|
Name |
Accession |
Description |
Interval |
E-value |
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
5-449 |
0e+00 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 531.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 5 ADLIGAEVSIAGYAETVRGRGAIAFVMLRDGTGHIQAFLKKDNMDEdTFAAVQSASRESTIQVTGVVaqKRPPKTKEGep 84
Cdd:PRK05159 12 PELDGEEVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKVDEE-LFETIKKLKRESVVSVTGTV--KANPKAPGG-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 85 tpppeYEITVSEANILSAAATPLPVGITDDVNVGLDIRLDNRHLDLRRAHVNAMFQLRSKVLQYGRDHLIGEGFNEMNSP 164
Cdd:PRK05159 87 -----VEVIPEEIEVLNKAEEPLPLDISGKVLAELDTRLDNRFLDLRRPRVRAIFKIRSEVLRAFREFLYENGFTEIFTP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 165 KIIASASEGGTNLFPMMYFDTPAFLSQSPQLYKQLAVLGGLERVFEIGPAFRAEKHDTYRHLNEFISFDIEGAWMND-ED 243
Cdd:PRK05159 162 KIVASGTEGGAELFPIDYFEKEAYLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSRHLNEYTSIDVEMGFIDDhED 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 244 VMGVQERMIHHIWSQVAANDLHLFEAINtyrasqdqdpVTVEIPSLPFPRIPYCEAIEIVQNGGGEIEWGEDIESHH--- 320
Cdd:PRK05159 242 VMDLLENLLRYMYEDVAENCEKELELLG----------IELPVPETPIPRITYDEAIEILKSKGNEISWGDDLDTEGerl 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 321 -CDIIAAKYPGFH-FLPRWPMSMKPFYIYHDESEkgstgGQLSRGFDLNYGRDEMTSGGQREHRVDVLEQNLRNMDLNPA 398
Cdd:PRK05159 312 lGEYVKEEYGSDFyFITDYPSEKRPFYTMPDEDD-----PEISKSFDLLFRGLEITSGGQRIHRYDMLVESIKEKGLNPE 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 663513271 399 DFTFYTDGFRYGAPPHAGWGLGVARLLMILTGAGNVREVVLFPRDRSRVTP 449
Cdd:PRK05159 387 SFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFPRDRHRLTP 437
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
5-449 |
1.27e-177 |
|
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: 503.43 E-value: 1.27e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 5 ADLIGAEVSIAGYAETVRGRGAIAFVMLRDGTGHIQAFLKKDNMDedTFAAVQSASRESTIQVTGVVAQkrppktkegEP 84
Cdd:COG0017 10 PEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKLE--NFEEAKKLTTESSVEVTGTVVE---------SP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 85 TPPPEYEITVSEANILSAAATPLPVGITDdvnVGLDIRLDNRHLDLRRAHVNAMFQLRSKVLQYGRDHLIGEGFNEMNSP 164
Cdd:COG0017 79 RAPQGVELQAEEIEVLGEADEPYPLQPKR---HSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVEVHTP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 165 KIIASASEGGTNLFPMMYFDTPAFLSQSPQLYKQLAVlGGLERVFEIGPAFRAEKHDTYRHLNEFISFDIEGAWMNDEDV 244
Cdd:COG0017 156 IITASATEGGGELFPVDYFGKEAYLTQSGQLYKEALA-MALEKVYTFGPTFRAEKSNTRRHLAEFWMIEPEMAFADLEDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 245 MGVQERMIHHIWSQV---AANDLHLFEaintyrasQDQDPVTVeIPSLPFPRIPYCEAIEIVQNGGGEIEWGEDIESHHC 321
Cdd:COG0017 235 MDLAEEMLKYIIKYVlenCPEELEFLG--------RDVERLEK-VPESPFPRITYTEAIEILKKSGEKVEWGDDLGTEHE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 322 DIIAAKY-PGFHFLPRWPMSMKPFYIYHDESEkgstgGQLSRGFDLNY-GRDEMTSGGQREHRVDVLEQNLRNMDLNPAD 399
Cdd:COG0017 306 RYLGEEFfKKPVFVTDYPKEIKAFYMKPNPDD-----PKTVAAFDLLApGIGEIIGGSQREHRYDVLVERIKEKGLDPED 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 663513271 400 FTFYTDGFRYGAPPHAGWGLGVARLLMILTGAGNVREVVLFPRDRSRVTP 449
Cdd:COG0017 381 YEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
9-449 |
1.19e-139 |
|
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: 406.90 E-value: 1.19e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 9 GAEVSIAGYAETVRGRGAIAFVMLRDGTGHIQAFLKKDNMDEDTFAAVQSASRESTIQVTGVVaqKRPPKTKEGeptppp 88
Cdd:TIGR00458 12 GQEVTFMGWVHEIRDLGGLIFVLLRDREGLIQITAPAKKVSKNLFKWAKKLNLESVVAVRGIV--KIKEKAPGG------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 89 eYEITVSEANILSAAATPLPVGITDDVNVGLDIRLDNRHLDLRRAHVNAMFQLRSKVLQYGRDHLIGEGFNEMNSPKIIA 168
Cdd:TIGR00458 84 -FEIIPTKIEVINEAKEPLPLDPTEKVPAELDTRLDYRFLDLRRPTVQAIFRIRSGVLESVREFLAEEGFIEVHTPKLVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 169 SASEGGTNLFPMMYFDTPAFLSQSPQLYKQLAVLGGLERVFEIGPAFRAEKHDTYRHLNEFISFDIEGAWMNDEDVMGVQ 248
Cdd:TIGR00458 163 SATEGGTELFPITYFEREAFLGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNTHRHLNEATSIDIEMAFEDHHDVMDIL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 249 ERMIHHIWSQVAANDLHLFEAINtyrasqdqdpVTVEIPSLPFPRIPYCEAIEIVQNGGGEIEWGEDIESHHCDIIAAKY 328
Cdd:TIGR00458 243 EELVVRVFEDVPERCAHQLETLE----------FKLEKPEGKFVRLTYDEAIEMANAKGVEIGWGEDLSTEAEKALGEEM 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 329 PGFHFLPRWPMSMKPFYIYHDESEKgstggQLSRGFDLNYGRDEMTSGGQREHRVDVLEQNLRNMDLNPADFTFYTDGFR 408
Cdd:TIGR00458 313 DGLYFITDWPTEIRPFYTMPDEDNP-----EISKSFDLMYRDLEISSGAQRIHLHDLLVERIKAKGLNPEGFKDYLEAFS 387
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 663513271 409 YGAPPHAGWGLGVARLLMILTGAGNVREVVLFPRDRSRVTP 449
Cdd:TIGR00458 388 YGMPPHAGWGLGAERFVMFLLGLKNIREAVLFPRDRKRLTP 428
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
116-444 |
4.38e-127 |
|
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: 370.74 E-value: 4.38e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 116 NVGLDIRLDNRHLDLRRAHVNAMFQLRSKVLQYGRDHLIGEGFNEMNSPKIIASASEGGTNLFPMMYFDTPAFLSQSPQL 195
Cdd:cd00776 1 DANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 196 YKQLAVlGGLERVFEIGPAFRAEKHDTYRHLNEFISFDIEGAWMND-EDVMGVQERMIHHIWSQVAANDLHLFEAINtyr 274
Cdd:cd00776 81 YKEMLI-AALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEDyNEVMDLIEELIKYIFKRVLERCAKELELVN--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 275 asqdQDPVTVEIPSLPFPRIPYCEAIEIVQNGGG--EIEWGEDIESHHCDIIAAKYPG-FHFLPRWPMSMKPFYIYHDES 351
Cdd:cd00776 157 ----QLNRELLKPLEPFPRITYDEAIELLREKGVeeEVKWGEDLSTEHERLLGEIVKGdPVFVTDYPKEIKPFYMKPDDD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 352 EkgstgGQLSRGFDLNY-GRDEMTSGGQREHRVDVLEQNLRNMDLNPADFTFYTDGFRYGAPPHAGWGLGVARLLMILTG 430
Cdd:cd00776 233 N-----PETVESFDLLMpGVGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLG 307
|
330
....*....|....
