|
Name |
Accession |
Description |
Interval |
E-value |
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
1-436 |
3.23e-177 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 502.41 E-value: 3.23e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 1 MERILIADLSAHLET-EVLIRASVDVARQQGKMAFFDFRDRSGAVQGVVFGK--PDVLEVAKELKQEYAVEVKGIVHKrp 77
Cdd:PRK05159 2 MKRHLTSELTPELDGeEVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKvdEELFETIKKLKRESVVSVTGTVKA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 78 ekmvNANVQNGdIELEITGITIVN-AAEPMPFDLDGDLN--LDTLLDNRPLTLRRKRERAVFKVQATITKAWREYLDGEG 154
Cdd:PRK05159 80 ----NPKAPGG-VEVIPEEIEVLNkAEEPLPLDISGKVLaeLDTRLDNRFLDLRRPRVRAIFKIRSEVLRAFREFLYENG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 155 FTEFQAPKLVGGDAEGGSEVFKVDYFDdKKAFLATSPQLYKQMMVGV-FERVYTIGQMFRAERSATTRHLSEISMMDFEM 233
Cdd:PRK05159 155 FTEIFTPKIVASGTEGGAELFPIDYFE-KEAYLAQSPQLYKQMMVGAgFERVFEIGPVFRAEEHNTSRHLNEYTSIDVEM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 234 GHVTSYLDVIATVSGLVKHITKRVEETCANELAFLGAEKVLVPEVIPVLSLAEIHDIIQKETGVDKHAElDMEPEDERFI 313
Cdd:PRK05159 234 GFIDDHEDVMDLLENLLRYMYEDVAENCEKELELLGIELPVPETPIPRITYDEAIEILKSKGNEISWGD-DLDTEGERLL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 314 CEYAAKNLGSDFVFVTQFPTAKRAFYTKANVENPEYSDSFDLLFRGLEMCSGAERISNHDDLVAKIASRGMDPEKFAFYL 393
Cdd:PRK05159 313 GEYVKEEYGSDFYFITDYPSEKRPFYTMPDEDDPEISKSFDLLFRGLEITSGGQRIHRYDMLVESIKEKGLNPESFEFYL 392
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1083564008 394 QAFKHGIPRHGGIGMGLERMTMKFCGLGNVKEATLFPRDMNRI 436
Cdd:PRK05159 393 EAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFPRDRHRL 435
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
2-436 |
1.54e-165 |
|
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: 472.61 E-value: 1.54e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 2 ERILIADL-SAHLETEVLIRASVDVARQQGKMAFFDFRDRSGAVQGVVF-GKPDVLEVAKELKQEYAVEVKGIVHKRPEK 79
Cdd:COG0017 1 KRTYIKDLlPEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKkDKLENFEEAKKLTTESSVEVTGTVVESPRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 80 mvnanvqNGDIELEITGITIVN-AAEPMPFDLDgDLNLDTLLDNRPLTLRRKRERAVFKVQATITKAWREYLDGEGFTEF 158
Cdd:COG0017 81 -------PQGVELQAEEIEVLGeADEPYPLQPK-RHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVEV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 159 QAPKLVGGDAEGGSEVFKVDYFDdKKAFLATSPQLYKQMMVGVFERVYTIGQMFRAERSATTRHLSEISMMDFEMGHVTs 238
Cdd:COG0017 153 HTPIITASATEGGGELFPVDYFG-KEAYLTQSGQLYKEALAMALEKVYTFGPTFRAEKSNTRRHLAEFWMIEPEMAFAD- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 239 YLDVIATVSGLVKHITKRVEETCANELAFLGAEKVLVPEVI----PVLSLAEIHDIIQKEtGVDKHAELDMEPEDERFIC 314
Cdd:COG0017 231 LEDVMDLAEEMLKYIIKYVLENCPEELEFLGRDVERLEKVPespfPRITYTEAIEILKKS-GEKVEWGDDLGTEHERYLG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 315 EYAaknlGSDFVFVTQFPTAKRAFYTKANVENPEYSDSFDLLFRGL-EMCSGAERISNHDDLVAKIASRGMDPEKFAFYL 393
