|
Name |
Accession |
Description |
Interval |
E-value |
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
5-504 |
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: 906.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 5 ELSEQEVVRRNSLEQLRNLGIDPYPAaEYTVNAYSAEIKRNFNDDENAA--KRQVSIAGRIMSRRIMGKATFMELQDAEG 82
Cdd:COG1190 6 DLNEQIRVRREKLEELREAGIDPYPN-KFPRTHTAAEIREKYDELEAEEetGDEVSVAGRIMAKRDMGKASFADLQDGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 83 RIQIYITRDDICPGEDKEFyntvvkKCTDIGDFIGVKGYVFRTQMGEISVHVQEMTFLSKAIRPLPvvkekdgEVFDGFT 162
Cdd:COG1190 85 RIQLYLRRDELGEEAYELF------KLLDLGDIVGVEGTVFRTKTGELSVKVEELTLLSKSLRPLP-------EKFHGLT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 163 DPEQRYRQRYVDLVVNSHVKDIFLKRTMVFNSMRSFFNERGYIEVDTPVLQSIPGGAAARPFITHHNALDIPLYLRIANE 242
Cdd:COG1190 152 DPETRYRQRYVDLIVNPEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 243 LYLKRLIVGGFDGVYEFSRNFRNEGMDRTHNPEFTAMEIYVAYKDYNWMMNFTEQMLERICMDVLGTTQVKVGEKLIDFK 322
Cdd:COG1190 232 LYLKRLIVGGFERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGTTKVTYQGQEIDLS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 323 APYKRVTMIEAIHEHTGIDISGM-NEAELRQVCDKLGVEHNETMGKGKLIDEIFGEKCEKNYIQPTFITDYPKEMSPLTK 401
Cdd:COG1190 312 PPWRRITMVEAIKEATGIDVTPLtDDEELRALAKELGIEVDPGWGRGKLIDELFEELVEPKLIQPTFVTDYPVEVSPLAK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 402 EHRTNPELTERFELMVNGKELANAYSELNDPIDQRERFEEQLKLSEKGDDEAMYIDNDFIRALEYGMPPTSGMGIGMDRL 481
Cdd:COG1190 392 RHRDDPGLTERFELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGLGIGIDRL 471
|
490 500
....*....|....*....|...
gi 922688387 482 VMLLTGQESIQEVLLFPQMKPEK 504
Cdd:COG1190 472 VMLLTDSPSIRDVILFPLMRPEK 494
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
5-504 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 886.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 5 ELSEQEVVRRNSLEQLRNLGIDPYPAaEYTVNAYSAEIKRNFNDDEN----AAKRQVSIAGRIMSRRIMGKATFMELQDA 80
Cdd:PRK00484 2 ELNEQIAVRREKLAELREQGIDPYPN-KFERTHTAAELRAKYDDKEKeeleELEIEVSVAGRVMLKRVMGKASFATLQDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 81 EGRIQIYITRDDICPGEDKEFyntvvkKCTDIGDFIGVKGYVFRTQMGEISVHVQEMTFLSKAIRPLPvvkekdgEVFDG 160
Cdd:PRK00484 81 SGRIQLYVSKDDVGEEALEAF------KKLDLGDIIGVEGTLFKTKTGELSVKATELTLLTKSLRPLP-------DKFHG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 161 FTDPEQRYRQRYVDLVVNSHVKDIFLKRTMVFNSMRSFFNERGYIEVDTPVLQSIPGGAAARPFITHHNALDIPLYLRIA 240
Cdd:PRK00484 148 LTDVETRYRQRYVDLIVNPESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARPFITHHNALDIDLYLRIA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 241 NELYLKRLIVGGFDGVYEFSRNFRNEGMDRTHNPEFTAMEIYVAYKDYNWMMNFTEQMLERICMDVLGTTQVKVGEKLID 320
Cdd:PRK00484 228 PELYLKRLIVGGFERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTYQGTEID 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 321 FKAPYKRVTMIEAIHEHTGIDISGMNEAELRQVCDKLGVEHNETMGKGKLIDEIFGEKCEKNYIQPTFITDYPKEMSPLT 400
Cdd:PRK00484 308 FGPPFKRLTMVDAIKEYTGVDFDDMTDEEARALAKELGIEVEKSWGLGKLINELFEEFVEPKLIQPTFITDYPVEISPLA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 401 KEHRTNPELTERFELMVNGKELANAYSELNDPIDQRERFEEQLKLSEKGDDEAMYIDNDFIRALEYGMPPTSGMGIGMDR 480
Cdd:PRK00484 388 KRHREDPGLTERFELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIGIDR 467
|
490 500
....*....|....*....|....
gi 922688387 481 LVMLLTGQESIQEVLLFPQMKPEK 504
Cdd:PRK00484 468 LVMLLTDSPSIRDVILFPLMRPEK 491
|
|
| lysS_bact |
TIGR00499 |
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ... |
5-504 |
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: 624.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 5 ELSEQEVVRRNSLEQLRNLGIDPYPAaEYTVNAYSAEIKRNFNDDENAA----KRQVSIAGRIMSRRIMGKATFMELQDA 80
Cdd:TIGR00499 1 ELNDQAQQRLEKLNRLRQTGNNPYLH-KFERTHSAQEFQEKYADLSNEElkekELKVSIAGRIKAIRSMGKATFITLQDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 81 EGRIQIYITRDDICpgEDKEFYNtvvKKCTDIGDFIGVKGYVFRTQMGEISVHVQEMTFLSKAIRPLPvvkekdgEVFDG 160
Cdd:TIGR00499 80 SGQIQLYVNKNKLP--EDFYEFD---EYLLDLGDIIGVTGYPFKTKTGELSVKVTELQILTKCLQPLP-------DKWHG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 161 FTDPEQRYRQRYVDLVVNSHVKDIFLKRTMVFNSMRSFFNERGYIEVDTPVLQSIPGGAAARPFITHHNALDIPLYLRIA 240
Cdd:TIGR00499 148 LTDQETRYRQRYLDLIVNPDVRQTFLKRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKPFITHHNALDMDLYLRIA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 241 NELYLKRLIVGGFDGVYEFSRNFRNEGMDRTHNPEFTAMEIYVAYKDYNWMMNFTEQMLERICMDVLGTTQVKVGEKLID 320
Cdd:TIGR00499 228 PELYLKRLIVGGLEKVYEIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTFIINYNDLEID 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 321 FKAPYKRVTMIEAIHEHTGIDISGMNEAE-LRQVCDKLGVEHNE-TMGKGKLIDEIFGEKCEKNYIQPTFITDYPKEMSP 398
Cdd:TIGR00499 308 LKPPWKRITMVDALEMVTGIDFDILKDDEtAKALAKEHGIEVAEdSLTLGHILNKFFEQFLEHTLIQPTFITHYPAEISP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 399 LTKEHRTNPELTERFELMVNGKELANAYSELNDPIDQRERFEEQLKLSEKGDDEAMYIDNDFIRALEYGMPPTSGMGIGM 478
Cdd:TIGR00499 388 LAKRDPSNPEFTERFELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGIGI 467
|
490 500
....*....|....*....|....*.
