|
Name |
Accession |
Description |
Interval |
E-value |
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
12-503 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 956.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 12 QELSELLQIRRNKLDELRKLGIDPFGGKYEREHHAGDILKQYDELSKEELEEKQVEVNLAGRIMAKRGMGKASFAHIQDL 91
Cdd:PRK00484 1 EELNEQIAVRREKLAELREQGIDPYPNKFERTHTAAELRAKYDDKEKEELEELEIEVSVAGRVMLKRVMGKASFATLQDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 92 SGRIQIYVRQDSIAEAQYEAFSILDLGDIIGVKGVLFKTKTGETTIKVKELEVLSKSLYPLPEKFHGLKDVELRYRQRYV 171
Cdd:PRK00484 81 SGRIQLYVSKDDVGEEALEAFKKLDLGDIIGVEGTLFKTKTGELSVKATELTLLTKSLRPLPDKFHGLTDVETRYRQRYV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 172 DLIINPDVQKTFIARSRIIQSMRRYLDSQGYLEVETPTLHSIAGGAAARPFITHHNALDMELYMRIAIELHLKRLIVGGL 251
Cdd:PRK00484 161 DLIVNPESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARPFITHHNALDIDLYLRIAPELYLKRLIVGGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 252 EKVYEIGRVYRNEGISTRHNPEFTMIELYEAYADYKDIMALTENMIAHIAQEVLGTQVISYQGHEVDLTPQWRRVSMVDA 331
Cdd:PRK00484 241 ERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTYQGTEIDFGPPFKRLTMVDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 332 VKEVVGVDFSvEMSNEEAHRLAKEHKVPVEPHMTFGHILNAFFEQFVEETLIQPTFITGHPVEISPLAKKNDVDPRFTDR 411
Cdd:PRK00484 321 IKEYTGVDFD-DMTDEEARALAKELGIEVEKSWGLGKLINELFEEFVEPKLIQPTFITDYPVEISPLAKRHREDPGLTER 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 412 FELFIVAREHANAFSELNDPIDQRQRFEAQMKEKEQGNDEAHEMDEDFLRALEYGMPPTGGLGIGIDRLIMLLTNSPSIR 491
Cdd:PRK00484 400 FELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIR 479
|
490
....*....|..
gi 1288434964 492 DVLLFPHMRNKE 503
Cdd:PRK00484 480 DVILFPLMRPEK 491
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
9-503 |
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: 952.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 9 EQEQELSELLQIRRNKLDELRKLGIDPFGGKYEREHHAGDILKQYDELSKEELEekQVEVNLAGRIMAKRGMGKASFAHI 88
Cdd:COG1190 2 SEEEDLNEQIRVRREKLEELREAGIDPYPNKFPRTHTAAEIREKYDELEAEEET--GDEVSVAGRIMAKRDMGKASFADL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 89 QDLSGRIQIYVRQDSIAEAQYEAFSILDLGDIIGVKGVLFKTKTGETTIKVKELEVLSKSLYPLPEKFHGLKDVELRYRQ 168
Cdd:COG1190 80 QDGSGRIQLYLRRDELGEEAYELFKLLDLGDIVGVEGTVFRTKTGELSVKVEELTLLSKSLRPLPEKFHGLTDPETRYRQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 169 RYVDLIINPDVQKTFIARSRIIQSMRRYLDSQGYLEVETPTLHSIAGGAAARPFITHHNALDMELYMRIAIELHLKRLIV 248
Cdd:COG1190 160 RYVDLIVNPEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 249 GGLEKVYEIGRVYRNEGISTRHNPEFTMIELYEAYADYKDIMALTENMIAHIAQEVLGTQVISYQGHEVDLTPQWRRVSM 328
Cdd:COG1190 240 GGFERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGTTKVTYQGQEIDLSPPWRRITM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 329 VDAVKEVVGVDFSVEMSNEEAHRLAKEHKVPVEPHMTFGHILNAFFEQFVEETLIQPTFITGHPVEISPLAKKNDVDPRF 408
Cdd:COG1190 320 VEAIKEATGIDVTPLTDDEELRALAKELGIEVDPGWGRGKLIDELFEELVEPKLIQPTFVTDYPVEVSPLAKRHRDDPGL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 409 TDRFELFIVAREHANAFSELNDPIDQRQRFEAQMKEKEQGNDEAHEMDEDFLRALEYGMPPTGGLGIGIDRLIMLLTNSP 488
Cdd:COG1190 400 TERFELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSP 479
|
490
....*....|....*
gi 1288434964 489 SIRDVLLFPHMRNKE 503
Cdd:COG1190 480 SIRDVILFPLMRPEK 494
|
|
| lysS_bact |
TIGR00499 |
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ... |
13-503 |
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: 745.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 13 ELSELLQIRRNKLDELRKLGIDPFGGKYEREHHAGDILKQYDELSKEELEEKQVEVNLAGRIMAKRGMGKASFAHIQDLS 92
Cdd:TIGR00499 1 ELNDQAQQRLEKLNRLRQTGNNPYLHKFERTHSAQEFQEKYADLSNEELKEKELKVSIAGRIKAIRSMGKATFITLQDES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 93 GRIQIYVRQDSIAEAQYEAF-SILDLGDIIGVKGVLFKTKTGETTIKVKELEVLSKSLYPLPEKFHGLKDVELRYRQRYV 171
Cdd:TIGR00499 81 GQIQLYVNKNKLPEDFYEFDeYLLDLGDIIGVTGYPFKTKTGELSVKVTELQILTKCLQPLPDKWHGLTDQETRYRQRYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 172 DLIINPDVQKTFIARSRIIQSMRRYLDSQGYLEVETPTLHSIAGGAAARPFITHHNALDMELYMRIAIELHLKRLIVGGL 251
Cdd:TIGR00499 161 DLIVNPDVRQTFLKRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKPFITHHNALDMDLYLRIAPELYLKRLIVGGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 252 EKVYEIGRVYRNEGISTRHNPEFTMIELYEAYADYKDIMALTENMIAHIAQEVLGTQVISYQGHEVDLTPQWRRVSMVDA 331
Cdd:TIGR00499 241 EKVYEIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTFIINYNDLEIDLKPPWKRITMVDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 332 VKEVVGVDFSVEMSNEEAHRLAKEHKVPV-EPHMTFGHILNAFFEQFVEETLIQPTFITGHPVEISPLAKKNDVDPRFTD 410
Cdd:TIGR00499 321 LEMVTGIDFDILKDDETAKALAKEHGIEVaEDSLTLGHILNKFFEQFLEHTLIQPTFITHYPAEISPLAKRDPSNPEFTE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 411 RFELFIVAREHANAFSELNDPIDQRQRFEAQMKEKEQGNDEAHEMDEDFLRALEYGMPPTGGLGIGIDRLIMLLTNSPSI 490
Cdd:TIGR00499 401 RFELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGIGIDRLVMLLTDAPSI 480
|
490
....*....|...
gi 1288434964 491 RDVLLFPHMRNKE 503
Cdd:TIGR00499 481 RDVLLFPQLRPQK 493
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
15-500 |
0e+00 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 704.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 15 SELLQIRRNKLDELRKLGIDPFGGKYEREHHAGDILKQYDELSKEELEEKqVEVNLAGRIMAKRGMGKASFAHIQDLSGR 94
Cdd:PLN02502 59 TQYRANRLKKVEALRAKGVEPYPYKFDVTHTAPELQEKYGSLENGEELED-VSVSVAGRIMAKRAFGKLAFYDLRDDGGK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 95 IQIYVRQDSIAEAQyEAF----SILDLGDIIGVKGVLFKTKTGETTIKVKELEVLSKSLYPLPEKFHGLKDVELRYRQRY 170
Cdd:PLN02502 138 IQLYADKKRLDLDE-EEFeklhSLVDRGDIVGVTGTPGKTKKGELSIFPTSFEVLTKCLLMLPDKYHGLTDQETRYRQRY 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 171 VDLIINPDVQKTFIARSRIIQSMRRYLDSQGYLEVETPTLHSIAGGAAARPFITHHNALDMELYMRIAIELHLKRLIVGG 250
Cdd:PLN02502 217 LDLIANPEVRDIFRTRAKIISYIRRFLDDRGFLEVETPMLNMIAGGAAARPFVTHHNDLNMDLYLRIATELHLKRLVVGG 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 251 LEKVYEIGRVYRNEGISTRHNPEFTMIELYEAYADYKDIMALTENMIAHIAQEVLGTQVISYQGHEVDLTPQWRRVSMVD 330
Cdd:PLN02502 297 FERVYEIGRQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKELTGSYKIKYHGIEIDFTPPFRRISMIS 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 331 AVKEVVGVDFSVEMSNEEAHRLAKE----HKVPVEPHMTFGHILNAFFEQFVEETLIQPTFITGHPVEISPLAKKNDVDP 406
Cdd:PLN02502 377 LVEEATGIDFPADLKSDEANAYLIAacekFDVKCPPPQTTGRLLNELFEEFLEETLVQPTFVLDHPVEMSPLAKPHRSKP 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 407 RFTDRFELFIVAREHANAFSELNDPIDQRQRFEAQMKEKEQGNDEAHEMDEDFLRALEYGMPPTGGLGIGIDRLIMLLTN 486
Cdd:PLN02502 457 GLTERFELFINGRELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRLVMLLTD 536
|
490
....*....|....
