|
Name |
Accession |
Description |
Interval |
E-value |
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
23-442 |
0e+00 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 644.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 23 EGTEVKLEGAVHIIRDMGEVAFVILRKSEGLVQCVYEEGSVDFP---LKDLKEESAVAVTGTVKKEDRAPGGVEVRLQTI 99
Cdd:PRK05159 15 DGEEVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKVDEELfetIKKLKRESVVSVTGTVKANPKAPGGVEVIPEEI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 100 TVLSEPTEPMPLAVNKWKMNTsLEAMLNMRPIALRNVRERAKFRIQEGVVRAFRDFLHSQGFTEIHTPKIGAKGAEGGAN 179
Cdd:PRK05159 95 EVLNKAEEPLPLDISGKVLAE-LDTRLDNRFLDLRRPRVRAIFKIRSEVLRAFREFLYENGFTEIFTPKIVASGTEGGAE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 180 IFKLEYFHRPAVLAQSPQFYKQMLVGV-FDRVFEVGPVFRAEKHNTKRHLNEYTSLDFEMGYIEDYTDIMAMETGFLQYM 258
Cdd:PRK05159 174 LFPIDYFEKEAYLAQSPQLYKQMMVGAgFERVFEIGPVFRAEEHNTSRHLNEYTSIDVEMGFIDDHEDVMDLLENLLRYM 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 259 VELLKKDYAKELEILKVMLPKTE-EIPTVPFTKAKELVAEKYNrKIRNPFDLEPEEELLIGQYFKEEYDADFVFVTEYPS 337
Cdd:PRK05159 254 YEDVAENCEKELELLGIELPVPEtPIPRITYDEAIEILKSKGN-EISWGDDLDTEGERLLGEYVKEEYGSDFYFITDYPS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 338 KKRPFYAMDDPEDKRYTKSFDLLFHGLEITTGGQRIHDYKMLSEKIAARGMTEEGMEQYLSAFKHGMPPHGGLGIGLERL 417
Cdd:PRK05159 333 EKRPFYTMPDEDDPEISKSFDLLFRGLEITSGGQRIHRYDMLVESIKEKGLNPESFEFYLEAFKYGMPPHGGFGLGLERL 412
|
410 420
....*....|....*....|....*
gi 941897655 418 TMKLIGEDNVRETTLFPRDLTRLEP 442
Cdd:PRK05159 413 TMKLLGLENIREAVLFPRDRHRLTP 437
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
11-442 |
0e+00 |
|
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: 531.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 11 EDISVKTLLEIPEGTEVKLEGAVHIIRDMGEVAFVILRKSEGLVQCVYEEGSVD--FPLKDLKEESAVAVTGTVKKEDRA 88
Cdd:COG0017 1 KRTYIKDLLPEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKLEnfEEAKKLTTESSVEVTGTVVESPRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 89 PGGVEVRLQTITVLSEPTEPMPLAVNKwkmnTSLEAMLNMRPIALRNVRERAKFRIQEGVVRAFRDFLHSQGFTEIHTPK 168
Cdd:COG0017 81 PQGVELQAEEIEVLGEADEPYPLQPKR----HSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVEVHTPI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 169 IGAKGAEGGANIFKLEYFHRPAVLAQSPQFYKQMLVGVFDRVFEVGPVFRAEKHNTKRHLNEYTSLDFEMGYIeDYTDIM 248
Cdd:COG0017 157 ITASATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMALEKVYTFGPTFRAEKSNTRRHLAEFWMIEPEMAFA-DLEDVM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 249 AMETGFLQYMVELLKKDYAKELEILKVMLPKTEEIPTVPF-----TKAKELVaEKYNRKIRNPFDLEPEEELLIGqyfkE 323
Cdd:COG0017 236 DLAEEMLKYIIKYVLENCPEELEFLGRDVERLEKVPESPFprityTEAIEIL-KKSGEKVEWGDDLGTEHERYLG----E 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 324 EYDADFVFVTEYPSKKRPFYAMDDPEDKRYTKSFDLLFHGL-EITTGGQRIHDYKMLSEKIAARGMTEEGMEQYLSAFKH 402
Cdd:COG0017 311 EFFKKPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAPGIgEIIGGSQREHRYDVLVERIKEKGLDPEDYEWYLDLRRY 390
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 941897655 403 GMPPHGGLGIGLERLTMKLIGEDNVRETTLFPRDLTRLEP 442
Cdd:COG0017 391 GSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
121-436 |
2.47e-131 |
|
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: 381.53 E-value: 2.47e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 121 SLEAMLNMRPIALRNVRERAKFRIQEGVVRAFRDFLHSQGFTEIHTPKIGAKGAEGGANIFKLEYFHRPAVLAQSPQFYK 200
Cdd:cd00776 3 NLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQLYK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 201 QMLVGVFDRVFEVGPVFRAEKHNTKRHLNEYTSLDFEMGYIEDYTDIMAMETGFLQYMVELLKKDYAKELEILKVM---- 276
Cdd:cd00776 83 EMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEDYNEVMDLIEELIKYIFKRVLERCAKELELVNQLnrel 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 277 LPKTEEIPTVPFTKAKELVAEKYNRKIRNPF-DLEPEEELLIGQYFKEeydaDFVFVTEYPSKKRPFYAMDDPEDKRYTK 355
Cdd:cd00776 163 LKPLEPFPRITYDEAIELLREKGVEEEVKWGeDLSTEHERLLGEIVKG----DPVFVTDYPKEIKPFYMKPDDDNPETVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 356 SFDLLFHG-LEITTGGQRIHDYKMLSEKIAARGMTEEGMEQYLSAFKHGMPPHGGLGIGLERLTMKLIGEDNVRETTLFP 434
Cdd:cd00776 239 SFDLLMPGvGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
..
gi 941897655 435 RD 436
Cdd:cd00776 319 RD 320
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
23-442 |
2.47e-128 |
|
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: 378.01 E-value: 2.47e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 23 EGTEVKLEGAVHIIRDMGEVAFVILRKSEGLVQCVYEEGSVDFPL----KDLKEESAVAVTGTVKKEDRAPGGVEVRLQT 98
Cdd:TIGR00458 11 DGQEVTFMGWVHEIRDLGGLIFVLLRDREGLIQITAPAKKVSKNLfkwaKKLNLESVVAVRGIVKIKEKAPGGFEIIPTK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 99 ITVLSEPTEPMPLAVNKwKMNTSLEAMLNMRPIALRNVRERAKFRIQEGVVRAFRDFLHSQGFTEIHTPKIGAKGAEGGA 178
Cdd:TIGR00458 91 IEVINEAKEPLPLDPTE-KVPAELDTRLDYRFLDLRRPTVQAIFRIRSGVLESVREFLAEEGFIEVHTPKLVASATEGGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 179 NIFKLEYFHRPAVLAQSPQFYKQMLVGV-FDRVFEVGPVFRAEKHNTKRHLNEYTSLDFEMGYiEDYTDIMAMETGFLQY 257
Cdd:TIGR00458 170 ELFPITYFEREAFLGQSPQLYKQQLMAAgFERVYEIGPIFRAEEHNTHRHLNEATSIDIEMAF-EDHHDVMDILEELVVR 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 258 MVELLKKDYAKELEILKVMLPKTEE-IPTVPFTKAKELVAEKyNRKIRNPFDLEPEEELLIGqyfkEEYDADFvFVTEYP 336
Cdd:TIGR00458 249 VFEDVPERCAHQLETLEFKLEKPEGkFVRLTYDEAIEMANAK-GVEIGWGEDLSTEAEKALG----EEMDGLY-FITDWP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 337 SKKRPFYAMDDPEDKRYTKSFDLLFHGLEITTGGQRIHDYKMLSEKIAARGMTEEGMEQYLSAFKHGMPPHGGLGIGLER 416
Cdd:TIGR00458 323 TEIRPFYTMPDEDNPEISKSFDLMYRDLEISSGAQRIHLHDLLVERIKAKGLNPEGFKDYLEAFSYGMPPHAGWGLGAER 402
|
410 420
....*....|....*....|....*.
