|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
1-505 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 990.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 1 MSEQQAQGADEAIDLNNELKTRREKLAALREQGVAFPNDFRRDHTSDQLHAEFDAKDNDELASLNVEVAVAGRMMTRRVM 80
Cdd:PRK12445 1 MSEQETRGANEAIDFNDELRNRREKLAALRQQGVAFPNDFRRDHTSDQLHEEFDAKDNQELESLNIEVSVAGRMMTRRIM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 81 GKASFVTLQDVGGRIQLYVARDDLPEGVYNEQFKKWDLGDIIAARGKLFKTQTGELSIHCTELRLLTKALRPLPDKFHGL 160
Cdd:PRK12445 81 GKASFVTLQDVGGRIQLYVARDSLPEGVYNDQFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFHGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 161 QDQEVRYRQRYLDLIANEESRHTFRIRSQILATMRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAP 240
Cdd:PRK12445 161 QDQEVRYRQRYLDLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 241 ELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYKDLIELTESLFRTLAQTVLGKTEVPYGDQVFDF 320
Cdd:PRK12445 241 ELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFDF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 321 GKPFEKLTMREAIKKHRPETNMADLDNFDAAKALAESLGIQVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPL 400
Cdd:PRK12445 321 GKPFEKLTMREAIKKYRPETDMADLDNFDAAKALAESIGITVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 401 ARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAQRFQDQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGID 480
Cdd:PRK12445 401 ARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGID 480
|
490 500
....*....|....*....|....*
gi 1082303951 481 RMVMLFTNSHTIRDVILFPAMRPQK 505
Cdd:PRK12445 481 RMIMLFTNSHTIRDVILFPAMRPQK 505
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
14-505 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 953.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 14 DLNNELKTRREKLAALREQGVA-FPNDFRRDHTSDQLHAEFDAKDNDELASLNVEVAVAGRMMTRRVMGKASFVTLQDVG 92
Cdd:PRK00484 2 ELNEQIAVRREKLAELREQGIDpYPNKFERTHTAAELRAKYDDKEKEELEELEIEVSVAGRVMLKRVMGKASFATLQDGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 93 GRIQLYVARDDLPEGVYnEQFKKWDLGDIIAARGKLFKTQTGELSIHCTELRLLTKALRPLPDKFHGLQDQEVRYRQRYL 172
Cdd:PRK00484 82 GRIQLYVSKDDVGEEAL-EAFKKLDLGDIIGVEGTLFKTKTGELSVKATELTLLTKSLRPLPDKFHGLTDVETRYRQRYV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 173 DLIANEESRHTFRIRSQILATMRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGF 252
Cdd:PRK00484 161 DLIVNPESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARPFITHHNALDIDLYLRIAPELYLKRLIVGGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 253 ERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYKDLIELTESLFRTLAQTVLGKTEVPYGDQVFDFGKPFEKLTMREA 332
Cdd:PRK00484 241 ERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTYQGTEIDFGPPFKRLTMVDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 333 IKKHRPEtnmaDLD--NFDAAKALAESLGIQVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEI 410
Cdd:PRK00484 321 IKEYTGV----DFDdmTDEEARALAKELGIEVEKSWGLGKLINELFEEFVEPKLIQPTFITDYPVEISPLAKRHREDPGL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 411 TDRFEFFIGGREIGNGFSELNDAEDQAQRFQDQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMVMLFTNSH 490
Cdd:PRK00484 397 TERFELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSP 476
|
490
....*....|....*
gi 1082303951 491 TIRDVILFPAMRPQK 505
Cdd:PRK00484 477 SIRDVILFPLMRPEK 491
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
1-505 |
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: 927.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 1 MSEQQaqgadeaiDLNNELKTRREKLAALREQGV-AFPNDFRRDHTSDQLHAEFDAKDNDElaSLNVEVAVAGRMMTRRV 79
Cdd:COG1190 1 MSEEE--------DLNEQIRVRREKLEELREAGIdPYPNKFPRTHTAAEIREKYDELEAEE--ETGDEVSVAGRIMAKRD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 80 MGKASFVTLQDVGGRIQLYVARDDLPEGVYnEQFKKWDLGDIIAARGKLFKTQTGELSIHCTELRLLTKALRPLPDKFHG 159
Cdd:COG1190 71 MGKASFADLQDGSGRIQLYLRRDELGEEAY-ELFKLLDLGDIVGVEGTVFRTKTGELSVKVEELTLLSKSLRPLPEKFHG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 160 LQDQEVRYRQRYLDLIANEESRHTFRIRSQILATMRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIA 239
Cdd:COG1190 150 LTDPETRYRQRYVDLIVNPEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 240 PELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYKDLIELTESLFRTLAQTVLGKTEVPYGDQVFD 319
Cdd:COG1190 230 PELYLKRLIVGGFERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGTTKVTYQGQEID 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 320 FGKPFEKLTMREAIKKHRpETNMADLDNFDAAKALAESLGIQVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSP 399
Cdd:COG1190 310 LSPPWRRITMVEAIKEAT-GIDVTPLTDDEELRALAKELGIEVDPGWGRGKLIDELFEELVEPKLIQPTFVTDYPVEVSP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 400 LARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAQRFQDQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGI 479
Cdd:COG1190 389 LAKRHRDDPGLTERFELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGLGIGI 468
|
490 500
....*....|....*....|....*.
gi 1082303951 480 DRMVMLFTNSHTIRDVILFPAMRPQK 505
Cdd:COG1190 469 DRLVMLLTDSPSIRDVILFPLMRPEK 494
|
|
| lysS_bact |
TIGR00499 |
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ... |
14-505 |
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: 717.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 14 DLNNELKTRREKLAALREQGV-AFPNDFRRDHTSDQLHAEFDAKDNDELASLNVEVAVAGRMMTRRVMGKASFVTLQDVG 92
Cdd:TIGR00499 1 ELNDQAQQRLEKLNRLRQTGNnPYLHKFERTHSAQEFQEKYADLSNEELKEKELKVSIAGRIKAIRSMGKATFITLQDES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 93 GRIQLYVARDDLPEGVYNEQFKKWDLGDIIAARGKLFKTQTGELSIHCTELRLLTKALRPLPDKFHGLQDQEVRYRQRYL 172
Cdd:TIGR00499 81 GQIQLYVNKNKLPEDFYEFDEYLLDLGDIIGVTGYPFKTKTGELSVKVTELQILTKCLQPLPDKWHGLTDQETRYRQRYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 173 DLIANEESRHTFRIRSQILATMRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGF 252
Cdd:TIGR00499 161 DLIVNPDVRQTFLKRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKPFITHHNALDMDLYLRIAPELYLKRLIVGGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 253 ERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYKDLIELTESLFRTLAQTVLGKTEVPYGDQVFDFGKPFEKLTMREA 332
Cdd:TIGR00499 241 EKVYEIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTFIINYNDLEIDLKPPWKRITMVDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 333 IKKHRPeTNMADLDNFDAAKALAESLGIQV-EKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEIT 411
Cdd:TIGR00499 321 LEMVTG-IDFDILKDDETAKALAKEHGIEVaEDSLTLGHILNKFFEQFLEHTLIQPTFITHYPAEISPLAKRDPSNPEFT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 412 DRFEFFIGGREIGNGFSELNDAEDQAQRFQDQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMVMLFTNSHT 491
Cdd:TIGR00499 400 ERFELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGIGIDRLVMLLTDAPS 479
|
490
....*....|....
