|
Name |
Accession |
Description |
Interval |
E-value |
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
13-500 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 908.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 13 QEENTLIALRKEKLAAGRAKGQA-FPNDFRRDSYCNDLQKQYVDKTKEELAEAAIPVKVAGRIMLNRG----SFMVIQDM 87
Cdd:PRK00484 1 EELNEQIAVRREKLAELREQGIDpYPNKFERTHTAAELRAKYDDKEKEELEELEIEVSVAGRVMLKRVmgkaSFATLQDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 88 TGRIQVYVNRKTLPEETLAEVKTWDLGDIIAAEGTLARSGKGDLYVEMTTVRLLTKSLRPLPDKHHGLTDTEQRYRQRYV 167
Cdd:PRK00484 81 SGRIQLYVSKDDVGEEALEAFKKLDLGDIIGVEGTLFKTKTGELSVKATELTLLTKSLRPLPDKFHGLTDVETRYRQRYV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 168 DLIVNEDVRETFRVRSQVIAHIRSFLMKRDFLEVETPMLQTIPGGAAAKPFETHHNALDMEMFLRIAPELYLKRLVVGGF 247
Cdd:PRK00484 161 DLIVNPESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARPFITHHNALDIDLYLRIAPELYLKRLIVGGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 248 EKVFEINRNFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQLVLGTTDVPYGDKVFHFGEPFVRLSVFDS 327
Cdd:PRK00484 241 ERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTYQGTEIDFGPPFKRLTMVDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 328 ILKYnpdlTAADL--QDVDKARAIAKKAGAKVLGFEGLGKLQVMIFEELVEHKLEQPHFITQYPFEVSPLARRNDENPSV 405
Cdd:PRK00484 321 IKEY----TGVDFddMTDEEARALAKELGIEVEKSWGLGKLINELFEEFVEPKLIQPTFITDYPVEISPLAKRHREDPGL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 406 TDRFELFIGGREIANAYSELNDAEDQAERFQAQVADKDAGDDEAMHYDADFVRALEYGMPPTAGEGIGIDRLVMLLTDSP 485
Cdd:PRK00484 397 TERFELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSP 476
|
490
....*....|....*
gi 492049176 486 SIRDVILFPHMRPQA 500
Cdd:PRK00484 477 SIRDVILFPLMRPEK 491
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
12-500 |
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: 871.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 12 QQEENTLIALRKEKLAAGRAKG-QAFPNDFRRDSYCNDLQKQYVDKTKEElaEAAIPVKVAGRIMLNRG----SFMVIQD 86
Cdd:COG1190 4 EEDLNEQIRVRREKLEELREAGiDPYPNKFPRTHTAAEIREKYDELEAEE--ETGDEVSVAGRIMAKRDmgkaSFADLQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 87 MTGRIQVYVNRKTLPEETLAEVKTWDLGDIIAAEGTLARSGKGDLYVEMTTVRLLTKSLRPLPDKHHGLTDTEQRYRQRY 166
Cdd:COG1190 82 GSGRIQLYLRRDELGEEAYELFKLLDLGDIVGVEGTVFRTKTGELSVKVEELTLLSKSLRPLPEKFHGLTDPETRYRQRY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 167 VDLIVNEDVRETFRVRSQVIAHIRSFLMKRDFLEVETPMLQTIPGGAAAKPFETHHNALDMEMFLRIAPELYLKRLVVGG 246
Cdd:COG1190 162 VDLIVNPEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 247 FEKVFEINRNFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQLVLGTTDVPYGDKVFHFGEPFVRLSVFD 326
Cdd:COG1190 242 FERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGTTKVTYQGQEIDLSPPWRRITMVE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 327 SILKYNpDLTAADLQDVDKARAIAKKAGAKVLGFEGLGKLQVMIFEELVEHKLEQPHFITQYPFEVSPLARRNDENPSVT 406
Cdd:COG1190 322 AIKEAT-GIDVTPLTDDEELRALAKELGIEVDPGWGRGKLIDELFEELVEPKLIQPTFVTDYPVEVSPLAKRHRDDPGLT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 407 DRFELFIGGREIANAYSELNDAEDQAERFQAQVADKDAGDDEAMHYDADFVRALEYGMPPTAGEGIGIDRLVMLLTDSPS 486
Cdd:COG1190 401 ERFELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSPS 480
|
490
....*....|....
gi 492049176 487 IRDVILFPHMRPQA 500
Cdd:COG1190 481 IRDVILFPLMRPEK 494
|
|
| lysS_bact |
TIGR00499 |
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ... |
14-499 |
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: 646.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 14 EENTLIALRKEKLAAGRAKGQ-AFPNDFRRDSYCNDLQKQYVDKTKEELAEAAIPVKVAGRIMLNRG----SFMVIQDMT 88
Cdd:TIGR00499 1 ELNDQAQQRLEKLNRLRQTGNnPYLHKFERTHSAQEFQEKYADLSNEELKEKELKVSIAGRIKAIRSmgkaTFITLQDES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 89 GRIQVYVNRKTLPEETLA-EVKTWDLGDIIAAEGTLARSGKGDLYVEMTTVRLLTKSLRPLPDKHHGLTDTEQRYRQRYV 167
Cdd:TIGR00499 81 GQIQLYVNKNKLPEDFYEfDEYLLDLGDIIGVTGYPFKTKTGELSVKVTELQILTKCLQPLPDKWHGLTDQETRYRQRYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 168 DLIVNEDVRETFRVRSQVIAHIRSFLMKRDFLEVETPMLQTIPGGAAAKPFETHHNALDMEMFLRIAPELYLKRLVVGGF 247
Cdd:TIGR00499 161 DLIVNPDVRQTFLKRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKPFITHHNALDMDLYLRIAPELYLKRLIVGGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 248 EKVFEINRNFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQLVLGTTDVPYGDKVFHFGEPFVRLSVFDS 327
Cdd:TIGR00499 241 EKVYEIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTFIINYNDLEIDLKPPWKRITMVDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 328 ILKyNPDLTAADLQDVDKARAIAKKAGAKVLGFE-GLGKLQVMIFEELVEHKLEQPHFITQYPFEVSPLARRNDENPSVT 406
Cdd:TIGR00499 321 LEM-VTGIDFDILKDDETAKALAKEHGIEVAEDSlTLGHILNKFFEQFLEHTLIQPTFITHYPAEISPLAKRDPSNPEFT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 407 DRFELFIGGREIANAYSELNDAEDQAERFQAQVADKDAGDDEAMHYDADFVRALEYGMPPTAGEGIGIDRLVMLLTDSPS 486
Cdd:TIGR00499 400 ERFELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGIGIDRLVMLLTDAPS 479
|
490
....*....|...
gi 492049176 487 IRDVILFPHMRPQ 499
Cdd:TIGR00499 480 IRDVLLFPQLRPQ 492
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
1-499 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 613.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 1 MSDQQLDPQALQQEENTLIALRKEKLAAGRAKGQAFPNDFRRDSYCNDLQKQYVDKTKEELAEAAIPVKVAGRIMLNR-- 78
Cdd:PRK12445 1 MSEQETRGANEAIDFNDELRNRREKLAALRQQGVAFPNDFRRDHTSDQLHEEFDAKDNQELESLNIEVSVAGRMMTRRim 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 79 --GSFMVIQDMTGRIQVYVNRKTLPEETLAE-VKTWDLGDIIAAEGTLARSGKGDLYVEMTTVRLLTKSLRPLPDKHHGL 155
Cdd:PRK12445 81 gkASFVTLQDVGGRIQLYVARDSLPEGVYNDqFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFHGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 156 TDTEQRYRQRYVDLIVNEDVRETFRVRSQVIAHIRSFLMKRDFLEVETPMLQTIPGGAAAKPFETHHNALDMEMFLRIAP 235
Cdd:PRK12445 161 QDQEVRYRQRYLDLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 236 ELYLKRLVVGGFEKVFEINRNFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQLVLGTTDVPYGDKVFHF 315
Cdd:PRK12445 241 ELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFDF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 316 GEPFVRLSVFDSILKYNPDLTAADLQDVDKARAIAKKAGAKVLGFEGLGKLQVMIFEELVEHKLEQPHFITQYPFEVSPL 395
Cdd:PRK12445 321 GKPFEKLTMREAIKKYRPETDMADLDNFDAAKALAESIGITVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 396 ARRNDENPSVTDRFELFIGGREIANAYSELNDAEDQAERFQAQVADKDAGDDEAMHYDADFVRALEYGMPPTAGEGIGID 475
Cdd:PRK12445 401 ARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGID 480
|
490 500
....*....|....*....|....
