|
Name |
Accession |
Description |
Interval |
E-value |
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
14-501 |
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: 893.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 14 QEDLSEVLQVRRDKLKKLQESGRDPFKEsRYDRTHYSMDIKDNFDSLE-----GKTTKIAGRIMSKRIQGKAGFIDIQDQ 88
Cdd:COG1190 4 EEDLNEQIRVRREKLEELREAGIDPYPN-KFPRTHTAAEIREKYDELEaeeetGDEVSVAGRIMAKRDMGKASFADLQDG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 89 EGRIQSYVRLDAIGEEEYSVFSTYDIGDIVGIEGEIFKTKKGEISVKAKSVVLLCKSLQVLPEKYHGLKDQELRYRQRYV 168
Cdd:COG1190 83 SGRIQLYLRRDELGEEAYELFKLLDLGDIVGVEGTVFRTKTGELSVKVEELTLLSKSLRPLPEKFHGLTDPETRYRQRYV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 169 DLIVNPEVKNAFLIRTKALKALRAYLDDRGFLEVETPILNTIAGGANARPFITNHNTLHIPMYLRIANELYLKRLIVGGF 248
Cdd:COG1190 163 DLIVNPEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 249 DKVYEMGRMFRNEGMDLKHNPEYTAIELYQAYADYTDMMEITENVIAHMAEVATGSMIVNYQGTEINFTPPWKRMSMEDC 328
Cdd:COG1190 243 ERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGTTKVTYQGQEIDLSPPWRRITMVEA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 329 VKEYSGVDFSTINTDEEALEVAREKGIEIKPGMRRGEVINAFFEEFGEDKLIQPTFITHHPVEVSPLSKRNVEDPRRTDR 408
Cdd:COG1190 323 IKEATGIDVTPLTDDEELRALAKELGIEVDPGWGRGKLIDELFEELVEPKLIQPTFVTDYPVEVSPLAKRHRDDPGLTER 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 409 FEAFANKWELANAFSELNDPIDQKGRFIDQLRKRELGDDEAFEMDEDFLKALEVGLPPTGGLGIGIDRVIMLLTNSPSIR 488
Cdd:COG1190 403 FELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIR 482
|
490
....*....|...
gi 489530229 489 DVLLFPTMKPIDN 501
Cdd:COG1190 483 DVILFPLMRPEKK 495
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
15-500 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 870.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 15 EDLSEVLQVRRDKLKKLQESGRDPFKEsRYDRTHYSMDIKDNFDSLEGK-------TTKIAGRIMSKRIQGKAGFIDIQD 87
Cdd:PRK00484 1 EELNEQIAVRREKLAELREQGIDPYPN-KFERTHTAAELRAKYDDKEKEeleeleiEVSVAGRVMLKRVMGKASFATLQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 88 QEGRIQSYVRLDAIGEEEYSVFSTYDIGDIVGIEGEIFKTKKGEISVKAKSVVLLCKSLQVLPEKYHGLKDQELRYRQRY 167
Cdd:PRK00484 80 GSGRIQLYVSKDDVGEEALEAFKKLDLGDIIGVEGTLFKTKTGELSVKATELTLLTKSLRPLPDKFHGLTDVETRYRQRY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 168 VDLIVNPEVKNAFLIRTKALKALRAYLDDRGFLEVETPILNTIAGGANARPFITNHNTLHIPMYLRIANELYLKRLIVGG 247
Cdd:PRK00484 160 VDLIVNPESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARPFITHHNALDIDLYLRIAPELYLKRLIVGG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 248 FDKVYEMGRMFRNEGMDLKHNPEYTAIELYQAYADYTDMMEITENVIAHMAEVATGSMIVNYQGTEINFTPPWKRMSMED 327
Cdd:PRK00484 240 FERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTYQGTEIDFGPPFKRLTMVD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 328 CVKEYSGVDFsTINTDEEALEVAREKGIEIKPGMRRGEVINAFFEEFGEDKLIQPTFITHHPVEVSPLSKRNVEDPRRTD 407
Cdd:PRK00484 320 AIKEYTGVDF-DDMTDEEARALAKELGIEVEKSWGLGKLINELFEEFVEPKLIQPTFITDYPVEISPLAKRHREDPGLTE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 408 RFEAFANKWELANAFSELNDPIDQKGRFIDQLRKRELGDDEAFEMDEDFLKALEVGLPPTGGLGIGIDRVIMLLTNSPSI 487
Cdd:PRK00484 399 RFELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSPSI 478
|
490
....*....|...
gi 489530229 488 RDVLLFPTMKPID 500
Cdd:PRK00484 479 RDVILFPLMRPEK 491
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
3-500 |
0e+00 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 661.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 3 NNQQSNEEAQIQEDLSEVLQVRRDKLKKLQESGRDPFkESRYDRTHYSMDIKDNFDSL------EGKTTKIAGRIMSKRI 76
Cdd:PLN02502 44 RSRKSAAADDETMDPTQYRANRLKKVEALRAKGVEPY-PYKFDVTHTAPELQEKYGSLengeelEDVSVSVAGRIMAKRA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 77 QGKAGFIDIQDQEGRIQSYVRLDAIGEEEYS---VFSTYDIGDIVGIEGEIFKTKKGEISVKAKSVVLLCKSLQVLPEKY 153
Cdd:PLN02502 123 FGKLAFYDLRDDGGKIQLYADKKRLDLDEEEfekLHSLVDRGDIVGVTGTPGKTKKGELSIFPTSFEVLTKCLLMLPDKY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 154 HGLKDQELRYRQRYVDLIVNPEVKNAFLIRTKALKALRAYLDDRGFLEVETPILNTIAGGANARPFITNHNTLHIPMYLR 233
Cdd:PLN02502 203 HGLTDQETRYRQRYLDLIANPEVRDIFRTRAKIISYIRRFLDDRGFLEVETPMLNMIAGGAAARPFVTHHNDLNMDLYLR 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 234 IANELYLKRLIVGGFDKVYEMGRMFRNEGMDLKHNPEYTAIELYQAYADYTDMMEITENVIAHMAEVATGSMIVNYQGTE 313
Cdd:PLN02502 283 IATELHLKRLVVGGFERVYEIGRQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKELTGSYKIKYHGIE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 314 INFTPPWKRMSMEDCVKEYSGVDFSTINTDEEA---LEVAREKG-IEIKPGMRRGEVINAFFEEFGEDKLIQPTFITHHP 389
Cdd:PLN02502 363 IDFTPPFRRISMISLVEEATGIDFPADLKSDEAnayLIAACEKFdVKCPPPQTTGRLLNELFEEFLEETLVQPTFVLDHP 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 390 VEVSPLSKRNVEDPRRTDRFEAFANKWELANAFSELNDPIDQKGRFIDQLRKRELGDDEAFEMDEDFLKALEVGLPPTGG 469
Cdd:PLN02502 443 VEMSPLAKPHRSKPGLTERFELFINGRELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGG 522
|
490 500 510
....*....|....*....|....*....|.
