRERFEAQLKEKeqGND-EAHEmddDFIEALEYGMPPTGGLGIGIDRLVMLLTNAPSIRDVLLFPHMRQR 494
Cdd:PRK05159 370 -------RYDMLVESIKEK--GLNpESFE---FYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFPRDRHR 434
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
50-494 |
1.52e-39 |
|
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: 148.05 E-value: 1.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 50 KEQLEENEVpvSLAGRIMTKRGKGKAGFAHVQDLTGQIQLYVRKDAIGEEQYEIFSSVDIGDLVGVEG-VLFKTK-VGEL 127
Cdd:TIGR00458 7 KPEMDGQEV--TFMGWVHEIRDLGGLIFVLLRDREGLIQITAPAKKVSKNLFKWAKKLNLESVVAVRGiVKIKEKaPGGF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 128 SIKVKDFTLLTKALRPLP----DKYHGlkDIEQRYRQRYLDLITnPESKQTFISRSRIIQSMRRYLDNHGYLEVETPMMH 203
Cdd:TIGR00458 85 EIIPTKIEVINEAKEPLPldptEKVPA--ELDTRLDYRFLDLRR-PTVQAIFRIRSGVLESVREFLAEEGFIEVHTPKLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 204 SIA--GGAAARPfVTHhnaLDMELYMRIAIELHLKRLIVGGLEKVYEIGRVFRNEGVST-RHNPEFTMIELYEAYADYKD 280
Cdd:TIGR00458 162 ASAteGGTELFP-ITY---FEREAFLGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNThRHLNEATSIDIEMAFEDHHD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 281 IMALTENLIAHIAQEVLGTTKIQYGDQEVDLtpEWTRLHMVdaikqytgvdfwgETSVEEARALAKEHGVEItehmQYGH 360
Cdd:TIGR00458 238 VMDILEELVVRVFEDVPERCAHQLETLEFKL--EKPEGKFV-------------RLTYDEAIEMANAKGVEI----GWGE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 361 IVNEFFEQKVEEQLIQPTFIYGHPVEISPL-AKKNAEDPRFTDRFELFIVAREHANAftelndpiDQRERFEAQLKEKEQ 439
Cdd:TIGR00458 299 DLSTEAEKALGEEMDGLYFITDWPTEIRPFyTMPDEDNPEISKSFDLMYRDLEISSG--------AQRIHLHDLLVERIK 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 502819918 440 GNDEAHEMDDDFIEALEYGMPPTGGLGIGIDRLVMLLTNAPSIRDVLLFPHMRQR 494
Cdd:TIGR00458 371 AKGLNPEGFKDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFPRDRKR 425
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
175-489 |
6.48e-37 |
|
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: 137.32 E-value: 6.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 175 FISRSRIIQSMRRYLDNHGYLEVETPMM-HSIAGGAaaRPFV----THHN---ALDM--ELYMRIaielhlkrLIVGGLE 244
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILtKSTPEGA--RDFLvpsrLHPGkfyALPQspQLFKQL--------LMVSGFD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 245 KVYEIGRVFRNEGVSTRHNPEFTMIELYEAYADYKDIMALTENLIAHIAQEVLGttkiqygdqeVDLTPEWTRLHMVDAI 324
Cdd:cd00777 71 RYFQIARCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG----------VELTTPFPRMTYAEAM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 325 KQYtGVDF-WgetsveearalakehgveitehmqyghiVNEF--FEQKVEEQLIQPTFiygHPV-----EISPLAKKNAE 396
Cdd:cd00777 141 ERY-GFKFlW----------------------------IVDFplFEWDEEEGRLVSAH---HPFtapkeEDLDLLEKDPE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 397 DPRfTDRFELFIVAREHANAFTELNDPIDQRERFEAQLKEKEqgndEAHEMDDDFIEALEYGMPPTGGLGIGIDRLVMLL 476
Cdd:cd00777 189 DAR-AQAYDLVLNGVELGGGSIRIHDPDIQEKVFEILGLSEE----EAEEKFGFLLEAFKYGAPPHGGIALGLDRLVMLL 263
|
330
....*....|...