gi 1288434964 487 SPSIRDVLLFPHMR 500
Cdd:PLN02502 537 SASIRDVIAFPAMK 550
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
176-500 |
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: 584.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 176 NPDVQKTFIARSRIIQSMRRYLDSQGYLEVETPTLHSIAGGAAARPFITHHNALDMELYMRIAIELHLKRLIVGGLEKVY 255
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 256 EIGRVYRNEGISTRHNPEFTMIELYEAYADYKDIMALTENMIAHIAQEVLGTQVISYQGHEVDLTPQWRRVSMVDAVKEV 335
Cdd:cd00775 81 EIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIEYGGKELDFTPPFKRVTMVDALKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 336 VGVDF---SVEMSNEEAHRLAKEHKVPVEPHMTFGHILNAFFEQFVEETLIQPTFITGHPVEISPLAKKNDVDPRFTDRF 412
Cdd:cd00775 161 TGIDFpelDLEQPEELAKLLAKLIKEKIEKPRTLGKLLDKLFEEFVEPTLIQPTFIIDHPVEISPLAKRHRSNPGLTERF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 413 ELFIVAREHANAFSELNDPIDQRQRFEAQMKEKEQGNDEAHEMDEDFLRALEYGMPPTGGLGIGIDRLIMLLTNSPSIRD 492
Cdd:cd00775 241 ELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLTDSNSIRD 320
|
....*...
gi 1288434964 493 VLLFPHMR 500
Cdd:cd00775 321 VILFPAMR 328
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
11-497 |
1.65e-178 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 530.31 E-value: 1.65e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 11 EQELSELLQIRRNKLDELRKLGIDPFGGKYEREHHAGDILkqydelskeeLEEKQVEVNLAGRIMAKRGMGKASFAHIQD 90
Cdd:PRK02983 607 EPRLPEQVRVRLAKLEALRAAGVDPYPVGVPPTHTVAEAL----------DAPTGEEVSVSGRVLRIRDYGGVLFADLRD 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 91 LSGRIQIYVRQDSIAEAQYEAF-SILDLGDIIGVKGVLFKTKTGETTIKVKELEVLSKSLYPLPEKFHGLKDVELRYRQR 169
Cdd:PRK02983 677 WSGELQVLLDASRLEQGSLADFrAAVDLGDLVEVTGTMGTSRNGTLSLLVTSWRLAGKCLRPLPDKWKGLTDPEARVRQR 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 170 YVDLIINPDVQKTFIARSRIIQSMRRYLDSQGYLEVETPTLHSIAGGAAARPFITHHNALDMELYMRIAIELHLKRLIVG 249
Cdd:PRK02983 757 YLDLAVNPEARDLLRARSAVVRAVRETLVARGFLEVETPILQQVHGGANARPFVTHINAYDMDLYLRIAPELYLKRLCVG 836
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 250 GLEKVYEIGRVYRNEGISTRHNPEFTMIELYEAYADYKDIMALTENMIAHIAQEVLGTQVI-----SYQGHEVDLTPQWR 324
Cdd:PRK02983 837 GVERVFELGRNFRNEGVDATHNPEFTLLEAYQAHADYDTMRDLTRELIQNAAQAAHGAPVVmrpdgDGVLEPVDISGPWP 916
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 325 RVSMVDAVKEVVGVDFSVEMSNEEAHRLAKEHKVPVEPHMTFGHILNAFFEQFVEETLIQPTFITGHPVEISPLAKKNDV 404
Cdd:PRK02983 917 VVTVHDAVSEALGEEIDPDTPLAELRKLCDAAGIPYRTDWDAGAVVLELYEHLVEDRTTFPTFYTDFPTSVSPLTRPHRS 996
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 405 DPRFTDRFELFIVAREHANAFSELNDPIDQRQRFEAQMKEKEQGNDEAHEMDEDFLRALEYGMPPTGGLGIGIDRLIMLL 484
Cdd:PRK02983 997 DPGLAERWDLVAWGVELGTAYSELTDPVEQRRRLTEQSLLAAGGDPEAMELDEDFLQALEYAMPPTGGLGMGVDRLVMLL 1076
|
490
....*....|...
gi 1288434964 485 TNSpSIRDVLLFP 497
Cdd:PRK02983 1077 TGR-SIRETLPFP 1088
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
3-500 |
4.00e-175 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 502.28 E-value: 4.00e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 3 EEMNNQEQEQELSELLQIRRNKLDELRKLGIdPFGGKYEREHHAGDILKQYDELSKEELEEKQVEVNLAGRIMAKRGMGK 82
Cdd:PRK12445 4 QETRGANEAIDFNDELRNRREKLAALRQQGV-AFPNDFRRDHTSDQLHEEFDAKDNQELESLNIEVSVAGRMMTRRIMGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 83 ASFAHIQDLSGRIQIYVRQDSIAEAQY-EAFSILDLGDIIGVKGVLFKTKTGETTIKVKELEVLSKSLYPLPEKFHGLKD 161
Cdd:PRK12445 83 ASFVTLQDVGGRIQLYVARDSLPEGVYnDQFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFHGLQD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 162 VELRYRQRYVDLIINPDVQKTFIARSRIIQSMRRYLDSQGYLEVETPTLHSIAGGAAARPFITHHNALDMELYMRIAIEL 241
Cdd:PRK12445 163 QEVRYRQRYLDLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPEL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 242 HLKRLIVGGLEKVYEIGRVYRNEGISTRHNPEFTMIELYEAYADYKDIMALTENMIAHIAQEVLGTQVISYQGHEVDLTP 321
Cdd:PRK12445 243 YLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFDFGK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 322 QWRRVSMVDAVKEVVGVDFSVEMSNEEAHR-LAKEHKVPVEPHMTFGHILNAFFEQFVEETLIQPTFITGHPVEISPLAK 400
Cdd:PRK12445 323 PFEKLTMREAIKKYRPETDMADLDNFDAAKaLAESIGITVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLAR 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 401 KNDVDPRFTDRFELFIVAREHANAFSELNDPIDQRQRFEAQMKEKEQGNDEAHEMDEDFLRALEYGMPPTGGLGIGIDRL 480
Cdd:PRK12445 403 RNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRM 482
|
490 500
....*....|....*....|
gi 1288434964 481 IMLLTNSPSIRDVLLFPHMR 500
Cdd:PRK12445 483 IMLFTNSHTIRDVILFPAMR 502
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
8-500 |
8.04e-142 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 420.19 E-value: 8.04e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 8 QEQEQELSELL--QIRRNKLDELRKLGIDPFGGKYEREHHAGDILKQYDELSKEELEEKQVeVNLAGRIMAKRGMG-KAS 84
Cdd:PTZ00417 74 KEEEAEVDPRLyyENRSKFIQEQKAKGINPYPHKFERTITVPEFVEKYQDLASGEHLEDTI-LNVTGRIMRVSASGqKLR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 85 FAHIQDLSGRIQI---YVRQDSIAEAQYEAFSILDLGDIIGVKGVLFKTKTGETTIKVKELEVLSKSLYPLPEKFhGLKD 161
Cdd:PTZ00417 153 FFDLVGDGAKIQVlanFAFHDHTKSNFAECYDKIRRGDIVGIVGFPGKSKKGELSIFPKETIILSPCLHMLPMKY-GLKD 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 162 VELRYRQRYVDLIINPDVQKTFIARSRIIQSMRRYLDSQGYLEVETPTLHSIAGGAAARPFITHHNALDMELYMRIAIEL 241
Cdd:PTZ00417 232 TEIRYRQRYLDLMINESTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLVAGGANARPFITHHNDLDLDLYLRIATEL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 242 HLKRLIVGGLEKVYEIGRVYRNEGISTRHNPEFTMIELYEAYADYKDIMALTENMIAHIAQEVLGTQVISY-------QG 314
Cdd:PTZ00417 312 PLKMLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHLFGTYKILYnkdgpekDP 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 315 HEVDLTPQWRRVSMVDAVKEVVGVDFSVEM-SNEEAHR---LAKEHKVPVEPHMTFGHILNAFFEQFVEETLI-QPTFIT 389
Cdd:PTZ00417 392 IEIDFTPPYPKVSIVEELEKLTNTKLEQPFdSPETINKminLIKENKIEMPNPPTAAKLLDQLASHFIENKYPnKPFFII 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 390 GHPVEISPLAKKNDVDPRFTDRFELFIVAREHANAFSELNDPIDQRQRFEAQMKEKEQGNDEAHEMDEDFLRALEYGMPP 469
Cdd:PTZ00417 472 EHPQIMSPLAKYHRSKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCTSLEYGLPP 551
|
490 500 510
....*....|....*....|....*....|.