gi 489530229 470 LGIGIDRVIMLLTNSPSIRDVLLFPTMKPID 500
Cdd:PLN02502 523 WGLGIDRLVMLLTDSASIRDVIAFPAMKPQD 553
|
|
| lysS_bact |
TIGR00499 |
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ... |
16-498 |
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: 652.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 16 DLSEVLQVRRDKLKKLQESGRDPFKeSRYDRTHYSMDIKDNFDSLEGKTTK-------IAGRIMSKRIQGKAGFIDIQDQ 88
Cdd:TIGR00499 1 ELNDQAQQRLEKLNRLRQTGNNPYL-HKFERTHSAQEFQEKYADLSNEELKekelkvsIAGRIKAIRSMGKATFITLQDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 89 EGRIQSYVRLDAIGEEEYSVF-STYDIGDIVGIEGEIFKTKKGEISVKAKSVVLLCKSLQVLPEKYHGLKDQELRYRQRY 167
Cdd:TIGR00499 80 SGQIQLYVNKNKLPEDFYEFDeYLLDLGDIIGVTGYPFKTKTGELSVKVTELQILTKCLQPLPDKWHGLTDQETRYRQRY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 168 VDLIVNPEVKNAFLIRTKALKALRAYLDDRGFLEVETPILNTIAGGANARPFITNHNTLHIPMYLRIANELYLKRLIVGG 247
Cdd:TIGR00499 160 LDLIVNPDVRQTFLKRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKPFITHHNALDMDLYLRIAPELYLKRLIVGG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 248 FDKVYEMGRMFRNEGMDLKHNPEYTAIELYQAYADYTDMMEITENVIAHMAEVATGSMIVNYQGTEINFTPPWKRMSMED 327
Cdd:TIGR00499 240 LEKVYEIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTFIINYNDLEIDLKPPWKRITMVD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 328 CVKEYSGVDFSTINTDEEALEVAREKGIEI-KPGMRRGEVINAFFEEFGEDKLIQPTFITHHPVEVSPLSKRNVEDPRRT 406
Cdd:TIGR00499 320 ALEMVTGIDFDILKDDETAKALAKEHGIEVaEDSLTLGHILNKFFEQFLEHTLIQPTFITHYPAEISPLAKRDPSNPEFT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 407 DRFEAFANKWELANAFSELNDPIDQKGRFIDQLRKRELGDDEAFEMDEDFLKALEVGLPPTGGLGIGIDRVIMLLTNSPS 486
Cdd:TIGR00499 400 ERFELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGIGIDRLVMLLTDAPS 479
|
490
....*....|..
gi 489530229 487 IRDVLLFPTMKP 498
Cdd:TIGR00499 480 IRDVLLFPQLRP 491
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
173-498 |
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: 526.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 173 NPEVKNAFLIRTKALKALRAYLDDRGFLEVETPILNTIAGGANARPFITNHNTLHIPMYLRIANELYLKRLIVGGFDKVY 252
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 253 EMGRMFRNEGMDLKHNPEYTAIELYQAYADYTDMMEITENVIAHMAEVATGSMIVNYQGTEINFTPPWKRMSMEDCVKEY 332
Cdd:cd00775 81 EIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIEYGGKELDFTPPFKRVTMVDALKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 333 SGVDF---STINTDEEALEVAREKGIEIKPGMRRGEVINAFFEEFGEDKLIQPTFITHHPVEVSPLSKRNVEDPRRTDRF 409
Cdd:cd00775 161 TGIDFpelDLEQPEELAKLLAKLIKEKIEKPRTLGKLLDKLFEEFVEPTLIQPTFIIDHPVEISPLAKRHRSNPGLTERF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 410 EAFANKWELANAFSELNDPIDQKGRFIDQLRKRELGDDEAFEMDEDFLKALEVGLPPTGGLGIGIDRVIMLLTNSPSIRD 489
Cdd:cd00775 241 ELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLTDSNSIRD 320
|
....*....
gi 489530229 490 VLLFPTMKP 498
Cdd:cd00775 321 VILFPAMRP 329
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
17-498 |
3.81e-167 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 501.42 E-value: 3.81e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 17 LSEVLQVRRDKLKKLQESGRDPFKESrYDRTHysmDIKDNFDSLEGKTTKIAGRIMSKRIQGKAGFIDIQDQEGRIQSYV 96
Cdd:PRK02983 610 LPEQVRVRLAKLEALRAAGVDPYPVG-VPPTH---TVAEALDAPTGEEVSVSGRVLRIRDYGGVLFADLRDWSGELQVLL 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 97 RLDAIGEEEYSVF-STYDIGDIVGIEGEIFKTKKGEISVKAKSVVLLCKSLQVLPEKYHGLKDQELRYRQRYVDLIVNPE 175
Cdd:PRK02983 686 DASRLEQGSLADFrAAVDLGDLVEVTGTMGTSRNGTLSLLVTSWRLAGKCLRPLPDKWKGLTDPEARVRQRYLDLAVNPE 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 176 VKNAFLIRTKALKALRAYLDDRGFLEVETPILNTIAGGANARPFITNHNTLHIPMYLRIANELYLKRLIVGGFDKVYEMG 255
Cdd:PRK02983 766 ARDLLRARSAVVRAVRETLVARGFLEVETPILQQVHGGANARPFVTHINAYDMDLYLRIAPELYLKRLCVGGVERVFELG 845
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 256 RMFRNEGMDLKHNPEYTAIELYQAYADYTDMMEITENVIAHMAEVATGSMIVNYQGTEINFTP-----PWKRMSMEDCVK 330
Cdd:PRK02983 846 RNFRNEGVDATHNPEFTLLEAYQAHADYDTMRDLTRELIQNAAQAAHGAPVVMRPDGDGVLEPvdisgPWPVVTVHDAVS 925
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 331 EYSGVDFSTINTDEEALEVAREKGIEIKPGMRRGEVINAFFEEFGEDKLIQPTFITHHPVEVSPLSKRNVEDPRRTDRFE 410
Cdd:PRK02983 926 EALGEEIDPDTPLAELRKLCDAAGIPYRTDWDAGAVVLELYEHLVEDRTTFPTFYTDFPTSVSPLTRPHRSDPGLAERWD 1005
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 411 AFANKWELANAFSELNDPIDQKGRFIDQLRKRELGDDEAFEMDEDFLKALEVGLPPTGGLGIGIDRVIMLLTNSpSIRDV 490
Cdd:PRK02983 1006 LVAWGVELGTAYSELTDPVEQRRRLTEQSLLAAGGDPEAMELDEDFLQALEYAMPPTGGLGMGVDRLVMLLTGR-SIRET 1084
|
....*...
gi 489530229 491 LLFPTMKP 498
Cdd:PRK02983 1085 LPFPLVKP 1092
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
4-498 |
1.49e-159 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 462.99 E-value: 1.49e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 4 NQQSNEEAQIQEDLSEVLQVRRDKLKKLQESG----RDPFKESRYDRTHYSMDIKDNfDSLEGKTTKI--AGRIMSKRIQ 77
Cdd:PRK12445 2 SEQETRGANEAIDFNDELRNRREKLAALRQQGvafpNDFRRDHTSDQLHEEFDAKDN-QELESLNIEVsvAGRMMTRRIM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 78 GKAGFIDIQDQEGRIQSYVRLDAIGEEEYS-VFSTYDIGDIVGIEGEIFKTKKGEISVKAKSVVLLCKSLQVLPEKYHGL 156
Cdd:PRK12445 81 GKASFVTLQDVGGRIQLYVARDSLPEGVYNdQFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFHGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 157 KDQELRYRQRYVDLIVNPEVKNAFLIRTKALKALRAYLDDRGFLEVETPILNTIAGGANARPFITNHNTLHIPMYLRIAN 236
Cdd:PRK12445 161 QDQEVRYRQRYLDLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 237 ELYLKRLIVGGFDKVYEMGRMFRNEGMDLKHNPEYTAIELYQAYADYTDMMEITENVIAHMAEVATGSMIVNYQGTEINF 316
Cdd:PRK12445 241 ELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFDF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 317 TPPWKRMSMEDCVKEYS-GVDFSTINTDEEALEVAREKGIEIKPGMRRGEVINAFFEEFGEDKLIQPTFITHHPVEVSPL 395
Cdd:PRK12445 321 GKPFEKLTMREAIKKYRpETDMADLDNFDAAKALAESIGITVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 396 SKRNVEDPRRTDRFEAFANKWELANAFSELNDPIDQKGRFIDQLRKRELGDDEAFEMDEDFLKALEVGLPPTGGLGIGID 475
Cdd:PRK12445 401 ARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGID 480
|
490 500
....*....|....*....|...