gi 1082303951 492 IRDVILFPAMRPQK 505
Cdd:TIGR00499 480 IRDVLLFPQLRPQK 493
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
2-504 |
0e+00 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 637.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 2 SEQQAQGADEAIDLNNELKTRREKLAALREQGV-AFPNDFRRDHTSDQLHAEFDAKDNDELASlNVEVAVAGRMMTRRVM 80
Cdd:PLN02502 45 SRKSAAADDETMDPTQYRANRLKKVEALRAKGVePYPYKFDVTHTAPELQEKYGSLENGEELE-DVSVSVAGRIMAKRAF 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 81 GKASFVTLQDVGGRIQLYV--ARDDLPEGVYnEQFKKW-DLGDIIAARGKLFKTQTGELSIHCTELRLLTKALRPLPDKF 157
Cdd:PLN02502 124 GKLAFYDLRDDGGKIQLYAdkKRLDLDEEEF-EKLHSLvDRGDIVGVTGTPGKTKKGELSIFPTSFEVLTKCLLMLPDKY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 158 HGLQDQEVRYRQRYLDLIANEESRHTFRIRSQILATMRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLR 237
Cdd:PLN02502 203 HGLTDQETRYRQRYLDLIANPEVRDIFRTRAKIISYIRRFLDDRGFLEVETPMLNMIAGGAAARPFVTHHNDLNMDLYLR 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 238 IAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYKDLIELTESLFRTLAQTVLGKTEVPYGDQV 317
Cdd:PLN02502 283 IATELHLKRLVVGGFERVYEIGRQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKELTGSYKIKYHGIE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 318 FDFGKPFEKLTMREAIKKHRPETNMADLDNFDAAKALA---ESLGIQVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYP 394
Cdd:PLN02502 363 IDFTPPFRRISMISLVEEATGIDFPADLKSDEANAYLIaacEKFDVKCPPPQTTGRLLNELFEEFLEETLVQPTFVLDHP 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 395 AEVSPLARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAQRFQDQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAG 474
Cdd:PLN02502 443 VEMSPLAKPHRSKPGLTERFELFINGRELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGG 522
|
490 500 510
....*....|....*....|....*....|
gi 1082303951 475 LGIGIDRMVMLFTNSHTIRDVILFPAMRPQ 504
Cdd:PLN02502 523 WGLGIDRLVMLLTDSASIRDVIAFPAMKPQ 552
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
177-503 |
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 1082303951 177 NEESRHTFRIRSQILATMRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGFERVF 256
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 257 EINRNFRNEGISVRHNPEFTMMELYMAYADYKDLIELTESLFRTLAQTVLGKTEVPYGDQVFDFGKPFEKLTMREAIKKH 336
Cdd:cd00775 81 EIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIEYGGKELDFTPPFKRVTMVDALKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 337 RPET--NMADLDNFDAAKALAESLGIQVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEITDRF 414
Cdd:cd00775 161 TGIDfpELDLEQPEELAKLLAKLIKEKIEKPRTLGKLLDKLFEEFVEPTLIQPTFIIDHPVEISPLAKRHRSNPGLTERF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 415 EFFIGGREIGNGFSELNDAEDQAQRFQDQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMVMLFTNSHTIRD 494
Cdd:cd00775 241 ELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLTDSNSIRD 320
|
....*....
gi 1082303951 495 VILFPAMRP 503
Cdd:cd00775 321 VILFPAMRP 329
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
20-505 |
2.59e-168 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 504.11 E-value: 2.59e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 20 KTRREKLAALREQGV-AFPNDFRRDHT-SDQLHAEFDAkdndelaslnvEVAVAGRMMTRRVMGKASFVTLQDVGGRIQL 97
Cdd:PRK02983 615 RVRLAKLEALRAAGVdPYPVGVPPTHTvAEALDAPTGE-----------EVSVSGRVLRIRDYGGVLFADLRDWSGELQV 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 98 YVARDDLPEGVYNEQFKKWDLGDIIAARGKLFKTQTGELSIHCTELRLLTKALRPLPDKFHGLQDQEVRYRQRYLDLIAN 177
Cdd:PRK02983 684 LLDASRLEQGSLADFRAAVDLGDLVEVTGTMGTSRNGTLSLLVTSWRLAGKCLRPLPDKWKGLTDPEARVRQRYLDLAVN 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 178 EESRHTFRIRSQILATMRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGFERVFE 257
Cdd:PRK02983 764 PEARDLLRARSAVVRAVRETLVARGFLEVETPILQQVHGGANARPFVTHINAYDMDLYLRIAPELYLKRLCVGGVERVFE 843
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 258 INRNFRNEGISVRHNPEFTMMELYMAYADYKDLIELTESLFRTLAQTVLGKTEVPYGD-----QVFDFGKPFEKLTMREA 332
Cdd:PRK02983 844 LGRNFRNEGVDATHNPEFTLLEAYQAHADYDTMRDLTRELIQNAAQAAHGAPVVMRPDgdgvlEPVDISGPWPVVTVHDA 923
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 333 IKKH-----RPETNMADLdnfdaaKALAESLGIQVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDVN 407
Cdd:PRK02983 924 VSEAlgeeiDPDTPLAEL------RKLCDAAGIPYRTDWDAGAVVLELYEHLVEDRTTFPTFYTDFPTSVSPLTRPHRSD 997
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 408 PEITDRFEFFIGGREIGNGFSELNDAEDQAQRFQDQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMVMLFT 487
Cdd:PRK02983 998 PGLAERWDLVAWGVELGTAYSELTDPVEQRRRLTEQSLLAAGGDPEAMELDEDFLQALEYAMPPTGGLGMGVDRLVMLLT 1077
|
490
....*....|....*...
gi 1082303951 488 NShTIRDVILFPAMRPQK 505
Cdd:PRK02983 1078 GR-SIRETLPFPLVKPRQ 1094
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
184-503 |
2.59e-142 |
|
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: 409.94 E-value: 2.59e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 184 FRIRSQILATMRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGFERVFEINRNFR 263
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 264 NEGISVRHNPEFTMMELYMAYADYKDLIELTESLFRTLAQTVLGKTEVPYGDQVFDFGKPFEKLTMREAIKKHRPetnma 343
Cdd:cd00669 81 NEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYGFELEDFGLPFPRLTYREALERYGQ----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 344 dldnfdaakalaeslgiqvekswglgrivteifdevaeahliqPTFITEYPAE-VSPLARRNDVNPEITDRFEFFIGGRE 422
Cdd:cd00669 156 -------------------------------------------PLFLTDYPAEmHSPLASPHDVNPEIADAFDLFINGVE 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 423 IGNGFSELNDAEDQAQRFQDQVNAKAAGddeaMFYDEDYVTALEYGLPPTAGLGIGIDRMVMLFTNSHTIRDVILFPAMR 502
Cdd:cd00669 193 VGNGSSRLHDPDIQAEVFQEQGINKEAG----MEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKMR 268
|
.
gi 1082303951 503 P 503
Cdd:cd00669 269 R 269
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
36-503 |
1.52e-129 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 388.98 E-value: 1.52e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 36 FPNDFRRDHTSDQLHAEFDAKDNDELASlNVEVAVAGRMMTRRVMG-KASFVTLQDVGGRIQLYV--ARDDLPEGVYNEQ 112
Cdd:PTZ00417 104 YPHKFERTITVPEFVEKYQDLASGEHLE-DTILNVTGRIMRVSASGqKLRFFDLVGDGAKIQVLAnfAFHDHTKSNFAEC 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 113 FKKWDLGDIIAARGKLFKTQTGELSIHCTELRLLTKALRPLPDKFhGLQDQEVRYRQRYLDLIANEESRHTFRIRSQILA 192
Cdd:PTZ00417 183 YDKIRRGDIVGIVGFPGKSKKGELSIFPKETIILSPCLHMLPMKY-GLKDTEIRYRQRYLDLMINESTRSTFITRTKIIN 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 193 TMRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHN 272
Cdd:PTZ00417 262 YLRNFLNDRGFIEVETPTMNLVAGGANARPFITHHNDLDLDLYLRIATELPLKMLIVGGIDKVYEIGKVFRNEGIDNTHN 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 273 PEFTMMELYMAYADYKDLIELTESLFRTLAQTVLGKTEVPYG------DQV-FDFGKPFEKLTMREAIKKhrpETNMADL 345
Cdd:PTZ00417 342 PEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHLFGTYKILYNkdgpekDPIeIDFTPPYPKVSIVEELEK---LTNTKLE 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 346 DNFDAAKALAESLGIQVEKSWGLGRIVT--EIFDEVAeAHLI------QPTFITEYPAEVSPLARRNDVNPEITDRFEFF 417
Cdd:PTZ00417 419 QPFDSPETINKMINLIKENKIEMPNPPTaaKLLDQLA-SHFIenkypnKPFFIIEHPQIMSPLAKYHRSKPGLTERLEMF 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 418 IGGREIGNGFSELNDAEDQAQRFQDQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMVMLFTNSHTIRDVIL 497
Cdd:PTZ00417 498 ICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVIL 577
|
....*.