gi 922688387 479 DRLVMLLTGQESIQEVLLFPQMKPEK 504
Cdd:TIGR00499 468 DRLVMLLTDAPSIRDVLLFPQLRPQK 493
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
12-503 |
0e+00 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 613.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 12 VRRNSLEQLRNLGIDPYPAaEYTVNAYSAEIKRNFNDDENAAKRQ---VSIAGRIMSRRIMGKATFMELQDAEGRIQIYI 88
Cdd:PLN02502 64 NRLKKVEALRAKGVEPYPY-KFDVTHTAPELQEKYGSLENGEELEdvsVSVAGRIMAKRAFGKLAFYDLRDDGGKIQLYA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 89 TRDDIcPGEDKEFYNtvVKKCTDIGDFIGVKGYVFRTQMGEISVHVQEMTFLSKAIRPLPvvkekdgEVFDGFTDPEQRY 168
Cdd:PLN02502 143 DKKRL-DLDEEEFEK--LHSLVDRGDIVGVTGTPGKTKKGELSIFPTSFEVLTKCLLMLP-------DKYHGLTDQETRY 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 169 RQRYVDLVVNSHVKDIFLKRTMVFNSMRSFFNERGYIEVDTPVLQSIPGGAAARPFITHHNALDIPLYLRIANELYLKRL 248
Cdd:PLN02502 213 RQRYLDLIANPEVRDIFRTRAKIISYIRRFLDDRGFLEVETPMLNMIAGGAAARPFVTHHNDLNMDLYLRIATELHLKRL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 249 IVGGFDGVYEFSRNFRNEGMDRTHNPEFTAMEIYVAYKDYNWMMNFTEQMLERICMDVLGTTQVKVGEKLIDFKAPYKRV 328
Cdd:PLN02502 293 VVGGFERVYEIGRQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKELTGSYKIKYHGIEIDFTPPFRRI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 329 TMIEAIHEHTGIDI-SGMNEAELRQVCDKLGVEHNETMGK----GKLIDEIFGEKCEKNYIQPTFITDYPKEMSPLTKEH 403
Cdd:PLN02502 373 SMISLVEEATGIDFpADLKSDEANAYLIAACEKFDVKCPPpqttGRLLNELFEEFLEETLVQPTFVLDHPVEMSPLAKPH 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 404 RTNPELTERFELMVNGKELANAYSELNDPIDQRERFEEQLKLSEKGDDEAMYIDNDFIRALEYGMPPTSGMGIGMDRLVM 483
Cdd:PLN02502 453 RSKPGLTERFELFINGRELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRLVM 532
|
490 500
....*....|....*....|
gi 922688387 484 LLTGQESIQEVLLFPQMKPE 503
Cdd:PLN02502 533 LLTDSASIRDVIAFPAMKPQ 552
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
178-502 |
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: 553.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 178 NSHVKDIFLKRTMVFNSMRSFFNERGYIEVDTPVLQSIPGGAAARPFITHHNALDIPLYLRIANELYLKRLIVGGFDGVY 257
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 258 EFSRNFRNEGMDRTHNPEFTAMEIYVAYKDYNWMMNFTEQMLERICMDVLGTTQVKVGEKLIDFKAPYKRVTMIEAIHEH 337
Cdd:cd00775 81 EIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIEYGGKELDFTPPFKRVTMVDALKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 338 TGIDISGMNE---AELRQVCDKLGVEHNE-TMGKGKLIDEIFGEKCEKNYIQPTFITDYPKEMSPLTKEHRTNPELTERF 413
Cdd:cd00775 161 TGIDFPELDLeqpEELAKLLAKLIKEKIEkPRTLGKLLDKLFEEFVEPTLIQPTFIIDHPVEISPLAKRHRSNPGLTERF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 414 ELMVNGKELANAYSELNDPIDQRERFEEQLKLSEKGDDEAMYIDNDFIRALEYGMPPTSGMGIGMDRLVMLLTGQESIQE 493
Cdd:cd00775 241 ELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLTDSNSIRD 320
|
....*....
gi 922688387 494 VLLFPQMKP 502
Cdd:cd00775 321 VILFPAMRP 329
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
6-504 |
2.24e-178 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 533.00 E-value: 2.24e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 6 LSEQEVVRRNSLEQLRNLGIDPYPAAEytvnAYSAEIKRNFNDDENaakRQVSIAGRIMSRRIMGKATFMELQDAEGRIQ 85
Cdd:PRK02983 610 LPEQVRVRLAKLEALRAAGVDPYPVGV----PPTHTVAEALDAPTG---EEVSVSGRVLRIRDYGGVLFADLRDWSGELQ 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 86 IYITRDDICPGEDKEFyntvvKKCTDIGDFIGVKGYVFRTQMGEISVHVQEMTFLSKAIRPLPvvkekdgEVFDGFTDPE 165
Cdd:PRK02983 683 VLLDASRLEQGSLADF-----RAAVDLGDLVEVTGTMGTSRNGTLSLLVTSWRLAGKCLRPLP-------DKWKGLTDPE 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 166 QRYRQRYVDLVVNSHVKDIFLKRTMVFNSMRSFFNERGYIEVDTPVLQSIPGGAAARPFITHHNALDIPLYLRIANELYL 245
Cdd:PRK02983 751 ARVRQRYLDLAVNPEARDLLRARSAVVRAVRETLVARGFLEVETPILQQVHGGANARPFVTHINAYDMDLYLRIAPELYL 830
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 246 KRLIVGGFDGVYEFSRNFRNEGMDRTHNPEFTAMEIYVAYKDYNWMMNFTEQMLERICMDVLGTTQV-----KVGEKLID 320
Cdd:PRK02983 831 KRLCVGGVERVFELGRNFRNEGVDATHNPEFTLLEAYQAHADYDTMRDLTRELIQNAAQAAHGAPVVmrpdgDGVLEPVD 910
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 321 FKAPYKRVTMIEAIHEHTGIDIS-GMNEAELRQVCDKLGVEHNETMGKGKLIDEIFGEKCEKNYIQPTFITDYPKEMSPL 399
Cdd:PRK02983 911 ISGPWPVVTVHDAVSEALGEEIDpDTPLAELRKLCDAAGIPYRTDWDAGAVVLELYEHLVEDRTTFPTFYTDFPTSVSPL 990
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 400 TKEHRTNPELTERFELMVNGKELANAYSELNDPIDQRERFEEQLKLSEKGDDEAMYIDNDFIRALEYGMPPTSGMGIGMD 479
Cdd:PRK02983 991 TRPHRSDPGLAERWDLVAWGVELGTAYSELTDPVEQRRRLTEQSLLAAGGDPEAMELDEDFLQALEYAMPPTGGLGMGVD 1070
|
490 500
....*....|....*....|....*
gi 922688387 480 RLVMLLTGQeSIQEVLLFPQMKPEK 504
Cdd:PRK02983 1071 RLVMLLTGR-SIRETLPFPLVKPRQ 1094
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
4-504 |
6.33e-166 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 481.87 E-value: 6.33e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 4 LELSEQEVVRRNSLEQLRNLGIdPYP---AAEYTVNAYSAEIKRNFNDDENAAKRQVSIAGRIMSRRIMGKATFMELQDA 80
Cdd:PRK12445 13 IDFNDELRNRREKLAALRQQGV-AFPndfRRDHTSDQLHEEFDAKDNQELESLNIEVSVAGRMMTRRIMGKASFVTLQDV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 81 EGRIQIYITRDDICPGedkeFYNTVVKKCtDIGDFIGVKGYVFRTQMGEISVHVQEMTFLSKAIRPLPvvkekdgEVFDG 160
Cdd:PRK12445 92 GGRIQLYVARDSLPEG----VYNDQFKKW-DLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLP-------DKFHG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 161 FTDPEQRYRQRYVDLVVNSHVKDIFLKRTMVFNSMRSFFNERGYIEVDTPVLQSIPGGAAARPFITHHNALDIPLYLRIA 240
Cdd:PRK12445 160 LQDQEVRYRQRYLDLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 241 NELYLKRLIVGGFDGVYEFSRNFRNEGMDRTHNPEFTAMEIYVAYKDYNWMMNFTEQMLERICMDVLGTTQVKVGEKLID 320
Cdd:PRK12445 240 PELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 321 FKAPYKRVTMIEAIHEH----TGIDISGMNEAelRQVCDKLGVEHNETMGKGKLIDEIFGEKCEKNYIQPTFITDYPKEM 396
Cdd:PRK12445 320 FGKPFEKLTMREAIKKYrpetDMADLDNFDAA--KALAESIGITVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 397 SPLTKEHRTNPELTERFELMVNGKELANAYSELNDPIDQRERFEEQLKLSEKGDDEAMYIDNDFIRALEYGMPPTSGMGI 476
Cdd:PRK12445 398 SPLARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGI 477
|
490 500
....*....|....*....|....*...
gi 922688387 477 GMDRLVMLLTGQESIQEVLLFPQMKPEK 504
Cdd:PRK12445 478 GIDRMIMLFTNSHTIRDVILFPAMRPQK 505
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
13-502 |
5.90e-125 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 379.74 E-value: 5.90e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 13 RRNSLEQLRNLGIDPYPAA-EYTVNAYS-AEIKRNFNDDENAAKRQVSIAGRIMSRRIMG-KATFMELQDAEGRIQIY-- 87
Cdd:PTZ00417 89 RSKFIQEQKAKGINPYPHKfERTITVPEfVEKYQDLASGEHLEDTILNVTGRIMRVSASGqKLRFFDLVGDGAKIQVLan 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 88 ITRDDICPGEDKEFYNTVVKkctdiGDFIGVKGYVFRTQMGEISVHVQEMTFLSKAIRPLPVVKekdgevfdGFTDPEQR 167
Cdd:PTZ00417 169 FAFHDHTKSNFAECYDKIRR-----GDIVGIVGFPGKSKKGELSIFPKETIILSPCLHMLPMKY--------GLKDTEIR 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 168 YRQRYVDLVVNSHVKDIFLKRTMVFNSMRSFFNERGYIEVDTPVLQSIPGGAAARPFITHHNALDIPLYLRIANELYLKR 247
Cdd:PTZ00417 236 YRQRYLDLMINESTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLVAGGANARPFITHHNDLDLDLYLRIATELPLKM 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 248 LIVGGFDGVYEFSRNFRNEGMDRTHNPEFTAMEIYVAYKDYNWMMNFTEQMLERICMDVLGTTQV---KVGEKL----ID 320
Cdd:PTZ00417 316 LIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHLFGTYKIlynKDGPEKdpieID 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 321 FKAPYKRVTMIEAIHEHTGIDISG-MNEAELRQVCDKLGVEHNETM----GKGKLIDEIFGEKCEKNYI-QPTFITDYPK 394
Cdd:PTZ00417 396 FTPPYPKVSIVEELEKLTNTKLEQpFDSPETINKMINLIKENKIEMpnppTAAKLLDQLASHFIENKYPnKPFFIIEHPQ 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 395 EMSPLTKEHRTNPELTERFELMVNGKELANAYSELNDPIDQRERFEEQLKLSEKGDDEAMYIDNDFIRALEYGMPPTSGM 474
Cdd:PTZ00417 476 IMSPLAKYHRSKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCTSLEYGLPPTGGL 555
|
490 500
....*....|....*....|....*...