gi 489530229 476 RVIMLLTNSPSIRDVLLFPTMKP 498
Cdd:PRK12445 481 RMIMLFTNSHTIRDVILFPAMRP 503
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
4-498 |
1.29e-132 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 396.69 E-value: 1.29e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 4 NQQSNEEAQIQ-----EDLSEVLQVRRDKlkklqesGRDPFKEsRYDRT----HYSMDIKD--NFDSLEGKTTKIAGRIM 72
Cdd:PTZ00417 71 DKKKEEEAEVDprlyyENRSKFIQEQKAK-------GINPYPH-KFERTitvpEFVEKYQDlaSGEHLEDTILNVTGRIM 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 73 SKRIQG-KAGFIDIQDQEGRIQSYVRLDAIGEEEYSVFSTYDI---GDIVGIEGEIFKTKKGEISVKAKSVVLLCKSLQV 148
Cdd:PTZ00417 143 RVSASGqKLRFFDLVGDGAKIQVLANFAFHDHTKSNFAECYDKirrGDIVGIVGFPGKSKKGELSIFPKETIILSPCLHM 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 149 LPEKYhGLKDQELRYRQRYVDLIVNPEVKNAFLIRTKALKALRAYLDDRGFLEVETPILNTIAGGANARPFITNHNTLHI 228
Cdd:PTZ00417 223 LPMKY-GLKDTEIRYRQRYLDLMINESTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLVAGGANARPFITHHNDLDL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 229 PMYLRIANELYLKRLIVGGFDKVYEMGRMFRNEGMDLKHNPEYTAIELYQAYADYTDMMEITENVIAHMAEVATGSMIVN 308
Cdd:PTZ00417 302 DLYLRIATELPLKMLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHLFGTYKIL 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 309 Y-------QGTEINFTPPWKRMSMEDCVKEYSGVD----FSTINTDEEALEVAREKGIEIKPGMRRGEVINAFFEEFGED 377
Cdd:PTZ00417 382 YnkdgpekDPIEIDFTPPYPKVSIVEELEKLTNTKleqpFDSPETINKMINLIKENKIEMPNPPTAAKLLDQLASHFIEN 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 378 KLI-QPTFITHHPVEVSPLSKRNVEDPRRTDRFEAFANKWELANAFSELNDPIDQKGRFIDQLRKRELGDDEAFEMDEDF 456
Cdd:PTZ00417 462 KYPnKPFFIIEHPQIMSPLAKYHRSKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAF 541
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 489530229 457 LKALEVGLPPTGGLGIGIDRVIMLLTNSPSIRDVLLFPTMKP 498
Cdd:PTZ00417 542 CTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFPTMRP 583
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
64-497 |
4.03e-121 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 369.75 E-value: 4.03e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 64 TTKIAGRIMSKRIQGKAGFIDIQDQEGRIQSYVRL--DAIGEEEYSVFSTYDIGDIVGIEGEIFKTKKGEISVKAKSVVL 141
Cdd:PTZ00385 109 TVRVAGRVTSVRDIGKIIFVTIRSNGNELQVVGQVgeHFTREDLKKLKVSLRVGDIIGADGVPCRMQRGELSVAASRMLI 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 142 L----CKSLQVLPE--KYHGLKDQELRYRQRYVDLIVNPEVKNAFLIRTKALKALRAYLDDRGFLEVETPILNTIAGGAN 215
Cdd:PTZ00385 189 LspyvCTDQVVCPNlrGFTVLQDNDVKYRYRFTDMMTNPCVIETIKKRHVMLQALRDYFNERNFVEVETPVLHTVASGAN 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 216 ARPFITNHNTLHIPMYLRIANELYLKRLIVGGFDKVYEMGRMFRNEGMDLKHNPEYTAIELYQAYADYTDMMEITENVIA 295
Cdd:PTZ00385 269 AKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTSCEFYAAYHTYEDLMPMTEDIFR 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 296 HMAEVATGSMIVNYQ-------GTEINFTPPWKRMSMEDCVKEYSGVDFSTINTDEEALEVAREKGIEIK-----PGMRR 363
Cdd:PTZ00385 349 QLAMRVNGTTVVQIYpenahgnPVTVDLGKPFRRVSVYDEIQRMSGVEFPPPNELNTPKGIAYMSVVMLRyniplPPVRT 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 364 -GEVINAFFEEFGEDKLIQPTFITHHPVEVSPLSKRNVEDPRRTDRFEAFANKWELANAFSELNDPIDQKGRFIDQLRKR 442
Cdd:PTZ00385 429 aAKMFEKLIDFFITDRVVEPTFVMDHPLFMSPLAKEQVSRPGLAERFELFVNGIEYCNAYSELNDPHEQYHRFQQQLVDR 508
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 489530229 443 ELGDDEAFEMDEDFLKALEVGLPPTGGLGIGIDRVIMLLTNSPSIRDVLLFPTMK 497
Cdd:PTZ00385 509 QGGDEEAMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFPLLR 563
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
158-497 |
1.29e-115 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 343.78 E-value: 1.29e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 158 DQELRYRQRYVDLiVNPEVKNAFLIRTKALKALRAYLDDRGFLEVETPILNTIAGGANARPFITNHNTLHIPMYLRIANE 237
Cdd:pfam00152 1 DEETRLKYRYLDL-RRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 238 LYLKRLIVGGFDKVYEMGRMFRNEGMDLKHNPEYTAIELYQAYADYTDMMEITENVIAHMAEVATGSMIVNYQGTEINFT 317
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 318 PPWKRMSMEDCVKEYSGVDFSTINTDEEalevarekgieiKPGMRRGevinafFEEFGEDKLIQPTFITHHPVEVSPLSK 397
Cdd:pfam00152 160 KPFPRITYAEAIEKLNGKDVEELGYGSD------------KPDLRFL------LELVIDKNKFNPLWVTDFPAEHHPFTM 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 398 RNVED-PRRTDRFEAFANKWELANAFSELNDPIDQKGRFIDQLRKRElgddEAFEMDEDFLKALEVGLPPTGGLGIGIDR 476
Cdd:pfam00152 222 PKDEDdPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDPE----EAEEKFGFYLDALKYGAPPHGGLGIGLDR 297
|
330 340
....*....|....*....|.