gi 663513271 431 AGNVREVVLFPRDR 444
Cdd:cd00776 308 LDNIREAILFPRDP 321
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
4-449 |
1.35e-97 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 302.78 E-value: 1.35e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 4 GADLIGAEVSIAGYAETVRGRGAIAFVMLRDGTGHIQ--AFLKKDNMDEDTFAAVQSASRESTIQVTGVVaqKRPPKTKE 81
Cdd:PLN02850 76 GEELAGSEVLIRGRVHTIRGKGKSAFLVLRQSGFTVQcvVFVSEVTVSKGMVKYAKQLSRESVVDVEGVV--SVPKKPVK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 82 GEPTPppeYEITVSEANILSAAATPLPVGITDD-----------------VNVGLDIRLDNRHLDLRRAHVNAMFQLRSK 144
Cdd:PLN02850 154 GTTQQ---VEIQVRKIYCVSKALATLPFNVEDAarseseiekalqtgeqlVRVGQDTRLNNRVLDLRTPANQAIFRIQSQ 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 145 VLQYGRDHLIGEGFNEMNSPKIIASASEGGTNLFPMMYFDTPAFLSQSPQLYKQLAVLGGLERVFEIGPAFRAEKHDTYR 224
Cdd:PLN02850 231 VCNLFREFLLSKGFVEIHTPKLIAGASEGGSAVFRLDYKGQPACLAQSPQLHKQMAICGDFRRVFEIGPVFRAEDSFTHR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 225 HLNEFISFDIEGAWMN--DEdVMGVQERMIHHIWSQVAANDLHLFEAINTYRASQdqdPVTVEIPSLpfpRIPYCEAIEI 302
Cdd:PLN02850 311 HLCEFTGLDLEMEIKEhySE-VLDVVDELFVAIFDGLNERCKKELEAIREQYPFE---PLKYLPKTL---RLTFAEGIQM 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 303 VQNGGGEIEWGEDI----ESHHCDIIAAKY-PGFHFLPRWPMSMKPFYIYHDESEkgstgGQLSRGFDLNYGRDEMTSGG 377
Cdd:PLN02850 384 LKEAGVEVDPLGDLntesERKLGQLVKEKYgTDFYILHRYPLAVRPFYTMPCPDD-----PKYSNSFDVFIRGEEIISGA 458
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663513271 378 QREHRVDVLEQNLRNMDLNPADFTFYTDGFRYGAPPHAGWGLGVARLLMILTGAGNVREVVLFPRDRSRVTP 449
Cdd:PLN02850 459 QRVHDPELLEKRAEECGIDVKTISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPRDPQRLAP 530
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
118-444 |
1.51e-96 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 292.93 E-value: 1.51e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 118 GLDIRLDNRHLDLRRAHVNAMFQLRSKVLQYGRDHLIGEGFNEMNSPKIIASASEGGTNLFPM------MYFdtpaFLSQ 191
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVpsralgKFY----ALPQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 192 SPQLYKQLAVLGGLERVFEIGPAFRAEKHDTYRHLnEFISFDIEGAWMNDEDVMGVQERMIHHIWSqvaandlhlfEAIN 271
Cdd:pfam00152 77 SPQLYKQLLMVAGFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVDYEDVMDLTEELIKEIFK----------EVEG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 272 TYRASQDqdPVTVEIPSlPFPRIPYCEAIEIVqNGGGEIEWGEDIESHH----CDIIAAKYP-GFHFLPRWPMSMKPFYI 346
Cdd:pfam00152 146 IAKELEG--GTLLDLKK-PFPRITYAEAIEKL-NGKDVEELGYGSDKPDlrflLELVIDKNKfNPLWVTDFPAEHHPFTM 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 347 YHDESEKGstggqLSRGFDLNYGRDEMTSGGQREHRVDVLEQNLRNMDLNPAD----FTFYTDGFRYGAPPHAGWGLGVA 422
Cdd:pfam00152 222 PKDEDDPA-----LAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDPEEaeekFGFYLDALKYGAPPHGGLGIGLD 296
|
330 340
....*....|....*....|..
gi 663513271 423 RLLMILTGAGNVREVVLFPRDR 444
Cdd:pfam00152 297 RLVMLLTGLESIREVIAFPKTR 318
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
5-449 |
9.39e-95 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 292.78 E-value: 9.39e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 5 ADLIGAEVSIAGYAETVRGRGAIAFVMLRDGTG--HIQAFLKKDnmdEDTFAAVQSASRESTIQVTGVVaqkrppKTKEG 82
Cdd:PRK03932 12 GKYVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCfkQLQVVKDNG---EEYFEEIKKLTTGSSVIVTGTV------VESPR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 83 EPTPppeYEITVSEANILSAAATPLPvgITDDvNVGLDIRLDNRHLDLRRAHVNAMFQLRSKVLQYGRDHLIGEGFNEMN 162
Cdd:PRK03932 83 AGQG---YELQATKIEVIGEDPEDYP--IQKK-RHSIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 163 SPKIIASASEGGTNLFPMM---------YFDTPAFLSQSPQLYKQLAVLGgLERVFEIGPAFRAEKHDTYRHLNEFISFD 233
Cdd:PRK03932 157 TPIITASDCEGAGELFRVTtldldfskdFFGKEAYLTVSGQLYAEAYAMA-LGKVYTFGPTFRAENSNTRRHLAEFWMIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 234 IEGAWMNDEDVMGVQERMIHHIWSQV---AANDLHLFEaintyRASQDQDPVTVE-IPSLPFPRIPYCEAIEIVQNGGGE 309
Cdd:PRK03932 236 PEMAFADLEDNMDLAEEMLKYVVKYVlenCPDDLEFLN-----RRVDKGDIERLEnFIESPFPRITYTEAIEILQKSGKK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 310 ----IEWGEDIESHHCDIIAAKYpgFH---FLPRWPMSMKPFYIYHDEsekgstGGQLSRGFDL---NYGrdEMTSGGQR 379
Cdd:PRK03932 311 fefpVEWGDDLGSEHERYLAEEH--FKkpvFVTNYPKDIKAFYMRLNP------DGKTVAAMDLlapGIG--EIIGGSQR 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 380 EHRVDVLEQNLRNMDLNPADFTFYTDGFRYGAPPHAGWGLGVARLLMILTGAGNVREVVLFPRDRSRVTP 449
Cdd:PRK03932 381 EERLDVLEARIKELGLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
8-442 |
2.52e-81 |
|
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: 258.08 E-value: 2.52e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 8 IGAEVSIAGYAETVRGRGAIAFVMLRDGT--GHIQAFLKKDnMDEDTFAAVQSASRESTIQVTGVVAQkrPPKTKEGept 85
Cdd:TIGR00457 15 VGDEVTVSGWVRTKRSSKKIIFLELNDGSslGPIQAVINGE-DNPYLFQLLKSLTTGSSVSVTGKVVE--SPGKGQP--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 86 pppeYEITVSEANILS-AAATPLPVGITDDvnvGLDIRLDNRHLDLRRAHVNAMFQLRSKVLQYGRDHLIGEGFNEMNSP 164
Cdd:TIGR00457 89 ----VELQVKKIEVVGeAEPDDYPLQKKEH---SLEFLRDIAHLRLRTNTLGAVMRVRNALSQAIHRYFQENGFTWVSPP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 165 KIIASASEGGTNLFPM---------MYFDTPAFLSQSPQLYKQLAVLGgLERVFEIGPAFRAEKHDTYRHLNEFISFDIE 235
Cdd:TIGR00457 162 ILTSNDCEGAGELFRVstgnidfsqDFFGKEAYLTVSGQLYLETYALA-LSKVYTFGPTFRAEKSNTSRHLSEFWMIEPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 236 GAWMNDEDVMGVQERMIHHIWSQV---AANDLHLFEAintyRASQDQDPVTVEIPSLPFPRIPYCEAIEIVQNGGGEIE- 311
Cdd:TIGR00457 241 MAFANLNDLLQLAETLIKYIIKAVlenCSQELKFLEK----NFDKDLIKRLENIINNKFARITYTDAIEILKESDKNFEy 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 312 ---WGEDIESHHCDIIAAKYpgFH---FLPRWPMSMKPFYIyhdeseKGSTGGQLSRGFDL---NYGrdEMTSGGQREHR 382
Cdd:TIGR00457 317 edfWGDDLQTEHERFLAEEY--FKppvFVTNYPKDIKAFYM------KLNDDGKTVAAMDLlapGIG--EIIGGSEREDD 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 383 VDVLEQNLRNMDLNPADFTFYTDGFRYGAPPHAGWGLGVARLLMILTGAGNVREVVLFPR 442
Cdd:TIGR00457 387 LDKLENRMKEMGLDTDALNWYLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPR 446
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
6-449 |
1.89e-79 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 256.46 E-value: 1.89e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 6 DLIGAEVSIAGYAETVRGRGAIAFVMLRDGTGHIQAFLK-KDNMDEDTFAAVQSASRESTIQVTGVVAQKRPPKTKegep 84
Cdd:PTZ00401 75 ELVDKTVLIRARVSTTRKKGKMAFMVLRDGSDSVQAMAAvEGDVPKEMIDFIGQIPTESIVDVEATVCKVEQPITS---- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 85 TPPPEYEITVSEANILSAAATPLPVGITD--------DVNVGLDIRLDNRHLDLRRAHVNAMFQLRSKVLQYGRDHLIGE 156
Cdd:PTZ00401 151 TSHSDIELKVKKIHTVTESLRTLPFTLEDasrkesdeGAKVNFDTRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLIDS 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 157 GFNEMNSPKIIASASEGGTNLFPMMYFDTPAFLSQSPQLYKQLAVLGGLERVFEIGPAFRAEKHDTYRHLNEFISFDIEg 236
Cdd:PTZ00401 231 DFCEIHSPKIINAPSEGGANVFKLEYFNRFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNTHRHLTEFVGLDVE- 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 237 AWMNDE--DVMGVQERMIHHIWSQVAANDLHL--------FE-----------------AINTYRASQDQDPVTVEIPSL 289
Cdd:PTZ00401 310 MRINEHyyEVLDLAESLFNYIFERLATHTKELkavcqqypFEplvwkltpermkelgvgVISEGVEPTDKYQARVHNMDS 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 290 PFPRIPYCEAIEIVQNGGGE-IEWGEDIESHH----CDIIAAKY-PGFHFLPRWPMSMKPFYIYHDESEKgstggQLSRG 363
Cdd:PTZ00401 390 RMLRINYMHCIELLNTVLEEkMAPTDDINTTNekllGKLVKERYgTDFFISDRFPSSARPFYTMECKDDE-----RFTNS 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 364 FDLNYGRDEMTSGGQREHRVDVLEQNLR--NMDLNPadFTFYTDGFRYGAPPHAGWGLGVARLLMILTGAGNVREVVLFP 441
Cdd:PTZ00401 465 YDMFIRGEEISSGAQRIHDPDLLLARAKmlNVDLTP--IKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFP 542
|
....*...