gi 941897655 417 LTMKLIGEDNVRETTLFPRDLTRLEP 442
Cdd:TIGR00458 403 FVMFLLGLKNIREAVLFPRDRKRLTP 428
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
7-442 |
1.33e-119 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 359.02 E-value: 1.33e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 7 VKKKEDISVKTLLEIPEGTEVKLEGAVHIIRDMGEVAFVILRKSEGLVQCVYEEGSVDFP------LKDLKEESAVAVTG 80
Cdd:PLN02850 64 VTGREWTDVSDLGEELAGSEVLIRGRVHTIRGKGKSAFLVLRQSGFTVQCVVFVSEVTVSkgmvkyAKQLSRESVVDVEG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 81 TVKKEDRAPGG----VEVRLQTITVLSEPTEPMPLAV-----NKWKMNTSLEA-----------MLNMRPIALRNVRERA 140
Cdd:PLN02850 144 VVSVPKKPVKGttqqVEIQVRKIYCVSKALATLPFNVedaarSESEIEKALQTgeqlvrvgqdtRLNNRVLDLRTPANQA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 141 KFRIQEGVVRAFRDFLHSQGFTEIHTPKIGAKGAEGGANIFKLEYFHRPAVLAQSPQFYKQMLV-GVFDRVFEVGPVFRA 219
Cdd:PLN02850 224 IFRIQSQVCNLFREFLLSKGFVEIHTPKLIAGASEGGSAVFRLDYKGQPACLAQSPQLHKQMAIcGDFRRVFEIGPVFRA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 220 EKHNTKRHLNEYTSLDFEMGYIEDYTDIMAMETGFLQYMVELLKKDYAKELEILK--------VMLPKTEEIPtvpFTKA 291
Cdd:PLN02850 304 EDSFTHRHLCEFTGLDLEMEIKEHYSEVLDVVDELFVAIFDGLNERCKKELEAIReqypfeplKYLPKTLRLT---FAEG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 292 KELVAEKyNRKIRNPFDLEPEEELLIGQYFKEEYDADFVFVTEYPSKKRPFYAMDDPEDKRYTKSFDLLFHGLEITTGGQ 371
Cdd:PLN02850 381 IQMLKEA-GVEVDPLGDLNTESERKLGQLVKEKYGTDFYILHRYPLAVRPFYTMPCPDDPKYSNSFDVFIRGEEIISGAQ 459
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 941897655 372 RIHDYKMLSEKIAARGMTEEGMEQYLSAFKHGMPPHGGLGIGLERLTMKLIGEDNVRETTLFPRDLTRLEP 442
Cdd:PLN02850 460 RVHDPELLEKRAEECGIDVKTISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPRDPQRLAP 530
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
121-436 |
7.52e-96 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 290.62 E-value: 7.52e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 121 SLEAMLNMRPIALRNVRERAKFRIQEGVVRAFRDFLHSQGFTEIHTPKIGAKGAEGGANIFKL------EYFHrpavLAQ 194
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVpsralgKFYA----LPQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 195 SPQFYKQML-VGVFDRVFEVGPVFRAEKHNTKRHLnEYTSLDFEMGYIeDYTDIMAMETGFLQYMVELLKKDYAKELEIL 273
Cdd:pfam00152 77 SPQLYKQLLmVAGFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFV-DYEDVMDLTEELIKEIFKEVEGIAKELEGGT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 274 KVMLPKTeeIPTVPFTKAKELVAEKYNRKirNPFDLEPEEELLIGQYFKEEYDADFVFVTEYPSKKRPFYAMDDPEDKRY 353
Cdd:pfam00152 155 LLDLKKP--FPRITYAEAIEKLNGKDVEE--LGYGSDKPDLRFLLELVIDKNKFNPLWVTDFPAEHHPFTMPKDEDDPAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 354 TKSFDLLFHGLEITTGGQRIHDYKMLSEKIAARGMTEEGMEQ----YLSAFKHGMPPHGGLGIGLERLTMKLIGEDNVRE 429
Cdd:pfam00152 231 AEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDPEEAEEkfgfYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIRE 310
|
....*..
gi 941897655 430 TTLFPRD 436
Cdd:pfam00152 311 VIAFPKT 317
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
27-442 |
9.11e-89 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 280.34 E-value: 9.11e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 27 VKLEGAVHIIRDMGEVAFVILRKSEGLVQCVYE-EGSV-----DFpLKDLKEESAVAVTGTVKKEDR-----APGGVEVR 95
Cdd:PTZ00401 81 VLIRARVSTTRKKGKMAFMVLRDGSDSVQAMAAvEGDVpkemiDF-IGQIPTESIVDVEATVCKVEQpitstSHSDIELK 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 96 LQTITVLSEPTEPMPLAVNKWKMNTSLEAM-------LNMRPIALRNVRERAKFRIQEGVVRAFRDFLHSQGFTEIHTPK 168
Cdd:PTZ00401 160 VKKIHTVTESLRTLPFTLEDASRKESDEGAkvnfdtrLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLIDSDFCEIHSPK 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 169 IGAKGAEGGANIFKLEYFHRPAVLAQSPQFYKQM-LVGVFDRVFEVGPVFRAEKHNTKRHLNEYTSLDFEMGYIEDYTDI 247
Cdd:PTZ00401 240 IINAPSEGGANVFKLEYFNRFAYLAQSPQLYKQMvLQGDVPRVFEVGPVFRSENSNTHRHLTEFVGLDVEMRINEHYYEV 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 248 MAMETGFLQYMVELLKKdYAKELEILKVMLPKTEEIPTVPFTKAKEL----------VAEKYNRKIRN------------ 305
Cdd:PTZ00401 320 LDLAESLFNYIFERLAT-HTKELKAVCQQYPFEPLVWKLTPERMKELgvgvisegvePTDKYQARVHNmdsrmlrinymh 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 306 ---------------PFDLEPEEELLIGQYFKEEYDADFVFVTEYPSKKRPFYAMDDPEDKRYTKSFDLLFHGLEITTGG 370
Cdd:PTZ00401 399 ciellntvleekmapTDDINTTNEKLLGKLVKERYGTDFFISDRFPSSARPFYTMECKDDERFTNSYDMFIRGEEISSGA 478
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 941897655 371 QRIHDYKMLSEKIAARGMTEEGMEQYLSAFKHGMPPHGGLGIGLERLTMKLIGEDNVRETTLFPRDLTRLEP 442
Cdd:PTZ00401 479 QRIHDPDLLLARAKMLNVDLTPIKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFPRDPQRTTP 550
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
10-442 |
1.18e-77 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 248.48 E-value: 1.18e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 10 KEDISVKTLLEIPE-GTEVKLEGAVHIIRDMGEVAFVILRKSEGL--VQCVYEEGSVDFP-LKDLKEESAVAVTGTVKKE 85
Cdd:PRK03932 1 MMRVSIKDILKGKYvGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFkqLQVVKDNGEEYFEeIKKLTTGSSVIVTGTVVES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 86 DRAPGGVEVRLQTITVLSEPTEPMPLAvnkwKMNTSLEAMLNMRPIALRNVRERAKFRIQEGVVRAFRDFLHSQGFTEIH 165
Cdd:PRK03932 81 PRAGQGYELQATKIEVIGEDPEDYPIQ----KKRHSIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 166 TPKIGAKGAEGGANIFKL---------EYFHRPAVLAQSPQFYKQMLVGVFDRVFEVGPVFRAEKHNTKRHLNEYTSLDF 236
Cdd:PRK03932 157 TPIITASDCEGAGELFRVttldldfskDFFGKEAYLTVSGQLYAEAYAMALGKVYTFGPTFRAENSNTRRHLAEFWMIEP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 237 EMGYIeDYTDIMAMETGFLQYMVELLKKDYAKELEIL-----KVMLPKTEEIPTVPF-----TKAKELVaEKYNRKIRNP 306
Cdd:PRK03932 237 EMAFA-DLEDNMDLAEEMLKYVVKYVLENCPDDLEFLnrrvdKGDIERLENFIESPFprityTEAIEIL-QKSGKKFEFP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 307 F----DLEPEEElligQYFKEEYdadF---VFVTEYPSKKRPFYAMDDPEDKRyTKSFDLLFHGL-EITTGGQRIHDYKM 378
Cdd:PRK03932 315 VewgdDLGSEHE----RYLAEEH---FkkpVFVTNYPKDIKAFYMRLNPDGKT-VAAMDLLAPGIgEIIGGSQREERLDV 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 941897655 379 LSEKIAARGMTEEGMEQYLSAFKHGMPPHGGLGIGLERLTMKLIGEDNVRETTLFPRDLTRLEP 442
Cdd:PRK03932 387 LEARIKELGLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
14-442 |
1.87e-77 |
|
asparaginyl-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, asnS, represents asparaginyl-tRNA synthetases from the three domains of life. Some species lack this enzyme and charge tRNA(asn) by misacylation with Asp, followed by transamidation of Asp to Asn. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273086 [Multi-domain] Cd Length: 453 Bit Score: 248.06 E-value: 1.87e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 14 SVKTLLEIPE---GTEVKLEGAVHIIRDMGEVAFVILR--KSEGLVQCV---YEEGSVDFPLKDLKEESAVAVTGTVKKE 85
Cdd:TIGR00457 3 AIKDLLQQVYkfvGDEVTVSGWVRTKRSSKKIIFLELNdgSSLGPIQAVingEDNPYLFQLLKSLTTGSSVSVTGKVVES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 86 DRAPGGVEVRLQTITVLSE-PTEPMPLAvnkwKMNTSLEAMLNMRPIALRNVRERAKFRIQEGVVRAFRDFLHSQGFTEI 164
