|
Name |
Accession |
Description |
Interval |
E-value |
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
1-488 |
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: 875.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 1 MQRRLEEREMLRKEGVRPYPFSFDVTAYSRQIKEQFDENSP-----QTVSVAGRIMAIRKMGKASFFNIQDSQGRIQIYI 75
Cdd:COG1190 11 IRVRREKLEELREAGIDPYPNKFPRTHTAAEIREKYDELEAeeetgDEVSVAGRIMAKRDMGKASFADLQDGSGRIQLYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 76 KRDEVGQEAYRVFKLLDIGDIVGVKGYSFRTKTGEISIHAQEFMLLSKSLRPIPiakEKevdgkkvtYDAFSDKELRYRQ 155
Cdd:COG1190 91 RRDELGEEAYELFKLLDLGDIVGVEGTVFRTKTGELSVKVEELTLLSKSLRPLP---EK--------FHGLTDPETRYRQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 156 RYVDLIVNPEVRETFVKRSAIVSFMRTFLSSKGYLEVETPILQPIYGGAAARPFTTHHNALDMELYLRIANELYLKRLIV 235
Cdd:COG1190 160 RYVDLIVNPEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 236 GGFDGVFEFAKDFRNEGIDRFHNPEFTQVELYVAYKDYLWMMELVEELLYRTNLEVNGRDSVTFLDHEISLKPPFRRMTI 315
Cdd:COG1190 240 GGFERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGTTKVTYQGQEIDLSPPWRRITM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 316 AESINEYCTCDITG-KNEAELRNIAKDLGLELDPKISSGKIIDEIFGEFVEPKLIQPTFITDYPVEMSPLAKGHRSKEGT 394
Cdd:COG1190 320 VEAIKEATGIDVTPlTDDEELRALAKELGIEVDPGWGRGKLIDELFEELVEPKLIQPTFVTDYPVEVSPLAKRHRDDPGL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 395 VERFELIVGGKELCNSFSELNDPVIQRQRLEEQAALRQRGDDEAMIVDEDFLRALEYGMPPCAGLGIGIDRLVMLLAGQD 474
Cdd:COG1190 400 TERFELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSP 479
|
490
....*....|....
gi 2173675722 475 SIRDVIFFPHMKPE 488
Cdd:COG1190 480 SIRDVILFPLMRPE 493
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
1-488 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 868.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 1 MQRRLEEREMLRKEGVRPYPFSFDVTAYSRQIKEQFD-------ENSPQTVSVAGRIMAIRKMGKASFFNIQDSQGRIQI 73
Cdd:PRK00484 7 IAVRREKLAELREQGIDPYPNKFERTHTAAELRAKYDdkekeelEELEIEVSVAGRVMLKRVMGKASFATLQDGSGRIQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 74 YIKRDEVGQEAYRVFKLLDIGDIVGVKGYSFRTKTGEISIHAQEFMLLSKSLRPIPiakEKevdgkkvtYDAFSDKELRY 153
Cdd:PRK00484 87 YVSKDDVGEEALEAFKKLDLGDIIGVEGTLFKTKTGELSVKATELTLLTKSLRPLP---DK--------FHGLTDVETRY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 154 RQRYVDLIVNPEVRETFVKRSAIVSFMRTFLSSKGYLEVETPILQPIYGGAAARPFTTHHNALDMELYLRIANELYLKRL 233
Cdd:PRK00484 156 RQRYVDLIVNPESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARPFITHHNALDIDLYLRIAPELYLKRL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 234 IVGGFDGVFEFAKDFRNEGIDRFHNPEFTQVELYVAYKDYLWMMELVEELLYRTNLEVNGRDSVTFLDHEISLKPPFRRM 313
Cdd:PRK00484 236 IVGGFERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTYQGTEIDFGPPFKRL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 314 TIAESINEYCTCDITGKNEAELRNIAKDLGLELDPKISSGKIIDEIFGEFVEPKLIQPTFITDYPVEMSPLAKGHRSKEG 393
Cdd:PRK00484 316 TMVDAIKEYTGVDFDDMTDEEARALAKELGIEVEKSWGLGKLINELFEEFVEPKLIQPTFITDYPVEISPLAKRHREDPG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 394 TVERFELIVGGKELCNSFSELNDPVIQRQRLEEQAALRQRGDDEAMIVDEDFLRALEYGMPPCAGLGIGIDRLVMLLAGQ 473
Cdd:PRK00484 396 LTERFELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDS 475
|
490
....*....|....*
gi 2173675722 474 DSIRDVIFFPHMKPE 488
Cdd:PRK00484 476 PSIRDVILFPLMRPE 490
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
4-488 |
0e+00 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 628.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 4 RLEEREMLRKEGVRPYPFSFDVTAYSRQIKEQF------DENSPQTVSVAGRIMAIRKMGKASFFNIQDSQGRIQIYI-- 75
Cdd:PLN02502 65 RLKKVEALRAKGVEPYPYKFDVTHTAPELQEKYgslengEELEDVSVSVAGRIMAKRAFGKLAFYDLRDDGGKIQLYAdk 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 76 KRDEVGQEAYRVFK-LLDIGDIVGVKGYSFRTKTGEISIHAQEFMLLSKSLRPIPiakekevdgKKvtYDAFSDKELRYR 154
Cdd:PLN02502 145 KRLDLDEEEFEKLHsLVDRGDIVGVTGTPGKTKKGELSIFPTSFEVLTKCLLMLP---------DK--YHGLTDQETRYR 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 155 QRYVDLIVNPEVRETFVKRSAIVSFMRTFLSSKGYLEVETPILQPIYGGAAARPFTTHHNALDMELYLRIANELYLKRLI 234
Cdd:PLN02502 214 QRYLDLIANPEVRDIFRTRAKIISYIRRFLDDRGFLEVETPMLNMIAGGAAARPFVTHHNDLNMDLYLRIATELHLKRLV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 235 VGGFDGVFEFAKDFRNEGIDRFHNPEFTQVELYVAYKDYLWMMELVEELLYRTNLEVNGRDSVTFLDHEISLKPPFRRMT 314
Cdd:PLN02502 294 VGGFERVYEIGRQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKELTGSYKIKYHGIEIDFTPPFRRIS 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 315 IAESINEYCTCDITGKNE-AELRNIAKDLGLELDPKI----SSGKIIDEIFGEFVEPKLIQPTFITDYPVEMSPLAKGHR 389
Cdd:PLN02502 374 MISLVEEATGIDFPADLKsDEANAYLIAACEKFDVKCpppqTTGRLLNELFEEFLEETLVQPTFVLDHPVEMSPLAKPHR 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 390 SKEGTVERFELIVGGKELCNSFSELNDPVIQRQRLEEQAALRQRGDDEAMIVDEDFLRALEYGMPPCAGLGIGIDRLVML 469
Cdd:PLN02502 454 SKPGLTERFELFINGRELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRLVML 533
|
490
....*....|....*....
gi 2173675722 470 LAGQDSIRDVIFFPHMKPE 488
Cdd:PLN02502 534 LTDSASIRDVIAFPAMKPQ 552
|
|
| lysS_bact |
TIGR00499 |
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ... |
1-487 |
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: 578.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 1 MQRRLEEREMLRKEGVRPYPFSFDVTAYSRQIKEQFD-------ENSPQTVSVAGRIMAIRKMGKASFFNIQDSQGRIQI 73
Cdd:TIGR00499 6 AQQRLEKLNRLRQTGNNPYLHKFERTHSAQEFQEKYAdlsneelKEKELKVSIAGRIKAIRSMGKATFITLQDESGQIQL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 74 YIKRDEVGQEAYRVFK-LLDIGDIVGVKGYSFRTKTGEISIHAQEFMLLSKSLRPIPiakEKevdgkkvtYDAFSDKELR 152
Cdd:TIGR00499 86 YVNKNKLPEDFYEFDEyLLDLGDIIGVTGYPFKTKTGELSVKVTELQILTKCLQPLP---DK--------WHGLTDQETR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 153 YRQRYVDLIVNPEVRETFVKRSAIVSFMRTFLSSKGYLEVETPILQPIYGGAAARPFTTHHNALDMELYLRIANELYLKR 232
Cdd:TIGR00499 155 YRQRYLDLIVNPDVRQTFLKRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKPFITHHNALDMDLYLRIAPELYLKR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 233 LIVGGFDGVFEFAKDFRNEGIDRFHNPEFTQVELYVAYKDYLWMMELVEELLYRTNLEVNGRDSVTFLDHEISLKPPFRR 312
Cdd:TIGR00499 235 LIVGGLEKVYEIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTFIINYNDLEIDLKPPWKR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 313 MTIAESIneyctCDITG------KNEAELRNIAKDLGLEL-DPKISSGKIIDEIFGEFVEPKLIQPTFITDYPVEMSPLA 385
Cdd:TIGR00499 315 ITMVDAL-----EMVTGidfdilKDDETAKALAKEHGIEVaEDSLTLGHILNKFFEQFLEHTLIQPTFITHYPAEISPLA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 386 KGHRSKEGTVERFELIVGGKELCNSFSELNDPVIQRQRLEEQAALRQRGDDEAMIVDEDFLRALEYGMPPCAGLGIGIDR 465
Cdd:TIGR00499 390 KRDPSNPEFTERFELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGIGIDR 469
|
490 500
....*....|....*....|..