gi 1082303951 498 FPAMRP 503
Cdd:PTZ00417 578 FPTMRP 583
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
162-502 |
3.89e-125 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 368.05 E-value: 3.89e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 162 DQEVRYRQRYLDLIaNEESRHTFRIRSQILATMRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPE 241
Cdd:pfam00152 1 DEETRLKYRYLDLR-RPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 242 LYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYKDLIELTESLFRTLAQTVLGKTEVPYGDQVFDFG 321
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 322 KPFEKLTMREAIKKHRPETNMADLDNFDAAKAlaeslgiqvekswglgRIVTEIfdeVAEAHLIQPTFITEYPAEVSPLA 401
Cdd:pfam00152 160 KPFPRITYAEAIEKLNGKDVEELGYGSDKPDL----------------RFLLEL---VIDKNKFNPLWVTDFPAEHHPFT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 402 RRNDVN-PEITDRFEFFIGGREIGNGFSELNDAEDQAQRFQDQVNAKaagdDEAMFYDEDYVTALEYGLPPTAGLGIGID 480
Cdd:pfam00152 221 MPKDEDdPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDP----EEAEEKFGFYLDALKYGAPPHGGLGIGLD 296
|
330 340
....*....|....*....|..
gi 1082303951 481 RMVMLFTNSHTIRDVILFPAMR 502
Cdd:pfam00152 297 RLVMLLTGLESIREVIAFPKTR 318
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
65-502 |
8.53e-116 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 355.88 E-value: 8.53e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 65 NVEVAVAGRMMTRRVMGKASFVTLQDVGGRIQLYV------ARDDLpegvynEQFK-KWDLGDIIAARGKLFKTQTGELS 137
Cdd:PTZ00385 107 QATVRVAGRVTSVRDIGKIIFVTIRSNGNELQVVGqvgehfTREDL------KKLKvSLRVGDIIGADGVPCRMQRGELS 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 138 IHCTELRLLT------KALRPLPDKFHGLQDQEVRYRQRYLDLIANEESRHTFRIRSQILATMRQFMVARGFMEVETPMM 211
Cdd:PTZ00385 181 VAASRMLILSpyvctdQVVCPNLRGFTVLQDNDVKYRYRFTDMMTNPCVIETIKKRHVMLQALRDYFNERNFVEVETPVL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 212 QVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYKDLI 291
Cdd:PTZ00385 261 HTVASGANAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTSCEFYAAYHTYEDLM 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 292 ELTESLFRTLAQTVLGKTEV------PYGDQV-FDFGKPFEKLTMREAIKKHR----PETNmadldNFDAAKALAESLGI 360
Cdd:PTZ00385 341 PMTEDIFRQLAMRVNGTTVVqiypenAHGNPVtVDLGKPFRRVSVYDEIQRMSgvefPPPN-----ELNTPKGIAYMSVV 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 361 QVEKSWGLG--RIVTEIFDEVAE----AHLIQPTFITEYPAEVSPLARRNDVNPEITDRFEFFIGGREIGNGFSELNDAE 434
Cdd:PTZ00385 416 MLRYNIPLPpvRTAAKMFEKLIDffitDRVVEPTFVMDHPLFMSPLAKEQVSRPGLAERFELFVNGIEYCNAYSELNDPH 495
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082303951 435 DQAQRFQDQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMVMLFTNSHTIRDVILFPAMR 502
Cdd:PTZ00385 496 EQYHRFQQQLVDRQGGDEEAMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFPLLR 563
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
180-496 |
2.22e-78 |
|
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: 247.71 E-value: 2.22e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 180 SRHTFRIRSQILATMRQFMVARGFMEVETPMMQVIPGG-ASARPFIT---HHNALDLDMYLRIAPELYLKRLVVGGFERV 255
Cdd:COG2269 2 SREALRARARLLAAIRAFFAERGVLEVETPALSVAPGTdPHLDSFATefiGPDGGGRPLYLHTSPEFAMKRLLAAGSGPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 256 FEINRNFRNEGISVRHNPEFTMMELYMAYADYKDLIELTESLFRTLAQTVLgktevpygdqvfdfGKPFEKLTMREAIKK 335
Cdd:COG2269 82 YQIAKVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAAG--------------FAPAERLSYQEAFLR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 336 HrpetnmADLD----NFDAAKALAESLGIQVEKSWGLGRIVTEIFDEVAEAHLIQ--PTFITEYPAEVSPLARRNDVNPE 409
Cdd:COG2269 148 Y------LGIDpltaDLDELAAAAAAAGLRVADDDDRDDLLDLLLSERVEPQLGRdrPTFLYDYPASQAALARISPDDPR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 410 ITDRFEFFIGGREIGNGFSELNDAEDQAQRFQDQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMVMLFTNS 489
Cdd:COG2269 222 VAERFELYACGVELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALGA 301
|
....*..
gi 1082303951 490 HTIRDVI 496
Cdd:COG2269 302 ERIDDVL 308
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
197-496 |
1.12e-72 |
|
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: 232.06 E-value: 1.12e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 197 FMVARGFMEVETPMMQVIPGGASA-RPFITH---HNALDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHN 272
Cdd:TIGR00462 1 FFAERGVLEVETPLLSPAPVTDPHlDAFATEfvgPDGQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 273 PEFTMMELYMAYADYKDLIELTESLFRTLAQtvlgktevpygdqvfDFGKPFEKLTMREAIKKHrpetnmADLD----NF 348
Cdd:TIGR00462 81 PEFTMLEWYRPGFDYHDLMDEVEALLQELLG---------------DPFAPAERLSYQEAFLRY------AGIDpltaSL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 349 DAAKALAESLGIQVekSWGLGR--IVTEIFDEVAEAHLIQ--PTFITEYPAEVSPLARRNDVNPEITDRFEFFIGGREIG 424
Cdd:TIGR00462 140 AELQAAAAAHGIRA--SEEDDRddLLDLLFSEKVEPHLGFgrPTFLYDYPASQAALARISPDDPRVAERFELYIKGLELA 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082303951 425 NGFSELNDAEDQAQRFQDQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMVMLFTNSHTIRDVI 496
Cdd:TIGR00462 218 NGFHELTDAAEQRRRFEADNALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDVL 289
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
67-174 |
1.10e-58 |
|
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: 189.23 E-value: 1.10e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 67 EVAVAGRMMTRRVMGKASFVTLQDVGGRIQLYVARDDLPEGVYNEQFKKWDLGDIIAARGKLFKTQTGELSIHCTELRLL 146
Cdd:cd04322 1 EVSVAGRIMSKRGSGKLSFADLQDESGKIQVYVNKDDLGEEEFEDFKKLLDLGDIIGVTGTPFKTKTGELSIFVKEFTLL 80
|
90 100
....*....|....*....|....*...