gi 502819918 477 TNAPSIRDVLLFP 489
Cdd:cd00777 264 TGSESIRDVIAFP 276
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
153-489 |
1.48e-36 |
|
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: 137.31 E-value: 1.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 153 DIEQRYRQRYLDLITnPESKQTFISRSRIIQSMRRYLDNHGYLEVETPMMHSIA--GGAAARPFvthhNALDMELYMRIA 230
Cdd:cd00776 3 NLETLLDNRHLDLRT-PKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDteGGAELFKV----SYFGKPAYLAQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 231 IELHLKRLIvGGLEKVYEIGRVFRNEGVST-RHNPEFTMIELYEAYA-DYKDIMALTENLIAHIAQEVL------GTTKI 302
Cdd:cd00776 78 PQLYKEMLI-AALERVYEIGPVFRAEKSNTrRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLercakeLELVN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 303 QYGDQEVDLTPEWTRLHMVDAIK--QYTGVDF---WGET-SVEEARALAKEHGVEitehmqyghivneffeqkveeqliq 376
Cdd:cd00776 157 QLNRELLKPLEPFPRITYDEAIEllREKGVEEevkWGEDlSTEHERLLGEIVKGD------------------------- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 377 PTFIYGHPVEISPL-AKKNAEDPRFTDRFELF------IVA---REHanaftelnDPIDQRERFeaqlkeKEQGNDeaHE 446
Cdd:cd00776 212 PVFVTDYPKEIKPFyMKPDDDNPETVESFDLLmpgvgeIVGgsqRIH--------DYDELEERI------KEHGLD--PE 275
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 502819918 447 MDDDFIEALEYGMPPTGGLGIGIDRLVMLLTNAPSIRDVLLFP 489
Cdd:cd00776 276 SFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
34-489 |
1.42e-33 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 133.65 E-value: 1.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 34 RTHTSqqliseyDELTKEQLEENevpVSLAGRIMTKRGKGKAGFAHVQDLTGQIQLYVRKDAigeEQYEIFSSVDIGDLV 113
Cdd:PRK00476 4 RTHYC-------GELRESHVGQT---VTLCGWVHRRRDHGGLIFIDLRDREGIVQVVFDPDA---EAFEVAESLRSEYVI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 114 GVEGVLF---------KTKVGELSIKVKDFTLLTKAlRPLP----DKYHGLKDIEQRYRqrYLDLiTNPESKQTFISRSR 180
Cdd:PRK00476 71 QVTGTVRarpegtvnpNLPTGEIEVLASELEVLNKS-KTLPfpidDEEDVSEELRLKYR--YLDL-RRPEMQKNLKLRSK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 181 IIQSMRRYLDNHGYLEVETPMM-HSIAGGaaARPFV----THHN---ALDM------ELYMriaielhlkrliVGGLEKV 246
Cdd:PRK00476 147 VTSAIRNFLDDNGFLEIETPILtKSTPEG--ARDYLvpsrVHPGkfyALPQspqlfkQLLM------------VAGFDRY 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 247 YEIGRVFRNEGVSTRHNPEFTMIELYEAYADYKDIMALTENLIAHIAQEVLGttkiqygdqeVDLTPEWTRLHMVDAIKQ 326
Cdd:PRK00476 213 YQIARCFRDEDLRADRQPEFTQIDIEMSFVTQEDVMALMEGLIRHVFKEVLG----------VDLPTPFPRMTYAEAMRR 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 327 YtGVD---------------FWGETSVEEARALAKEHGV-------------------EITEHM-QYGH------IVNE- 364
Cdd:PRK00476 283 Y-GSDkpdlrfglelvdvtdLFKDSGFKVFAGAANDGGRvkairvpggaaqlsrkqidELTEFAkIYGAkglayiKVNEd 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 365 --------FFEQKVEEQLIQPT---------FIYGHP-----------VEIS-------------------PLAKKNAED 397
Cdd:PRK00476 362 glkgpiakFLSEEELAALLERTgakdgdlifFGADKAkvvndalgalrLKLGkelglidedkfaflwvvdfPMFEYDEEE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 398 PR-------FT-----DRFELFIVAREHANAF--------TEL-------NDPIDQRERFEAqLKEKEQgndEAHEMDDD 450
Cdd:PRK00476 442 GRwvaahhpFTmpkdeDLDELETTDPGKARAYaydlvlngYELgggsiriHRPEIQEKVFEI-LGISEE---EAEEKFGF 517
|
570 580 590
....*....|....*....|....*....|....*....