gi 2173675722 466 LVMLLAGQDSIRDVIFFPHMKP 487
Cdd:TIGR00499 470 LVMLLTDAPSIRDVLLFPQLRP 491
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
163-487 |
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: 546.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 163 NPEVRETFVKRSAIVSFMRTFLSSKGYLEVETPILQPIYGGAAARPFTTHHNALDMELYLRIANELYLKRLIVGGFDGVF 242
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 243 EFAKDFRNEGIDRFHNPEFTQVELYVAYKDYLWMMELVEELLYRTNLEVNGRDSVTFLDHEISLKPPFRRMTIAESINEY 322
Cdd:cd00775 81 EIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIEYGGKELDFTPPFKRVTMVDALKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 323 CTCDITGKNEAELRNIAKDL----GLELDPKISSGKIIDEIFGEFVEPKLIQPTFITDYPVEMSPLAKGHRSKEGTVERF 398
Cdd:cd00775 161 TGIDFPELDLEQPEELAKLLakliKEKIEKPRTLGKLLDKLFEEFVEPTLIQPTFIIDHPVEISPLAKRHRSNPGLTERF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 399 ELIVGGKELCNSFSELNDPVIQRQRLEEQAALRQRGDDEAMIVDEDFLRALEYGMPPCAGLGIGIDRLVMLLAGQDSIRD 478
Cdd:cd00775 241 ELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLTDSNSIRD 320
|
....*....
gi 2173675722 479 VIFFPHMKP 487
Cdd:cd00775 321 VILFPAMRP 329
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
4-488 |
1.56e-175 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 522.22 E-value: 1.56e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 4 RLEEREMLRKEGVRPYPFSFDvtaYSRQIKEQFDENSPQTVSVAGRIMAIRKMGKASFFNIQDSQGRIQIYIKRDEVGQE 83
Cdd:PRK02983 617 RLAKLEALRAAGVDPYPVGVP---PTHTVAEALDAPTGEEVSVSGRVLRIRDYGGVLFADLRDWSGELQVLLDASRLEQG 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 84 AYRVFK-LLDIGDIVGVKGYSFRTKTGEISIHAQEFMLLSKSLRPIPiakekevdgKKvtYDAFSDKELRYRQRYVDLIV 162
Cdd:PRK02983 694 SLADFRaAVDLGDLVEVTGTMGTSRNGTLSLLVTSWRLAGKCLRPLP---------DK--WKGLTDPEARVRQRYLDLAV 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 163 NPEVRETFVKRSAIVSFMRTFLSSKGYLEVETPILQPIYGGAAARPFTTHHNALDMELYLRIANELYLKRLIVGGFDGVF 242
Cdd:PRK02983 763 NPEARDLLRARSAVVRAVRETLVARGFLEVETPILQQVHGGANARPFVTHINAYDMDLYLRIAPELYLKRLCVGGVERVF 842
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 243 EFAKDFRNEGIDRFHNPEFTQVELYVAYKDYLWMMELVEELLYRTNLEVNGRDSVTFLDHEISLKP-----PFRRMTIAE 317
Cdd:PRK02983 843 ELGRNFRNEGVDATHNPEFTLLEAYQAHADYDTMRDLTRELIQNAAQAAHGAPVVMRPDGDGVLEPvdisgPWPVVTVHD 922
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 318 SINEYCTCDIT-GKNEAELRNIAKDLGLELDPKISSGKIIDEIFGEFVEPKLIQPTFITDYPVEMSPLAKGHRSKEGTVE 396
Cdd:PRK02983 923 AVSEALGEEIDpDTPLAELRKLCDAAGIPYRTDWDAGAVVLELYEHLVEDRTTFPTFYTDFPTSVSPLTRPHRSDPGLAE 1002
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 397 RFELIVGGKELCNSFSELNDPVIQRQRLEEQAALRQRGDDEAMIVDEDFLRALEYGMPPCAGLGIGIDRLVMLLAGQdSI 476
Cdd:PRK02983 1003 RWDLVAWGVELGTAYSELTDPVEQRRRLTEQSLLAAGGDPEAMELDEDFLQALEYAMPPTGGLGMGVDRLVMLLTGR-SI 1081
|
490
....*....|..
gi 2173675722 477 RDVIFFPHMKPE 488
Cdd:PRK02983 1082 RETLPFPLVKPR 1093
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
1-488 |
8.56e-155 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 449.90 E-value: 8.56e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 1 MQRRLEEREMLRKEGVrPYPFSFDVTAYSRQIKEQFDENSPQT-------VSVAGRIMAIRKMGKASFFNIQDSQGRIQI 73
Cdd:PRK12445 19 LRNRREKLAALRQQGV-AFPNDFRRDHTSDQLHEEFDAKDNQEleslnieVSVAGRMMTRRIMGKASFVTLQDVGGRIQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 74 YIKRDEVGQEAYR-VFKLLDIGDIVGVKGYSFRTKTGEISIHAQEFMLLSKSLRPIPIakekevdgkkvTYDAFSDKELR 152
Cdd:PRK12445 98 YVARDSLPEGVYNdQFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPD-----------KFHGLQDQEVR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 153 YRQRYVDLIVNPEVRETFVKRSAIVSFMRTFLSSKGYLEVETPILQPIYGGAAARPFTTHHNALDMELYLRIANELYLKR 232
Cdd:PRK12445 167 YRQRYLDLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 233 LIVGGFDGVFEFAKDFRNEGIDRFHNPEFTQVELYVAYKDYLWMMELVEELLYRTNLEVNGRDSVTFLDHEISLKPPFRR 312
Cdd:PRK12445 247 LVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFDFGKPFEK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 313 MTIAESINEYctcdITGKNEAELRN------IAKDLGLELDPKISSGKIIDEIFGEFVEPKLIQPTFITDYPVEMSPLAK 386
Cdd:PRK12445 327 LTMREAIKKY----RPETDMADLDNfdaakaLAESIGITVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLAR 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 387 GHRSKEGTVERFELIVGGKELCNSFSELNDPVIQRQRLEEQAALRQRGDDEAMIVDEDFLRALEYGMPPCAGLGIGIDRL 466
Cdd:PRK12445 403 RNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRM 482
|
490 500
....*....|....*....|..