gi 1288434964 470 TGGLGIGIDRLIMLLTNSPSIRDVLLFPHMR 500
Cdd:PTZ00417 552 TGGLGLGIDRITMFLTNKNCIKDVILFPTMR 582
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
161-500 |
9.66e-127 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 371.90 E-value: 9.66e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 161 DVELRYRQRYVDLIiNPDVQKTFIARSRIIQSMRRYLDSQGYLEVETPTLHSIAGGAAARPFITHHNALDMELYMRIAIE 240
Cdd:pfam00152 1 DEETRLKYRYLDLR-RPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 241 LHLKRLIVGGLEKVYEIGRVYRNEGISTRHNPEFTMIELYEAYADYKDIMALTENMIAHIAQEVLGTQVISYQGHEVDLT 320
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 321 PQWRRVSMVDAVKEVVGVDFSvemsneeahrlaKEHKVPVEPHMTFGhilnafFEQFVEETLIQPTFITGHPVEISPLAK 400
Cdd:pfam00152 160 KPFPRITYAEAIEKLNGKDVE------------ELGYGSDKPDLRFL------LELVIDKNKFNPLWVTDFPAEHHPFTM 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 401 KNDVD-PRFTDRFELFIVAREHANAFSELNDPIDQRQRFEAQMKEKEqgndEAHEMDEDFLRALEYGMPPTGGLGIGIDR 479
Cdd:pfam00152 222 PKDEDdPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDPE----EAEEKFGFYLDALKYGAPPHGGLGIGLDR 297
|
330 340
....*....|....*....|.
gi 1288434964 480 LIMLLTNSPSIRDVLLFPHMR 500
Cdd:pfam00152 298 LVMLLTGLESIREVIAFPKTR 318
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
65-500 |
1.07e-126 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 384.00 E-value: 1.07e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 65 QVEVNLAGRIMAKRGMGKASFAHIQDLSGRIQI--YVRQDSIAEAQYEAFSILDLGDIIGVKGVLFKTKTGETTIKVKEL 142
Cdd:PTZ00385 107 QATVRVAGRVTSVRDIGKIIFVTIRSNGNELQVvgQVGEHFTREDLKKLKVSLRVGDIIGADGVPCRMQRGELSVAASRM 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 143 EVLS------KSLYPLPEKFHGLKDVELRYRQRYVDLIINPDVQKTFIARSRIIQSMRRYLDSQGYLEVETPTLHSIAGG 216
Cdd:PTZ00385 187 LILSpyvctdQVVCPNLRGFTVLQDNDVKYRYRFTDMMTNPCVIETIKKRHVMLQALRDYFNERNFVEVETPVLHTVASG 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 217 AAARPFITHHNALDMELYMRIAIELHLKRLIVGGLEKVYEIGRVYRNEGISTRHNPEFTMIELYEAYADYKDIMALTENM 296
Cdd:PTZ00385 267 ANAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTSCEFYAAYHTYEDLMPMTEDI 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 297 IAHIAQEVLGTQVISYQGH-------EVDLTPQWRRVSMVDAVKEVVGVDFSVEMSNEEAHRLAK------EHKVPVEPH 363
Cdd:PTZ00385 347 FRQLAMRVNGTTVVQIYPEnahgnpvTVDLGKPFRRVSVYDEIQRMSGVEFPPPNELNTPKGIAYmsvvmlRYNIPLPPV 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 364 MTFGHILNAFFEQFVEETLIQPTFITGHPVEISPLAKKNDVDPRFTDRFELFIVAREHANAFSELNDPIDQRQRFEAQMK 443
Cdd:PTZ00385 427 RTAAKMFEKLIDFFITDRVVEPTFVMDHPLFMSPLAKEQVSRPGLAERFELFVNGIEYCNAYSELNDPHEQYHRFQQQLV 506
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1288434964 444 EKEQGNDEAHEMDEDFLRALEYGMPPTGGLGIGIDRLIMLLTNSPSIRDVLLFPHMR 500
Cdd:PTZ00385 507 DRQGGDEEAMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFPLLR 563
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
183-500 |
1.48e-100 |
|
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: 303.24 E-value: 1.48e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 183 FIARSRIIQSMRRYLDSQGYLEVETPTLHSIAGGAAARPFITHHNALDMELYMRIAIELHLKRLIVGGLEKVYEIGRVYR 262
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 263 NEGISTRHNPEFTMIELYEAYADYKDIMALTENMIAHIAQEVLGTQVISYQGHEVDLTPQWRRVSMVDAvkevvgvdfsv 342
Cdd:cd00669 81 NEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYGFELEDFGLPFPRLTYREA----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 343 emsneeahrlakehkvpvephmtfghilnaffeqfvEETLIQPTFITGHPVEI-SPLAKKNDVDPRFTDRFELFIVAREH 421
Cdd:cd00669 150 ------------------------------------LERYGQPLFLTDYPAEMhSPLASPHDVNPEIADAFDLFINGVEV 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1288434964 422 ANAFSELNDPIDQRQRFEAQMKEKEQGndeaHEMDEDFLRALEYGMPPTGGLGIGIDRLIMLLTNSPSIRDVLLFPHMR 500
Cdd:cd00669 194 GNGSSRLHDPDIQAEVFQEQGINKEAG----MEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKMR 268
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
185-494 |
2.43e-82 |
|
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: 257.73 E-value: 2.43e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 185 ARSRIIQSMRRYLDSQGYLEVETPTLhSIAGGAAA--RPFIT---HHNALDMELYMRIAIELHLKRLIVGGLEKVYEIGR 259
Cdd:COG2269 8 ARARLLAAIRAFFAERGVLEVETPAL-SVAPGTDPhlDSFATefiGPDGGGRPLYLHTSPEFAMKRLLAAGSGPIYQIAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 260 VYRNEGISTRHNPEFTMIELYEAYADYKDIMALTENMIAHIAQEVLgtqvisyqghevdlTPQWRRVSMVDAVKEVVGVD 339
Cdd:COG2269 87 VFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAAG--------------FAPAERLSYQEAFLRYLGID 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 340 -FSVEMsnEEAHRLAKEHKVPVEPHMTFGHILNAFFEQFVEETLIQ--PTFITGHPVEISPLAKKNDVDPRFTDRFELFI 416
Cdd:COG2269 153 pLTADL--DELAAAAAAAGLRVADDDDRDDLLDLLLSERVEPQLGRdrPTFLYDYPASQAALARISPDDPRVAERFELYA 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1288434964 417 VAREHANAFSELNDPIDQRQRFEAQMKEKEQGNDEAHEMDEDFLRALEYGMPPTGGLGIGIDRLIMLLTNSPSIRDVL 494
Cdd:COG2269 231 CGVELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALGAERIDDVL 308
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
200-494 |
2.75e-73 |
|
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: 233.60 E-value: 2.75e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 200 QGYLEVETPTLhSIAGGAAA--RPFITH---HNALDMELYMRIAIELHLKRLIVGGLEKVYEIGRVYRNEGISTRHNPEF 274
Cdd:TIGR00462 5 RGVLEVETPLL-SPAPVTDPhlDAFATEfvgPDGQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRHNPEF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 275 TMIELYEAYADYKDIMALTENMIAHIAQevlgtqvisyqghevDLTPQWRRVSMVDAVKEVVGVD-FSVEMsnEEAHRLA 353
Cdd:TIGR00462 84 TMLEWYRPGFDYHDLMDEVEALLQELLG---------------DPFAPAERLSYQEAFLRYAGIDpLTASL--AELQAAA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 354 KEHKVPVEPHMTFGHILNAFFEQFVEETLIQ--PTFITGHPVEISPLAKKNDVDPRFTDRFELFIVAREHANAFSELNDP 431
Cdd:TIGR00462 147 AAHGIRASEEDDRDDLLDLLFSEKVEPHLGFgrPTFLYDYPASQAALARISPDDPRVAERFELYIKGLELANGFHELTDA 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1288434964 432 IDQRQRFEAQMKEKEQGNDEAHEMDEDFLRALEYGMPPTGGLGIGIDRLIMLLTNSPSIRDVL 494
Cdd:TIGR00462 227 AEQRRRFEADNALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDVL 289
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
67-173 |
8.57e-59 |
|
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These enzymes are homodimeric class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Included in this group are E. coli LysS and LysU. These two isoforms of LysRS are encoded by distinct genes which are differently regulated. Eukaryotes contain 2 sets of aaRSs, both of which encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Saccharomyces cerevisiae cytoplasmic and mitochondrial LysRSs have been shown to participate in the mitochondrial import of the only nuclear-encoded tRNA of S. cerevisiae (tRNAlysCUU). The gene for human LysRS encodes both the cytoplasmic and the mitochondrial isoforms of LysRS. In addition to their housekeeping role, human lysRS may function as a signaling molecule that activates immune cells and tomato LysRS may participate in a root-specific process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging.
