|
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: 994.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 1 MSEQETRGANEAIDFNDELRNRREKLAALRQQGVAFPNDFRRDHTSDQLHEEFDAKDNQELESLNIEVSVAGRMMTRRIM 80
Cdd:PRK12445 1 MSEQETRGANEAIDFNDELRNRREKLAALRQQGVAFPNDFRRDHTSDQLHEEFDAKDNQELESLNIEVSVAGRMMTRRIM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 81 GKASFVTLQDVGGRIQLYVARDSLPEGVYNDQFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFHGL 160
Cdd:PRK12445 81 GKASFVTLQDVGGRIQLYVARDSLPEGVYNDQFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFHGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 161 QDQEVRYRQRYLDLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAP 240
Cdd:PRK12445 161 QDQEVRYRQRYLDLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 241 ELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFDF 320
Cdd:PRK12445 241 ELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFDF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 321 GKPFEKLTMREAIKKYRPETDMADLDNFDAAKALAESIGITVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPL 400
Cdd:PRK12445 321 GKPFEKLTMREAIKKYRPETDMADLDNFDAAKALAESIGITVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 401 ARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGID 480
Cdd:PRK12445 401 ARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGID 480
|
490 500
....*....|....*....|....*
gi 15834365 481 RMIMLFTNSHTIRDVILFPAMRPQK 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: 961.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 14 DFNDELRNRREKLAALRQQGVA-FPNDFRRDHTSDQLHEEFDAKDNQELESLNIEVSVAGRMMTRRIMGKASFVTLQDVG 92
Cdd:PRK00484 2 ELNEQIAVRREKLAELREQGIDpYPNKFERTHTAAELRAKYDDKEKEELEELEIEVSVAGRVMLKRVMGKASFATLQDGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 93 GRIQLYVARDSLPEGVYnDQFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFHGLQDQEVRYRQRYL 172
Cdd:PRK00484 82 GRIQLYVSKDDVGEEAL-EAFKKLDLGDIIGVEGTLFKTKTGELSVKATELTLLTKSLRPLPDKFHGLTDVETRYRQRYV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 173 DLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGF 252
Cdd:PRK00484 161 DLIVNPESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARPFITHHNALDIDLYLRIAPELYLKRLIVGGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 253 ERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFDFGKPFEKLTMREA 332
Cdd:PRK00484 241 ERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTYQGTEIDFGPPFKRLTMVDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 333 IKKYrpetDMADLD--NFDAAKALAESIGITVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEI 410
Cdd:PRK00484 321 IKEY----TGVDFDdmTDEEARALAKELGIEVEKSWGLGKLINELFEEFVEPKLIQPTFITDYPVEISPLAKRHREDPGL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 411 TDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSH 490
Cdd:PRK00484 397 TERFELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSP 476
|
490
....*....|....*
gi 15834365 491 TIRDVILFPAMRPQK 505
Cdd:PRK00484 477 SIRDVILFPLMRPEK 491
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
10-505 |
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: 936.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 10 NEAIDFNDELRNRREKLAALRQQGV-AFPNDFRRDHTSDQLHEEFDAKDNQELEslNIEVSVAGRMMTRRIMGKASFVTL 88
Cdd:COG1190 2 SEEEDLNEQIRVRREKLEELREAGIdPYPNKFPRTHTAAEIREKYDELEAEEET--GDEVSVAGRIMAKRDMGKASFADL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 89 QDVGGRIQLYVARDSLPEGVYnDQFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFHGLQDQEVRYR 168
Cdd:COG1190 80 QDGSGRIQLYLRRDELGEEAY-ELFKLLDLGDIVGVEGTVFRTKTGELSVKVEELTLLSKSLRPLPEKFHGLTDPETRYR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 169 QRYLDLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLV 248
Cdd:COG1190 159 QRYVDLIVNPEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 249 VGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFDFGKPFEKLT 328
Cdd:COG1190 239 VGGFERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGTTKVTYQGQEIDLSPPWRRIT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 329 MREAIKKYRpETDMADLDNFDAAKALAESIGITVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDVNP 408
Cdd:COG1190 319 MVEAIKEAT-GIDVTPLTDDEELRALAKELGIEVDPGWGRGKLIDELFEELVEPKLIQPTFVTDYPVEVSPLAKRHRDDP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 409 EITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTN 488
Cdd:COG1190 398 GLTERFELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTD 477
|
490
....*....|....*..
gi 15834365 489 SHTIRDVILFPAMRPQK 505
Cdd:COG1190 478 SPSIRDVILFPLMRPEK 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: 727.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 14 DFNDELRNRREKLAALRQQGV-AFPNDFRRDHTSDQLHEEFDAKDNQELESLNIEVSVAGRMMTRRIMGKASFVTLQDVG 92
Cdd:TIGR00499 1 ELNDQAQQRLEKLNRLRQTGNnPYLHKFERTHSAQEFQEKYADLSNEELKEKELKVSIAGRIKAIRSMGKATFITLQDES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 93 GRIQLYVARDSLPEGVYNDQFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFHGLQDQEVRYRQRYL 172
Cdd:TIGR00499 81 GQIQLYVNKNKLPEDFYEFDEYLLDLGDIIGVTGYPFKTKTGELSVKVTELQILTKCLQPLPDKWHGLTDQETRYRQRYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 173 DLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGF 252
Cdd:TIGR00499 161 DLIVNPDVRQTFLKRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKPFITHHNALDMDLYLRIAPELYLKRLIVGGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 253 ERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFDFGKPFEKLTMREA 332
Cdd:TIGR00499 241 EKVYEIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTFIINYNDLEIDLKPPWKRITMVDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 333 IKKYRPeTDMADLDNFDAAKALAESIGITV-EKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEIT 411
Cdd:TIGR00499 321 LEMVTG-IDFDILKDDETAKALAKEHGIEVaEDSLTLGHILNKFFEQFLEHTLIQPTFITHYPAEISPLAKRDPSNPEFT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 412 DRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHT 491
Cdd:TIGR00499 400 ERFELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGIGIDRLVMLLTDAPS 479
|
490
....*....|....