gi 1082303951 147 TKALRPLPDKFHGLQDQEVRYRQRYLDL 174
Cdd:cd04322 81 SKSLRPLPEKFHGLTDVETRYRQRYLDL 108
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
187-495 |
6.06e-57 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 191.68 E-value: 6.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 187 RSQILATMRQFMVARGFMEVETPMMQ----------------VIPGGASArpfithhnaldLDMYLRIAPELYLKRLVVG 250
Cdd:PRK09350 8 RAKIIAEIRRFFADRGVLEVETPILSqatvtdihlvpfetrfVGPGASQG-----------KTLWLMTSPEYHMKRLLAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 251 GFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYKDLIELTESLFRtlaqtvlgktevpygdQVFDFGkPFEKLTMR 330
Cdd:PRK09350 77 GSGPIFQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQ----------------QVLDCE-PAESLSYQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 331 EAIKKHrpetnmADLDNFDAAKalaESLgIQVEKSWGLGRIVTE----------IFDEVAEAHLIQ--PTFITEYPAEVS 398
Cdd:PRK09350 140 QAFLRY------LGIDPLSADK---TQL-REVAAKLGLSNIADEeedrdtllqlLFTFGVEPNIGKekPTFVYHFPASQA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 399 PLARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAQRF-QDQVNAKAAGDDEaMFYDEDYVTALEYGLPPTAGLGI 477
Cdd:PRK09350 210 ALAKISTEDHRVAERFEVYFKGIELANGFHELTDAREQRQRFeQDNRKRAARGLPQ-QPIDENLIAALEAGLPDCSGVAL 288
|
330
....*....|....*...
gi 1082303951 478 GIDRMVMLFTNSHTIRDV 495
Cdd:PRK09350 289 GVDRLIMLALGAESISEV 306
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
67-502 |
2.07e-48 |
|
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: 172.54 E-value: 2.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 67 EVAVAGRMMTRRVMGKASFVTLQDVGGRIQLYVARDDLPEgvyNEQFKKWDLGDIIAARGKLFKTQT--GELSIHCTELR 144
Cdd:COG0017 16 EVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKLEN---FEEAKKLTTESSVEVTGTVVESPRapQGVELQAEEIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 145 LLTKALRPLP-DKF-HGLqdqEVRYRQRYLDLIANEEsRHTFRIRSQILATMRQFMVARGFMEVETPMMqvIP----GGA 218
Cdd:COG0017 93 VLGEADEPYPlQPKrHSL---EFLLDNRHLRLRTNRF-GAIFRIRSELARAIREFFQERGFVEVHTPII--TAsateGGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 219 sarpfithhnaldlDM----------YLRIAPELYlKRLVVGGFERVFEINRNFRNEGiS--VRHNPEFTMMELYMAYAD 286
Cdd:COG0017 167 --------------ELfpvdyfgkeaYLTQSGQLY-KEALAMALEKVYTFGPTFRAEK-SntRRHLAEFWMIEPEMAFAD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 287 YKDLIELTESLFRTLAQTVLGKtevpYGDQVFDFGK-----------PFEKLTMREAIKkhrpetnmadldnfdaakaLA 355
Cdd:COG0017 231 LEDVMDLAEEMLKYIIKYVLEN----CPEELEFLGRdverlekvpesPFPRITYTEAIE-------------------IL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 356 ESLGIQVEksWG--LG----RIVTEIFDEvaeahliQPTFITEYPAEVSPL-ARRNDVNPEITDRFEFFIGG-REIGNGF 427
Cdd:COG0017 288 KKSGEKVE--WGddLGteheRYLGEEFFK-------KPVFVTDYPKEIKAFyMKPNPDDPKTVAAFDLLAPGiGEIIGGS 358
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082303951 428 SELNDAEDQAQRFQDQvnakaaGDDEAMFydEDYVTALEYGLPPTAGLGIGIDRMVMLFTNSHTIRDVILFPAMR 502
Cdd:COG0017 359 QREHRYDVLVERIKEK------GLDPEDY--EWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDP 425
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
67-499 |
7.96e-48 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 171.14 E-value: 7.96e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 67 EVAVAGRMMTRRVMGKASFVTLQDVGGRIQLYVARDDLPEGVynEQFKKWDLGDIIAARGKLFKTQT--GELSIHCTELR 144
Cdd:PRK05159 18 EVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKVDEELF--ETIKKLKRESVVSVTGTVKANPKapGGVEVIPEEIE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 145 LLTKALRPLPDKFHG--LQDQEVRYRQRYLDLiANEESRHTFRIRSQILATMRQFMVARGFMEVETPmmQVIP----GGA 218
Cdd:PRK05159 96 VLNKAEEPLPLDISGkvLAELDTRLDNRFLDL-RRPRVRAIFKIRSEVLRAFREFLYENGFTEIFTP--KIVAsgteGGA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 219 SARPfITHhnaLDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGI-SVRHNPEFTMMELYMAYAD-YKDLIELTES 296
Cdd:PRK05159 173 ELFP-IDY---FEKEAYLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHnTSRHLNEYTSIDVEMGFIDdHEDVMDLLEN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 297 LFRTLAQTVLGKtevpYGDQVFDFG-------KPFEKLTMREAIKKHRPETN-MADLDNFDAAkalAESLgiqvekswgL 368
Cdd:PRK05159 249 LLRYMYEDVAEN----CEKELELLGielpvpeTPIPRITYDEAIEILKSKGNeISWGDDLDTE---GERL---------L 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 369 GRIVTEifdEVAEAHLiqptFITEYPAEVSPL-ARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAQRFQDQvnak 447
Cdd:PRK05159 313 GEYVKE---EYGSDFY----FITDYPSEKRPFyTMPDEDDPEISKSFDLLFRGLEITSGGQRIHRYDMLVESIKEK---- 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1082303951 448 aaGDDEAMFydEDYVTALEYGLPPTAGLGIGIDRMVMLFTNSHTIRDVILFP 499
Cdd:PRK05159 382 --GLNPESF--EFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFP 429
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
161-499 |
9.24e-43 |
|
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: 154.65 E-value: 9.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 161 QDQEVRYRQRYLDLIANEESRhTFRIRSQILATMRQFMVARGFMEVETPMMQVIP--GGASARPFithhNALDLDMYLRI 238
Cdd:cd00776 2 ANLETLLDNRHLDLRTPKVQA-IFRIRSEVLRAFREFLRENGFTEVHTPKITSTDteGGAELFKV----SYFGKPAYLAQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 239 APELYlKRLVVGGFERVFEINRNFRNE-GISVRHNPEFTMMELYMAYA-DYKDLIELTESLFRTLAQTVL------GKTE 310
Cdd:cd00776 77 SPQLY-KEMLIAALERVYEIGPVFRAEkSNTRRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLercakeLELV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 311 VPYGDQVFDFGKPFEKLTMREAIK---KHRPETNMADLDNFDAA--KALAEslgiqvekswglgrivtEIFDEvaeahli 385
Cdd:cd00776 156 NQLNRELLKPLEPFPRITYDEAIEllrEKGVEEEVKWGEDLSTEheRLLGE-----------------IVKGD------- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 386 qPTFITEYPAEVSPL-ARRNDVNPEITDRFEFFI-GGREIGNGFSELNDAEDQAQRFqdqvnaKAAGDDEAMFydEDYVT 463
Cdd:cd00776 212 -PVFVTDYPKEIKPFyMKPDDDNPETVESFDLLMpGVGEIVGGSQRIHDYDELEERI------KEHGLDPESF--EWYLD 282
|
330 340 350
....*....|....*....|....*....|....*.
