|
Name |
Accession |
Description |
Interval |
E-value |
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
2-432 |
0e+00 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 692.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 2 TKLISIKDA--PKYVDQEVKMHVWLTDKRSSGKIMFLQFRDGTAFFQAVLLKKNVsEELFEQAKNLRQEASLYVTGTINK 79
Cdd:PRK03932 1 MMRVSIKDIlkGKYVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDNG-EEYFEEIKKLTTGSSVIVTGTVVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 80 DERSHFGYELQISDFQVV-TNNDGYPIGNKEHGIDFLLDHRHLWLRSKRPFAIMKIRNVAFKAIVDYFEDNGFIKFDAPI 158
Cdd:PRK03932 80 SPRAGQGYELQATKIEVIgEDPEDYPIQKKRHSIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVDTPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 159 LMHSAPEGTTELFHI---------EYFNSDAYLSQSGQLYGEVGAHAFGKIFTFGPTFRAEESKTRRHLTEFWMMEPEMA 229
Cdd:PRK03932 160 ITASDCEGAGELFRVttldldfskDFFGKEAYLTVSGQLYAEAYAMALGKVYTFGPTFRAENSNTRRHLAEFWMIEPEMA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 230 WMHQDESLEIQEGLLKFVTKRILDNCEYELSILGR-----DPEKLRPTTEGNFARLSYDEAVKMLQDAGRDF----KWGD 300
Cdd:PRK03932 240 FADLEDNMDLAEEMLKYVVKYVLENCPDDLEFLNRrvdkgDIERLENFIESPFPRITYTEAIEILQKSGKKFefpvEWGD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 301 DFGAPDEAFISEQY-DRPVFILNYPTAIKPFYMKKNPENPlEYLCADVLAPeGYGEIIGGSEREEDYDTLKAQIEEAGLD 379
Cdd:PRK03932 320 DLGSEHERYLAEEHfKKPVFVTNYPKDIKAFYMRLNPDGK-TVAAMDLLAP-GIGEIIGGSQREERLDVLEARIKELGLN 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 496667790 380 LKDYEWYLDLRKYGSVPHSGFGIGFERFLGWICKLDHIREAIPFPRLINRLEP 432
Cdd:PRK03932 398 KEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
3-432 |
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: 663.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 3 KLISIKDA-PKYVDQEVKMHVWLTDKRSSGKIMFLQFRDGTAFFQAVLLKKNVseELFEQAKNLRQEASLYVTGTINKDE 81
Cdd:COG0017 1 KRTYIKDLlPEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKL--ENFEEAKKLTTESSVEVTGTVVESP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 82 RSHFGYELQISDFQVV-TNNDGYPIGNKEHGIDFLLDHRHLWLRSKRPFAIMKIRNVAFKAIVDYFEDNGFIKFDAPILM 160
Cdd:COG0017 79 RAPQGVELQAEEIEVLgEADEPYPLQPKRHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVEVHTPIIT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 161 HSAPEGTTELFHIEYFNSDAYLSQSGQLYGEVGAHAFGKIFTFGPTFRAEESKTRRHLTEFWMMEPEMAWMHQDESLEIQ 240
Cdd:COG0017 159 ASATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMALEKVYTFGPTFRAEKSNTRRHLAEFWMIEPEMAFADLEDVMDLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 241 EGLLKFVTKRILDNCEYELSILGRDPEKLRPTTEGNFARLSYDEAVKMLQDAGRDFKWGDDFGAPDEAFISEQY-DRPVF 319
Cdd:COG0017 239 EEMLKYIIKYVLENCPEELEFLGRDVERLEKVPESPFPRITYTEAIEILKKSGEKVEWGDDLGTEHERYLGEEFfKKPVF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 320 ILNYPTAIKPFYMKKNPENPLEYLCADVLAPeGYGEIIGGSEREEDYDTLKAQIEEAGLDLKDYEWYLDLRKYGSVPHSG 399
Cdd:COG0017 319 VTDYPKEIKAFYMKPNPDDPKTVAAFDLLAP-GIGEIIGGSQREHRYDVLVERIKEKGLDPEDYEWYLDLRRYGSVPHAG 397
|
410 420 430
....*....|....*....|....*....|...
gi 496667790 400 FGIGFERFLGWICKLDHIREAIPFPRLINRLEP 432
Cdd:COG0017 398 FGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
7-432 |
0e+00 |
|
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: 512.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 7 IKDAPKYVDQEVKMHVWLTDKRSSGKIMFLQFRDGT--AFFQAVLlKKNVSEELFEQAKNLRQEASLYVTGTINKDERSH 84
Cdd:TIGR00457 8 LQQVYKFVGDEVTVSGWVRTKRSSKKIIFLELNDGSslGPIQAVI-NGEDNPYLFQLLKSLTTGSSVSVTGKVVESPGKG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 85 FGYELQISDFQVV--TNNDGYPIGNKEHGIDFLLDHRHLWLRSKRPFAIMKIRNVAFKAIVDYFEDNGFIKFDAPILMHS 162
Cdd:TIGR00457 87 QPVELQVKKIEVVgeAEPDDYPLQKKEHSLEFLRDIAHLRLRTNTLGAVMRVRNALSQAIHRYFQENGFTWVSPPILTSN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 163 APEGTTELFHI---------EYFNSDAYLSQSGQLYGEVGAHAFGKIFTFGPTFRAEESKTRRHLTEFWMMEPEMAWMHQ 233
Cdd:TIGR00457 167 DCEGAGELFRVstgnidfsqDFFGKEAYLTVSGQLYLETYALALSKVYTFGPTFRAEKSNTSRHLSEFWMIEPEMAFANL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 234 DESLEIQEGLLKFVTKRILDNCEYELSILGRDPEK-----LRPTTEGNFARLSYDEAVKMLQDAGRDFK----WGDDFGA 304
Cdd:TIGR00457 247 NDLLQLAETLIKYIIKAVLENCSQELKFLEKNFDKdlikrLENIINNKFARITYTDAIEILKESDKNFEyedfWGDDLQT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 305 PDEAFISEQYD-RPVFILNYPTAIKPFYMKKNpENPLEYLCADVLAPeGYGEIIGGSEREEDYDTLKAQIEEAGLDLKDY 383
Cdd:TIGR00457 327 EHERFLAEEYFkPPVFVTNYPKDIKAFYMKLN-DDGKTVAAMDLLAP-GIGEIIGGSEREDDLDKLENRMKEMGLDTDAL 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 496667790 384 EWYLDLRKYGSVPHSGFGIGFERFLGWICKLDHIREAIPFPRLINRLEP 432
Cdd:TIGR00457 405 NWYLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGNINF 453
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
109-425 |
7.63e-143 |
|
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: 410.42 E-value: 7.63e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 109 EHGIDFLLDHRHLWLRSKRPFAIMKIRNVAFKAIVDYFEDNGFIKFDAPILMHSAPEGTTELFHIEYFNSDAYLSQSGQL 188
Cdd:cd00776 1 DANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 189 YGEVGAHAFGKIFTFGPTFRAEESKTRRHLTEFWMMEPEMAWM-HQDESLEIQEGLLKFVTKRILDNCEYELSILGRDPE 267
Cdd:cd00776 81 YKEMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAKELELVNQLNR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 268 KLRPtTEGNFARLSYDEAVKMLQDAG--RDFKWGDDFGAPDEAFISEQY-DRPVFILNYPTAIKPFYMKKNPENPLEYLC 344
Cdd:cd00776 161 ELLK-PLEPFPRITYDEAIELLREKGveEEVKWGEDLSTEHERLLGEIVkGDPVFVTDYPKEIKPFYMKPDDDNPETVES 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 345 ADVLAPeGYGEIIGGSEREEDYDTLKAQIEEAGLDLKDYEWYLDLRKYGSVPHSGFGIGFERFLGWICKLDHIREAIPFP 424
Cdd:cd00776 240 FDLLMP-GVGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
.