gi 663513271 442 RDRSRVTP 449
Cdd:PTZ00401 543 RDPQRTTP 550
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
139-444 |
8.84e-65 |
|
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: 209.25 E-value: 8.84e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 139 FQLRSKVLQYGRDHLIGEGFNEMNSPKIIASASEGGTNLFPMMYFDTP--AFLSQSPQLYKQLAVLGGLERVFEIGPAFR 216
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGldYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 217 AEkHDTYRHLNEFISFDIEGAWMNDEDVMGVQERMIHHIWSQVAANDLHLFEAIntyrasqdqdpvtVEIPSLPFPRIPY 296
Cdd:cd00669 81 NE-DLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYGFE-------------LEDFGLPFPRLTY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 297 CEAIEivqngggeiewgedieshhcdiiaaKYPGFHFLPRWPMSMKPFYIY-HDESEkgstggQLSRGFDLNYGRDEMTS 375
Cdd:cd00669 147 REALE-------------------------RYGQPLFLTDYPAEMHSPLASpHDVNP------EIADAFDLFINGVEVGN 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663513271 376 GGQREHRVDVLEQNLRNMDLNPAD----FTFYTDGFRYGAPPHAGWGLGVARLLMILTGAGNVREVVLFPRDR 444
Cdd:cd00669 196 GSSRLHDPDIQAEVFQEQGINKEAgmeyFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKMR 268
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
5-441 |
8.60e-57 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 197.21 E-value: 8.60e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 5 ADLIGAEVSIAGYAETVRGRGAIAFVMLRDGTGHIQAFLkkdNMDEDTFAAVQSASRESTIQVTGVVaQKRPPKTKEGE- 83
Cdd:PRK00476 13 ESHVGQTVTLCGWVHRRRDHGGLIFIDLRDREGIVQVVF---DPDAEAFEVAESLRSEYVIQVTGTV-RARPEGTVNPNl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 84 PTPppEYEITVSEANILSAAATPlPVGITDDVNVGLDIRLDNRHLDLRRAHVNAMFQLRSKVLQYGRDHLIGEGFNEMNS 163
Cdd:PRK00476 89 PTG--EIEVLASELEVLNKSKTL-PFPIDDEEDVSEELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDDNGFLEIET 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 164 PKIIASASEGG------TNLFPMMYFdtpAfLSQSPQLYKQLAVLGGLERVFEIGPAFRAEkhDtyrhLN-----EFISF 232
Cdd:PRK00476 166 PILTKSTPEGArdylvpSRVHPGKFY---A-LPQSPQLFKQLLMVAGFDRYYQIARCFRDE--D----LRadrqpEFTQI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 233 DIEGAWMNDEDVMGVQERMIHHIWSQVAandlhlfeaintyrasqdqdpvTVEIPsLPFPRIPYCEAI------------ 300
Cdd:PRK00476 236 DIEMSFVTQEDVMALMEGLIRHVFKEVL----------------------GVDLP-TPFPRMTYAEAMrrygsdkpdlrf 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 301 --------EIVQN----------------------GGGE------------------------IEWGED----------- 315
Cdd:PRK00476 293 glelvdvtDLFKDsgfkvfagaandggrvkairvpGGAAqlsrkqideltefakiygakglayIKVNEDglkgpiakfls 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 316 -------IESHHC---DII---AAKY-----------------------PGFHFL-----P---------RW-----PMS 340
Cdd:PRK00476 373 eeelaalLERTGAkdgDLIffgADKAkvvndalgalrlklgkelglideDKFAFLwvvdfPmfeydeeegRWvaahhPFT 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 341 MkPFYIYHDESEKGSTGGQLSRGFD--LN-YgrdEMTSGGQREHRVDVLEQNLRNMDLNPAD----FTFYTDGFRYGAPP 413
Cdd:PRK00476 453 M-PKDEDLDELETTDPGKARAYAYDlvLNgY---ELGGGSIRIHRPEIQEKVFEILGISEEEaeekFGFLLDALKYGAPP 528
|
570 580
....*....|....*....|....*...
gi 663513271 414 HAGWGLGVARLLMILTGAGNVREVVLFP 441
Cdd:PRK00476 529 HGGIAFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
5-441 |
4.78e-55 |
|
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: 192.52 E-value: 4.78e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 5 ADLIGAEVSIAGYAETVRGRGAIAFVMLRDGTGHIQAFLKKDNmDEDTFAAVQSASRESTIQVTGVVaQKRPPKTKEGE- 83
Cdd:COG0173 12 ESDVGQEVTLSGWVHRRRDHGGLIFIDLRDRYGITQVVFDPDD-SAEAFEKAEKLRSEYVIAVTGKV-RARPEGTVNPKl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 84 PTPppEYEITVSEANILSAAATPlPVGITDDVNVGLDIRLDNRHLDLRRAHVNAMFQLRSKVLQYGRDHLIGEGFNEMNS 163
Cdd:COG0173 90 PTG--EIEVLASELEILNKAKTP-PFQIDDDTDVSEELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDENGFLEIET 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 164 PKIIASASEG------------GTnlfpmmyfdtpaF--LSQSPQLYKQLAVLGGLERVFEIGPAFRAEkhDtyrhLN-- 227
Cdd:COG0173 167 PILTKSTPEGardylvpsrvhpGK------------FyaLPQSPQLFKQLLMVSGFDRYFQIARCFRDE--D----LRad 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 228 ---EFISFDIEGAWMNDEDVMGVQERMIHHIWSQVAANDLhlfeaintyrasqdqdpvtveipSLPFPRIPYCEAI---- 300
Cdd:COG0173 229 rqpEFTQLDIEMSFVDQEDVFELMEGLIRHLFKEVLGVEL-----------------------PTPFPRMTYAEAMeryg 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 301 ----------------EIVQN----------------------GGGE-----------------------IEWGED-IES 318
Cdd:COG0173 286 sdkpdlrfglelvdvtDIFKDsgfkvfagaaenggrvkainvpGGASlsrkqideltefakqygakglayIKVNEDgLKS 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 319 ------------------------------------------------HHCDIIAAKypGFHFL-----P---------R 336
Cdd:COG0173 366 piakflseeelaailerlgakpgdliffvadkpkvvnkalgalrlklgKELGLIDED--EFAFLwvvdfPlfeydeeegR 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 337 W-----PMSM-KPFYIYHDESEKGSTggqLSRGFD--LNyGrDEMTSGGQREHRVDVLEQNLRNMDLNPAD----FTFYT 404
Cdd:COG0173 444 WvamhhPFTMpKDEDLDLLETDPGKV---RAKAYDlvLN-G-YELGGGSIRIHDPELQEKVFELLGISEEEaeekFGFLL 518
|
570 580 590
....*....|....*....|....*....|....*..