Pssm-ID: 239817 [Multi-domain] Cd Length: 108 Bit Score: 189.61 E-value: 8.57e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 67 EVNLAGRIMAKRGMGKASFAHIQDLSGRIQIYVRQDSIAEAQYEAF-SILDLGDIIGVKGVLFKTKTGETTIKVKELEVL 145
Cdd:cd04322 1 EVSVAGRIMSKRGSGKLSFADLQDESGKIQVYVNKDDLGEEEFEDFkKLLDLGDIIGVTGTPFKTKTGELSIFVKEFTLL 80
|
90 100
....*....|....*....|....*...
gi 1288434964 146 SKSLYPLPEKFHGLKDVELRYRQRYVDL 173
Cdd:cd04322 81 SKSLRPLPEKFHGLTDVETRYRQRYLDL 108
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
181-493 |
1.53e-56 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 190.53 E-value: 1.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 181 KTFIARSRIIQSMRRYLDSQGYLEVETPTL-HSIAGGAAARPFITHHNALDME----LYMRIAIELHLKRLIVGGLEKVY 255
Cdd:PRK09350 3 PNLLKRAKIIAEIRRFFADRGVLEVETPILsQATVTDIHLVPFETRFVGPGASqgktLWLMTSPEYHMKRLLAAGSGPIF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 256 EIGRVYRNEGISTRHNPEFTMIELYEAYADYKDIMALTENMIahiaQEVLG---TQVISYQghevdltpqwrrvsmvDAV 332
Cdd:PRK09350 83 QICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLL----QQVLDcepAESLSYQ----------------QAF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 333 KEVVGVDfSVEMSNEEAHRLAKEHkvpvephmtfgHILNAFFEQFVEETLIQ---------------PTFITGHPVEISP 397
Cdd:PRK09350 143 LRYLGID-PLSADKTQLREVAAKL-----------GLSNIADEEEDRDTLLQllftfgvepnigkekPTFVYHFPASQAA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 398 LAKKNDVDPRFTDRFELFIVAREHANAFSELNDPIDQRQRFEAQMKEKEQGNDEAHEMDEDFLRALEYGMPPTGGLGIGI 477
Cdd:PRK09350 211 LAKISTEDHRVAERFEVYFKGIELANGFHELTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCSGVALGV 290
|
330
....*....|....*.
gi 1288434964 478 DRLIMLLTNSPSIRDV 493
Cdd:PRK09350 291 DRLIMLALGAESISEV 306
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
67-501 |
5.86e-51 |
|
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: 179.48 E-value: 5.86e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 67 EVNLAGRIMAKRGMGKASFAHIQDLSGRIQIYVRQDSIAEaqYEAFSILDLGDIIGVKGVLFKTKTGETT--IKVKELEV 144
Cdd:COG0017 16 EVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKLEN--FEEAKKLTTESSVEVTGTVVESPRAPQGveLQAEEIEV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 145 LSKSL--YPLPEKFHGLkdvELRYRQRYVDLIiNPDVQKTFIARSRIIQSMRRYLDSQGYLEVETPTL-HSIAGGAAA-- 219
Cdd:COG0017 94 LGEADepYPLQPKRHSL---EFLLDNRHLRLR-TNRFGAIFRIRSELARAIREFFQERGFVEVHTPIItASATEGGGElf 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 220 ------RP-FITHHNALDMELYMriaielhlkrlivGGLEKVYEIGRVYRNEGIST-RHNPEFTMIELYEAYADYKDIMA 291
Cdd:COG0017 170 pvdyfgKEaYLTQSGQLYKEALA-------------MALEKVYTFGPTFRAEKSNTrRHLAEFWMIEPEMAFADLEDVMD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 292 LTENMIAHIAQEVLgtqviSYQGHEVDLTPQWrrvsmVDAVKEVVGVDFsVEMSNEEAHRLAKEHKVPVE-------PHM 364
Cdd:COG0017 237 LAEEMLKYIIKYVL-----ENCPEELEFLGRD-----VERLEKVPESPF-PRITYTEAIEILKKSGEKVEwgddlgtEHE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 365 TFghILNAFFEQFVeetliqptFITGHPVEISPL-AKKNDVDPRFTDRFELF------IVA---REHanafselndpidQ 434
Cdd:COG0017 306 RY--LGEEFFKKPV--------FVTDYPKEIKAFyMKPNPDDPKTVAAFDLLapgigeIIGgsqREH------------R 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1288434964 435 RQRFEAQMKEkeqgndeaHEMDED----FLRALEYGMPPTGGLGIGIDRLIMLLTNSPSIRDVLLFPHMRN 501
Cdd:COG0017 364 YDVLVERIKE--------KGLDPEdyewYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPG 426
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
67-497 |
1.76e-47 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 170.37 E-value: 1.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 67 EVNLAGRIMAKRGMGKASFAHIQDLSGRIQIYVRQDSIAEAqYEAFSILDLGDIIGVKGVLF---KTKTG-EttIKVKEL 142
Cdd:PRK05159 18 EVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKVDEEL-FETIKKLKRESVVSVTGTVKanpKAPGGvE--VIPEEI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 143 EVLSKSLYPLPEKFHGLKDVEL--RYRQRYVDLIiNPDVQKTFIARSRIIQSMRRYLDSQGYLEVETPTLHSIA--GGAA 218
Cdd:PRK05159 95 EVLNKAEEPLPLDISGKVLAELdtRLDNRFLDLR-RPRVRAIFKIRSEVLRAFREFLYENGFTEIFTPKIVASGteGGAE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 219 ARPfITHhnaLDMELYMRIAIELHlKRLIVG-GLEKVYEIGRVYRNEGIST-RHNPEFTMIELYEAYAD-YKDIMALTEN 295
Cdd:PRK05159 174 LFP-IDY---FEKEAYLAQSPQLY-KQMMVGaGFERVFEIGPVFRAEEHNTsRHLNEYTSIDVEMGFIDdHEDVMDLLEN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 296 MIAHIAQEVLGTqvisyqgHEVDLtpqwrrvsmvdavkEVVGVDFSVEMSN------EEAHRLAKEHKVPVEPHMTFG-- 367
Cdd:PRK05159 249 LLRYMYEDVAEN-------CEKEL--------------ELLGIELPVPETPiprityDEAIEILKSKGNEISWGDDLDte 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 368 --HILNAFFEqfvEETLIQPTFITGHPVEISPL-AKKNDVDPRFTDRFELF-----IVA---REHanafselndpidQRQ 436
Cdd:PRK05159 308 geRLLGEYVK---EEYGSDFYFITDYPSEKRPFyTMPDEDDPEISKSFDLLfrgleITSggqRIH------------RYD 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1288434964 437 RFEAQMKEKeqGNDEahEMDEDFLRALEYGMPPTGGLGIGIDRLIMLLTNSPSIRDVLLFP 497
Cdd:PRK05159 373 MLVESIKEK--GLNP--ESFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFP 429
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
67-502 |
3.92e-40 |
|
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: 149.97 E-value: 3.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 67 EVNLAGRIMAKRGMGKASFAHIQDLSGRIQIYVRQDSIAEAQYEAFSILDLGDIIGVKG-VLFKTKT-GETTIKVKELEV 144
Cdd:TIGR00458 14 EVTFMGWVHEIRDLGGLIFVLLRDREGLIQITAPAKKVSKNLFKWAKKLNLESVVAVRGiVKIKEKApGGFEIIPTKIEV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 145 LSKSLYPLP----EKFHGLKDVELRYRqrYVDLIiNPDVQKTFIARSRIIQSMRRYLDSQGYLEVETPTLHSIA--GGAA 218