gi 496667790 425 R 425
Cdd:cd00776 319 R 319
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
1-432 |
8.79e-115 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 342.94 E-value: 8.79e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 1 MTKLISIKDAPKYVD-QEVKMHVWLTDKRSSGKIMFLQFRDGTAFFQAVLLKKNVsEELFEQAKNLRQEASLYVTGTINK 79
Cdd:PRK05159 1 MMKRHLTSELTPELDgEEVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKVD-EELFETIKKLKRESVVSVTGTVKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 80 DERSHFGYELQISDFQVVTN-NDGYPI---GNKEHGIDFLLDHRHLWLRSKRPFAIMKIRNVAFKAIVDYFEDNGFIKFD 155
Cdd:PRK05159 80 NPKAPGGVEVIPEEIEVLNKaEEPLPLdisGKVLAELDTRLDNRFLDLRRPRVRAIFKIRSEVLRAFREFLYENGFTEIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 156 APILMHSAPEGTTELFHIEYFNSDAYLSQSGQLYGE--VGAhAFGKIFTFGPTFRAEESKTRRHLTEFWMMEPEMAWMHQ 233
Cdd:PRK05159 160 TPKIVASGTEGGAELFPIDYFEKEAYLAQSPQLYKQmmVGA-GFERVFEIGPVFRAEEHNTSRHLNEYTSIDVEMGFIDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 234 DES-LEIQEGLLKFVTKRILDNCEYELSILGRDPeklrPTTEGNFARLSYDEAVKMLQDAGRDFKWGDDFGAPDEAFISE 312
Cdd:PRK05159 239 HEDvMDLLENLLRYMYEDVAENCEKELELLGIEL----PVPETPIPRITYDEAIEILKSKGNEISWGDDLDTEGERLLGE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 313 QYDR-----PVFILNYPTAIKPFYMKKNPENPLEYLCADVLAPEGygEIIGGSEREEDYDTLKAQIEEAGLDLKDYEWYL 387
Cdd:PRK05159 315 YVKEeygsdFYFITDYPSEKRPFYTMPDEDDPEISKSFDLLFRGL--EITSGGQRIHRYDMLVESIKEKGLNPESFEFYL 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 496667790 388 DLRKYGSVPHSGFGIGFERFLGWICKLDHIREAIPFPRLINRLEP 432
Cdd:PRK05159 393 EAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFPRDRHRLTP 437
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
2-426 |
5.92e-95 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 296.50 E-value: 5.92e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 2 TKLISIKDAP----KYVDQEVKMHVWLTDKRSSGKIMFLQFRDGTAF--FQAVLlkkNVSEELFEQAKN--LRQEASLYV 73
Cdd:PLN02603 90 LRIADVKGGEdeglARVGKTLNVMGWVRTLRAQSSVTFIEVNDGSCLsnMQCVM---TPDAEGYDQVESglITTGASVLV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 74 TGTINKDERSHFGYELQISDFQVVTNND-GYPIGNKEHGIDFLLDHRHLWLRSKRPFAIMKIRNVAFKAIVDYFEDNGFI 152
Cdd:PLN02603 167 QGTVVSSQGGKQKVELKVSKIVVVGKSDpSYPIQKKRVSREFLRTKAHLRPRTNTFGAVARVRNALAYATHKFFQENGFV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 153 KFDAPILMHSAPEGTTELFHI------------------------------EYFNSDAYLSQSGQLYGEVGAHAFGKIFT 202
Cdd:PLN02603 247 WVSSPIITASDCEGAGEQFCVttlipnsaenggslvddipktkdglidwsqDFFGKPAFLTVSGQLNGETYATALSDVYT 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 203 FGPTFRAEESKTRRHLTEFWMMEPEMAWMHQDESLEIQEGLLKFVTKRILDNCEYELSILGRDPEK-----LRPTTEGNF 277
Cdd:PLN02603 327 FGPTFRAENSNTSRHLAEFWMIEPELAFADLNDDMACATAYLQYVVKYILENCKEDMEFFNTWIEKgiidrLSDVVEKNF 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 278 ARLSYDEAVKMLQDAGRDF----KWGDDFGAPDEAFISEQY--DRPVFILNYPTAIKPFYMKKNPENPlEYLCADVLAPE 351
Cdd:PLN02603 407 VQLSYTDAIELLLKAKKKFefpvKWGLDLQSEHERYITEEAfgGRPVIIRDYPKEIKAFYMRENDDGK-TVAAMDMLVPR 485
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496667790 352 gYGEIIGGSEREEDYDTLKAQIEEAGLDLKDYEWYLDLRKYGSVPHSGFGIGFERFLGWICKLDHIREAIPFPRL 426
Cdd:PLN02603 486 -VGELIGGSQREERLEYLEARLDELKLNKESYWWYLDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFPRV 559
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
16-432 |
5.82e-88 |
|
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: 274.01 E-value: 5.82e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 16 QEVKMHVWLTDKRSSGKIMFLQFRDGTAFFQAVLLKKNVSEELFEQAKNLRQEASLYVTGTINKDERSHFGYELQISDFQ 95
Cdd:TIGR00458 13 QEVTFMGWVHEIRDLGGLIFVLLRDREGLIQITAPAKKVSKNLFKWAKKLNLESVVAVRGIVKIKEKAPGGFEIIPTKIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 96 VVTNNDG----YPIGNKEHGIDFLLDHRHLWLRSKRPFAIMKIRNVAFKAIVDYFEDNGFIKFDAPILMHSAPEGTTELF 171
Cdd:TIGR00458 93 VINEAKEplplDPTEKVPAELDTRLDYRFLDLRRPTVQAIFRIRSGVLESVREFLAEEGFIEVHTPKLVASATEGGTELF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 172 HIEYFNSDAYLSQSGQLYGEV-GAHAFGKIFTFGPTFRAEESKTRRHLTEFWMMEPEMAWMHQDESLEIQEGLLKFVTKR 250
Cdd:TIGR00458 173 PITYFEREAFLGQSPQLYKQQlMAAGFERVYEIGPIFRAEEHNTHRHLNEATSIDIEMAFEDHHDVMDILEELVVRVFED 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 251 ILDNCEYELSILGRDPEKlrptTEGNFARLSYDEAVKMLQDAGRDFKWGDDFGAPDEAFISEQYDRPVFILNYPTAIKPF 330
Cdd:TIGR00458 253 VPERCAHQLETLEFKLEK----PEGKFVRLTYDEAIEMANAKGVEIGWGEDLSTEAEKALGEEMDGLYFITDWPTEIRPF 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 331 YMKKNPENPLEYLCADVLapEGYGEIIGGSEREEDYDTLKAQIEEAGLDLKDYEWYLDLRKYGSVPHSGFGIGFERFLGW 410
Cdd:TIGR00458 329 YTMPDEDNPEISKSFDLM--YRDLEISSGAQRIHLHDLLVERIKAKGLNPEGFKDYLEAFSYGMPPHAGWGLGAERFVMF 406
|
410 420
....*....|....*....|..