gi 492049176 476 RLVMLLTDSPSIRDVILFPHMRPQ 499
Cdd:PRK12445 481 RMIMLFTNSHTIRDVILFPAMRPQ 504
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
2-499 |
0e+00 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 604.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 2 SDQQLDPQALQqeentliALRKEKLAAGRAKGQ-AFPNDFRRDSYCNDLQKQYVDKTKEELAEAAIpVKVAGRIMLNRGS 80
Cdd:PLN02502 52 DDETMDPTQYR-------ANRLKKVEALRAKGVePYPYKFDVTHTAPELQEKYGSLENGEELEDVS-VSVAGRIMAKRAF 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 81 ----FMVIQDMTGRIQVYVNRK--TLPEETLAEVKTW-DLGDIIAAEGTLARSGKGDLYVEMTTVRLLTKSLRPLPDKHH 153
Cdd:PLN02502 124 gklaFYDLRDDGGKIQLYADKKrlDLDEEEFEKLHSLvDRGDIVGVTGTPGKTKKGELSIFPTSFEVLTKCLLMLPDKYH 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 154 GLTDTEQRYRQRYVDLIVNEDVRETFRVRSQVIAHIRSFLMKRDFLEVETPMLQTIPGGAAAKPFETHHNALDMEMFLRI 233
Cdd:PLN02502 204 GLTDQETRYRQRYLDLIANPEVRDIFRTRAKIISYIRRFLDDRGFLEVETPMLNMIAGGAAARPFVTHHNDLNMDLYLRI 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 234 APELYLKRLVVGGFEKVFEINRNFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQLVLGTTDVPYGDKVF 313
Cdd:PLN02502 284 ATELHLKRLVVGGFERVYEIGRQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKELTGSYKIKYHGIEI 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 314 HFGEPFVRLSVFDSILKYNPDLTAADLQDvDKARAIAKKAGAK----VLGFEGLGKLQVMIFEELVEHKLEQPHFITQYP 389
Cdd:PLN02502 364 DFTPPFRRISMISLVEEATGIDFPADLKS-DEANAYLIAACEKfdvkCPPPQTTGRLLNELFEEFLEETLVQPTFVLDHP 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 390 FEVSPLARRNDENPSVTDRFELFIGGREIANAYSELNDAEDQAERFQAQVADKDAGDDEAMHYDADFVRALEYGMPPTAG 469
Cdd:PLN02502 443 VEMSPLAKPHRSKPGLTERFELFINGRELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGG 522
|
490 500 510
....*....|....*....|....*....|
gi 492049176 470 EGIGIDRLVMLLTDSPSIRDVILFPHMRPQ 499
Cdd:PLN02502 523 WGLGIDRLVMLLTDSASIRDVIAFPAMKPQ 552
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
172-498 |
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: 540.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 172 NEDVRETFRVRSQVIAHIRSFLMKRDFLEVETPMLQTIPGGAAAKPFETHHNALDMEMFLRIAPELYLKRLVVGGFEKVF 251
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 252 EINRNFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQLVLGTTDVPYGDKVFHFGEPFVRLSVFDSILKY 331
Cdd:cd00775 81 EIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIEYGGKELDFTPPFKRVTMVDALKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 332 NP--DLTAADLQDVDKARAIAKKAGAKVLGFEGLGKLQVMIFEELVEHKLEQPHFITQYPFEVSPLARRNDENPSVTDRF 409
Cdd:cd00775 161 TGidFPELDLEQPEELAKLLAKLIKEKIEKPRTLGKLLDKLFEEFVEPTLIQPTFIIDHPVEISPLAKRHRSNPGLTERF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 410 ELFIGGREIANAYSELNDAEDQAERFQAQVADKDAGDDEAMHYDADFVRALEYGMPPTAGEGIGIDRLVMLLTDSPSIRD 489
Cdd:cd00775 241 ELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLTDSNSIRD 320
|
....*....
gi 492049176 490 VILFPHMRP 498
Cdd:cd00775 321 VILFPAMRP 329
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
22-499 |
9.17e-163 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 489.48 E-value: 9.17e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 22 RKEKLAAGRAKG-QAFPNDFRRDSYCndlqKQYVDKTKEElaeaaiPVKVAGRIMLNRG----SFMVIQDMTGRIQVYVN 96
Cdd:PRK02983 617 RLAKLEALRAAGvDPYPVGVPPTHTV----AEALDAPTGE------EVSVSGRVLRIRDyggvLFADLRDWSGELQVLLD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 97 RKTLPEETLAEVK-TWDLGDIIAAEGTLARSGKGDLYVEMTTVRLLTKSLRPLPDKHHGLTDTEQRYRQRYVDLIVNEDV 175
Cdd:PRK02983 687 ASRLEQGSLADFRaAVDLGDLVEVTGTMGTSRNGTLSLLVTSWRLAGKCLRPLPDKWKGLTDPEARVRQRYLDLAVNPEA 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 176 RETFRVRSQVIAHIRSFLMKRDFLEVETPMLQTIPGGAAAKPFETHHNALDMEMFLRIAPELYLKRLVVGGFEKVFEINR 255
Cdd:PRK02983 767 RDLLRARSAVVRAVRETLVARGFLEVETPILQQVHGGANARPFVTHINAYDMDLYLRIAPELYLKRLCVGGVERVFELGR 846
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 256 NFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQLVLGTTDVPYGDKvfHFGEPFVRLS-------VFDSI 328
Cdd:PRK02983 847 NFRNEGVDATHNPEFTLLEAYQAHADYDTMRDLTRELIQNAAQAAHGAPVVMRPDG--DGVLEPVDISgpwpvvtVHDAV 924
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 329 -----LKYNPDLTAADLqdvdkaRAIAKKAGAKVLGFEGLGKLQVMIFEELVEHKLEQPHFITQYPFEVSPLARRNDENP 403
Cdd:PRK02983 925 sealgEEIDPDTPLAEL------RKLCDAAGIPYRTDWDAGAVVLELYEHLVEDRTTFPTFYTDFPTSVSPLTRPHRSDP 998
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 404 SVTDRFELFIGGREIANAYSELNDAEDQAERFQAQVADKDAGDDEAMHYDADFVRALEYGMPPTAGEGIGIDRLVMLLTD 483
Cdd:PRK02983 999 GLAERWDLVAWGVELGTAYSELTDPVEQRRRLTEQSLLAAGGDPEAMELDEDFLQALEYAMPPTGGLGMGVDRLVMLLTG 1078
|
490
....*....|....*.
gi 492049176 484 SpSIRDVILFPHMRPQ 499
Cdd:PRK02983 1079 R-SIRETLPFPLVKPR 1093
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
157-497 |
2.03e-124 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 365.74 E-value: 2.03e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 157 DTEQRYRQRYVDLiVNEDVRETFRVRSQVIAHIRSFLMKRDFLEVETPMLQTIPGGAAAKPFETHHNALDMEMFLRIAPE 236
Cdd:pfam00152 1 DEETRLKYRYLDL-RRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 237 LYLKRLVVGGFEKVFEINRNFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQLVLGTTDVPYGDKVFHFG 316
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 317 EPFVRLSVFDSILKYNPDLTAADLQDVDKAraiakkagakvlgfeglgKLQVMIfEELVEHKLEQPHFITQYPFEVSPLA 396
Cdd:pfam00152 160 KPFPRITYAEAIEKLNGKDVEELGYGSDKP------------------DLRFLL-ELVIDKNKFNPLWVTDFPAEHHPFT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 397 RRNDEN-PSVTDRFELFIGGREIANAYSELNDAEDQAERFQAQVADKdagdDEAMHYDADFVRALEYGMPPTAGEGIGID 475
Cdd:pfam00152 221 MPKDEDdPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDP----EEAEEKFGFYLDALKYGAPPHGGLGIGLD 296
|
330 340
....*....|....*....|..