Cdd:TIGR00457 83 PGKGQPVELQVKKIEVVGEaEPDDYPLQ----KKEHSLEFLRDIAHLRLRTNTLGAVMRVRNALSQAIHRYFQENGFTWV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 165 HTPKIGAKGAEGGANIFKL---------EYFHRPAVLAQSPQFYKQMLVGVFDRVFEVGPVFRAEKHNTKRHLNEYTSLD 235
Cdd:TIGR00457 159 SPPILTSNDCEGAGELFRVstgnidfsqDFFGKEAYLTVSGQLYLETYALALSKVYTFGPTFRAEKSNTSRHLSEFWMIE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 236 FEMGYIeDYTDIMAMETGFLQYMVELLKKDYAKELEIL-----KVMLPKTEEI-----PTVPFTKAKELVAEKYNRKIRN 305
Cdd:TIGR00457 239 PEMAFA-NLNDLLQLAETLIKYIIKAVLENCSQELKFLeknfdKDLIKRLENIinnkfARITYTDAIEILKESDKNFEYE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 306 PF---DLEPEEElligQYFKEEYDADFVFVTEYPSKKRPFYaMDDPEDKRYTKSFDLLFHGL-EITTGGQRIHDYKMLSE 381
Cdd:TIGR00457 318 DFwgdDLQTEHE----RFLAEEYFKPPVFVTNYPKDIKAFY-MKLNDDGKTVAAMDLLAPGIgEIIGGSEREDDLDKLEN 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 941897655 382 KIAARGMTEEGMEQYLSAFKHGMPPHGGLGIGLERLTMKLIGEDNVRETTLFPRDLTRLEP 442
Cdd:TIGR00457 393 RMKEMGLDTDALNWYLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGNINF 453
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
142-436 |
1.99e-59 |
|
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: 195.39 E-value: 1.99e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 142 FRIQEGVVRAFRDFLHSQGFTEIHTPKIGAKGAEGGANIFKLEYFHRP--AVLAQSPQFYKQML-VGVFDRVFEVGPVFR 218
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGldYYLRISPQLFKKRLmVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 219 AEkHNTKRHLNEYTSLDFEMGYIeDYTDIMAMETGFLQYMVELLKKDYAKELEILKVMLPKteEIPTVPFTKAKElvaek 298
Cdd:cd00669 81 NE-DLRARHQPEFTMMDLEMAFA-DYEDVIELTERLVRHLAREVLGVTAVTYGFELEDFGL--PFPRLTYREALE----- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 299 ynrKIRNPFdlepeeelligqyfkeeydadfvFVTEYPSKKRPFYAMDDPEDKRYTKSFDLLFHGLEITTGGQRIHDYKM 378
Cdd:cd00669 152 ---RYGQPL-----------------------FLTDYPAEMHSPLASPHDVNPEIADAFDLFINGVEVGNGSSRLHDPDI 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 941897655 379 LSEKIAARGMTEE-GMEQ---YLSAFKHGMPPHGGLGIGLERLTMKLIGEDNVRETTLFPRD 436
Cdd:cd00669 206 QAEVFQEQGINKEaGMEYfefYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKM 267
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
142-435 |
1.48e-45 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 160.96 E-value: 1.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 142 FRIQEGVVRAFRDFLHSQGFTEIHTPKIGA-------KGAEGGANIFKLEYFHRPAVLAQSPQFYKQMLVGVFDRVFEVG 214
Cdd:PRK06462 30 LKVQSSILRYTREFLDGRGFVEVLPPIISPstdplmgLGSDLPVKQISIDFYGVEYYLADSMILHKQLALRMLGKIFYLS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 215 PVFRAE--KHNTKRHLNEYTSLDFEMgYIEDYTDIMAMETGFLQYMVELLKKDYAKELEILKVMLPK-TEEIPTVPFTKA 291
Cdd:PRK06462 110 PNFRLEpvDKDTGRHLYEFTQLDIEI-EGADLDEVMDLIEDLIKYLVKELLEEHEDELEFFGRDLPHlKRPFKRITHKEA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 292 KELVAEKYNRKIrnpfdlePEEELL-IGQYFKEEYDADFVFVTEYPSKKRPFYAMDDPEDKRYTKSFDLLF---HGlEIT 367
Cdd:PRK06462 189 VEILNEEGCRGI-------DLEELGsEGEKSLSEHFEEPFWIIDIPKGSREFYDREDPERPGVLRNYDLLLpegYG-EAV 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 941897655 368 TGGQRIHDYKMLSEKIAARGMTEEGMEQYLSAFKHGMPPHGGLGIGLERLTMKLIGEDNVRETTLFPR 435
Cdd:PRK06462 261 SGGEREYEYEEIVERIREHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQPFPR 328
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
24-434 |
1.93e-39 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 149.45 E-value: 1.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 24 GTEVKLEGAVHIIRDMGEVAFVILRKSEGLVQCVYEEGSVDFPL-KDLKEESAVAVTGTVKK-------EDRAPGGVEVR 95
Cdd:PRK00476 17 GQTVTLCGWVHRRRDHGGLIFIDLRDREGIVQVVFDPDAEAFEVaESLRSEYVIQVTGTVRArpegtvnPNLPTGEIEVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 96 LQTITVLSEPtEPMPLAVNKwKMNTSLEAMLNMRPIALRN--VRERAKFRIQegVVRAFRDFLHSQGFTEIHTPKIGAKG 173
Cdd:PRK00476 97 ASELEVLNKS-KTLPFPIDD-EEDVSEELRLKYRYLDLRRpeMQKNLKLRSK--VTSAIRNFLDDNGFLEIETPILTKST 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 174 AEGG------ANIFKLEYFhrpAvLAQSPQFYKQML-VGVFDRVFEVGPVFRAEKHNTKRHLnEYTSLDFEMGYIEDyTD 246
Cdd:PRK00476 173 PEGArdylvpSRVHPGKFY---A-LPQSPQLFKQLLmVAGFDRYYQIARCFRDEDLRADRQP-EFTQIDIEMSFVTQ-ED 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 247 IMAMETGFLQYMV-ELLKKD---------YAK--------------ELEILKVmlpkTEEIPTVPF------TKAKELV- 295
Cdd:PRK00476 247 VMALMEGLIRHVFkEVLGVDlptpfprmtYAEamrrygsdkpdlrfGLELVDV----TDLFKDSGFkvfagaANDGGRVk 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 296 -------AEKYNRK------------------------------------------IRNPFDLEPEEELLIG-------- 318
Cdd:PRK00476 323 airvpggAAQLSRKqideltefakiygakglayikvnedglkgpiakflseeelaaLLERTGAKDGDLIFFGadkakvvn 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 319 -------QYFKEEYDA------DFVFVTEYpskkrPFYAMDDpEDKRYT---------------------------KSFD 358
Cdd:PRK00476 403 dalgalrLKLGKELGLidedkfAFLWVVDF-----PMFEYDE-EEGRWVaahhpftmpkdedldelettdpgkaraYAYD 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 359 LLFHGLEITTGGQRIHDYKMLSEKIAARGMTEEgmEQY------LSAFKHGMPPHGGLGIGLERLTMKLIGEDNVRETTL 432
Cdd:PRK00476 477 LVLNGYELGGGSIRIHRPEIQEKVFEILGISEE--EAEekfgflLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIA 554
|
..
gi 941897655 433 FP 434
Cdd:PRK00476 555 FP 556
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
24-434 |
5.43e-35 |
|
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: 136.67 E-value: 5.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 24 GTEVKLEGAVHIIRDMGEVAFVILRKSEGLVQCVY--EEGSVDFPL-KDLKEESAVAVTGTVKKedRAP---------GG 91
Cdd:COG0173 16 GQEVTLSGWVHRRRDHGGLIFIDLRDRYGITQVVFdpDDSAEAFEKaEKLRSEYVIAVTGKVRA--RPEgtvnpklptGE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 92 VEVRLQTITVLSEpTEPMPLAVNKwKMNTSLEAMLNMRPIALRN--VRERAKFRIQegVVRAFRDFLHSQGFTEIHTPkI 169
Cdd:COG0173 94 IEVLASELEILNK-AKTPPFQIDD-DTDVSEELRLKYRYLDLRRpeMQKNLILRHK--VTKAIRNYLDENGFLEIETP-I 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 170 GAKGAEGGAnifkleyfhR----PA--------VLAQSPQFYKQML-VGVFDRVFEVGPVFRAEKHNTKRHLnEYTSLDF 236
Cdd:COG0173 169 LTKSTPEGA---------RdylvPSrvhpgkfyALPQSPQLFKQLLmVSGFDRYFQIARCFRDEDLRADRQP-EFTQLDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 237 EMGYIEDyTDIMAMETGFLQYMV-ELLKKD---------YAK--------------ELEILKVmlpkTEEIPTVPFT--- 289
Cdd:COG0173 239 EMSFVDQ-EDVFELMEGLIRHLFkEVLGVElptpfprmtYAEamerygsdkpdlrfGLELVDV----TDIFKDSGFKvfa 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 290 ---KAKELV-------AEKYNRK------------------------------------------IRNPFDLEP------ 311
Cdd:COG0173 314 gaaENGGRVkainvpgGASLSRKqideltefakqygakglayikvnedglkspiakflseeelaaILERLGAKPgdliff 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 312 ---EEE----------LLIGQ----YFKEEYdaDFVFVTEYpskkrPFYAMDDpEDKRYT-------------------- 354
Cdd:COG0173 394 vadKPKvvnkalgalrLKLGKelglIDEDEF--AFLWVVDF-----PLFEYDE-EEGRWVamhhpftmpkdedldlletd 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 355 ------KSFDLLFHGLEITTGGQRIHD----YKMLseKIAarGMTEEGMEQ----YLSAFKHGMPPHGGLGIGLERLTMK 420
Cdd:COG0173 466 pgkvraKAYDLVLNGYELGGGSIRIHDpelqEKVF--ELL--GISEEEAEEkfgfLLEAFKYGAPPHGGIAFGLDRLVML 541
|
570
....*....|....