gi 496667790 411 ICKLDHIREAIPFPRLINRLEP 432
Cdd:TIGR00458 407 LLGLKNIREAVLFPRDRKRLTP 428
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
6-425 |
6.64e-80 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 257.61 E-value: 6.64e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 6 SIKDAP----KYVDQEVKMHVWLTDKRSSGK--IMFLQFRDGTAffqAVLLKKNVSEELFEQAKNLRQEASLYVTGTIN- 78
Cdd:PLN02221 37 SILDRPdggaGLAGQKVRIGGWVKTGREQGKgtFAFLEVNDGSC---PANLQVMVDSSLYDLSTLVATGTCVTVDGVLKv 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 79 --KDERSHFGYELQISDFQVVTNNDG--YPIGNKEHGIDFLLDHRHLWLRSKRPFAIMKIRNVAFKAIVDYFEDNGFIKF 154
Cdd:PLN02221 114 ppEGKGTKQKIELSVEKVIDVGTVDPtkYPLPKTKLTLEFLRDVLHLRSRTNSISAVARIRNALAFATHSFFQEHSFLYI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 155 DAPILMHSAPEGTTELF--------------------------------------------------------------- 171
Cdd:PLN02221 194 HTPIITTSDCEGAGEMFqvttlinyterleqdlidnpppteadveaarlivkergevvaqlkaakaskeeitaavaelki 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 172 ------HIE---------------------YFNSDAYLSQSGQLYGEVGAHAFGKIFTFGPTFRAEESKTRRHLTEFWMM 224
Cdd:PLN02221 274 akeslaHIEersklkpglpkkdgkidyskdFFGRQAFLTVSGQLQVETYACALSSVYTFGPTFRAENSHTSRHLAEFWMV 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 225 EPEMAWMHQDESLEIQEGLLKFVTKRILDNCEYELSILGRD-----PEKLRPTTEGNFARLSYDEAVKMLQDA---GRDF 296
Cdd:PLN02221 354 EPEIAFADLEDDMNCAEAYVKYMCKWLLDKCFDDMELMAKNfdsgcIDRLRMVASTPFGRITYTEAIELLEEAvakGKEF 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 297 ----KWGDDFGAPDEAFISEQ-YDRPVFILNYPTAIKPFYMKKNpENPLEYLCADVLAPEgYGEIIGGSEREEDYDTLKA 371
Cdd:PLN02221 434 dnnvEWGIDLASEHERYLTEVlFQKPLIVYNYPKGIKAFYMRLN-DDEKTVAAMDVLVPK-VGELIGGSQREERYDVIKQ 511
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 496667790 372 QIEEAGLDLKDYEWYLDLRKYGSVPHSGFGIGFERFLGWICKLDHIREAIPFPR 425
Cdd:PLN02221 512 RIEEMGLPIEPYEWYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPR 565
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
111-426 |
2.06e-79 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 248.25 E-value: 2.06e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 111 GIDFLLDHRHLWLRSKRPFAIMKIRNVAFKAIVDYFEDNGFIKFDAPILMHSAPEGTTELF------HIEYFnsdaYLSQ 184
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFlvpsraLGKFY----ALPQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 185 SGQLYGE--VGAhAFGKIFTFGPTFRAEESKTRRHLtEFWMMEPEMAWMHQDESLEIQEGLLKFVTKRILDNCEYELSIL 262
Cdd:pfam00152 77 SPQLYKQllMVA-GFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGGT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 263 GRDPEKlrpttegNFARLSYDEAVKMLQDAGrDFKWGDDFGAPDEAF-----ISEQYDRPVFILNYPTAIKPFYMKKNPE 337
Cdd:pfam00152 155 LLDLKK-------PFPRITYAEAIEKLNGKD-VEELGYGSDKPDLRFllelvIDKNKFNPLWVTDFPAEHHPFTMPKDED 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 338 NPLEYLCADVLAPeGYgEIIGGSEREEDYDTLKAQIEEAGLD----LKDYEWYLDLRKYGSVPHSGFGIGFERFLGWICK 413
Cdd:pfam00152 227 DPALAEAFDLVLN-GV-EIGGGSIRIHDPELQEERFEEQGLDpeeaEEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTG 304
|
330
....*....|...
gi 496667790 414 LDHIREAIPFPRL 426
Cdd:pfam00152 305 LESIREVIAFPKT 317
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
12-425 |
1.24e-75 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 246.86 E-value: 1.24e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 12 KYVDQEVKMHVW--LTDKRSSGKIMFLQFRDGTAFFQ-AVLLKKNVS--EELFEQAKN--LRQEASLYVTGTINKDERSH 84
Cdd:PTZ00425 78 KYIDQIITVCGWskAVRKQGGGRFCFVNLNDGSCHLNlQIIVDQSIEnyEKLLKCGVGccFRFTGKLIISPVQNENKKGL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 85 F--GYELQISD-----FQVVTNN---DGYPIGNKEHGIDFLLDHRHLWLRSKRPFAIMKIRNVAFKAIVDYFEDNGFIKF 154
Cdd:PTZ00425 158 LkeNVELALKDnsihnFEIYGENldpQKYPLSKKNHGKEFLREVAHLRPRSYFISSVIRIRNALAIATHLFFQSRGFLYI 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 155 DAPILMHSAPEGTTELFHI------------------------------------------------------------- 173
Cdd:PTZ00425 238 HTPLITTSDCEGGGEMFTVttllgedadyraiprvnkknkkgekredilntcnannnngnssssnavsspaypdqylidy 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 174 --EYFNSDAYLSQSGQLYGEVGAHAFGKIFTFGPTFRAEESKTRRHLTEFWMMEPEMAWMHQDESLEIQEGLLKFVTKRI 251
Cdd:PTZ00425 318 kkDFFSKQAFLTVSGQLSLENLCSSMGDVYTFGPTFRAENSHTSRHLAEFWMIEPEIAFADLYDNMELAESYIKYCIGYV 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 252 LDNCEYELSILGRDPEK-----LRPTTEGNFARLSYDEAVKMLQDAGRDF----KWGDDFGAPDEAFISEQ-YDRPVFIL 321
Cdd:PTZ00425 398 LNNNFDDIYYFEENVETglisrLKNILDEDFAKITYTNVIDLLQPYSDSFevpvKWGMDLQSEHERFVAEQiFKKPVIVY 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 322 NYPTAIKPFYMKKNPENPlEYLCADVLAPEgYGEIIGGSEREEDYDTLKAQIEEAGLDLKDYEWYLDLRKYGSVPHSGFG 401
Cdd:PTZ00425 478 NYPKDLKAFYMKLNEDQK-TVAAMDVLVPK-IGEVIGGSQREDNLERLDKMIKEKKLNMESYWWYRQLRKFGSHPHAGFG 555
|
490 500
....*....|....*....|....