gi 663513271 405 DGFRYGAPPHAGWGLGVARLLMILTGAGNVREVVLFP 441
Cdd:COG0173 519 EAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
139-441 |
1.04e-40 |
|
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: 146.57 E-value: 1.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 139 FQLRSKVLQYGRDHLIGEGFNEMNSPKIIASASEGG------TNLFPMMYFDTPaflsQSPQLYKQLAVLGGLERVFEIG 212
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTPEGArdflvpSRLHPGKFYALP----QSPQLFKQLLMVSGFDRYFQIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 213 PAFRAEKHDTYRHlNEFISFDIEGAWMNDEDVMGVQERMIHHIWSQVAAndlhlfeaintyrasqdqdpvtVEIPSlPFP 292
Cdd:cd00777 77 RCFRDEDLRADRQ-PEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG----------------------VELTT-PFP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 293 RIPYCEAIEivqngggeiewgedieshhcdiiaaKYpGFHFL--PRWPM-----------SM-KPFYIYHDESE---KGS 355
Cdd:cd00777 133 RMTYAEAME-------------------------RY-GFKFLwiVDFPLfewdeeegrlvSAhHPFTAPKEEDLdllEKD 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 356 TGGQLSRGFDLNYGRDEMTSGGQREHRVDVLEQNLRNMDLNPAD----FTFYTDGFRYGAPPHAGWGLGVARLLMILTGA 431
Cdd:cd00777 187 PEDARAQAYDLVLNGVELGGGSIRIHDPDIQEKVFEILGLSEEEaeekFGFLLEAFKYGAPPHGGIALGLDRLVMLLTGS 266
|
330
....*....|
gi 663513271 432 GNVREVVLFP 441
Cdd:cd00777 267 ESIRDVIAFP 276
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
4-442 |
6.77e-40 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 150.51 E-value: 6.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 4 GADLIGAEVSIAGYAETVRGRGAIAFVMLRDGT--GHIQAFLkkdNMDEDTFAAVQSAS--RESTIQVTGVVAQKRPPKT 79
Cdd:PLN02603 102 GLARVGKTLNVMGWVRTLRAQSSVTFIEVNDGSclSNMQCVM---TPDAEGYDQVESGLitTGASVLVQGTVVSSQGGKQ 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 80 KegeptpppeYEITVSEANILSAAATPLPVgitDDVNVGLDIRLDNRHLDLRRAHVNAMFQLRSkVLQYGRDHLIGE-GF 158
Cdd:PLN02603 179 K---------VELKVSKIVVVGKSDPSYPI---QKKRVSREFLRTKAHLRPRTNTFGAVARVRN-ALAYATHKFFQEnGF 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 159 NEMNSPKIIASASEGG------TNLFP------------------------MMYFDTPAFLSQSPQLYKQlAVLGGLERV 208
Cdd:PLN02603 246 VWVSSPIITASDCEGAgeqfcvTTLIPnsaenggslvddipktkdglidwsQDFFGKPAFLTVSGQLNGE-TYATALSDV 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 209 FEIGPAFRAEKHDTYRHLNEFISFDIEGAWMNDEDVMGVQERMIHHIWSQVAANDLHLFEAINTYRASQDQDPVTvEIPS 288
Cdd:PLN02603 325 YTFGPTFRAENSNTSRHLAEFWMIEPELAFADLNDDMACATAYLQYVVKYILENCKEDMEFFNTWIEKGIIDRLS-DVVE 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 289 LPFPRIPYCEAIEIVQNGGGE----IEWGEDIESHHCDIIAAK-YPGFHFLPR-WPMSMKPFYIyhDESEKGSTGGQLsr 362
Cdd:PLN02603 404 KNFVQLSYTDAIELLLKAKKKfefpVKWGLDLQSEHERYITEEaFGGRPVIIRdYPKEIKAFYM--RENDDGKTVAAM-- 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 363 gfDLNYGR-DEMTSGGQREHRVDVLEQNLRNMDLNPADFTFYTDGFRYGAPPHAGWGLGVARLLMILTGAGNVREVVLFP 441
Cdd:PLN02603 480 --DMLVPRvGELIGGSQREERLEYLEARLDELKLNKESYWWYLDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFP 557
|
.
gi 663513271 442 R 442
Cdd:PLN02603 558 R 558
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
8-442 |
2.63e-38 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 147.24 E-value: 2.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 8 IGAEVSIAGYAETVRGRGAIAFVMLRDGTGHIQAFlkkdnMDEDTFAAVQSASR----ESTIQVTGVVaQKRP-----PK 78
Cdd:PLN02903 71 VGSRVTLCGWVDLHRDMGGLTFLDVRDHTGIVQVV-----TLPDEFPEAHRTANrlrnEYVVAVEGTV-RSRPqespnKK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 79 TKEGEptpppeYEITVSEANILSAAATPLPVGIT----DDVNVGLDIRLDNRHLDLRRAHVNAMFQLRSKVLQYGRDHLI 154
Cdd:PLN02903 145 MKTGS------VEVVAESVDILNVVTKSLPFLVTtadeQKDSIKEEVRLRYRVLDLRRPQMNANLRLRHRVVKLIRRYLE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 155 G-EGFNEMNSPKIIASASEGGTNLFPMMYFDTPAF--LSQSPQLYKQLAVLGGLERVFEIGPAFRAEKHDTYRHlNEFIS 231
Cdd:PLN02903 219 DvHGFVEIETPILSRSTPEGARDYLVPSRVQPGTFyaLPQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQ-PEFTQ 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 232 FDIEGAWMNDEDVMGVQERMIHHIWSQVAANDL-------HLFEAINTYRASQ----------DQDPVTVEIPSLPFP-- 292
Cdd:PLN02903 298 LDMELAFTPLEDMLKLNEDLIRQVFKEIKGVQLpnpfprlTYAEAMSKYGSDKpdlryglelvDVSDVFAESSFKVFAga 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 293 ----------RIP----------------YCEAIEIVQNG--------GGEIEWGEDI---------------------- 316
Cdd:PLN02903 378 lesggvvkaiCVPdgkkisnntalkkgdiYNEAIKSGAKGlaflkvldDGELEGIKALveslspeqaeqllaacgagpgd 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 317 -------------------------------ESHHCDIIAAKYPGFHFLP---RWPMSMKPFYIYHDESEKGSTGGQlSR 362
Cdd:PLN02903 458 lilfaagptssvnktldrlrqfiaktldlidPSRHSILWVTDFPMFEWNEdeqRLEALHHPFTAPNPEDMGDLSSAR-AL 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 363 GFDLNYGRDEMTSGGQREHRVDVLEQNLRNMDLNPAD----FTFYTDGFRYGAPPHAGWGLGVARLLMILTGAGNVREVV 438
Cdd:PLN02903 537 AYDMVYNGVEIGGGSLRIYRRDVQQKVLEAIGLSPEEaeskFGYLLEALDMGAPPHGGIAYGLDRLVMLLAGAKSIRDVI 616
|
....
gi 663513271 439 LFPR 442
Cdd:PLN02903 617 AFPK 620
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
6-449 |
5.27e-37 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 143.97 E-value: 5.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 6 DLIGAEVSIAGYAETVRGRGAIAFVMLRDGTGHIQAFLKKDNMDEDTFAAVQSASRESTIQVTGVVaQKRPPKTkEGEPT 85
Cdd:PRK12820 15 DDTGREVCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFSPEAAPADVYELAASLRAEFCVALQGEV-QKRLEET-ENPHI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 86 PPPEYEITVSEANILSAAATpLPVGITDDV-----------NVGLDIRLDNRHLDLRRAHVNAMFQLRSKVLQYGRDHLI 154
Cdd:PRK12820 93 ETGDIEVFVRELSILAASEA-LPFAISDKAmtagagsagadAVNEDLRLQYRYLDIRRPAMQDHLAKRHRIIKCARDFLD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 155 GEGFNEMNSPKIIASASEGG------TNLFPMMYFDTPaflsQSPQLYKQLAVLGGLERVFEIGPAFRAEKHDTYRHlNE 228
Cdd:PRK12820 172 SRGFLEIETPILTKSTPEGArdylvpSRIHPKEFYALP----QSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQ-PE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 229 FISFDIEGAWMNDEDVMGVQERMIhhiwsqvaandLHLFEAINtyrasqdqdpvtVEIPSlPFPRIPYCEAIE------- 301
Cdd:PRK12820 247 FTQLDIEASFIDEEFIFELIEELT-----------ARMFAIGG------------IALPR-PFPRMPYAEAMDttgsdrp 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 302 -------------------------IVQNGG--------GEIE-------------------------W----------- 312
Cdd:PRK12820 303 dlrfdlkfadatdifentrygifkqILQRGGrikginikGQSEklsknvlqneyakeiapsfgakgmtWmraeaggldsn 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 313 ------------------GED------IESHHCDIIAAKY--------------PGFHFLPRW----PM----------- 339
Cdd:PRK12820 383 ivqffsadekealkrrfhAEDgdviimIADASCAIVLSALgqlrlhladrlgliPEGVFHPLWitdfPLfeatddggvts 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 340 SMKPFYIYHDES-EKGSTGGQL---SRGFDLNYGRDEMTSGGQREHRVDVLEQNLRNMDLNPAD----FTFYTDGFRYGA 411
Cdd:PRK12820 463 SHHPFTAPDREDfDPGDIEELLdlrSRAYDLVVNGEELGGGSIRINDKDIQLRIFAALGLSEEDiedkFGFFLRAFDFAA 542
|
570 580 590
....*....|....*....|....*....|....*...