gi 1082303951 464 ALEYGLPPTAGLGIGIDRMVMLFTNSHTIRDVILFP 499
Cdd:cd00776 283 LRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
1-499 |
3.34e-34 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 135.22 E-value: 3.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 1 MSEQQAQgaDEAIDLNNELKTRREKLAALREQGVAFP-NDFRRDHTSDQLHAEFDAKDNDELASLNVE-----VAVAGRM 74
Cdd:PLN02850 13 ISKKAAK--KAAAKAEKLRREATAKAAAASLEDEDDPlASNYGDVPLEELQSKVTGREWTDVSDLGEElagseVLIRGRV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 75 MTRRVMGKASFVTLQDVGGRIQ--LYVARDDLPEGV--YNEQFKK---WDLGDIIAARGKLFKTQTGELSIHCTELRLLT 147
Cdd:PLN02850 91 HTIRGKGKSAFLVLRQSGFTVQcvVFVSEVTVSKGMvkYAKQLSResvVDVEGVVSVPKKPVKGTTQQVEIQVRKIYCVS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 148 KALRPLP-----------DKFHGLQD--------QEVRYRQRYLDL--IANEEsrhTFRIRSQILATMRQFMVARGFMEV 206
Cdd:PLN02850 171 KALATLPfnvedaarsesEIEKALQTgeqlvrvgQDTRLNNRVLDLrtPANQA---IFRIQSQVCNLFREFLLSKGFVEI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 207 ETPmmQVIPG---GASArpfithhnALDLDMY-----LRIAPELYLKRLVVGGFERVFEINRNFRNE-GISVRHNPEFTM 277
Cdd:PLN02850 248 HTP--KLIAGaseGGSA--------VFRLDYKgqpacLAQSPQLHKQMAICGDFRRVFEIGPVFRAEdSFTHRHLCEFTG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 278 MELYMAYAD-YKDLIELTESLFRTLAQTV-------LGKTEVPYGDQVFDFGKPFEKLTMREAI---KKHRPET-NMADL 345
Cdd:PLN02850 318 LDLEMEIKEhYSEVLDVVDELFVAIFDGLnerckkeLEAIREQYPFEPLKYLPKTLRLTFAEGIqmlKEAGVEVdPLGDL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 346 DNfdaakalaeslgiqvEKSWGLGRIV-----TEIFdevaeahliqptFITEYPAEVSPLARRNDV-NPEITDRFEFFIG 419
Cdd:PLN02850 398 NT---------------ESERKLGQLVkekygTDFY------------ILHRYPLAVRPFYTMPCPdDPKYSNSFDVFIR 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 420 GREIGNGFSELNDAEDQAQRfqdqvnAKAAGDDEAMFydEDYVTALEYGLPPTAGLGIGIDRMVMLFTNSHTIRDVILFP 499
Cdd:PLN02850 451 GEEIISGAQRVHDPELLEKR------AEECGIDVKTI--STYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFP 522
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
184-499 |
7.01e-32 |
|
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: 123.45 E-value: 7.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 184 FRIRSQILATMRQFMVARGFMEVETPMM-QVIPGGAsaRPFI----THHN---ALDLdmylriAPELYLKRLVVGGFERV 255
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILtKSTPEGA--RDFLvpsrLHPGkfyALPQ------SPQLFKQLLMVSGFDRY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 256 FEINRNFRNEGISVRHNPEFTMMELYMAYADYKDLIELTESLFRTLAQTVLGKtEVPygdqvfdfgKPFEKLTMREAIKK 335
Cdd:cd00777 73 FQIARCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLGV-ELT---------TPFPRMTYAEAMER 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 336 HrpetnmadldnfdaakalaeslGIQVekSWglgriVTE--IFDEVAEAHLIQPT---FiTEYPAEVSPLarrNDVNPE- 409
Cdd:cd00777 143 Y----------------------GFKF--LW-----IVDfpLFEWDEEEGRLVSAhhpF-TAPKEEDLDL---LEKDPEd 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 410 -ITDRFEFFIGGREIGNGFSELNDAEDQAQRFqdqvnaKAAGDDEAMFYDE--DYVTALEYGLPPTAGLGIGIDRMVMLF 486
Cdd:cd00777 190 aRAQAYDLVLNGVELGGGSIRIHDPDIQEKVF------EILGLSEEEAEEKfgFLLEAFKYGAPPHGGIALGLDRLVMLL 263
|
330
....*....|...
gi 1082303951 487 TNSHTIRDVILFP 499
Cdd:cd00777 264 TGSESIRDVIAFP 276
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
67-499 |
1.23e-30 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 125.56 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 67 EVAVAGRMMTRRVMGKASFVTLQDVGGRIQLyVARDDLP-----EGVYNEqfkkwdlgDIIAARGKLF---------KTQ 132
Cdd:PRK00476 19 TVTLCGWVHRRRDHGGLIFIDLRDREGIVQV-VFDPDAEafevaESLRSE--------YVIQVTGTVRarpegtvnpNLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 133 TGELSIHCTELRLLTKAlRPLPdkFHGLQDQ----EVRYRQRYLDLiANEESRHTFRIRSQILATMRQFMVARGFMEVET 208
Cdd:PRK00476 90 TGEIEVLASELEVLNKS-KTLP--FPIDDEEdvseELRLKYRYLDL-RRPEMQKNLKLRSKVTSAIRNFLDDNGFLEIET 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 209 PMMqvipgGAS----ARPFI----THHN---ALDLdmylriAPELYLKRLVVGGFERVFEINRNFRNEgiSVRHN--PEF 275
Cdd:PRK00476 166 PIL-----TKStpegARDYLvpsrVHPGkfyALPQ------SPQLFKQLLMVAGFDRYYQIARCFRDE--DLRADrqPEF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 276 TMMELYMAYADYKDLIELTESLFRTLAQTVLGKtevpygdqvfDFGKPFEKLTMREAIKKH---RPET-------NMADL 345
Cdd:PRK00476 233 TQIDIEMSFVTQEDVMALMEGLIRHVFKEVLGV----------DLPTPFPRMTYAEAMRRYgsdKPDLrfglelvDVTDL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 346 ---DNFDAAKALAESLG----IQVEKswGLGRIVTEIFDEVAEahliqptFITEYPA------------EVSPLARR--N 404
Cdd:PRK00476 303 fkdSGFKVFAGAANDGGrvkaIRVPG--GAAQLSRKQIDELTE-------FAKIYGAkglayikvnedgLKGPIAKFlsE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 405 DVNPEITDRFE-------FFIGGR-------------EIGNGFSELNDAE---------------DQAQRF--------- 440
Cdd:PRK00476 374 EELAALLERTGakdgdliFFGADKakvvndalgalrlKLGKELGLIDEDKfaflwvvdfpmfeydEEEGRWvaahhpftm 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 441 -----------QDQVNAKAAGDD---------------------EAMF----YDEDYV--------TALEYGLPPTAGLG 476
Cdd:PRK00476 454 pkdedldeletTDPGKARAYAYDlvlngyelgggsirihrpeiqEKVFeilgISEEEAeekfgfllDALKYGAPPHGGIA 533
|
570 580
....*....|....*....|...