gi 941897655 421 LIGEDNVRETTLFP 434
Cdd:COG0173 542 LAGEDSIRDVIAFP 555
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
148-434 |
1.24e-34 |
|
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: 130.00 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 148 VVRAFRDFLHSQGFTEIHTPkIGAKGAEGGANIFKLEYFHRPA---VLAQSPQFYKQML-VGVFDRVFEVGPVFRAEKHN 223
Cdd:cd00777 7 VIKAIRNFLDEQGFVEIETP-ILTKSTPEGARDFLVPSRLHPGkfyALPQSPQLFKQLLmVSGFDRYFQIARCFRDEDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 224 TKRHlNEYTSLDFEMGYIEDyTDIMAMETGFLQYMVEllkkdyakelEILKVMLPKTeeIPTVPFTKAKelvaEKYNRKI 303
Cdd:cd00777 86 ADRQ-PEFTQIDIEMSFVDQ-EDIMSLIEGLLKYVFK----------EVLGVELTTP--FPRMTYAEAM----ERYGFKF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 304 R--NPFDL-EPEEEllIGQYF---------KEEYDADFVfvteypskkrpfyamDDPEDKRyTKSFDLLFHGLEITTGGQ 371
Cdd:cd00777 148 LwiVDFPLfEWDEE--EGRLVsahhpftapKEEDLDLLE---------------KDPEDAR-AQAYDLVLNGVELGGGSI 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 941897655 372 RIHDYKMLSEKIAARGMTEEGMEQ----YLSAFKHGMPPHGGLGIGLERLTMKLIGEDNVRETTLFP 434
Cdd:cd00777 210 RIHDPDIQEKVFEILGLSEEEAEEkfgfLLEAFKYGAPPHGGIALGLDRLVMLLTGSESIRDVIAFP 276
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
24-435 |
5.08e-34 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 133.95 E-value: 5.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 24 GTEVKLEGAVHIIRDMGEVAFVILRKSEGL--VQCVYE---EGSVDFPLKDLKEESAVAVTGTVKKEDRAPGGVEVRLQT 98
Cdd:PLN02603 107 GKTLNVMGWVRTLRAQSSVTFIEVNDGSCLsnMQCVMTpdaEGYDQVESGLITTGASVLVQGTVVSSQGGKQKVELKVSK 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 99 ITVLSEPTEPMPLAvNKWKMNTSLEAMLNMRPialRNVRERAKFRIQEGVVRAFRDFLHSQGFTEIHTPKIGAKGAEGGA 178
Cdd:PLN02603 187 IVVVGKSDPSYPIQ-KKRVSREFLRTKAHLRP---RTNTFGAVARVRNALAYATHKFFQENGFVWVSSPIITASDCEGAG 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 179 NIFKL------------------------------EYFHRPAVLAQSPQFYKQMLVGVFDRVFEVGPVFRAEKHNTKRHL 228
Cdd:PLN02603 263 EQFCVttlipnsaenggslvddipktkdglidwsqDFFGKPAFLTVSGQLNGETYATALSDVYTFGPTFRAENSNTSRHL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 229 NEYTSLDFEMGYiEDYTDIMAMETGFLQYMVELLKKDYAKELEILKVMLPK----------TEEIPTVPFTKAKELVAeK 298
Cdd:PLN02603 343 AEFWMIEPELAF-ADLNDDMACATAYLQYVVKYILENCKEDMEFFNTWIEKgiidrlsdvvEKNFVQLSYTDAIELLL-K 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 299 YNRKIRNP----FDLEPEEElligQYFKEE-YDADFVFVTEYPSKKRPFYaMDDPEDKRYTKSFDLLFHGL-EITTGGQR 372
Cdd:PLN02603 421 AKKKFEFPvkwgLDLQSEHE----RYITEEaFGGRPVIIRDYPKEIKAFY-MRENDDGKTVAAMDMLVPRVgELIGGSQR 495
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 941897655 373 IHDYKMLSEKIAARGMTEEGMEQYLSAFKHGMPPHGGLGIGLERLTMKLIGEDNVRETTLFPR 435
Cdd:PLN02603 496 EERLEYLEARLDELKLNKESYWWYLDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFPR 558
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
20-434 |
2.72e-32 |
|
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: 128.23 E-value: 2.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 20 EIPEGTEVKLEGAVHIIRDMGEVAFVILRKSEGLVQcVYeegsvdFPLKDLKEESA-----------VAVTGTVKKEDRa 88
Cdd:COG1190 52 EEETGDEVSVAGRIMAKRDMGKASFADLQDGSGRIQ-LY------LRRDELGEEAYelfklldlgdiVGVEGTVFRTKT- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 89 pGGVEVRLQTITVLSEPTEPMPlavNKWKMNTSLEAM-------LNMRPIALRNVRERAKfriqegVVRAFRDFLHSQGF 161
Cdd:COG1190 124 -GELSVKVEELTLLSKSLRPLP---EKFHGLTDPETRyrqryvdLIVNPEVRETFRKRSK------IIRAIRRFLDERGF 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 162 TEIHTPKIGAkgAEGGAN----IFKLEYFHRPAVLAQSPQFY-KQMLVGVFDRVFEVGPVFRAE----KHNTkrhlnEYT 232
Cdd:COG1190 194 LEVETPMLQP--IAGGAAarpfITHHNALDMDLYLRIAPELYlKRLIVGGFERVFEIGRNFRNEgidtTHNP-----EFT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 233 SLDFEMGYiEDYTDIMAMETGFLQYMVEllkkdyakelEILkvmlpKTEEIP--------TVPFTKA--KELVAEKYNrk 302
Cdd:COG1190 267 MLELYQAY-ADYNDMMDLTEELIREAAE----------AVL-----GTTKVTyqgqeidlSPPWRRItmVEAIKEATG-- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 303 iRNPFDLEPEEEL-------------------LIGQYFKEeydadFV--------FVTEYPSKKRPFyAMDDPEDKRYTK 355
Cdd:COG1190 329 -IDVTPLTDDEELralakelgievdpgwgrgkLIDELFEE-----LVepkliqptFVTDYPVEVSPL-AKRHRDDPGLTE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 356 SFDLLFHGLEITTGgqrihdYkmlSE---------------KIAARGmTEEGM---EQYLSAFKHGMPPHGGLGIGLERL 417
Cdd:COG1190 402 RFELFIAGREIANA------F---SElndpidqrerfeeqlELKAAG-DDEAMpmdEDFLRALEYGMPPTGGLGIGIDRL 471
|
490
....*....|....*..
gi 941897655 418 TMKLIGEDNVRETTLFP 434
Cdd:COG1190 472 VMLLTDSPSIRDVILFP 488
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
135-434 |
2.86e-32 |
|
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: 125.00 E-value: 2.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 135 NVRERAKFRIQEGVVRAFRDFLHSQGFTEIHTPKIgaKGAEGGA---------NIFKLEYFHRPAvlaqsPQFY-KQMLV 204
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPML--QPIAGGAaarpfithhNALDMDLYLRIA-----PELYlKRLIV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 205 GVFDRVFEVGPVFRAEKHNTkRHLNEYTSLDFEMGYIeDYTDIMAMETGFLQYMVELLKKDyakeleiLKVMLPKTEEIP 284
Cdd:cd00775 74 GGFERVYEIGRNFRNEGIDL-THNPEFTMIEFYEAYA-DYNDMMDLTEDLFSGLVKKINGK-------TKIEYGGKELDF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 285 TVPFTKA--KELVAEKYNRKIRNPFDLEPEEEL-LIGQYFKEEYDAD-------------FV--------FVTEYPSKKR 340
Cdd:cd00775 145 TPPFKRVtmVDALKEKTGIDFPELDLEQPEELAkLLAKLIKEKIEKPrtlgklldklfeeFVeptliqptFIIDHPVEIS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 341 PFyAMDDPEDKRYTKSFDLLFHGLEITTGGQRIHD----YKMLSEKIAARGMT-EEGM---EQYLSAFKHGMPPHGGLGI 412
Cdd:cd00775 225 PL-AKRHRSNPGLTERFELFICGKEIANAYTELNDpfdqRERFEEQAKQKEAGdDEAMmmdEDFVTALEYGMPPTGGLGI 303
|
330 340
....*....|....*....|..