gi 492049176 476 RLVMLLTDSPSIRDVILFPHMR 497
Cdd:pfam00152 297 RLVMLLTGLESIREVIAFPKTR 318
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
3-498 |
3.38e-121 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 367.03 E-value: 3.38e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 3 DQQLDPQALQQEENTLIALRKeklaagrAKG-QAFPNDFRRDSYCNDLQKQYVDKTKEELAEAAiPVKVAGRIMLNRGSF 81
Cdd:PTZ00417 77 EAEVDPRLYYENRSKFIQEQK-------AKGiNPYPHKFERTITVPEFVEKYQDLASGEHLEDT-ILNVTGRIMRVSASG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 82 MVIQ--DMTG---RIQVYVNRKTLPEETLAEVKTWD---LGDIIAAEGTLARSGKGDLYVEMTTVRLLTKSLRPLPDKHh 153
Cdd:PTZ00417 149 QKLRffDLVGdgaKIQVLANFAFHDHTKSNFAECYDkirRGDIVGIVGFPGKSKKGELSIFPKETIILSPCLHMLPMKY- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 154 GLTDTEQRYRQRYVDLIVNEDVRETFRVRSQVIAHIRSFLMKRDFLEVETPMLQTIPGGAAAKPFETHHNALDMEMFLRI 233
Cdd:PTZ00417 228 GLKDTEIRYRQRYLDLMINESTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLVAGGANARPFITHHNDLDLDLYLRI 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 234 APELYLKRLVVGGFEKVFEINRNFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQLVLGT------TDVP 307
Cdd:PTZ00417 308 ATELPLKMLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHLFGTykilynKDGP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 308 YGDKV-FHFGEPFVRLSVFDSILKynpdLTAADLQD-------VDKARAIAKKAGAKVLGFEGLGKLQVMIFEELVEHKL 379
Cdd:PTZ00417 388 EKDPIeIDFTPPYPKVSIVEELEK----LTNTKLEQpfdspetINKMINLIKENKIEMPNPPTAAKLLDQLASHFIENKY 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 380 -EQPHFITQYPFEVSPLARRNDENPSVTDRFELFIGGREIANAYSELNDAEDQAERFQAQVADKDAGDDEAMHYDADFVR 458
Cdd:PTZ00417 464 pNKPFFIIEHPQIMSPLAKYHRSKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCT 543
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 492049176 459 ALEYGMPPTAGEGIGIDRLVMLLTDSPSIRDVILFPHMRP 498
Cdd:PTZ00417 544 SLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFPTMRP 583
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
179-498 |
1.12e-116 |
|
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: 344.46 E-value: 1.12e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 179 FRVRSQVIAHIRSFLMKRDFLEVETPMLQTIPGGAAAKPFETHHNALDMEMFLRIAPELYLKRLVVGGFEKVFEINRNFR 258
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 259 NEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQLVLGTTDVPYGDKVFHFGEPFVRLSvfdsilkynpdltaa 338
Cdd:cd00669 81 NEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYGFELEDFGLPFPRLT--------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 339 dlqdvdkaraiakkagakvlgfeglgklqvmiFEELVEhKLEQPHFITQYPFE-VSPLARRNDENPSVTDRFELFIGGRE 417
Cdd:cd00669 146 --------------------------------YREALE-RYGQPLFLTDYPAEmHSPLASPHDVNPEIADAFDLFINGVE 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 418 IANAYSELNDAEDQAERFQAQVADKDAGddeaMHYDADFVRALEYGMPPTAGEGIGIDRLVMLLTDSPSIRDVILFPHMR 497
Cdd:cd00669 193 VGNGSSRLHDPDIQAEVFQEQGINKEAG----MEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKMR 268
|
.
gi 492049176 498 P 498
Cdd:cd00669 269 R 269
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
63-497 |
4.60e-112 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 345.86 E-value: 4.60e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 63 EAAIPVKVAGRIM----LNRGSFMVIQDMTGRIQVYVN-RKTLPEETLAEVK-TWDLGDIIAAEGTLARSGKGDLYVEMT 136
Cdd:PTZ00385 105 AAQATVRVAGRVTsvrdIGKIIFVTIRSNGNELQVVGQvGEHFTREDLKKLKvSLRVGDIIGADGVPCRMQRGELSVAAS 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 137 TVRLLT------KSLRPLPDKHHGLTDTEQRYRQRYVDLIVNEDVRETFRVRSQVIAHIRSFLMKRDFLEVETPMLQTIP 210
Cdd:PTZ00385 185 RMLILSpyvctdQVVCPNLRGFTVLQDNDVKYRYRFTDMMTNPCVIETIKKRHVMLQALRDYFNERNFVEVETPVLHTVA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 211 GGAAAKPFETHHNALDMEMFLRIAPELYLKRLVVGGFEKVFEINRNFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTE 290
Cdd:PTZ00385 265 SGANAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTSCEFYAAYHTYEDLMPMTE 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 291 ELFRELAQLVLGTTDV------PYGDKV-FHFGEPFVRLSVFDSILKynpdLTAADL---QDVDKARAIAKKAGAKV--- 357
Cdd:PTZ00385 345 DIFRQLAMRVNGTTVVqiypenAHGNPVtVDLGKPFRRVSVYDEIQR----MSGVEFpppNELNTPKGIAYMSVVMLryn 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 358 LGFEGLgKLQVMIFEELVE----HKLEQPHFITQYPFEVSPLARRNDENPSVTDRFELFIGGREIANAYSELNDAEDQAE 433
Cdd:PTZ00385 421 IPLPPV-RTAAKMFEKLIDffitDRVVEPTFVMDHPLFMSPLAKEQVSRPGLAERFELFVNGIEYCNAYSELNDPHEQYH 499
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492049176 434 RFQAQVADKDAGDDEAMHYDADFVRALEYGMPPTAGEGIGIDRLVMLLTDSPSIRDVILFPHMR 497
Cdd:PTZ00385 500 RFQQQLVDRQGGDEEAMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFPLLR 563
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
176-491 |
2.46e-80 |
|
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: 252.33 E-value: 2.46e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 176 RETFRVRSQVIAHIRSFLMKRDFLEVETPMLQTIPGGAAA-KPFET---HHNALDMEMFLRIAPELYLKRLVVGGFEKVF 251
Cdd:COG2269 3 REALRARARLLAAIRAFFAERGVLEVETPALSVAPGTDPHlDSFATefiGPDGGGRPLYLHTSPEFAMKRLLAAGSGPIY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 252 EINRNFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQLVLGttdvpygdkvfhfgEPFVRLSVFDSILKY 331
Cdd:COG2269 83 QIAKVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAAGF--------------APAERLSYQEAFLRY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 332 -NPDLTAADLQDVdkaRAIAKKAGAKV---LGFEGLgkLQVmIFEELVEHKL--EQPHFITQYPFEVSPLARRNDENPSV 405
Cdd:COG2269 149 lGIDPLTADLDEL---AAAAAAAGLRVaddDDRDDL--LDL-LLSERVEPQLgrDRPTFLYDYPASQAALARISPDDPRV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 406 TDRFELFIGGREIANAYSELNDAEDQAERFQAQVADKDAGDDEAMHYDADFVRALEYGMPPTAGEGIGIDRLVMLLTDSP 485
Cdd:COG2269 223 AERFELYACGVELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALGAE 302
|
....*.