gi 922688387 475 GIGMDRLVMLLTGQESIQEVLLFPQMKP 502
Cdd:PTZ00417 556 GLGIDRITMFLTNKNCIKDVILFPTMRP 583
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
163-501 |
1.97e-124 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 368.82 E-value: 1.97e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 163 DPEQRYRQRYVDLVvNSHVKDIFLKRTMVFNSMRSFFNERGYIEVDTPVLQSIPGGAAARPFITHHNALDIPLYLRIANE 242
Cdd:pfam00152 1 DEETRLKYRYLDLR-RPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 243 LYLKRLIVGGFDGVYEFSRNFRNEGMDRTHNPEFTAMEIYVAYKDYNWMMNFTEQMLERICMDVLGTTQVKVGEKLIDFK 322
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 323 APYKRVTMIEAIHEHTGIDIS----GMNEAELRqvcdklgvehnetmgkgkLIDEIFGEKCEKNyiqPTFITDYPKEMSP 398
Cdd:pfam00152 160 KPFPRITYAEAIEKLNGKDVEelgyGSDKPDLR------------------FLLELVIDKNKFN---PLWVTDFPAEHHP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 399 LTKEHRTN-PELTERFELMVNGKELANAYSELNDPIDQRERFEEQLKLSEkgddEAMYIDNDFIRALEYGMPPTSGMGIG 477
Cdd:pfam00152 219 FTMPKDEDdPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDPE----EAEEKFGFYLDALKYGAPPHGGLGIG 294
|
330 340
....*....|....*....|....
gi 922688387 478 MDRLVMLLTGQESIQEVLLFPQMK 501
Cdd:pfam00152 295 LDRLVMLLTGLESIREVIAFPKTR 318
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
50-516 |
8.97e-117 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 360.89 E-value: 8.97e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 50 ENAAKRQVSIAGRIMSRRIMGKATFMELQDAEGRIQI------YITRDDIcpgedkefynTVVKKCTDIGDFIGVKGYVF 123
Cdd:PTZ00385 103 DRAAQATVRVAGRVTSVRDIGKIIFVTIRSNGNELQVvgqvgeHFTREDL----------KKLKVSLRVGDIIGADGVPC 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 124 RTQMGEISVHVQEMTFLSKAIRPLPVVKeKDGEVFDGFTDPEQRYRQRYVDLVVNSHVKDIFLKRTMVFNSMRSFFNERG 203
Cdd:PTZ00385 173 RMQRGELSVAASRMLILSPYVCTDQVVC-PNLRGFTVLQDNDVKYRYRFTDMMTNPCVIETIKKRHVMLQALRDYFNERN 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 204 YIEVDTPVLQSIPGGAAARPFITHHNALDIPLYLRIANELYLKRLIVGGFDGVYEFSRNFRNEGMDRTHNPEFTAMEIYV 283
Cdd:PTZ00385 252 FVEVETPVLHTVASGANAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTSCEFYA 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 284 AYKDYNWMMNFTEQMLERICMDVLGTTQVKV-------GEKLIDFKAPYKRVTMIEAIHEHTGIDISGMNE-------AE 349
Cdd:PTZ00385 332 AYHTYEDLMPMTEDIFRQLAMRVNGTTVVQIypenahgNPVTVDLGKPFRRVSVYDEIQRMSGVEFPPPNElntpkgiAY 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 350 LRQVCDKLGVEHNETMGKGKLIDEIFGEKCEKNYIQPTFITDYPKEMSPLTKEHRTNPELTERFELMVNGKELANAYSEL 429
Cdd:PTZ00385 412 MSVVMLRYNIPLPPVRTAAKMFEKLIDFFITDRVVEPTFVMDHPLFMSPLAKEQVSRPGLAERFELFVNGIEYCNAYSEL 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 430 NDPIDQRERFEEQLKLSEKGDDEAMYIDNDFIRALEYGMPPTSGMGIGMDRLVMLLTGQESIQEVLLFPQMKpEKVAPRD 509
Cdd:PTZ00385 492 NDPHEQYHRFQQQLVDRQGGDEEAMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFPLLR-QDIRSHD 570
|
....*..
gi 922688387 510 TKEKFAV 516
Cdd:PTZ00385 571 SKRRHKT 577
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
185-502 |
1.30e-96 |
|
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: 295.54 E-value: 1.30e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 185 FLKRTMVFNSMRSFFNERGYIEVDTPVLQSIPGGAAARPFITHHNALDIPLYLRIANELYLKRLIVGGFDGVYEFSRNFR 264
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 265 NEGMDRTHNPEFTAMEIYVAYKDYNWMMNFTEQMLERICMDVLGTTQVKVGEKLIDFKAPYKRVTMIEAIhehtgidisg 344
Cdd:cd00669 81 NEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYGFELEDFGLPFPRLTYREAL---------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 345 mneaelrqvcdklgvehnetmgkgklideifgekceKNYIQPTFITDYPKEM-SPLTKEHRTNPELTERFELMVNGKELA 423
Cdd:cd00669 151 ------------------------------------ERYGQPLFLTDYPAEMhSPLASPHDVNPEIADAFDLFINGVEVG 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 922688387 424 NAYSELNDPIDQRERFEEQLKlsekGDDEAMYIDNDFIRALEYGMPPTSGMGIGMDRLVMLLTGQESIQEVLLFPQMKP 502
Cdd:cd00669 195 NGSSRLHDPDIQAEVFQEQGI----NKEAGMEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKMRR 269
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
186-495 |
1.01e-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: 253.10 E-value: 1.01e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 186 LKRTMVFNSMRSFFNERGYIEVDTPVLQSIPGGAAA-RPFIT---HHNALDIPLYLRIANELYLKRLIVGGFDGVYEFSR 261
Cdd:COG2269 7 RARARLLAAIRAFFAERGVLEVETPALSVAPGTDPHlDSFATefiGPDGGGRPLYLHTSPEFAMKRLLAAGSGPIYQIAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 262 NFRNEGMDRTHNPEFTAMEIYVAYKDYNWMMNFTEQMLERicmdVLGTTQvkvgeklidfKAPYKRVTMIEAIHEHTGID 341
Cdd:COG2269 87 VFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQL----VLGAAG----------FAPAERLSYQEAFLRYLGID 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 342 ISGMNEAELRQVCDKLGVEHNETMGKGKLIDEIFGEKCEKNYIQ--PTFITDYPKEMSPLTKEHRTNPELTERFELMVNG 419
Cdd:COG2269 153 PLTADLDELAAAAAAAGLRVADDDDRDDLLDLLLSERVEPQLGRdrPTFLYDYPASQAALARISPDDPRVAERFELYACG 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 922688387 420 KELANAYSELNDPIDQRERFEEQLKLSEKGDDEAMYIDNDFIRALEYGMPPTSGMGIGMDRLVMLLTGQESIQEVL 495
Cdd:COG2269 233 VELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALGAERIDDVL 308
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
198-495 |
1.53e-79 |
|
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: 252.09 E-value: 1.53e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 198 FFNERGYIEVDTPVLQSIPGGAAA-RPFITH---HNALDIPLYLRIANELYLKRLIVGGFDGVYEFSRNFRNEGMDRTHN 273
Cdd:TIGR00462 1 FFAERGVLEVETPLLSPAPVTDPHlDAFATEfvgPDGQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 274 PEFTAMEIYVAYKDYNWMMNFTEQMLERICMDVLgttqvkvgeklidfkAPYKRVTMIEAIHEHTGIDISGMNEAELRQV 353
Cdd:TIGR00462 81 PEFTMLEWYRPGFDYHDLMDEVEALLQELLGDPF---------------APAERLSYQEAFLRYAGIDPLTASLAELQAA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 354 CDKLGVEHNETMGKGKLIDEIFGEKCEKNYIQ--PTFITDYPKEMSPLTKEHRTNPELTERFELMVNGKELANAYSELND 431
Cdd:TIGR00462 146 AAAHGIRASEEDDRDDLLDLLFSEKVEPHLGFgrPTFLYDYPASQAALARISPDDPRVAERFELYIKGLELANGFHELTD 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 922688387 432 PIDQRERFEEQLKLSEKGDDEAMYIDNDFIRALEYGMPPTSGMGIGMDRLVMLLTGQESIQEVL 495
Cdd:TIGR00462 226 AAEQRRRFEADNALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDVL 289
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
182-494 |
5.36e-58 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 196.30 E-value: 5.36e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 182 KDIFLKRTMVFNSMRSFFNERGYIEVDTPVLQSIP--------------GGAAARPfithhnaldIPLYLRIANELYLKR 247
Cdd:PRK09350 2 IPNLLKRAKIIAEIRRFFADRGVLEVETPILSQATvtdihlvpfetrfvGPGASQG---------KTLWLMTSPEYHMKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 248 LIVGGFDGVYEFSRNFRNEGMDRTHNPEFTAMEIYVAYKDYNWMMNFTEQMLericmdvlgttqvkvgeKLIDFKAPYKR 327
Cdd:PRK09350 73 LLAAGSGPIFQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLL-----------------QQVLDCEPAES 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 328 VTMIEAIHEHTGIDISGMNEAELRQVCDKLGVEH--NETMGKGKLIDEIFGEKCEKNYIQ--PTFITDYPKEMSPLTKEH 403
Cdd:PRK09350 136 LSYQQAFLRYLGIDPLSADKTQLREVAAKLGLSNiaDEEEDRDTLLQLLFTFGVEPNIGKekPTFVYHFPASQAALAKIS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 404 RTNPELTERFELMVNGKELANAYSELNDPIDQRERFEEQLKLSEKGDDEAMYIDNDFIRALEYGMPPTSGMGIGMDRLVM 483
Cdd:PRK09350 216 TEDHRVAERFEVYFKGIELANGFHELTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCSGVALGVDRLIM 295
|
330
....*....|.