gi 941897655 413 GLERLTMKLIGEDNVRETTLFP 434
Cdd:cd00775 304 GIDRLVMLLTDSNSIRDVILFP 325
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
23-434 |
1.63e-31 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 126.64 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 23 EGTEVKLEGAVHIIRDMGEVAFVILRKSEGLVQCVYEEGSVD------FPLKDL-KEESAVAVTGTVKKEDRapGGVEVR 95
Cdd:PLN02502 107 EDVSVSVAGRIMAKRAFGKLAFYDLRDDGGKIQLYADKKRLDldeeefEKLHSLvDRGDIVGVTGTPGKTKK--GELSIF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 96 LQTITVLSEPTEPMPlavNKWKMNTSLEAMLNMRPIAL-RNVRERAKFRIQEGVVRAFRDFLHSQGFTEIHTPKIgaKGA 174
Cdd:PLN02502 185 PTSFEVLTKCLLMLP---DKYHGLTDQETRYRQRYLDLiANPEVRDIFRTRAKIISYIRRFLDDRGFLEVETPML--NMI 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 175 EGGANIFKLEYFH----RPAVLAQSPQFY-KQMLVGVFDRVFEVGPVFRAEKHNTkRHLNEYTSLDFEMGYiEDYTDIMA 249
Cdd:PLN02502 260 AGGAAARPFVTHHndlnMDLYLRIATELHlKRLVVGGFERVYEIGRQFRNEGIST-RHNPEFTTCEFYQAY-ADYNDMME 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 250 METGFLQYMVELLKKDY--------------------AKEL-EILKVMLPKTEEIPTVpfTKAKELVAEKYNRKIRNPfd 308
Cdd:PLN02502 338 LTEEMVSGMVKELTGSYkikyhgieidftppfrrismISLVeEATGIDFPADLKSDEA--NAYLIAACEKFDVKCPPP-- 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 309 lePEEELLIGQYFKEEYDADFV---FVTEYPSKKRPFyAMDDPEDKRYTKSFDLLFHGLEITTGGQRIHD----YKMLSE 381
Cdd:PLN02502 414 --QTTGRLLNELFEEFLEETLVqptFVLDHPVEMSPL-AKPHRSKPGLTERFELFINGRELANAFSELTDpvdqRERFEE 490
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 941897655 382 KIAARGMTE-EGM---EQYLSAFKHGMPPHGGLGIGLERLTMKLIGEDNVRETTLFP 434
Cdd:PLN02502 491 QVKQHNAGDdEAMaldEDFCTALEYGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFP 547
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
24-438 |
2.34e-31 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 126.83 E-value: 2.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 24 GTEVKLEGAVHIIRDMGEVAFVILRKSEGLVQCVYEEGSvdFP-----LKDLKEESAVAVTGTVKKE------DRAP-GG 91
Cdd:PLN02903 72 GSRVTLCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDE--FPeahrtANRLRNEYVVAVEGTVRSRpqespnKKMKtGS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 92 VEVRLQTITVLSEPTEPMPLAV---NKWKMNTSLEAMLNMRPIALRNVRERAKFRIQEGVVRAFRDFLHS-QGFTEIHTP 167
Cdd:PLN02903 150 VEVVAESVDILNVVTKSLPFLVttaDEQKDSIKEEVRLRYRVLDLRRPQMNANLRLRHRVVKLIRRYLEDvHGFVEIETP 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 168 kIGAKGAEGGANIFKLEYFHRPA---VLAQSPQFYKQML-VGVFDRVFEVGPVFRAEKHNTKRHlNEYTSLDFEMGyied 243
Cdd:PLN02903 230 -ILSRSTPEGARDYLVPSRVQPGtfyALPQSPQLFKQMLmVSGFDRYYQIARCFRDEDLRADRQ-PEFTQLDMELA---- 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 244 YTDIMAMetgfLQYMVELLKKDYakeLEILKVMLPKT---------------------------------EEIPTVPFTK 290
Cdd:PLN02903 304 FTPLEDM----LKLNEDLIRQVF---KEIKGVQLPNPfprltyaeamskygsdkpdlryglelvdvsdvfAESSFKVFAG 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 291 A-------KELV----AEKYNRKIRNPFD---------------------------------LEPE--EELL-------- 316
Cdd:PLN02903 377 AlesggvvKAICvpdgKKISNNTALKKGDiyneaiksgakglaflkvlddgelegikalvesLSPEqaEQLLaacgagpg 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 317 -------------------IGQYFKEEYDA------DFVFVTEYP------SKKR------PFYA--MDDPEDKRYTK-- 355
Cdd:PLN02903 457 dlilfaagptssvnktldrLRQFIAKTLDLidpsrhSILWVTDFPmfewneDEQRlealhhPFTApnPEDMGDLSSARal 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 356 SFDLLFHGLEITTGGQRIHDYKMLSEKIAARGMT-EEGMEQY---LSAFKHGMPPHGGLGIGLERLTMKLIGEDNVRETT 431
Cdd:PLN02903 537 AYDMVYNGVEIGGGSLRIYRRDVQQKVLEAIGLSpEEAESKFgylLEALDMGAPPHGGIAYGLDRLVMLLAGAKSIRDVI 616
|
....*..
gi 941897655 432 LFPRDLT 438
Cdd:PLN02903 617 AFPKTTT 623
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
22-434 |
2.42e-30 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 122.51 E-value: 2.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 22 PEGTEVKLEGAVHIIRDMGEVAFVILRKSEGLVQcVYeegsvdFPLKDLKEESA-----------VAVTGTVKKEDRapG 90
Cdd:PRK00484 52 ELEIEVSVAGRVMLKRVMGKASFATLQDGSGRIQ-LY------VSKDDVGEEALeafkkldlgdiIGVEGTLFKTKT--G 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 91 GVEVRLQTITVLSEPTEPMPlavNKWKMNTSLEAMLNMRPIAL---RNVRERAKFRIQegVVRAFRDFLHSQGFTEIHTP 167
Cdd:PRK00484 123 ELSVKATELTLLTKSLRPLP---DKFHGLTDVETRYRQRYVDLivnPESRETFRKRSK--IISAIRRFLDNRGFLEVETP 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 168 ---KIgakgaEGGA---------NIFKLEYFHRPAvlaqsPQFY-KQMLVGVFDRVFEVGPVFRAE----KHNTkrhlnE 230
Cdd:PRK00484 198 mlqPI-----AGGAaarpfithhNALDIDLYLRIA-----PELYlKRLIVGGFERVYEIGRNFRNEgidtRHNP-----E 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 231 YTSLDFEMGYiEDYTDIMAMETGFLQYMVEL---------------LKKDYAKeLEILKVMLPKT-EEIPTVPFTKAKEL 294
Cdd:PRK00484 263 FTMLEFYQAY-ADYNDMMDLTEELIRHLAQAvlgttkvtyqgteidFGPPFKR-LTMVDAIKEYTgVDFDDMTDEEARAL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 295 vAEKYNRKIRNPFDLepeeELLIGQYFKEeydadFV--------FVTEYPSKKRPFyAMDDPEDKRYTKSFDLLFHGLEI 366
Cdd:PRK00484 341 -AKELGIEVEKSWGL----GKLINELFEE-----FVepkliqptFITDYPVEISPL-AKRHREDPGLTERFELFIGGREI 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 367 TTGgqrihdykmLSE---------------KIAARGmTEEGM---EQYLSAFKHGMPPHGGLGIGLERLTMKLIGEDNVR 428
Cdd:PRK00484 410 ANA---------FSElndpidqrerfeaqvEAKEAG-DDEAMfmdEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIR 479
|
....*.
gi 941897655 429 ETTLFP 434
Cdd:PRK00484 480 DVILFP 485
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
24-436 |
2.72e-30 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 123.94 E-value: 2.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 24 GTEVKLEGAVHIIRDMGEVAFVILRKSEGLVQCVY--EEGSVDF--PLKDLKEESAVAVTGTVKK---EDRAP----GGV 92
Cdd:PRK12820 18 GREVCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFspEAAPADVyeLAASLRAEFCVALQGEVQKrleETENPhietGDI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 93 EVRLQTITVLSEpTEPMPLAVNKWKM----------NTSLEAMLNMRPIALRNVRERAKFRIQEGVVRAFRDFLHSQGFT 162
Cdd:PRK12820 98 EVFVRELSILAA-SEALPFAISDKAMtagagsagadAVNEDLRLQYRYLDIRRPAMQDHLAKRHRIIKCARDFLDSRGFL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 163 EIHTPKIGAKGAEGGANIFKLEYFHRPA--VLAQSPQFYKQML-VGVFDRVFEVGPVFRAEKHNTKRHlNEYTSLDFEMG 239
Cdd:PRK12820 177 EIETPILTKSTPEGARDYLVPSRIHPKEfyALPQSPQLFKQLLmIAGFERYFQLARCFRDEDLRPNRQ-PEFTQLDIEAS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 240 YIEDytdimametgflQYMVELLKKDYAKELEILKVMLPKTeeIPTVPFTKA---------------------------- 291
Cdd:PRK12820 256 FIDE------------EFIFELIEELTARMFAIGGIALPRP--FPRMPYAEAmdttgsdrpdlrfdlkfadatdifentr 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 292 ---------------------------KELVAEKYNRKIRNPFD------LEPEEELL---IGQYFKEE----------- 324
Cdd:PRK12820 322 ygifkqilqrggrikginikgqseklsKNVLQNEYAKEIAPSFGakgmtwMRAEAGGLdsnIVQFFSADekealkrrfha 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 325 YDADF-------------------------------------VFVTEYP-----------SKKRPFYAMD----DPEDKR 352
Cdd:PRK12820 402 EDGDViimiadascaivlsalgqlrlhladrlglipegvfhpLWITDFPlfeatddggvtSSHHPFTAPDredfDPGDIE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 353 -----YTKSFDLLFHGLEITTGGQRIHDYKMLSEKIAARGMTEEGMEQ----YLSAFKHGMPPHGGLGIGLERLTMKLIG 423
Cdd:PRK12820 482 elldlRSRAYDLVVNGEELGGGSIRINDKDIQLRIFAALGLSEEDIEDkfgfFLRAFDFAAPPHGGIALGLDRVVSMILQ 561
|
570
....*....|...