gi 1082303951 477 IGIDRMVMLFTNSHTIRDVILFP 499
Cdd:PRK00476 534 FGLDRLVMLLAGADSIRDVIAFP 556
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
41-499 |
4.80e-28 |
|
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: 117.79 E-value: 4.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 41 RRDHTSDQLhaefDAKDNDElaslnvEVAVAGRMMTRRVMGKASFVTLQDVGGRIQLyVARDDLPEGVYnEQFKKWDLGD 120
Cdd:COG0173 2 YRTHYCGEL----RESDVGQ------EVTLSGWVHRRRDHGGLIFIDLRDRYGITQV-VFDPDDSAEAF-EKAEKLRSEY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 121 IIAARGKLF---------KTQTGELSIHCTELRLLTKAlRPLPdkFHgLQDQ-----EVRYRQRYLDLiANEESRHTFRI 186
Cdd:COG0173 70 VIAVTGKVRarpegtvnpKLPTGEIEVLASELEILNKA-KTPP--FQ-IDDDtdvseELRLKYRYLDL-RRPEMQKNLIL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 187 RSQILATMRQFMVARGFMEVETPMMqvipgGAS----ARpfithhnalDldmYL---RI----------APELYLKRLVV 249
Cdd:COG0173 145 RHKVTKAIRNYLDENGFLEIETPIL-----TKStpegAR---------D---YLvpsRVhpgkfyalpqSPQLFKQLLMV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 250 GGFERVFEINRNFRNEgiSVRHN--PEFTMMELYMAYADYKDLIELTESLFRTLAQTVLGKtevpygdqvfDFGKPFEKL 327
Cdd:COG0173 208 SGFDRYFQIARCFRDE--DLRADrqPEFTQLDIEMSFVDQEDVFELMEGLIRHLFKEVLGV----------ELPTPFPRM 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 328 TMREAIKKH---RPET----NMADLDN---------FDAA-------KAL-------------------AESLG------ 359
Cdd:COG0173 276 TYAEAMERYgsdKPDLrfglELVDVTDifkdsgfkvFAGAaenggrvKAInvpggaslsrkqideltefAKQYGakglay 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 360 IQVEKSwGLGRIVTEIFDEVAEAHLIQPT---------FITEYPAEVSP--------LARRNDVNPE-------ITD--- 412
Cdd:COG0173 356 IKVNED-GLKSPIAKFLSEEELAAILERLgakpgdlifFVADKPKVVNKalgalrlkLGKELGLIDEdefaflwVVDfpl 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 413 --------RFEF----F--------------------------IGGREIGNGFSELNDAEDQAQRFqdqvnaKAAG--DD 452
Cdd:COG0173 435 feydeeegRWVAmhhpFtmpkdedldlletdpgkvrakaydlvLNGYELGGGSIRIHDPELQEKVF------ELLGisEE 508
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1082303951 453 EAM-----FYDedyvtALEYGLPPTAGLGIGIDRMVMLFTNSHTIRDVILFP 499
Cdd:COG0173 509 EAEekfgfLLE-----AFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
41-499 |
1.11e-27 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 116.81 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 41 RRDHTSDQLhaefdaKDNDELAslnvEVAVAGRMMTRRVMGKASFVTLQDVGGRIQLYVARDDLPEGVynEQFKKWDLGD 120
Cdd:PLN02903 58 SRSHLCGAL------SVNDVGS----RVTLCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDEFPEAH--RTANRLRNEY 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 121 IIAARGKLF---------KTQTGELSIHCTELRLLTKALRPLPDKFHGLQDQ------EVRYRQRYLDLIANEESRHtFR 185
Cdd:PLN02903 126 VVAVEGTVRsrpqespnkKMKTGSVEVVAESVDILNVVTKSLPFLVTTADEQkdsikeEVRLRYRVLDLRRPQMNAN-LR 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 186 IRSQILATMRQFMVAR-GFMEVETPMM-QVIPGGAsaRPFITHHNALDLDMY-LRIAPELYLKRLVVGGFERVFEINRNF 262
Cdd:PLN02903 205 LRHRVVKLIRRYLEDVhGFVEIETPILsRSTPEGA--RDYLVPSRVQPGTFYaLPQSPQLFKQMLMVSGFDRYYQIARCF 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 263 RNEGISVRHNPEFTMMELYMAYADYKDLIELTESLFRTLAQTVLG----------------------KTEVPYGDQVFDF 320
Cdd:PLN02903 283 RDEDLRADRQPEFTQLDMELAFTPLEDMLKLNEDLIRQVFKEIKGvqlpnpfprltyaeamskygsdKPDLRYGLELVDV 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 321 GKPFEKLTMR------------------------------------EAIK---KHRPETNMADLDNFDAAKALAESLGIQ 361
Cdd:PLN02903 363 SDVFAESSFKvfagalesggvvkaicvpdgkkisnntalkkgdiynEAIKsgaKGLAFLKVLDDGELEGIKALVESLSPE 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 362 VEK------SWGLGRI----------VTEIFDEV-----AEAHLIQPT-----FITEYPA-EVSPLARRNDV-------- 406
Cdd:PLN02903 443 QAEqllaacGAGPGDLilfaagptssVNKTLDRLrqfiaKTLDLIDPSrhsilWVTDFPMfEWNEDEQRLEAlhhpftap 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 407 NPEITD--------RFEFFIGGREIGNGFSELNDAEDQaQRFQDQVNAKAAGDDEAMFYdedYVTALEYGLPPTAGLGIG 478
Cdd:PLN02903 523 NPEDMGdlssaralAYDMVYNGVEIGGGSLRIYRRDVQ-QKVLEAIGLSPEEAESKFGY---LLEALDMGAPPHGGIAYG 598
|
570 580
....*....|....*....|.
gi 1082303951 479 IDRMVMLFTNSHTIRDVILFP 499
Cdd:PLN02903 599 LDRLVMLLAGAKSIRDVIAFP 619
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
186-482 |
4.42e-27 |
|
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: 108.36 E-value: 4.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 186 IRSQILATMRQFMVARGFMEVETPMMQVIPGGASAR----PFITHHNALDLDMYLRIAPELYLKRLVVG----GFERVFE 257
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGhepkDLLPVGAENEEDLYLRPTLEPGLVRLFVShirkLPLRLAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 258 INRNFRNEGISV--RHNPEFTMMELYMAYAD------YKDLIELTESLFRTLAQtvlgktevpygdqvfdfgkpfekltm 329
Cdd:cd00768 81 IGPAFRNEGGRRglRRVREFTQLEGEVFGEDgeeaseFEELIELTEELLRALGI-------------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 330 reaikkhrpetnmadldnfdaakalaeslgiqvekswglgrivteifdevaeahLIQPTFITEYPAEVSPlarrndvnPE 409
Cdd:cd00768 135 ------------------------------------------------------KLDIVFVEKTPGEFSP--------GG 152
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082303951 410 ITDRFEFFI-----GGREIGNGFSELNDAEDQAQRFqdqvnakaagddeamfydeDYVTALEYGLPPTAGLGIGIDRM 482
Cdd:cd00768 153 AGPGFEIEVdhpegRGLEIGSGGYRQDEQARAADLY-------------------FLDEALEYRYPPTIGFGLGLERL 211
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
67-502 |
9.97e-25 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 108.15 E-value: 9.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 67 EVAVAGRMMTRRVMGKASFVTLQDVGGRIQLYVARDDLPEGVYnEQFKKWDLGDIIAARGKLFK---------TQTGELS 137
Cdd:PRK12820 20 EVCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFSPEAAPADVY-ELAASLRAEFCVALQGEVQKrleetenphIETGDIE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 138 IHCTELRLLTKALR---PLPDKF------HGLQD---QEVRYRQRYLDLIANEESRHTFRiRSQILATMRQFMVARGFME 205
Cdd:PRK12820 99 VFVRELSILAASEAlpfAISDKAmtagagSAGADavnEDLRLQYRYLDIRRPAMQDHLAK-RHRIIKCARDFLDSRGFLE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 206 VETPMMQV-IPGGAsaRPFITHHNALDLDMY-LRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMA 283
Cdd:PRK12820 178 IETPILTKsTPEGA--RDYLVPSRIHPKEFYaLPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEFTQLDIEAS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 284 YADYKDLIELTESLfrTLAQTVLGKTEVPygdqvfdfgKPFEKLTMREAIKKH---RPET----NMADLDNF-------- 348
Cdd:PRK12820 256 FIDEEFIFELIEEL--TARMFAIGGIALP---------RPFPRMPYAEAMDTTgsdRPDLrfdlKFADATDIfentrygi 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 349 ------------------------------DAAKALAESLG------IQVEKSwGLGRIVTEIFDE-------------- 378
Cdd:PRK12820 325 fkqilqrggrikginikgqseklsknvlqnEYAKEIAPSFGakgmtwMRAEAG-GLDSNIVQFFSAdekealkrrfhaed 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 379 ------VAEA--------------HL-----------IQPTFITEYP-----------AEVSPLAR--RNDVNP----EI 410
Cdd:PRK12820 404 gdviimIADAscaivlsalgqlrlHLadrlglipegvFHPLWITDFPlfeatddggvtSSHHPFTApdREDFDPgdieEL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 411 TD----RFEFFIGGREIGNGFSELNDAEDQAQRFqdqvnaKAAGDDEAMFYDE--DYVTALEYGLPPTAGLGIGIDRMVM 484
Cdd:PRK12820 484 LDlrsrAYDLVVNGEELGGGSIRINDKDIQLRIF------AALGLSEEDIEDKfgFFLRAFDFAAPPHGGIALGLDRVVS 557
|
570
....*....|....*...