Cdd:COG0017 310 EEF----FKKPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAPGIgEIIGGSQREHRYDVLVERIKEKGLDPEDYEWYL 385
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1083564008 394 QAFKHGIPRHGGIGMGLERMTMKFCGLGNVKEATLFPRDMNRI 436
Cdd:COG0017 386 DLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRL 428
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
113-433 |
5.54e-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: 370.36 E-value: 5.54e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 113 DLNLDTLLDNRPLTLRRKRERAVFKVQATITKAWREYLDGEGFTEFQAPKLVGGDAEGGSEVFKVDYFDdKKAFLATSPQ 192
Cdd:cd00776 1 DANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFG-KPAYLAQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 193 LYKQMMVGVFERVYTIGQMFRAERSATTRHLSEISMMDFEMGHVTSYLDVIATVSGLVKHITKRVEETCANELAF---LG 269
Cdd:cd00776 80 LYKEMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEDYNEVMDLIEELIKYIFKRVLERCAKELELvnqLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 270 AEKVLVPEVIPVLSLAEIHDIIQKETGVDKH-AELDMEPEDERFICEYaaknLGSDFVFVTQFPTAKRAFYTKANVENPE 348
Cdd:cd00776 160 RELLKPLEPFPRITYDEAIELLREKGVEEEVkWGEDLSTEHERLLGEI----VKGDPVFVTDYPKEIKPFYMKPDDDNPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 349 YSDSFDLLFRG-LEMCSGAERISNHDDLVAKIASRGMDPEKFAFYLQAFKHGIPRHGGIGMGLERMTMKFCGLGNVKEAT 427
Cdd:cd00776 236 TVESFDLLMPGvGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAI 315
|
....*.
gi 1083564008 428 LFPRDM 433
Cdd:cd00776 316 LFPRDP 321
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
7-436 |
5.81e-108 |
|
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: 325.63 E-value: 5.81e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 7 ADLSAHLET-EVLIRASVDVARQQGKMAFFDFRDRSGAVQGVV---FGKPDVLEVAKELKQEYAVEVKGIVhKRPEKMVn 82
Cdd:TIGR00458 4 ADIKPEMDGqEVTFMGWVHEIRDLGGLIFVLLRDREGLIQITApakKVSKNLFKWAKKLNLESVVAVRGIV-KIKEKAP- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 83 anvqnGDIELEITGITIVNAA-EPMPFDLDGDL--NLDTLLDNRPLTLRRKRERAVFKVQATITKAWREYLDGEGFTEFQ 159
Cdd:TIGR00458 82 -----GGFEIIPTKIEVINEAkEPLPLDPTEKVpaELDTRLDYRFLDLRRPTVQAIFRIRSGVLESVREFLAEEGFIEVH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 160 APKLVGGDAEGGSEVFKVDYFDdKKAFLATSPQLYKQ-MMVGVFERVYTIGQMFRAERSATTRHLSEISMMDFEMGhVTS 238
Cdd:TIGR00458 157 TPKLVASATEGGTELFPITYFE-REAFLGQSPQLYKQqLMAAGFERVYEIGPIFRAEEHNTHRHLNEATSIDIEMA-FED 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 239 YLDVIATVSGLVKHITKRVEETCANELAFLGAEKVLVPEVIPVLSLAEIHDIIQKETGVDKHAElDMEPEDERFICEyaa 318
Cdd:TIGR00458 235 HHDVMDILEELVVRVFEDVPERCAHQLETLEFKLEKPEGKFVRLTYDEAIEMANAKGVEIGWGE-DLSTEAEKALGE--- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 319 kNLGSDFvFVTQFPTAKRAFYTKANVENPEYSDSFDLLFRGLEMCSGAERISNHDDLVAKIASRGMDPEKFAFYLQAFKH 398
Cdd:TIGR00458 311 -EMDGLY-FITDWPTEIRPFYTMPDEDNPEISKSFDLMYRDLEISSGAQRIHLHDLLVERIKAKGLNPEGFKDYLEAFSY 388
|
410 420 430
....*....|....*....|....*....|....*...