gi 941897655 424 EDNVRETTLFPRD 436
Cdd:PRK12820 562 TPSIREVIAFPKN 574
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
14-434 |
2.84e-30 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 124.31 E-value: 2.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 14 SVKTLLEIPEGTEVKLEGAVHIIRDMGEVAFVILRKSEGLVQCVYEEGSVD----------FPLKDLkeesaVAVTGTVK 83
Cdd:PRK02983 641 TVAEALDAPTGEEVSVSGRVLRIRDYGGVLFADLRDWSGELQVLLDASRLEqgsladfraaVDLGDL-----VEVTGTMG 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 84 KEDRapGGVEVRLQTITVLSEPTEPMPlavNKWKMNTSLEAMLNMRPIALR-NVRERAKFRIQEGVVRAFRDFLHSQGFT 162
Cdd:PRK02983 716 TSRN--GTLSLLVTSWRLAGKCLRPLP---DKWKGLTDPEARVRQRYLDLAvNPEARDLLRARSAVVRAVRETLVARGFL 790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 163 EIHTPKIGAkgAEGGANIfkleyfhRPAV-----------LAQSPQFY-KQMLVGVFDRVFEVGPVFRAE----KHNTkr 226
Cdd:PRK02983 791 EVETPILQQ--VHGGANA-------RPFVthinaydmdlyLRIAPELYlKRLCVGGVERVFELGRNFRNEgvdaTHNP-- 859
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 227 hlnEYTSLDFEMGYiEDYTDIMAMETGFLQYM-------VELLKKDYAKELEILKVmlpkTEEIPTVPFTKAkelVAEKY 299
Cdd:PRK02983 860 ---EFTLLEAYQAH-ADYDTMRDLTRELIQNAaqaahgaPVVMRPDGDGVLEPVDI----SGPWPVVTVHDA---VSEAL 928
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 300 N------------RKIRNPFDLEPEEELLIGQYFKEEYDAdFV--------FVTEYPSKKRPFyAMDDPEDKRYTKSFDL 359
Cdd:PRK02983 929 GeeidpdtplaelRKLCDAAGIPYRTDWDAGAVVLELYEH-LVedrttfptFYTDFPTSVSPL-TRPHRSDPGLAERWDL 1006
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 360 LFHGLEITTGGQRIHD----YKMLSEK-IAARGMTEEGM---EQYLSAFKHGMPPHGGLGIGLERLTMKLIGEdNVRETT 431
Cdd:PRK02983 1007 VAWGVELGTAYSELTDpveqRRRLTEQsLLAAGGDPEAMeldEDFLQALEYAMPPTGGLGMGVDRLVMLLTGR-SIRETL 1085
|
...
gi 941897655 432 LFP 434
Cdd:PRK02983 1086 PFP 1088
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
128-435 |
8.54e-28 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 115.89 E-value: 8.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 128 MRPIAlrNVRERAKF-----RIQEGVVRAFRDFLHSQGFTEIHTPKIGAKGAEGGANIF--------------------- 181
Cdd:PTZ00425 198 LREVA--HLRPRSYFissviRIRNALAIATHLFFQSRGFLYIHTPLITTSDCEGGGEMFtvttllgedadyraiprvnkk 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 182 ------------------------------------------KLEYFHRPAVLAQSPQFYKQMLVGVFDRVFEVGPVFRA 219
Cdd:PTZ00425 276 nkkgekredilntcnannnngnssssnavsspaypdqylidyKKDFFSKQAFLTVSGQLSLENLCSSMGDVYTFGPTFRA 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 220 EKHNTKRHLNEYTSLDFEMGYIEDYtDIMAMETGFLQYMVELLKKD-----YAKELEILKVMLPK-----TEEIPTVPFT 289
Cdd:PTZ00425 356 ENSHTSRHLAEFWMIEPEIAFADLY-DNMELAESYIKYCIGYVLNNnfddiYYFEENVETGLISRlknilDEDFAKITYT 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 290 KAKELV---AEKYNRKIRNPFDLEPEEELLIG-QYFKEEydadfVFVTEYPSKKRPFYaMDDPEDKRYTKSFDLLFHGL- 364
Cdd:PTZ00425 435 NVIDLLqpySDSFEVPVKWGMDLQSEHERFVAeQIFKKP-----VIVYNYPKDLKAFY-MKLNEDQKTVAAMDVLVPKIg 508
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 941897655 365 EITTGGQRIHDYKMLSEKIAARGMTEEGMEQYLSAFKHGMPPHGGLGIGLERLTMKLIGEDNVRETTLFPR 435
Cdd:PTZ00425 509 EVIGGSQREDNLERLDKMIKEKKLNMESYWWYRQLRKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFPR 579
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
26-434 |
2.92e-26 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 110.92 E-value: 2.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 26 EVKLEGAVHIIRDMGEVAFVILRKSEGLVQCVYE-----EGSVDFPLKDLKEESAVAVTGTVKKEDraPGGVEVRLQTIT 100
Cdd:PRK12445 67 EVSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVArdslpEGVYNDQFKKWDLGDIIGARGTLFKTQ--TGELSIHCTELR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 101 VLSEPTEPMPlavNKWKMNTSLEAMLNMRPIAL-RNVRERAKFRIQEGVVRAFRDFLHSQGFTEIHTP--KIGAKGAEGG 177
Cdd:PRK12445 145 LLTKALRPLP---DKFHGLQDQEVRYRQRYLDLiANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPmmQVIPGGASAR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 178 ANIFKLEYFHRPAVLAQSPQFY-KQMLVGVFDRVFEVGPVFRAEKHNTkRHLNEYTSLDFEMGYiEDYTDIMAM-ETGFL 255
Cdd:PRK12445 222 PFITHHNALDLDMYLRIAPELYlKRLVVGGFERVFEINRNFRNEGISV-RHNPEFTMMELYMAY-ADYHDLIELtESLFR 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 256 QYMVELLKK----------DYAKELEIL------KVMLPKTEEIPTVPFTKAKELvAEKYNRKIRNPFDLEPeeelLIGQ 319
Cdd:PRK12445 300 TLAQEVLGTtkvtygehvfDFGKPFEKLtmreaiKKYRPETDMADLDNFDAAKAL-AESIGITVEKSWGLGR----IVTE 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 320 YFKEEYDADFV---FVTEYPSKKRPFYAMDD--PEdkrYTKSFDLLFHGLEITTGGQRIHDYKMLSEKI-----AARGMT 389
Cdd:PRK12445 375 IFDEVAEAHLIqptFITEYPAEVSPLARRNDvnPE---ITDRFEFFIGGREIGNGFSELNDAEDQAERFqeqvnAKAAGD 451
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 941897655 390 EEGM---EQYLSAFKHGMPPHGGLGIGLERLTMKLIGEDNVRETTLFP 434
Cdd:PRK12445 452 DEAMfydEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
13-435 |
2.30e-25 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 108.54 E-value: 2.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 13 ISVKTLLEIPEG------TEVKLEGAVHIIRDMGEVAFVILRKSEGlvQCVYE-EGSVDFPLKDLKEESA----VAVTGT 81
Cdd:PLN02221 33 VLIRSILDRPDGgaglagQKVRIGGWVKTGREQGKGTFAFLEVNDG--SCPANlQVMVDSSLYDLSTLVAtgtcVTVDGV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 82 VKKEDRAPGGVE-VRLQTITVLS-EPTEPMPLAVNKWKMNTS-LEAMLNMRPialRNVRERAKFRIQEGVVRAFRDFLHS 158
Cdd:PLN02221 111 LKVPPEGKGTKQkIELSVEKVIDvGTVDPTKYPLPKTKLTLEfLRDVLHLRS---RTNSISAVARIRNALAFATHSFFQE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 159 QGFTEIHTPKIGAKGAEGGANIFKL------------------------------------------------------- 183
Cdd:PLN02221 188 HSFLYIHTPIITTSDCEGAGEMFQVttlinyterleqdlidnpppteadveaarlivkergevvaqlkaakaskeeitaa 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 184 -----------------------------------EYFHRPAVLAQSPQFYKQMLVGVFDRVFEVGPVFRAEKHNTKRHL 228
Cdd:PLN02221 268 vaelkiakeslahieersklkpglpkkdgkidyskDFFGRQAFLTVSGQLQVETYACALSSVYTFGPTFRAENSHTSRHL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 229 NEYTSLDFEMGYiEDYTDIMAMETGFLQYMVELLKKDYAKELEIL-----KVMLPKTEEIPTVPF-----TKAKELVAE- 297
Cdd:PLN02221 348 AEFWMVEPEIAF-ADLEDDMNCAEAYVKYMCKWLLDKCFDDMELMaknfdSGCIDRLRMVASTPFgrityTEAIELLEEa 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 298 -----KYNRKIRNPFDLEPEEElligQYFKEEYDADFVFVTEYPSKKRPFYaMDDPEDKRYTKSFDLLFHGL-EITTGGQ 371
Cdd:PLN02221 427 vakgkEFDNNVEWGIDLASEHE----RYLTEVLFQKPLIVYNYPKGIKAFY-MRLNDDEKTVAAMDVLVPKVgELIGGSQ 501
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 941897655 372 RIHDYKMLSEKIAARGMTEEGMEQYLSAFKHGMPPHGGLGIGLERLTMKLIGEDNVRETTLFPR 435
Cdd:PLN02221 502 REERYDVIKQRIEEMGLPIEPYEWYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPR 565
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
23-111 |
2.17e-23 |
|
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: 94.30 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 23 EGTEVKLEGAVHIIRDMGEVAFVILRKSEGLVQCVYEEGSVDFPL----KDLKEESAVAVTGTVKKEDRAPGGVEVRLQT 98
Cdd:cd04316 11 DGEEVTVAGWVHEIRDLGGIKFVILRDREGIVQVTAPKKKVDKELfktvRKLSRESVISVTGTVKAEPKAPNGVEIIPEE 90
|
90
....*....|...