gi 492049176 486 SIRDVI 491
Cdd:COG2269 303 RIDDVL 308
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
192-491 |
5.81e-75 |
|
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: 237.83 E-value: 5.81e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 192 FLMKRDFLEVETPMLQTIPGGAAA-KPFETH---HNALDMEMFLRIAPELYLKRLVVGGFEKVFEINRNFRNEGVSTRHN 267
Cdd:TIGR00462 1 FFAERGVLEVETPLLSPAPVTDPHlDAFATEfvgPDGQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 268 PEFTMLEFYQAYADYEDNMDLTEELFRELAQlvlgttdvpygdkvfHFGEPFVRLSVFDSILKYNP-DLTAADLQDVDKA 346
Cdd:TIGR00462 81 PEFTMLEWYRPGFDYHDLMDEVEALLQELLG---------------DPFAPAERLSYQEAFLRYAGiDPLTASLAELQAA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 347 RAIAKKAGAKVLGFEGLgkLQVmIFEELVEHKL--EQPHFITQYPFEVSPLARRNDENPSVTDRFELFIGGREIANAYSE 424
Cdd:TIGR00462 146 AAAHGIRASEEDDRDDL--LDL-LFSEKVEPHLgfGRPTFLYDYPASQAALARISPDDPRVAERFELYIKGLELANGFHE 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492049176 425 LNDAEDQAERFQAQVADKDAGDDEAMHYDADFVRALEYGMPPTAGEGIGIDRLVMLLTDSPSIRDVI 491
Cdd:TIGR00462 223 LTDAAEQRRRFEADNALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDVL 289
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
177-490 |
2.57e-54 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 184.75 E-value: 2.57e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 177 ETFRVRSQVIAHIRSFLMKRDFLEVETPMLQTIPG-GAAAKPFETHHNALDME----MFLRIAPELYLKRLVVGGFEKVF 251
Cdd:PRK09350 3 PNLLKRAKIIAEIRRFFADRGVLEVETPILSQATVtDIHLVPFETRFVGPGASqgktLWLMTSPEYHMKRLLAAGSGPIF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 252 EINRNFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFrelaQLVLGTtdvpygdkvfhfgEPFVRLSVFDSILKY 331
Cdd:PRK09350 83 QICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLL----QQVLDC-------------EPAESLSYQQAFLRY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 332 npdlTAADLQDVDKA--RAIAKKagakvLGFEGLGK--------LQvMIFEELVEHKL--EQPHFITQYPFEVSPLARRN 399
Cdd:PRK09350 146 ----LGIDPLSADKTqlREVAAK-----LGLSNIADeeedrdtlLQ-LLFTFGVEPNIgkEKPTFVYHFPASQAALAKIS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 400 DENPSVTDRFELFIGGREIANAYSELNDAEDQAERFQAQVADKDAGDDEAMHYDADFVRALEYGMPPTAGEGIGIDRLVM 479
Cdd:PRK09350 216 TEDHRVAERFEVYFKGIELANGFHELTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCSGVALGVDRLIM 295
|
330
....*....|.
gi 492049176 480 LLTDSPSIRDV 490
Cdd:PRK09350 296 LALGAESISEV 306
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
68-169 |
7.03e-50 |
|
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: 166.11 E-value: 7.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 68 VKVAGRIMLNRGS----FMVIQDMTGRIQVYVNRKTLPEETLAEVK-TWDLGDIIAAEGTLARSGKGDLYVEMTTVRLLT 142
Cdd:cd04322 2 VSVAGRIMSKRGSgklsFADLQDESGKIQVYVNKDDLGEEEFEDFKkLLDLGDIIGVTGTPFKTKTGELSIFVKEFTLLS 81
|
90 100
....*....|....*....|....*..
gi 492049176 143 KSLRPLPDKHHGLTDTEQRYRQRYVDL 169
Cdd:cd04322 82 KSLRPLPEKFHGLTDVETRYRQRYLDL 108
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
45-497 |
7.82e-49 |
|
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: 173.70 E-value: 7.82e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 45 YCNDLQKQYVDKTkeelaeaaipVKVAGRIMLNRGS----FMVIQDMTGRIQVYVNRKTLPE-ETLAEVKTwdlGDIIAA 119
Cdd:COG0017 4 YIKDLLPEHVGQE----------VTVAGWVRTKRDSggisFLILRDGSGFIQVVVKKDKLENfEEAKKLTT---ESSVEV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 120 EGTLARSGKGDLYVEM--TTVRLLTKSLRPLP--DKHHGLtdtEQRYRQRYVDLIVNEdVRETFRVRSQVIAHIRSFLMK 195
Cdd:COG0017 71 TGTVVESPRAPQGVELqaEEIEVLGEADEPYPlqPKRHSL---EFLLDNRHLRLRTNR-FGAIFRIRSELARAIREFFQE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 196 RDFLEVETPMLqtIPGGA--AAKPFETHHnaLDMEMFLRIAPELYlKRLVVGGFEKVFEINRNFRNEGVST-RHNPEFTM 272
Cdd:COG0017 147 RGFVEVHTPII--TASATegGGELFPVDY--FGKEAYLTQSGQLY-KEALAMALEKVYTFGPTFRAEKSNTrRHLAEFWM 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 273 LEFYQAYADYEDNMDLTEELFRELAQLVLGTtdvpYGDKVFHFGEPFVRLSVFDS----ILKYnpdltaadlqdvDKARA 348
Cdd:COG0017 222 IEPEMAFADLEDVMDLAEEMLKYIIKYVLEN----CPEELEFLGRDVERLEKVPEspfpRITY------------TEAIE 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 349 IAKKAGAKVLGFEGLGKlqvmifEE---LVEHKLEQPHFITQYPFEVSPL-ARRNDENPSVTDRFELfiggreIANAYSE 424
Cdd:COG0017 286 ILKKSGEKVEWGDDLGT------EHeryLGEEFFKKPVFVTDYPKEIKAFyMKPNPDDPKTVAAFDL------LAPGIGE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 425 L-------NDAEDQAERFQAQVADKDAgddeamhYDaDFVRALEYGMPPTAGEGIGIDRLVMLLTDSPSIRDVILFPHMR 497
Cdd:COG0017 354 IiggsqreHRYDVLVERIKEKGLDPED-------YE-WYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDP 425
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
81-497 |
5.28e-46 |
|
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: 166.15 E-value: 5.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 81 FMVIQDMTGRIQVYVNRKTLPEETLAEVKTWDLGDIIAAEGTLARSGK--GDLYVEMTTVRLLTKSLRPLP----DKHHG 154
Cdd:TIGR00458 32 FVLLRDREGLIQITAPAKKVSKNLFKWAKKLNLESVVAVRGIVKIKEKapGGFEIIPTKIEVINEAKEPLPldptEKVPA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 155 LTDTeqRYRQRYVDLiVNEDVRETFRVRSQVIAHIRSFLMKRDFLEVETPMLQTIPGGAAAKPFETHHnaLDMEMFLRIA 234
Cdd:TIGR00458 112 ELDT--RLDYRFLDL-RRPTVQAIFRIRSGVLESVREFLAEEGFIEVHTPKLVASATEGGTELFPITY--FEREAFLGQS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 235 PELYLKRLVVGGFEKVFEINRNFRNEGVST-RHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQLVLGTTDVPYGDKVF 313
Cdd:TIGR00458 187 PQLYKQQLMAAGFERVYEIGPIFRAEEHNThRHLNEATSIDIEMAFEDHHDVMDILEELVVRVFEDVPERCAHQLETLEF 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 314 HF---GEPFVRLSVfdsilkynpdltaadlqdvDKARAIAKKAGAKVLGFEGLGKLQvmifEELVEHKLEQPHFITQYPF 390
Cdd:TIGR00458 267 KLekpEGKFVRLTY-------------------DEAIEMANAKGVEIGWGEDLSTEA----EKALGEEMDGLYFITDWPT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 391 EVSPLARRNDE-NPSVTDRFELFIGGREIANAYSELNDAEDQAERFQAQVADKDAGDDeamhydadFVRALEYGMPPTAG 469
Cdd:TIGR00458 324 EIRPFYTMPDEdNPEISKSFDLMYRDLEISSGAQRIHLHDLLVERIKAKGLNPEGFKD--------YLEAFSYGMPPHAG 395
|
410 420
....*....|....*....|....*...