gi 922688387 484 LLTGQESIQEV 494
Cdd:PRK09350 296 LALGAESISEV 306
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
56-175 |
5.13e-53 |
|
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: 176.13 E-value: 5.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 56 QVSIAGRIMSRRIMGKATFMELQDAEGRIQIYITRDDICPGEDKEFyntvvKKCTDIGDFIGVKGYVFRTQMGEISVHVQ 135
Cdd:cd04322 1 EVSVAGRIMSKRGSGKLSFADLQDESGKIQVYVNKDDLGEEEFEDF-----KKLLDLGDIIGVTGTPFKTKTGELSIFVK 75
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 922688387 136 EMTFLSKAIRPLPvvkekdgEVFDGFTDPEQRYRQRYVDL 175
Cdd:cd04322 76 EFTLLSKSLRPLP-------EKFHGLTDVETRYRQRYLDL 108
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
38-498 |
1.90e-44 |
|
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: 163.30 E-value: 1.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 38 YSAEIKRNFNDDEnaakrqVSIAGRIMSRRIMGKATFMELQDAEGRIQIyitrddICPGEDKEFYNTVvKKCTdIGDFIG 117
Cdd:COG0017 4 YIKDLLPEHVGQE------VTVAGWVRTKRDSGGISFLILRDGSGFIQV------VVKKDKLENFEEA-KKLT-TESSVE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 118 VKGYVFRTQM--GEISVHVQEMTFLSKAIRPLPVVKEKdgevfdgfTDPEQRYRQRYVDLVVNShVKDIFLKRTMVFNSM 195
Cdd:COG0017 70 VTGTVVESPRapQGVELQAEEIEVLGEADEPYPLQPKR--------HSLEFLLDNRHLRLRTNR-FGAIFRIRSELARAI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 196 RSFFNERGYIEVDTPVL-QSIPGGAAArpfithhnaL------DIPLYLRIANELYlKRLIVGGFDGVYEFSRNFRNEGM 268
Cdd:COG0017 141 REFFQERGFVEVHTPIItASATEGGGE---------LfpvdyfGKEAYLTQSGQLY-KEALAMALEKVYTFGPTFRAEKS 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 269 D-RTHNPEFTAMEIYVAYKDYNWMMNFTEQMLERIC----------MDVLGTTQVKVgEKLIdfKAPYKRVTMIEAIheh 337
Cdd:COG0017 211 NtRRHLAEFWMIEPEMAFADLEDVMDLAEEMLKYIIkyvlencpeeLEFLGRDVERL-EKVP--ESPFPRITYTEAI--- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 338 tgiDISGMNEAELRQVCDkLGVEHnEtmgkgKLIDEIFGEKceknyiqPTFITDYPKEMSPL-TKEHRTNPELTERFELM 416
Cdd:COG0017 285 ---EILKKSGEKVEWGDD-LGTEH-E-----RYLGEEFFKK-------PVFVTDYPKEIKAFyMKPNPDDPKTVAAFDLL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 417 VNGkelanaYSELndpI--DQRE-RFEEQLK-LSEKGDDEAMYidNDFIRALEYGMPPTSGMGIGMDRLVMLLTGQESIQ 492
Cdd:COG0017 348 APG------IGEI---IggSQREhRYDVLVErIKEKGLDPEDY--EWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIR 416
|
....*.
gi 922688387 493 EVLLFP 498
Cdd:COG0017 417 EVIPFP 422
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
38-498 |
1.21e-42 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 158.43 E-value: 1.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 38 YSAEIKRNFNDDEnaakrqVSIAGRIMSRRIMGKATFMELQDAEGRIQIYITRDdicpgEDKEFYNTVVKkcTDIGDFIG 117
Cdd:PRK05159 6 LTSELTPELDGEE------VTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKK-----VDEELFETIKK--LKRESVVS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 118 VKGYVFRTQM--GEISVHVQEMTFLSKAIRPLP--VVKEKDgevfdgfTDPEQRYRQRYVDLVvNSHVKDIFLKRTMVFN 193
Cdd:PRK05159 73 VTGTVKANPKapGGVEVIPEEIEVLNKAEEPLPldISGKVL-------AELDTRLDNRFLDLR-RPRVRAIFKIRSEVLR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 194 SMRSFFNERGYIEVDTP--VLQSIPGGAAARPfITHhnaLDIPLYLRIANELYlKRLIVG-GFDGVYEFSRNFRNEGMDR 270
Cdd:PRK05159 145 AFREFLYENGFTEIFTPkiVASGTEGGAELFP-IDY---FEKEAYLAQSPQLY-KQMMVGaGFERVFEIGPVFRAEEHNT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 271 T-HNPEFTAMEIYVAY-KDYNWMMNFTEQMLERICMDVLGTTQVKV---GEKLIDFKAPYKRVTMIEAIhehtgiDISGM 345
Cdd:PRK05159 220 SrHLNEYTSIDVEMGFiDDHEDVMDLLENLLRYMYEDVAENCEKELellGIELPVPETPIPRITYDEAI------EILKS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 346 NEAELRQVCDkLGVEHNetmgkgKLIDEIFGEKCEKNYIqptFITDYPKEMSPL-TKEHRTNPELTERFELMVNGKELAN 424
Cdd:PRK05159 294 KGNEISWGDD-LDTEGE------RLLGEYVKEEYGSDFY---FITDYPSEKRPFyTMPDEDDPEISKSFDLLFRGLEITS 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 922688387 425 AyselndpiDQRE-RFEEQL-KLSEKG---DDEAMYIDndfirALEYGMPPTSGMGIGMDRLVMLLTGQESIQEVLLFP 498
Cdd:PRK05159 364 G--------GQRIhRYDMLVeSIKEKGlnpESFEFYLE-----AFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFP 429
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
38-507 |
6.52e-38 |
|
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative asparaginyl-tRNA synthetases (asnS), archaeal/eukaryotic type aspartyl-tRNA synthetases (aspS_arch), and bacterial type aspartyl-tRNA synthetases (aspS_bact), there is a striking similarity between asnS and aspS_arch in gap pattern and in sequence, and a striking divergence of aspS_bact. Consequently, a separate model was built for each of the three groups. This model, aspS_arch, represents aspartyl-tRNA synthetases from the eukaryotic cytosol and from the Archaea. In some species, this enzyme aminoacylates tRNA for both Asp and Asn; Asp-tRNA(asn) is subsequently transamidated to Asn-tRNA(asn). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273087 [Multi-domain] Cd Length: 428 Bit Score: 144.97 E-value: 6.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 38 YSAEIKRNFNDDEnaakrqVSIAGRIMSRRIMGKATFMELQDAEGRIQIYITRDDIcpgeDKEFYNTVVKkcTDIGDFIG 117
Cdd:TIGR00458 2 YSADIKPEMDGQE------VTFMGWVHEIRDLGGLIFVLLRDREGLIQITAPAKKV----SKNLFKWAKK--LNLESVVA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 118 VKGYVFRTQ--MGEISVHVQEMTFLSKAIRPLPVVKEKDGEvfdgfTDPEQRYRQRYVDLVVNShVKDIFLKRTMVFNSM 195
Cdd:TIGR00458 70 VRGIVKIKEkaPGGFEIIPTKIEVINEAKEPLPLDPTEKVP-----AELDTRLDYRFLDLRRPT-VQAIFRIRSGVLESV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 196 RSFFNERGYIEVDTPVLQSIP--GGAAARPfITHhnaLDIPLYLRIANELYLKRLIVGGFDGVYEFSRNFRNEGMD-RTH 272
Cdd:TIGR00458 144 REFLAEEGFIEVHTPKLVASAteGGTELFP-ITY---FEREAFLGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNtHRH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 273 NPEFTAMEIYVAYKDYNWMMNFTEQMLERI-------CMDVLGTtqvkVGEKLIDFKAPYKRVTMIEAIhehtgidisgm 345
Cdd:TIGR00458 220 LNEATSIDIEMAFEDHHDVMDILEELVVRVfedvperCAHQLET----LEFKLEKPEGKFVRLTYDEAI----------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 346 neaelrQVCDKLGVE--HNETMGKGKLidEIFGEKCEKNYiqptFITDYPKEMSPL-TKEHRTNPELTERFELMVNGKEL 422
Cdd:TIGR00458 285 ------EMANAKGVEigWGEDLSTEAE--KALGEEMDGLY----FITDWPTEIRPFyTMPDEDNPEISKSFDLMYRDLEI 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 423 ANAYSELNDPIDQRERFEEQlKLSEKGDDeamyidnDFIRALEYGMPPTSGMGIGMDRLVMLLTGQESIQEVLLFPQmKP 502
Cdd:TIGR00458 353 SSGAQRIHLHDLLVERIKAK-GLNPEGFK-------DYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFPR-DR 423
|
....*
gi 922688387 503 EKVAP 507
Cdd:TIGR00458 424 KRLTP 428
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
163-498 |
8.65e-36 |
|
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure and the presence of three characteristic sequence motifs in the core domain. This family includes AsnRS as well as a subgroup of AspRS. AsnRS and AspRS are homodimers, which attach either asparagine or aspartate to the 3'OH group of ribose of the appropriate tRNA. While archaea lack asnRS, they possess a non-discriminating aspRS, which can mischarge Asp-tRNA with Asn. Subsequently, a tRNA-dependent aspartate amidotransferase converts the bound aspartate to asparagine. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate.