gi 489530229 477 VIMLLTNSPSIRDVLLFPTMK 497
Cdd:pfam00152 298 LVMLLTGLESIREVIAFPKTR 318
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
180-498 |
3.68e-92 |
|
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: 282.06 E-value: 3.68e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 180 FLIRTKALKALRAYLDDRGFLEVETPILNTIAGGANARPFITNHNTLHIPMYLRIANELYLKRLIVGGFDKVYEMGRMFR 259
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 260 NEGMDLKHNPEYTAIELYQAYADYTDMMEITENVIAHMAEVATGSMIVNYQGTEINFTPPWKRMSMedcvkeysgvdfst 339
Cdd:cd00669 81 NEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYGFELEDFGLPFPRLTY-------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 340 intdEEALEvarekgieikpgmrrgevinaffeefgedKLIQPTFITHHPVE-VSPLSKRNVEDPRRTDRFEAFANKWEL 418
Cdd:cd00669 147 ----REALE-----------------------------RYGQPLFLTDYPAEmHSPLASPHDVNPEIADAFDLFINGVEV 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 419 ANAFSELNDPIDQKGRFIDQLRkrelGDDEAFEMDEDFLKALEVGLPPTGGLGIGIDRVIMLLTNSPSIRDVLLFPTMKP 498
Cdd:cd00669 194 GNGSSRLHDPDIQAEVFQEQGI----NKEAGMEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKMRR 269
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
183-491 |
9.21e-70 |
|
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: 225.37 E-value: 9.21e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 183 RTKALKALRAYLDDRGFLEVETPILnTIAGG--ANARPFITN---HNTLHIPMYLRIANELYLKRLIVGGFDKVYEMGRM 257
Cdd:COG2269 9 RARLLAAIRAFFAERGVLEVETPAL-SVAPGtdPHLDSFATEfigPDGGGRPLYLHTSPEFAMKRLLAAGSGPIYQIAKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 258 FRNEGMDLKHNPEYTAIELYQAYADYTDMMEITENVIAHMAEVATgsmivnyqgteinfTPPWKRMSMEDCVKEYSGVDF 337
Cdd:COG2269 88 FRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAAG--------------FAPAERLSYQEAFLRYLGIDP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 338 STinTDEEAL-EVAREKGIEIKPGMRRGEVINAFFEEFGEDKLIQ--PTFITHHPVEVSPLSKRNVEDPRRTDRFEAFAN 414
Cdd:COG2269 154 LT--ADLDELaAAAAAAGLRVADDDDRDDLLDLLLSERVEPQLGRdrPTFLYDYPASQAALARISPDDPRVAERFELYAC 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489530229 415 KWELANAFSELNDPIDQKGRFIDQLRKRELGDDEAFEMDEDFLKALEVGLPPTGGLGIGIDRVIMLLTNSPSIRDVL 491
Cdd:COG2269 232 GVELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALGAERIDDVL 308
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
193-491 |
6.00e-65 |
|
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: 212.41 E-value: 6.00e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 193 YLDDRGFLEVETPILnTIAGG--ANARPFITNHNTLHI---PMYLRIANELYLKRLIVGGFDKVYEMGRMFRNEGMDLKH 267
Cdd:TIGR00462 1 FFAERGVLEVETPLL-SPAPVtdPHLDAFATEFVGPDGqgrPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 268 NPEYTAIELYQAYADYTDMMEITENVIAHMAEVATgsmivnyqgteinftPPWKRMSMEDCVKEYSGVDFSTInTDEEAL 347
Cdd:TIGR00462 80 NPEFTMLEWYRPGFDYHDLMDEVEALLQELLGDPF---------------APAERLSYQEAFLRYAGIDPLTA-SLAELQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 348 EVAREKGIEIKPGMRRGEVINAFFEE-----FGEDKliqPTFITHHPVEVSPLSKRNVEDPRRTDRFEAFANKWELANAF 422
Cdd:TIGR00462 144 AAAAAHGIRASEEDDRDDLLDLLFSEkvephLGFGR---PTFLYDYPASQAALARISPDDPRVAERFELYIKGLELANGF 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 423 SELNDPIDQKGRFI-DQLRKRELGdDEAFEMDEDFLKALEVGLPPTGGLGIGIDRVIMLLTNSPSIRDVL 491
Cdd:TIGR00462 221 HELTDAAEQRRRFEaDNALRKALG-LPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDVL 289
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
66-170 |
2.20e-55 |
|
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These enzymes are homodimeric class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Included in this group are E. coli LysS and LysU. These two isoforms of LysRS are encoded by distinct genes which are differently regulated. Eukaryotes contain 2 sets of aaRSs, both of which encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Saccharomyces cerevisiae cytoplasmic and mitochondrial LysRSs have been shown to participate in the mitochondrial import of the only nuclear-encoded tRNA of S. cerevisiae (tRNAlysCUU). The gene for human LysRS encodes both the cytoplasmic and the mitochondrial isoforms of LysRS. In addition to their housekeeping role, human lysRS may function as a signaling molecule that activates immune cells and tomato LysRS may participate in a root-specific process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging.
Pssm-ID: 239817 [Multi-domain] Cd Length: 108 Bit Score: 180.75 E-value: 2.20e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 66 KIAGRIMSKRIQGKAGFIDIQDQEGRIQSYVRLDAIGEEEYSVF-STYDIGDIVGIEGEIFKTKKGEISVKAKSVVLLCK 144
Cdd:cd04322 3 SVAGRIMSKRGSGKLSFADLQDESGKIQVYVNKDDLGEEEFEDFkKLLDLGDIIGVTGTPFKTKTGELSIFVKEFTLLSK 82
|
90 100
....*....|....*....|....*.
gi 489530229 145 SLQVLPEKYHGLKDQELRYRQRYVDL 170
Cdd:cd04322 83 SLRPLPEKFHGLTDVETRYRQRYLDL 108
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
180-490 |
1.52e-53 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 182.82 E-value: 1.52e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 180 FLIRTKALKALRAYLDDRGFLEVETPIL----NTiagGANARPFITNHNTLH----IPMYLRIANELYLKRLIVGGFDKV 251
Cdd:PRK09350 5 LLKRAKIIAEIRRFFADRGVLEVETPILsqatVT---DIHLVPFETRFVGPGasqgKTLWLMTSPEYHMKRLLAAGSGPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 252 YEMGRMFRNEGMDLKHNPEYTAIELYQAYADYTDMMEITENVIahmaevatgsmivnyqgTEINFTPPWKRMSMEDCVKE 331
Cdd:PRK09350 82 FQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLL-----------------QQVLDCEPAESLSYQQAFLR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 332 YSGVDfsTINTDEEAL-EVAREKGI--EIKPGMRRGEVINAFFEEFGEDKLIQ--PTFITHHPVEVSPLSKRNVEDPRRT 406
Cdd:PRK09350 145 YLGID--PLSADKTQLrEVAAKLGLsnIADEEEDRDTLLQLLFTFGVEPNIGKekPTFVYHFPASQAALAKISTEDHRVA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 407 DRFEAFANKWELANAFSELNDPIDQKGRFIDQLRKRELGDDEAFEMDEDFLKALEVGLPPTGGLGIGIDRVIMLLTNSPS 486
Cdd:PRK09350 223 ERFEVYFKGIELANGFHELTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCSGVALGVDRLIMLALGAES 302
|
....
gi 489530229 487 IRDV 490
Cdd:PRK09350 303 ISEV 306
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
46-494 |
2.29e-48 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 172.68 E-value: 2.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 46 RTHYSMDIKDNfdsLEGKTTKIAGRIMSKRIQGKAGFIDIQDQEGRIQSYVRLDAIgEEEYSVFSTYDIGDIVGIEGEIF 125
Cdd:PRK05159 3 KRHLTSELTPE---LDGEEVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKVD-EELFETIKKLKRESVVSVTGTVK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 126 KTKK--GEISVKAKSVVLLCKSLQVLPEKYHGLKDQEL--RYRQRYVDLiVNPEVKNAFLIRTKALKALRAYLDDRGFLE 201
Cdd:PRK05159 79 ANPKapGGVEVIPEEIEVLNKAEEPLPLDISGKVLAELdtRLDNRFLDL-RRPRVRAIFKIRSEVLRAFREFLYENGFTE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 202 VETP-ILNTIA-GGANARPFITNHNtlhiPMYLRIANELYlKRLIVG-GFDKVYEMGRMFRNEgmdlKHNP-----EYTA 273
Cdd:PRK05159 158 IFTPkIVASGTeGGAELFPIDYFEK----EAYLAQSPQLY-KQMMVGaGFERVFEIGPVFRAE----EHNTsrhlnEYTS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 274 IELYQAYAD-YTDMMEITENVIAHMAEVATgsmivnyqgteinftppwkrmsmEDCVKEYS--GVDFSTINTD------E 344
Cdd:PRK05159 229 IDVEMGFIDdHEDVMDLLENLLRYMYEDVA-----------------------ENCEKELEllGIELPVPETPiprityD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 345 EALEVAREKGIEIKPG---MRRGEVinAFFEEFGEDKLIQPTFITHHPVEVSPL-SKRNVEDPRRTDRFEAFANKWELAN 420
Cdd:PRK05159 286 EAIEILKSKGNEISWGddlDTEGER--LLGEYVKEEYGSDFYFITDYPSEKRPFyTMPDEDDPEISKSFDLLFRGLEITS 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489530229 421 AFSELNDPidqkGRFIDQLRKRELgDDEAFemdEDFLKALEVGLPPTGGLGIGIDRVIMLLTNSPSIRDVLLFP 494
Cdd:PRK05159 364 GGQRIHRY----DMLVESIKEKGL-NPESF---EFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFP 429
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
46-494 |
4.59e-39 |
|
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: 147.12 E-value: 4.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 46 RTHYsmdIKDNFDSLEGKTTKIAGRIMSKRIQGKAGFIDIQDQEGRIQsyVRLDAIGEEEYSVFSTYDIGDIVGIEGEIF 125
Cdd:COG0017 1 KRTY---IKDLLPEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGFIQ--VVVKKDKLENFEEAKKLTTESSVEVTGTVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 126 KT--KKGEISVKAKSVVLLCKSLQVLP--EKYHGLkdqELRYRQRYVDLiVNPEVKNAFLIRTKALKALRAYLDDRGFLE 201
Cdd:COG0017 76 ESprAPQGVELQAEEIEVLGEADEPYPlqPKRHSL---EFLLDNRHLRL-RTNRFGAIFRIRSELARAIREFFQERGFVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 202 VETPILNTIA--GGAnarpfitnhNTLHI-----PMYLRIANELYlKRLIVGGFDKVYEMGRMFRNEgmdlKHNP----- 269
Cdd:COG0017 152 VHTPIITASAteGGG---------ELFPVdyfgkEAYLTQSGQLY-KEALAMALEKVYTFGPTFRAE----KSNTrrhla 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 270 EYTAIELYQAYADYTDMMEITENVIAHMAEVatgsmIVNYQGTEINF------------TPPWKRMSMedcvkeysgvdf 337
Cdd:COG0017 218 EFWMIEPEMAFADLEDVMDLAEEMLKYIIKY-----VLENCPEELEFlgrdverlekvpESPFPRITY------------ 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 338 stintdEEALEVAREKGIEIKPGM---RRGEVINAffEEFGEDkliqPTFITHHPVEVSPL-SKRNVEDPRRTDRFEAfa 413
Cdd:COG0017 281 ------TEAIEILKKSGEKVEWGDdlgTEHERYLG--EEFFKK----PVFVTDYPKEIKAFyMKPNPDDPKTVAAFDL-- 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 414 nkweLANAFSEL-------NDPidqkgrfiDQLRKR--ELG-DDEAFemdEDFLKALEVGLPPTGGLGIGIDRVIMLLTN 483
Cdd:COG0017 347 ----LAPGIGEIiggsqreHRY--------DVLVERikEKGlDPEDY---EWYLDLRRYGSVPHAGFGLGLERLVMWLTG 411
|
490
....*....|.