gi 1082303951 485 LFTNSHTIRDVILFPAMR 502
Cdd:PRK12820 558 MILQTPSIREVIAFPKNR 575
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
175-499 |
1.22e-24 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 104.72 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 175 IANEESRHTFRIRSQILATMRQFMVARGFMEVETPMMQVI-----PGGASARPFITHHNALDLDMYLRIAPELYlKRLVV 249
Cdd:PRK06462 21 ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIISPStdplmGLGSDLPVKQISIDFYGVEYYLADSMILH-KQLAL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 250 GGFERVFEINRNFRNEG---ISVRHNPEFTMMELYMAYADYKDLIELTESLFRTLAQTVLGKtevpYGDQVFDFG----- 321
Cdd:PRK06462 100 RMLGKIFYLSPNFRLEPvdkDTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEE----HEDELEFFGrdlph 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 322 --KPFEKLTMREAIKkhrpetnmaDLDNFDAAKALAESLGIQVEKSwglgriVTEIFDEvaeahliqPTFITEYPAEVSP 399
Cdd:PRK06462 176 lkRPFKRITHKEAVE---------ILNEEGCRGIDLEELGSEGEKS------LSEHFEE--------PFWIIDIPKGSRE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 400 LARRNDvnPEITDRFEFF--IggreIGNGFSELNDA---EDQAQRFQDQVnaKAAGDDEAMFydEDYVTALEYGLPPTAG 474
Cdd:PRK06462 233 FYDRED--PERPGVLRNYdlL----LPEGYGEAVSGgerEYEYEEIVERI--REHGVDPEKY--KWYLEMAKEGPLPSAG 302
|
330 340
....*....|....*....|....*
gi 1082303951 475 LGIGIDRMVMLFTNSHTIRDVILFP 499
Cdd:PRK06462 303 FGIGVERLTRYICGLRHIREVQPFP 327
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
68-505 |
2.99e-24 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 106.23 E-value: 2.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 68 VAVAGRMMTRRVMGKASFVTLQDVGGRIQLYVA-RDDLPEGV--YNEQFKKWDLGDIIA----ARGKLFKTQTGELSIHC 140
Cdd:PTZ00401 81 VLIRARVSTTRKKGKMAFMVLRDGSDSVQAMAAvEGDVPKEMidFIGQIPTESIVDVEAtvckVEQPITSTSHSDIELKV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 141 TELRLLTKALRPLPDKFHGLQDQE----------VRYRQRYLDLiANEESRHTFRIRSQILATMRQFMVARGFMEVETPM 210
Cdd:PTZ00401 161 KKIHTVTESLRTLPFTLEDASRKEsdegakvnfdTRLNSRWMDL-RTPASGAIFRLQSRVCQYFRQFLIDSDFCEIHSPK 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 211 MQVIPGGASARPFITHHnaLDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISV-RHNPEFTMMELYMAYAD-YK 288
Cdd:PTZ00401 240 IINAPSEGGANVFKLEY--FNRFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNThRHLTEFVGLDVEMRINEhYY 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 289 DLIELTESLFRTLAQTVLGKT-EVPYGDQVFdfgkPFEKL-------TMRE--------------------------AIK 334
Cdd:PTZ00401 318 EVLDLAESLFNYIFERLATHTkELKAVCQQY----PFEPLvwkltpeRMKElgvgvisegveptdkyqarvhnmdsrMLR 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 335 KHRP----------ETNMADLDNFDAAKalAESLGIQVEKSWGLGRIVTEIFDEVAeahliQPTFITEYPaevsplarrN 404
Cdd:PTZ00401 394 INYMhciellntvlEEKMAPTDDINTTN--EKLLGKLVKERYGTDFFISDRFPSSA-----RPFYTMECK---------D 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 405 DVnpEITDRFEFFIGGREIGNGFSELNDAEDQAQRfqdqvnAKAAGDDEAMFydEDYVTALEYGLPPTAGLGIGIDRMVM 484
Cdd:PTZ00401 458 DE--RFTNSYDMFIRGEEISSGAQRIHDPDLLLAR------AKMLNVDLTPI--KEYVDSFRLGAWPHGGFGVGLERVVM 527
|
490 500
....*....|....*....|.
gi 1082303951 485 LFTNSHTIRDVILFPaMRPQK 505
Cdd:PTZ00401 528 LYLGLSNVRLASLFP-RDPQR 547
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
67-499 |
1.22e-19 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 91.32 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 67 EVAVAGRMMTRRVMGKASFVTLQDVGGRIQLYVARDDLPEgvYNEQFKKWDLGDIIAARGKLFKTQT--GELSIHCTELR 144
Cdd:PRK03932 18 EVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDNGEE--YFEEIKKLTTGSSVIVTGTVVESPRagQGYELQATKIE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 145 LLTKALR--PLPDKFHGLQdqevryrqrYLDLIANEESRH-----TFRIRSQILATMRQFMVARGFMEVETPMmqvipgg 217
Cdd:PRK03932 96 VIGEDPEdyPIQKKRHSIE---------FLREIAHLRPRTnkfgaVMRIRNTLAQAIHEFFNENGFVWVDTPI------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 218 asarpfITHHNA-----------LDLDM---------YLRIAPELYLKRLVVgGFERVFEINRNFRNEGiS--VRHNPEF 275
Cdd:PRK03932 160 ------ITASDCegagelfrvttLDLDFskdffgkeaYLTVSGQLYAEAYAM-ALGKVYTFGPTFRAEN-SntRRHLAEF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 276 TMMELYMAYADYKDLIELTESLFRTLAQTVL--GKTEVPYGDQVFDFG----------KPFEKLTMREAIKKhrpetnma 343
Cdd:PRK03932 232 WMIEPEMAFADLEDNMDLAEEMLKYVVKYVLenCPDDLEFLNRRVDKGdierlenfieSPFPRITYTEAIEI-------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 344 dldnfdaakaLAESlGIQVEK--SWG--LG----RIVTE-IFDevaeahliQPTFITEYPAEVSPL-ARRNDVN------ 407
Cdd:PRK03932 304 ----------LQKS-GKKFEFpvEWGddLGseheRYLAEeHFK--------KPVFVTNYPKDIKAFyMRLNPDGktvaam 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 408 ----P---EItdrfeffIGG--REigngfselNDAEDQAQRFQDQvnakaaGDDEamfydEDYVTALE---YGLPPTAGL 475
Cdd:PRK03932 365 dllaPgigEI-------IGGsqRE--------ERLDVLEARIKEL------GLNK-----EDYWWYLDlrrYGSVPHSGF 418
|
490 500
....*....|....*....|....