gi 663513271 412 PPHAGWGLGVARLLMILTGAGNVREVVLFPRDRSRVTP 449
Cdd:PRK12820 543 PPHGGIALGLDRVVSMILQTPSIREVIAFPKNRSAACP 580
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
139-442 |
7.47e-36 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 135.15 E-value: 7.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 139 FQLRSKVLQYGRDHLIGEGFNEMNSPKI--IASASEGGTNLFPMM-----YFDTPAFLSQSPQLYKQLAVLGgLERVFEI 211
Cdd:PRK06462 30 LKVQSSILRYTREFLDGRGFVEVLPPIIspSTDPLMGLGSDLPVKqisidFYGVEYYLADSMILHKQLALRM-LGKIFYL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 212 GPAFRAE--KHDTYRHLNEFISFDIEGAWMNDEDVMGVQERMIHHIWSqvaandlhlfEAINTYRASQDQDPVTVEIPSL 289
Cdd:PRK06462 109 SPNFRLEpvDKDTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVK----------ELLEEHEDELEFFGRDLPHLKR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 290 PFPRIPYCEAIEIVQNGGGEIEWGEDIESHHCDIIAAKYPGFHFLPRWPMSMKPFYiyhDESEKGSTGgqLSRGFDLNY- 368
Cdd:PRK06462 179 PFKRITHKEAVEILNEEGCRGIDLEELGSEGEKSLSEHFEEPFWIIDIPKGSREFY---DREDPERPG--VLRNYDLLLp 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663513271 369 -GRDEMTSGGQREHRVDVLEQNLRNMDLNPADFTFYTDGFRYGAPPHAGWGLGVARLLMILTGAGNVREVVLFPR 442
Cdd:PRK06462 254 eGYGEAVSGGEREYEYEEIVERIREHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQPFPR 328
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
9-441 |
1.55e-35 |
|
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: 137.47 E-value: 1.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 9 GAEVSIAGYAETVRGRGAIAFVMLRDGTGHIQAFLKKDNMDEDTFAAVQSASRESTIQVTGVVAqkrppKTKEGEPTppp 88
Cdd:COG1190 56 GDEVSVAGRIMAKRDMGKASFADLQDGSGRIQLYLRRDELGEEAYELFKLLDLGDIVGVEGTVF-----RTKTGELS--- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 89 eyeITVSEANILSAAATPLPV---GITDdvnvgLDIRLDNRHLDL-RRAHVNAMFQLRSKVLQYGRDHLIGEGFNEMNSP 164
Cdd:COG1190 128 ---VKVEELTLLSKSLRPLPEkfhGLTD-----PETRYRQRYVDLiVNPEVRETFRKRSKIIRAIRRFLDERGFLEVETP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 165 KI--IAsaseGGTNLFP----MMYFDTPAFLSQSPQLY-KQLAVlGGLERVFEIGPAFRAEKHDTyRHLNEFISfdIEG- 236
Cdd:COG1190 200 MLqpIA----GGAAARPfithHNALDMDLYLRIAPELYlKRLIV-GGFERVFEIGRNFRNEGIDT-THNPEFTM--LELy 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 237 -AWMNDEDVMGVQERMIHHiwsqvAANDLHlfeaiNTYRAS-QDQdpvTVEIpSLPFPRIPYCEAIEivQNGGGEIEWGE 314
Cdd:COG1190 272 qAYADYNDMMDLTEELIRE-----AAEAVL-----GTTKVTyQGQ---EIDL-SPPWRRITMVEAIK--EATGIDVTPLT 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 315 DIEShhCDIIAAKYpGFHFLPRWPMS---------------MKPFYIYH-----------DESEKGST--------GGQL 360
Cdd:COG1190 336 DDEE--LRALAKEL-GIEVDPGWGRGklidelfeelvepklIQPTFVTDypvevsplakrHRDDPGLTerfelfiaGREI 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 361 SRGF-DLNYGRDemtsggQREhRvdvLEQNLRN----------MDlnpADFtfytdgFR---YGAPPHAGWGLGVARLLM 426
Cdd:COG1190 413 ANAFsELNDPID------QRE-R---FEEQLELkaagddeampMD---EDF------LRaleYGMPPTGGLGIGIDRLVM 473
|
490
....*....|....*
gi 663513271 427 ILTGAGNVREVVLFP 441
Cdd:COG1190 474 LLTDSPSIRDVILFP 488
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
9-441 |
2.27e-35 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 136.76 E-value: 2.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 9 GAEVSIAGYAETVRGRGAIAFVMLRDGTGHIQAFLKKDNMDEDTFAAVQSASRESTIQVTGVVAqkrppKTKEGEPTppp 88
Cdd:PRK00484 54 EIEVSVAGRVMLKRVMGKASFATLQDGSGRIQLYVSKDDVGEEALEAFKKLDLGDIIGVEGTLF-----KTKTGELS--- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 89 eyeITVSEANILSAAATPLPV---GITDDvnvglDIRLDNRHLDL-RRAHVNAMFQLRSKVLQYGRDHLIGEGFNEMNSP 164
Cdd:PRK00484 126 ---VKATELTLLTKSLRPLPDkfhGLTDV-----ETRYRQRYVDLiVNPESRETFRKRSKIISAIRRFLDNRGFLEVETP 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 165 --KIIAsaseGGTNLFPMM----YFDTPAFLSQSPQLY-KQLAVlGGLERVFEIGPAFRAEKHDTyRHLNEFISFDIEGA 237
Cdd:PRK00484 198 mlQPIA----GGAAARPFIthhnALDIDLYLRIAPELYlKRLIV-GGFERVYEIGRNFRNEGIDT-RHNPEFTMLEFYQA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 238 WMNDEDVMGVQERMIHHIwsqvaANDLHLFEAInTYrasQDQdpvtvEIP-SLPFPRIPYCEAI-EIVqngggeiewGED 315
Cdd:PRK00484 272 YADYNDMMDLTEELIRHL-----AQAVLGTTKV-TY---QGT-----EIDfGPPFKRLTMVDAIkEYT---------GVD 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 316 IESHHCDII--AAKYPGFHFLPRW---------------PMSMKPFYIYH-----------DESEKGST--------GGQ 359
Cdd:PRK00484 329 FDDMTDEEAraLAKELGIEVEKSWglgklinelfeefvePKLIQPTFITDypveisplakrHREDPGLTerfelfigGRE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 360 LSRGF-DLNYGRDemtsggQREhRvdvLEQNLRN----------MDlnpADFtfytdgFR---YGAPPHAGWGLGVARLL 425
Cdd:PRK00484 409 IANAFsELNDPID------QRE-R---FEAQVEAkeagddeamfMD---EDF------LRaleYGMPPTGGLGIGIDRLV 469
|
490
....*....|....*.
gi 663513271 426 MILTGAGNVREVVLFP 441
Cdd:PRK00484 470 MLLTDSPSIRDVILFP 485
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
1-441 |
1.71e-33 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 132.42 E-value: 1.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 1 MNGGADLIGAEVSIAGYAETVRGRGAIAFVMLRDGTGHIQAFLKKDN--MDEDTFAAVQSASRESTIqvtgVVAQKRPPK 78
Cdd:PLN02502 100 LENGEELEDVSVSVAGRIMAKRAFGKLAFYDLRDDGGKIQLYADKKRldLDEEEFEKLHSLVDRGDI----VGVTGTPGK 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 79 TKEGEPTpppeyeITVSEANILSAAATPLP---VGITDdvnvgLDIRLDNRHLDL-RRAHVNAMFQLRSKVLQYGRDHLI 154
Cdd:PLN02502 176 TKKGELS------IFPTSFEVLTKCLLMLPdkyHGLTD-----QETRYRQRYLDLiANPEVRDIFRTRAKIISYIRRFLD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 155 GEGFNEMNSP--KIIAsaseGGTNLFPMMYF----DTPAFLSQSPQLY-KQLaVLGGLERVFEIGPAFRAEKHDTyRHLN 227
Cdd:PLN02502 245 DRGFLEVETPmlNMIA----GGAAARPFVTHhndlNMDLYLRIATELHlKRL-VVGGFERVYEIGRQFRNEGIST-RHNP 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 228 EFISFDIEGAWMNDEDVMGVQERMIhhiwSQVAandlhlfEAIN-----TYRAsqdqdpvtVEIpSL--PFPRIPyceAI 300
Cdd:PLN02502 319 EFTTCEFYQAYADYNDMMELTEEMV----SGMV-------KELTgsykiKYHG--------IEI-DFtpPFRRIS---MI 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 301 EIVQNGGGeIEWGEDIES--------HHCDIIAAKYPGFHFLPR----------------------WPMSMKPFYIYHdE 350
Cdd:PLN02502 376 SLVEEATG-IDFPADLKSdeanayliAACEKFDVKCPPPQTTGRllnelfeefleetlvqptfvldHPVEMSPLAKPH-R 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 351 SEKGstggqLSRGFDL-NYGRD------EMTSG-GQREHRVDVLEQnlRNMDLNPA---DFTFYTdGFRYGAPPHAGWGL 419
Cdd:PLN02502 454 SKPG-----LTERFELfINGRElanafsELTDPvDQRERFEEQVKQ--HNAGDDEAmalDEDFCT-ALEYGLPPTGGWGL 525
|
490 500
....*....|....*....|..