gi 492049176 470 EGIGIDRLVMLLTDSPSIRDVILFPHMR 497
Cdd:TIGR00458 396 WGLGAERFVMFLLGLKNIREAVLFPRDR 423
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
41-494 |
1.27e-43 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 159.59 E-value: 1.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 41 RRDSYCNDLQKQYVDKTkeelaeaaipVKVAG---RIM-LNRGSFMVIQDMTGRIQVYVNRKTLPEeTLAEVKTWDLGDI 116
Cdd:PRK05159 2 MKRHLTSELTPELDGEE----------VTLAGwvhEIRdLGGIAFLILRDRSGIIQVVVKKKVDEE-LFETIKKLKRESV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 117 IAAEGTLARSGKGDLYVE--MTTVRLLTKSLRPLPDKHHG--LTDTEQRYRQRYVDLiVNEDVRETFRVRSQVIAHIRSF 192
Cdd:PRK05159 71 VSVTGTVKANPKAPGGVEviPEEIEVLNKAEEPLPLDISGkvLAELDTRLDNRFLDL-RRPRVRAIFKIRSEVLRAFREF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 193 LMKRDFLEVETPML--QTIPGGAAAKP---FEThhnaldmEMFLRIAPELYLKRLVVGGFEKVFEINRNFRNEGVST-RH 266
Cdd:PRK05159 150 LYENGFTEIFTPKIvaSGTEGGAELFPidyFEK-------EAYLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTsRH 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 267 NPEFTMLEFYQAYAD-YEDNMDLTEELFRELAQLVLGTtdvpYGDKVFHFG-------EPFVRlsvfdsiLKYnpdltaa 338
Cdd:PRK05159 223 LNEYTSIDVEMGFIDdHEDVMDLLENLLRYMYEDVAEN----CEKELELLGielpvpeTPIPR-------ITY------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 339 dlqdvDKARAIAKKAGAKVLGFEGLGKLQVMIFEELVEHKLEQPH-FITQYPFEVSPL-ARRNDENPSVTDRFELFIGGR 416
Cdd:PRK05159 285 -----DEAIEILKSKGNEISWGDDLDTEGERLLGEYVKEEYGSDFyFITDYPSEKRPFyTMPDEDDPEISKSFDLLFRGL 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492049176 417 EIANAYSELNDAEDQAERFQAQvadkdaG-DDEAMHYdadFVRALEYGMPPTAGEGIGIDRLVMLLTDSPSIRDVILFP 494
Cdd:PRK05159 360 EITSGGQRIHRYDMLVESIKEK------GlNPESFEF---YLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFP 429
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
157-494 |
4.71e-39 |
|
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: 144.25 E-value: 4.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 157 DTEQRYRQRYVDLIVNEdVRETFRVRSQVIAHIRSFLMKRDFLEVETPMLQTIP--GGAAAKPFethhNALDMEMFLRIA 234
Cdd:cd00776 3 NLETLLDNRHLDLRTPK-VQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDteGGAELFKV----SYFGKPAYLAQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 235 PELYlKRLVVGGFEKVFEINRNFRNEGVST-RHNPEFTMLEFYQAYA-DYEDNMDLTEELFRELAQLVL------GTTDV 306
Cdd:cd00776 78 PQLY-KEMLIAALERVYEIGPVFRAEKSNTrRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLercakeLELVN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 307 PYGDKVFHFGEPFVRLSvfdsilkYnpdltaadlqdvDKARAIAKKAG--AKVLGFEGLGKLQvmifEE-LVEHKLEQPH 383
Cdd:cd00776 157 QLNRELLKPLEPFPRIT-------Y------------DEAIELLREKGveEEVKWGEDLSTEH----ERlLGEIVKGDPV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 384 FITQYPFEVSPL-ARRNDENPSVTDRFELFI-GGREIANAYSELNDAEDQAERFqaqvadKDAGDDEAMHYDadFVRALE 461
Cdd:cd00776 214 FVTDYPKEIKPFyMKPDDDNPETVESFDLLMpGVGEIVGGSQRIHDYDELEERI------KEHGLDPESFEW--YLDLRK 285
|
330 340 350
....*....|....*....|....*....|...
gi 492049176 462 YGMPPTAGEGIGIDRLVMLLTDSPSIRDVILFP 494
Cdd:cd00776 286 YGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
179-494 |
2.33e-32 |
|
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. AspRS is a homodimer, which attaches a specific amino acid to the 3' OH group of ribose of the appropriate tRNA. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. AspRS in this family differ from those found in the AsxRS family by a GAD insert in the core domain.
Pssm-ID: 238400 [Multi-domain] Cd Length: 280 Bit Score: 124.99 E-value: 2.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 179 FRVRSQVIAHIRSFLMKRDFLEVETPML-QTIPGGAA--AKPFETHHNaldmeMF--LRIAPELYLKRLVVGGFEKVFEI 253
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILtKSTPEGARdfLVPSRLHPG-----KFyaLPQSPQLFKQLLMVSGFDRYFQI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 254 NRNFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQLVLGTTDVpygdkvfhfgEPFVRLSVFDSILKYnp 333
Cdd:cd00777 76 ARCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLGVELT----------TPFPRMTYAEAMERY-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 334 dltaadlqdvdkaraiakkagakvlGFEGLGKLQVMIFEELVEH-KLEQPHfitqYPF-----EVSPLARRNDENpSVTD 407
Cdd:cd00777 144 -------------------------GFKFLWIVDFPLFEWDEEEgRLVSAH----HPFtapkeEDLDLLEKDPED-ARAQ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 408 RFELFIGGREIANAYSELNDAEDQAERFqaqvadKDAGDDEAMHYD--ADFVRALEYGMPPTAGEGIGIDRLVMLLTDSP 485
Cdd:cd00777 194 AYDLVLNGVELGGGSIRIHDPDIQEKVF------EILGLSEEEAEEkfGFLLEAFKYGAPPHGGIALGLDRLVMLLTGSE 267
|
....*....
gi 492049176 486 SIRDVILFP 494
Cdd:cd00777 268 SIRDVIAFP 276
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
39-494 |
1.15e-29 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 122.48 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 39 DFRRDSYCNDLQKQYVDKTkeelaeaaipVKVAG---RImlnR--GS--FMVIQDMTGRIQVYVNrktlPEETLAEVKTw 111
Cdd:PRK00476 1 HMMRTHYCGELRESHVGQT----------VTLCGwvhRR---RdhGGliFIDLRDREGIVQVVFD----PDAEAFEVAE- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 112 DLG--DIIAAEGTL-ARSGK--------GDLYVEMTTVRLLTKS--LrPLPDKHHGLTDTEQRYRQRYVDLiVNEDVRET 178
Cdd:PRK00476 63 SLRseYVIQVTGTVrARPEGtvnpnlptGEIEVLASELEVLNKSktL-PFPIDDEEDVSEELRLKYRYLDL-RRPEMQKN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 179 FRVRSQVIAHIRSFLMKRDFLEVETPML--QTiPGGAAakpfethhnalDmemFL---RI----------APELYLKRLV 243
Cdd:PRK00476 141 LKLRSKVTSAIRNFLDDNGFLEIETPILtkST-PEGAR-----------D---YLvpsRVhpgkfyalpqSPQLFKQLLM 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 244 VGGFEKVFEINRNFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQLVLGTtDVPygdkvfhfgEPFVRLS 323
Cdd:PRK00476 206 VAGFDRYYQIARCFRDEDLRADRQPEFTQIDIEMSFVTQEDVMALMEGLIRHVFKEVLGV-DLP---------TPFPRMT 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 324 VFDSILKY---NPDL--------------------------------------TAADL--QDVDKARAIAKKAGAKVLGF 360
Cdd:PRK00476 276 YAEAMRRYgsdKPDLrfglelvdvtdlfkdsgfkvfagaandggrvkairvpgGAAQLsrKQIDELTEFAKIYGAKGLAY 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 361 -----------------------------------------------EGLGKLQVMIFEE--LVEHKLEQPHFITQYP-F 390
Cdd:PRK00476 356 ikvnedglkgpiakflseeelaallertgakdgdliffgadkakvvnDALGALRLKLGKElgLIDEDKFAFLWVVDFPmF 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 391 EVSplarrNDEN-----------PSVTDRFELFIG--GREIANAY------SEL-------NDAEDQAERFQAqvadkdA 444
Cdd:PRK00476 436 EYD-----EEEGrwvaahhpftmPKDEDLDELETTdpGKARAYAYdlvlngYELgggsiriHRPEIQEKVFEI------L 504
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 492049176 445 G--DDEAmhyDADF---VRALEYGMPPTAGEGIGIDRLVMLLTDSPSIRDVILFP 494