Cdd:TIGR00458 94 INEAKEPLPldptEKVPAELDTRLDYR--FLDLR-RPTVQAIFRIRSGVLESVREFLAEEGFIEVHTPKLVASAteGGTE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 219 ARPfITHhnaLDMELYMRIAIELHLKRLIVGGLEKVYEIGRVYRNEGIST-RHNPEFTMIELYEAYADYKDIMALTENMI 297
Cdd:TIGR00458 171 LFP-ITY---FEREAFLGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNThRHLNEATSIDIEMAFEDHHDVMDILEELV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 298 AHIAQEVlgtqvisYQGHEVDLTPQWRRVSMVDAVKEVVGVDFSVEMSNEEAHRLAKEHKVPVEPHMTFGHILNAFFeqf 377
Cdd:TIGR00458 247 VRVFEDV-------PERCAHQLETLEFKLEKPEGKFVRLTYDEAIEMANAKGVEIGWGEDLSTEAEKALGEEMDGLY--- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 378 veetliqptFITGHPVEISPL-AKKNDVDPRFTDRFELFIVAREHANAfselndpiDQRQRFEAQMKEKEQGNDEAHEMD 456
Cdd:TIGR00458 317 ---------FITDWPTEIRPFyTMPDEDNPEISKSFDLMYRDLEISSG--------AQRIHLHDLLVERIKAKGLNPEGF 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1288434964 457 EDFLRALEYGMPPTGGLGIGIDRLIMLLTNSPSIRDVLLFPHMRNK 502
Cdd:TIGR00458 380 KDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFPRDRKR 425
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
183-497 |
4.64e-36 |
|
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: 135.01 E-value: 4.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 183 FIARSRIIQSMRRYLDSQGYLEVETPTL-HSIAGGAaaRPFI----THHN---ALDM--ELYMRIaielhlkrLIVGGLE 252
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILtKSTPEGA--RDFLvpsrLHPGkfyALPQspQLFKQL--------LMVSGFD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 253 KVYEIGRVYRNEGISTRHNPEFTMIELYEAYADYKDIMALTENMIAHIAQEVLGtqvisyqgheVDLTPQWRRVSMVDAV 332
Cdd:cd00777 71 RYFQIARCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG----------VELTTPFPRMTYAEAM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 333 KE-----VVGVDFSVEMSNEEAHRLAKEHkvpvepHMtfghilnafFEQFVEETLiqptfitghpveisPLAKKNDVDPR 407
Cdd:cd00777 141 ERygfkfLWIVDFPLFEWDEEEGRLVSAH------HP---------FTAPKEEDL--------------DLLEKDPEDAR 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 408 fTDRFELFIVAREHANAFSELNDPIDQRQRFEAQMKEKEqgndEAHEMDEDFLRALEYGMPPTGGLGIGIDRLIMLLTNS 487
Cdd:cd00777 192 -AQAYDLVLNGVELGGGSIRIHDPDIQEKVFEILGLSEE----EAEEKFGFLLEAFKYGAPPHGGIALGLDRLVMLLTGS 266
|
330
....*....|
gi 1288434964 488 PSIRDVLLFP 497
Cdd:cd00777 267 ESIRDVIAFP 276
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
67-497 |
5.60e-36 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 140.97 E-value: 5.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 67 EVNLAGRIMAKRGMGKASFAHIQDLSGRIQIYVRQDSiaeaqyEAFSILD-LG--DIIGVKGVLF---------KTKTGE 134
Cdd:PRK00476 19 TVTLCGWVHRRRDHGGLIFIDLRDREGIVQVVFDPDA------EAFEVAEsLRseYVIQVTGTVRarpegtvnpNLPTGE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 135 TTIKVKELEVLSKSLyPLP----EKFHGLKDVELRYRqrYVDLIiNPDVQKTFIARSRIIQSMRRYLDSQGYLEVETPTL 210
Cdd:PRK00476 93 IEVLASELEVLNKSK-TLPfpidDEEDVSEELRLKYR--YLDLR-RPEMQKNLKLRSKVTSAIRNFLDDNGFLEIETPIL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 211 -HSIAGGaaARPFI----THHN---ALDM------ELYMriaielhlkrliVGGLEKVYEIGRVYRNEGISTRHNPEFTM 276
Cdd:PRK00476 169 tKSTPEG--ARDYLvpsrVHPGkfyALPQspqlfkQLLM------------VAGFDRYYQIARCFRDEDLRADRQPEFTQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 277 IELYEAYADYKDIMALTENMIAHIAQEVLGtqvisyqgheVDLTPQWRRVS--------------------MVDAVKEVV 336
Cdd:PRK00476 235 IDIEMSFVTQEDVMALMEGLIRHVFKEVLG----------VDLPTPFPRMTyaeamrrygsdkpdlrfgleLVDVTDLFK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 337 GVDFSV---------------------EMSNEEAHRL---AKEHK------VPVEPHMTFGHILNaFFEQFVEETLIQPT 386
Cdd:PRK00476 305 DSGFKVfagaandggrvkairvpggaaQLSRKQIDELtefAKIYGakglayIKVNEDGLKGPIAK-FLSEEELAALLERT 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 387 ---------FITGHP-----------VEIS-------------------PLAKKNDVDPR-------FT-----DRFELF 415
Cdd:PRK00476 384 gakdgdlifFGADKAkvvndalgalrLKLGkelglidedkfaflwvvdfPMFEYDEEEGRwvaahhpFTmpkdeDLDELE 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 416 IVAREHANAFS--------EL-------NDPIDQRQRFEA-QMKEKEQgndeahemDEDF---LRALEYGMPPTGGLGIG 476
Cdd:PRK00476 464 TTDPGKARAYAydlvlngyELgggsiriHRPEIQEKVFEIlGISEEEA--------EEKFgflLDALKYGAPPHGGIAFG 535
|
570 580
....*....|....*....|.
gi 1288434964 477 IDRLIMLLTNSPSIRDVLLFP 497
Cdd:PRK00476 536 LDRLVMLLAGADSIRDVIAFP 556
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
161-497 |
2.42e-35 |
|
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: 134.23 E-value: 2.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 161 DVELRYR--QRYVDLIiNPDVQKTFIARSRIIQSMRRYLDSQGYLEVETPTLHSIA--GGAAARPFithhNALDMELYMR 236
Cdd:cd00776 1 DANLETLldNRHLDLR-TPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDteGGAELFKV----SYFGKPAYLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 237 IAIELHLKRLIvGGLEKVYEIGRVYRNEGIST-RHNPEFTMIELYEAYA-DYKDIMALTENMIAHIAQEVLgtqviSYQG 314
Cdd:cd00776 76 QSPQLYKEMLI-AALERVYEIGPVFRAEKSNTrRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVL-----ERCA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 315 HEVDLtpqwrrVSMVDAVKEVVGVDFsVEMSNEEAHRLAKEHKVPVEPhmTFGHILNAFFEQFVEETLIQ-PTFITGHPV 393
Cdd:cd00776 150 KELEL------VNQLNRELLKPLEPF-PRITYDEAIELLREKGVEEEV--KWGEDLSTEHERLLGEIVKGdPVFVTDYPK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 394 EISPL-AKKNDVDPRFTDRFELF------IVA---REHanafselnDPIDQRQRFeaqmkeKEQGNDeaHEMDEDFLRAL 463
Cdd:cd00776 221 EIKPFyMKPDDDNPETVESFDLLmpgvgeIVGgsqRIH--------DYDELEERI------KEHGLD--PESFEWYLDLR 284
|
330 340 350
....*....|....*....|....*....|....