gi 1083564008 399 GIPRHGGIGMGLERMTMKFCGLGNVKEATLFPRDMNRI 436
Cdd:TIGR00458 389 GMPPHAGWGLGAERFVMFLLGLKNIREAVLFPRDRKRL 426
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
6-436 |
3.78e-106 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 324.35 E-value: 3.78e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 6 IADLSAHL-ETEVLIRASVDVARQQGKMAFFDFRDRSGAVQGVVFGKPDV-----LEVAKELKQEYAVEVKGIVhKRPEK 79
Cdd:PLN02850 72 VSDLGEELaGSEVLIRGRVHTIRGKGKSAFLVLRQSGFTVQCVVFVSEVTvskgmVKYAKQLSRESVVDVEGVV-SVPKK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 80 MVNANVQngDIELEITGI-TIVNAAEPMPFDLD-------------------GDLNLDTLLDNRPLTLRRKRERAVFKVQ 139
Cdd:PLN02850 151 PVKGTTQ--QVEIQVRKIyCVSKALATLPFNVEdaarseseiekalqtgeqlVRVGQDTRLNNRVLDLRTPANQAIFRIQ 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 140 ATITKAWREYLDGEGFTEFQAPKLVGGDAEGGSEVFKVDYFDdKKAFLATSPQLYKQMMV-GVFERVYTIGQMFRAERSA 218
Cdd:PLN02850 229 SQVCNLFREFLLSKGFVEIHTPKLIAGASEGGSAVFRLDYKG-QPACLAQSPQLHKQMAIcGDFRRVFEIGPVFRAEDSF 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 219 TTRHLSEISMMDFEMGHVTSYLDVIATVSGLVKHITKRVEETCANELAFLGAE------KVLVPEVipVLSLAEIHDIIq 292
Cdd:PLN02850 308 THRHLCEFTGLDLEMEIKEHYSEVLDVVDELFVAIFDGLNERCKKELEAIREQypfeplKYLPKTL--RLTFAEGIQML- 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 293 KETGVDKHAELDMEPEDERFICEYAAKNLGSDFVFVTQFPTAKRAFYTKANVENPEYSDSFDLLFRGLEMCSGAERIsnH 372
Cdd:PLN02850 385 KEAGVEVDPLGDLNTESERKLGQLVKEKYGTDFYILHRYPLAVRPFYTMPCPDDPKYSNSFDVFIRGEEIISGAQRV--H 462
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1083564008 373 D-DLVAKIASR-GMDPEKFAFYLQAFKHGIPRHGGIGMGLERMTMKFCGLGNVKEATLFPRDMNRI 436
Cdd:PLN02850 463 DpELLEKRAEEcGIDVKTISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPRDPQRL 528
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
115-432 |
1.15e-90 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 277.52 E-value: 1.15e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 115 NLDTLLDNRPLTLRRKRERAVFKVQATITKAWREYLDGEGFTEFQAPKLVGGDAEGGSEVFKV------DYFddkkaFLA 188
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVpsralgKFY-----ALP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 189 TSPQLYKQ-MMVGVFERVYTIGQMFRAERSATTRHLsEISMMDFEMGHVtSYLDVIATVSGLVKHITKRVEEtCANELaf 267
Cdd:pfam00152 76 QSPQLYKQlLMVAGFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFV-DYEDVMDLTEELIKEIFKEVEG-IAKEL-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 268 LGAEKVLVPEVIPVLSLAEIHDIIQKETGVDKhaELDMEPEDERFICEYAAKNLGSDFVFVTQFPTAKRAFYTKANVENP 347
Cdd:pfam00152 151 EGGTLLDLKKPFPRITYAEAIEKLNGKDVEEL--GYGSDKPDLRFLLELVIDKNKFNPLWVTDFPAEHHPFTMPKDEDDP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 348 EYSDSFDLLFRGLEMCSGAERISNHDDLVAKIASRGMDP----EKFAFYLQAFKHGIPRHGGIGMGLERMTMKFCGLGNV 423
Cdd:pfam00152 229 ALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDPeeaeEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESI 308
|
....*....