gi 489530229 484 SPSIRDVLLFP 494
Cdd:COG0017 412 LENIREVIPFP 422
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
158-494 |
1.39e-32 |
|
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: 126.91 E-value: 1.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 158 DQELRYRQRYVDLiVNPEVKNAFLIRTKALKALRAYLDDRGFLEVETPILNTIA--GGANARP---FITnhntlhiPMYL 232
Cdd:cd00776 3 NLETLLDNRHLDL-RTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDteGGAELFKvsyFGK-------PAYL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 233 RIANELYLKRLIvGGFDKVYEMGRMFRNEgmdlKHNP-----EYTAIELYQAYA-DYTDMMEITENVIAHMAE------V 300
Cdd:cd00776 75 AQSPQLYKEMLI-AALERVYEIGPVFRAE----KSNTrrhlsEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKrvlercA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 301 ATGSMIVNYQGTEINFTPPWKRMSmedcvkeYSgvdfstintdeEALEVAREKGIEIKPGMrrGEVINAFFEEF-GEDKL 379
Cdd:cd00776 150 KELELVNQLNRELLKPLEPFPRIT-------YD-----------EAIELLREKGVEEEVKW--GEDLSTEHERLlGEIVK 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 380 IQPTFITHHPVEVSPL-SKRNVEDPRRTDRFEAFANKW-ELANAFSELNDPidqkgrfiDQLRKR--ELGDD-EAFEmde 454
Cdd:cd00776 210 GDPVFVTDYPKEIKPFyMKPDDDNPETVESFDLLMPGVgEIVGGSQRIHDY--------DELEERikEHGLDpESFE--- 278
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 489530229 455 DFLKALEVGLPPTGGLGIGIDRVIMLLTNSPSIRDVLLFP 494
Cdd:cd00776 279 WYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
180-494 |
1.90e-31 |
|
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: 122.68 E-value: 1.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 180 FLIRTKALKALRAYLDDRGFLEVETPILN--TIAGganARPFITNhNTLHIPMY--LRIANELYLKRLIVGGFDKVYEMG 255
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTksTPEG---ARDFLVP-SRLHPGKFyaLPQSPQLFKQLLMVSGFDRYFQIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 256 RMFRNEGMDLKHNPEYTAIELYQAYADYTDMMEITENVIAHMAEVATGsmivnyqgteINFTPPWKRMSMEDCVKEYsGV 335
Cdd:cd00777 77 RCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG----------VELTTPFPRMTYAEAMERY-GF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 336 DFSTIntdeealevarekgieikpgmrrgeVINAFFEEFGEDKLIQPTfitHHPV-----EVSPLSKRNVEDPRrTDRFE 410
Cdd:cd00777 146 KFLWI-------------------------VDFPLFEWDEEEGRLVSA---HHPFtapkeEDLDLLEKDPEDAR-AQAYD 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 411 AFANKWELANAFSELNDPIDQKGRFIDQLrkreLGDDEAFEMDEDFLKALEVGLPPTGGLGIGIDRVIMLLTNSPSIRDV 490
Cdd:cd00777 197 LVLNGVELGGGSIRIHDPDIQEKVFEILG----LSEEEAEEKFGFLLEAFKYGAPPHGGIALGLDRLVMLLTGSESIRDV 272
|
....
gi 489530229 491 LLFP 494
Cdd:cd00777 273 IAFP 276
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
46-494 |
2.80e-29 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 121.33 E-value: 2.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 46 RTHYSMDIKDnfdSLEGKTTKIAGRIMSKRIQGKAGFIDIQDQEGRIQSYVRLDAigeEEYSVFSTYDIGDIVGIEGEIF 125
Cdd:PRK00476 4 RTHYCGELRE---SHVGQTVTLCGWVHRRRDHGGLIFIDLRDREGIVQVVFDPDA---EAFEVAESLRSEYVIQVTGTVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 126 ---------KTKKGEISVKAKSVVLLCKSlQVLP----EKYHGLKDQELRYRqrYVDLiVNPEVKNAFLIRTKALKALRA 192
Cdd:PRK00476 78 arpegtvnpNLPTGEIEVLASELEVLNKS-KTLPfpidDEEDVSEELRLKYR--YLDL-RRPEMQKNLKLRSKVTSAIRN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 193 YLDDRGFLEVETPILN--TIAGganARPFItnhntlhIPMylRI-ANELY--------LKRLI-VGGFDKVYEMGRMFRN 260
Cdd:PRK00476 154 FLDDNGFLEIETPILTksTPEG---ARDYL-------VPS--RVhPGKFYalpqspqlFKQLLmVAGFDRYYQIARCFRD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 261 EgmDLKHN--PEYTAIELYQAYADYTDMMEITENVIAHMAEVATGsmivnyqgteINFTPPWKRMSMEDCVKEYsG---- 334
Cdd:PRK00476 222 E--DLRADrqPEFTQIDIEMSFVTQEDVMALMEGLIRHVFKEVLG----------VDLPTPFPRMTYAEAMRRY-Gsdkp 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 335 --------VDFSTINTDEE-------ALEVAREKGIEIKPG---MRRGEV--INAFFEEFGEDKLIqptFITHHPVEV-S 393
Cdd:PRK00476 289 dlrfglelVDVTDLFKDSGfkvfagaANDGGRVKAIRVPGGaaqLSRKQIdeLTEFAKIYGAKGLA---YIKVNEDGLkG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 394 PLSKrNVEDPRR---TDRFEA-------F-ANKWELANAF---------SELNdPIDQK-------------------GR 434
Cdd:PRK00476 366 PIAK-FLSEEELaalLERTGAkdgdlifFgADKAKVVNDAlgalrlklgKELG-LIDEDkfaflwvvdfpmfeydeeeGR 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 435 F--------------IDQLRKR-----------------ELG-------DDE----AFEM----DED-------FLKALE 461
Cdd:PRK00476 444 WvaahhpftmpkdedLDELETTdpgkarayaydlvlngyELGggsirihRPEiqekVFEIlgisEEEaeekfgfLLDALK 523
|
570 580 590
....*....|....*....|....*....|...