gi 15834365 492 IRDVILFPAMRPQK 505
Cdd:TIGR00499 480 IRDVLLFPQLRPQK 493
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
21-504 |
0e+00 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 647.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 21 NRREKLAALRQQGV-AFPNDFRRDHTSDQLHEEFDAKDN-QELEslNIEVSVAGRMMTRRIMGKASFVTLQDVGGRIQLY 98
Cdd:PLN02502 64 NRLKKVEALRAKGVePYPYKFDVTHTAPELQEKYGSLENgEELE--DVSVSVAGRIMAKRAFGKLAFYDLRDDGGKIQLY 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 99 VARDSLpeGVYNDQFKKW----DLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFHGLQDQEVRYRQRYLDL 174
Cdd:PLN02502 142 ADKKRL--DLDEEEFEKLhslvDRGDIVGVTGTPGKTKKGELSIFPTSFEVLTKCLLMLPDKYHGLTDQETRYRQRYLDL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 175 IANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGFER 254
Cdd:PLN02502 220 IANPEVRDIFRTRAKIISYIRRFLDDRGFLEVETPMLNMIAGGAAARPFVTHHNDLNMDLYLRIATELHLKRLVVGGFER 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 255 VFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFDFGKPFEKLTMREAIK 334
Cdd:PLN02502 300 VYEIGRQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKELTGSYKIKYHGIEIDFTPPFRRISMISLVE 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 335 KYRPETDMADLDNFDAAKALA---ESIGITVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEIT 411
Cdd:PLN02502 380 EATGIDFPADLKSDEANAYLIaacEKFDVKCPPPQTTGRLLNELFEEFLEETLVQPTFVLDHPVEMSPLAKPHRSKPGLT 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 412 DRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHT 491
Cdd:PLN02502 460 ERFELFINGRELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRLVMLLTDSAS 539
|
490
....*....|...
gi 15834365 492 IRDVILFPAMRPQ 504
Cdd:PLN02502 540 IRDVIAFPAMKPQ 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: 601.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 177 NDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGFERVF 256
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 257 EINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFDFGKPFEKLTMREAIKKY 336
Cdd:cd00775 81 EIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIEYGGKELDFTPPFKRVTMVDALKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 337 RPETDM--ADLDNFDAAKALAESIGITVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEITDRF 414
Cdd:cd00775 161 TGIDFPelDLEQPEELAKLLAKLIKEKIEKPRTLGKLLDKLFEEFVEPTLIQPTFIIDHPVEISPLAKRHRSNPGLTERF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 415 EFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRD 494
Cdd:cd00775 241 ELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLTDSNSIRD 320
|
....*....
gi 15834365 495 VILFPAMRP 503
Cdd:cd00775 321 VILFPAMRP 329
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
20-505 |
5.32e-173 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 516.44 E-value: 5.32e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 20 RNRREKLAALRQQGV-AFPNDFRRDHTsdqLHEEFDAKDNQEleslnieVSVAGRMMTRRIMGKASFVTLQDVGGRIQLY 98
Cdd:PRK02983 615 RVRLAKLEALRAAGVdPYPVGVPPTHT---VAEALDAPTGEE-------VSVSGRVLRIRDYGGVLFADLRDWSGELQVL 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 99 VARDSLPEGVYNDQFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFHGLQDQEVRYRQRYLDLIAND 178
Cdd:PRK02983 685 LDASRLEQGSLADFRAAVDLGDLVEVTGTMGTSRNGTLSLLVTSWRLAGKCLRPLPDKWKGLTDPEARVRQRYLDLAVNP 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 179 KSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGFERVFEI 258
Cdd:PRK02983 765 EARDLLRARSAVVRAVRETLVARGFLEVETPILQQVHGGANARPFVTHINAYDMDLYLRIAPELYLKRLCVGGVERVFEL 844
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 259 NRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVT-----YGEHVFDFGKPFEKLTMREAI 333
Cdd:PRK02983 845 GRNFRNEGVDATHNPEFTLLEAYQAHADYDTMRDLTRELIQNAAQAAHGAPVVMrpdgdGVLEPVDISGPWPVVTVHDAV 924
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 334 -----KKYRPETDMADLdnfdaaKALAESIGITVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDVNP 408
Cdd:PRK02983 925 sealgEEIDPDTPLAEL------RKLCDAAGIPYRTDWDAGAVVLELYEHLVEDRTTFPTFYTDFPTSVSPLTRPHRSDP 998
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 409 EITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTN 488
Cdd:PRK02983 999 GLAERWDLVAWGVELGTAYSELTDPVEQRRRLTEQSLLAAGGDPEAMELDEDFLQALEYAMPPTGGLGMGVDRLVMLLTG 1078
|
490
....*....|....*..
gi 15834365 489 ShTIRDVILFPAMRPQK 505
Cdd:PRK02983 1079 R-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 |
1.19e-147 |
|
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: 423.43 E-value: 1.19e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 184 FVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGFERVFEINRNFR 263
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 264 NEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFDFGKPFEKLTMREAIKKYRPetdma 343
Cdd:cd00669 81 NEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYGFELEDFGLPFPRLTYREALERYGQ----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 344 dldnfdaakalaesigitvekswglgrivteifdevaeahliqPTFITEYPAE-VSPLARRNDVNPEITDRFEFFIGGRE 422
Cdd:cd00669 156 -------------------------------------------PLFLTDYPAEmHSPLASPHDVNPEIADAFDLFINGVE 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 423 IGNGFSELNDAEDQAERFQEQVNAKAAGddeaMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFPAMR 502
Cdd:cd00669 193 VGNGSSRLHDPDIQAEVFQEQGINKEAG----MEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKMR 268
|
.
gi 15834365 503 P 503
Cdd:cd00669 269 R 269
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
21-503 |
2.31e-135 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 403.62 E-value: 2.31e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 21 NRREKLAALRQQGV-AFPNDFRRDHTSDQLHEEF-DAKDNQELEslNIEVSVAGRMMTRRIMG-KASFVTLQDVGGRIQL 97
Cdd:PTZ00417 88 NRSKFIQEQKAKGInPYPHKFERTITVPEFVEKYqDLASGEHLE--DTILNVTGRIMRVSASGqKLRFFDLVGDGAKIQV 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 98 YV--ARDSLPEGVYNDQFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFhGLQDQEVRYRQRYLDLI 175
Cdd:PTZ00417 166 LAnfAFHDHTKSNFAECYDKIRRGDIVGIVGFPGKSKKGELSIFPKETIILSPCLHMLPMKY-GLKDTEIRYRQRYLDLM 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 176 ANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGFERV 255
Cdd:PTZ00417 245 INESTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLVAGGANARPFITHHNDLDLDLYLRIATELPLKMLIVGGIDKV 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 256 FEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEH-------VFDFGKPFEKLT 328
Cdd:PTZ00417 325 YEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHLFGTYKILYNKDgpekdpiEIDFTPPYPKVS 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 329 MREAIKKYrpeTDMADLDNFDAAKALAESIGITVEKSWGLGRIVT--EIFDEVAeAHLI------QPTFITEYPAEVSPL 400
Cdd:PTZ00417 405 IVEELEKL---TNTKLEQPFDSPETINKMINLIKENKIEMPNPPTaaKLLDQLA-SHFIenkypnKPFFIIEHPQIMSPL 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 401 ARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGID 480
Cdd:PTZ00417 481 AKYHRSKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCTSLEYGLPPTGGLGLGID 560
|
490 500
....*....|....*....|...