Cdd:PRK00476 505 GisEEEA---EEKFgflLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
41-494 |
2.79e-27 |
|
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439943 [Multi-domain] Cd Length: 589 Bit Score: 115.48 E-value: 2.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 41 RRDSYCNDLQKQYVDKTkeelaeaaipVKVAGRImlNR----GS--FMVIQDMTGRIQVYVNRKTlPEETLAEVKTWDLG 114
Cdd:COG0173 2 YRTHYCGELRESDVGQE----------VTLSGWV--HRrrdhGGliFIDLRDRYGITQVVFDPDD-SAEAFEKAEKLRSE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 115 DIIAAEGTL-ARSGK--------GDLYVEMTTVRLLTKSlRPLPDKHHGLTDT--EQRYRQRYVDLiVNEDVRETFRVRS 183
Cdd:COG0173 69 YVIAVTGKVrARPEGtvnpklptGEIEVLASELEILNKA-KTPPFQIDDDTDVseELRLKYRYLDL-RRPEMQKNLILRH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 184 QVIAHIRSFLMKRDFLEVETPMLQ--TiPGGAAakpfethhnalDmemFL---RI----------APELYLKRLVVGGFE 248
Cdd:COG0173 147 KVTKAIRNYLDENGFLEIETPILTksT-PEGAR-----------D---YLvpsRVhpgkfyalpqSPQLFKQLLMVSGFD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 249 KVFEINRNFRNEgvSTRHN--PEFTMLEFYQAYADYEDNMDLTEELFRELAQLVLGTtDVPygdkvfhfgEPFVRLSVFD 326
Cdd:COG0173 212 RYFQIARCFRDE--DLRADrqPEFTQLDIEMSFVDQEDVFELMEGLIRHLFKEVLGV-ELP---------TPFPRMTYAE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 327 SILKY---NPDL-------------------------------------TAADL--QDVDKARAIAKKAGAKVLGF---- 360
Cdd:COG0173 280 AMERYgsdKPDLrfglelvdvtdifkdsgfkvfagaaenggrvkainvpGGASLsrKQIDELTEFAKQYGAKGLAYikvn 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 361 -------------------------------------------EGLGKLQVMIFEEL---VEHKLEqPHFITQYP-FEVS 393
Cdd:COG0173 360 edglkspiakflseeelaailerlgakpgdliffvadkpkvvnKALGALRLKLGKELgliDEDEFA-FLWVVDFPlFEYD 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 394 PLARR------------------NDENPsvtdrfelfigGREIANAY------SEL-------NDAEDQAERFQAqvadk 442
Cdd:COG0173 439 EEEGRwvamhhpftmpkdedldlLETDP-----------GKVRAKAYdlvlngYELgggsiriHDPELQEKVFEL----- 502
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 492049176 443 dAG--DDEAmhyDADF---VRALEYGMPPTAGEGIGIDRLVMLLTDSPSIRDVILFP 494
Cdd:COG0173 503 -LGisEEEA---EEKFgflLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
9-494 |
1.80e-25 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 109.41 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 9 QALQQEENTLIALRKEKLAAGRAKGQAFPNDFRRDSY----CNDLQKQY-------VDKTKEELAEAAipVKVAGRIMLN 77
Cdd:PLN02850 16 KAAKKAAAKAEKLRREATAKAAAASLEDEDDPLASNYgdvpLEELQSKVtgrewtdVSDLGEELAGSE--VLIRGRVHTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 78 RG----SFMVIQDMTGRIQ--VYVNRKTLPEETLAEVKTWDLGDIIAAEGTLA------RSGKGDLYVEMTTVRLLTKSL 145
Cdd:PLN02850 94 RGkgksAFLVLRQSGFTVQcvVFVSEVTVSKGMVKYAKQLSRESVVDVEGVVSvpkkpvKGTTQQVEIQVRKIYCVSKAL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 146 RPLP-----------DKHHGLTDTEQ--------RYRQRYVDLIV--NEDVretFRVRSQVIAHIRSFLMKRDFLEVETP 204
Cdd:PLN02850 174 ATLPfnvedaarsesEIEKALQTGEQlvrvgqdtRLNNRVLDLRTpaNQAI---FRIQSQVCNLFREFLLSKGFVEIHTP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 205 ML--QTIPGGAAAkpFETHHNAldMEMFLRIAPELYLKRLVVGGFEKVFEINRNFRNEGVST-RHNPEFTMLEFYQAYAD 281
Cdd:PLN02850 251 KLiaGASEGGSAV--FRLDYKG--QPACLAQSPQLHKQMAICGDFRRVFEIGPVFRAEDSFThRHLCEFTGLDLEMEIKE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 282 -YEDNMDLTEELF------------RELAQLvlgttdvpygDKVFHFgEPfvrlsvfdsiLKYNPD---LTAADlqdvdk 345
Cdd:PLN02850 327 hYSEVLDVVDELFvaifdglnerckKELEAI----------REQYPF-EP----------LKYLPKtlrLTFAE------ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 346 ARAIAKKAGAKVLGFEGLGKLQVMIFEELVEHKLEQPHFI-TQYPFEVSPLARRND-ENPSVTDRFELFIGGREIANAYS 423
Cdd:PLN02850 380 GIQMLKEAGVEVDPLGDLNTESERKLGQLVKEKYGTDFYIlHRYPLAVRPFYTMPCpDDPKYSNSFDVFIRGEEIISGAQ 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492049176 424 ELNDAEDQAERFQAQVADKDAGddeamhydADFVRALEYGMPPTAGEGIGIDRLVMLLTDSPSIRDVILFP 494
Cdd:PLN02850 460 RVHDPELLEKRAEECGIDVKTI--------STYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFP 522
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
170-494 |
8.86e-25 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 104.72 E-value: 8.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 170 IVNEDVRETFRVRSQVIAHIRSFLMKRDFLEVETPMLQTI-----PGGAAAKPFETHHNALDMEMFLRIAPELYlKRLVV 244
Cdd:PRK06462 21 ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIISPStdplmGLGSDLPVKQISIDFYGVEYYLADSMILH-KQLAL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 245 GGFEKVFEINRNFRNEGV---STRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQLVLGTTD---VPYGDKVFHFGEP 318
Cdd:PRK06462 100 RMLGKIFYLSPNFRLEPVdkdTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHEdelEFFGRDLPHLKRP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 319 FVRLsvfdsilkynpdltaadlqDVDKARAIAKKAGAKVLGFEGLGKlqvmIFEELVEHKLEQPHFITQYPFEVSPLARR 398
Cdd:PRK06462 180 FKRI-------------------THKEAVEILNEEGCRGIDLEELGS----EGEKSLSEHFEEPFWIIDIPKGSREFYDR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 399 ND-ENPSVTDRFELF--------IGGREianayselndAEDQAERFQAQVadKDAGDDEAmHYDaDFVRALEYGMPPTAG 469
Cdd:PRK06462 237 EDpERPGVLRNYDLLlpegygeaVSGGE----------REYEYEEIVERI--REHGVDPE-KYK-WYLEMAKEGPLPSAG 302
|
330 340
....*....|....*....|....*
gi 492049176 470 EGIGIDRLVMLLTDSPSIRDVILFP 494
Cdd:PRK06462 303 FGIGVERLTRYICGLRHIREVQPFP 327
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
41-494 |
3.08e-23 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 103.33 E-value: 3.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 41 RRDSYCNDLQKQYVDKTkeelaeaaipVKVAGRIMLNRG----SFMVIQDMTGRIQVYVNRKTLPE--ETLAEVKtwdLG 114
Cdd:PLN02903 58 SRSHLCGALSVNDVGSR----------VTLCGWVDLHRDmgglTFLDVRDHTGIVQVVTLPDEFPEahRTANRLR---NE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 115 DIIAAEGTL-ARSGK--------GDLYVEMTTVRLLTKSLRPLP------DKHHGLTDTEQRYRQRYVDLIVNEDVReTF 179
Cdd:PLN02903 125 YVVAVEGTVrSRPQEspnkkmktGSVEVVAESVDILNVVTKSLPflvttaDEQKDSIKEEVRLRYRVLDLRRPQMNA-NL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 180 RVRSQVIAHIRSFLMKR-DFLEVETPML-QTIPGGAaakpfethhnaLDMEMFLRI----------APELYLKRLVVGGF 247
Cdd:PLN02903 204 RLRHRVVKLIRRYLEDVhGFVEIETPILsRSTPEGA-----------RDYLVPSRVqpgtfyalpqSPQLFKQMLMVSGF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 248 EKVFEINRNFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQLVLGtTDVPygdkvfhfgEPFVRLSVFDS 327
Cdd:PLN02903 273 DRYYQIARCFRDEDLRADRQPEFTQLDMELAFTPLEDMLKLNEDLIRQVFKEIKG-VQLP---------NPFPRLTYAEA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 328 ILKYNPD-------LTAADLQDV-------------------------DKARAI-------------AKKAGAKVLGF-- 360