gi 489530229 462 VGLPPTGGLGIGIDRVIMLLTNSPSIRDVLLFP 494
Cdd:PRK00476 524 YGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
46-494 |
4.17e-26 |
|
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: 112.01 E-value: 4.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 46 RTHYSMDIKDnfdSLEGKTTKIAGRIMSKRIQGKAGFIDIQDQEGRIQsyVRLD-AIGEEEYSVFSTYDIGDIVGIEGEI 124
Cdd:COG0173 3 RTHYCGELRE---SDVGQEVTLSGWVHRRRDHGGLIFIDLRDRYGITQ--VVFDpDDSAEAFEKAEKLRSEYVIAVTGKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 125 F---------KTKKGEISVKAKSVVLLCKSlQVLP------EKYhglkDQELRYRQRYVDLiVNPEVKNAFLIRTKALKA 189
Cdd:COG0173 78 RarpegtvnpKLPTGEIEVLASELEILNKA-KTPPfqidddTDV----SEELRLKYRYLDL-RRPEMQKNLILRHKVTKA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 190 LRAYLDDRGFLEVETPILN--TIAGganARPFItnhntlhIPMylRI-ANELY--------LKRLI-VGGFDKVYEMGRM 257
Cdd:COG0173 152 IRNYLDENGFLEIETPILTksTPEG---ARDYL-------VPS--RVhPGKFYalpqspqlFKQLLmVSGFDRYFQIARC 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 258 FRNEgmDLKHN--PEYTAIELYQAYADYTDMMEITENVIAHMAEVATGsmivnyqgteINFTPPWKRMSMEDCVKEYsG- 334
Cdd:COG0173 220 FRDE--DLRADrqPEFTQLDIEMSFVDQEDVFELMEGLIRHLFKEVLG----------VELPTPFPRMTYAEAMERY-Gs 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 335 -----------VDFSTI--NTD----EEALEVA-REKGIEIKPG--MRRGEV--INAFFEEFG----------EDKLIqp 382
Cdd:COG0173 287 dkpdlrfglelVDVTDIfkDSGfkvfAGAAENGgRVKAINVPGGasLSRKQIdeLTEFAKQYGakglayikvnEDGLK-- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 383 tfithhpvevSPLSKrNVEDPRR---TDRFEA-------F-ANKWELANAF---------SELNdPIDQK---------- 432
Cdd:COG0173 365 ----------SPIAK-FLSEEELaaiLERLGAkpgdlifFvADKPKVVNKAlgalrlklgKELG-LIDEDefaflwvvdf 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 433 ---------GRF--------------IDQLRKR----------------ELG-------DDE----AFEM----DED--- 455
Cdd:COG0173 433 plfeydeeeGRWvamhhpftmpkdedLDLLETDpgkvrakaydlvlngyELGggsirihDPElqekVFELlgisEEEaee 512
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 489530229 456 ----FLKALEVGLPPTGGLGIGIDRVIMLLTNSPSIRDVLLFP 494
Cdd:COG0173 513 kfgfLLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
62-494 |
1.57e-23 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 104.30 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 62 GKTTKIAGRIMSKRIQGKAGFIDIQDQEGRIQSYVRLDAIGEEEYSVFSTYDIGDIVGIEGEIFK---------TKKGEI 132
Cdd:PRK12820 18 GREVCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFSPEAAPADVYELAASLRAEFCVALQGEVQKrleetenphIETGDI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 133 SVKAKSVVLLCKSlQVLP----EKY------HGLKD---QELRYRQRYVDlIVNPEVKNAFLIRTKALKALRAYLDDRGF 199
Cdd:PRK12820 98 EVFVRELSILAAS-EALPfaisDKAmtagagSAGADavnEDLRLQYRYLD-IRRPAMQDHLAKRHRIIKCARDFLDSRGF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 200 LEVETPILnTIAGGANARPFITNHNTLHIPMY-LRIANELYLKRLIVGGFDKVYEMGRMFRNEGMDLKHNPEYTAIELYQ 278
Cdd:PRK12820 176 LEIETPIL-TKSTPEGARDYLVPSRIHPKEFYaLPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEFTQLDIEA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 279 AYADYTDMMEITENVIAHMAEVATgsmivnyqgteINFTPPWKRMSMEDCVKEYsGVDFSTINTDEEALEV--------- 349
Cdd:PRK12820 255 SFIDEEFIFELIEELTARMFAIGG-----------IALPRPFPRMPYAEAMDTT-GSDRPDLRFDLKFADAtdifentry 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 350 ----------AREKGI--------------------EIKP-----GM---------------------RRGEVINAFFEE 373
Cdd:PRK12820 323 gifkqilqrgGRIKGInikgqseklsknvlqneyakEIAPsfgakGMtwmraeaggldsnivqffsadEKEALKRRFHAE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 374 FGE-------------------------DKL-------IQPTFIT----------------HHPV------EVSPLSKRN 399
Cdd:PRK12820 403 DGDviimiadascaivlsalgqlrlhlaDRLglipegvFHPLWITdfplfeatddggvtssHHPFtapdreDFDPGDIEE 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 400 VEDpRRTDRFEAFANKWELANAFSELNDPIDQKGRFID-QLRKRELGDDEAFemdedFLKALEVGLPPTGGLGIGIDRVI 478
Cdd:PRK12820 483 LLD-LRSRAYDLVVNGEELGGGSIRINDKDIQLRIFAAlGLSEEDIEDKFGF-----FLRAFDFAAPPHGGIALGLDRVV 556
|
570
....*....|....*.