gi 2173675722 467 VMLLAGQDSIRDVIFFPHMKPE 488
Cdd:PRK12445 483 IMLFTNSHTIRDVILFPAMRPQ 504
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
12-487 |
5.69e-126 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 378.97 E-value: 5.69e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 12 RKEGVRPYPFSFDVTAYSRQIKEQFD--------ENSPqtVSVAGRIMAIRKMG-KASFFNIQDSQGRIQI---YIKRDE 79
Cdd:PTZ00417 97 KAKGINPYPHKFERTITVPEFVEKYQdlasgehlEDTI--LNVTGRIMRVSASGqKLRFFDLVGDGAKIQVlanFAFHDH 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 80 VGQEAYRVFKLLDIGDIVGVKGYSFRTKTGEISIHAQEFMLLSKSLRPIPIAKekevdgkkvtydAFSDKELRYRQRYVD 159
Cdd:PTZ00417 175 TKSNFAECYDKIRRGDIVGIVGFPGKSKKGELSIFPKETIILSPCLHMLPMKY------------GLKDTEIRYRQRYLD 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 160 LIVNPEVRETFVKRSAIVSFMRTFLSSKGYLEVETPILQPIYGGAAARPFTTHHNALDMELYLRIANELYLKRLIVGGFD 239
Cdd:PTZ00417 243 LMINESTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLVAGGANARPFITHHNDLDLDLYLRIATELPLKMLIVGGID 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 240 GVFEFAKDFRNEGIDRFHNPEFTQVELYVAYKDYLWMMELVEELLYRTNLEVNGRDSVTFLDH-------EISLKPPFRR 312
Cdd:PTZ00417 323 KVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHLFGTYKILYNKDgpekdpiEIDFTPPYPK 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 313 MTIAESINEYCTCDIT---GKNEA--ELRNIAKDLGLELDPKISSGKIIDEIFGEFVEPKLI-QPTFITDYPVEMSPLAK 386
Cdd:PTZ00417 403 VSIVEELEKLTNTKLEqpfDSPETinKMINLIKENKIEMPNPPTAAKLLDQLASHFIENKYPnKPFFIIEHPQIMSPLAK 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 387 GHRSKEGTVERFELIVGGKELCNSFSELNDPVIQRQRLEEQAALRQRGDDEAMIVDEDFLRALEYGMPPCAGLGIGIDRL 466
Cdd:PTZ00417 483 YHRSKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCTSLEYGLPPTGGLGLGIDRI 562
|
490 500
....*....|....*....|.
gi 2173675722 467 VMLLAGQDSIRDVIFFPHMKP 487
Cdd:PTZ00417 563 TMFLTNKNCIKDVILFPTMRP 583
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
22-486 |
6.06e-120 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 365.89 E-value: 6.06e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 22 SFDVTAYSRQIKEQF------DENSPQTVSVAGRIMAIRKMGKASFFNIQDSQGRIQIYIKRDE-VGQEAYRVFKL-LDI 93
Cdd:PTZ00385 82 SFRGITPISEVRERYgylasgDRAAQATVRVAGRVTSVRDIGKIIFVTIRSNGNELQVVGQVGEhFTREDLKKLKVsLRV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 94 GDIVGVKGYSFRTKTGEISIHAQEFMLLSKSlrpipIAKEKEVDGKKVTYDAFSDKELRYRQRYVDLIVNPEVRETFVKR 173
Cdd:PTZ00385 162 GDIIGADGVPCRMQRGELSVAASRMLILSPY-----VCTDQVVCPNLRGFTVLQDNDVKYRYRFTDMMTNPCVIETIKKR 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 174 SAIVSFMRTFLSSKGYLEVETPILQPIYGGAAARPFTTHHNALDMELYLRIANELYLKRLIVGGFDGVFEFAKDFRNEGI 253
Cdd:PTZ00385 237 HVMLQALRDYFNERNFVEVETPVLHTVASGANAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 254 DRFHNPEFTQVELYVAYKDYLWMMELVEELLYRTNLEVNGRDSVTF-------LDHEISLKPPFRRMTIAESINEYCTCD 326
Cdd:PTZ00385 317 DRSHNPEFTSCEFYAAYHTYEDLMPMTEDIFRQLAMRVNGTTVVQIypenahgNPVTVDLGKPFRRVSVYDEIQRMSGVE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 327 ITGKNE-------AELRNIAKDLGLELDPKISSGKIIDEIFGEFVEPKLIQPTFITDYPVEMSPLAKGHRSKEGTVERFE 399
Cdd:PTZ00385 397 FPPPNElntpkgiAYMSVVMLRYNIPLPPVRTAAKMFEKLIDFFITDRVVEPTFVMDHPLFMSPLAKEQVSRPGLAERFE 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 400 LIVGGKELCNSFSELNDPVIQRQRLEEQAALRQRGDDEAMIVDEDFLRALEYGMPPCAGLGIGIDRLVMLLAGQDSIRDV 479
Cdd:PTZ00385 477 LFVNGIEYCNAYSELNDPHEQYHRFQQQLVDRQGGDEEAMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDG 556
|
....*..
gi 2173675722 480 IFFPHMK 486
Cdd:PTZ00385 557 IIFPLLR 563
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
148-486 |
5.57e-118 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 349.17 E-value: 5.57e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 148 DKELRYRQRYVDLiVNPEVRETFVKRSAIVSFMRTFLSSKGYLEVETPILQPIYGGAAARPFTTHHNALDMELYLRIANE 227
Cdd:pfam00152 1 DEETRLKYRYLDL-RRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 228 LYLKRLIVGGFDGVFEFAKDFRNEGIDRFHNPEFTQVELYVAYKDYLWMMELVEELLYRTNLEVNGRDSVTFLDHEISLK 307
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 308 PPFRRMTIAESIN----EYCTCDITGKNEAELRNiakdlGLELdpkissgkiideifgeFVEPKLIQPTFITDYPVEMSP 383
Cdd:pfam00152 160 KPFPRITYAEAIEklngKDVEELGYGSDKPDLRF-----LLEL----------------VIDKNKFNPLWVTDFPAEHHP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 384 LAKGHRSK-EGTVERFELIVGGKELCNSFSELNDPVIQRQRLEEQaalrQRGDDEAMIVDEDFLRALEYGMPPCAGLGIG 462
Cdd:pfam00152 219 FTMPKDEDdPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQ----GLDPEEAEEKFGFYLDALKYGAPPHGGLGIG 294
|
330 340
....*....|....*....|....
gi 2173675722 463 IDRLVMLLAGQDSIRDVIFFPHMK 486
Cdd:pfam00152 295 LDRLVMLLTGLESIREVIAFPKTR 318
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
170-487 |
5.22e-90 |
|
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: 275.51 E-value: 5.22e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 170 FVKRSAIVSFMRTFLSSKGYLEVETPILQPIYGGAAARPFTTHHNALDMELYLRIANELYLKRLIVGGFDGVFEFAKDFR 249
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 250 NEGIDRFHNPEFTQVELYVAYKDYLWMMELVEELLYRTNLEVNGRDSVTFLDHEISLKPPFRRMTIAESINEYctcditg 329
Cdd:cd00669 81 NEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYGFELEDFGLPFPRLTYREALERY------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 330 kneaelrniakdlgleldpkissgkiideifgefvepklIQPTFITDYPVEM-SPLAKGHRSKEGTVERFELIVGGKELC 408
Cdd:cd00669 154 ---------------------------------------GQPLFLTDYPAEMhSPLASPHDVNPEIADAFDLFINGVEVG 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2173675722 409 NSFSELNDPVIQRQRLEEQAalrqRGDDEAMIVDEDFLRALEYGMPPCAGLGIGIDRLVMLLAGQDSIRDVIFFPHMKP 487
Cdd:cd00669 195 NGSSRLHDPDIQAEVFQEQG----INKEAGMEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKMRR 269
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
183-480 |
1.19e-81 |
|
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: 254.78 E-value: 1.19e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 183 FLSSKGYLEVETPILQPiYGGAAA--RPFTTH---HNALDMELYLRIANELYLKRLIVGGFDGVFEFAKDFRNEGIDRFH 257
Cdd:TIGR00462 1 FFAERGVLEVETPLLSP-APVTDPhlDAFATEfvgPDGQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 258 NPEFTQVELYVAYKDYLWMMELVEELLYrtnlEVNGRDSvtfldheislkPPFRRMTIAESINEYCTCDITGKNEAELRN 337
Cdd:TIGR00462 80 NPEFTMLEWYRPGFDYHDLMDEVEALLQ----ELLGDPF-----------APAERLSYQEAFLRYAGIDPLTASLAELQA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 338 IAKDLGLELDPKISSGKIIDEIFGEFVEPKLIQ--PTFITDYPVEMSPLAKGHRSKEGTVERFELIVGGKELCNSFSELN 415
Cdd:TIGR00462 145 AAAAHGIRASEEDDRDDLLDLLFSEKVEPHLGFgrPTFLYDYPASQAALARISPDDPRVAERFELYIKGLELANGFHELT 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2173675722 416 DPVIQRQRLEEQAALRQRGDDEAMIVDEDFLRALEYGMPPCAGLGIGIDRLVMLLAGQDSIRDVI 480
Cdd:TIGR00462 225 DAAEQRRRFEADNALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDVL 289
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
167-480 |
1.30e-79 |
|
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441870 [Multi-domain] Cd Length: 309 Bit Score: 250.41 E-value: 1.30e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 167 RETFVKRSAIVSFMRTFLSSKGYLEVETPILQPiYGGAAA--RPFTT---HHNALDMELYLRIANELYLKRLIVGGFDGV 241
Cdd:COG2269 3 REALRARARLLAAIRAFFAERGVLEVETPALSV-APGTDPhlDSFATefiGPDGGGRPLYLHTSPEFAMKRLLAAGSGPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 242 FEFAKDFRNEGIDRFHNPEFTQVELYVAYKDYLWMMELVEELLyRTNLEVNGRdsvtfldheislkPPFRRMTIAESINE 321
Cdd:COG2269 82 YQIAKVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALL-QLVLGAAGF-------------APAERLSYQEAFLR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 322 YCTCDITGKNEAELRNIAKDLGLELDPKISSGKIIDEIFGEFVEPKLIQ--PTFITDYPVEMSPLAKGHRSKEGTVERFE 399
Cdd:COG2269 148 YLGIDPLTADLDELAAAAAAAGLRVADDDDRDDLLDLLLSERVEPQLGRdrPTFLYDYPASQAALARISPDDPRVAERFE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 400 LIVGGKELCNSFSELNDPVIQRQRLEEQAALRQRGDDEAMIVDEDFLRALEYGMPPCAGLGIGIDRLVMLLAGQDSIRDV 479
Cdd:COG2269 228 LYACGVELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALGAERIDDV 307
|
.