gi 1083564008 424 KEATLFPRD 432
Cdd:pfam00152 309 REVIAFPKT 317
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
1-437 |
6.49e-84 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 264.66 E-value: 6.49e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 1 MERILIADLSA--HLETEVLIRASVDVARQQGKMAFFDFRDRSGAVQGVVF--GKPDVLEVAKELKQEYAVEVKGIVHKR 76
Cdd:PRK03932 1 MMRVSIKDILKgkYVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVkdNGEEYFEEIKKLTTGSSVIVTGTVVES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 77 PEKmvnanvqNGDIELEITGITIV-NAAEPMPFDLDgDLNLDTLLDNRPLTLRRKRERAVFKVQATITKAWREYLDGEGF 155
Cdd:PRK03932 81 PRA-------GQGYELQATKIEVIgEDPEDYPIQKK-RHSIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 156 TEFQAPKLVGGDAEGGSEVFKV---------DYFdDKKAFLATSPQLYKQMMVGVFERVYTIGQMFRAERSATTRHLSEI 226
Cdd:PRK03932 153 VWVDTPIITASDCEGAGELFRVttldldfskDFF-GKEAYLTVSGQLYAEAYAMALGKVYTFGPTFRAENSNTRRHLAEF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 227 SMMDFEMGHVTsyLDVIATVS-GLVKHITKRVEETCANELAFLG----------AEKVLVPEvIPVLSLAEIHDIIQKEt 295
Cdd:PRK03932 232 WMIEPEMAFAD--LEDNMDLAeEMLKYVVKYVLENCPDDLEFLNrrvdkgdierLENFIESP-FPRITYTEAIEILQKS- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 296 gvDKHAE------LDMEPEDERFICEYAAKNLgsdfVFVTQFPTAKRAFYTKANVENPEYSdSFDLLFRGL-EMCSGAER 368
Cdd:PRK03932 308 --GKKFEfpvewgDDLGSEHERYLAEEHFKKP----VFVTNYPKDIKAFYMRLNPDGKTVA-AMDLLAPGIgEIIGGSQR 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083564008 369 ISNHDDLVAKIASRGMDPEKFAFYLQAFKHGIPRHGGIGMGLERMTMKFCGLGNVKEATLFPRDMNRID 437
Cdd:PRK03932 381 EERLDVLEARIKELGLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAE 449
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
5-437 |
1.97e-77 |
|
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative asparaginyl-tRNA synthetases (asnS), archaeal/eukaryotic type aspartyl-tRNA synthetases (aspS_arch), and bacterial type aspartyl-tRNA synthetases (aspS_bact), there is a striking similarity between asnS and aspS_arch in gap pattern and in sequence, and a striking divergence of aspS_bact. Consequently, a separate model was built for each of the three groups. This model, asnS, represents asparaginyl-tRNA synthetases from the three domains of life. Some species lack this enzyme and charge tRNA(asn) by misacylation with Asp, followed by transamidation of Asp to Asn. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273086 [Multi-domain] Cd Length: 453 Bit Score: 248.06 E-value: 1.97e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 5 LIADLSAHLETEVLIRASVDVARQQGKMAFFDFRDRS--GAVQGVVFGK--PDVLEVAKELKQEYAVEVKGIVHKRPEKm 80
Cdd:TIGR00457 7 LLQQVYKFVGDEVTVSGWVRTKRSSKKIIFLELNDGSslGPIQAVINGEdnPYLFQLLKSLTTGSSVSVTGKVVESPGK- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 81 vnanvqNGDIELEITGITIVNAAEPMPFDLD-GDLNLDTLLDNRPLTLRRKRERAVFKVQATITKAWREYLDGEGFTEFQ 159
Cdd:TIGR00457 86 ------GQPVELQVKKIEVVGEAEPDDYPLQkKEHSLEFLRDIAHLRLRTNTLGAVMRVRNALSQAIHRYFQENGFTWVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 160 APKLVGGDAEGGSEVFKV---------DYFDdKKAFLATSPQLYKQMMVGVFERVYTIGQMFRAERSATTRHLSEISMMD 230
Cdd:TIGR00457 160 PPILTSNDCEGAGELFRVstgnidfsqDFFG-KEAYLTVSGQLYLETYALALSKVYTFGPTFRAEKSNTSRHLSEFWMIE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 231 FEMGHVTsYLDVIATVSGLVKHITKRVEETCANELAFLGA--EKVLVP---EVI----PVLSLAEIHDIIQKEtgvDKHA 301