gi 941897655 99 ITVLSEPTEPMPL 111
Cdd:cd04316 91 IEVLSEAKTPLPL 103
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
27-434 |
3.29e-22 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 99.34 E-value: 3.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 27 VKLEGAVHIIRDMGEVAFVILRKSEGLVQCVYEEGSvDFPLKDLKEESAVAVTGTVKKEDRAP-----GGVEVRLQTITV 101
Cdd:PTZ00385 110 VRVAGRVTSVRDIGKIIFVTIRSNGNELQVVGQVGE-HFTREDLKKLKVSLRVGDIIGADGVPcrmqrGELSVAASRMLI 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 102 LSeptepmPLAVNKWKMNTSLEAMLNMRPialRNVRERAKF-------------RIQEGVVRAFRDFLHSQGFTEIHTPK 168
Cdd:PTZ00385 189 LS------PYVCTDQVVCPNLRGFTVLQD---NDVKYRYRFtdmmtnpcvietiKKRHVMLQALRDYFNERNFVEVETPV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 169 IGAKGAEGGANIFKLEYFHRPA--VLAQSPQFY-KQMLVGVFDRVFEVGPVFRAEKHNtKRHLNEYTSLDFEMGYiEDYT 245
Cdd:PTZ00385 260 LHTVASGANAKSFVTHHNANAMdlFLRVAPELHlKQCIVGGMERIYEIGKVFRNEDAD-RSHNPEFTSCEFYAAY-HTYE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 246 DIMAM-ETGFLQYMvelLKKDYAKELEI---------LKVMLPKT-------EEIPT---VPFTKAKELVAEK---YNRK 302
Cdd:PTZ00385 338 DLMPMtEDIFRQLA---MRVNGTTVVQIypenahgnpVTVDLGKPfrrvsvyDEIQRmsgVEFPPPNELNTPKgiaYMSV 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 303 I--RNPFDLEPEE------ELLIgQYFKEEYDADFVFVTEYPSKKRPFyAMDDPEDKRYTKSFDLLFHGLEITTGGQRIH 374
Cdd:PTZ00385 415 VmlRYNIPLPPVRtaakmfEKLI-DFFITDRVVEPTFVMDHPLFMSPL-AKEQVSRPGLAERFELFVNGIEYCNAYSELN 492
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 941897655 375 D-----YKMLSEKIAARGMTEEGM---EQYLSAFKHGMPPHGGLGIGLERLTMKLIGEDNVRETTLFP 434
Cdd:PTZ00385 493 DpheqyHRFQQQLVDRQGGDEEAMpldETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFP 560
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
181-435 |
7.65e-22 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 98.40 E-value: 7.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 181 FKLEYFHRPAVLAQSPQFYKQMLVGVFDRVFEVGPVFRAEKHNTKRHLNEYTSLDFEMGYiEDYTDIMAMETGFLQYMVE 260
Cdd:PLN02532 363 FSKDFFSRPTYLTVSGRLHLESYACALGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAF-SELEDAMNCAEDYFKFLCK 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 261 LLKKDYAKELEILKVMLPKT-----EEIPTVPFTKAKELVA-EKYNRKIRNPFDLEPE------EELLigQYFKEEYDAD 328
Cdd:PLN02532 442 WVLENCSEDMKFVSKRIDKTistrlEAIISSSLQRISYTEAvDLLKQATDKKFETKPEwgialtTEHL--SYLADEIYKK 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 329 FVFVTEYPSKKRPFYAMDDpEDKRYTKSFDLLF-HGLEITTGGQRIHDYKMLSEKIAARGMTEEGMEQYLSAFKHGMPPH 407
Cdd:PLN02532 520 PVIIYNYPKELKPFYVRLN-DDGKTVAAFDLVVpKVGTVITGSQNEERMDILNARIEELGLPREQYEWYLDLRRHGTVKH 598
|
250 260
....*....|....*....|....*...
gi 941897655 408 GGLGIGLERLTMKLIGEDNVRETTLFPR 435
Cdd:PLN02532 599 SGFSLGFELMVLFATGLPDVRDAIPFPR 626
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
135-434 |
1.63e-19 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 90.84 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 135 NVRERAKFRIQEGVVRAFRDFLHSQGFTEIHTPKIGAkgAEGGANI---------FKLEYFHRPAVlaQSPqfYKQMLVG 205
Cdd:PTZ00417 246 NESTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNL--VAGGANArpfithhndLDLDLYLRIAT--ELP--LKMLIVG 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 206 VFDRVFEVGPVFRAEK-HNTkrHLNEYTSLDFEMGYiEDYTDIMAMETGFLQYMVELLKKDYakeleilKVMLPKT--EE 282
Cdd:PTZ00417 320 GIDKVYEIGKVFRNEGiDNT--HNPEFTSCEFYWAY-ADFYDLIKWSEDFFSQLVMHLFGTY-------KILYNKDgpEK 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 283 IP-----TVPFTKAK--ELVAEKYNRKIRNPFDlEPEE-------------------------ELLIGQYFKEEYDADFV 330
Cdd:PTZ00417 390 DPieidfTPPYPKVSivEELEKLTNTKLEQPFD-SPETinkminlikenkiempnpptaakllDQLASHFIENKYPNKPF 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 331 FVTEYPSKKRPF--YAMDDPEdkrYTKSFDLLFHGLEITTGGQRIHD-YKM-----LSEKIAARGMTEEGM--EQYLSAF 400
Cdd:PTZ00417 469 FIIEHPQIMSPLakYHRSKPG---LTERLEMFICGKEVLNAYTELNDpFKQkecfsAQQKDREKGDAEAFQfdAAFCTSL 545
|
330 340 350
....*....|....*....|....*....|....
gi 941897655 401 KHGMPPHGGLGIGLERLTMKLIGEDNVRETTLFP 434
Cdd:PTZ00417 546 EYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFP 579
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
26-104 |
5.76e-18 |
|
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: 78.38 E-value: 5.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 26 EVKLEGAVHIIRDMGEVAFVILRKSEGLVQCVYEEGSVDFP---LKDLKEESAVAVTGTVKK---EDRAPGGVEVRLQTI 99
Cdd:cd04100 1 EVTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEELGEFfeeAEKLRTESVVGVTGTVVKrpeGNLATGEIELQAEEL 80
|
....*
gi 941897655 100 TVLSE 104
Cdd:cd04100 81 EVLSK 85
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
26-104 |
1.14e-17 |
|
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and Saccharomyces cerevisiae cytoplasmic asparaginyl-tRNA synthetase (AsnRS), in Brugia malayai AsnRs and, in various putative bacterial AsnRSs. This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. AsnRS is immunodominant antigen of the filarial nematode B. malayai and 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: 239818 [Multi-domain] Cd Length: 84 Bit Score: 77.27 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 26 EVKLEGAVHIIRDMGEVAFVILRKSEGLVQCVYEEGSVDFPL--KDLKEESAVAVTGTVKKEDR---APGGVEVRLQTIT 100
Cdd:cd04323 1 RVKVFGWVHRLRSQKKLMFLVLRDGTGFLQCVLSKKLVTEFYdaKSLTQESSVEVTGEVKEDPRakqAPGGYELQVDYLE 80
|
....
gi 941897655 101 VLSE 104
Cdd:cd04323 81 IIGE 84
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
150-417 |
9.80e-15 |
|
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.