gi 663513271 420 GVARLLMILTGAGNVREVVLFP 441
Cdd:PLN02502 526 GIDRLVMLLTDSASIRDVIAFP 547
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
2-442 |
1.53e-30 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 123.95 E-value: 1.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 2 NGGADLIGAEVSIAGYAETVR--GRGAIAFVMLRDGTGHIQAFLKKDNMDEDTFAAVQSASresTIQVTGVVaqKRPPKT 79
Cdd:PLN02221 43 DGGAGLAGQKVRIGGWVKTGReqGKGTFAFLEVNDGSCPANLQVMVDSSLYDLSTLVATGT---CVTVDGVL--KVPPEG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 80 KeGEPTPPPEYEITVSEANILSAAATPLPvgitdDVNVGLDIRLDNRHLDLRRAHVNAMFQLRSkVLQYGRDHLIGE-GF 158
Cdd:PLN02221 118 K-GTKQKIELSVEKVIDVGTVDPTKYPLP-----KTKLTLEFLRDVLHLRSRTNSISAVARIRN-ALAFATHSFFQEhSF 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 159 NEMNSPKIIASASEGGTNLFPMM--------------------------------------------------------- 181
Cdd:PLN02221 191 LYIHTPIITTSDCEGAGEMFQVTtlinyterleqdlidnpppteadveaarlivkergevvaqlkaakaskeeitaavae 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 182 ---------------------------------YFDTPAFLSQSPQLYKQLAVLGgLERVFEIGPAFRAEKHDTYRHLNE 228
Cdd:PLN02221 271 lkiakeslahieersklkpglpkkdgkidyskdFFGRQAFLTVSGQLQVETYACA-LSSVYTFGPTFRAENSHTSRHLAE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 229 FISFDIEGAWMNDEDVMGVQERMIHHI--W-SQVAANDLHLFeAINTYRASQDQDPVtveIPSLPFPRIPYCEAIEIVQN 305
Cdd:PLN02221 350 FWMVEPEIAFADLEDDMNCAEAYVKYMckWlLDKCFDDMELM-AKNFDSGCIDRLRM---VASTPFGRITYTEAIELLEE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 306 ---GGGE----IEWGEDIESHH----CDIIAAKyPGFHFlpRWPMSMKPFYIYHDESEKGSTGGQLsrgfdLNYGRDEMT 374
Cdd:PLN02221 426 avaKGKEfdnnVEWGIDLASEHerylTEVLFQK-PLIVY--NYPKGIKAFYMRLNDDEKTVAAMDV-----LVPKVGELI 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663513271 375 SGGQREHRVDVLEQNLRNMDLNPADFTFYTDGFRYGAPPHAGWGLGVARLLMILTGAGNVREVVLFPR 442
Cdd:PLN02221 498 GGSQREERYDVIKQRIEEMGLPIEPYEWYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPR 565
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
182-442 |
1.18e-28 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 118.59 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 182 YFDTPAFLSQSPQLYKQlAVLGGLERVFEIGPAFRAEKHDTYRHLNEFISFDIEGAWMNDEDVMGVQERMIHHIWSQVAA 261
Cdd:PTZ00425 321 FFSKQAFLTVSGQLSLE-NLCSSMGDVYTFGPTFRAENSHTSRHLAEFWMIEPEIAFADLYDNMELAESYIKYCIGYVLN 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 262 N---DLHLFEA------INTYRASQDQDpvtveipslpFPRIPYCEAIEIVQNGGGE----IEWGEDIESHHCDIIAAK- 327
Cdd:PTZ00425 400 NnfdDIYYFEEnvetglISRLKNILDED----------FAKITYTNVIDLLQPYSDSfevpVKWGMDLQSEHERFVAEQi 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 328 YPGFHFLPRWPMSMKPFYIYHDESEKGSTGGQLsrgfdLNYGRDEMTSGGQREHRVDVLEQNLRNMDLNPADFTFYTDGF 407
Cdd:PTZ00425 470 FKKPVIVYNYPKDLKAFYMKLNEDQKTVAAMDV-----LVPKIGEVIGGSQREDNLERLDKMIKEKKLNMESYWWYRQLR 544
|
250 260 270
....*....|....*....|....*....|....*
gi 663513271 408 RYGAPPHAGWGLGVARLLMILTGAGNVREVVLFPR 442
Cdd:PTZ00425 545 KFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFPR 579
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
9-441 |
2.54e-27 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 115.45 E-value: 2.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 9 GAEVSIAGYAETVRGRGAIAFVMLRDGTGHIQAFLKKDNMDEDTFAAVQSA-SRESTIQVTGVVAQkrppkTKEGEPTpp 87
Cdd:PRK02983 651 GEEVSVSGRVLRIRDYGGVLFADLRDWSGELQVLLDASRLEQGSLADFRAAvDLGDLVEVTGTMGT-----SRNGTLS-- 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 88 peyeITVSEANILSAAATPLP---VGITDDvnvglDIRLDNRHLDLRrahVN----AMFQLRSKVLQYGRDHLIGEGFNE 160
Cdd:PRK02983 724 ----LLVTSWRLAGKCLRPLPdkwKGLTDP-----EARVRQRYLDLA---VNpearDLLRARSAVVRAVRETLVARGFLE 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 161 MNSPkiIASASEGGTNLFP----MMYFDTPAFLSQSPQLY-KQLAVlGGLERVFEIGPAFRAEKHDtYRHLNEFISFDIE 235
Cdd:PRK02983 792 VETP--ILQQVHGGANARPfvthINAYDMDLYLRIAPELYlKRLCV-GGVERVFELGRNFRNEGVD-ATHNPEFTLLEAY 867
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 236 GAWmNDEDVMGV-QERMIHHiwSQVAANDLHLFeaintYRASQDQDPVTVEIpSLPFPRIPYCEAI-EIVqngGGEIEWG 313
Cdd:PRK02983 868 QAH-ADYDTMRDlTRELIQN--AAQAAHGAPVV-----MRPDGDGVLEPVDI-SGPWPVVTVHDAVsEAL---GEEIDPD 935
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 314 EDIES--HHCDiiAAkypGFHFLPRWPMSMKPFYIYHDESEKGSTGGQLSRGFDLNygrdemTSGGQREHR--------- 382
Cdd:PRK02983 936 TPLAElrKLCD--AA---GIPYRTDWDAGAVVLELYEHLVEDRTTFPTFYTDFPTS------VSPLTRPHRsdpglaerw 1004
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 383 ----------------VDVLEQNLR--------------NMDLNpADFtfyTDGFRYGAPPHAGWGLGVARLLMILTGAg 432
Cdd:PRK02983 1005 dlvawgvelgtayselTDPVEQRRRlteqsllaaggdpeAMELD-EDF---LQALEYAMPPTGGLGMGVDRLVMLLTGR- 1079
|
....*....