gi 15834365 481 RMIMLFTNSHTIRDVILFPAMRP 503
Cdd:PTZ00417 561 RITMFLTNKNCIKDVILFPTMRP 583
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
162-502 |
9.39e-125 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 366.89 E-value: 9.39e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 162 DQEVRYRQRYLDLIaNDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPE 241
Cdd:pfam00152 1 DEETRLKYRYLDLR-RPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 242 LYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFDFG 321
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 322 KPFEKLTMREAIKKYRPETDMADLDNFDAAKAlaesigitvekswglgRIVTEIfdeVAEAHLIQPTFITEYPAEVSPLA 401
Cdd:pfam00152 160 KPFPRITYAEAIEKLNGKDVEELGYGSDKPDL----------------RFLLEL---VIDKNKFNPLWVTDFPAEHHPFT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 402 RRNDVN-PEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKaagdDEAMFYDEDYVTALEYGLPPTAGLGIGID 480
Cdd:pfam00152 221 MPKDEDdPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDP----EEAEEKFGFYLDALKYGAPPHGGLGIGLD 296
|
330 340
....*....|....*....|..
gi 15834365 481 RMIMLFTNSHTIRDVILFPAMR 502
Cdd:pfam00152 297 RLVMLLTGLESIREVIAFPKTR 318
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
40-502 |
5.23e-118 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 361.66 E-value: 5.23e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 40 FRRDHTSDQLHEEFDAKDNQELESlNIEVSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVardSLPEGVYNDQFKKWD-- 117
Cdd:PTZ00385 83 FRGITPISEVRERYGYLASGDRAA-QATVRVAGRVTSVRDIGKIIFVTIRSNGNELQVVG---QVGEHFTREDLKKLKvs 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 118 --LGDIIGARGTLFKTQTGELSIHCTELRLLT------KALRPLPDKFHGLQDQEVRYRQRYLDLIANDKSRQTFVVRSK 189
Cdd:PTZ00385 159 lrVGDIIGADGVPCRMQRGELSVAASRMLILSpyvctdQVVCPNLRGFTVLQDNDVKYRYRFTDMMTNPCVIETIKKRHV 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 190 ILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISV 269
Cdd:PTZ00385 239 MLQALRDYFNERNFVEVETPVLHTVASGANAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDADR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 270 RHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVT-YGEHV------FDFGKPFEKLTMREAIKKYRpETDM 342
Cdd:PTZ00385 319 SHNPEFTSCEFYAAYHTYEDLMPMTEDIFRQLAMRVNGTTVVQiYPENAhgnpvtVDLGKPFRRVSVYDEIQRMS-GVEF 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 343 ADLDNFDAAKALAESIGITVEKSWGLG--RIVTEIFDEVAE----AHLIQPTFITEYPAEVSPLARRNDVNPEITDRFEF 416
Cdd:PTZ00385 398 PPPNELNTPKGIAYMSVVMLRYNIPLPpvRTAAKMFEKLIDffitDRVVEPTFVMDHPLFMSPLAKEQVSRPGLAERFEL 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 417 FIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVI 496
Cdd:PTZ00385 478 FVNGIEYCNAYSELNDPHEQYHRFQQQLVDRQGGDEEAMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGI 557
|
....*.
gi 15834365 497 LFPAMR 502
Cdd:PTZ00385 558 IFPLLR 563
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
180-496 |
4.04e-79 |
|
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: 249.64 E-value: 4.04e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 180 SRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGG-ASARPFIT---HHNALDLDMYLRIAPELYLKRLVVGGFERV 255
Cdd:COG2269 2 SREALRARARLLAAIRAFFAERGVLEVETPALSVAPGTdPHLDSFATefiGPDGGGRPLYLHTSPEFAMKRLLAAGSGPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 256 FEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLgttkvtygehvfdfGKPFEKLTMREAIKK 335
Cdd:COG2269 82 YQIAKVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAAG--------------FAPAERLSYQEAFLR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 336 YrpetdmADLD----NFDAAKALAESIGITVEKSWGLGRIVTEIFDEVAEAHLIQ--PTFITEYPAEVSPLARRNDVNPE 409
Cdd:COG2269 148 Y------LGIDpltaDLDELAAAAAAAGLRVADDDDRDDLLDLLLSERVEPQLGRdrPTFLYDYPASQAALARISPDDPR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 410 ITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNS 489
Cdd:COG2269 222 VAERFELYACGVELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALGA 301
|
....*..
gi 15834365 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 |
6.15e-74 |
|
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: 235.52 E-value: 6.15e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 197 FMVARGFMEVETPMMQVIPGGASA-RPFITH---HNALDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHN 272
Cdd:TIGR00462 1 FFAERGVLEVETPLLSPAPVTDPHlDAFATEfvgPDGQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 273 PEFTMMELYMAYADYHDLIELTESLFRTLAQevlgttkvtygehvfDFGKPFEKLTMREAIKKYrpetdmADLD----NF 348
Cdd:TIGR00462 81 PEFTMLEWYRPGFDYHDLMDEVEALLQELLG---------------DPFAPAERLSYQEAFLRY------AGIDpltaSL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 349 DAAKALAESIGITVekSWGLGR--IVTEIFDEVAEAHLIQ--PTFITEYPAEVSPLARRNDVNPEITDRFEFFIGGREIG 424
Cdd:TIGR00462 140 AELQAAAAAHGIRA--SEEDDRddLLDLLFSEKVEPHLGFgrPTFLYDYPASQAALARISPDDPRVAERFELYIKGLELA 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15834365 425 NGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVI 496
Cdd:TIGR00462 218 NGFHELTDAAEQRRRFEADNALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDVL 289
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
67-174 |
1.22e-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: 191.92 E-value: 1.22e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 67 EVSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEGVYNDQFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLL 146
Cdd:cd04322 1 EVSVAGRIMSKRGSGKLSFADLQDESGKIQVYVNKDDLGEEEFEDFKKLLDLGDIIGVTGTPFKTKTGELSIFVKEFTLL 80
|
90 100
....*....|....*....|....*...
gi 15834365 147 TKALRPLPDKFHGLQDQEVRYRQRYLDL 174
Cdd:cd04322 81 SKSLRPLPEKFHGLTDVETRYRQRYLDL 108
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
187-495 |
1.30e-58 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 195.92 E-value: 1.30e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 187 RSKILAAIRQFMVARGFMEVETPMMQVIPG-GASARPFITHHNALD----LDMYLRIAPELYLKRLVVGGFERVFEINRN 261
Cdd:PRK09350 8 RAKIIAEIRRFFADRGVLEVETPILSQATVtDIHLVPFETRFVGPGasqgKTLWLMTSPEYHMKRLLAAGSGPIFQICKS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 262 FRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFrtlaQEVLGTtkvtygehvfdfgKPFEKLTMREAIKKYrpetd 341
Cdd:PRK09350 88 FRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLL----QQVLDC-------------EPAESLSYQQAFLRY----- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 342 mADLDNFDAAKA-LAEsigitVEKSWGLGRIVTE----------IFDEVAEAHLIQ--PTFITEYPAEVSPLARRNDVNP 408
Cdd:PRK09350 146 -LGIDPLSADKTqLRE-----VAAKLGLSNIADEeedrdtllqlLFTFGVEPNIGKekPTFVYHFPASQAALAKISTEDH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 409 EITDRFEFFIGGREIGNGFSELNDAEDQAERFqEQVNAK-AAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFT 487
Cdd:PRK09350 220 RVAERFEVYFKGIELANGFHELTDAREQRQRF-EQDNRKrAARGLPQQPIDENLIAALEAGLPDCSGVALGVDRLIMLAL 298
|
....*...