Pssm-ID: 238399 [Multi-domain] Cd Length: 322 Bit Score: 136.54 E-value: 8.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 163 DPEQRYRQRYVDLVVNShVKDIFLKRTMVFNSMRSFFNERGYIEVDTPVLQSIP--GGAAARPFithhNALDIPLYLRIA 240
Cdd:cd00776 3 NLETLLDNRHLDLRTPK-VQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDteGGAELFKV----SYFGKPAYLAQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 241 NELYLKRLIvGGFDGVYEFSRNFRNEGMD-RTHNPEFTAMEIYVAY-KDYNWMMNFTEQMLERICMDVL------GTTQV 312
Cdd:cd00776 78 PQLYKEMLI-AALERVYEIGPVFRAEKSNtRRHLSEFWMLEAEMAFiEDYNEVMDLIEELIKYIFKRVLercakeLELVN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 313 KVGEKLIDFKAPYKRVTMIEAIHEhtgidisgmneaeLRQVCDKLGVEHNETMGKG--KLIDEIFGEKceknyiqPTFIT 390
Cdd:cd00776 157 QLNRELLKPLEPFPRITYDEAIEL-------------LREKGVEEEVKWGEDLSTEheRLLGEIVKGD-------PVFVT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 391 DYPKEMSPL-TKEHRTNPELTERFELMVNGK-ELANAYSELNDPIDQRERFEEqlklseKGDDEAMYidNDFIRALEYGM 468
Cdd:cd00776 217 DYPKEIKPFyMKPDDDNPETVESFDLLMPGVgEIVGGSQRIHDYDELEERIKE------HGLDPESF--EWYLDLRKYGM 288
|
330 340 350
....*....|....*....|....*....|
gi 922688387 469 PPTSGMGIGMDRLVMLLTGQESIQEVLLFP 498
Cdd:cd00776 289 PPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
185-498 |
1.23e-26 |
|
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: 109.59 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 185 FLKRTMVFNSMRSFFNERGYIEVDTPVL-QSIPGGAaaRPFI----THHN---ALDIplylriANELYLKRLIVGGFDGV 256
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILtKSTPEGA--RDFLvpsrLHPGkfyALPQ------SPQLFKQLLMVSGFDRY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 257 YEFSRNFRNEGM--DRthNPEFTAMEIYVAYKDYNWMMNFTEQMLERICMDVLGttqvkvgeklIDFKAPYKRVTMIEAI 334
Cdd:cd00777 73 FQIARCFRDEDLraDR--QPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG----------VELTTPFPRMTYAEAM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 335 HEHtGIDIS--------GMNEAElrqvcDKLGVEHNE-TMGKGKLIDEIfgekceknyiqptfitdypkemspltkehRT 405
Cdd:cd00777 141 ERY-GFKFLwivdfplfEWDEEE-----GRLVSAHHPfTAPKEEDLDLL-----------------------------EK 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 406 NPE--LTERFELMVNGKELANAYSELNDPIDQRERFEeQLKLSEKGDDEAMyidNDFIRALEYGMPPTSGMGIGMDRLVM 483
Cdd:cd00777 186 DPEdaRAQAYDLVLNGVELGGGSIRIHDPDIQEKVFE-ILGLSEEEAEEKF---GFLLEAFKYGAPPHGGIALGLDRLVM 261
|
330
....*....|....*
gi 922688387 484 LLTGQESIQEVLLFP 498
Cdd:cd00777 262 LLTGSESIRDVIAFP 276
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
55-513 |
2.62e-25 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 110.85 E-value: 2.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 55 RQVSIAGRIMSRRIMGKATFMELQDAEGRIQIYITRDDICPGEDKEFYNTVVKKCtdigdfIGVKGYVFR---------T 125
Cdd:PRK12820 19 REVCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFSPEAAPADVYELAASLRAEFC------VALQGEVQKrleetenphI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 126 QMGEISVHVQEMTFLSKA-IRPLPVVKEK----DGEVFDGFTDPEQRYRQRYVDLVVNShVKDIFLKRTMVFNSMRSFFN 200
Cdd:PRK12820 93 ETGDIEVFVRELSILAASeALPFAISDKAmtagAGSAGADAVNEDLRLQYRYLDIRRPA-MQDHLAKRHRIIKCARDFLD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 201 ERGYIEVDTPVL-QSIPGGAaaRPFITHHNALDIPLY-LRIANELYLKRLIVGGFDGVYEFSRNFRNEGMDRTHNPEFTA 278
Cdd:PRK12820 172 SRGFLEIETPILtKSTPEGA--RDYLVPSRIHPKEFYaLPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEFTQ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 279 MEIYVAYKDYNWMMNFTEQMLERI-------------------CMDVLGTTQ--VKVGEKLIDFKAPYKRVT--MIEAIH 335
Cdd:PRK12820 250 LDIEASFIDEEFIFELIEELTARMfaiggialprpfprmpyaeAMDTTGSDRpdLRFDLKFADATDIFENTRygIFKQIL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 336 EH----TGIDISGMNEAELRQVC-DKLGVEHNETMG-KGKLIDEIFGEKCEKNYIQ------------------------ 385
Cdd:PRK12820 330 QRggriKGINIKGQSEKLSKNVLqNEYAKEIAPSFGaKGMTWMRAEAGGLDSNIVQffsadekealkrrfhaedgdviim 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 386 ---------------------------------PTFITDYP----KEMSPLTKEHR--TNPELTE--------------- 411
Cdd:PRK12820 410 iadascaivlsalgqlrlhladrlglipegvfhPLWITDFPlfeaTDDGGVTSSHHpfTAPDREDfdpgdieelldlrsr 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 412 RFELMVNGKELANAYSELNDPIDQRERFeEQLKLSEKGDDEAMYIdndFIRALEYGMPPTSGMGIGMDRLVMLLTGQESI 491
Cdd:PRK12820 490 AYDLVVNGEELGGGSIRINDKDIQLRIF-AALGLSEEDIEDKFGF---FLRAFDFAAPPHGGIALGLDRVVSMILQTPSI 565
|
570 580
....*....|....*....|....*.