Cdd:TIGR00457 239 PEMAFAN-LNDLLQLAETLIKYIIKAVLENCSQELKFLEKnfDKDLIKrleNIInnkfARITYTDAIEILKES---DKNF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 302 E------LDMEPEDERFICEYAAKNLgsdfVFVTQFPTAKRAFYTKANvENPEYSDSFDLLFRGL-EMCSGAERISNHDD 374
Cdd:TIGR00457 315 EyedfwgDDLQTEHERFLAEEYFKPP----VFVTNYPKDIKAFYMKLN-DDGKTVAAMDLLAPGIgEIIGGSEREDDLDK 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083564008 375 LVAKIASRGMDPEKFAFYLQAFKHGIPRHGGIGMGLERMTMKFCGLGNVKEATLFPRDMNRID 437
Cdd:TIGR00457 390 LENRMKEMGLDTDALNWYLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGNIN 452
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
6-436 |
5.03e-76 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 247.21 E-value: 5.03e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 6 IADLS--AHLETEVLIRASVDVARQQGKMAFFDFRDRSGAVQGVVFGKPDV----LEVAKELKQEYAVEVKGIVHKRPEK 79
Cdd:PTZ00401 68 VAVLSkpELVDKTVLIRARVSTTRKKGKMAFMVLRDGSDSVQAMAAVEGDVpkemIDFIGQIPTESIVDVEATVCKVEQP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 80 MVNANVQngDIELEITGI-TIVNAAEPMPFDLD----------GDLNLDTLLDNRPLTLRRKRERAVFKVQATITKAWRE 148
Cdd:PTZ00401 148 ITSTSHS--DIELKVKKIhTVTESLRTLPFTLEdasrkesdegAKVNFDTRLNSRWMDLRTPASGAIFRLQSRVCQYFRQ 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 149 YLDGEGFTEFQAPKLVGGDAEGGSEVFKVDYFdDKKAFLATSPQLYKQMMV-GVFERVYTIGQMFRAERSATTRHLSEIS 227
Cdd:PTZ00401 226 FLIDSDFCEIHSPKIINAPSEGGANVFKLEYF-NRFAYLAQSPQLYKQMVLqGDVPRVFEVGPVFRSENSNTHRHLTEFV 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 228 MMDFEMGHVTSYLDVIATVSGLVKHI-------TKRVEETCaNELAFLGAEKVLVPEVIPVLSLAEIHDIIQKetgVDKH 300
Cdd:PTZ00401 305 GLDVEMRINEHYYEVLDLAESLFNYIferlathTKELKAVC-QQYPFEPLVWKLTPERMKELGVGVISEGVEP---TDKY 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 301 A--------------------------ELDMEPED------ERFICEYAAKNLGSDFVFVTQFPTAKRAFYTKANVENPE 348
Cdd:PTZ00401 381 QarvhnmdsrmlrinymhciellntvlEEKMAPTDdinttnEKLLGKLVKERYGTDFFISDRFPSSARPFYTMECKDDER 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 349 YSDSFDLLFRGLEMCSGAERISNHDDLVAKIASRGMDPEKFAFYLQAFKHGIPRHGGIGMGLERMTMKFCGLGNVKEATL 428
Cdd:PTZ00401 461 FTNSYDMFIRGEEISSGAQRIHDPDLLLARAKMLNVDLTPIKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASL 540
|
....*...
gi 1083564008 429 FPRDMNRI 436
Cdd:PTZ00401 541 FPRDPQRT 548
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
136-432 |
1.67e-55 |
|
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: 184.99 E-value: 1.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 136 FKVQATITKAWREYLDGEGFTEFQAPKLVGGDAEGGSEVFKVDYFD-DKKAFLATSPQLYKQ-MMVGVFERVYTIGQMFR 213
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNAlGLDYYLRISPQLFKKrLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 214 AErSATTRHLSEISMMDFEMGHVTsYLDVIATVSGLVKHITKRVEETCANELAFLGAEkvlVPEVIPVLSLAEihdiiqk 293
Cdd:cd00669 81 NE-DLRARHQPEFTMMDLEMAFAD-YEDVIELTERLVRHLAREVLGVTAVTYGFELED---FGLPFPRLTYRE------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 294 etgvdkhaeldmepederficeyAAKNLGSdFVFVTQFPTAKRAFYTKANVENPEYSDSFDLLFRGLEMCSGAERISNHD 373