gi 15834365 488 NSHTIRDV 495
Cdd:PRK09350 299 GAESISEV 306
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
67-499 |
1.78e-48 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 173.07 E-value: 1.78e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 67 EVSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEGVynDQFKKWDLGDIIGARGTLFKTQT--GELSIHCTELR 144
Cdd:PRK05159 18 EVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKVDEELF--ETIKKLKRESVVSVTGTVKANPKapGGVEVIPEEIE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 145 LLTKALRPLPDKFHG--LQDQEVRYRQRYLDLiANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPmmQVIP----GGA 218
Cdd:PRK05159 96 VLNKAEEPLPLDISGkvLAELDTRLDNRFLDL-RRPRVRAIFKIRSEVLRAFREFLYENGFTEIFTP--KIVAsgteGGA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 219 SARPfITHhnaLDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGI-SVRHNPEFTMMELYMAYAD-YHDLIELTES 296
Cdd:PRK05159 173 ELFP-IDY---FEKEAYLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHnTSRHLNEYTSIDVEMGFIDdHEDVMDLLEN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 297 LFRTLAQEVlgttKVTYGEHVFDFG-------KPFEKLTMREAI----KKYRPETDMADLDNfDAAKALAEsigitveks 365
Cdd:PRK05159 249 LLRYMYEDV----AENCEKELELLGielpvpeTPIPRITYDEAIeilkSKGNEISWGDDLDT-EGERLLGE--------- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 366 wglgrivteifdEVAEAHLIQPTFITEYPAEVSPL-ARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQv 444
Cdd:PRK05159 315 ------------YVKEEYGSDFYFITDYPSEKRPFyTMPDEDDPEISKSFDLLFRGLEITSGGQRIHRYDMLVESIKEK- 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 15834365 445 nakaaGDDEAMFydEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
Cdd:PRK05159 382 -----GLNPESF--EFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFP 429
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
67-502 |
2.23e-45 |
|
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: 164.45 E-value: 2.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 67 EVSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEgvyNDQFKKWDLGDIIGARGTLFKTQT--GELSIHCTELR 144
Cdd:COG0017 16 EVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKLEN---FEEAKKLTTESSVEVTGTVVESPRapQGVELQAEEIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 145 LLTKALRPLP--DKFHGLqdqEVRYRQRYLDLIANdKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMqvIP----GGA 218
Cdd:COG0017 93 VLGEADEPYPlqPKRHSL---EFLLDNRHLRLRTN-RFGAIFRIRSELARAIREFFQERGFVEVHTPII--TAsateGGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 219 SARP---FithhnalDLDMYLRIAPELYlKRLVVGGFERVFEINRNFRNEGiS--VRHNPEFTMMELYMAYADYHDLIEL 293
Cdd:COG0017 167 ELFPvdyF-------GKEAYLTQSGQLY-KEALAMALEKVYTFGPTFRAEK-SntRRHLAEFWMIEPEMAFADLEDVMDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 294 TESLFRTLAQEVLGTtkvtYGEHVFDFGK-----------PFEKLTMREAIKkyrpetdmadldnfdaakaLAESIGITV 362
Cdd:COG0017 238 AEEMLKYIIKYVLEN----CPEELEFLGRdverlekvpesPFPRITYTEAIE-------------------ILKKSGEKV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 363 EksWG--LG----RIVTEIFDEvaeahliQPTFITEYPAEVSPL-ARRNDVNPEITDRFEFFIGG-REIGNGFSELNDAE 434
Cdd:COG0017 295 E--WGddLGteheRYLGEEFFK-------KPVFVTDYPKEIKAFyMKPNPDDPKTVAAFDLLAPGiGEIIGGSQREHRYD 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15834365 435 DQAERFQEQvnakaaGDDEAMFydEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFPAMR 502
Cdd:COG0017 366 VLVERIKEK------GLDPEDY--EWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDP 425
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
161-499 |
8.25e-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: 8.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 161 QDQEVRYRQRYLDLiANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIP--GGASARPFithhNALDLDMYLRI 238
Cdd:cd00776 2 ANLETLLDNRHLDL-RTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDteGGAELFKV----SYFGKPAYLAQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 239 APELYlKRLVVGGFERVFEINRNFRNE-GISVRHNPEFTMMELYMAYA-DYHDLIELTESLFRTLAQEVL------GTTK 310
Cdd:cd00776 77 SPQLY-KEMLIAALERVYEIGPVFRAEkSNTRRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLercakeLELV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 311 VTYGEHVFDFGKPFEKLTMREAIKkyrpetdmadldnfdaakaLAESIGITVEKSWGLG------RIVTEIFDEVaeahl 384
Cdd:cd00776 156 NQLNRELLKPLEPFPRITYDEAIE-------------------LLREKGVEEEVKWGEDlsteheRLLGEIVKGD----- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 385 iqPTFITEYPAEVSPL-ARRNDVNPEITDRFEFFI-GGREIGNGFSELNDAEDQAERFQEQvnakaaGDDEAMFydEDYV 462
Cdd:cd00776 212 --PVFVTDYPKEIKPFyMKPDDDNPETVESFDLLMpGVGEIVGGSQRIHDYDELEERIKEH------GLDPESF--EWYL 281
|
330 340 350
....*....|....*....|....*....|....*..