gi 2173675722 480 I 480
Cdd:COG2269 308 L 308
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
168-479 |
9.23e-60 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 198.61 E-value: 9.23e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 168 ETFVKRSAIVSFMRTFLSSKGYLEVETPILQP-------IYggaaarPFTTHHNALDME----LYLRIANELYLKRLIVG 236
Cdd:PRK09350 3 PNLLKRAKIIAEIRRFFADRGVLEVETPILSQatvtdihLV------PFETRFVGPGASqgktLWLMTSPEYHMKRLLAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 237 GFDGVFEFAKDFRNEGIDRFHNPEFTQVELYVAYKDYLWMMELVEELLyrtnlevngrdsvtfldHEISLKPPFRRMTIA 316
Cdd:PRK09350 77 GSGPIFQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLL-----------------QQVLDCEPAESLSYQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 317 ESINEYCTCDITGKNEAELRNIAKDLGL--ELDPKISSGKIIDEIFGEFVEPKLIQ--PTFITDYPVEMSPLAKGHRSKE 392
Cdd:PRK09350 140 QAFLRYLGIDPLSADKTQLREVAAKLGLsnIADEEEDRDTLLQLLFTFGVEPNIGKekPTFVYHFPASQAALAKISTEDH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 393 GTVERFELIVGGKELCNSFSELNDPVIQRQRLEEQAALRQRGDDEAMIVDEDFLRALEYGMPPCAGLGIGIDRLVMLLAG 472
Cdd:PRK09350 220 RVAERFEVYFKGIELANGFHELTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCSGVALGVDRLIMLALG 299
|
....*..
gi 2173675722 473 QDSIRDV 479
Cdd:PRK09350 300 AESISEV 306
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
43-160 |
5.99e-53 |
|
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These enzymes are homodimeric class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Included in this group are E. coli LysS and LysU. These two isoforms of LysRS are encoded by distinct genes which are differently regulated. Eukaryotes contain 2 sets of aaRSs, both of which encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Saccharomyces cerevisiae cytoplasmic and mitochondrial LysRSs have been shown to participate in the mitochondrial import of the only nuclear-encoded tRNA of S. cerevisiae (tRNAlysCUU). The gene for human LysRS encodes both the cytoplasmic and the mitochondrial isoforms of LysRS. In addition to their housekeeping role, human lysRS may function as a signaling molecule that activates immune cells and tomato LysRS may participate in a root-specific process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging.
Pssm-ID: 239817 [Multi-domain] Cd Length: 108 Bit Score: 173.82 E-value: 5.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 43 TVSVAGRIMAIRKMGKASFFNIQDSQGRIQIYIKRDEVGQEAYRVFK-LLDIGDIVGVKGYSFRTKTGEISIHAQEFMLL 121
Cdd:cd04322 1 EVSVAGRIMSKRGSGKLSFADLQDESGKIQVYVNKDDLGEEEFEDFKkLLDLGDIIGVTGTPFKTKTGELSIFVKEFTLL 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 2173675722 122 SKSLRPIPiakEKevdgkkvtYDAFSDKELRYRQRYVDL 160
Cdd:cd04322 81 SKSLRPLP---EK--------FHGLTDVETRYRQRYLDL 108
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
26-483 |
3.86e-44 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 160.74 E-value: 3.86e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 26 TAYSRQIKEQFDEnspQTVSVAGRIMAIRKMGKASFFNIQDSQGRIQIYIKRDEVgQEAYRVFKLLDIGDIVGVKG---Y 102
Cdd:PRK05159 4 RHLTSELTPELDG---EEVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKVD-EELFETIKKLKRESVVSVTGtvkA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 103 SFRTKTGeISIHAQEFMLLSKSLRPIPIakekEVDGKKvtyDAFSDKELRYRqrYVDLiVNPEVRETFVKRSAIVSFMRT 182
Cdd:PRK05159 80 NPKAPGG-VEVIPEEIEVLNKAEEPLPL----DISGKV---LAELDTRLDNR--FLDL-RRPRVRAIFKIRSEVLRAFRE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 183 FLSSKGYLEVETP--ILQPIYGGAAARPFTTHHNaldmELYLRIANELYlKRLIVG-GFDGVFEFAKDFRNEGID-RFHN 258
Cdd:PRK05159 149 FLYENGFTEIFTPkiVASGTEGGAELFPIDYFEK----EAYLAQSPQLY-KQMMVGaGFERVFEIGPVFRAEEHNtSRHL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 259 PEFTQVELYVAY-KDYLWMMELVEELLYRTNLEV--NGRDSVTFLDHEISLKP-PFRRMTIAESIneyctcDITGKNEAE 334
Cdd:PRK05159 224 NEYTSIDVEMGFiDDHEDVMDLLENLLRYMYEDVaeNCEKELELLGIELPVPEtPIPRITYDEAI------EILKSKGNE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 335 LRNIaKDLGLELDPKIssGKIIDEIFG-EFVepkliqptFITDYPVEMSPL-AKGHRSKEGTVERFELIVGGKELCNSFS 412
Cdd:PRK05159 298 ISWG-DDLDTEGERLL--GEYVKEEYGsDFY--------FITDYPSEKRPFyTMPDEDDPEISKSFDLLFRGLEITSGGQ 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2173675722 413 ELNDpviqRQRLEEQaaLRQRG-DDEAMivdEDFLRALEYGMPPCAGLGIGIDRLVMLLAGQDSIRDVIFFP 483
Cdd:PRK05159 367 RIHR----YDMLVES--IKEKGlNPESF---EFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFP 429
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
32-483 |
3.90e-41 |
|
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: 152.51 E-value: 3.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 32 IKEQFDENSPQTVSVAGRIMAIRKMGKASFFNIQDSQGRIQIYIKRDEVgqEAYRVFKLLDIGDIVGVKGY---SFRTKT 108
Cdd:COG0017 5 IKDLLPEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKL--ENFEEAKKLTTESSVEVTGTvveSPRAPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 109 GeISIHAQEFMLLSKSLRPIPIAKEKevdgkkvtydafSDKELRYRQRYVDLiVNPEVRETFVKRSAIVSFMRTFLSSKG 188
Cdd:COG0017 83 G-VELQAEEIEVLGEADEPYPLQPKR------------HSLEFLLDNRHLRL-RTNRFGAIFRIRSELARAIREFFQERG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 189 YLEVETPIlqpIYGGA---AARPFTTHHnaLDMELYLRIANELYlKRLIVGGFDGVFEFAKDFRNEGID-RFHNPEFTQV 264
Cdd:COG0017 149 FVEVHTPI---ITASAtegGGELFPVDY--FGKEAYLTQSGQLY-KEALAMALEKVYTFGPTFRAEKSNtRRHLAEFWMI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 265 ELYVAYKDYLWMMELVEELL---YRTNLEvNGRDSVTFLDHEIS-----LKPPFRRMTIAESIneyctcDITGKNEAELR 336
Cdd:COG0017 223 EPEMAFADLEDVMDLAEEMLkyiIKYVLE-NCPEELEFLGRDVErlekvPESPFPRITYTEAI------EILKKSGEKVE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 337 NiakdlGLELDPKISsgKIIDEIFGEfvepkliQPTFITDYPVEMSPL-AKGHRSKEGTVERFELIVGG-KELCnSFSel 414
Cdd:COG0017 296 W-----GDDLGTEHE--RYLGEEFFK-------KPVFVTDYPKEIKAFyMKPNPDDPKTVAAFDLLAPGiGEII-GGS-- 358
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2173675722 415 ndpviQRQ-RLEE-QAALRQRG-DDEAMivdEDFLRALEYGMPPCAGLGIGIDRLVMLLAGQDSIRDVIFFP 483