gi 502819918 451 FIEALEYGMPPTGGLGIGIDRLVMLLTNAPSIRDVLLFP 489
Cdd:PRK00476 518 LLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
4-494 |
6.75e-31 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 125.59 E-value: 6.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 4 EELNDQFLVRREKMSNlrDQGIDPFGQRFERTHTSQ-QLISEYDELTK-----EQLEENEVpvSLAGRIMTKRGKGKAGF 77
Cdd:PLN02850 26 EKLRREATAKAAAASL--EDEDDPLASNYGDVPLEElQSKVTGREWTDvsdlgEELAGSEV--LIRGRVHTIRGKGKSAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 78 AHVQDLTGQIQ--LYVRKDAIGEEQYEIFSSVDIGDLVGVEGVLFKTKVG------ELSIKVKDFTLLTKALRPLP---- 145
Cdd:PLN02850 102 LVLRQSGFTVQcvVFVSEVTVSKGMVKYAKQLSRESVVDVEGVVSVPKKPvkgttqQVEIQVRKIYCVSKALATLPfnve 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 146 DKYHGLKDIEQ---------------RYRQRYLDLITnPESKQTFISRSRIIQSMRRYLDNHGYLEVETP--MMHSIAGG 208
Cdd:PLN02850 182 DAARSESEIEKalqtgeqlvrvgqdtRLNNRVLDLRT-PANQAIFRIQSQVCNLFREFLLSKGFVEIHTPklIAGASEGG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 209 AAArpFVTHHNALDMELYMriAIELHLKRLIVGGLEKVYEIGRVFRNEGVST-RHNPEFTMIEL-YEAYADYKDIMALTE 286
Cdd:PLN02850 261 SAV--FRLDYKGQPACLAQ--SPQLHKQMAICGDFRRVFEIGPVFRAEDSFThRHLCEFTGLDLeMEIKEHYSEVLDVVD 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 287 NLIAHI--------AQEvLGTTKIQYGDQEVDLTPEWTRLHMVDAIK--QYTG--VDFWGETSVEEARALakehGVEITE 354
Cdd:PLN02850 337 ELFVAIfdglnercKKE-LEAIREQYPFEPLKYLPKTLRLTFAEGIQmlKEAGveVDPLGDLNTESERKL----GQLVKE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 355 hmQYGhivNEFFeqkveeqliqptFIYGHPVEISPL-AKKNAEDPRFTDRFELFIVAREHANAFTELNDPidqrERFEAQ 433
Cdd:PLN02850 412 --KYG---TDFY------------ILHRYPLAVRPFyTMPCPDDPKYSNSFDVFIRGEEIISGAQRVHDP----ELLEKR 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502819918 434 LKEKeqGNDEahEMDDDFIEALEYGMPPTGGLGIGIDRLVMLLTNAPSIRDVLLFPHMRQR 494
Cdd:PLN02850 471 AEEC--GIDV--KTISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPRDPQR 527
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
34-489 |
4.30e-27 |
|
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: 114.71 E-value: 4.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 34 RTHTSqqliseyDELTKEQLEENevpVSLAGRIMTKRGKGKAGFAHVQDLTGQIQLYVRKDaIGEEQYEIFSSVDIGDLV 113
Cdd:COG0173 3 RTHYC-------GELRESDVGQE---VTLSGWVHRRRDHGGLIFIDLRDRYGITQVVFDPD-DSAEAFEKAEKLRSEYVI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 114 GVEGVLF---------KTKVGELSIKVKDFTLLTKAlRPLPDKYHGLKDI--EQRYRQRYLDLiTNPESKQTFISRSRII 182
Cdd:COG0173 72 AVTGKVRarpegtvnpKLPTGEIEVLASELEILNKA-KTPPFQIDDDTDVseELRLKYRYLDL-RRPEMQKNLILRHKVT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 183 QSMRRYLDNHGYLEVETPMMhsiagGAA----ARPFV----THHN---ALDM--ELYmriaielhlKRLI-VGGLEKVYE 248
Cdd:COG0173 150 KAIRNYLDENGFLEIETPIL-----TKStpegARDYLvpsrVHPGkfyALPQspQLF---------KQLLmVSGFDRYFQ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 249 IGRVFRNEgvSTRHN--PEFTMIELYEAYADYKDIMALTENLIAHIAQEVLGttkiqygdqeVDLTPEWTRLHMVDAIKQ 326