Cdd:PLN02903 343 MSKYGSDkpdlrygLELVDVSDVfaessfkvfagalesggvvkaicvpDGKKISnntalkkgdiyneAIKSGAKGLAFlk 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 361 -------EG----LGKLQVMIFEELVEHKLEQPHFITQypFEVSPLARRNdenpSVTDRFELFIG---GREIANAYS--- 423
Cdd:PLN02903 423 vlddgelEGikalVESLSPEQAEQLLAACGAGPGDLIL--FAAGPTSSVN----KTLDRLRQFIAktlDLIDPSRHSilw 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 424 -------ELNDAEDQAER----FQAQVADkDAGD---DEAMHYDADF--------------------------------- 456
Cdd:PLN02903 497 vtdfpmfEWNEDEQRLEAlhhpFTAPNPE-DMGDlssARALAYDMVYngveigggslriyrrdvqqkvleaiglspeeae 575
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 492049176 457 ------VRALEYGMPPTAGEGIGIDRLVMLLTDSPSIRDVILFP 494
Cdd:PLN02903 576 skfgylLEALDMGAPPHGGIAYGLDRLVMLLAGAKSIRDVIAFP 619
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
44-494 |
9.92e-23 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 101.22 E-value: 9.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 44 SYCNDLQKQYVDKTKEELAEAAIPVKVAGRIMLNRG--SFMVIQDMTGRIQVYVNRK------------TLPEETLAEVK 109
Cdd:PTZ00401 59 TYKSRTFIPVAVLSKPELVDKTVLIRARVSTTRKKGkmAFMVLRDGSDSVQAMAAVEgdvpkemidfigQIPTESIVDVE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 110 twdlGDIIAAEGTLARSGKGDLYVEMTTVRLLTKSLRPLP----DKHHGLTDT------EQRYRQRYVDLIVNEDvRETF 179
Cdd:PTZ00401 139 ----ATVCKVEQPITSTSHSDIELKVKKIHTVTESLRTLPftleDASRKESDEgakvnfDTRLNSRWMDLRTPAS-GAIF 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 180 RVRSQVIAHIRSFLMKRDFLEVETPMLQTIPGGAAAKPFETHHnaLDMEMFLRIAPELYLKRLVVGGFEKVFEINRNFRN 259
Cdd:PTZ00401 214 RLQSRVCQYFRQFLIDSDFCEIHSPKIINAPSEGGANVFKLEY--FNRFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRS 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 260 EGVST-RHNPEFTMLEFYQAYAD-YEDNMDLTEELFREL-AQLVLGTTDVPYGDKVFHFgEPFVRLSVFDSILKYNPDLT 336
Cdd:PTZ00401 292 ENSNThRHLTEFVGLDVEMRINEhYYEVLDLAESLFNYIfERLATHTKELKAVCQQYPF-EPLVWKLTPERMKELGVGVI 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 337 AADLQDVDKARAIAKKAGAKVLGFEGLGKLQVM--IFEE------------------LVEHKLEQPHFIT-QYPFEVSP- 394
Cdd:PTZ00401 371 SEGVEPTDKYQARVHNMDSRMLRINYMHCIELLntVLEEkmaptddinttnekllgkLVKERYGTDFFISdRFPSSARPf 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 395 --LARRNDENpsVTDRFELFIGGREIANAYSELNDAEDQAERfqAQVADKDAGDDEamhydaDFVRALEYGMPPTAGEGI 472
Cdd:PTZ00401 451 ytMECKDDER--FTNSYDMFIRGEEISSGAQRIHDPDLLLAR--AKMLNVDLTPIK------EYVDSFRLGAWPHGGFGV 520
|
490 500
....*....|....*....|..
gi 492049176 473 GIDRLVMLLTDSPSIRDVILFP 494
Cdd:PTZ00401 521 GLERVVMLYLGLSNVRLASLFP 542
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
81-500 |
1.81e-22 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 101.22 E-value: 1.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 81 FMVIQDMTGRIQVYVNrktlPEETLAEVktWDLGDIIAAEGTLARSGK---------------GDLYVEMTTVRLLTKS- 144
Cdd:PRK12820 38 FIHLRDRNGFIQAVFS----PEAAPADV--YELAASLRAEFCVALQGEvqkrleetenphietGDIEVFVRELSILAASe 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 145 LRPLPDKHHGLT-----------DTEQRYRQRYVDlIVNEDVRETFRVRSQVIAHIRSFLMKRDFLEVETPML-QTIPGG 212
Cdd:PRK12820 112 ALPFAISDKAMTagagsagadavNEDLRLQYRYLD-IRRPAMQDHLAKRHRIIKCARDFLDSRGFLEIETPILtKSTPEG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 213 AAAK--PFETHHNALdmeMFLRIAPELYLKRLVVGGFEKVFEINRNFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTE 290
Cdd:PRK12820 191 ARDYlvPSRIHPKEF---YALPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEFTQLDIEASFIDEEFIFELIE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 291 ELFREL-----AQLVLGTTDVPYGDKV---------FHFGEPFV---------RLSVFDSILK------------YNPDL 335
Cdd:PRK12820 268 ELTARMfaiggIALPRPFPRMPYAEAMdttgsdrpdLRFDLKFAdatdifentRYGIFKQILQrggrikginikgQSEKL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 336 TAADLQDvDKARAIAKKAGAKVLGFEGL--GKLQVMIFEELVEHKLE--------------------------------- 380
Cdd:PRK12820 348 SKNVLQN-EYAKEIAPSFGAKGMTWMRAeaGGLDSNIVQFFSADEKEalkrrfhaedgdviimiadascaivlsalgqlr 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 381 ---------------QPHFITQYP-FEVS----------PLAR--RNDENP-------SVTDR-FELFIGGREIANAYSE 424
Cdd:PRK12820 427 lhladrlglipegvfHPLWITDFPlFEATddggvtsshhPFTApdREDFDPgdieellDLRSRaYDLVVNGEELGGGSIR 506
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492049176 425 LNDAEDQAERFQA-QVADKDAGDDEAMhydadFVRALEYGMPPTAGEGIGIDRLVMLLTDSPSIRDVILFPHMRPQA 500
Cdd:PRK12820 507 INDKDIQLRIFAAlGLSEEDIEDKFGF-----FLRAFDFAAPPHGGIALGLDRVVSMILQTPSIREVIAFPKNRSAA 578
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
181-298 |
2.07e-18 |
|
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: 83.71 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 181 VRSQVIAHIRSFLMKRDFLEVETPMLQTIPGGAAA----KPFETHHNALDMEMFLRIAPELYLKRLVVG----GFEKVFE 252
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAghepKDLLPVGAENEEDLYLRPTLEPGLVRLFVShirkLPLRLAE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 492049176 253 INRNFRNEG--VSTRHNPEFTMLEFYQAYADYEDN------MDLTEELFRELAQ 298
Cdd:cd00768 81 IGPAFRNEGgrRGLRRVREFTQLEGEVFGEDGEEAsefeelIELTEELLRALGI 134
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
49-496 |
1.68e-16 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 81.69 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 49 LQKQYVDKTkeelaeaaipVKVAGRIMLNRGS----FMVIQDMTGRIQVYVnRKTLPEETLAEVKTWDLGDIIAAEGTLA 124
Cdd:PRK03932 10 LKGKYVGQE----------VTVRGWVRTKRDSgkiaFLQLRDGSCFKQLQV-VKDNGEEYFEEIKKLTTGSSVIVTGTVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 125 RS-GKGDLY-VEMTTVRLLTKSLR--PLPDKHHGLtDT--EQRY------RQRYVdlivnedvretFRVRSQVIAHIRSF 192
Cdd:PRK03932 79 ESpRAGQGYeLQATKIEVIGEDPEdyPIQKKRHSI-EFlrEIAHlrprtnKFGAV-----------MRIRNTLAQAIHEF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 193 LMKRDFLEVETPMLQTIPGGAAAKPFETHHNALDM-------EMFLRIAPELYLKRLVVGgFEKVFEINRNFRNEGVST- 264
Cdd:PRK03932 147 FNENGFVWVDTPIITASDCEGAGELFRVTTLDLDFskdffgkEAYLTVSGQLYAEAYAMA-LGKVYTFGPTFRAENSNTr 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 265 RHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQLVL--------------GTTDVpygDKVFHFGE-PFVRLSvfdsil 329
Cdd:PRK03932 226 RHLAEFWMIEPEMAFADLEDNMDLAEEMLKYVVKYVLencpddleflnrrvDKGDI---ERLENFIEsPFPRIT------ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 330 kYnpdltaadlqdvDKARAIAKKAGAKV---------LGFEglgklqvmifEE--LVEHKLEQPHFITQYPFEVSPL-AR 397
Cdd:PRK03932 297 -Y------------TEAIEILQKSGKKFefpvewgddLGSE----------HEryLAEEHFKKPVFVTNYPKDIKAFyMR 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 398 RNDENPSV--TDRF-----ELfIGGREIANAYSELNdaedqaERFQAQVADKDagddeamHYD--ADFVRaleYGMPPTA 468
Cdd:PRK03932 354 LNPDGKTVaaMDLLapgigEI-IGGSQREERLDVLE------ARIKELGLNKE-------DYWwyLDLRR---YGSVPHS 416
|
490 500
....*....|....*....|....*...