gi 15834365 463 TALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
Cdd:cd00776 282 DLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
1-499 |
3.04e-33 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 132.52 E-value: 3.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 1 MSEQETRGANEAIDFNDELRNRREKLAALRQQGVAFP-NDFRRDHTSDQLHEEFDAKDNQELESLNIE-----VSVAGRM 74
Cdd:PLN02850 11 EKISKKAAKKAAAKAEKLRREATAKAAAASLEDEDDPlASNYGDVPLEELQSKVTGREWTDVSDLGEElagseVLIRGRV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 75 MTRRIMGKASFVTLQDVGGRIQ--LYVARDSLPEGV--YNDQFKKWDLGDIIGA--------RGTlfkTQTGElsIHCTE 142
Cdd:PLN02850 91 HTIRGKGKSAFLVLRQSGFTVQcvVFVSEVTVSKGMvkYAKQLSRESVVDVEGVvsvpkkpvKGT---TQQVE--IQVRK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 143 LRLLTKALRPLP-----------DKFHGLQD--------QEVRYRQRYLDL--IANdksRQTFVVRSKILAAIRQFMVAR 201
Cdd:PLN02850 166 IYCVSKALATLPfnvedaarsesEIEKALQTgeqlvrvgQDTRLNNRVLDLrtPAN---QAIFRIQSQVCNLFREFLLSK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 202 GFMEVETPmmQVIPG---GASArpfithhnALDLDMY-----LRIAPELYLKRLVVGGFERVFEINRNFRNE-GISVRHN 272
Cdd:PLN02850 243 GFVEIHTP--KLIAGaseGGSA--------VFRLDYKgqpacLAQSPQLHKQMAICGDFRRVFEIGPVFRAEdSFTHRHL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 273 PEFTMMELYMAYAD-YHDLIELTESLFRTL--------AQEvLGTTKVTYGEHVFDFGKPFEKLTMREAIKKYRPETDMA 343
Cdd:PLN02850 313 CEFTGLDLEMEIKEhYSEVLDVVDELFVAIfdglnercKKE-LEAIREQYPFEPLKYLPKTLRLTFAEGIQMLKEAGVEV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 344 D-LDNFDAAKALAesigitvekswgLGRIV-----TEIFdevaeahliqptFITEYPAEVSPLARRNDV-NPEITDRFEF 416
Cdd:PLN02850 392 DpLGDLNTESERK------------LGQLVkekygTDFY------------ILHRYPLAVRPFYTMPCPdDPKYSNSFDV 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 417 FIGGREIGNGFSELNDAEDQAERfqeqvnAKAAGDDEAMFydEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVI 496
Cdd:PLN02850 448 FIRGEEIISGAQRVHDPELLEKR------AEECGIDVKTI--STYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTS 519
|
...
gi 15834365 497 LFP 499
Cdd:PLN02850 520 LFP 522
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
184-499 |
5.19e-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: 123.84 E-value: 5.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 184 FVVRSKILAAIRQFMVARGFMEVETPMM-QVIPGGAsaRPFI----THHN---ALDLdmylriAPELYLKRLVVGGFERV 255
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILtKSTPEGA--RDFLvpsrLHPGkfyALPQ------SPQLFKQLLMVSGFDRY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 256 FEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTtkvtygehvfDFGKPFEKLTMREAIKK 335
Cdd:cd00777 73 FQIARCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLGV----------ELTTPFPRMTYAEAMER 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 336 YrpetdmadldnfdaakalaesiGITVekSWglgriVTE--IFDEVAEAHLIQPT---FiTEYPAEVSPLarrNDVNPE- 409
Cdd:cd00777 143 Y----------------------GFKF--LW-----IVDfpLFEWDEEEGRLVSAhhpF-TAPKEEDLDL---LEKDPEd 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 410 -ITDRFEFFIGGREIGNGFSELNDAEDQAERFqeqvnaKAAGDDEAMFYDE--DYVTALEYGLPPTAGLGIGIDRMIMLF 486
Cdd:cd00777 190 aRAQAYDLVLNGVELGGGSIRIHDPDIQEKVF------EILGLSEEEAEEKfgFLLEAFKYGAPPHGGIALGLDRLVMLL 263
|
330
....*....|...
gi 15834365 487 TNSHTIRDVILFP 499
Cdd:cd00777 264 TGSESIRDVIAFP 276
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
133-499 |
4.67e-31 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 126.72 E-value: 4.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 133 TGELSIHCTELRLLTKAlRPLPdkFHGLQDQ----EVRYRQRYLDLiANDKSRQTFVVRSKILAAIRQFMVARGFMEVET 208
Cdd:PRK00476 90 TGEIEVLASELEVLNKS-KTLP--FPIDDEEdvseELRLKYRYLDL-RRPEMQKNLKLRSKVTSAIRNFLDDNGFLEIET 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 209 PMMqvipgGAS----ARPFI----THHN---ALDLdmylriAPELYLKRLVVGGFERVFEINRNFRNEgiSVRHN--PEF 275
Cdd:PRK00476 166 PIL-----TKStpegARDYLvpsrVHPGkfyALPQ------SPQLFKQLLMVAGFDRYYQIARCFRDE--DLRADrqPEF 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 276 TMMELYMAYADYHDLIELTESLFRTLAQEVLGttkvtygehvFDFGKPFEKLTMREAIKKY---RPET-------DMADL 345
Cdd:PRK00476 233 TQIDIEMSFVTQEDVMALMEGLIRHVFKEVLG----------VDLPTPFPRMTYAEAMRRYgsdKPDLrfglelvDVTDL 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 346 ---DNFDAAKALAESIG----ITVEKswGLGRIVTEIFDEVAEahliqptFITEYPA------------EVSPLARR--N 404
Cdd:PRK00476 303 fkdSGFKVFAGAANDGGrvkaIRVPG--GAAQLSRKQIDELTE-------FAKIYGAkglayikvnedgLKGPIAKFlsE 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 405 DVNPEITDRFE-------FFIGGR-------------EIG--------NGFS----------ELN--------------- 431
Cdd:PRK00476 374 EELAALLERTGakdgdliFFGADKakvvndalgalrlKLGkelglideDKFAflwvvdfpmfEYDeeegrwvaahhpftm 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 432 ----DAEDQAERFQEQVNAKA----------AG-------DD--EAMF----YDEDYV--------TALEYGLPPTAGLG 476
Cdd:PRK00476 454 pkdeDLDELETTDPGKARAYAydlvlngyelGGgsirihrPEiqEKVFeilgISEEEAeekfgfllDALKYGAPPHGGIA 533
|
490 500
....*....|....*....|...