gi 922688387 492 QEVLLFPQMK----PEKVAPRDTKEK 513
Cdd:PRK12820 566 REVIAFPKNRsaacPLTGAPSEVAQE 591
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
56-498 |
4.19e-23 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 103.22 E-value: 4.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 56 QVSIAGRIMSRRIMGKATFMELQDAEGRIQIYITrddicpgEDKEFYNTV--VKK--CtdigdfIGVKGYVFR------- 124
Cdd:PRK00476 19 TVTLCGWVHRRRDHGGLIFIDLRDREGIVQVVFD-------PDAEAFEVAesLRSeyV------IQVTGTVRArpegtvn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 125 TQM--GEISVHVQEMTFLSKAiRPLPVVKEKDGEVfdgftDPEQRYRQRYVDLVvNSHVKDIFLKRTMVFNSMRSFFNER 202
Cdd:PRK00476 86 PNLptGEIEVLASELEVLNKS-KTLPFPIDDEEDV-----SEELRLKYRYLDLR-RPEMQKNLKLRSKVTSAIRNFLDDN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 203 GYIEVDTPVL-QSIPGGaaARPFI----THHN---ALdiP----LYlrianelylKRLI-VGGFDGVYEFSRNFRNEGM- 268
Cdd:PRK00476 159 GFLEIETPILtKSTPEG--ARDYLvpsrVHPGkfyAL--PqspqLF---------KQLLmVAGFDRYYQIARCFRDEDLr 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 269 -DRthNPEFTAMEIYVAYKDYNWMMNFTEQMLERICMDVLGttqVKVGE-------------------------KLID-- 320
Cdd:PRK00476 226 aDR--QPEFTQIDIEMSFVTQEDVMALMEGLIRHVFKEVLG---VDLPTpfprmtyaeamrrygsdkpdlrfglELVDvt 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 321 ----------FKAPYKRVTMIEAIH-------------------------------EHTGIDISG-----MNEAELRQVC 354
Cdd:PRK00476 301 dlfkdsgfkvFAGAANDGGRVKAIRvpggaaqlsrkqideltefakiygakglayiKVNEDGLKGpiakfLSEEELAALL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 355 DKLGVEH--------------NETMGK-----GK---LIDEifgekcekNYIQPTFITDYP-----KEMSPLTKEH---- 403
Cdd:PRK00476 381 ERTGAKDgdliffgadkakvvNDALGAlrlklGKelgLIDE--------DKFAFLWVVDFPmfeydEEEGRWVAAHhpft 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 404 RTNPELTERFELMVNGKELANAY------SEL-------NDPIDQRERFEEqLKLSEkgdDEAmyiDNDF---IRALEYG 467
Cdd:PRK00476 453 MPKDEDLDELETTDPGKARAYAYdlvlngYELgggsiriHRPEIQEKVFEI-LGISE---EEA---EEKFgflLDALKYG 525
|
570 580 590
....*....|....*....|....*....|.
gi 922688387 468 MPPTSGMGIGMDRLVMLLTGQESIQEVLLFP 498
Cdd:PRK00476 526 APPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
176-507 |
2.04e-21 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 95.47 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 176 VVNSHVKDIFLKRTMVFNSMRSFFNERGYIEVDTPVLQSI-----PGGAAARPFithhnALDIPLYlriANELYL----- 245
Cdd:PRK06462 21 ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIISPStdplmGLGSDLPVK-----QISIDFY---GVEYYLadsmi 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 246 --KRLIVGGFDGVYEFSRNFRNEGMDR---THNPEFTAMEIYVAYKDYNWMMNFTEQMLERICMDVLGTTQ---VKVGEK 317
Cdd:PRK06462 93 lhKQLALRMLGKIFYLSPNFRLEPVDKdtgRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHEdelEFFGRD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 318 LIDFKAPYKRVTMIEAIHEHTGIDISGMNEAELRQVCDKLGVEHNEtmgkgklideifgekceknyiQPTFITDYPKEMS 397
Cdd:PRK06462 173 LPHLKRPFKRITHKEAVEILNEEGCRGIDLEELGSEGEKSLSEHFE---------------------EPFWIIDIPKGSR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 398 PL-TKEHRTNPELTERFELMvngkeLANAYSELndpIDQRERFEEQLKLSEK----GDDEAMYidNDFIRALEYGMPPTS 472
Cdd:PRK06462 232 EFyDREDPERPGVLRNYDLL-----LPEGYGEA---VSGGEREYEYEEIVERirehGVDPEKY--KWYLEMAKEGPLPSA 301
|
330 340 350
....*....|....*....|....*....|....*
gi 922688387 473 GMGIGMDRLVMLLTGQESIQEVLLFPQmKPEKVAP 507
Cdd:PRK06462 302 GFGIGVERLTRYICGLRHIREVQPFPR-VPGIVAL 335
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
50-512 |
2.66e-19 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 91.77 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 50 ENAAKRQVSIAGRIMSRRIMGKATFMELQDAEGRIQIYITRDDicPGEDKEFYNTVVKKCTdigdfIGVKGYVF------ 123
Cdd:PLN02903 68 VNDVGSRVTLCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDE--FPEAHRTANRLRNEYV-----VAVEGTVRsrpqes 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 124 ---RTQMGEISVHVQEMTFLSKAIRPLP-VVKEKDGEvfDGFTDPEQRYRQRYVDLVVNSHVKDIFLkRTMVFNSMRSFF 199
Cdd:PLN02903 141 pnkKMKTGSVEVVAESVDILNVVTKSLPfLVTTADEQ--KDSIKEEVRLRYRVLDLRRPQMNANLRL-RHRVVKLIRRYL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 200 NER-GYIEVDTPVL-QSIPGGAaaRPFITHHNALDIPLY-LRIANELYLKRLIVGGFDGVYEFSRNFRNEGMDRTHNPEF 276
Cdd:PLN02903 218 EDVhGFVEIETPILsRSTPEGA--RDYLVPSRVQPGTFYaLPQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEF 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 277 TAMEIYVAYKDYNWMMNFTEQMLERICMDVLGttqvkvgeklIDFKAPYKRVTMIEAIHEHTG-----------IDISGM 345
Cdd:PLN02903 296 TQLDMELAFTPLEDMLKLNEDLIRQVFKEIKG----------VQLPNPFPRLTYAEAMSKYGSdkpdlryglelVDVSDV 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 346 ------------------------------------------NEA-----------------EL---RQVCDKLGVEHNE 363
Cdd:PLN02903 366 faessfkvfagalesggvvkaicvpdgkkisnntalkkgdiyNEAiksgakglaflkvlddgELegiKALVESLSPEQAE 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 364 TM------GKGKLIDEIFGEKCEKN--------YIQPT------------FITDYPK-EMSPltKEHR----------TN 406
Cdd:PLN02903 446 QLlaacgaGPGDLILFAAGPTSSVNktldrlrqFIAKTldlidpsrhsilWVTDFPMfEWNE--DEQRlealhhpftaPN 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 407 PELTE--------RFELMVNGKELANAYSElndpIDQRERFEEQLKLSEKGDDEAmyiDNDF---IRALEYGMPPTSGMG 475
Cdd:PLN02903 524 PEDMGdlssaralAYDMVYNGVEIGGGSLR----IYRRDVQQKVLEAIGLSPEEA---ESKFgylLEALDMGAPPHGGIA 596
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 922688387 476 IGMDRLVMLLTGQESIQEVLLFPQMK---------PEKVAPRDTKE 512
Cdd:PLN02903 597 YGLDRLVMLLAGAKSIRDVIAFPKTTtaqcaltraPSEVDDKQLQD 642
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
56-500 |
4.25e-18 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 87.09 E-value: 4.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 56 QVSIAGRIMSRRIMGKATFMELQDAEGRIQIYITRDDicpgedKEFYNTVVKKCTdIGDFIGVKGYVFRTQ--MGEISVH 133
Cdd:PRK03932 18 EVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDN------GEEYFEEIKKLT-TGSSVIVTGTVVESPraGQGYELQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 134 VQEMTFLSKAIRPLPVVKEKDGEVFdgftdpeqryrqryvdLVVNSHVK-------DIFLKRTMVFNSMRSFFNERGYIE 206
Cdd:PRK03932 91 ATKIEVIGEDPEDYPIQKKRHSIEF----------------LREIAHLRprtnkfgAVMRIRNTLAQAIHEFFNENGFVW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 207 VDTPVLQ-SIPGGAAARpFITHHNALDI-------PLYLRIANELYLKRLIVGgFDGVYEFSRNFRNEGMD-RTHNPEFT 277
Cdd:PRK03932 155 VDTPIITaSDCEGAGEL-FRVTTLDLDFskdffgkEAYLTVSGQLYAEAYAMA-LGKVYTFGPTFRAENSNtRRHLAEFW 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 278 AMEIYVAYKDYNWMMNFTEQMLERIC----------MDVLGTTQVK-VGEKLIDF-KAPYKRVTMIEAIhehtgiDI--- 342
Cdd:PRK03932 233 MIEPEMAFADLEDNMDLAEEMLKYVVkyvlencpddLEFLNRRVDKgDIERLENFiESPFPRITYTEAI------EIlqk 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 343 SGMNEAELRQVCDKLGVEHnETMgkgkLIDEIFGekceknyiQPTFITDYPKEMSPLTkeHRTNPElterfelmvnGKEL 422
Cdd:PRK03932 307 SGKKFEFPVEWGDDLGSEH-ERY----LAEEHFK--------KPVFVTNYPKDIKAFY--MRLNPD----------GKTV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 423 ANA------YSELndpI--DQRE-RFE------EQLKLSEKgdDEAMYIDndfIRalEYGMPPTSGMGIGMDRLVMLLTG 487
Cdd:PRK03932 362 AAMdllapgIGEI---IggSQREeRLDvleariKELGLNKE--DYWWYLD---LR--RYGSVPHSGFGLGFERLVAYITG 431
|
490
....*....|...