Cdd:COG0173 216 IARCFRDE--DLRADrqPEFTQLDIEMSFVDQEDVFELMEGLIRHLFKEVLG----------VELPTPFPRMTYAEAMER 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 327 YtGVD------------------------FwgetsveeaRALAKEHGV------------------EITEHM-QYGH--- 360
Cdd:COG0173 284 Y-GSDkpdlrfglelvdvtdifkdsgfkvF---------AGAAENGGRvkainvpggaslsrkqidELTEFAkQYGAkgl 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 361 ---IVNE---------FFEQKVEEQLIQPT---------FIYGHP-----------VEispLAKK----NAEDPRF---T 401
Cdd:COG0173 354 ayiKVNEdglkspiakFLSEEELAAILERLgakpgdlifFVADKPkvvnkalgalrLK---LGKElgliDEDEFAFlwvV 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 402 DrFELF--------IVAREH---------------------ANAF------TEL-------NDPIDQRERFEAqLkekeq 439
Cdd:COG0173 431 D-FPLFeydeeegrWVAMHHpftmpkdedldlletdpgkvrAKAYdlvlngYELgggsiriHDPELQEKVFEL-L----- 503
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 502819918 440 GNDEAhEMDDDF---IEALEYGMPPTGGLGIGIDRLVMLLTNAPSIRDVLLFP 489
Cdd:COG0173 504 GISEE-EAEEKFgflLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
52-489 |
9.69e-27 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 114.12 E-value: 9.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 52 QLEENEV--PVSLAGRIMTKRGKGKAGFAHVQDLTGQIQLYVRKDAIgEEQYEIFSSVDIGDLVGVEGVLF--------- 120
Cdd:PLN02903 65 ALSVNDVgsRVTLCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDEF-PEAHRTANRLRNEYVVAVEGTVRsrpqespnk 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 121 KTKVGELSIKVKDFTLLTKALRPLP-------DKYHGLKDiEQRYRQRYLDLiTNPESKQTFISRSRIIQSMRRYL-DNH 192
Cdd:PLN02903 144 KMKTGSVEVVAESVDILNVVTKSLPflvttadEQKDSIKE-EVRLRYRVLDL-RRPQMNANLRLRHRVVKLIRRYLeDVH 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 193 GYLEVETPMMhsiaggaaARPfvTHHNALDMELYMRI----------AIELHLKRLIVGGLEKVYEIGRVFRNEGVSTRH 262
Cdd:PLN02903 222 GFVEIETPIL--------SRS--TPEGARDYLVPSRVqpgtfyalpqSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 263 NPEFTMIELYEAYADYKDIMALTENLIAHIAQEVLGTT-------------KIQYGDQEVDltpewTR--LHMVDAIKQY 327
Cdd:PLN02903 292 QPEFTQLDMELAFTPLEDMLKLNEDLIRQVFKEIKGVQlpnpfprltyaeaMSKYGSDKPD-----LRygLELVDVSDVF 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 328 TGVDF-WGETSVEEA---RALAKEHGVEI--TEHMQYGHIVNEF----------------------------FEQKVEEQ 373
Cdd:PLN02903 367 AESSFkVFAGALESGgvvKAICVPDGKKIsnNTALKKGDIYNEAiksgakglaflkvlddgelegikalvesLSPEQAEQ 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 374 LIQPT---------FIYGHPVEISplakknaedpRFTDRFELFIvARE--------HANAFT------ELNDPIDQRE-- 428
Cdd:PLN02903 447 LLAACgagpgdlilFAAGPTSSVN----------KTLDRLRQFI-AKTldlidpsrHSILWVtdfpmfEWNEDEQRLEal 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 429 ----------------------------------------RFEAQLKEKEQGNDEAHEMDDDF---IEALEYGMPPTGGL 465
Cdd:PLN02903 516 hhpftapnpedmgdlssaralaydmvyngveigggslriyRRDVQQKVLEAIGLSPEEAESKFgylLEALDMGAPPHGGI 595
|
570 580
....*....|....*....|....