gi 15834365 477 IGIDRMIMLFTNSHTIRDVILFP 499
Cdd:PRK00476 534 FGLDRLVMLLAGADSIRDVIAFP 556
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
133-499 |
8.00e-29 |
|
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: 120.10 E-value: 8.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 133 TGELSIHCTELRLLTKAlRPLPdkFHgLQDQ-----EVRYRQRYLDLiANDKSRQTFVVRSKILAAIRQFMVARGFMEVE 207
Cdd:COG0173 91 TGEIEVLASELEILNKA-KTPP--FQ-IDDDtdvseELRLKYRYLDL-RRPEMQKNLILRHKVTKAIRNYLDENGFLEIE 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 208 TPMMqvipgGAS----ARpfithhnalDldmYL---RI----------APELYLKRLVVGGFERVFEINRNFRNEgiSVR 270
Cdd:COG0173 166 TPIL-----TKStpegAR---------D---YLvpsRVhpgkfyalpqSPQLFKQLLMVSGFDRYFQIARCFRDE--DLR 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 271 HN--PEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGttkvtygehvFDFGKPFEKLTMREAIKKY---RPET----D 341
Cdd:COG0173 227 ADrqPEFTQLDIEMSFVDQEDVFELMEGLIRHLFKEVLG----------VELPTPFPRMTYAEAMERYgsdKPDLrfglE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 342 MADLDN---------FDAAKALAESI-GITVEK-------------SW-------GLGRI-VTE---------IFDEVAE 381
Cdd:COG0173 297 LVDVTDifkdsgfkvFAGAAENGGRVkAINVPGgaslsrkqideltEFakqygakGLAYIkVNEdglkspiakFLSEEEL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 382 AHLIQPT---------FITEYPAEVSP--------LARRNDVNPE-------ITD-----------RFEF----F----- 417
Cdd:COG0173 377 AAILERLgakpgdlifFVADKPKVVNKalgalrlkLGKELGLIDEdefaflwVVDfplfeydeeegRWVAmhhpFtmpkd 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 418 ---------------------IGGREIGNGFSELNDAEDQAERFqeqvnaKAAG--DDEAM-----FYDedyvtALEYGL 469
Cdd:COG0173 457 edldlletdpgkvrakaydlvLNGYELGGGSIRIHDPELQEKVF------ELLGisEEEAEekfgfLLE-----AFKYGA 525
|
490 500 510
....*....|....*....|....*....|
gi 15834365 470 PPTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
Cdd:COG0173 526 PPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
67-499 |
1.31e-28 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 119.89 E-value: 1.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 67 EVSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPE--GVYNDQFKKWdlgdIIGARGTLF---------KTQTGE 135
Cdd:PLN02903 74 RVTLCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDEFPEahRTANRLRNEY----VVAVEGTVRsrpqespnkKMKTGS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 136 LSIHCTELRLLTKALRPLPDKFHGLQDQ------EVRYRQRYLDLIANDKSRQtFVVRSKILAAIRQFMVAR-GFMEVET 208
Cdd:PLN02903 150 VEVVAESVDILNVVTKSLPFLVTTADEQkdsikeEVRLRYRVLDLRRPQMNAN-LRLRHRVVKLIRRYLEDVhGFVEIET 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 209 PMM-QVIPGGAsaRPFITHHNALDLDMY-LRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYAD 286
Cdd:PLN02903 229 PILsRSTPEGA--RDYLVPSRVQPGTFYaLPQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEFTQLDMELAFTP 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 287 YHDLIELTESLFRTLAQEVLGTtkvtygehvfDFGKPFEKLTMREAIKKY---RPET----DMADLDN------------ 347
Cdd:PLN02903 307 LEDMLKLNEDLIRQVFKEIKGV----------QLPNPFPRLTYAEAMSKYgsdKPDLryglELVDVSDvfaessfkvfag 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 348 ----------------------------------------------------FDAAKALAESIG---------------- 359
Cdd:PLN02903 377 alesggvvkaicvpdgkkisnntalkkgdiyneaiksgakglaflkvlddgeLEGIKALVESLSpeqaeqllaacgagpg 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 360 ----------ITVEKSwgLGRIVTEIFDEVAeahLIQPT-----FITEYPA-EVSPLARRNDV--------NPEITD--- 412
Cdd:PLN02903 457 dlilfaagptSSVNKT--LDRLRQFIAKTLD---LIDPSrhsilWVTDFPMfEWNEDEQRLEAlhhpftapNPEDMGdls 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 413 -----RFEFFIGGREIGNGFSELNDAEDQaERFQEQVNAKAAGDDEAMFYdedYVTALEYGLPPTAGLGIGIDRMIMLFT 487
Cdd:PLN02903 532 saralAYDMVYNGVEIGGGSLRIYRRDVQ-QKVLEAIGLSPEEAESKFGY---LLEALDMGAPPHGGIAYGLDRLVMLLA 607
|
570
....*....|..
gi 15834365 488 NSHTIRDVILFP 499
Cdd:PLN02903 608 GAKSIRDVIAFP 619
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
186-482 |
3.57e-28 |
|
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: 111.44 E-value: 3.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 186 VRSKILAAIRQFMVARGFMEVETPMMQVIPGGASAR----PFITHHNALDLDMYLRIAPELYLKRLVVG----GFERVFE 257
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGhepkDLLPVGAENEEDLYLRPTLEPGLVRLFVShirkLPLRLAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 258 INRNFRNEGISV--RHNPEFTMMELYMAYAD------YHDLIELTESLFRTLAQEvlgttkvtygehvfdfgkpfekltm 329
Cdd:cd00768 81 IGPAFRNEGGRRglRRVREFTQLEGEVFGEDgeeaseFEELIELTEELLRALGIK------------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 330 reaikkyrpetdmadldnfdaakalaesigitvekswglgrivteifdevaeahlIQPTFITEYPAEVSPlarrndvnPE 409
Cdd:cd00768 136 -------------------------------------------------------LDIVFVEKTPGEFSP--------GG 152
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15834365 410 ITDRFEFFI-----GGREIGNGFSELNDAEDQAERFqeqvnakaagddeamfydeDYVTALEYGLPPTAGLGIGIDRM 482
Cdd:cd00768 153 AGPGFEIEVdhpegRGLEIGSGGYRQDEQARAADLY-------------------FLDEALEYRYPPTIGFGLGLERL 211
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
68-505 |
3.43e-24 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 105.85 E-value: 3.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 68 VSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVA-RDSLPEGVYnDQFKKWDLGDIIGARGTLFK-------TQTGELSIH 139
Cdd:PTZ00401 81 VLIRARVSTTRKKGKMAFMVLRDGSDSVQAMAAvEGDVPKEMI-DFIGQIPTESIVDVEATVCKveqpitsTSHSDIELK 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 140 CTELRLLTKALRPLPDKFHGLQDQE----------VRYRQRYLDLiANDKSRQTFVVRSKILAAIRQFMVARGFMEVETP 209
Cdd:PTZ00401 160 VKKIHTVTESLRTLPFTLEDASRKEsdegakvnfdTRLNSRWMDL-RTPASGAIFRLQSRVCQYFRQFLIDSDFCEIHSP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 210 MMQVIPGGASARPFITHHnaLDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISV-RHNPEFTMMELYMAYAD-Y 287