gi 1288434964 464 EYGMPPTGGLGIGIDRLIMLLTNSPSIRDVLLFP 497
Cdd:cd00776 285 KYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
67-497 |
8.49e-32 |
|
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: 128.58 E-value: 8.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 67 EVNLAGRIMAKRGMGKASFAHIQDLSGRIQIYVRQDSIAEAqYEAFSILDLGDIIGVKGVLF---------KTKTGETTI 137
Cdd:COG0173 18 EVTLSGWVHRRRDHGGLIFIDLRDRYGITQVVFDPDDSAEA-FEKAEKLRSEYVIAVTGKVRarpegtvnpKLPTGEIEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 138 KVKELEVLSKSLyPLPEKFHGLKDV--ELRYRQRYVDLIiNPDVQKTFIARSRIIQSMRRYLDSQGYLEVETPTLhsiag 215
Cdd:COG0173 97 LASELEILNKAK-TPPFQIDDDTDVseELRLKYRYLDLR-RPEMQKNLILRHKVTKAIRNYLDENGFLEIETPIL----- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 216 GAA----ARPFI----THHN---ALDM--ELYmriaielhlKRLI-VGGLEKVYEIGRVYRNEgiSTRHN--PEFTMIEL 279
Cdd:COG0173 170 TKStpegARDYLvpsrVHPGkfyALPQspQLF---------KQLLmVSGFDRYFQIARCFRDE--DLRADrqPEFTQLDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 280 YEAYADYKDIMALTENMIAHIAQEVLGtqvisyqgheVDLTPQWRRVS--------------------MVDaVKEVV-GV 338
Cdd:COG0173 239 EMSFVDQEDVFELMEGLIRHLFKEVLG----------VELPTPFPRMTyaeamerygsdkpdlrfgleLVD-VTDIFkDS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 339 DFSV--------------------EMSNEEAHRL---AKEHKVP------VEPHMTFGHILNaFFEQFVEETLIQPT--- 386
Cdd:COG0173 308 GFKVfagaaenggrvkainvpggaSLSRKQIDELtefAKQYGAKglayikVNEDGLKSPIAK-FLSEEELAAILERLgak 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 387 ------FITGHP-----------VEispLAKKND-VDP---RF---TDrFELF--------IVAREH------------- 421
Cdd:COG0173 387 pgdlifFVADKPkvvnkalgalrLK---LGKELGlIDEdefAFlwvVD-FPLFeydeeegrWVAMHHpftmpkdedldll 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 422 --------ANAF------SEL-------NDPIDQRQRFEAqmkekeQGNDEAhEMDEDF---LRALEYGMPPTGGLGIGI 477
Cdd:COG0173 463 etdpgkvrAKAYdlvlngYELgggsiriHDPELQEKVFEL------LGISEE-EAEEKFgflLEAFKYGAPPHGGIAFGL 535
|
570 580
....*....|....*....|
gi 1288434964 478 DRLIMLLTNSPSIRDVLLFP 497
Cdd:COG0173 536 DRLVMLLAGEDSIRDVIAFP 555
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
67-501 |
1.46e-27 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 116.62 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 67 EVNLAGRIMAKRGMGKASFAHIQDLSGRIQIYVRQDSIAEAQYEAFSILDLGDIIGVKGVLFK---------TKTGETTI 137
Cdd:PRK12820 20 EVCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFSPEAAPADVYELAASLRAEFCVALQGEVQKrleetenphIETGDIEV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 138 KVKELEVLSKSL---YPLPEKF-----------HGLKDVELRYRqrYVDlIINPDVQKTFIARSRIIQSMRRYLDSQGYL 203
Cdd:PRK12820 100 FVRELSILAASEalpFAISDKAmtagagsagadAVNEDLRLQYR--YLD-IRRPAMQDHLAKRHRIIKCARDFLDSRGFL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 204 EVETPTLhSIAGGAAARPFITHHNALDMELY-MRIAIELHLKRLIVGGLEKVYEIGRVYRNEGISTRHNPEFTMIELYEA 282
Cdd:PRK12820 177 EIETPIL-TKSTPEGARDYLVPSRIHPKEFYaLPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEFTQLDIEAS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 283 YADYKDIMALTENMIAHIAqEVLGTQV------ISYqGHEVDLT----PQWR-RVSMVDAV-----------KEVV---- 336
Cdd:PRK12820 256 FIDEEFIFELIEELTARMF-AIGGIALprpfprMPY-AEAMDTTgsdrPDLRfDLKFADATdifentrygifKQILqrgg 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 337 ---GVDFSVEMSNEEAHRLAKEHKVPVEPH-----MTF---------GHILNAFFEQ----------------------- 376
Cdd:PRK12820 334 rikGINIKGQSEKLSKNVLQNEYAKEIAPSfgakgMTWmraeaggldSNIVQFFSADekealkrrfhaedgdviimiada 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 377 ---------------------FVEETLIQPTFITGHPV----------------------EISPLAKKNDVDPRfTDRFE 413
Cdd:PRK12820 414 scaivlsalgqlrlhladrlgLIPEGVFHPLWITDFPLfeatddggvtsshhpftapdreDFDPGDIEELLDLR-SRAYD 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 414 LFIVAREHANAFSELNDPIDQRQRFEA-QMKEKEQGNDEAHemdedFLRALEYGMPPTGGLGIGIDRLIMLLTNSPSIRD 492
Cdd:PRK12820 493 LVVNGEELGGGSIRINDKDIQLRIFAAlGLSEEDIEDKFGF-----FLRAFDFAAPPHGGIALGLDRVVSMILQTPSIRE 567
|
....*....
gi 1288434964 493 VLLFPHMRN 501
Cdd:PRK12820 568 VIAFPKNRS 576
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
67-497 |
1.42e-26 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 113.73 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 67 EVNLAGRIMAKRGMGKASFAHIQDLSGRIQIYVRQDSIAEAqYEAFSILDLGDIIGVKGVLF---------KTKTGETTI 137
Cdd:PLN02903 74 RVTLCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDEFPEA-HRTANRLRNEYVVAVEGTVRsrpqespnkKMKTGSVEV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 138 KVKELEVLSKSLYPLPEKFHGLKDV------ELRYRQRYVDLiINPDVQKTFIARSRIIQSMRRYL-DSQGYLEVETPTL 210
Cdd:PLN02903 153 VAESVDILNVVTKSLPFLVTTADEQkdsikeEVRLRYRVLDL-RRPQMNANLRLRHRVVKLIRRYLeDVHGFVEIETPIL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 211 -HSIAGGaaARPFITHHNALDMELY-MRIAIELHLKRLIVGGLEKVYEIGRVYRNEGISTRHNPEFTMIELYEAYADYKD 288
Cdd:PLN02903 232 sRSTPEG--ARDYLVPSRVQPGTFYaLPQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEFTQLDMELAFTPLED 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 289 IMALTENMIAHIAQEVLGtqvisyqgheVDLTPQWRRVSMVDA-------------------VKEVV-GVDFSVEMSNEE 348
Cdd:PLN02903 310 MLKLNEDLIRQVFKEIKG----------VQLPNPFPRLTYAEAmskygsdkpdlryglelvdVSDVFaESSFKVFAGALE 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 349 AHRLAKEHKVP---------VEPHmtfGHILN----------AFF-----------------------EQFVEETLIQP- 385
Cdd:PLN02903 380 SGGVVKAICVPdgkkisnntALKK---GDIYNeaiksgakglAFLkvlddgelegikalveslspeqaEQLLAACGAGPg 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 386 ---TFITGHpveisplakkNDVDPRFTDRFELFI-----VAREHANAFSELND-PI----DQRQRFEA------------ 440
Cdd:PLN02903 457 dliLFAAGP----------TSSVNKTLDRLRQFIaktldLIDPSRHSILWVTDfPMfewnEDEQRLEAlhhpftapnped 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 441 ---------------------------------QMKEKEQGNDEAHEMDEDF---LRALEYGMPPTGGLGIGIDRLIMLL 484
Cdd:PLN02903 527 mgdlssaralaydmvyngveigggslriyrrdvQQKVLEAIGLSPEEAESKFgylLEALDMGAPPHGGIAYGLDRLVMLL 606
|
570
....*....|...
gi 1288434964 485 TNSPSIRDVLLFP 497
Cdd:PLN02903 607 AGAKSIRDVIAFP 619
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
67-501 |
4.37e-25 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 107.50 E-value: 4.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 67 EVNLAGRIMAKRGMGKASFAHIQDLSGRIQIYVRQDSiAEAQYEAFSILDLGDIIGVKGVLFKT--KTGETTIKVKELEV 144
Cdd:PRK03932 18 EVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDN-GEEYFEEIKKLTTGSSVIVTGTVVESprAGQGYELQATKIEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 145 LSKSL--YPLPEKFHG---LKDV-ELRYRQRyvdliinpdvqkTFIA----RSRIIQSMRRYLDSQGYLEVETPTLHSIA 214
Cdd:PRK03932 97 IGEDPedYPIQKKRHSiefLREIaHLRPRTN------------KFGAvmriRNTLAQAIHEFFNENGFVWVDTPIITASD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 215 GGAAARPFITHHNALDME---------------LYMRIAIElhlkrlivgGLEKVYEIGRVYRNEGIST-RHNPEFTMIE 278
Cdd:PRK03932 165 CEGAGELFRVTTLDLDFSkdffgkeayltvsgqLYAEAYAM---------ALGKVYTFGPTFRAENSNTrRHLAEFWMIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 279 LYEAYADYKDIMALTENMIAHIAQEVLgtqvisyQGHEVDLTPQWRRVSM--VDAVKEVVGVDFsVEMSNEEAHRLAKEH 356
Cdd:PRK03932 236 PEMAFADLEDNMDLAEEMLKYVVKYVL-------ENCPDDLEFLNRRVDKgdIERLENFIESPF-PRITYTEAIEILQKS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 357 KVPVEPHMTFGHILNAFFEQFVEETLIQ-PTFITGHPVEISPLAKKNDVDPRftdrfelfIVA----------------- 418
Cdd:PRK03932 308 GKKFEFPVEWGDDLGSEHERYLAEEHFKkPVFVTNYPKDIKAFYMRLNPDGK--------TVAamdllapgigeiiggsq 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 419 REHanafsELnDPIDQRqrfeaqMKEkeqgndeaHEMD-EDF-----LRalEYGMPPTGGLGIGIDRLIMLLTNSPSIRD 492
Cdd:PRK03932 380 REE-----RL-DVLEAR------IKE--------LGLNkEDYwwyldLR--RYGSVPHSGFGLGFERLVAYITGLDNIRD 437
|
....*....