gi 496667790 402 IGFERFLGWICKLDHIREAIPFPR 425
Cdd:PTZ00425 556 LGFERLIMLVTGVDNIKDTIPFPR 579
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
122-425 |
1.64e-73 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 233.76 E-value: 1.64e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 122 WLRSKRPFAIMKIRNVAFKAIVDYFEDNGFIKFDAPI-------LMHSAPEGTTELFHIEYFNSDAYLSQSGQLYGEVGA 194
Cdd:PRK06462 20 HISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIispstdpLMGLGSDLPVKQISIDFYGVEYYLADSMILHKQLAL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 195 HAFGKIFTFGPTFRAE--ESKTRRHLTEFWMMEPEMAWMHQDESLEIQEGLLKFVTKRILDNCEYELSILGRDPEKLRpt 272
Cdd:PRK06462 100 RMLGKIFYLSPNFRLEpvDKDTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHEDELEFFGRDLPHLK-- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 273 teGNFARLSYDEAVKMLQDAGRDFKWGDDFGAPDEAFISEQYDRPVFILNYPTAIKPFYMKKNPENPLEYLCADVLAPEG 352
Cdd:PRK06462 178 --RPFKRITHKEAVEILNEEGCRGIDLEELGSEGEKSLSEHFEEPFWIIDIPKGSREFYDREDPERPGVLRNYDLLLPEG 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496667790 353 YGEIIGGSEREEDYDTLKAQIEEAGLDLKDYEWYLDLRKYGSVPHSGFGIGFERFLGWICKLDHIREAIPFPR 425
Cdd:PRK06462 256 YGEAVSGGEREYEYEEIVERIREHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQPFPR 328
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
11-432 |
1.81e-61 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 208.02 E-value: 1.81e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 11 PKYVDQEVKMHVWLTDKRSSGKIMFLQFRDGTAFFQAVLL--KKNVSEELFEQAKNLRQEASLYVTGTINKDERSHFG-- 86
Cdd:PLN02850 77 EELAGSEVLIRGRVHTIRGKGKSAFLVLRQSGFTVQCVVFvsEVTVSKGMVKYAKQLSRESVVDVEGVVSVPKKPVKGtt 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 87 --YELQISDFQVVTNNDG-YPI-----GNKEHGI---------------DFLLDHRHLWLRSKRPFAIMKIRNVAFKAIV 143
Cdd:PLN02850 157 qqVEIQVRKIYCVSKALAtLPFnvedaARSESEIekalqtgeqlvrvgqDTRLNNRVLDLRTPANQAIFRIQSQVCNLFR 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 144 DYFEDNGFIKFDAPILMHSAPEGTTELFHIEYFNSDAYLSQSGQLYGEVGAHA-FGKIFTFGPTFRAEESKTRRHLTEFW 222
Cdd:PLN02850 237 EFLLSKGFVEIHTPKLIAGASEGGSAVFRLDYKGQPACLAQSPQLHKQMAICGdFRRVFEIGPVFRAEDSFTHRHLCEFT 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 223 MMEPEMAW-MHQDESLEIQEGLLKFVTKRILDNCEYELSILGR-----DPEKLRPTTegnfaRLSYDEAVKMLQDAGRDF 296
Cdd:PLN02850 317 GLDLEMEIkEHYSEVLDVVDELFVAIFDGLNERCKKELEAIREqypfePLKYLPKTL-----RLTFAEGIQMLKEAGVEV 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 297 KWGDDFGAPDE----AFISEQYDRPVFILN-YPTAIKPFYMKKNPENPLEYLCADVLApEGYgEIIGGSEREEDYDTLKA 371
Cdd:PLN02850 392 DPLGDLNTESErklgQLVKEKYGTDFYILHrYPLAVRPFYTMPCPDDPKYSNSFDVFI-RGE-EIISGAQRVHDPELLEK 469
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496667790 372 QIEEAGLDLKDYEWYLDLRKYGSVPHSGFGIGFERFLGWICKLDHIREAIPFPRLINRLEP 432
Cdd:PLN02850 470 RAEECGIDVKTISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPRDPQRLAP 530
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
101-425 |
7.63e-61 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 208.57 E-value: 7.63e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 101 DGYPIGNKEHGIDFLLDHRHLWLRSKRPFAIMKIRNVAFKAIVDYFEDNGFIKFDAPILMHSAPEGTTELFHI------- 173
Cdd:PLN02532 204 EKYPLSKKRLPLDMLRDFSHFRPRTTTVASVTRVRSALTHATHTFFQDHGFLYVQVPIITTTDATGFGEMFRVttllgks 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 --------------------------------------------------------------------------------
Cdd:PLN02532 284 ddkeekkpvhetegisleavkaaikektnlveelkrsesnrealvaaeqdlrktnqlasqleakeklktgtsvkadklsf 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 174 --EYFNSDAYLSQSGQLYGEVGAHAFGKIFTFGPTFRAEESKTRRHLTEFWMMEPEMAWMHQDESLEIQEGLLKFVTKRI 251
Cdd:PLN02532 364 skDFFSRPTYLTVSGRLHLESYACALGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAFSELEDAMNCAEDYFKFLCKWV 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 252 LDNCEYELSILGRDPEK-----LRPTTEGNFARLSYDEAVKMLQDA-GRDFK----WGDDFGAPDEAFISEQ-YDRPVFI 320
Cdd:PLN02532 444 LENCSEDMKFVSKRIDKtistrLEAIISSSLQRISYTEAVDLLKQAtDKKFEtkpeWGIALTTEHLSYLADEiYKKPVII 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 321 LNYPTAIKPFYMKKNPEnpLEYLCA-DVLAPEGyGEIIGGSEREEDYDTLKAQIEEAGLDLKDYEWYLDLRKYGSVPHSG 399
Cdd:PLN02532 524 YNYPKELKPFYVRLNDD--GKTVAAfDLVVPKV-GTVITGSQNEERMDILNARIEELGLPREQYEWYLDLRRHGTVKHSG 600
|
410 420
....*....|....*....|....*.