gi 489530229 479 MLLTNSPSIRDVLLFP 494
Cdd:PRK12820 557 SMILQTPSIREVIAFP 572
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
46-494 |
2.68e-23 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 103.71 E-value: 2.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 46 RTHYSMDIKDNfDslEGKTTKIAGRIMSKRIQGKAGFIDIQDQEGRIQsYVRLDAIGEEEYSVFSTYDIGDIVGIEGEIF 125
Cdd:PLN02903 59 RSHLCGALSVN-D--VGSRVTLCGWVDLHRDMGGLTFLDVRDHTGIVQ-VVTLPDEFPEAHRTANRLRNEYVVAVEGTVR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 126 ---------KTKKGEISVKAKSVVLLCKSLQVLPEKYHGLKDQ------ELRYRQRYVDLiVNPEVKNAFLIRTKALKAL 190
Cdd:PLN02903 135 srpqespnkKMKTGSVEVVAESVDILNVVTKSLPFLVTTADEQkdsikeEVRLRYRVLDL-RRPQMNANLRLRHRVVKLI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 191 RAYLDDR-GFLEVETPILN--TIAGganARPFITNHNTLHIPMY-LRIANELYLKRLIVGGFDKVYEMGRMFRNEGMDLK 266
Cdd:PLN02903 214 RRYLEDVhGFVEIETPILSrsTPEG---ARDYLVPSRVQPGTFYaLPQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRAD 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 267 HNPEYTAIELYQAYADYTDMMEITENVIAHmaevatgsmiVNYQGTEINFTPPWKRMSMEDCVKEYsGVDFSTINTDEEA 346
Cdd:PLN02903 291 RQPEFTQLDMELAFTPLEDMLKLNEDLIRQ----------VFKEIKGVQLPNPFPRLTYAEAMSKY-GSDKPDLRYGLEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 347 LEV--------------AREKGIEIK----PG---------MRRGEVINAF---------FEEFGEDKLIQPTfithhPV 390
Cdd:PLN02903 360 VDVsdvfaessfkvfagALESGGVVKaicvPDgkkisnntaLKKGDIYNEAiksgakglaFLKVLDDGELEGI-----KA 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 391 EVSPLSKRNVED------------------PRRT-----DRFEAFANK-------------WELANAFSELND------- 427
Cdd:PLN02903 435 LVESLSPEQAEQllaacgagpgdlilfaagPTSSvnktlDRLRQFIAKtldlidpsrhsilWVTDFPMFEWNEdeqrlea 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 428 ---------PIDQKG----RFID-------------QLR--KRE----------LGDDEAFEMDEDFLKALEVGLPPTGG 469
Cdd:PLN02903 515 lhhpftapnPEDMGDlssaRALAydmvyngveigggSLRiyRRDvqqkvleaigLSPEEAESKFGYLLEALDMGAPPHGG 594
|
570 580
....*....|....*....|....*
gi 489530229 470 LGIGIDRVIMLLTNSPSIRDVLLFP 494
Cdd:PLN02903 595 IAYGLDRLVMLLAGAKSIRDVIAFP 619
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
2-494 |
1.26e-19 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 91.98 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 2 KNNQQSNEEAQIQEDLSEVLQVRRDKLKKLQES----GRDPFKESRYDRTHYSMDIKD-NFDSLEGKTTKIAGRIMSKRI 76
Cdd:PTZ00401 13 VEKKQSDKEARKAARLAEEKARAAEKAALVEKYkdvfGAAPMVQSTTYKSRTFIPVAVlSKPELVDKTVLIRARVSTTRK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 77 QGKAGFIDIQDQEGRIQSYVRLDAIGEEEYSVF-------STYDI-GDIVGIEGEIFKTKKGEISVKAKSVVLLCKSLQV 148
Cdd:PTZ00401 93 KGKMAFMVLRDGSDSVQAMAAVEGDVPKEMIDFigqipteSIVDVeATVCKVEQPITSTSHSDIELKVKKIHTVTESLRT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 149 LP---------EKYHGLK-DQELRYRQRYVDLiVNPEVKNAFLIRTKALKALRAYLDDRGFLEVETP-ILNTIA-GGANa 216
Cdd:PTZ00401 173 LPftledasrkESDEGAKvNFDTRLNSRWMDL-RTPASGAIFRLQSRVCQYFRQFLIDSDFCEIHSPkIINAPSeGGAN- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 217 rpfITNHNTLHIPMYLRIANELYLKRLIVGGFDKVYEMGRMFRNEGMDL-KHNPEYTAIELYQAYAD-YTDMMEITENVI 294
Cdd:PTZ00401 251 ---VFKLEYFNRFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNThRHLTEFVGLDVEMRINEhYYEVLDLAESLF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 295 AHMAE-VATGSMIVNYQGTEINFTPPWKRMSMEDcVKEYsGVDFSTINTDEEALEVAREKGIEIKpgMRRG------EVI 367
Cdd:PTZ00401 328 NYIFErLATHTKELKAVCQQYPFEPLVWKLTPER-MKEL-GVGVISEGVEPTDKYQARVHNMDSR--MLRInymhciELL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 368 NAFFEE-----------------------FGEDKLIQPTFithhPVEVSPLSKRNV-EDPRRTDRFEAFANKWELANAFS 423
Cdd:PTZ00401 404 NTVLEEkmaptddinttnekllgklvkerYGTDFFISDRF----PSSARPFYTMECkDDERFTNSYDMFIRGEEISSGAQ 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489530229 424 ELNDPidqkgrfiDQLRKRElgddEAFEMD----EDFLKALEVGLPPTGGLGIGIDRVIMLLTNSPSIRDVLLFP 494
Cdd:PTZ00401 480 RIHDP--------DLLLARA----KMLNVDltpiKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFP 542
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
171-494 |
2.16e-18 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 86.23 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 171 IVNPEVKNAFLIRTKALKALRAYLDDRGFLEVETPILNTIAGGANARPFITNHNTLHIPMYlriANELYL-------KRL 243
Cdd:PRK06462 21 ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIISPSTDPLMGLGSDLPVKQISIDFY---GVEYYLadsmilhKQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 244 IVGGFDKVYEMGRMFRNEGMD---LKHNPEYTAIELYQAYADYTDMMEITENVIAHMAE--VATGSMIVNYQGTEIN-FT 317
Cdd:PRK06462 98 ALRMLGKIFYLSPNFRLEPVDkdtGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKelLEEHEDELEFFGRDLPhLK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 318 PPWKRMSMedcvkeysgvdfstintdEEALEVAREKGIEIKPgmrrGEVINAFFEEFGEDKLIQPTFITHHPVEVSPLSK 397
Cdd:PRK06462 178 RPFKRITH------------------KEAVEILNEEGCRGID----LEELGSEGEKSLSEHFEEPFWIIDIPKGSREFYD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 398 RnvEDPRRTDRFEAF---------------ANKWELAnafselndpidqkgRFIDQLRKRELgDDEAFemdEDFLKALEV 462
Cdd:PRK06462 236 R--EDPERPGVLRNYdlllpegygeavsggEREYEYE--------------EIVERIREHGV-DPEKY---KWYLEMAKE 295
|
330 340 350
....*....|....*....|....*....|..
gi 489530229 463 GLPPTGGLGIGIDRVIMLLTNSPSIRDVLLFP 494
Cdd:PRK06462 296 GPLPSAGFGIGVERLTRYICGLRHIREVQPFP 327
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
52-494 |
8.73e-17 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 82.83 E-value: 8.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 52 DIKDNFDSLEGKTTKIAGRIMSKRIQGKAGFIDIQDQEGRIQS--YVRLDAIGEEEYSVFSTYDIGDIVGIEGEIFKTKK 129
Cdd:PLN02850 71 DVSDLGEELAGSEVLIRGRVHTIRGKGKSAFLVLRQSGFTVQCvvFVSEVTVSKGMVKYAKQLSRESVVDVEGVVSVPKK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 130 G------EISVKAKSVVLLCKSLQVLP-----------EKYHGLKD--------QELRYRQRYVDLIVnPEVKNAFLIRT 184
Cdd:PLN02850 151 PvkgttqQVEIQVRKIYCVSKALATLPfnvedaarsesEIEKALQTgeqlvrvgQDTRLNNRVLDLRT-PANQAIFRIQS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 185 KALKALRAYLDDRGFLEVETPILntIAGGAN--ARPFITNHNTlhIPMYLRIANELYLKRLIVGGFDKVYEMGRMFRNEG 262
Cdd:PLN02850 230 QVCNLFREFLLSKGFVEIHTPKL--IAGASEggSAVFRLDYKG--QPACLAQSPQLHKQMAICGDFRRVFEIGPVFRAED 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 263 MDL-KHNPEYTAIELYQAYAD-YTDMMEITENVIAHMAevatgsmivnyqgTEINftppwkrmsmEDCVKEYSGV----D 336
Cdd:PLN02850 306 SFThRHLCEFTGLDLEMEIKEhYSEVLDVVDELFVAIF-------------DGLN----------ERCKKELEAIreqyP 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 337 FSTIN--------TDEEALEVAREKGIEIKP------GMRR--GEVINaffEEFGEDkliqpTFITH-HPVEVSPL-SKR 398
Cdd:PLN02850 363 FEPLKylpktlrlTFAEGIQMLKEAGVEVDPlgdlntESERklGQLVK---EKYGTD-----FYILHrYPLAVRPFyTMP 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 399 NVEDPRRTDRFEAFANKWELANAFSELNDPidqkgRFIDQlRKRELGDDeaFEMDEDFLKALEVGLPPTGGLGIGIDRVI 478
Cdd:PLN02850 435 CPDDPKYSNSFDVFIRGEEIISGAQRVHDP-----ELLEK-RAEECGID--VKTISTYIDSFRYGAPPHGGFGVGLERVV 506
|
490
....*....|....*.
gi 489530229 479 MLLTNSPSIRDVLLFP 494
Cdd:PLN02850 507 MLFCGLNNIRKTSLFP 522
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
66-144 |
1.26e-15 |
|
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: 71.83 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 66 KIAGRIMSKRIQGKAGFIDIQDQEGRIQSYVRLDAIGeEEYSVFSTYDIGDIVGIEGEIFKT-----KKGEISVKAKSVV 140
Cdd:cd04100 3 TLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEELG-EFFEEAEKLRTESVVGVTGTVVKRpegnlATGEIELQAEELE 81
|
....