gi 1288434964 493 VLLFPHMRN 501
Cdd:PRK03932 438 VIPFPRTPG 446
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
67-497 |
2.80e-20 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 93.62 E-value: 2.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 67 EVNLAGRIMAKRGMGKASFAHIQDLSGRIQ--IYVRQDSIAE------AQYEAFSILDLGDIIGVKGVLFKTKTGETTIK 138
Cdd:PLN02850 83 EVLIRGRVHTIRGKGKSAFLVLRQSGFTVQcvVFVSEVTVSKgmvkyaKQLSRESVVDVEGVVSVPKKPVKGTTQQVEIQ 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 139 VKELEVLSKSLYPLP-----------EKFHGLKD--------VELRYRQRYVDLIInPDVQKTFIARSRIIQSMRRYLDS 199
Cdd:PLN02850 163 VRKIYCVSKALATLPfnvedaarsesEIEKALQTgeqlvrvgQDTRLNNRVLDLRT-PANQAIFRIQSQVCNLFREFLLS 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 200 QGYLEVETPTLhsIAG----GAAArpFITHHNALDMELYMriAIELHLKRLIVGGLEKVYEIGRVYRNEGIST-RHNPEF 274
Cdd:PLN02850 242 KGFVEIHTPKL--IAGasegGSAV--FRLDYKGQPACLAQ--SPQLHKQMAICGDFRRVFEIGPVFRAEDSFThRHLCEF 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 275 TMIEL-YEAYADYKDIMALTENMIAHIAQ----------EVLGTQvisYQGHEVDLTPQWRRVSMvdavkevvgvdfsve 343
Cdd:PLN02850 316 TGLDLeMEIKEHYSEVLDVVDELFVAIFDglnerckkelEAIREQ---YPFEPLKYLPKTLRLTF--------------- 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 344 msnEEAHRLAKEHKVPVEPHMTFGHILNAFFEQFVEETLIQPTFI-TGHPVEISPLAKKNDV-DPRFTDRFELFIVAREH 421
Cdd:PLN02850 378 ---AEGIQMLKEAGVEVDPLGDLNTESERKLGQLVKEKYGTDFYIlHRYPLAVRPFYTMPCPdDPKYSNSFDVFIRGEEI 454
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1288434964 422 ANAFSELNDPIDQRQRFEAQMKEKEQGndeahemdEDFLRALEYGMPPTGGLGIGIDRLIMLLTNSPSIRDVLLFP 497
Cdd:PLN02850 455 ISGAQRVHDPELLEKRAEECGIDVKTI--------STYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFP 522
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
67-147 |
3.86e-19 |
|
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: 81.84 E-value: 3.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 67 EVNLAGRIMAKRGMGKASFAHIQDLSGRIQIYVRQDSIAEAQYEAfSILDLGDIIGVKGVLFKT-----KTGETTIKVKE 141
Cdd:cd04100 1 EVTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEELGEFFEEA-EKLRTESVVGVTGTVVKRpegnlATGEIELQAEE 79
|
....*.
gi 1288434964 142 LEVLSK 147
Cdd:cd04100 80 LEVLSK 85
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
174-497 |
2.01e-18 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 86.23 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 174 IINPDVQKTFIARSRIIQSMRRYLDSQGYLEVETPTLHSIA-----GGAAARPFITHHNALDMELYMRIAIELHlKRLIV 248
Cdd:PRK06462 21 ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIISPSTdplmgLGSDLPVKQISIDFYGVEYYLADSMILH-KQLAL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 249 GGLEKVYEIGRVYRNEG---ISTRHNPEFTMIELYEAYADYKDIMALTENMIAHIAQEVLGT--QVISYQGHEV-DLTPQ 322
Cdd:PRK06462 100 RMLGKIFYLSPNFRLEPvdkDTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEheDELEFFGRDLpHLKRP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 323 WRRVSMVDAVKEVvgvdfsvemsNEEAHRLAKEHKVPVEphmtfghilnafFEQFVEETLIQPTFITGHPVEISPLAKKN 402
Cdd:PRK06462 180 FKRITHKEAVEIL----------NEEGCRGIDLEELGSE------------GEKSLSEHFEEPFWIIDIPKGSREFYDRE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 403 DVD-PRFTDRFELFIV----------AREHanafsELNDPIDqrqrfeaqmKEKEQGNDEAHEmdEDFLRALEYGMPPTG 471
Cdd:PRK06462 238 DPErPGVLRNYDLLLPegygeavsggEREY-----EYEEIVE---------RIREHGVDPEKY--KWYLEMAKEGPLPSA 301
|
330 340
....*....|....*....|....*.
gi 1288434964 472 GLGIGIDRLIMLLTNSPSIRDVLLFP 497
Cdd:PRK06462 302 GFGIGVERLTRYICGLRHIREVQPFP 327
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
68-497 |
2.36e-17 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 84.66 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 68 VNLAGRIMAKRGMGKASFAHIQDLSGRIQ--IYVRQDSIAE-----AQYEAFSILDL-GDIIGVKGVLFKTKTGETTIKV 139
Cdd:PTZ00401 81 VLIRARVSTTRKKGKMAFMVLRDGSDSVQamAAVEGDVPKEmidfiGQIPTESIVDVeATVCKVEQPITSTSHSDIELKV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 140 KELEVLSKSLYPLP---------EKFHGLK-DVELRYRQRYVDLIiNPDVQKTFIARSRIIQSMRRYLDSQGYLEVETPT 209
Cdd:PTZ00401 161 KKIHTVTESLRTLPftledasrkESDEGAKvNFDTRLNSRWMDLR-TPASGAIFRLQSRVCQYFRQFLIDSDFCEIHSPK 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 210 LHSIAGGAAARPFITHHnaLDMELYMRIAIELHLKRLIVGGLEKVYEIGRVYRNEGIST-RHNPEFTMIELyEAYAD--Y 286
Cdd:PTZ00401 240 IINAPSEGGANVFKLEY--FNRFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNThRHLTEFVGLDV-EMRINehY 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 287 KDIMALTENMIAHIAQEVLG--------TQVISYQGHEVDLTPQWRRVSMVDAVKE-VVGVDF---SVEMSNEEAHRLAK 354
Cdd:PTZ00401 317 YEVLDLAESLFNYIFERLAThtkelkavCQQYPFEPLVWKLTPERMKELGVGVISEgVEPTDKyqaRVHNMDSRMLRINY 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 355 EHKVP-----VEPHMTFGHILNAFFE----QFVEETLIQPTFITGH-PVEISP---LAKKNDVdpRFTDRFELFIVAREH 421
Cdd:PTZ00401 397 MHCIEllntvLEEKMAPTDDINTTNEkllgKLVKERYGTDFFISDRfPSSARPfytMECKDDE--RFTNSYDMFIRGEEI 474
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1288434964 422 ANAFSELNDPIDQRQRfeAQMKEKEQGNdeahemDEDFLRALEYGMPPTGGLGIGIDRLIMLLTNSPSIRDVLLFP 497
Cdd:PTZ00401 475 SSGAQRIHDPDLLLAR--AKMLNVDLTP------IKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFP 542
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
68-145 |
6.45e-16 |
|
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic acids. The family includes the anti-codon binding domain of lysyl, aspartyl, and asparaginyl -tRNA synthetases (See pfam00152). Aminoacyl-tRNA synthetases catalyze the addition of an amino acid to the appropriate tRNA molecule EC:6.1.1.-. This family also includes part of RecG helicase involved in DNA repair. Replication factor A is a hetero-trimeric complex, that contains a subunit in this family. This domain is also found at the C-terminus of bacterial DNA polymerase III alpha chain.