gi 502819918 466 GIGIDRLVMLLTNAPSIRDVLLFP 489
Cdd:PLN02903 596 AYGLDRLVMLLAGAKSIRDVIAFP 619
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
46-494 |
9.84e-27 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 112.51 E-value: 9.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 46 DELTKEQLEENevpVSLAGRIMTKRGKGKAGFAHVQDLTGQIQLYVRKDAiGEEQYEIFSSVDIGDLVGVEGVLFKT--K 123
Cdd:PRK03932 8 DILKGKYVGQE---VTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDN-GEEYFEEIKKLTTGSSVIVTGTVVESprA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 124 VGELSIKVKDFTLLTKALR--PLPDKYHG---LKDIeqryrqRYLDLITNpesKQTFIS--RSRIIQSMRRYLDNHGYLE 196
Cdd:PRK03932 84 GQGYELQATKIEVIGEDPEdyPIQKKRHSiefLREI------AHLRPRTN---KFGAVMriRNTLAQAIHEFFNENGFVW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 197 VETPMMHSIAGGAAARPFVTHHNALDME---------------LYMRIAIElhlkrlivgGLEKVYEIGRVFRNEGVST- 260
Cdd:PRK03932 155 VDTPIITASDCEGAGELFRVTTLDLDFSkdffgkeayltvsgqLYAEAYAM---------ALGKVYTFGPTFRAENSNTr 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 261 RHNPEFTMIELYEAYADYKDIMALTENLIAHIAQEVLGTTKiqygdQEVDLTPEWTRLHMVDAIKQYTGVDFwGETSVEE 340
Cdd:PRK03932 226 RHLAEFWMIEPEMAFADLEDNMDLAEEMLKYVVKYVLENCP-----DDLEFLNRRVDKGDIERLENFIESPF-PRITYTE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 341 ARALAKEHGVEI-----------TEHMQYghIVNEFFEqkveeqliQPTFIYGHPVEISPLAKKNAEDPRftdrfelfIV 409
Cdd:PRK03932 300 AIEILQKSGKKFefpvewgddlgSEHERY--LAEEHFK--------KPVFVTNYPKDIKAFYMRLNPDGK--------TV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 410 ArehanAFtelndpiD-------------QRE-RFEaQLKE--KEQGNDEahemdddfiEALE-------YGMPPTGGLG 466
Cdd:PRK03932 362 A-----AM-------DllapgigeiiggsQREeRLD-VLEAriKELGLNK---------EDYWwyldlrrYGSVPHSGFG 419
|
490 500
....*....|....*....|....*...
gi 502819918 467 IGIDRLVMLLTNAPSIRDVLLFPHMRQR 494
Cdd:PRK03932 420 LGFERLVAYITGLDNIRDVIPFPRTPGR 447
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
35-494 |
4.39e-26 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 111.62 E-value: 4.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 35 THTSQQLISEYDeLTKEQLEENEVPVSlaGRIMTKRGKGKAGFAHVQDLTGQIQLYVRK---------DAIGEEQYEifS 105
Cdd:PTZ00401 59 TYKSRTFIPVAV-LSKPELVDKTVLIR--ARVSTTRKKGKMAFMVLRDGSDSVQAMAAVegdvpkemiDFIGQIPTE--S 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 106 SVDI-GDLVGVEGVLFKTKVGELSIKVKDFTLLTKALRPLP---------DKYHGLK-DIEQRYRQRYLDLITnPESKQT 174
Cdd:PTZ00401 134 IVDVeATVCKVEQPITSTSHSDIELKVKKIHTVTESLRTLPftledasrkESDEGAKvNFDTRLNSRWMDLRT-PASGAI 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 175 FISRSRIIQSMRRYLDNHGYLEVETPMMHSIAGGAAARPFVTHHnaLDMELYMRIAIELHLKRLIVGGLEKVYEIGRVFR 254
Cdd:PTZ00401 213 FRLQSRVCQYFRQFLIDSDFCEIHSPKIINAPSEGGANVFKLEY--FNRFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFR 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 255 NEGVST-RHNPEFTMIELyEAYAD--YKDIMALTENLIAHIAQEVLGTTK------IQYGDQEV--DLTPEWTRLHMVDA 323
Cdd:PTZ00401 291 SENSNThRHLTEFVGLDV-EMRINehYYEVLDLAESLFNYIFERLATHTKelkavcQQYPFEPLvwKLTPERMKELGVGV 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 324 IKQYTgvdfwGETSVEEARALAKEHGVEITEHMQYGHIVNEFFEQKVE---------EQLIQPTFI--YGHPVEISPLAK 392
Cdd:PTZ00401 370 ISEGV-----EPTDKYQARVHNMDSRMLRINYMHCIELLNTVLEEKMAptddinttnEKLLGKLVKerYGTDFFISDRFP 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 393 KNA---------EDPRFTDRFELFIVAREHANAFTELNDPidqrerfEAQLKEKEQGNDEAHEMdDDFIEALEYGMPPTG 463
Cdd:PTZ00401 445 SSArpfytmeckDDERFTNSYDMFIRGEEISSGAQRIHDP-------DLLLARAKMLNVDLTPI-KEYVDSFRLGAWPHG 516
|
490 500 510
....*....|....*....|....*....|.