gi 663513271 433 NVREVVLFP 441
Cdd:PRK02983 1080 SIRETLPFP 1088
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
139-441 |
7.26e-25 |
|
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: 104.59 E-value: 7.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 139 FQLRSKVLQYGRDHLIGEGFNEMNSP--KIIAsaseGGTNLFPMMYF----DTPAFLSQSPQLY-KQLAVlGGLERVFEI 211
Cdd:cd00775 8 FIVRSKIISYIRKFLDDRGFLEVETPmlQPIA----GGAAARPFITHhnalDMDLYLRIAPELYlKRLIV-GGFERVYEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 212 GPAFRAEKHDTyRHLNEFISFDIEGAWMNDEDVMGVQERMIHhiwsqvaandlHLFEAINtyrasqdqDPVTVEIPSL-- 289
Cdd:cd00775 83 GRNFRNEGIDL-THNPEFTMIEFYEAYADYNDMMDLTEDLFS-----------GLVKKIN--------GKTKIEYGGKel 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 290 ----PFPRIPYCEAIE---------------------IVQNGGGEIEW------------GEDIESHHCDiiaakyPGF- 331
Cdd:cd00775 143 dftpPFKRVTMVDALKektgidfpeldleqpeelaklLAKLIKEKIEKprtlgklldklfEEFVEPTLIQ------PTFi 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 332 -HFlprwPMSMKPFYIYHDeSEKGST--------GGQLSRGF-DLNYGRDemtsggQREHRVD-VLEQNLRNMDLNPADF 400
Cdd:cd00775 217 iDH----PVEISPLAKRHR-SNPGLTerfelficGKEIANAYtELNDPFD------QRERFEEqAKQKEAGDDEAMMMDE 285
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 663513271 401 TFYTdGFRYGAPPHAGWGLGVARLLMILTGAGNVREVVLFP 441
Cdd:cd00775 286 DFVT-ALEYGMPPTGGLGIGIDRLVMLLTDSNSIRDVILFP 325
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
8-446 |
1.82e-24 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 105.53 E-value: 1.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 8 IGAEVSIAGYAETVRGRGAIAFVMLRDGTGHIQAFLKKDNMDEDTFAAVQSASRESTIqvtgVVAQKRPPKTKEGEptpp 87
Cdd:PRK12445 64 LNIEVSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEGVYNDQFKKWDLGDI----IGARGTLFKTQTGE---- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 88 peYEITVSEANILSAAATPLP---VGITDDvnvglDIRLDNRHLDL-RRAHVNAMFQLRSKVLQYGRDHLIGEGFNEMNS 163
Cdd:PRK12445 136 --LSIHCTELRLLTKALRPLPdkfHGLQDQ-----EVRYRQRYLDLiANDKSRQTFVVRSKILAAIRQFMVARGFMEVET 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 164 PkiIASASEGGTNLFPMMY----FDTPAFLSQSPQLYKQLAVLGGLERVFEIGPAFRAEKhDTYRHLNEFISFDIEGAWM 239
Cdd:PRK12445 209 P--MMQVIPGGASARPFIThhnaLDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEG-ISVRHNPEFTMMELYMAYA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 240 NDEDVMGVQERMIHHIWSQVAANDL-----HLFEAINTYRASQDQDPVTVEIPSLPFPRIPYCEAIEIVQNGGG---EIE 311
Cdd:PRK12445 286 DYHDLIELTESLFRTLAQEVLGTTKvtygeHVFDFGKPFEKLTMREAIKKYRPETDMADLDNFDAAKALAESIGitvEKS 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 312 W--GEDIESHHCDIIAAKYPGFHFLPRWPMSMKPFyiyhdeSEKGSTGGQLSRGFDLNYGRDEMTSG----GQREHRVDV 385
Cdd:PRK12445 366 WglGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPL------ARRNDVNPEITDRFEFFIGGREIGNGfselNDAEDQAER 439
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663513271 386 LEQNLRNMDLNPADFTFYTDGF----RYGAPPHAGWGLGVARLLMILTGAGNVREVVLFPRDRSR 446
Cdd:PRK12445 440 FQEQVNAKAAGDDEAMFYDEDYvtalEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFPAMRPQ 504
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
67-444 |
1.55e-23 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 103.55 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 67 VTGVVAqkRPPKTKEGEPTPPPEyeitvsEANILSAAATPLPV--GITDDvnvglDIRLDNRHLDLR-RAHVNAMFQLRS 143
Cdd:PTZ00417 191 IVGIVG--FPGKSKKGELSIFPK------ETIILSPCLHMLPMkyGLKDT-----EIRYRQRYLDLMiNESTRSTFITRT 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 144 KVLQYGRDHLIGEGFNEMNSPKIIASAseGGTNLFPMMY----FDTPAFLSQSPQLYKQLAVLGGLERVFEIGPAFRAEK 219
Cdd:PTZ00417 258 KIINYLRNFLNDRGFIEVETPTMNLVA--GGANARPFIThhndLDLDLYLRIATELPLKMLIVGGIDKVYEIGKVFRNEG 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 220 HDTyRHLNEFISFDIEGAWMNDEDVMGVQErmihHIWSQVAandLHLFeaiNTYRAS-----QDQDPVTVEIpSLPFPRI 294
Cdd:PTZ00417 336 IDN-THNPEFTSCEFYWAYADFYDLIKWSE----DFFSQLV---MHLF---GTYKILynkdgPEKDPIEIDF-TPPYPKV 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 295 PYCEAIEIVQNGGGEIEWGED---------IESHHCDI-----------------IAAKYPGF-HFLPRWPMSMKPFYIY 347
Cdd:PTZ00417 404 SIVEELEKLTNTKLEQPFDSPetinkminlIKENKIEMpnpptaaklldqlashfIENKYPNKpFFIIEHPQIMSPLAKY 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 348 HdESEKGST--------GGQLSRGF-DLN--YGRDEMTSGGQREHrvdvleqnlRNMDLNPADF-TFYTDGFRYGAPPHA 415
Cdd:PTZ00417 484 H-RSKPGLTerlemficGKEVLNAYtELNdpFKQKECFSAQQKDR---------EKGDAEAFQFdAAFCTSLEYGLPPTG 553
|
410 420
....*....|....*....|....*....
gi 663513271 416 GWGLGVARLLMILTGAGNVREVVLFPRDR 444
Cdd:PTZ00417 554 GLGLGIDRITMFLTNKNCIKDVILFPTMR 582
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
4-132 |
4.82e-23 |
|
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: 94.13 E-value: 4.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 4 GADLIGAEVSIAGYAETVRGRGAIAFVMLRDGTGHIQAFLKKDNMDEdtFAAVQSASRESTIQVTGVVaQKRPPKTKEge 83
Cdd:cd04317 9 RESHVGQEVTLCGWVQRRRDHGGLIFIDLRDRYGIVQVVFDPEEAPE--FELAEKLRNESVIQVTGKV-RARPEGTVN-- 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 663513271 84 PT-PPPEYEITVSEANILSAAATpLPVGITDDVNVGLDIRLDNRHLDLRR 132
Cdd:cd04317 84 PKlPTGEIEVVASELEVLNKAKT-LPFEIDDDVNVSEELRLKYRYLDLRR 132
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
6-112 |
9.23e-22 |
|
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: 89.68 E-value: 9.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 6 DLIGAEVSIAGYAETVRGRGAIAFVMLRDGTGHIQAFLKKDNMDEDTFAAVQSASRESTIQVTGVVaqkrppktkEGEPT 85
Cdd:cd04316 9 ELDGEEVTVAGWVHEIRDLGGIKFVILRDREGIVQVTAPKKKVDKELFKTVRKLSRESVISVTGTV---------KAEPK 79
|
90 100
....*....|....*....|....*..
gi 663513271 86 PPPEYEITVSEANILSAAATPLPVGIT 112
Cdd:cd04316 80 APNGVEIIPEEIEVLSEAKTPLPLDPT 106
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
10-441 |
1.32e-21 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 97.80 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 10 AEVSIAGYAETVRGRGAIAFVMLRDGTGHIQAFLK-KDNMDEDTFAAVQSASRESTIqvtgVVAQKRPPKTKEGEptppp 88
Cdd:PTZ00385 108 ATVRVAGRVTSVRDIGKIIFVTIRSNGNELQVVGQvGEHFTREDLKKLKVSLRVGDI----IGADGVPCRMQRGE----- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 89 eYEITVSEANILSaaatplPVGITDDVnVGLDIR----LDNRHLDLRRAHVNAM--------FQLRSKVLQYGRDHLIGE 156
Cdd:PTZ00385 179 -LSVAASRMLILS------PYVCTDQV-VCPNLRgftvLQDNDVKYRYRFTDMMtnpcvietIKKRHVMLQALRDYFNER 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 157 GFNEMNSPKIIASASEGGTNLFPMMYFDTPA--FLSQSPQLYKQLAVLGGLERVFEIGPAFRAEKHDTyRHLNEFISFDI 234
Cdd:PTZ00385 251 NFVEVETPVLHTVASGANAKSFVTHHNANAMdlFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDADR-SHNPEFTSCEF 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 235 EGAWMNDEDVMGVQERMIHHIWSQVAANdlhlfEAINTYRASQDQDPVTVEIPSlPFPRIPYCEaiEIVQNGGGEIEWGE 314
Cdd:PTZ00385 330 YAAYHTYEDLMPMTEDIFRQLAMRVNGT-----TVVQIYPENAHGNPVTVDLGK-PFRRVSVYD--EIQRMSGVEFPPPN 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 315 DIES----HHCDIIAAKY----PGFH----------------------FLPRWPMSMKPFyiyhdESEKGSTGGQLSR-- 362
Cdd:PTZ00385 402 ELNTpkgiAYMSVVMLRYniplPPVRtaakmfeklidffitdrvveptFVMDHPLFMSPL-----AKEQVSRPGLAERfe 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 363 ----GFDLNYGRDEMTSGGQREHRV--DVLEQNLRNMDLNPADFTFYTDgFRYGAPPHAGWGLGVARLLMILTGAGNVRE 436
Cdd:PTZ00385 477 lfvnGIEYCNAYSELNDPHEQYHRFqqQLVDRQGGDEEAMPLDETFLKS-LQVGLPPTAGWGMGIDRALMLLTNSSNIRD 555
|
....*
gi 663513271 437 VVLFP 441
Cdd:PTZ00385 556 GIIFP 560
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
178-447 |
7.52e-21 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 95.32 E-value: 7.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 178 FPMMYFDTPAFLSQSPQLYKQlAVLGGLERVFEIGPAFRAEKHDTYRHLNEFISFDIEGAWMNDEDVMGVQERMIHHIWS 257
Cdd:PLN02532 363 FSKDFFSRPTYLTVSGRLHLE-SYACALGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAFSELEDAMNCAEDYFKFLCK 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 258 QVAAN---DLHLFeainTYRASQDQDPVTVEIPSLPFPRIPYCEAIEIVQNGGG-----EIEWGEDIESHHCDIIAAK-Y 328
Cdd:PLN02532 442 WVLENcseDMKFV----SKRIDKTISTRLEAIISSSLQRISYTEAVDLLKQATDkkfetKPEWGIALTTEHLSYLADEiY 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 329 PGFHFLPRWPMSMKPFYIYHDESekgstgGQLSRGFDLNYGR-DEMTSGGQREHRVDVLEQNLRNMDLNPADFTFYTDGF 407
Cdd:PLN02532 518 KKPVIIYNYPKELKPFYVRLNDD------GKTVAAFDLVVPKvGTVITGSQNEERMDILNARIEELGLPREQYEWYLDLR 591
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 663513271 408 RYGAPPHAGWGLGVARLLMILTGAGNVREVVLFPRDRSRV 447
Cdd:PLN02532 592 RHGTVKHSGFSLGFELMVLFATGLPDVRDAIPFPRSWGKA 631
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
11-101 |
5.23e-19 |
|
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. Class 2b aaRSs include the homodimeric aspartyl-, asparaginyl-, and lysyl-tRNA synthetases (AspRS, AsnRS, and LysRS). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Included in this group are archeal and archeal-like AspRSs which are non-discriminating and can charge both tRNAAsp and tRNAAsn. E. coli cells have two isoforms of LysRSs (LysS and LysU) encoded by two distinct genes, which are differentially regulated. The cytoplasmic and the mitochondrial isoforms of human LysRS are encoded by a single gene. Yeast cytoplasmic and mitochondrial LysRSs participate in mitochondrial import of cytoplasmic tRNAlysCUU. In addition to their housekeeping role, human LysRS may function as a signaling molecule that activates immune cells. Tomato LysRS may participate in a process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging. AsnRS is immunodominant antigen of the filarial nematode Brugia malayai and is of interest as a target for anti-parasitic drug design. Human AsnRS has been shown to be a pro-inflammatory chemokine which interacts with CCR3 chemokine receptors on T cells, immature dendritic cells and macrophages.