Pssm-ID: 460164 [Multi-domain] Cd Length: 75 Bit Score: 72.27 E-value: 6.45e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1288434964 68 VNLAGRIMAK-RGMGKASFAHIQDLSGRIQIYVRqdsiAEAQYEAFSILDLGDIIGVKGVLFKTKTGETTIKVKELEVL 145
Cdd:pfam01336 1 VTVAGRVTSIrRSGGKLLFLTLRDGTGSIQVVVF----KEEAEKLAKKLKEGDVVRVTGKVKKRKGGELELVVEEIELL 75
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
186-314 |
1.34e-13 |
|
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: 69.84 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 186 RSRIIQSMRRYLDSQGYLEVETPTLHSIAGGAAAR----PFITHHNALDMELYMRIAIELHLKRLIVGGL----EKVYEI 257
Cdd:cd00768 2 RSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGhepkDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIrklpLRLAEI 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1288434964 258 GRVYRNEGIS--TRHNPEFTMIELYEAYAD------YKDIMALTENMIAHIAQEVLGTQVISYQG 314
Cdd:cd00768 82 GPAFRNEGGRrgLRRVREFTQLEGEVFGEDgeeaseFEELIELTEELLRALGIKLDIVFVEKTPG 146
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
251-497 |
6.06e-13 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 71.16 E-value: 6.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 251 LEKVYEIGRVYRNEGIST-RHNPEFTMIELYEAYADYKDIMALTENMIAHIAQEVLGTQvisyqGHEVDLTPQWRRVSMV 329
Cdd:PLN02603 321 LSDVYTFGPTFRAENSNTsRHLAEFWMIEPELAFADLNDDMACATAYLQYVVKYILENC-----KEDMEFFNTWIEKGII 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 330 DAVKEVVGVDFsVEMSNEEAHRL----AKEHKVPVEphmtFGHILNAFFEQFVEETLI--QPTFITGHPVEISPLAKKND 403
Cdd:PLN02603 396 DRLSDVVEKNF-VQLSYTDAIELllkaKKKFEFPVK----WGLDLQSEHERYITEEAFggRPVIIRDYPKEIKAFYMREN 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 404 VDPRFTDRFELfIVARehanaFSELndpIDQRQRfEAQMKEKEQGNDEAHEMDEDFLRALE---YGMPPTGGLGIGIDRL 480
Cdd:PLN02603 471 DDGKTVAAMDM-LVPR-----VGEL---IGGSQR-EERLEYLEARLDELKLNKESYWWYLDlrrYGSVPHAGFGLGFERL 540
|
250
....*....|....*..
gi 1288434964 481 IMLLTNSPSIRDVLLFP 497
Cdd:PLN02603 541 VQFATGIDNIRDAIPFP 557
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
232-497 |
1.79e-12 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 69.67 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 232 ELYMRIAIELHLKRLiVGGLEKVYEIGRVYRNEGIST-RHNPEFTMIELYEAYADYKDIMALTENMIAHIAQEVLGTQV- 309
Cdd:PTZ00425 325 QAFLTVSGQLSLENL-CSSMGDVYTFGPTFRAENSHTsRHLAEFWMIEPEIAFADLYDNMELAESYIKYCIGYVLNNNFd 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 310 -ISYQGHEVDltpqwrrVSMVDAVKEVVGVDFS-VEMSN--EEAHRLAKEHKVPVEphmtFGHILNAFFEQFVEETLIQ- 384
Cdd:PTZ00425 404 dIYYFEENVE-------TGLISRLKNILDEDFAkITYTNviDLLQPYSDSFEVPVK----WGMDLQSEHERFVAEQIFKk 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 385 PTFITGHPVEISPLAKKNDVDPRFTDRFELFIVAREHANAFSELNDPIdqrQRFEAQMKEKEQgNDEAHEmdedFLRAL- 463
Cdd:PTZ00425 473 PVIVYNYPKDLKAFYMKLNEDQKTVAAMDVLVPKIGEVIGGSQREDNL---ERLDKMIKEKKL-NMESYW----WYRQLr 544
|
250 260 270
....*....|....*....|....*....|....
gi 1288434964 464 EYGMPPTGGLGIGIDRLIMLLTNSPSIRDVLLFP 497
Cdd:PTZ00425 545 KFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFP 578
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
67-173 |
3.37e-10 |
|
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: 57.92 E-value: 3.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 67 EVNLAGRIMAKRGMGKASFAHIQDLSGRIQIYVRQDSIAEaqYEAFSILDLGDIIGVKGVLF---------KTKTGETTI 137
Cdd:cd04317 16 EVTLCGWVQRRRDHGGLIFIDLRDRYGIVQVVFDPEEAPE--FELAEKLRNESVIQVTGKVRarpegtvnpKLPTGEIEV 93
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1288434964 138 KVKELEVLSKSlYPLPekF----HGLKDVELRYRQRYVDL 173
Cdd:cd04317 94 VASELEVLNKA-KTLP--FeiddDVNVSEELRLKYRYLDL 130
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
251-497 |
9.95e-08 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 54.61 E-value: 9.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 251 LEKVYEIGRVYRNEGIST-RHNPEFTMIELYEAYADYKDIMALTENMIAHIAQEVLgtqviSYQGHEVDLTPQWRRVSMV 329
Cdd:PLN02221 326 LSSVYTFGPTFRAENSHTsRHLAEFWMVEPEIAFADLEDDMNCAEAYVKYMCKWLL-----DKCFDDMELMAKNFDSGCI 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 330 DAVKEVVGVDF-------SVEMSnEEAHRLAKEHKVPVEphmtFGHILNAFFEQFVEETLIQ-PTFITGHPVEISPLAKK 401
Cdd:PLN02221 401 DRLRMVASTPFgrityteAIELL-EEAVAKGKEFDNNVE----WGIDLASEHERYLTEVLFQkPLIVYNYPKGIKAFYMR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 402 NDVDPRFTDRFELFIvarehaNAFSELNDPIDQRQRFEA-QMKEKEQGND-EAHEMDEDFLRaleYGMPPTGGLGIGIDR 479
Cdd:PLN02221 476 LNDDEKTVAAMDVLV------PKVGELIGGSQREERYDViKQRIEEMGLPiEPYEWYLDLRR---YGTVKHCGFGLGFER 546
|
250
....*....|....*...
gi 1288434964 480 LIMLLTNSPSIRDVLLFP 497
Cdd:PLN02221 547 MILFATGIDNIRDVIPFP 564
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
232-502 |
3.44e-06 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 49.48 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 232 ELYMRIAIELHLKRLiVGGLEKVYEIGRVYRNEGI-STRHNPEFTMIELYEAYADYKDIMALTENMIAHIAQEVLGTQV- 309
Cdd:PLN02532 371 PTYLTVSGRLHLESY-ACALGNVYTFGPRFRADRIdSARHLAEMWMVEVEMAFSELEDAMNCAEDYFKFLCKWVLENCSe 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 310 -ISYQGHEVD----------LTPQWRRVS---MVDAVKEVVGVDFsvEMSNEEAHRLAKEHkvpvephmtfghilnafFE 375
Cdd:PLN02532 450 dMKFVSKRIDktistrleaiISSSLQRISyteAVDLLKQATDKKF--ETKPEWGIALTTEH-----------------LS 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 376 QFVEETLIQPTFITGHPVEISPL-AKKNDvDPRFTDRFEL-------FIVAREHANAFSELNDPID----QRQRFEAQMK 443
Cdd:PLN02532 511 YLADEIYKKPVIIYNYPKELKPFyVRLND-DGKTVAAFDLvvpkvgtVITGSQNEERMDILNARIEelglPREQYEWYLD 589
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1288434964 444 EKEQGNDEaHEmdedflraleygmpptgGLGIGIDRLIMLLTNSPSIRDVLLFPHMRNK 502
Cdd:PLN02532 590 LRRHGTVK-HS-----------------GFSLGFELMVLFATGLPDVRDAIPFPRSWGK 630
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
67-153 |
2.07e-04 |
|
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the homodimeric non-discriminating (ND) Pyrococcus kodakaraensis aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. P. kodakaraensis AspRS is a class 2b aaRS. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. P. kodakaraensis ND-AspRS can charge both tRNAAsp and tRNAAsn. Some of the enzymes in this group may be discriminating, based on the presence of homologs of asparaginyl-tRNA synthetase (AsnRS) in their completed genomes.
Pssm-ID: 239811 [Multi-domain] Cd Length: 108 Bit Score: 40.76 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288434964 67 EVNLAGRIMAKRGMGKASFAHIQDLSGRIQIYVRQDSIAEAQYEAFSILDLGDIIGVKGVLFKTKTGETTIKV--KELEV 144
Cdd:cd04316 14 EVTVAGWVHEIRDLGGIKFVILRDREGIVQVTAPKKKVDKELFKTVRKLSRESVISVTGTVKAEPKAPNGVEIipEEIEV 93
|
....*....
gi 1288434964 145 LSKSLYPLP 153
Cdd:cd04316 94 LSEAKTPLP 102
|
|
| |