gi 496667790 400 FGIGFERFLGWICKLDHIREAIPFPR 425
Cdd:PLN02532 601 FSLGFELMVLFATGLPDVRDAIPFPR 626
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
11-432 |
2.91e-43 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 159.39 E-value: 2.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 11 PKYVDQEVKMHVWLTDKRSSGKIMFLQFRDGTAFFQA-VLLKKNVSEELFEQAKNLRQEASLYVTGTINKDER-----SH 84
Cdd:PTZ00401 74 PELVDKTVLIRARVSTTRKKGKMAFMVLRDGSDSVQAmAAVEGDVPKEMIDFIGQIPTESIVDVEATVCKVEQpitstSH 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 85 FGYELQISDFQVVTNN--------DGYPIGNKEHGI----DFLLDHRHLWLRSKRPFAIMKIRNVAFKAIVDYFEDNGFI 152
Cdd:PTZ00401 154 SDIELKVKKIHTVTESlrtlpftlEDASRKESDEGAkvnfDTRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLIDSDFC 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 153 KFDAPILMHSAPEGTTELFHIEYFNSDAYLSQSGQLYGEVGAHA-FGKIFTFGPTFRAEESKTRRHLTEFWMMEPEMAW- 230
Cdd:PTZ00401 234 EIHSPKIINAPSEGGANVFKLEYFNRFAYLAQSPQLYKQMVLQGdVPRVFEVGPVFRSENSNTHRHLTEFVGLDVEMRIn 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 231 MHQDESLEIQEGLLKFV-------TKRILDNCE---YELSILGRDPEKLR------------PT---------TEGNFAR 279
Cdd:PTZ00401 314 EHYYEVLDLAESLFNYIferlathTKELKAVCQqypFEPLVWKLTPERMKelgvgvisegvePTdkyqarvhnMDSRMLR 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 280 LSYDEAVKMLQDA-GRDFKWGDDFGAPDEAF----ISEQYDRPVFILN-YPTAIKPFYMKKNPEnpleylcaDVLAPEGY 353
Cdd:PTZ00401 394 INYMHCIELLNTVlEEKMAPTDDINTTNEKLlgklVKERYGTDFFISDrFPSSARPFYTMECKD--------DERFTNSY 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 354 G------EIIGGSEREEDYDTLKAQIEEAGLDLKDYEWYLDLRKYGSVPHSGFGIGFERFLGWICKLDHIREAIPFPRLI 427
Cdd:PTZ00401 466 DmfirgeEISSGAQRIHDPDLLLARAKMLNVDLTPIKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFPRDP 545
|
....*
gi 496667790 428 NRLEP 432
Cdd:PTZ00401 546 QRTTP 550
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
132-425 |
3.69e-41 |
|
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: 147.24 E-value: 3.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 132 MKIRNVAFKAIVDYFEDNGFIKFDAPILMHSAPEGTTELFHIEYFNS--DAYLSQSGQLYGE-VGAHAFGKIFTFGPTFR 208
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALglDYYLRISPQLFKKrLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 209 AEESKTRrHLTEFWMMEPEMAWMHQDESLEIQEGLLKFVTKRILDNCEYELSILGRDPekLRPttegnFARLSYDEAVkm 288
Cdd:cd00669 81 NEDLRAR-HQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYGFELEDF--GLP-----FPRLTYREAL-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 289 lqdagrdfkwgddfgapdeafisEQYDRPVFILNYPTAIKPFYMKKNPENPLEYLCADVLApEGYgEIIGGSEREEDYDT 368
Cdd:cd00669 151 -----------------------ERYGQPLFLTDYPAEMHSPLASPHDVNPEIADAFDLFI-NGV-EVGNGSSRLHDPDI 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496667790 369 LKAQIEEAGLD----LKDYEWYLDLRKYGSVPHSGFGIGFERFLGWICKLDHIREAIPFPR 425
Cdd:cd00669 206 QAEVFQEQGINkeagMEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPK 266
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
17-97 |
2.53e-26 |
|
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: 101.16 E-value: 2.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 17 EVKMHVWLTDKRSSGKIMFLQFRDGTAFFQAVLLKKNVSEelFEQAKNLRQEASLYVTGTINKDERS---HFGYELQISD 93
Cdd:cd04323 1 RVKVFGWVHRLRSQKKLMFLVLRDGTGFLQCVLSKKLVTE--FYDAKSLTQESSVEVTGEVKEDPRAkqaPGGYELQVDY 78
|
....
gi 496667790 94 FQVV 97
Cdd:cd04323 79 LEII 82
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
132-424 |
5.75e-20 |
|
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: 89.17 E-value: 5.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 132 MKIRNVAFKAIVDYFEDNGFIKFDAPILMHSAPEGTTELF-----HIEYFNSdayLSQSGQLYGE---VGAhaFGKIFTF 203
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTPEGARDFLvpsrlHPGKFYA---LPQSPQLFKQllmVSG--FDRYFQI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 204 GPTFRAEESKTRRHlTEFWMMEPEMAWMHQDESLEIQEGLLKFVTKRILDnceyelsilgrdpeklrPTTEGNFARLSYD 283
Cdd:cd00777 76 ARCFRDEDLRADRQ-PEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG-----------------VELTTPFPRMTYA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 284 EAvkmLQDAGRDFKWGDDFgaPDEAFiSEQYDRPVFILNYPTAIKPFY---MKKNPENPLEYLCADVLapEGYgEIIGGS 360
Cdd:cd00777 138 EA---MERYGFKFLWIVDF--PLFEW-DEEEGRLVSAHHPFTAPKEEDldlLEKDPEDARAQAYDLVL--NGV-ELGGGS 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496667790 361 EREEDYDTLKAQIEEAGLDLKD----YEWYLDLRKYGSVPHSGFGIGFERFLGWICKLDHIREAIPFP 424
Cdd:cd00777 209 IRIHDPDIQEKVFEILGLSEEEaeekFGFLLEAFKYGAPPHGGIALGLDRLVMLLTGSESIRDVIAFP 276
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
27-424 |
6.99e-18 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 85.53 E-value: 6.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 27 KRSSGKIMFLQFRDGTAFFQAVLLKKNVSEELFEQAKNLRQEASLYVTGTI---NKDERShfgyeLQISDFQVVT---Nn 100