Cdd:COG0017 359 -----QREhRYDVlVERIKEKGlDPEDY---EWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFP 422
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
44-483 |
7.36e-33 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 132.42 E-value: 7.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 44 VSVAGRIMAIRKMGKASFFNIQDSQGRIQIYIKRDEVGQEAYRVFKLLDIGDIVGVKGYSFR---------TKTGEISIH 114
Cdd:PRK12820 21 VCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFSPEAAPADVYELAASLRAEFCVALQGEVQKrleetenphIETGDIEVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 115 AQEFMLLSKS-LRPIPIAKEKEVDGKKVTYDAFSDKELRYRQRYVDlIVNPEVRETFVKRSAIVSFMRTFLSSKGYLEVE 193
Cdd:PRK12820 101 VRELSILAASeALPFAISDKAMTAGAGSAGADAVNEDLRLQYRYLD-IRRPAMQDHLAKRHRIIKCARDFLDSRGFLEIE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 194 TPILQpIYGGAAARPFTTHHNALDMELY-LRIANELYLKRLIVGGFDGVFEFAKDFRNEGIDRFHNPEFTQVELYVAYKD 272
Cdd:PRK12820 180 TPILT-KSTPEGARDYLVPSRIHPKEFYaLPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEFTQLDIEASFID 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 273 YLWMMELVEELLYRTnLEVNGrdsvtfldheISLKPPFRRMTIAESINEYCT---------------------------- 324
Cdd:PRK12820 259 EEFIFELIEELTARM-FAIGG----------IALPRPFPRMPYAEAMDTTGSdrpdlrfdlkfadatdifentrygifkq 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 325 ----------CDITGKNEAELRNIAK-DLGLELDP----------KISSGKI---IDEIFGE------------------ 362
Cdd:PRK12820 328 ilqrggrikgINIKGQSEKLSKNVLQnEYAKEIAPsfgakgmtwmRAEAGGLdsnIVQFFSAdekealkrrfhaedgdvi 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 363 ---------------------------FVEPKLIQPTFITDYPV-----------EMSPLAKGHRSK--EGTVER----- 397
Cdd:PRK12820 408 imiadascaivlsalgqlrlhladrlgLIPEGVFHPLWITDFPLfeatddggvtsSHHPFTAPDREDfdPGDIEElldlr 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 398 ---FELIVGGKELCNSFSELNDPVIQRQrleeqaALRQRGDDEAMIVDE--DFLRALEYGMPPCAGLGIGIDRLVMLLAG 472
Cdd:PRK12820 488 sraYDLVVNGEELGGGSIRINDKDIQLR------IFAALGLSEEDIEDKfgFFLRAFDFAAPPHGGIALGLDRVVSMILQ 561
|
570
....*....|.
gi 2173675722 473 QDSIRDVIFFP 483
Cdd:PRK12820 562 TPSIREVIAFP 572
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
42-483 |
8.66e-32 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 128.65 E-value: 8.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 42 QTVSVAGRIMAIRKMGKASFFNIQDSQGRIQIYIKRDevgQEAYRVFKLLDIGDIVGVKG-YSFRT--------KTGEIS 112
Cdd:PRK00476 18 QTVTLCGWVHRRRDHGGLIFIDLRDREGIVQVVFDPD---AEAFEVAESLRSEYVIQVTGtVRARPegtvnpnlPTGEIE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 113 IHAQEFMLLSKS--LrPIPIAKEKEVDgkkvtydafsdKELRYRQRYVDLiVNPEVRETFVKRSAIVSFMRTFLSSKGYL 190
Cdd:PRK00476 95 VLASELEVLNKSktL-PFPIDDEEDVS-----------EELRLKYRYLDL-RRPEMQKNLKLRSKVTSAIRNFLDDNGFL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 191 EVETPILqpiygGAA----ARpftthhnalDmelYL---RI-ANELY--------LKRLI-VGGFDGVFEFAKDFRNEGI 253
Cdd:PRK00476 162 EIETPIL-----TKStpegAR---------D---YLvpsRVhPGKFYalpqspqlFKQLLmVAGFDRYYQIARCFRDEDL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 254 --DRfhNPEFTQVEL---YVAYKDylwMMELVEELLYRTNLEVNGRDsvtfldheisLKPPFRRMTIAESINEY------ 322
Cdd:PRK00476 225 raDR--QPEFTQIDIemsFVTQED---VMALMEGLIRHVFKEVLGVD----------LPTPFPRMTYAEAMRRYgsdkpd 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 323 ---------CT-------------------------------------CD-----------------------ITG---K 330
Cdd:PRK00476 290 lrfglelvdVTdlfkdsgfkvfagaandggrvkairvpggaaqlsrkqIDeltefakiygakglayikvnedgLKGpiaK 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 331 N--EAELRNIAKDLGLEL---------DPKISS---GKIIDEIFGEF--VEPKLIQPTFITDYP-VEMSPLAKG----H- 388
Cdd:PRK00476 370 FlsEEELAALLERTGAKDgdliffgadKAKVVNdalGALRLKLGKELglIDEDKFAFLWVVDFPmFEYDEEEGRwvaaHh 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 389 ---RSKEGTVERFEL------------IVggkelCNSFsEL-------NDPVIQRQRLEeqaALrqrGDDEAMiVDEDF- 445
Cdd:PRK00476 450 pftMPKDEDLDELETtdpgkarayaydLV-----LNGY-ELgggsiriHRPEIQEKVFE---IL---GISEEE-AEEKFg 516
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2173675722 446 --LRALEYGMPPCAGLGIGIDRLVMLLAGQDSIRDVIFFP 483
Cdd:PRK00476 517 flLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
42-483 |
4.76e-30 |
|
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: 123.18 E-value: 4.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 42 QTVSVAGRIMAIRKMGKASFFNIQDSQGRIQIYIkRDEVGQEAYRVFKLLDIGDIVGVKGY-SFRT--------KTGEIS 112
Cdd:COG0173 17 QEVTLSGWVHRRRDHGGLIFIDLRDRYGITQVVF-DPDDSAEAFEKAEKLRSEYVIAVTGKvRARPegtvnpklPTGEIE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 113 IHAQEFMLLSKSLR-PIPIAKEKEVDgkkvtydafsdKELRYRQRYVDLiVNPEVRETFVKRSAIVSFMRTFLSSKGYLE 191
Cdd:COG0173 96 VLASELEILNKAKTpPFQIDDDTDVS-----------EELRLKYRYLDL-RRPEMQKNLILRHKVTKAIRNYLDENGFLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 192 VETPILqpiygGAA----ARpftthhnalDmelYL---RI-ANELY--------LKRLI-VGGFDGVFEFAKDFRNEGI- 253
Cdd:COG0173 164 IETPIL-----TKStpegAR---------D---YLvpsRVhPGKFYalpqspqlFKQLLmVSGFDRYFQIARCFRDEDLr 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 254 -DRfhNPEFTQVEL---YVAYKDylwMMELVEELLYRTNLEVNGrdsvtfldheISLKPPFRRMTIAESINEYCT----- 324
Cdd:COG0173 227 aDR--QPEFTQLDIemsFVDQED---VFELMEGLIRHLFKEVLG----------VELPTPFPRMTYAEAMERYGSdkpdl 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 325 ------CDIT------------------------------------------------------------------GKN- 331
Cdd:COG0173 292 rfglelVDVTdifkdsgfkvfagaaenggrvkainvpggaslsrkqideltefakqygakglayikvnedglkspiAKFl 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 332 -EAELRNIAKDLGLEL---------DPKI---SSGKIIDEIFGEF--VEPKLIQPTFITDYP-VEMSPLAKGHRS----- 390
Cdd:COG0173 372 sEEELAAILERLGAKPgdliffvadKPKVvnkALGALRLKLGKELglIDEDEFAFLWVVDFPlFEYDEEEGRWVAmhhpf 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 391 ---KEGTVERFEL-----------IVggkelCNSFsEL-------NDPVIQRQRLEeqaALRqRGDDEAmivDEDF---L 446
Cdd:COG0173 452 tmpKDEDLDLLETdpgkvrakaydLV-----LNGY-ELgggsiriHDPELQEKVFE---LLG-ISEEEA---EEKFgflL 518
|
570 580 590
....*....|....*....|....*....|....*..