gi 922688387 488 QESIQEVLLFPQM 500
Cdd:PRK03932 432 LDNIRDVIPFPRT 444
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
56-498 |
7.23e-18 |
|
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: 86.98 E-value: 7.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 56 QVSIAGRIMSRRIMGKATFMELQDAEGRIQIYITrddicPGEDKEFYNTV-------VkkctdigdfIGVKGYVFR---- 124
Cdd:COG0173 18 EVTLSGWVHRRRDHGGLIFIDLRDRYGITQVVFD-----PDDSAEAFEKAeklrseyV---------IAVTGKVRArpeg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 125 ---TQM--GEISVHVQEMTFLSKAiRPLPVVKEKDGEVfdgftDPEQRYRQRYVDLVvNSHVKDIFLKRTMVFNSMRSFF 199
Cdd:COG0173 84 tvnPKLptGEIEVLASELEILNKA-KTPPFQIDDDTDV-----SEELRLKYRYLDLR-RPEMQKNLILRHKVTKAIRNYL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 200 NERGYIEVDTPVL-QSIPGGAaaRPFI----THHN---ALdiP----LYlrianelylKRLI-VGGFDGVYEFSRNFRNE 266
Cdd:COG0173 157 DENGFLEIETPILtKSTPEGA--RDYLvpsrVHPGkfyAL--PqspqLF---------KQLLmVSGFDRYFQIARCFRDE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 267 GM--DRthNPEFTA--MEI-YVAYKDynwMMNFTEQMLERICMDVLGttqvkvgeklIDFKAPYKRVTMIEAIH------ 335
Cdd:COG0173 224 DLraDR--QPEFTQldIEMsFVDQED---VFELMEGLIRHLFKEVLG----------VELPTPFPRMTYAEAMErygsdk 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 336 -------EHT-------------------------GIDISG--------------------------------------- 344
Cdd:COG0173 289 pdlrfglELVdvtdifkdsgfkvfagaaenggrvkAINVPGgaslsrkqideltefakqygakglayikvnedglkspia 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 345 --MNEAELRQVCDKLGVEH--------------NETMGK-----GK---LIDEifgekcekNYIQPTFITDYPK-EMSPl 399
Cdd:COG0173 369 kfLSEEELAAILERLGAKPgdliffvadkpkvvNKALGAlrlklGKelgLIDE--------DEFAFLWVVDFPLfEYDE- 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 400 tKEHR--------TNPeLTERFELMVN--GKELANAY------SEL-------NDPIDQRERFEeQLKLSEkgdDEAmyi 456
Cdd:COG0173 440 -EEGRwvamhhpfTMP-KDEDLDLLETdpGKVRAKAYdlvlngYELgggsiriHDPELQEKVFE-LLGISE---EEA--- 510
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 922688387 457 DNDF---IRALEYGMPPTSGMGIGMDRLVMLLTGQESIQEVLLFP 498
Cdd:COG0173 511 EEKFgflLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
49-507 |
5.66e-17 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 83.99 E-value: 5.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 49 DENAAKRQVSIAGRIMSRRIMGKATFMELQDAEGRIQ--IYITRDDICPGEDKefYNTVVKKcTDIGDFIGV-----KGY 121
Cdd:PLN02850 76 GEELAGSEVLIRGRVHTIRGKGKSAFLVLRQSGFTVQcvVFVSEVTVSKGMVK--YAKQLSR-ESVVDVEGVvsvpkKPV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 122 VFRTQMGEIsvHVQEMTFLSKAIRPLPVV----------KEKDGEVFDGFTDPEQ--RYRQRYVDLVVNSHvKDIFLKRT 189
Cdd:PLN02850 153 KGTTQQVEI--QVRKIYCVSKALATLPFNvedaarseseIEKALQTGEQLVRVGQdtRLNNRVLDLRTPAN-QAIFRIQS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 190 MVFNSMRSFFNERGYIEVDTPVL--QSIPGGAAArpFITHHNAldIPLYLRIANELYLKRLIVGGFDGVYEFSRNFRNE- 266
Cdd:PLN02850 230 QVCNLFREFLLSKGFVEIHTPKLiaGASEGGSAV--FRLDYKG--QPACLAQSPQLHKQMAICGDFRRVFEIGPVFRAEd 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 267 GMDRTHNPEFTAMEIYVAYKD-YNWMMNFTEQM-------LERICMDVLGTTQVKVGEKLIDFKAPYKRVTMIEAIH--E 336
Cdd:PLN02850 306 SFTHRHLCEFTGLDLEMEIKEhYSEVLDVVDELfvaifdgLNERCKKELEAIREQYPFEPLKYLPKTLRLTFAEGIQmlK 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 337 HTGIDISGM----NEAELrqvcdKLGvehnetmgkgKLIDEIFGEKceknyiqpTFITD-YPKEMSPL-TKEHRTNPELT 410
Cdd:PLN02850 386 EAGVEVDPLgdlnTESER-----KLG----------QLVKEKYGTD--------FYILHrYPLAVRPFyTMPCPDDPKYS 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 411 ERFELMVNGKELANAYSELNDPidqrERFEEQLKlsEKG---DDEAMYIDndfirALEYGMPPTSGMGIGMDRLVMLLTG 487
Cdd:PLN02850 443 NSFDVFIRGEEIISGAQRVHDP----ELLEKRAE--ECGidvKTISTYID-----SFRYGAPPHGGFGVGLERVVMLFCG 511
|
490 500
....*....|....*....|
gi 922688387 488 QESIQEVLLFPQmKPEKVAP 507
Cdd:PLN02850 512 LNNIRKTSLFPR-DPQRLAP 530
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
56-142 |
6.47e-16 |
|
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. Class 2b aaRSs include the homodimeric aspartyl-, asparaginyl-, and lysyl-tRNA synthetases (AspRS, AsnRS, and LysRS). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Included in this group are archeal and archeal-like AspRSs which are non-discriminating and can charge both tRNAAsp and tRNAAsn. E. coli cells have two isoforms of LysRSs (LysS and LysU) encoded by two distinct genes, which are differentially regulated. The cytoplasmic and the mitochondrial isoforms of human LysRS are encoded by a single gene. Yeast cytoplasmic and mitochondrial LysRSs participate in mitochondrial import of cytoplasmic tRNAlysCUU. In addition to their housekeeping role, human LysRS may function as a signaling molecule that activates immune cells. Tomato LysRS may participate in a process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging. AsnRS is immunodominant antigen of the filarial nematode Brugia malayai and is of interest as a target for anti-parasitic drug design. Human AsnRS has been shown to be a pro-inflammatory chemokine which interacts with CCR3 chemokine receptors on T cells, immature dendritic cells and macrophages.
Pssm-ID: 239766 [Multi-domain] Cd Length: 85 Bit Score: 72.98 E-value: 6.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 56 QVSIAGRIMSRRIMGKATFMELQDAEGRIQIYITrddicPGEDKEFYNTVvkKCTDIGDFIGVKGYVFRTQ-----MGEI 130
Cdd:cd04100 1 EVTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVN-----KEELGEFFEEA--EKLRTESVVGVTGTVVKRPegnlaTGEI 73
|
90
....*....|..
gi 922688387 131 SVHVQEMTFLSK 142
Cdd:cd04100 74 ELQAEELEVLSK 85
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
188-288 |
3.70e-15 |
|
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.
Pssm-ID: 238391 [Multi-domain] Cd Length: 211 Bit Score: 74.46 E-value: 3.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 188 RTMVFNSMRSFFNERGYIEVDTPVLQSIPGGAAAR----PFITHHNALDIPLYLRIANELYLKRLIVG----GFDGVYEF 259
Cdd:cd00768 2 RSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGhepkDLLPVGAENEEDLYLRPTLEPGLVRLFVShirkLPLRLAEI 81
|
90 100 110
....*....|....*....|....*....|.
gi 922688387 260 SRNFRNEGMDR--THNPEFTAMEIYVAYKDY 288
Cdd:cd00768 82 GPAFRNEGGRRglRRVREFTQLEGEVFGEDG 112
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
50-507 |
3.12e-14 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 75.41 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 50 ENAAKRQVSIAGRIMSRRIMGKATFMELQDAEGRIQIYITRDDICPGEDKEFYNTVvkKCTDIGDF----IGVKGYVFRT 125
Cdd:PTZ00401 74 PELVDKTVLIRARVSTTRKKGKMAFMVLRDGSDSVQAMAAVEGDVPKEMIDFIGQI--PTESIVDVeatvCKVEQPITST 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 126 QMGEISVHVQEMTFLSKAIRPLPVV------KEKDGEVFDGFtdpEQRYRQRYVDLVVNSHvKDIFLKRTMVFNSMRSFF 199
Cdd:PTZ00401 152 SHSDIELKVKKIHTVTESLRTLPFTledasrKESDEGAKVNF---DTRLNSRWMDLRTPAS-GAIFRLQSRVCQYFRQFL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 200 NERGYIEVDTPVLQSIPGGAAARPFITHHNALDIplYLRIANELYLKRLIVGGFDGVYEFSRNFRNEGMD-RTHNPEFTA 278
Cdd:PTZ00401 228 IDSDFCEIHSPKIINAPSEGGANVFKLEYFNRFA--YLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNtHRHLTEFVG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 279 MEIYVAYKD-YNWMMNFTEQM--------------LERIC----------------MDVLGTTQVKVGEKLID-FKAPYK 326
Cdd:PTZ00401 306 LDVEMRINEhYYEVLDLAESLfnyiferlathtkeLKAVCqqypfeplvwkltperMKELGVGVISEGVEPTDkYQARVH 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 327 RVT--MIEAIHEHTGIDISGMNEAELRQVCDKlgvehNETMGK--GKLIDEIFGEKceknyiqpTFITD-YPKEMSPL-T 400
Cdd:PTZ00401 386 NMDsrMLRINYMHCIELLNTVLEEKMAPTDDI-----NTTNEKllGKLVKERYGTD--------FFISDrFPSSARPFyT 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 401 KEHRTNPELTERFELMVNGKELANAYSELNDPIDQRERFEE-QLKLSEKGDdeamYIDndfirALEYGMPPTSGMGIGMD 479
Cdd:PTZ00401 453 MECKDDERFTNSYDMFIRGEEISSGAQRIHDPDLLLARAKMlNVDLTPIKE----YVD-----SFRLGAWPHGGFGVGLE 523
|
490 500
....*....|....*....|....*...