Cdd:PRK00484 66 KRVMGKASFATLQDGSGRIQLYVSKDDVGEEALEAFKKLDLGDIIGVEGTLfktKTGELS-----VKATELTLLTkslR- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 101 dgyPIGNKEHGidfLLD------HRHLWL----RSKRPFaimKIRNVAFKAIVDYFEDNGFIKFDAPIlMHSAPEG---- 166
Cdd:PRK00484 140 ---PLPDKFHG---LTDvetryrQRYVDLivnpESRETF---RKRSKIISAIRRFLDNRGFLEVETPM-LQPIAGGaaar 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 167 --TTelfHIEYFNSDAYLSQSGQLYGE---VGAhaFGKIFTFGPTFRAEESKTRrHLTEFWMMEPEMAWMHQDESLEIQE 241
Cdd:PRK00484 210 pfIT---HHNALDIDLYLRIAPELYLKrliVGG--FERVYEIGRNFRNEGIDTR-HNPEFTMLEFYQAYADYNDMMDLTE 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 242 GLLKFVTKRIL-------DNCEYELSilgrdpeklrptteGNFARLSYDEAVKmlQDAGRDFKWGDDFGAPD-------- 306
Cdd:PRK00484 284 ELIRHLAQAVLgttkvtyQGTEIDFG--------------PPFKRLTMVDAIK--EYTGVDFDDMTDEEARAlakelgie 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 307 ---------------EAFISEQYDRPVFILNYPTAIKPFyMKKNPENPleylcadvlapeGYGE----IIGGSER----- 362
Cdd:PRK00484 348 vekswglgklinelfEEFVEPKLIQPTFITDYPVEISPL-AKRHREDP------------GLTErfelFIGGREIanafs 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496667790 363 -----EEDYDTLKAQIE--EAG------LDlKDYewyldLR--KYGSVPHSGFGIGFERFLGWICKLDHIREAIPFP 424
Cdd:PRK00484 415 elndpIDQRERFEAQVEakEAGddeamfMD-EDF-----LRalEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
17-121 |
9.43e-18 |
|
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: 78.33 E-value: 9.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 17 EVKMHVWLTDKRSSGKIMFLQFRDGTAFFQAVLlKKNVSEELFEQAKNLRQEASLYVTGTINKDERSHFGYELQISDFQV 96
Cdd:cd04319 1 KVTLAGWVYRKREVGKKAFIVLRDSTGIVQAVF-SKDLNEEAYREAKKVGIESSVIVEGAVKADPRAPGGAEVHGEKLEI 79
|
90 100
....*....|....*....|....*
gi 496667790 97 VTNNDGYPIgNKEHGIDFLLDHRHL 121
Cdd:cd04319 80 IQNVEFFPI-TEDASDEFLLDVRHL 103
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
10-357 |
6.19e-16 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 80.03 E-value: 6.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 10 APKYVDQEVKMHVWLTDKRSSGKIMFLQFRDGTAFFQAVLLKKNVSEELFEQAKNLRQEASLYVTGTINK----DERSHF 85
Cdd:PRK12820 13 SLDDTGREVCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFSPEAAPADVYELAASLRAEFCVALQGEVQKrleeTENPHI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 86 ---GYELQISDFQVVTNNDGYPIGNKEHGI--------------DFLLDHRHLWLRSKRPFAIMKIRNVAFKAIVDYFED 148
Cdd:PRK12820 93 etgDIEVFVRELSILAASEALPFAISDKAMtagagsagadavneDLRLQYRYLDIRRPAMQDHLAKRHRIIKCARDFLDS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 149 NGFIKFDAPILMHSAPEGTTELF-----HIEYFNSdayLSQSGQLYGEVGAHA-FGKIFTFGPTFRAEESKTRRHlTEFW 222
Cdd:PRK12820 173 RGFLEIETPILTKSTPEGARDYLvpsriHPKEFYA---LPQSPQLFKQLLMIAgFERYFQLARCFRDEDLRPNRQ-PEFT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 223 MMEPEMAWMHQDESLEIQEGLlkfvTKRILDNCEYELSilgrdpeklRPttegnFARLSYDEAVKMLQDAGRDFKWGDDF 302
Cdd:PRK12820 249 QLDIEASFIDEEFIFELIEEL----TARMFAIGGIALP---------RP-----FPRMPYAEAMDTTGSDRPDLRFDLKF 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 496667790 303 GAPDEAFISEQYDRPVFILNYPTAIKPFYMKKNPENpleyLCADVLAPEGYGEII 357
Cdd:PRK12820 311 ADATDIFENTRYGIFKQILQRGGRIKGINIKGQSEK----LSKNVLQNEYAKEIA 361
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
23-97 |
2.09e-14 |
|
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: 68.36 E-value: 2.09e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496667790 23 WLTDKRSSGKIMFLQFRDGTAFFQAVlLKKNVSEELFEQAKNLRQEASLYVTGTINKDERSHF---GYELQISDFQVV 97
Cdd:cd04100 7 WVHSRRDHGGLIFIDLRDGSGIVQVV-VNKEELGEFFEEAEKLRTESVVGVTGTVVKRPEGNLatgEIELQAEELEVL 83
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
14-309 |
4.67e-14 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 74.05 E-value: 4.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 14 VDQEVKMHVWLTDKRSSGKIMFLQFRDGTAFFQAVLLKKNvSEELFEQAKNLRQEASLYVTGTI--------NKDERSHF 85
Cdd:PLN02903 71 VGSRVTLCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDE-FPEAHRTANRLRNEYVVAVEGTVrsrpqespNKKMKTGS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 86 ----GYELQIsdFQVVTNNDGYPIGNKEHGIDFL-----LDHRHLWLRSKRPFAIMKIRNVAFKAIVDYFED-NGFIKFD 155
Cdd:PLN02903 150 vevvAESVDI--LNVVTKSLPFLVTTADEQKDSIkeevrLRYRVLDLRRPQMNANLRLRHRVVKLIRRYLEDvHGFVEIE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 156 APILMHSAPEGTTELFHIEYFNSDAY--LSQSGQLYGEVGAHA-FGKIFTFGPTFRAEESKTRRHlTEFWMMEPEMAWMH 232
Cdd:PLN02903 228 TPILSRSTPEGARDYLVPSRVQPGTFyaLPQSPQLFKQMLMVSgFDRYYQIARCFRDEDLRADRQ-PEFTQLDMELAFTP 306
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496667790 233 QDESLEIQEGLLKFVTKRILDnceYELSilgrDPeklrpttegnFARLSYDEAVKmlqdagrdfKWGDDfgAPDEAF 309
Cdd:PLN02903 307 LEDMLKLNEDLIRQVFKEIKG---VQLP----NP----------FPRLTYAEAMS---------KYGSD--KPDLRY 355