gi 2173675722 447 RALEYGMPPCAGLGIGIDRLVMLLAGQDSIRDVIFFP 483
Cdd:COG0173 519 EAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
150-483 |
7.64e-30 |
|
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: 118.82 E-value: 7.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 150 ELRYRQRYVDLiVNPEVRETFVKRSAIVSFMRTFLSSKGYLEVETPIL--QPIYGGAaaRPFTTHHnaLDMELYLRIANE 227
Cdd:cd00776 5 ETLLDNRHLDL-RTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKItsTDTEGGA--ELFKVSY--FGKPAYLAQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 228 LYLKRLIvGGFDGVFEFAKDFRNEGID-RFHNPEFTQVELYVAY-KDYLWMMELVEELLYRT--NLEVNGRDSVTFLD-- 301
Cdd:cd00776 80 LYKEMLI-AALERVYEIGPVFRAEKSNtRRHLSEFWMLEAEMAFiEDYNEVMDLIEELIKYIfkRVLERCAKELELVNql 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 302 --HEISLKPPFRRMTIAESINeyctcditgkneaelrnIAKDLGLELDPK----ISSG---KIIDEIFGEFVepkliqpt 372
Cdd:cd00776 159 nrELLKPLEPFPRITYDEAIE-----------------LLREKGVEEEVKwgedLSTEherLLGEIVKGDPV-------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 373 FITDYPVEMSPL-AKGHRSKEGTVERFELIV-GGKELCnSFSelndpviQR-QRLEE-QAALRQRGDDEAMIvdEDFLRA 448
Cdd:cd00776 214 FVTDYPKEIKPFyMKPDDDNPETVESFDLLMpGVGEIV-GGS-------QRiHDYDElEERIKEHGLDPESF--EWYLDL 283
|
330 340 350
....*....|....*....|....*....|....*
gi 2173675722 449 LEYGMPPCAGLGIGIDRLVMLLAGQDSIRDVIFFP 483
Cdd:cd00776 284 RKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
170-483 |
1.07e-28 |
|
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: 114.59 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 170 FVKRSAIVSFMRTFLSSKGYLEVETPIL---QPiyGGAA-----ARPFTTHHNALDMelylriANELYLKRLIVGGFDGV 241
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILtksTP--EGARdflvpSRLHPGKFYALPQ------SPQLFKQLLMVSGFDRY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 242 FEFAKDFRNEGI--DRfhNPEFTQVELYVAYKDYLWMMELVEELLYRTNLEVNGRDsvtfldheisLKPPFRRMTIAESI 319
Cdd:cd00777 73 FQIARCFRDEDLraDR--QPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLGVE----------LTTPFPRMTYAEAM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 320 NEYctcditgkneaelrniakdlGLEldpkissgkiideifgefvepkliqPTFITDYPV-EMSPLAKGHRS-------- 390
Cdd:cd00777 141 ERY--------------------GFK-------------------------FLWIVDFPLfEWDEEEGRLVSahhpftap 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 391 KEGTVERFE------------LIVGGKELCNSFSELNDPVIQRQrleeqaALRQRGDDEAMIVDE--DFLRALEYGMPPC 456
Cdd:cd00777 176 KEEDLDLLEkdpedaraqaydLVLNGVELGGGSIRIHDPDIQEK------VFEILGLSEEEAEEKfgFLLEAFKYGAPPH 249
|
330 340
....*....|....*....|....*..
gi 2173675722 457 AGLGIGIDRLVMLLAGQDSIRDVIFFP 483
Cdd:cd00777 250 GGIALGLDRLVMLLTGSESIRDVIAFP 276
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
43-483 |
1.79e-27 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 116.04 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 43 TVSVAGRIMAIRKMGKASFFNIQDSQGRIQIYIKRDEVgQEAYRVFKLLDIGDIVGVKGY---------SFRTKTGEISI 113
Cdd:PLN02903 74 RVTLCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDEF-PEAHRTANRLRNEYVVAVEGTvrsrpqespNKKMKTGSVEV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 114 HAQEFMLLSKSLRPIPIAKEKEVDGKKVTydafsDKELRYRQRYVDLiVNPEVRETFVKRSAIVSFMRTFLSSK-GYLEV 192
Cdd:PLN02903 153 VAESVDILNVVTKSLPFLVTTADEQKDSI-----KEEVRLRYRVLDL-RRPQMNANLRLRHRVVKLIRRYLEDVhGFVEI 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 193 ETPILqpiyggaaARPftTHHNALDMELYLRI----------ANELYLKRLIVGGFDGVFEFAKDFRNEGIDRFHNPEFT 262
Cdd:PLN02903 227 ETPIL--------SRS--TPEGARDYLVPSRVqpgtfyalpqSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEFT 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 263 QVELYVAYKDYLWMMELVEELLYRTNLEVNGrdsvtfldheISLKPPFRRMTIAESINEYctcditGKNEAELR------ 336
Cdd:PLN02903 297 QLDMELAFTPLEDMLKLNEDLIRQVFKEIKG----------VQLPNPFPRLTYAEAMSKY------GSDKPDLRyglelv 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 337 ---------------------NIAKDLGLELDPKISSGKIID--EIFGEFVEPKLIQPTFI---TDYPVEMSP------- 383
Cdd:PLN02903 361 dvsdvfaessfkvfagalesgGVVKAICVPDGKKISNNTALKkgDIYNEAIKSGAKGLAFLkvlDDGELEGIKalvesls 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 384 --------------------LAKGHRSK-EGTVERFELIVgGKEL------------CNSFS--ELNDPviqRQRLE--- 425
Cdd:PLN02903 441 peqaeqllaacgagpgdlilFAAGPTSSvNKTLDRLRQFI-AKTLdlidpsrhsilwVTDFPmfEWNED---EQRLEalh 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 426 -------------------------------------------EQAALRQRG--DDEAmivDEDF---LRALEYGMPPCA 457
Cdd:PLN02903 517 hpftapnpedmgdlssaralaydmvyngveigggslriyrrdvQQKVLEAIGlsPEEA---ESKFgylLEALDMGAPPHG 593
|
570 580
....*....|....*....|....*.