gi 922688387 480 RLVMLLTGQESIQEVLLFPQmKPEKVAP 507
Cdd:PTZ00401 524 RVVMLYLGLSNVRLASLFPR-DPQRTTP 550
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
57-140 |
8.40e-14 |
|
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic acids. The family includes the anti-codon binding domain of lysyl, aspartyl, and asparaginyl -tRNA synthetases (See pfam00152). Aminoacyl-tRNA synthetases catalyze the addition of an amino acid to the appropriate tRNA molecule EC:6.1.1.-. This family also includes part of RecG helicase involved in DNA repair. Replication factor A is a hetero-trimeric complex, that contains a subunit in this family. This domain is also found at the C-terminus of bacterial DNA polymerase III alpha chain.
Pssm-ID: 460164 [Multi-domain] Cd Length: 75 Bit Score: 66.49 E-value: 8.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 57 VSIAGRIMS-RRIMGKATFMELQDAEGRIQIYITrddicPGEDKEFYNTVvkkctDIGDFIGVKGYVFRTQMGEISVHVQ 135
Cdd:pfam01336 1 VTVAGRVTSiRRSGGKLLFLTLRDGTGSIQVVVF-----KEEAEKLAKKL-----KEGDVVRVTGKVKKRKGGELELVVE 70
|
....*
gi 922688387 136 EMTFL 140
Cdd:pfam01336 71 EIELL 75
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
40-500 |
2.36e-08 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 56.91 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 40 AEIKRNfnDDENAAK--RQVSIAGRIMSRRIMGKATFMELQDAE--GRIQIYITrddicpgEDKEFYNTVVKKCTDIGDF 115
Cdd:PLN02603 93 ADVKGG--EDEGLARvgKTLNVMGWVRTLRAQSSVTFIEVNDGSclSNMQCVMT-------PDAEGYDQVESGLITTGAS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 116 IGVKGYVFRTQMGE--ISVHVQEMTFLSKAIRPLPVVKEKdgeVFDGFTDPEQRYRQRYVDLVVNSHVKDIFLKRTmvfn 193
Cdd:PLN02603 164 VLVQGTVVSSQGGKqkVELKVSKIVVVGKSDPSYPIQKKR---VSREFLRTKAHLRPRTNTFGAVARVRNALAYAT---- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 194 smRSFFNERGYIEVDTPVLQ-SIPGGAAARPFIT------HHNA----LDIP-----------------LYLRIANELYL 245
Cdd:PLN02603 237 --HKFFQENGFVWVSSPIITaSDCEGAGEQFCVTtlipnsAENGgslvDDIPktkdglidwsqdffgkpAFLTVSGQLNG 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 246 KRLIVGGFDgVYEFSRNFRNEGMDRT-HNPEFTAMEIYVAYKDYNWMMNFTEQMLERICMDVLGT---------TQVKVG 315
Cdd:PLN02603 315 ETYATALSD-VYTFGPTFRAENSNTSrHLAEFWMIEPELAFADLNDDMACATAYLQYVVKYILENckedmeffnTWIEKG 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 316 --EKLIDF-KAPYKRVTMIEAIHehtgIDISGMNEAE--LRQVCDkLGVEHNETmgkgkLIDEIFGEKceknyiqPTFIT 390
Cdd:PLN02603 394 iiDRLSDVvEKNFVQLSYTDAIE----LLLKAKKKFEfpVKWGLD-LQSEHERY-----ITEEAFGGR-------PVIIR 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 391 DYPKEMSPLTKEHRTNPELTERFELMVngkelanaySELNDPIDQRERfEEQLKLSEKGDDEAMYIDNDFIRALE---YG 467
Cdd:PLN02603 457 DYPKEIKAFYMRENDDGKTVAAMDMLV---------PRVGELIGGSQR-EERLEYLEARLDELKLNKESYWWYLDlrrYG 526
|
490 500 510
....*....|....*....|....*....|...
gi 922688387 468 MPPTSGMGIGMDRLVMLLTGQESIQEVLLFPQM 500
Cdd:PLN02603 527 SVPHAGFGLGFERLVQFATGIDNIRDAIPFPRV 559
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
234-501 |
1.34e-06 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 51.41 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 234 PLYLRIANELYLKRLiVGGFDGVYEFSRNFRNEGMDRT-HNPEFTAMEIYVAYKDYNWMMNFTEQMLERICMDVLG--TT 310
Cdd:PLN02532 371 PTYLTVSGRLHLESY-ACALGNVYTFGPRFRADRIDSArHLAEMWMVEVEMAFSELEDAMNCAEDYFKFLCKWVLEncSE 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 311 QVKVGEKLIDfKApykRVTMIEAIHEHTGIDISGMnEA--ELRQVCDKlGVEHNETMG-------KGKLIDEIfgekcek 381
Cdd:PLN02532 450 DMKFVSKRID-KT---ISTRLEAIISSSLQRISYT-EAvdLLKQATDK-KFETKPEWGialttehLSYLADEI------- 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 382 nYIQPTFITDYPKEMSPLTKEHRTNPELTERFELMV--NGKELANAYSE-----LNDPID----QRERFEEQLKLSEKGD 450
Cdd:PLN02532 517 -YKKPVIIYNYPKELKPFYVRLNDDGKTVAAFDLVVpkVGTVITGSQNEermdiLNARIEelglPREQYEWYLDLRRHGT 595
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 922688387 451 DEamyidndfiraleygmppTSGMGIGMDRLVMLLTGQESIQEVLLFPQMK 501
Cdd:PLN02532 596 VK------------------HSGFSLGFELMVLFATGLPDVRDAIPFPRSW 628
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
38-148 |
4.41e-06 |
|
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: 45.77 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 38 YSAEIKRNFNDDEnaakrqVSIAGRIMSRRIMGKATFMELQDAEGRIQIYITRDDicpgEDKEFYNTVVKKCTDigDFIG 117
Cdd:cd04316 2 YSAEITPELDGEE------VTVAGWVHEIRDLGGIKFVILRDREGIVQVTAPKKK----VDKELFKTVRKLSRE--SVIS 69
|
90 100 110
....*....|....*....|....*....|...
gi 922688387 118 VKGYVFRTQM--GEISVHVQEMTFLSKAIRPLP 148
Cdd:cd04316 70 VTGTVKAEPKapNGVEIIPEEIEVLSEAKTPLP 102
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
236-499 |
2.03e-05 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 47.33 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 236 YLRIANELYLKRLIVGGFDgVYEFSRNFRNEGMDRT-HNPEFTAMEIYVAYKDYNWMMNFTEQMLeRICMD-VLGTT--- 310
Cdd:PTZ00425 327 FLTVSGQLSLENLCSSMGD-VYTFGPTFRAENSHTSrHLAEFWMIEPEIAFADLYDNMELAESYI-KYCIGyVLNNNfdd 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 311 ----QVKVGEKLID-----FKAPYKRVTMIEAIhehtgiDISgMNEAELRQVCDKLGV----EHNETMGkgklideifge 377
Cdd:PTZ00425 405 iyyfEENVETGLISrlkniLDEDFAKITYTNVI------DLL-QPYSDSFEVPVKWGMdlqsEHERFVA----------- 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922688387 378 kcEKNYIQPTFITDYPKEMSPLTKEHRTNPELTERFELMVN--GKELANAYSElndpiDQRERFEEQLKlSEKGDDEAMY 455
Cdd:PTZ00425 467 --EQIFKKPVIVYNYPKDLKAFYMKLNEDQKTVAAMDVLVPkiGEVIGGSQRE-----DNLERLDKMIK-EKKLNMESYW 538
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 922688387 456 idndFIRAL-EYGMPPTSGMGIGMDRLVMLLTGQESIQEVLLFPQ 499
Cdd:PTZ00425 539 ----WYRQLrKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFPR 579
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