gi 1082303951 476 GIGIDRMVMLFTNSHTIRDVILFP 499
Cdd:PRK03932 419 GLGFERLVAYITGLDNIRDVIPFP 442
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
67-148 |
1.06e-17 |
|
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. Class 2b aaRSs include the homodimeric aspartyl-, asparaginyl-, and lysyl-tRNA synthetases (AspRS, AsnRS, and LysRS). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Included in this group are archeal and archeal-like AspRSs which are non-discriminating and can charge both tRNAAsp and tRNAAsn. E. coli cells have two isoforms of LysRSs (LysS and LysU) encoded by two distinct genes, which are differentially regulated. The cytoplasmic and the mitochondrial isoforms of human LysRS are encoded by a single gene. Yeast cytoplasmic and mitochondrial LysRSs participate in mitochondrial import of cytoplasmic tRNAlysCUU. In addition to their housekeeping role, human LysRS may function as a signaling molecule that activates immune cells. Tomato LysRS may participate in a process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging. AsnRS is immunodominant antigen of the filarial nematode Brugia malayai and is of interest as a target for anti-parasitic drug design. Human AsnRS has been shown to be a pro-inflammatory chemokine which interacts with CCR3 chemokine receptors on T cells, immature dendritic cells and macrophages.
Pssm-ID: 239766 [Multi-domain] Cd Length: 85 Bit Score: 77.61 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 67 EVAVAGRMMTRRVMGKASFVTLQDVGGRIQLYVARDDLPEGVynEQFKKWDLGDIIAARGKLFKTQ-----TGELSIHCT 141
Cdd:cd04100 1 EVTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEELGEFF--EEAEKLRTESVVGVTGTVVKRPegnlaTGEIELQAE 78
|
....*..
gi 1082303951 142 ELRLLTK 148
Cdd:cd04100 79 ELEVLSK 85
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
68-146 |
1.38e-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: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 68 VAVAGRMMT-RRVMGKASFVTLQDVGGRIQLYVarddlPEGVYNEQFKKWDLGDIIAARGKLFKTQTGELSIHCTELRLL 146
Cdd:pfam01336 1 VTVAGRVTSiRRSGGKLLFLTLRDGTGSIQVVV-----FKEEAEKLAKKLKEGDVVRVTGKVKKRKGGELELVVEEIELL 75
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
235-499 |
2.56e-10 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 62.73 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 235 YLRIAPELYLKRLVvGGFERVFEINRNFRNEGI-SVRHNPEFTMMELYMAYADYKDLIELTESLFRTLAQTVLGKTevpy 313
Cdd:PTZ00425 327 FLTVSGQLSLENLC-SSMGDVYTFGPTFRAENShTSRHLAEFWMIEPEIAFADLYDNMELAESYIKYCIGYVLNNN---- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 314 gdqvFDFGKPFEKLTMREAIKKHRpetNMADlDNF---------DAAKALAESLGIQVEksWGLGrIVTEIFDEVAEAHL 384
Cdd:PTZ00425 402 ----FDDIYYFEENVETGLISRLK---NILD-EDFakitytnviDLLQPYSDSFEVPVK--WGMD-LQSEHERFVAEQIF 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 385 IQPTFITEYPAEVSPLARRNDVNPEITDRFEFFIG--GREIGNgfselNDAEDQAQRFQDQVNAKAAGDDEAMFYDEdyv 462
Cdd:PTZ00425 471 KKPVIVYNYPKDLKAFYMKLNEDQKTVAAMDVLVPkiGEVIGG-----SQREDNLERLDKMIKEKKLNMESYWWYRQ--- 542
|
250 260 270
....*....|....*....|....*....|....*..
gi 1082303951 463 tALEYGLPPTAGLGIGIDRMVMLFTNSHTIRDVILFP 499
Cdd:PTZ00425 543 -LRKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFP 578
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
42-174 |
1.26e-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: 50.60 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 42 RDHTSDQLhaefDAKDNDElaslnvEVAVAGRMMTRRVMGKASFVTLQDVGGRIQLYVARDDLPEgvyNEQFKKWDLGDI 121
Cdd:cd04317 1 RTHYCGEL----RESHVGQ------EVTLCGWVQRRRDHGGLIFIDLRDRYGIVQVVFDPEEAPE---FELAEKLRNESV 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082303951 122 IAARGKLF---------KTQTGELSIHCTELRLLTKAlRPLP----DKFHGlqDQEVRYRQRYLDL 174
Cdd:cd04317 68 IQVTGKVRarpegtvnpKLPTGEIEVVASELEVLNKA-KTLPfeidDDVNV--SEELRLKYRYLDL 130
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
255-499 |
1.43e-06 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 50.74 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 255 VFEINRNFRNEGISV-RHNPEFTMMELYMAYADYKDLIELTESLFRTLAQTVLGKTEvpyGDQVFdFGKPFEKLTMREAi 333
Cdd:PLN02603 324 VYTFGPTFRAENSNTsRHLAEFWMIEPELAFADLNDDMACATAYLQYVVKYILENCK---EDMEF-FNTWIEKGIIDRL- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 334 kKHRPETNMADLDNFDAAKALAES-LGIQVEKSWGLG------RIVTEifdevaEAHLIQPTFITEYPAEVSPL-ARRND 405
Cdd:PLN02603 399 -SDVVEKNFVQLSYTDAIELLLKAkKKFEFPVKWGLDlqseheRYITE------EAFGGRPVIIRDYPKEIKAFyMREND 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 406 VNPEIT------DRFEFFIGGREigngfselndAEDQAQRFQDQVnakaagdDEAMFYDEDYVTALE---YGLPPTAGLG 476
Cdd:PLN02603 472 DGKTVAamdmlvPRVGELIGGSQ----------REERLEYLEARL-------DELKLNKESYWWYLDlrrYGSVPHAGFG 534
|
250 260
....*....|....*....|...
gi 1082303951 477 IGIDRMVMLFTNSHTIRDVILFP 499
Cdd:PLN02603 535 LGFERLVQFATGIDNIRDAIPFP 557
|
|
| pylS |
PRK09537 |
pyrrolysine--tRNA(Pyl) ligase; |
154-278 |
3.75e-06 |
|
pyrrolysine--tRNA(Pyl) ligase;
Pssm-ID: 236555 [Multi-domain] Cd Length: 417 Bit Score: 49.07 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 154 PDKFHGLQDQEVRYRQRYLDLIANEESRHTFrirSQILATMRQFMVARGFMEVETPMMqvIPGGASARPFITHHNAL--- 230
Cdd:PRK09537 176 KPKFKELESELVSRRKNDLKQMYEEDREDYL---GKLERDITKFFVDRGFLEIKSPIL--IPAEYIERMGIDNDTELskq 250
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1082303951 231 ----DLDMYLR--IAPELY--LKRL--VVGGFERVFEINRNFRNEGISVRHNPEFTMM 278
Cdd:PRK09537 251 ifrvDKNFCLRpmLAPGLYnyLRKLdrILPDPIKIFEIGPCYRKESDGKEHLEEFTMV 308
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
67-155 |
1.28e-04 |
|
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: 41.15 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082303951 67 EVAVAGRMMTRRVMGKASFVTLQDVGGRIQLyVARDDLPEGVYNEQFKKWDLGDIIAARGKLF---KTQTGeLSIHCTEL 143
Cdd:cd04316 14 EVTVAGWVHEIRDLGGIKFVILRDREGIVQV-TAPKKKVDKELFKTVRKLSRESVISVTGTVKaepKAPNG-VEIIPEEI 91
|
90
....*....|..
gi 1082303951 144 RLLTKALRPLPD 155
Cdd:cd04316 92 EVLSEAKTPLPL 103
|
|
| |