gi 2173675722 458 GLGIGIDRLVMLLAGQDSIRDVIFFP 483
Cdd:PLN02903 594 GIAYGLDRLVMLLAGAKSIRDVIAFP 619
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
149-483 |
4.04e-22 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 97.01 E-value: 4.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 149 KELRYRQRYVDL-------IVNPEVRETFVKRSAIVSFMRTFLSSKGYLEVETPILQPI-----YGGAAARPFTTHHNAL 216
Cdd:PRK06462 2 DLERYPKEYEEFlrmswkhISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIISPStdplmGLGSDLPVKQISIDFY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 217 DMELYLRIANELYlKRLIVGGFDGVFEFAKDFRNEGIDRF---HNPEFTQVELYVAYKDYLWMMELVEELLYRT--NLEV 291
Cdd:PRK06462 82 GVEYYLADSMILH-KQLALRMLGKIFYLSPNFRLEPVDKDtgrHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLvkELLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 292 NGRDSVTFLDHEIS-LKPPFRRMTIAESINEYCTCDITGKNEAELRNIAKdlgleldpkissgKIIDEIFGEfvepkliq 370
Cdd:PRK06462 161 EHEDELEFFGRDLPhLKRPFKRITHKEAVEILNEEGCRGIDLEELGSEGE-------------KSLSEHFEE-------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 371 PTFITDYPVEMSPL-AKGHRSKEGTVERFELI--------VGGKELCNSFSElndpVIQRqrleeqaaLRQRGDDEAMIv 441
Cdd:PRK06462 220 PFWIIDIPKGSREFyDREDPERPGVLRNYDLLlpegygeaVSGGEREYEYEE----IVER--------IREHGVDPEKY- 286
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2173675722 442 dEDFLRALEYGMPPCAGLGIGIDRLVMLLAGQDSIRDVIFFP 483
Cdd:PRK06462 287 -KWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQPFP 327
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
42-483 |
4.29e-21 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 96.31 E-value: 4.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 42 QTVSVAGRIMAIRKMGKASFFNIQDSQGRIQ--IYIKRDEVGQEAYRVFKLL------DIGDIVGVKGYSFRTKTGEISI 113
Cdd:PLN02850 82 SEVLIRGRVHTIRGKGKSAFLVLRQSGFTVQcvVFVSEVTVSKGMVKYAKQLsresvvDVEGVVSVPKKPVKGTTQQVEI 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 114 HAQEFMLLSKSLRPIPIA--------KEKEVDGKKVTYDAFSDKELRYRQRYVDLIVnPEVRETFVKRSAIVSFMRTFLS 185
Cdd:PLN02850 162 QVRKIYCVSKALATLPFNvedaarseSEIEKALQTGEQLVRVGQDTRLNNRVLDLRT-PANQAIFRIQSQVCNLFREFLL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 186 SKGYLEVETP--ILQPIYGGAAArpFTTHHN------ALDMELYLRIAnelylkrlIVGGFDGVFEFAKDFRNEgiDRF- 256
Cdd:PLN02850 241 SKGFVEIHTPklIAGASEGGSAV--FRLDYKgqpaclAQSPQLHKQMA--------ICGDFRRVFEIGPVFRAE--DSFt 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 257 --HNPEFTQVELYVAYKD-YLWMMELVEELL----------YRTNLEVNGR----DSVTFLdheislkPPFRRMTIAESI 319
Cdd:PLN02850 309 hrHLCEFTGLDLEMEIKEhYSEVLDVVDELFvaifdglnerCKKELEAIREqypfEPLKYL-------PKTLRLTFAEGI 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 320 NEYctcditgKNEAELRNIAKDLGLELDPKIssGKIIDEIFG-EFvepkliqptFITD-YPVEMSPLAKGHRSKEGTVER 397
Cdd:PLN02850 382 QML-------KEAGVEVDPLGDLNTESERKL--GQLVKEKYGtDF---------YILHrYPLAVRPFYTMPCPDDPKYSN 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 398 -FELIVGGKELCNSFSELNDPVIQRQRLEEqaalrqRGDDEAMIvdEDFLRALEYGMPPCAGLGIGIDRLVMLLAGQDSI 476
Cdd:PLN02850 444 sFDVFIRGEEIISGAQRVHDPELLEKRAEE------CGIDVKTI--STYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNI 515
|
....*..
gi 2173675722 477 RDVIFFP 483
Cdd:PLN02850 516 RKTSLFP 522
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
43-123 |
1.57e-17 |
|
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: 77.22 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 43 TVSVAGRIMAIRKMGKASFFNIQDSQGRIQIYIKRDEVGqEAYRVFKLLDIGDIVGVKGYSFRT-----KTGEISIHAQE 117
Cdd:cd04100 1 EVTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEELG-EFFEEAEKLRTESVVGVTGTVVKRpegnlATGEIELQAEE 79
|
....*.
gi 2173675722 118 FMLLSK 123
Cdd:cd04100 80 LEVLSK 85
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
44-121 |
2.74e-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: 73.42 E-value: 2.74e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2173675722 44 VSVAGRIMAI-RKMGKASFFNIQDSQGRIQIYIKRDEvgqeAYRVFKLLDIGDIVGVKGYSFRTKTGEISIHAQEFMLL 121
Cdd:pfam01336 1 VTVAGRVTSIrRSGGKLLFLTLRDGTGSIQVVVFKEE----AEKLAKKLKEGDVVRVTGKVKKRKGGELELVVEEIELL 75
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
173-284 |
4.00e-16 |
|
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: 77.16 E-value: 4.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 173 RSAIVSFMRTFLSSKGYLEVETPILQPIYGGAAAR----PFTTHHNALDMELYLRIANELYLKRLIVG----GFDGVFEF 244
Cdd:cd00768 2 RSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGhepkDLLPVGAENEEDLYLRPTLEPGLVRLFVShirkLPLRLAEI 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2173675722 245 AKDFRNEGIDRF--HNPEFTQVELYVAYKDYLW------MMELVEELL 284
Cdd:cd00768 82 GPAFRNEGGRRGlrRVREFTQLEGEVFGEDGEEasefeeLIELTEELL 129
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
37-483 |
2.29e-14 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 75.41 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 37 DENSPQTVSVAGRIMAIRKMGKASFFNIQDSQGRIQIYIK-RDEVGQEAYRVFKLLDIGDIVGVKGYSFR-------TKT 108
Cdd:PTZ00401 74 PELVDKTVLIRARVSTTRKKGKMAFMVLRDGSDSVQAMAAvEGDVPKEMIDFIGQIPTESIVDVEATVCKveqpitsTSH 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 109 GEISIHAQEFMLLSKSLRPIPI----AKEKEVD-GKKVTYDAfsdkelRYRQRYVDLiVNPEVRETFVKRSAIVSFMRTF 183
Cdd:PTZ00401 154 SDIELKVKKIHTVTESLRTLPFtledASRKESDeGAKVNFDT------RLNSRWMDL-RTPASGAIFRLQSRVCQYFRQF 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 184 LSSKGYLEVETP--ILQPIYGGAAArpFTTHHnaLDMELYLRIANELYLKRLIVGGFDGVFEFAKDFRNEGIDRF-HNPE 260
Cdd:PTZ00401 227 LIDSDFCEIHSPkiINAPSEGGANV--FKLEY--FNRFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNTHrHLTE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 261 FT--QVELYVAyKDYLWMMELVEELLYRTNLEVNGRDS-VTFLDHEISLKPPFRRMTiAESINEYCTCDI------TGKN 331
Cdd:PTZ00401 303 FVglDVEMRIN-EHYYEVLDLAESLFNYIFERLATHTKeLKAVCQQYPFEPLVWKLT-PERMKELGVGVIsegvepTDKY 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 332 EAELRNIAKD------------LGLELDPKISSGKII----DEIFGEFVEPKLIQPTFITD-YPVEMSPL-AKGHRSKEG 393
Cdd:PTZ00401 381 QARVHNMDSRmlrinymhcielLNTVLEEKMAPTDDInttnEKLLGKLVKERYGTDFFISDrFPSSARPFyTMECKDDER 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 394 TVERFELIVGGKELCNSFSELNDPVIQRQRLeeqaalrqrgddEAMIVD----EDFLRALEYGMPPCAGLGIGIDRLVML 469
Cdd:PTZ00401 461 FTNSYDMFIRGEEISSGAQRIHDPDLLLARA------------KMLNVDltpiKEYVDSFRLGAWPHGGFGVGLERVVML 528
|
490
....*....|....
gi 2173675722 470 LAGQDSIRDVIFFP 483
Cdd:PTZ00401 529 YLGLSNVRLASLFP 542
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
32-485 |
1.51e-11 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 66.28 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 32 IKEQFDENSP-QTVSVAGRIMAIRKMGKASFFNIQDSQGRIQIYIKRDEvGQEAYRVFKLLDIGDIVGVKG---YSFRTK 107
Cdd:PRK03932 6 IKDILKGKYVgQEVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDN-GEEYFEEIKKLTTGSSVIVTGtvvESPRAG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 108 TGeISIHAQEFMLLSKSLRPIPIAKekevdgKKVTYDAFSD-KELRYRQRyvdlivnpEVRETFVKRSAIVSFMRTFLSS 186
Cdd:PRK03932 85 QG-YELQATKIEVIGEDPEDYPIQK------KRHSIEFLREiAHLRPRTN--------KFGAVMRIRNTLAQAIHEFFNE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 187 KGYLEVETPILQPIYGGAAARPFTTHHNALDM-------ELYLRIANELYLKRLIVGgFDGVFEFAKDFRNEGID-RFHN 258
Cdd:PRK03932 150 NGFVWVDTPIITASDCEGAGELFRVTTLDLDFskdffgkEAYLTVSGQLYAEAYAMA-LGKVYTFGPTFRAENSNtRRHL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 259 PEFTQVELYVAYKDYLWMMELVEELLY---RTNLEvNGRDSVTFLDHEIS----------LKPPFRRMTIAESINeyctc 325
Cdd:PRK03932 229 AEFWMIEPEMAFADLEDNMDLAEEMLKyvvKYVLE-NCPDDLEFLNRRVDkgdierlenfIESPFPRITYTEAIE----- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 326 ditgkneaelrnIAKDLGLELDPKISSGK---------IIDEIFGefvepkliQPTFITDYPVE-----MSPLAKGhrsk 391
Cdd:PRK03932 303 ------------ILQKSGKKFEFPVEWGDdlgseheryLAEEHFK--------KPVFVTNYPKDikafyMRLNPDG---- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 392 eGTVERFEL-------IVGGKelcnsfselndpviqrQRLEEQAALRQRGDDEAMIVdEDF-----LRalEYGMPPCAGL 459
Cdd:PRK03932 359 -KTVAAMDLlapgigeIIGGS----------------QREERLDVLEARIKELGLNK-EDYwwyldLR--RYGSVPHSGF 418
|
490 500
....*....|....*....|....*.