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
12-285 |
1.34e-13 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 72.41 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 12 KYVDQEVKMHVWLTDKRSSGKIMFLQFRDGTAFFQAVLlkkNVSEELFEQAKNLRQEASLYVTG--------TINKDERS 83
Cdd:PRK00476 14 SHVGQTVTLCGWVHRRRDHGGLIFIDLRDREGIVQVVF---DPDAEAFEVAESLRSEYVIQVTGtvrarpegTVNPNLPT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 84 hfG-YELQISDFQVVTNNDGYPI---GNKEHGIDFLLDHRHLWLRSKRPFAIMKIRNVAFKAIVDYFEDNGFIKFDAPIL 159
Cdd:PRK00476 91 --GeIEVLASELEVLNKSKTLPFpidDEEDVSEELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDDNGFLEIETPIL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 160 MHSAPEGT------TELFHIEYFnsdAyLSQSGQLY-------GevgahaFGKIFTFGPTFRAEESKTRRhLTEFWMMEP 226
Cdd:PRK00476 169 TKSTPEGArdylvpSRVHPGKFY---A-LPQSPQLFkqllmvaG------FDRYYQIARCFRDEDLRADR-QPEFTQIDI 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 496667790 227 EMAWMHQDESLEIQEGLLKFVTKRILDnceYELSIlgrdpeklrpttegNFARLSYDEA 285
Cdd:PRK00476 238 EMSFVTQEDVMALMEGLIRHVFKEVLG---VDLPT--------------PFPRMTYAEA 279
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
17-426 |
1.63e-13 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 72.02 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 17 EVKMHVWLTDKRSSGKIMFLQFRDGTAFFQAVLLKKNVSEELF-EQAKNLRQEASLYVTGTINKDERSHFgyELQISDFQ 95
Cdd:PRK12445 67 EVSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEGVYnDQFKKWDLGDIIGARGTLFKTQTGEL--SIHCTELR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 96 VVTNNDgYPIGNKEHGI-DFLLDHRHLWL------RSKRPFaimKIRNVAFKAIVDYFEDNGFIKFDAPiLMHSAPEGTT 168
Cdd:PRK12445 145 LLTKAL-RPLPDKFHGLqDQEVRYRQRYLdliandKSRQTF---VVRSKILAAIRQFMVARGFMEVETP-MMQVIPGGAS 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 169 ELFHIEYFNS---DAYLSQSGQLY-GEVGAHAFGKIFTFGPTFRaEESKTRRHLTEFWMMEPEMAWMHQDESLEIQEGLL 244
Cdd:PRK12445 220 ARPFITHHNAldlDMYLRIAPELYlKRLVVGGFERVFEINRNFR-NEGISVRHNPEFTMMELYMAYADYHDLIELTESLF 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 245 KFVTKRILDNCEY----ELSILGRDPEKL---------RPTTegNFARLSYDEAVKMLQDA---GRDFKWG------DDF 302
Cdd:PRK12445 299 RTLAQEVLGTTKVtygeHVFDFGKPFEKLtmreaikkyRPET--DMADLDNFDAAKALAESigiTVEKSWGlgrivtEIF 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 303 GAPDEAFISEqydrPVFILNYPTAIKPFyMKKNPENP-----LEYLCADVLAPEGYGEIIGGSEREEDYDTlKAQIEEAG 377
Cdd:PRK12445 377 DEVAEAHLIQ----PTFITEYPAEVSPL-ARRNDVNPeitdrFEFFIGGREIGNGFSELNDAEDQAERFQE-QVNAKAAG 450
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 496667790 378 LDLKDY--EWYLDLRKYGSVPHSGFGIGFERFLGWICKLDHIREAIPFPRL 426
Cdd:PRK12445 451 DDEAMFydEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFPAM 501
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
140-426 |
3.73e-13 |
|
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: 69.92 E-value: 3.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 140 KAIVDYFEDNGFIKFDAPIlMHSAPEGTTELFHIEYFNS---DAYLSQSGQLYGE---VGAhaFGKIFTFGPTFRaEESK 213
Cdd:cd00775 16 SYIRKFLDDRGFLEVETPM-LQPIAGGAAARPFITHHNAldmDLYLRIAPELYLKrliVGG--FERVYEIGRNFR-NEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 214 TRRHLTEFWMMEPEMAWMHQDESLEIQEGLLKFVTKRILDNCEYELSilGRDPEKLRPttegnFARLSYDEAVKmlQDAG 293
Cdd:cd00775 92 DLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIEYG--GKELDFTPP-----FKRVTMVDALK--EKTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 294 RDFKWGDDFGAPDEA---------------------------FISEQYDRPVFILNYPTAIKPFyMKKNPENPleylcad 346
Cdd:cd00775 163 IDFPELDLEQPEELAkllaklikekiekprtlgklldklfeeFVEPTLIQPTFIIDHPVEISPL-AKRHRSNP------- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 347 vlapeGYGE----IIGGSEREEDYDTL------------KAQIEEAGLD---LKDYEwYLDLRKYGSVPHSGFGIGFERF 407
Cdd:cd00775 235 -----GLTErfelFICGKEIANAYTELndpfdqrerfeeQAKQKEAGDDeamMMDED-FVTALEYGMPPTGGLGIGIDRL 308
|
330
....*....|....*....
gi 496667790 408 LGWICKLDHIREAIPFPRL 426
Cdd:cd00775 309 VMLLTDSNSIRDVILFPAM 327
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
11-89 |
5.06e-13 |
|
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: 65.03 E-value: 5.06e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496667790 11 PKYVDQEVKMHVWLTDKRSSGKIMFLQFRDGTAFFQAVLLKKNVSEELFEQAKNLRQEASLYVTGTINKDERSHFGYEL 89
Cdd:cd04316 8 PELDGEEVTVAGWVHEIRDLGGIKFVILRDREGIVQVTAPKKKVDKELFKTVRKLSRESVISVTGTVKAEPKAPNGVEI 86
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
18-97 |
1.58e-12 |
|
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: 62.64 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 18 VKMHVWLTDK-RSSGKIMFLQFRDGTAFFQAVLLKknvsEELFEQAKNLRQEASLYVTGTINKDERShfGYELQISDFQV 96
Cdd:pfam01336 1 VTVAGRVTSIrRSGGKLLFLTLRDGTGSIQVVVFK----EEAEKLAKKLKEGDVVRVTGKVKKRKGG--ELELVVEEIEL 74
|
.