Cdd:PTZ00401 239 KIINAPSEGGANVFKLEY--FNRFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNThRHLTEFVGLDVEMRINEhY 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 288 HDLIELTESLFRTLAQEVLGTTKVTygEHVFDfGKPFEKL-------TMRE----AIKKYRPETDM--ADLDNFDA---- 350
Cdd:PTZ00401 317 YEVLDLAESLFNYIFERLATHTKEL--KAVCQ-QYPFEPLvwkltpeRMKElgvgVISEGVEPTDKyqARVHNMDSrmlr 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 351 ----------------AKALAESIGITVEKSwgLGRIVTEIFDevaeahliQPTFITE-YPAEVSP---LARRNDVnpEI 410
Cdd:PTZ00401 394 inymhciellntvleeKMAPTDDINTTNEKL--LGKLVKERYG--------TDFFISDrFPSSARPfytMECKDDE--RF 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 411 TDRFEFFIGGREIGNGFSELNDAEDQAERfqeqvnAKAAGDDEAMFydEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSH 490
Cdd:PTZ00401 462 TNSYDMFIRGEEISSGAQRIHDPDLLLAR------AKMLNVDLTPI--KEYVDSFRLGAWPHGGFGVGLERVVMLYLGLS 533
|
490
....*....|....*
gi 15834365 491 TIRDVILFPaMRPQK 505
Cdd:PTZ00401 534 NVRLASLFP-RDPQR 547
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
175-499 |
3.85e-24 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 103.18 E-value: 3.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 175 IANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVI-----PGGASARPFITHHNALDLDMYLRIAPELYlKRLVV 249
Cdd:PRK06462 21 ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIISPStdplmGLGSDLPVKQISIDFYGVEYYLADSMILH-KQLAL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 250 GGFERVFEINRNFRNEG---ISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTtkvtYGEHVFDFG----- 321
Cdd:PRK06462 100 RMLGKIFYLSPNFRLEPvdkDTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEE----HEDELEFFGrdlph 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 322 --KPFEKLTMREAIKkyrpetdmaDLDNFDAAKALAESIGITVEKSwglgriVTEIFDEvaeahliqPTFITEYPAEVSP 399
Cdd:PRK06462 176 lkRPFKRITHKEAVE---------ILNEEGCRGIDLEELGSEGEKS------LSEHFEE--------PFWIIDIPKGSRE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 400 LARRNDvnPEITDRFEFF--IggreIGNGFSELNDAEDQAERFQEQV-NAKAAGDDEAMFydEDYVTALEYGLPPTAGLG 476
Cdd:PRK06462 233 FYDRED--PERPGVLRNYdlL----LPEGYGEAVSGGEREYEYEEIVeRIREHGVDPEKY--KWYLEMAKEGPLPSAGFG 304
|
330 340
....*....|....*....|...
gi 15834365 477 IGIDRMIMLFTNSHTIRDVILFP 499
Cdd:PRK06462 305 IGVERLTRYICGLRHIREVQPFP 327
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
67-502 |
1.60e-22 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 101.22 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 67 EVSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEGVYnDQFKKWDLGDIIGARGTLFK---------TQTGELS 137
Cdd:PRK12820 20 EVCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFSPEAAPADVY-ELAASLRAEFCVALQGEVQKrleetenphIETGDIE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 138 IHCTELRLLTKALR---PLPDKF------HGLQD---QEVRYRQRYLDlIANDKSRQTFVVRSKILAAIRQFMVARGFME 205
Cdd:PRK12820 99 VFVRELSILAASEAlpfAISDKAmtagagSAGADavnEDLRLQYRYLD-IRRPAMQDHLAKRHRIIKCARDFLDSRGFLE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 206 VETPMMQV-IPGGAsaRPFITHHNALDLDMY-LRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMA 283
Cdd:PRK12820 178 IETPILTKsTPEGA--RDYLVPSRIHPKEFYaLPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEFTQLDIEAS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 284 YADYHDLIELTESLFRTLAqEVLGttkvtygehvFDFGKPFEKLTMREAIKKY---RPET----DMADLDNF-------- 348
Cdd:PRK12820 256 FIDEEFIFELIEELTARMF-AIGG----------IALPRPFPRMPYAEAMDTTgsdRPDLrfdlKFADATDIfentrygi 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 349 ------------------------------DAAKALAESIGITvEKSW------GLGRIVTEIFDE-------------- 378
Cdd:PRK12820 325 fkqilqrggrikginikgqseklsknvlqnEYAKEIAPSFGAK-GMTWmraeagGLDSNIVQFFSAdekealkrrfhaed 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 379 ------VAEA--------------HL-----------IQPTFITEYP-----------AEVSPLAR--RNDVNP----EI 410
Cdd:PRK12820 404 gdviimIADAscaivlsalgqlrlHLadrlglipegvFHPLWITDFPlfeatddggvtSSHHPFTApdREDFDPgdieEL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 411 TD----RFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFydedYVTALEYGLPPTAGLGIGIDRMIMLF 486
Cdd:PRK12820 484 LDlrsrAYDLVVNGEELGGGSIRINDKDIQLRIFAALGLSEEDIEDKFGF----FLRAFDFAAPPHGGIALGLDRVVSMI 559
|
570
....*....|....*.
gi 15834365 487 TNSHTIRDVILFPAMR 502
Cdd:PRK12820 560 LQTPSIREVIAFPKNR 575
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
67-499 |
2.89e-18 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 87.09 E-value: 2.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 67 EVSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEgvYNDQFKKWDLGDIIGARGTLFKTQT--GELSIHCTELR 144
Cdd:PRK03932 18 EVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDNGEE--YFEEIKKLTTGSSVIVTGTVVESPRagQGYELQATKIE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 145 LLTKALR--PLPDKFHG---LQDQevryrqRYLDLIANdKSRQTFVVRSKILAAIRQFMVARGFMEVETPMmqvipggas 219
Cdd:PRK03932 96 VIGEDPEdyPIQKKRHSiefLREI------AHLRPRTN-KFGAVMRIRNTLAQAIHEFFNENGFVWVDTPI--------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 220 arpfITHHNA-----------LDLDM---------YLRIAPELYLKRLVVgGFERVFEINRNFRNEGiS--VRHNPEFTM 277
Cdd:PRK03932 160 ----ITASDCegagelfrvttLDLDFskdffgkeaYLTVSGQLYAEAYAM-ALGKVYTFGPTFRAEN-SntRRHLAEFWM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 278 MELYMAYADYHDLIELTESLFRTLAQEVL--------------GTTKVTYGEHVFDfgKPFEKLTMREAIKkyrpetdma 343
Cdd:PRK03932 234 IEPEMAFADLEDNMDLAEEMLKYVVKYVLencpddleflnrrvDKGDIERLENFIE--SPFPRITYTEAIE--------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 344 dldnfdaakaLAESIGITVEK--SWG--LG----RIVTE-IFDevaeahliQPTFITEYPAEVSPL-ARRNDVN------ 407
Cdd:PRK03932 303 ----------ILQKSGKKFEFpvEWGddLGseheRYLAEeHFK--------KPVFVTNYPKDIKAFyMRLNPDGktvaam 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 408 ----P---EItdrfeffIGG--REigngfselNDAEDQAERFQEQvnakaaGDDEamfydEDYVTALE---YGLPPTAGL 475
Cdd:PRK03932 365 dllaPgigEI-------IGGsqRE--------ERLDVLEARIKEL------GLNK-----EDYWWYLDlrrYGSVPHSGF 418
|
490 500
....*....|....*....|....