Pssm-ID: 239766 [Multi-domain] Cd Length: 85 Bit Score: 81.07 E-value: 5.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 11 EVSIAGYAETVRGRGAIAFVMLRDGTGHIQAFLKKDNMDEdTFAAVQSASRESTIQVTGVVaQKRPPKTkegepTPPPEY 90
Cdd:cd04100 1 EVTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEELGE-FFEEAEKLRTESVVGVTGTV-VKRPEGN-----LATGEI 73
|
90
....*....|.
gi 663513271 91 EITVSEANILS 101
Cdd:cd04100 74 ELQAEELEVLS 84
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
141-424 |
6.42e-13 |
|
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.
Pssm-ID: 238391 [Multi-domain] Cd Length: 211 Bit Score: 67.53 E-value: 6.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 141 LRSKVLQYGRDHLIGEGFNEMNSPKIIASASEGGTN------LFPMMYFDTPAFLSQSPQLYKQLAVLGGL----ERVFE 210
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGhepkdlLPVGAENEEDLYLRPTLEPGLVRLFVSHIrklpLRLAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 211 IGPAFRAEKHDTY-RHLNEFISFDIEGAWMNDEDVMGVQErMIHHIWSQVAandlHLFEAintyrasqdqDPVTVEIPSL 289
Cdd:cd00768 81 IGPAFRNEGGRRGlRRVREFTQLEGEVFGEDGEEASEFEE-LIELTEELLR----ALGIK----------LDIVFVEKTP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 290 PFPRIPYCEaieivqngggeiewgedieshhcdiiaakyPGFHFLPRWPmsmkpfyiyhdesekgstggqLSRGFdlnyg 369
Cdd:cd00768 146 GEFSPGGAG------------------------------PGFEIEVDHP---------------------EGRGL----- 169
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 663513271 370 rdEMTSGGQREHRVDvleqnlrnmdlNPADFTFYTDGFRYGAPPHAGWGLGVARL 424
Cdd:cd00768 170 --EIGSGGYRQDEQA-----------RAADLYFLDEALEYRYPPTIGFGLGLERL 211
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
11-101 |
1.52e-12 |
|
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: 63.02 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 11 EVSIAGYAETVRGRGAIAFVMLRDGTGHIQAFLKKDNMDEdtFAAVQSASRESTIQVTGVVaqKRPPKTKegepTPPPEY 90
Cdd:cd04323 1 RVKVFGWVHRLRSQKKLMFLVLRDGTGFLQCVLSKKLVTE--FYDAKSLTQESSVEVTGEV--KEDPRAK----QAPGGY 72
|
90
....*....|.
gi 663513271 91 EITVSEANILS 101
Cdd:cd04323 73 ELQVDYLEIIG 83
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
11-113 |
6.38e-10 |
|
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: 56.03 E-value: 6.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 11 EVSIAGYAETVRGRGA-IAFVMLRDGTGHIQAFL--KKDNMDEDTFAAVQSASRESTIQVTGVVaqKRPPKTKEGepTPP 87
Cdd:cd04320 1 EVLIRARVHTSRAQGAkLAFLVLRQQGYTIQGVLaaSAEGVSKQMVKWAGSLSKESIVDVEGTV--KKPEEPIKS--CTQ 76
|
90 100
....*....|....*....|....*.
gi 663513271 88 PEYEITVSEANILSAAATPLPVGITD 113
Cdd:cd04320 77 QDVELHIEKIYVVSEAAEPLPFQLED 102
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
12-100 |
1.10e-08 |
|
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: 51.85 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 12 VSIAGYAETV-RGRGAIAFVMLRDGTGHIQAFLKKDNMDEDtfaaVQSASRESTIQVTGVVaqkrppktkegEPTPPPEY 90
Cdd:pfam01336 1 VTVAGRVTSIrRSGGKLLFLTLRDGTGSIQVVVFKEEAEKL----AKKLKEGDVVRVTGKV-----------KKRKGGEL 65
|
90
....*....|
gi 663513271 91 EITVSEANIL 100
Cdd:pfam01336 66 ELVVEEIELL 75
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
11-128 |
5.64e-07 |
|
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: 47.90 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 11 EVSIAGYAETVRGRGAIAFVMLRDGTGHIQAFLKKdNMDEDTFAAVQSASRESTIQVTGVVAQkrppktkegEPTPPPEY 90
Cdd:cd04319 1 KVTLAGWVYRKREVGKKAFIVLRDSTGIVQAVFSK-DLNEEAYREAKKVGIESSVIVEGAVKA---------DPRAPGGA 70
|
90 100 110
....*....|....*....|....*....|....*...
gi 663513271 91 EITVSEANILSaAATPLPvgITDDVNVglDIRLDNRHL 128
Cdd:cd04319 71 EVHGEKLEIIQ-NVEFFP--ITEDASD--EFLLDVRHL 103
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
11-100 |
7.52e-06 |
|
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: 43.71 E-value: 7.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 11 EVSIAGYAETVRGRGAIAFVMLRDGT--GHIQAFLKKDNMDedtFAAVQSASRESTIQVTGVVaqKRPPKTKEgeptppp 88
Cdd:cd04318 1 EVTVNGWVRSVRDSKKISFIELNDGSclKNLQVVVDKELTN---FKEILKLSTGSSIRVEGVL--VKSPGAKQ------- 68
|
90
....*....|..
gi 663513271 89 EYEITVSEANIL 100
Cdd:cd04318 69 PFELQAEKIEVL 80
|
|
| ScAspRS_mt_like_N |
cd04321 |
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
11-102 |
1.28e-05 |
|
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: 43.46 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 11 EVSIAGYAETVRGRGA-IAFVMLRDGTGHIQAFLkkDNMDEDTFAAVQSASRESTIQVTGVVAQKRPpktKEGEPTppPE 89
Cdd:cd04321 1 KVTLNGWIDRKPRIVKkLSFADLRDPNGDIIQLV--STAKKDAFSLLKSITAESPVQVRGKLQLKEA---KSSEKN--DE 73
|
90
....*....|...
gi 663513271 90 YEITVSEANILSA 102
Cdd:cd04321 74 WELVVDDIQTLNA 86
|
|
| YhcR |
COG4085 |
DNA/RNA endonuclease YhcR, contains UshA esterase domain [RNA processing and modification]; |
6-72 |
3.16e-03 |
|
DNA/RNA endonuclease YhcR, contains UshA esterase domain [RNA processing and modification];
Pssm-ID: 443261 [Multi-domain] Cd Length: 131 Bit Score: 37.73 E-value: 3.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513271 6 DLIGAEVSIAGYAETVRGR--GAIAFVMLRDGTGHIQAFLKKDNMDEDTFAAVQ-SASRESTIQVTGVVA 72
Cdd:COG4085 39 EGLGEYVTVEGVVTAVKVArdGGILFLKLQDGTGGINVYAFGDVAEELLNYGPFpEIKEGDKVRVTGRVT 108
|
|
| |