gi 502819918 464 GLGIGIDRLVMLLTNAPSIRDVLLFPHMRQR 494
Cdd:PTZ00401 517 GFGVGLERVVMLYLGLSNVRLASLFPRDPQR 547
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
60-492 |
1.07e-25 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 110.85 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 60 VSLAGRIMTKRGKGKAGFAHVQDLTGQIQLYVRKDAIGEEQYEIFSSVDIGDLVGVEGVLFK---------TKVGELSIK 130
Cdd:PRK12820 21 VCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFSPEAAPADVYELAASLRAEFCVALQGEVQKrleetenphIETGDIEVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 131 VKDFTLLTKALR---PLPDKY-----------HGLKDIEQRYRqrYLDlITNPESKQTFISRSRIIQSMRRYLDNHGYLE 196
Cdd:PRK12820 101 VRELSILAASEAlpfAISDKAmtagagsagadAVNEDLRLQYR--YLD-IRRPAMQDHLAKRHRIIKCARDFLDSRGFLE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 197 VETPMMhSIAGGAAARPFVTHHNALDMELY-MRIAIELHLKRLIVGGLEKVYEIGRVFRNEGVSTRHNPEFTMIELYEAY 275
Cdd:PRK12820 178 IETPIL-TKSTPEGARDYLVPSRIHPKEFYaLPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEFTQLDIEASF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 276 ADYKDIMALTENLIAHI-------------------AQEVLGTTK--IQYGDQEVDLTP--EWTRLHMVDAIKQ----YT 328
Cdd:PRK12820 257 IDEEFIFELIEELTARMfaiggialprpfprmpyaeAMDTTGSDRpdLRFDLKFADATDifENTRYGIFKQILQrggrIK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 329 GVDFWGETSVEEARALAKEHGVEI-----TEHMQY---------GHIVNEFFEQKVEEQL-------------------- 374
Cdd:PRK12820 337 GINIKGQSEKLSKNVLQNEYAKEIapsfgAKGMTWmraeaggldSNIVQFFSADEKEALKrrfhaedgdviimiadasca 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 375 ------------------IQPTFIYgHPVEIS--PLAKKNAED-----------PRFTD---------------RFELFI 408
Cdd:PRK12820 417 ivlsalgqlrlhladrlgLIPEGVF-HPLWITdfPLFEATDDGgvtsshhpftaPDREDfdpgdieelldlrsrAYDLVV 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 409 VAREHANAFTELNDPIDQRERFEA-QLKEKEQGNDEAHemdddFIEALEYGMPPTGGLGIGIDRLVMLLTNAPSIRDVLL 487
Cdd:PRK12820 496 NGEELGGGSIRINDKDIQLRIFAAlGLSEEDIEDKFGF-----FLRAFDFAAPPHGGIALGLDRVVSMILQTPSIREVIA 570
|
....*
gi 502819918 488 FPHMR 492
Cdd:PRK12820 571 FPKNR 575
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
166-489 |
2.11e-21 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 95.09 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 166 ITNPESKQTFISRSRIIQSMRRYLDNHGYLEVETPMMHSIA-----GGAAARPFVTHHNALDMELYMRIAIELHlKRLIV 240
Cdd:PRK06462 21 ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIISPSTdplmgLGSDLPVKQISIDFYGVEYYLADSMILH-KQLAL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 241 GGLEKVYEIGRVFRNEGV---STRHNPEFTMIELYEAYADYKDIMALTENLIAHIAQEVLGTTKIQYGDQEVDLtPEWTR 317
Cdd:PRK06462 100 RMLGKIFYLSPNFRLEPVdkdTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHEDELEFFGRDL-PHLKR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 318 lhmvdAIKQYTgvdfwgetsVEEARALAKEHGVEITEHMQYGhivnEFFEQKVEEQLIQPTFIYGHPVEISPLAKKnaED 397
Cdd:PRK06462 179 -----PFKRIT---------HKEAVEILNEEGCRGIDLEELG----SEGEKSLSEHFEEPFWIIDIPKGSREFYDR--ED 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 398 PRFTDR---FELFIV----------AREHanaftELNDPIDqrerfeaqlKEKEQGNDEAHEmdDDFIEALEYGMPPTGG 464
Cdd:PRK06462 239 PERPGVlrnYDLLLPegygeavsggEREY-----EYEEIVE---------RIREHGVDPEKY--KWYLEMAKEGPLPSAG 302
|
330 340
....*....|....*....|....*
gi 502819918 465 LGIGIDRLVMLLTNAPSIRDVLLFP 489
Cdd:PRK06462 303 FGIGVERLTRYICGLRHIREVQPFP 327
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
60-137 |
1.50e-16 |
|
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: 74.19 E-value: 1.50e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502819918 60 VSLAGRIMTK-RGKGKAGFAHVQDLTGQIQLYVRKdaigEEQYEIFSSVDIGDLVGVEGVLFKTKVGELSIKVKDFTLL 137