gi 496667790 97 V 97
Cdd:pfam01336 75 L 75
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
12-285 |
3.79e-10 |
|
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: 61.94 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 12 KYVDQEVKMHVWLTDKRSSGKIMFLQFRDGTAFFQaVLLKKNVSEELFEQAKNLRQEASLYVTG--------TINKDERS 83
Cdd:COG0173 13 SDVGQEVTLSGWVHRRRDHGGLIFIDLRDRYGITQ-VVFDPDDSAEAFEKAEKLRSEYVIAVTGkvrarpegTVNPKLPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 84 hfG-YELQISDFQVVTNNDGYPI---GNKEHGIDFLLDHRHLWLRSKRPFAIMKIRNVAFKAIVDYFEDNGFIKFDAPIL 159
Cdd:COG0173 92 --GeIEVLASELEILNKAKTPPFqidDDTDVSEELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDENGFLEIETPIL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 160 MHSAPEGttelfhieyfnsdA--------------Y-LSQSGQLY-------GevgahaFGKIFTFGPTFRAEESKTRRH 217
Cdd:COG0173 170 TKSTPEG-------------ArdylvpsrvhpgkfYaLPQSPQLFkqllmvsG------FDRYFQIARCFRDEDLRADRQ 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496667790 218 LtEFWMMEPEMAWMHQDESLEIQEGLLKFVTKRILDnceYELSilgrdpeklRPttegnFARLSYDEA 285
Cdd:COG0173 231 P-EFTQLDIEMSFVDQEDVFELMEGLIRHLFKEVLG---VELP---------TP-----FPRMTYAEA 280
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
134-407 |
1.00e-08 |
|
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: 55.20 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 134 IRNVAFKAIVDYFEDNGFIKFDAPILMHSAPEGTT------ELFHIEYFNSDAYLSQSG-----QLYGEVGAHAFGKIFT 202
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAghepkdLLPVGAENEEDLYLRPTLepglvRLFVSHIRKLPLRLAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 203 FGPTFRAEE-SKTRRHLTEFWMMEPEMAwMHQDESLEIQEGLLKFVtkrildnceYELsilgrdpeklrpttegnFARLs 281
Cdd:cd00768 81 IGPAFRNEGgRRGLRRVREFTQLEGEVF-GEDGEEASEFEELIELT---------EEL-----------------LRAL- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 282 ydeavkmlqdagrdfkwgddfgapdeafisEQYDRPVFILNYPTAIKPFYMKKNPEnpleylcADVLAPEGYGEIIGGSE 361
Cdd:cd00768 133 ------------------------------GIKLDIVFVEKTPGEFSPGGAGPGFE-------IEVDHPEGRGLEIGSGG 175
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 496667790 362 REEDYDTLKAQIeeagldlkdyEWYLDLRKYGSVPHSGFGIGFERF 407
Cdd:cd00768 176 YRQDEQARAADL----------YFLDEALEYRYPPTIGFGLGLERL 211
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
27-426 |
6.42e-07 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 51.53 E-value: 6.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 27 KRSSGKIMFLQFRDGTAFFQAVLLKKNVS--EELFEQAKNLRQEASLY-VTGTINKDERShfgyELQI--SDFQVVTNNd 101
Cdd:PLN02502 120 KRAFGKLAFYDLRDDGGKIQLYADKKRLDldEEEFEKLHSLVDRGDIVgVTGTPGKTKKG----ELSIfpTSFEVLTKC- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 102 GYPIGNKEHGidfLLD------HRHLWLRSKRPFA-IMKIRNVAFKAIVDYFEDNGFIKFDAPIlMHSAPEGTTELFHIE 174
Cdd:PLN02502 195 LLMLPDKYHG---LTDqetryrQRYLDLIANPEVRdIFRTRAKIISYIRRFLDDRGFLEVETPM-LNMIAGGAAARPFVT 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 175 YFNS---DAYLSQSGQLYGE---VGahAFGKIFTFGPTFRAEESKTrRHLTEFWMMEPEMAWMHQDESLEIQEGLLKFVT 248
Cdd:PLN02502 271 HHNDlnmDLYLRIATELHLKrlvVG--GFERVYEIGRQFRNEGIST-RHNPEFTTCEFYQAYADYNDMMELTEEMVSGMV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 249 KRI-----LDNCEYELSiLGRdP-------EKLRPTTEGNF-ARLSYDEAVKMLQDAGRDFKwgDDFGAPD--------- 306
Cdd:PLN02502 348 KELtgsykIKYHGIEID-FTP-PfrrismiSLVEEATGIDFpADLKSDEANAYLIAACEKFD--VKCPPPQttgrllnel 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 307 -EAFISEQYDRPVFILNYPTAIKPFyMKKNPENP-----LE-YLCADVLApEGYGEI---IGGSEREEDY--DTLKAQIE 374
Cdd:PLN02502 424 fEEFLEETLVQPTFVLDHPVEMSPL-AKPHRSKPglterFElFINGRELA-NAFSELtdpVDQRERFEEQvkQHNAGDDE 501
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 496667790 375 EAGLDlkdyEWYLDLRKYGSVPHSGFGIGFERFLGWICKLDHIREAIPFPRL 426
Cdd:PLN02502 502 AMALD----EDFCTALEYGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFPAM 549
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
12-79 |
4.79e-06 |
|
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli aspartyl-tRNA synthetase (AspRS), the human mitochondrial (mt) AspRS-2, the discriminating (D) Thermus thermophilus AspRS-1, and the nondiscriminating (ND) Helicobacter pylori AspRS. These homodimeric enzymes are class2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. Human mtAspRS participates in mitochondrial biosynthesis; this enzyme been shown to charge E.coli native tRNAsp in addition to in vitro transcribed human mitochondrial tRNAsp. T. thermophilus is rare among bacteria in having both a D_AspRS and a ND_AspRS. H.pylori ND-AspRS can charge both tRNAASp and tRNAAsn, it is fractionally more efficient at aminoacylating tRNAAsp over tRNAAsn. The H.pylori genome does not contain AsnRS.
Pssm-ID: 239812 [Multi-domain] Cd Length: 135 Bit Score: 45.98 E-value: 4.79e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496667790 12 KYVDQEVKMHVWLTDKRSSGKIMFLQFRDGTAFFQAVLLKKNVSEelFEQAKNLRQEASLYVTGTINK 79
Cdd:cd04317 11 SHVGQEVTLCGWVQRRRDHGGLIFIDLRDRYGIVQVVFDPEEAPE--FELAEKLRNESVIQVTGKVRA 76
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
23-97 |
7.50e-06 |
|
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: 44.48 E-value: 7.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496667790 23 WLTDKRS-SGKIMFLQFRDGTAFFQAVLLKK--NVSEELFEQAKNLRQEASLYVTGTINKDER-----SHFGYELQISDF 94
Cdd:cd04320 7 RVHTSRAqGAKLAFLVLRQQGYTIQGVLAASaeGVSKQMVKWAGSLSKESIVDVEGTVKKPEEpikscTQQDVELHIEKI 86
|
...
gi 496667790 95 QVV 97
Cdd:cd04320 87 YVV 89
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
23-97 |
4.68e-03 |
|
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: 36.00 E-value: 4.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496667790 23 WLTDKRSSGKIMFLQFRDGTAF--FQAVLlkkNVSEELFEQAKNLRQEASLYVTGTINKDERSHFGYELQISDFQVV 97
Cdd:cd04318 7 WVRSVRDSKKISFIELNDGSCLknLQVVV---DKELTNFKEILKLSTGSSIRVEGVLVKSPGAKQPFELQAEKIEVL 80
|
|
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