gi 492049176 469 GEGIGIDRLVMLLTDSPSIRDVILFPHM 496
Cdd:PRK03932 417 GFGLGFERLVAYITGLDNIRDVIPFPRT 444
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
68-141 |
4.23e-11 |
|
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: 58.79 E-value: 4.23e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492049176 68 VKVAGRIMLNRGS-----FMVIQDMTGRIQVYVNrktlPEETLAEVKTWDLGDIIAAEGTLARSGKGDLYVEMTTVRLL 141
Cdd:pfam01336 1 VTVAGRVTSIRRSggkllFLTLRDGTGSIQVVVF----KEEAEKLAKKLKEGDVVRVTGKVKKRKGGELELVVEEIELL 75
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
228-494 |
1.68e-10 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 63.50 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 228 EMFLRIAPELYLKRLVvGGFEKVFEINRNFRNEGVST-RHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQLVLGTT-- 304
Cdd:PTZ00425 325 QAFLTVSGQLSLENLC-SSMGDVYTFGPTFRAENSHTsRHLAEFWMIEPEIAFADLYDNMELAESYIKYCIGYVLNNNfd 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 305 DVPYGDKVFHFG----------EPFVRLS---VFDSILKYN-----PDLTAADLQDvDKARAIAKKagakvlgfeglgkl 366
Cdd:PTZ00425 404 DIYYFEENVETGlisrlknildEDFAKITytnVIDLLQPYSdsfevPVKWGMDLQS-EHERFVAEQ-------------- 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 367 qvmIFEelvehkleQPHFITQYPFEVSPL-ARRNDENPSVT------DRFELFIGGREianayselndAEDQAERFQAQV 439
Cdd:PTZ00425 469 ---IFK--------KPVIVYNYPKDLKAFyMKLNEDQKTVAamdvlvPKIGEVIGGSQ----------REDNLERLDKMI 527
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 492049176 440 ADKDAGDDEAMHYdadfvRAL-EYGMPPTAGEGIGIDRLVMLLTDSPSIRDVILFP 494
Cdd:PTZ00425 528 KEKKLNMESYWWY-----RQLrKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFP 578
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
250-494 |
5.04e-07 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 52.28 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 250 VFEINRNFRNEGVST-RHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQLVLGTT--DVPYGDKVFHFG---------- 316
Cdd:PLN02603 324 VYTFGPTFRAENSNTsRHLAEFWMIEPELAFADLNDDMACATAYLQYVVKYILENCkeDMEFFNTWIEKGiidrlsdvve 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 317 EPFVRLSVFDSI---LKYN-----PDLTAADLQDvDKARAIAKKAgakvlgFEGlgklqvmifeelvehkleQPHFITQY 388
Cdd:PLN02603 404 KNFVQLSYTDAIellLKAKkkfefPVKWGLDLQS-EHERYITEEA------FGG------------------RPVIIRDY 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 389 PFEVSPL-ARRNDENPSVT------DRFELFIGGREianayselndAEDQAERFQAQVaDKDAGDDEAMHYDADFVRale 461
Cdd:PLN02603 459 PKEIKAFyMRENDDGKTVAamdmlvPRVGELIGGSQ----------REERLEYLEARL-DELKLNKESYWWYLDLRR--- 524
|
250 260 270
....*....|....*....|....*....|...
gi 492049176 462 YGMPPTAGEGIGIDRLVMLLTDSPSIRDVILFP 494
Cdd:PLN02603 525 YGSVPHAGFGLGFERLVQFATGIDNIRDAIPFP 557
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
42-169 |
3.95e-06 |
|
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: 46.36 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 42 RDSYCNDLQKQYVDKTkeelaeaaipVKVAGRIMLNRG----SFMVIQDMTGRIQVYVNRKTLPEETLAEvktwDLG--D 115
Cdd:cd04317 1 RTHYCGELRESHVGQE----------VTLCGWVQRRRDhgglIFIDLRDRYGIVQVVFDPEEAPEFELAE----KLRneS 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492049176 116 IIAAEGT-LARSGK--------GDLYVEMTTVRLLTKSlRPLP----DKHHGLTDTEQRYrqRYVDL 169
Cdd:cd04317 67 VIQVTGKvRARPEGtvnpklptGEIEVVASELEVLNKA-KTLPfeidDDVNVSEELRLKY--RYLDL 130
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
68-150 |
1.23e-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: 44.23 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 68 VKVAGRIM----LNRGSFMVIQDMTGRIQVYVNRKTLPEETLAEVKTWDLGDIIAAEGTLARSGKGDLYVEM--TTVRLL 141
Cdd:cd04316 15 VTVAGWVHeirdLGGIKFVILRDREGIVQVTAPKKKVDKELFKTVRKLSRESVISVTGTVKAEPKAPNGVEIipEEIEVL 94
|
....*....
gi 492049176 142 TKSLRPLPD 150
Cdd:cd04316 95 SEAKTPLPL 103
|
|
| pylS |
PRK09537 |
pyrrolysine--tRNA(Pyl) ligase; |
189-277 |
6.07e-05 |
|
pyrrolysine--tRNA(Pyl) ligase;
Pssm-ID: 236555 [Multi-domain] Cd Length: 417 Bit Score: 45.22 E-value: 6.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049176 189 IRSFLMKRDFLEVETPMLqtIPGGAAAK---PFETHHNA----LDMEMFLR--IAPELY--LKRL--VVGGFEKVFEINR 255
Cdd:PRK09537 213 ITKFFVDRGFLEIKSPIL--IPAEYIERmgiDNDTELSKqifrVDKNFCLRpmLAPGLYnyLRKLdrILPDPIKIFEIGP 290
|
90 100
....*....|....*....|..
gi 492049176 256 NFRNEGVSTRHNPEFTMLEFYQ 277
Cdd:PRK09537 291 CYRKESDGKEHLEEFTMVNFCQ 312
|
|
| |