gi 15834365 476 GIGIDRMIMLFTNSHTIRDVILFP 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 |
6.43e-18 |
|
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: 78.38 E-value: 6.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 67 EVSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEGVynDQFKKWDLGDIIGARGTLFKTQ-----TGELSIHCT 141
Cdd:cd04100 1 EVTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEELGEFF--EEAEKLRTESVVGVTGTVVKRPegnlaTGEIELQAE 78
|
....*..
gi 15834365 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 |
1.44e-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: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 68 VSVAGRMMT-RRIMGKASFVTLQDVGGRIQLYVardslPEGVYNDQFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLL 146
Cdd:pfam01336 1 VTVAGRVTSiRRSGGKLLFLTLRDGTGSIQVVV-----FKEEAEKLAKKLKEGDVVRVTGKVKKRKGGELELVVEEIELL 75
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
235-499 |
8.38e-12 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 67.36 E-value: 8.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 235 YLRIAPELYLKRLVvGGFERVFEINRNFRNEGI-SVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTkvty 313
Cdd:PTZ00425 327 FLTVSGQLSLENLC-SSMGDVYTFGPTFRAENShTSRHLAEFWMIEPEIAFADLYDNMELAESYIKYCIGYVLNNN---- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 314 gehvFDFGKPFEKLTMREAIKKYRP--ETDMADLDNFDAAKAL---AESIGITVEksWGLGrIVTEIFDEVAEAHLIQPT 388
Cdd:PTZ00425 402 ----FDDIYYFEENVETGLISRLKNilDEDFAKITYTNVIDLLqpySDSFEVPVK--WGMD-LQSEHERFVAEQIFKKPV 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 389 FITEYPAEVSPLARRNDVNPEITDRFEFFIG--GREIGNgfselNDAEDQAERFQEQVNAKAAGDDEAMFYDEdyvtALE 466
Cdd:PTZ00425 475 IVYNYPKDLKAFYMKLNEDQKTVAAMDVLVPkiGEVIGG-----SQREDNLERLDKMIKEKKLNMESYWWYRQ----LRK 545
|
250 260 270
....*....|....*....|....*....|...
gi 15834365 467 YGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
Cdd:PTZ00425 546 FGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFP 578
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
42-174 |
3.85e-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: 49.06 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 42 RDHTSDQLHEEFDAKdnqeleslniEVSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEgvyNDQFKKWDLGDI 121
Cdd:cd04317 1 RTHYCGELRESHVGQ----------EVTLCGWVQRRRDHGGLIFIDLRDRYGIVQVVFDPEEAPE---FELAEKLRNESV 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15834365 122 IGARGTLF---------KTQTGELSIHCTELRLLTKAlRPLP----DKFHGlqDQEVRYRQRYLDL 174
Cdd:cd04317 68 IQVTGKVRarpegtvnpKLPTGEIEVVASELEVLNKA-KTLPfeidDDVNV--SEELRLKYRYLDL 130
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
67-499 |
8.26e-07 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 51.51 E-value: 8.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 67 EVSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEGVynDQFKKWDL--GDIIGARGTLFKTQTGELSIhctELR 144
Cdd:PLN02603 109 TLNVMGWVRTLRAQSSVTFIEVNDGSCLSNMQCVMTPDAEGY--DQVESGLIttGASVLVQGTVVSSQGGKQKV---ELK 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 145 LLTKALRPLPDKFHGLQDQevRYRQRYLDLIANDKSR-QTF----VVRSKILAAIRQFMVARGFMEVETPMMQ------- 212
Cdd:PLN02603 184 VSKIVVVGKSDPSYPIQKK--RVSREFLRTKAHLRPRtNTFgavaRVRNALAYATHKFFQENGFVWVSSPIITasdcega 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 213 --------VIPGGASARPFITHHNALDLDMYLRIAPELYLKR--LVVGG----------FERVFEINRNFRNEGISV-RH 271
Cdd:PLN02603 262 geqfcvttLIPNSAENGGSLVDDIPKTKDGLIDWSQDFFGKPafLTVSGqlngetyataLSDVYTFGPTFRAENSNTsRH 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 272 NPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKvtygEHVFDFGKPFEKLTMREAIKKYrpETDMADLDNFDAA 351
Cdd:PLN02603 342 LAEFWMIEPELAFADLNDDMACATAYLQYVVKYILENCK----EDMEFFNTWIEKGIIDRLSDVV--EKNFVQLSYTDAI 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 352 KALAES---IGITVEksWGLG------RIVTEifdevaEAHLIQPTFITEYPAEVSPLARRNDVNPEITDRFEFFIggRE 422
Cdd:PLN02603 416 ELLLKAkkkFEFPVK--WGLDlqseheRYITE------EAFGGRPVIIRDYPKEIKAFYMRENDDGKTVAAMDMLV--PR 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 423 IGngfsELNDAEDQAERFqEQVNAKAagdDEAMFYDEDYVTALE---YGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
Cdd:PLN02603 486 VG----ELIGGSQREERL-EYLEARL---DELKLNKESYWWYLDlrrYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFP 557
|
|
| pylS |
PRK09537 |
pyrrolysine--tRNA(Pyl) ligase; |
154-278 |
6.23e-06 |
|
pyrrolysine--tRNA(Pyl) ligase;
Pssm-ID: 236555 [Multi-domain] Cd Length: 417 Bit Score: 48.68 E-value: 6.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 154 PDKFHGLQDQEV-RYRQRYLDLIANDKSRQTfvvrSKILAAIRQFMVARGFMEVETPMMqvIPGGASARPFITHHNAL-- 230
Cdd:PRK09537 176 KPKFKELESELVsRRKNDLKQMYEEDREDYL----GKLERDITKFFVDRGFLEIKSPIL--IPAEYIERMGIDNDTELsk 249
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 15834365 231 -----DLDMYLR--IAPELY--LKRL--VVGGFERVFEINRNFRNEGISVRHNPEFTMM 278
Cdd:PRK09537 250 qifrvDKNFCLRpmLAPGLYnyLRKLdrILPDPIKIFEIGPCYRKESDGKEHLEEFTMV 308
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
67-155 |
1.48e-03 |
|
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: 38.45 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834365 67 EVSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEGVYnDQFKKWDLGDIIGARGTLF---KTQTGeLSIHCTEL 143
Cdd:cd04316 14 EVTVAGWVHEIRDLGGIKFVILRDREGIVQVTAPKKKVDKELF-KTVRKLSRESVISVTGTVKaepKAPNG-VEIIPEEI 91
|
90
....*....|..
gi 15834365 144 RLLTKALRPLPD 155
Cdd:cd04316 92 EVLSEAKTPLPL 103
|
|
| |