gi 489530229 141 LLCK 144
Cdd:cd04100 82 VLSK 85
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
66-142 |
1.02e-13 |
|
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: 66.10 E-value: 1.02e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489530229 66 KIAGRIMSK-RIQGKAGFIDIQDQEGRIQSYVRldaiGEEEYSVFSTYDIGDIVGIEGEIFKTKKGEISVKAKSVVLL 142
Cdd:pfam01336 2 TVAGRVTSIrRSGGKLLFLTLRDGTGSIQVVVF----KEEAEKLAKKLKEGDVVRVTGKVKKRKGGELELVVEEIELL 75
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
182-299 |
1.13e-12 |
|
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: 67.14 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 182 IRTKALKALRAYLDDRGFLEVETPILNTIAGGANAR----PFITNHNTLHIPMYLRIANELYLKRLIVG----GFDKVYE 253
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGhepkDLLPVGAENEEDLYLRPTLEPGLVRLFVShirkLPLRLAE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 489530229 254 MGRMFRNEG--MDLKHNPEYTAIELYQAYADYTD------MMEITENVIAHMAE 299
Cdd:cd00768 81 IGPAFRNEGgrRGLRRVREFTQLEGEVFGEDGEEasefeeLIELTEELLRALGI 134
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
51-496 |
1.00e-10 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 63.59 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 51 MDIKDNF-DSLEGKTTKIAGRIMSKRIQGKAGFIDIQDQEGRIQSYVRLDAiGEEEYSVFSTYDIGDIVGIEGEIFKT-- 127
Cdd:PRK03932 4 VSIKDILkGKYVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDN-GEEYFEEIKKLTTGSSVIVTGTVVESpr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 128 KKGEISVKAKSVVLLCKSLQVLP--EKYHG---LKDQ-ELRYRQRYVDLIvnpevknaFLIRTKALKALRAYLDDRGFLE 201
Cdd:PRK03932 83 AGQGYELQATKIEVIGEDPEDYPiqKKRHSiefLREIaHLRPRTNKFGAV--------MRIRNTLAQAIHEFFNENGFVW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 202 VETPILNTIAG-GAnARPFITNHNTLHI-------PMYLRIANELYLKRLIVgGFDKVYEMGRMFRNEgmdlK-----HN 268
Cdd:PRK03932 155 VDTPIITASDCeGA-GELFRVTTLDLDFskdffgkEAYLTVSGQLYAEAYAM-ALGKVYTFGPTFRAE----NsntrrHL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 269 PEYTAIELYQAYADYTDMMEITENVIAHMAEVatgsmIVNYQGTEINFTPPWKRMSMEDCVKEYSGVDFSTInTDEEALE 348
Cdd:PRK03932 229 AEFWMIEPEMAFADLEDNMDLAEEMLKYVVKY-----VLENCPDDLEFLNRRVDKGDIERLENFIESPFPRI-TYTEAIE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 349 VAREKGIEIKpgmrrgevinaFFEEFGEDklIQ--------------PTFITHHPVEVSPLSKRNVED-----------P 403
Cdd:PRK03932 303 ILQKSGKKFE-----------FPVEWGDD--LGseherylaeehfkkPVFVTNYPKDIKAFYMRLNPDgktvaamdllaP 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 404 R---------RTDRFEafankwELANAFSELNDPIDQKGRFIDqLRKrelgddeafemdedflkaleVGLPPTGGLGIGI 474
Cdd:PRK03932 370 GigeiiggsqREERLD------VLEARIKELGLNKEDYWWYLD-LRR--------------------YGSVPHSGFGLGF 422
|
490 500
....*....|....*....|..
gi 489530229 475 DRVIMLLTNSPSIRDVLLFPTM 496
Cdd:PRK03932 423 ERLVAYITGLDNIRDVIPFPRT 444
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
46-170 |
5.20e-09 |
|
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli aspartyl-tRNA synthetase (AspRS), the human mitochondrial (mt) AspRS-2, the discriminating (D) Thermus thermophilus AspRS-1, and the nondiscriminating (ND) Helicobacter pylori AspRS. These homodimeric enzymes are class2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. Human mtAspRS participates in mitochondrial biosynthesis; this enzyme been shown to charge E.coli native tRNAsp in addition to in vitro transcribed human mitochondrial tRNAsp. T. thermophilus is rare among bacteria in having both a D_AspRS and a ND_AspRS. H.pylori ND-AspRS can charge both tRNAASp and tRNAAsn, it is fractionally more efficient at aminoacylating tRNAAsp over tRNAAsn. The H.pylori genome does not contain AsnRS.
Pssm-ID: 239812 [Multi-domain] Cd Length: 135 Bit Score: 54.45 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 46 RTHYSMDIKDnfdSLEGKTTKIAGRIMSKRIQGKAGFIDIQDQEGRIQsyVRLDAIGEEEYSVFSTYDIGDIVGIEGEIF 125
Cdd:cd04317 1 RTHYCGELRE---SHVGQEVTLCGWVQRRRDHGGLIFIDLRDRYGIVQ--VVFDPEEAPEFELAEKLRNESVIQVTGKVR 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 489530229 126 KTKK---------GEISVKAKSVVLLCKSlQVLP--EKYHGLKDQELRYRQRYVDL 170
Cdd:cd04317 76 ARPEgtvnpklptGEIEVVASELEVLNKA-KTLPfeIDDDVNVSEELRLKYRYLDL 130
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
48-150 |
1.89e-05 |
|
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the homodimeric non-discriminating (ND) Pyrococcus kodakaraensis aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. P. kodakaraensis AspRS is a class 2b aaRS. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. P. kodakaraensis ND-AspRS can charge both tRNAAsp and tRNAAsn. Some of the enzymes in this group may be discriminating, based on the presence of homologs of asparaginyl-tRNA synthetase (AsnRS) in their completed genomes.
Pssm-ID: 239811 [Multi-domain] Cd Length: 108 Bit Score: 43.84 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 48 HYSMDIKDNFDsleGKTTKIAGRIMSKRIQGKAGFIDIQDQEGRIQSYVRLDAIGEEEYSVFSTYDIGDIVGIEGEIFKT 127
Cdd:cd04316 1 HYSAEITPELD---GEEVTVAGWVHEIRDLGGIKFVILRDREGIVQVTAPKKKVDKELFKTVRKLSRESVISVTGTVKAE 77
|
90 100
....*....|....*....|....*
gi 489530229 128 KK--GEISVKAKSVVLLCKSLQVLP 150
Cdd:cd04316 78 PKapNGVEIIPEEIEVLSEAKTPLP 102
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
66-142 |
7.93e-04 |
|
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli asparaginyl-tRNA synthetase (AsnRS) and, in Arabidopsis thaliana and Saccharomyces cerevisiae mitochondrial (mt) AsnRS. This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. 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. S. cerevisiae mtAsnRS can charge E.coli tRNA with asparagines. Mutations in the gene for S. cerevisiae mtAsnRS has been found to induce a "petite" phenotype typical for a mutation in a nuclear gene that results in a non-functioning mitochondrial protein synthesis system.
Pssm-ID: 239813 [Multi-domain] Cd Length: 82 Bit Score: 38.32 E-value: 7.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530229 66 KIAGRIMSKRIQGKAGFIDIQDqeGR----IQSYVRLDAIGEEEYSVFSTydiGDIVGIEGEIFKT--KKGEISVKAKSV 139
Cdd:cd04318 3 TVNGWVRSVRDSKKISFIELND--GSclknLQVVVDKELTNFKEILKLST---GSSIRVEGVLVKSpgAKQPFELQAEKI 77
|
...
gi 489530229 140 VLL 142
Cdd:cd04318 78 EVL 80
|
|
| |