Cdd:cd00669 149 -----------------------ALERYGQ-PLFLTDYPAEMHSPLASPHDVNPEIADAFDLFINGVEVGNGSSRLHDPD 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083564008 374 DLVAKIASRGMDPE----KFAFYLQAFKHGIPRHGGIGMGLERMTMKFCGLGNVKEATLFPRD 432
Cdd:cd00669 205 IQAEVFQEQGINKEagmeYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKM 267
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
133-431 |
1.54e-49 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 171.36 E-value: 1.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 133 RAVFKVQATITKAWREYLDGEGFTEFQAP-------KLVGGDAEGGSEVFKVDYFDdKKAFLATSPQLYKQMMVGVFERV 205
Cdd:PRK06462 27 RKVLKVQSSILRYTREFLDGRGFVEVLPPiispstdPLMGLGSDLPVKQISIDFYG-VEYYLADSMILHKQLALRMLGKI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 206 YTIGQMFRAE--RSATTRHLSEISMMDFEMGHvTSYLDVIATVSGLVKHITKRVEETCANELAFLGAEkvlVPEV---IP 280
Cdd:PRK06462 106 FYLSPNFRLEpvDKDTGRHLYEFTQLDIEIEG-ADLDEVMDLIEDLIKYLVKELLEEHEDELEFFGRD---LPHLkrpFK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 281 VLSLAEIHDIIQKEtGVDKHAELDMEPEDERFICEYAAKNlgsdfVFVTQFPTAKRAFYTKANVENPEYSDSFDLLF-RG 359
Cdd:PRK06462 182 RITHKEAVEILNEE-GCRGIDLEELGSEGEKSLSEHFEEP-----FWIIDIPKGSREFYDREDPERPGVLRNYDLLLpEG 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083564008 360 L-EMCSGAERISNHDDLVAKIASRGMDPEKFAFYLQAFKHGIPRHGGIGMGLERMTMKFCGLGNVKEATLFPR 431
Cdd:PRK06462 256 YgEAVSGGEREYEYEEIVERIREHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQPFPR 328
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
10-430 |
2.50e-46 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 168.71 E-value: 2.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 10 SAHLETEVLIRASVDVARQQGKMAFFDFRDRSGAVQGVVFGKPDVLEVAKELKQEYAVEVKGIVHKRPEKMVNANVQNGD 89
Cdd:PRK00476 13 ESHVGQTVTLCGWVHRRRDHGGLIFIDLRDREGIVQVVFDPDAEAFEVAESLRSEYVIQVTGTVRARPEGTVNPNLPTGE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 90 IELEITGITIVNAAEPMPFDLDGDLNL--DTLLDNRPLTLRRKRERAVFKVQATITKAWREYLDGEGFTEFQAPKLVGGD 167
Cdd:PRK00476 93 IEVLASELEVLNKSKTLPFPIDDEEDVseELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDDNGFLEIETPILTKST 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 168 AEGG------SEVFKVDYFddkkAfLATSPQLYKQM-MVGVFERVYTIGQMF-----RAERSattrhlSEISMMDFEMGH 235
Cdd:PRK00476 173 PEGArdylvpSRVHPGKFY----A-LPQSPQLFKQLlMVAGFDRYYQIARCFrdedlRADRQ------PEFTQIDIEMSF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 236 VTSyLDVIATVSGLVKHITKrveetcanelAFLGAEkvlVPEVIPVLSLAE-----------------IHDI--IQKETG 296
Cdd:PRK00476 242 VTQ-EDVMALMEGLIRHVFK----------EVLGVD---LPTPFPRMTYAEamrrygsdkpdlrfgleLVDVtdLFKDSG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 297 -----------------------------------------------------------VDKH----------AELDMEP 307
Cdd:PRK00476 308 fkvfagaandggrvkairvpggaaqlsrkqideltefakiygakglayikvnedglkgpIAKFlseeelaallERTGAKD 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 308 EDERFIC----EYAAKNLGS-----------------DFVFVTQFP------------------TA-KRAFYTKANVENP 347
Cdd:PRK00476 388 GDLIFFGadkaKVVNDALGAlrlklgkelglidedkfAFLWVVDFPmfeydeeegrwvaahhpfTMpKDEDLDELETTDP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 348 E--YSDSFDLLFRGLEMCSGAERIsnHD-DLVAKI-ASRGMDPE----KFAFYLQAFKHGIPRHGGIGMGLERMTMKFCG 419
Cdd:PRK00476 468 GkaRAYAYDLVLNGYELGGGSIRI--HRpEIQEKVfEILGISEEeaeeKFGFLLDALKYGAPPHGGIAFGLDRLVMLLAG 545
|
570
....*....|.