Pssm-ID: 238391 [Multi-domain] Cd Length: 211 Bit Score: 72.92 E-value: 9.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 150 RAFRDFLHSQGFTEIHTPKIGAKGAEGGAN-IFKLEYFHRP-----AVLAQSPQFYK-QMLVGV----FDRVFEVGPVFR 218
Cdd:cd00768 7 QKLRRFMAELGFQEVETPIVEREPLLEKAGhEPKDLLPVGAeneedLYLRPTLEPGLvRLFVSHirklPLRLAEIGPAFR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 219 AE-KHNTKRHLNEYTSLDFEmgyiedytdiMAMETGFLQYMVELLKKDYAkeleilkvmlpkteeiptvpftkakELVAE 297
Cdd:cd00768 87 NEgGRRGLRRVREFTQLEGE----------VFGEDGEEASEFEELIELTE-------------------------ELLRA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 298 kynrkirnpfdlepeeelligqyfkEEYDADFVFVTEYPSKKRPFYAmddpedkryTKSFDLLF-----HGLEITTGGQR 372
Cdd:cd00768 132 -------------------------LGIKLDIVFVEKTPGEFSPGGA---------GPGFEIEVdhpegRGLEIGSGGYR 177
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 941897655 373 IHDYKMLSEKIaargmteegmeQYLSAFKHGMPPHGGLGIGLERL 417
Cdd:cd00768 178 QDEQARAADLY-----------FLDEALEYRYPPTIGFGLGLERL 211
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
24-115 |
2.78e-14 |
|
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: 69.47 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 24 GTEVKLEGAVHIIRDMGEVAFVILRKSEGLVQCVY--EEGSVDFPLKDLKEESAVAVTGTVKK---EDRAP----GGVEV 94
Cdd:cd04317 14 GQEVTLCGWVQRRRDHGGLIFIDLRDRYGIVQVVFdpEEAPEFELAEKLRNESVIQVTGKVRArpeGTVNPklptGEIEV 93
|
90 100
....*....|....*....|.
gi 941897655 95 RLQTITVLSePTEPMPLAVNK 115
Cdd:cd04317 94 VASELEVLN-KAKTLPFEIDD 113
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
26-129 |
2.93e-13 |
|
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus horikoshii AsnRS asparaginyl-tRNA synthetase (AsnRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The archeal enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose.
Pssm-ID: 239814 [Multi-domain] Cd Length: 103 Bit Score: 65.62 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 26 EVKLEGAVHIIRDMGEVAFVILRKSEGLVQCVYEEGSVDFPLKDLKE---ESAVAVTGTVKKEDRAPGGVEVRLQTITVL 102
Cdd:cd04319 1 KVTLAGWVYRKREVGKKAFIVLRDSTGIVQAVFSKDLNEEAYREAKKvgiESSVIVEGAVKADPRAPGGAEVHGEKLEII 80
|
90 100
....*....|....*....|....*..
gi 941897655 103 sEPTEPMPLavnkwKMNTSLEAMLNMR 129
Cdd:cd04319 81 -QNVEFFPI-----TEDASDEFLLDVR 101
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
27-102 |
6.63e-10 |
|
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: 55.32 E-value: 6.63e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 941897655 27 VKLEGAVH-IIRDMGEVAFVILRKSEGLVQCVYEEGSVDFPLKDLKEESAVAVTGTVKKedRAPGGVEVRLQTITVL 102
Cdd:pfam01336 1 VTVAGRVTsIRRSGGKLLFLTLRDGTGSIQVVVFKEEAEKLAKKLKEGDVVRVTGKVKK--RKGGELELVVEEIELL 75
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
26-114 |
3.09e-09 |
|
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces cerevisiae and human cytoplasmic aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis.
Pssm-ID: 239815 [Multi-domain] Cd Length: 102 Bit Score: 54.11 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 26 EVKLEGAVHIIRDMGE-VAFVILRKSEGLVQCVYEEGS-------VDFpLKDLKEESAVAVTGTVKKEDR-----APGGV 92
Cdd:cd04320 1 EVLIRARVHTSRAQGAkLAFLVLRQQGYTIQGVLAASAegvskqmVKW-AGSLSKESIVDVEGTVKKPEEpikscTQQDV 79
|
90 100
....*....|....*....|..
gi 941897655 93 EVRLQTITVLSEPTEPMPLAVN 114
Cdd:cd04320 80 ELHIEKIYVVSEAAEPLPFQLE 101
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
135-429 |
5.35e-08 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 54.16 E-value: 5.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 135 NVRERAKFriqegvVRAFRDFLHSQGFTEIHTPKIG-----------------AKGAEGGANIFkleyfhrpavLAQSPQ 197
Cdd:PRK09350 4 NLLKRAKI------IAEIRRFFADRGVLEVETPILSqatvtdihlvpfetrfvGPGASQGKTLW----------LMTSPE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 198 FY-KQMLVGVFDRVFEVGPVFRAEKhNTKRHLNEYTSLD-FEMGYieDYTDIMAMETGFLQYmveLLKKDYAKELEILKV 275
Cdd:PRK09350 68 YHmKRLLAAGSGPIFQICKSFRNEE-AGRYHNPEFTMLEwYRPHY--DMYRLMNEVDDLLQQ---VLDCEPAESLSYQQA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 276 MLPKTEEIP-TVPFTKAKElVAEKYnrKIRNPFDLEPEEELLIGQYFKEEYDADF-----VFVTEYPSKKRPfYAMDDPE 349
Cdd:PRK09350 142 FLRYLGIDPlSADKTQLRE-VAAKL--GLSNIADEEEDRDTLLQLLFTFGVEPNIgkekpTFVYHFPASQAA-LAKISTE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 350 DKRYTKSFDLLFHGLEITTG-------GQRIHDYKMLSEKIAARGMTEEGM-EQYLSAFKHGMPPHGGLGIGLERLTMKL 421
Cdd:PRK09350 218 DHRVAERFEVYFKGIELANGfheltdaREQRQRFEQDNRKRAARGLPQQPIdENLIAALEAGLPDCSGVALGVDRLIMLA 297
|
....*...
gi 941897655 422 IGEDNVRE 429
Cdd:PRK09350 298 LGAESISE 305
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
26-104 |
4.56e-05 |
|
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli asparaginyl-tRNA synthetase (AsnRS) and, in Arabidopsis thaliana and Saccharomyces cerevisiae mitochondrial (mt) AsnRS. This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. S. cerevisiae mtAsnRS can charge E.coli tRNA with asparagines. Mutations in the gene for S. cerevisiae mtAsnRS has been found to induce a "petite" phenotype typical for a mutation in a nuclear gene that results in a non-functioning mitochondrial protein synthesis system.
Pssm-ID: 239813 [Multi-domain] Cd Length: 82 Bit Score: 41.78 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 26 EVKLEGAVHIIRDMGEVAFVILrkSEGL----VQCVYEEGSVDFP-LKDLKEESAVAVTGTVKKEDRAPGGVEVRLQTIT 100
Cdd:cd04318 1 EVTVNGWVRSVRDSKKISFIEL--NDGSclknLQVVVDKELTNFKeILKLSTGSSIRVEGVLVKSPGAKQPFELQAEKIE 78
|
....
gi 941897655 101 VLSE 104
Cdd:cd04318 79 VLGE 82
|
|
| ScAspRS_mt_like_N |
cd04321 |
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
26-104 |
1.08e-03 |
|
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces cerevisiae mitochondrial (mt) aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this fungal group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Mutations in the gene for S. cerevisiae mtAspRS result in a "petite" phenotype typical for a mutation in a nuclear gene that results in a non-functioning mitochondrial protein synthesis system.
Pssm-ID: 239816 [Multi-domain] Cd Length: 86 Bit Score: 38.07 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 26 EVKLEGAVHIIRD-MGEVAFVILRKSEG-LVQCVYEEGSVDFP-LKDLKEESAVAVTGTVK----KEDRAPGGVEVRLQT 98
Cdd:cd04321 1 KVTLNGWIDRKPRiVKKLSFADLRDPNGdIIQLVSTAKKDAFSlLKSITAESPVQVRGKLQlkeaKSSEKNDEWELVVDD 80
|
....*.
gi 941897655 99 ITVLSE 104
Cdd:cd04321 81 IQTLNA 86
|
|
| pylS |
PRK09537 |
pyrrolysine--tRNA(Pyl) ligase; |
88-258 |
4.63e-03 |
|
pyrrolysine--tRNA(Pyl) ligase;
Pssm-ID: 236555 [Multi-domain] Cd Length: 417 Bit Score: 39.05 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 88 APGGVEVRLQTITVLSEPTEPMPLAVNKWKMNTSLEAMLNMRPIALRNVRERAKFRIQEGVVRAFRDFLHSQGFTEIHTP 167
Cdd:PRK09537 149 APALTPSQKDRLETLLSPKDKISLNSEKPKFKELESELVSRRKNDLKQMYEEDREDYLGKLERDITKFFVDRGFLEIKSP 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941897655 168 ---------KIG-AKGAEGGANIFKLEYFH--RPaVLAqsPQFYKQMlvGVFDRV-------FEVGPVFRAEKhNTKRHL 228
Cdd:PRK09537 229 ilipaeyieRMGiDNDTELSKQIFRVDKNFclRP-MLA--PGLYNYL--RKLDRIlpdpikiFEIGPCYRKES-DGKEHL 302
|
170 180 190
....*....|....*....|....*....|.
gi 941897655 229 NEYTSLDF-EMGYIEDYTDIMAMETGFLQYM 258
Cdd:PRK09537 303 EEFTMVNFcQMGSGCTRENLENIIDDFLKHL 333
|
|
| |