Cdd:pfam01336 1 VTVAGRVTSIrRSGGKLLFLTLRDGTGSIQVVVFK----EEAEKLAKKLKEGDVVRVTGKVKKRKGGELELVVEEIELL 75
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
60-139 |
3.20e-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: 73.37 E-value: 3.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 60 VSLAGRIMTKRGKGKAGFAHVQDLTGQIQLYVRKDAIGEEqYEIFSSVDIGDLVGVEGVLFKT-----KVGELSIKVKDF 134
Cdd:cd04100 2 VTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEELGEF-FEEAEKLRTESVVGVTGTVVKRpegnlATGEIELQAEEL 80
|
....*
gi 502819918 135 TLLTK 139
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 ... |
177-389 |
5.08e-16 |
|
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: 76.77 E-value: 5.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 177 SRSRIIQSMRRYLDNHGYLEVETPMMHSIAGGAAAR----PFVTHHNALDMELYMRIAIELHLKRLIVGGL----EKVYE 248
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGhepkDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIrklpLRLAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 249 IGRVFRNEG--VSTRHNPEFTMIELYEAYAD------YKDIMALTENLIAHIAQEVLGTTKIQYGDQEVDltPEWTRlhm 320
Cdd:cd00768 81 IGPAFRNEGgrRGLRRVREFTQLEGEVFGEDgeeaseFEELIELTEELLRALGIKLDIVFVEKTPGEFSP--GGAGP--- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502819918 321 vdaikqytGVDFWGETSVEEARalakehgvEITEhmqyGHIVNEFFEQKVEEQLIQPTFIYGHPVEISP 389
Cdd:cd00768 156 --------GFEIEVDHPEGRGL--------EIGS----GGYRQDEQARAADLYFLDEALEYRYPPTIGF 204
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
224-489 |
1.21e-12 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 70.05 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 224 ELYMRIAIELHLKRLiVGGLEKVYEIGRVFRNEGVST-RHNPEFTMIELYEAYADYKDIMALTENLIAHIAQEVLGTT-- 300
Cdd:PTZ00425 325 QAFLTVSGQLSLENL-CSSMGDVYTFGPTFRAENSHTsRHLAEFWMIEPEIAFADLYDNMELAESYIKYCIGYVLNNNfd 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 301 KIQYGDQEVD----------LTPEWTRLHMVDAIKQYTGVDFWGETSVEEARALAKEHgveitehmqyghivneffEQKV 370
Cdd:PTZ00425 404 DIYYFEENVEtglisrlkniLDEDFAKITYTNVIDLLQPYSDSFEVPVKWGMDLQSEH------------------ERFV 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 371 EEQLIQ-PTFIYGHPVEISPLAKKNAEDPRFTDRFELFIVAREHANAFTELNDPIdqrERFEAQLKEKEQgNDEAHEMdd 449
Cdd:PTZ00425 466 AEQIFKkPVIVYNYPKDLKAFYMKLNEDQKTVAAMDVLVPKIGEVIGGSQREDNL---ERLDKMIKEKKL-NMESYWW-- 539
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 502819918 450 dFIEALEYGMPPTGGLGIGIDRLVMLLTNAPSIRDVLLFP 489
Cdd:PTZ00425 540 -YRQLRKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFP 578
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
243-489 |
1.10e-11 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 66.92 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 243 LEKVYEIGRVFRNEGVST-RHNPEFTMIELYEAYADYKDIMALTENLIAHIAQEVLGTTKiqygdQEVDLTPEWTRLHMV 321
Cdd:PLN02603 321 LSDVYTFGPTFRAENSNTsRHLAEFWMIEPELAFADLNDDMACATAYLQYVVKYILENCK-----EDMEFFNTWIEKGII 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 322 DAIKQYTGVDFWGETSVEEARALAK---------EHGVEI-TEHMQYghIVNEFFEQKveeqliqPTFIYGHPVEISPLA 391
Cdd:PLN02603 396 DRLSDVVEKNFVQLSYTDAIELLLKakkkfefpvKWGLDLqSEHERY--ITEEAFGGR-------PVIIRDYPKEIKAFY 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 392 KKNAEDPRFTDRFELfIVARehanaFTELNDPIDQRERF---EAQLKEKEQgNDEAHEMdddFIEALEYGMPPTGGLGIG 468
Cdd:PLN02603 467 MRENDDGKTVAAMDM-LVPR-----VGELIGGSQREERLeylEARLDELKL-NKESYWW---YLDLRRYGSVPHAGFGLG 536
|
250 260
....*....|....*....|.