gi 1083564008 420 LGNVKEATLFP 430
Cdd:PRK00476 546 ADSIRDVIAFP 556
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
23-430 |
2.75e-42 |
|
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: 157.47 E-value: 2.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 23 VDVARQQGKMAFFDFRDRSGAVQgVVF---GKPDVLEVAKELKQEYAVEVKGIVHKRPEKMVNANVQNGDIELEITGITI 99
Cdd:COG0173 25 VHRRRDHGGLIFIDLRDRYGITQ-VVFdpdDSAEAFEKAEKLRSEYVIAVTGKVRARPEGTVNPKLPTGEIEVLASELEI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 100 VNAAEPMPFDLDGDLNL--DTLLDNRPLTLRRKRERAVFKVQATITKAWREYLDGEGFTEFQAPKLVGGDAEGG------ 171
Cdd:COG0173 104 LNKAKTPPFQIDDDTDVseELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDENGFLEIETPILTKSTPEGArdylvp 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 172 SEVFKVDYFddkkAfLATSPQLYKQM-MVGVFERVYTIGQMF-----RAERSAttrhlsEISMMDFEMGHVTSYlDVIAT 245
Cdd:COG0173 184 SRVHPGKFY----A-LPQSPQLFKQLlMVSGFDRYFQIARCFrdedlRADRQP------EFTQLDIEMSFVDQE-DVFEL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 246 VSGLVKHITKrveetcanelAFLGAEkvlVPEVIPVLSLAE-----------------IHDI--IQKETG---------- 296
Cdd:COG0173 252 MEGLIRHLFK----------EVLGVE---LPTPFPRMTYAEamerygsdkpdlrfgleLVDVtdIFKDSGfkvfagaaen 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 297 ------------------------------------------------VDKH----------AELDMEPEDERFIC---- 314
Cdd:COG0173 319 ggrvkainvpggaslsrkqideltefakqygakglayikvnedglkspIAKFlseeelaailERLGAKPGDLIFFVadkp 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 315 EYAAKNLGS-----------------DFVFVTQFP------TAKR------AFyTKANVE-------NPE--YSDSFDLL 356
Cdd:COG0173 399 KVVNKALGAlrlklgkelglidedefAFLWVVDFPlfeydeEEGRwvamhhPF-TMPKDEdldlletDPGkvRAKAYDLV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 357 FRGLEMCSGAERIsnHD-DLVAKIASR-GMDPE----KFAFYLQAFKHGIPRHGGIGMGLERMTMKFCGLGNVKEATLFP 430
Cdd:COG0173 478 LNGYELGGGSIRI--HDpELQEKVFELlGISEEeaeeKFGFLLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
15-431 |
6.02e-32 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 128.37 E-value: 6.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 15 TEVLIRASVDVARQQGKMAFFDFRDRSGAVQGVVFGK--PDVLEVAKELKQEYAVEVKGIVHKRPEKMVNANVQNGDIEL 92
Cdd:PLN02903 73 SRVTLCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDefPEAHRTANRLRNEYVVAVEGTVRSRPQESPNKKMKTGSVEV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 93 EITGITIVNA-AEPMPF------DLDGDLNLDTLLDNRPLTLRRKRERAVFKVQATITKAWREYL-DGEGFTEFQAPKLV 164
Cdd:PLN02903 153 VAESVDILNVvTKSLPFlvttadEQKDSIKEEVRLRYRVLDLRRPQMNANLRLRHRVVKLIRRYLeDVHGFVEIETPILS 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 165 GGDAEGG------SEVFKVDYFDdkkafLATSPQLYKQM-MVGVFERVYTIGQMFRAERSATTRHlSEISMMDFEMGhVT 237
Cdd:PLN02903 233 RSTPEGArdylvpSRVQPGTFYA-----LPQSPQLFKQMlMVSGFDRYYQIARCFRDEDLRADRQ-PEFTQLDMELA-FT 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 238 SYLDVIATVSGLVKHITKRVEE----------TCANELAFLGAEKvlvPEVIPVLSLAEIHDIIQK-----------ETG 296
Cdd:PLN02903 306 PLEDMLKLNEDLIRQVFKEIKGvqlpnpfprlTYAEAMSKYGSDK---PDLRYGLELVDVSDVFAEssfkvfagaleSGG 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 297 VDK----------------------------------------HAELD--------MEPED-ERFICE------------ 315