gi 2173675722 460 GIGIDRLVMLLAGQDSIRDVIFFPHM 485
Cdd:PRK03932 419 GLGFERLVAYITGLDNIRDVIPFPRT 444
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
42-160 |
2.75e-09 |
|
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli aspartyl-tRNA synthetase (AspRS), the human mitochondrial (mt) AspRS-2, the discriminating (D) Thermus thermophilus AspRS-1, and the nondiscriminating (ND) Helicobacter pylori AspRS. These homodimeric enzymes are class2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. Human mtAspRS participates in mitochondrial biosynthesis; this enzyme been shown to charge E.coli native tRNAsp in addition to in vitro transcribed human mitochondrial tRNAsp. T. thermophilus is rare among bacteria in having both a D_AspRS and a ND_AspRS. H.pylori ND-AspRS can charge both tRNAASp and tRNAAsn, it is fractionally more efficient at aminoacylating tRNAAsp over tRNAAsn. The H.pylori genome does not contain AsnRS.
Pssm-ID: 239812 [Multi-domain] Cd Length: 135 Bit Score: 55.22 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 42 QTVSVAGRIMAIRKMGKASFFNIQDSQGRIQIYIKRDEvgQEAYRVFKLLDIGDIVGVKG-YSFRT--------KTGEIS 112
Cdd:cd04317 15 QEVTLCGWVQRRRDHGGLIFIDLRDRYGIVQVVFDPEE--APEFELAEKLRNESVIQVTGkVRARPegtvnpklPTGEIE 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2173675722 113 IHAQEFMLLSKSLR-PIPIAKEKEVdgkkvtydafsDKELRYRQRYVDL 160
Cdd:cd04317 93 VVASELEVLNKAKTlPFEIDDDVNV-----------SEELRLKYRYLDL 130
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
28-130 |
4.78e-09 |
|
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: 53.86 E-value: 4.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 28 YSRQIKEqfdENSPQTVSVAGRIMAIRKMGKASFFNIQDSQGRIQIYIKRDEVGQEAYRVFKLLDIGDIVGVKG---YSF 104
Cdd:cd04316 2 YSAEITP---ELDGEEVTVAGWVHEIRDLGGIKFVILRDREGIVQVTAPKKKVDKELFKTVRKLSRESVISVTGtvkAEP 78
|
90 100
....*....|....*....|....*.
gi 2173675722 105 RTKTGeISIHAQEFMLLSKSLRPIPI 130
Cdd:cd04316 79 KAPNG-VEIIPEEIEVLSEAKTPLPL 103
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
219-483 |
3.31e-07 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 52.72 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 219 ELYLRIANELYLKRLIVGGFDgVFEFAKDFR--NEGIDRfHNPEFTQVELYVAYKDYLWMMELVEELL-----YRTNlev 291
Cdd:PTZ00425 325 QAFLTVSGQLSLENLCSSMGD-VYTFGPTFRaeNSHTSR-HLAEFWMIEPEIAFADLYDNMELAESYIkycigYVLN--- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 292 NGRDSVTFLDHEISLKPPFRRMTIaesINEYCTcDITGKNEAELRNIAKDlglELDPKISSGKIIDEIFGEFVEPKLIQ- 370
Cdd:PTZ00425 400 NNFDDIYYFEENVETGLISRLKNI---LDEDFA-KITYTNVIDLLQPYSD---SFEVPVKWGMDLQSEHERFVAEQIFKk 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 371 PTFITDYPVEMSPLAKGHRSKEGTVERFELIV-------GGKELCNSFSELNDPVIQRQ-RLEEQAALRQrgddeamivd 442
Cdd:PTZ00425 473 PVIVYNYPKDLKAFYMKLNEDQKTVAAMDVLVpkigeviGGSQREDNLERLDKMIKEKKlNMESYWWYRQ---------- 542
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2173675722 443 edfLRalEYGMPPCAGLGIGIDRLVMLLAGQDSIRDVIFFP 483
Cdd:PTZ00425 543 ---LR--KFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFP 578
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
355-483 |
1.88e-06 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 50.36 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 355 IIDEIFGEfvepkliQPTFITDYPVEMSPLAKGHRSKEGTVERFELIVggkelcnsfSELNDPVIQRQRLEEQAALRQRg 434
Cdd:PLN02603 443 ITEEAFGG-------RPVIIRDYPKEIKAFYMRENDDGKTVAAMDMLV---------PRVGELIGGSQREERLEYLEAR- 505
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2173675722 435 DDEAMIVDEDFLRALE---YGMPPCAGLGIGIDRLVMLLAGQDSIRDVIFFP 483
Cdd:PLN02603 506 LDELKLNKESYWWYLDlrrYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFP 557
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
241-483 |
7.73e-06 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 48.45 E-value: 7.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 241 VFEFAKDFR--NEGIDRfHNPEFTQVELYVAYKD-------------YL--WMMELVeellyRTNLEVNGR--DSVTFLD 301
Cdd:PLN02221 329 VYTFGPTFRaeNSHTSR-HLAEFWMVEPEIAFADleddmncaeayvkYMckWLLDKC-----FDDMELMAKnfDSGCIDR 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 302 HEISLKPPFRRMTIAESIneyctcditgkneaELRNIAKDLGLELDPKISSGKIIDEIFGEFVEPKLIQ-PTFITDYPVE 380
Cdd:PLN02221 403 LRMVASTPFGRITYTEAI--------------ELLEEAVAKGKEFDNNVEWGIDLASEHERYLTEVLFQkPLIVYNYPKG 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 381 MSPLAKGHRSKEGTVERFELIVggkelcnsfSELNDPVIQRQRLEEQAALRQRGDDEAMIVD--EDFLRALEYGMPPCAG 458
Cdd:PLN02221 469 IKAFYMRLNDDEKTVAAMDVLV---------PKVGELIGGSQREERYDVIKQRIEEMGLPIEpyEWYLDLRRYGTVKHCG 539
|
250 260
....*....|....*....|....*
gi 2173675722 459 LGIGIDRLVMLLAGQDSIRDVIFFP 483
Cdd:PLN02221 540 FGLGFERMILFATGIDNIRDVIPFP 564
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
241-483 |
8.24e-04 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 41.78 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 241 VFEFAKDFRNEGIDRF-HNPEFTQVELYVAYKDYLWMMELVEE---LLYRTNLEvNGRDSVTFLDHEI----------SL 306
Cdd:PLN02532 392 VYTFGPRFRADRIDSArHLAEMWMVEVEMAFSELEDAMNCAEDyfkFLCKWVLE-NCSEDMKFVSKRIdktistrleaII 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 307 KPPFRRMTIAESINEYCTCdITGKNEAELrniakDLGLELDPKISSgKIIDEIFGefvepkliQPTFITDYPVEMSPLAK 386
Cdd:PLN02532 471 SSSLQRISYTEAVDLLKQA-TDKKFETKP-----EWGIALTTEHLS-YLADEIYK--------KPVIIYNYPKELKPFYV 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173675722 387 GHRSKEGTVERFELIV--GGKELCNSFSE---------LNDPVIQRQRLEEQAALRQRGDDEAmivdedflraleygmpp 455
Cdd:PLN02532 536 RLNDDGKTVAAFDLVVpkVGTVITGSQNEermdilnarIEELGLPREQYEWYLDLRRHGTVKH----------------- 598
|
250 260
....*....|....*....|....*...
gi 2173675722 456 cAGLGIGIDRLVMLLAGQDSIRDVIFFP 483
Cdd:PLN02532 599 -SGFSLGFELMVLFATGLPDVRDAIPFP 625
|
|
| |