gi 502819918 469 IDRLVMLLTNAPSIRDVLLFP 489
Cdd:PLN02603 537 FERLVQFATGIDNIRDAIPFP 557
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
224-489 |
1.10e-10 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 64.12 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 224 ELYMRIAIELHLKRLiVGGLEKVYEIGRVFRNEG-VSTRHNPEFTMIELYEAYADYKDIMALTENLIAHIAQEVLG--TT 300
Cdd:PLN02532 371 PTYLTVSGRLHLESY-ACALGNVYTFGPRFRADRiDSARHLAEMWMVEVEMAFSELEDAMNCAEDYFKFLCKWVLEncSE 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 301 KIQYGDQEVD----------LTPEWTRL---HMVDAIKQYTGVDFwgETSVEEARALAkehgveiTEHMQYghIVNEFFE 367
Cdd:PLN02532 450 DMKFVSKRIDktistrleaiISSSLQRIsytEAVDLLKQATDKKF--ETKPEWGIALT-------TEHLSY--LADEIYK 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 368 QkveeqliqPTFIYGHPVEISPLAKKNAEDPRFTDRFEL-------FIVAREHANAFTELNDPID----QRERFEAQLKE 436
Cdd:PLN02532 519 K--------PVIIYNYPKELKPFYVRLNDDGKTVAAFDLvvpkvgtVITGSQNEERMDILNARIEelglPREQYEWYLDL 590
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 502819918 437 KEQGNDEaHEmdddfiealeygmpptgGLGIGIDRLVMLLTNAPSIRDVLLFP 489
Cdd:PLN02532 591 RRHGTVK-HS-----------------GFSLGFELMVLFATGLPDVRDAIPFP 625
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
243-489 |
4.46e-09 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 58.85 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 243 LEKVYEIGRVFRNEGVST-RHNPEFTMIELYEAYADYKDIMALTENLIAHIAQEVLGTTkiqYGDQEvdLTPEWTRLHMV 321
Cdd:PLN02221 326 LSSVYTFGPTFRAENSHTsRHLAEFWMVEPEIAFADLEDDMNCAEAYVKYMCKWLLDKC---FDDME--LMAKNFDSGCI 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 322 DAIKQYTGVDFwGETSVEEARALAKE---HGVEITEHMQYGHIVNEFFEQKVEEQLIQ-PTFIYGHPVEISPLAKKNAED 397
Cdd:PLN02221 401 DRLRMVASTPF-GRITYTEAIELLEEavaKGKEFDNNVEWGIDLASEHERYLTEVLFQkPLIVYNYPKGIKAFYMRLNDD 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 398 PRFTDRFELFIvarehaNAFTELNDPIDQRERFEAqLKEKEQGNDEAHEMDDDFIEALEYGMPPTGGLGIGIDRLVMLLT 477
Cdd:PLN02221 480 EKTVAAMDVLV------PKVGELIGGSQREERYDV-IKQRIEEMGLPIEPYEWYLDLRRYGTVKHCGFGLGFERMILFAT 552
|
250
....*....|..
gi 502819918 478 NAPSIRDVLLFP 489
Cdd:PLN02221 553 GIDNIRDVIPFP 564
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
34-165 |
6.37e-07 |
|
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: 48.67 E-value: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 34 RTHTSqqliseyDELTKEQLEENevpVSLAGRIMTKRGKGKAGFAHVQDLTGQIQLYVRKDAigEEQYEIFSSVDIGDLV 113
Cdd:cd04317 1 RTHYC-------GELRESHVGQE---VTLCGWVQRRRDHGGLIFIDLRDRYGIVQVVFDPEE--APEFELAEKLRNESVI 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502819918 114 GVEGVLF---------KTKVGELSIKVKDFTLLTKAlRPLP----DKYHGLKDIEQRYrqRYLDL 165
Cdd:cd04317 69 QVTGKVRarpegtvnpKLPTGEIEVVASELEVLNKA-KTLPfeidDDVNVSEELRLKY--RYLDL 130
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
60-119 |
7.80e-03 |
|
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus horikoshii AsnRS asparaginyl-tRNA synthetase (AsnRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The archeal enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). 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.
Pssm-ID: 239814 [Multi-domain] Cd Length: 103 Bit Score: 35.96 E-value: 7.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819918 60 VSLAGRIMTKRGKGKAGFAHVQDLTGQIQLYVRKDaIGEEQYEIFSSVDIGDLVGVEGVL 119
Cdd:cd04319 2 VTLAGWVYRKREVGKKAFIVLRDSTGIVQAVFSKD-LNEEAYREAKKVGIESSVIVEGAV 60
|
|
| |