Cdd:PLN02903 383 VVKaicvpdgkkisnntalkkgdiyneaiksgakglaflkvldDGELEgikalvesLSPEQaEQLLAAcgagpgdlilfa 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 316 ----------------YAAKNLG------SDFVFVTQFP------TAKR--AFYTKANVENPEYSD--------SFDLLF 357
Cdd:PLN02903 463 agptssvnktldrlrqFIAKTLDlidpsrHSILWVTDFPmfewneDEQRleALHHPFTAPNPEDMGdlssaralAYDMVY 542
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564008 358 RGLEMCSGAERISNHDDLVAKIASRGMDPE----KFAFYLQAFKHGIPRHGGIGMGLERMTMKFCGLGNVKEATLFPR 431
Cdd:PLN02903 543 NGVEIGGGSLRIYRRDVQQKVLEAIGLSPEeaesKFGYLLEALDMGAPPHGGIAYGLDRLVMLLAGAKSIRDVIAFPK 620
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
90-431 |
1.78e-29 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 120.85 E-value: 1.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 90 IELEITGITIVNAAEPmPFDLDGDLN----LDTLLDNRPltlRRKRERAVFKVQATITKAWREYLDGEGFTEFQAPKLVG 165
Cdd:PLN02603 180 VELKVSKIVVVGKSDP-SYPIQKKRVsrefLRTKAHLRP---RTNTFGAVARVRNALAYATHKFFQENGFVWVSSPIITA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 166 GDAEGGSEVF--------------------------KVDYFDD---KKAFLATSPQLYKQMMVGVFERVYTIGQMFRAER 216
Cdd:PLN02603 256 SDCEGAGEQFcvttlipnsaenggslvddipktkdgLIDWSQDffgKPAFLTVSGQLNGETYATALSDVYTFGPTFRAEN 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 217 SATTRHLSEISMMDFEMGhVTSYLDVIATVSGLVKHITKRVEETCANELAFLGA--EKVLVPEVIPVLSLAEIH----DI 290
Cdd:PLN02603 336 SNTSRHLAEFWMIEPELA-FADLNDDMACATAYLQYVVKYILENCKEDMEFFNTwiEKGIIDRLSDVVEKNFVQlsytDA 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 291 IQKETGVDKHAE------LDMEPEDERFICEYAaknLGSDFVFVTQFPTAKRAFYTKANvENPEYSDSFDLLF-RGLEMC 363
Cdd:PLN02603 415 IELLLKAKKKFEfpvkwgLDLQSEHERYITEEA---FGGRPVIIRDYPKEIKAFYMREN-DDGKTVAAMDMLVpRVGELI 490
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564008 364 SGAERISNHDDLVAKIASRGMDPEKFAFYLQAFKHGIPRHGGIGMGLERMTMKFCGLGNVKEATLFPR 431
Cdd:PLN02603 491 GGSQREERLEYLEARLDELKLNKESYWWYLDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFPR 558
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
142-430 |
2.52e-29 |
|
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: 115.75 E-value: 2.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 142 ITKAWREYLDGEGFTEFQAPKLVGGDAEGGSEvFKVDYFDDKKAF--LATSPQLYKQM-MVGVFERVYTIGQMFRAERSA 218
Cdd:cd00777 7 VIKAIRNFLDEQGFVEIETPILTKSTPEGARD-FLVPSRLHPGKFyaLPQSPQLFKQLlMVSGFDRYFQIARCFRDEDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 219 TTRHlSEISMMDFEMGHVTSyLDVIATVSGLVKHITKRVEetcanelaflgaeKVLVPEVIPVLSLAEihdiiqketgvd 298
Cdd:cd00777 86 ADRQ-PEFTQIDIEMSFVDQ-EDIMSLIEGLLKYVFKEVL-------------GVELTTPFPRMTYAE------------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 299 khaeldmepederficeyAAKNLGSDFVFVTQFP------------------TAKRAFYTKANVENPE--YSDSFDLLFR 358
Cdd:cd00777 139 ------------------AMERYGFKFLWIVDFPlfewdeeegrlvsahhpfTAPKEEDLDLLEKDPEdaRAQAYDLVLN 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564008 359 GLEMCSGAERIsnHD-DLVAKI-ASRGMDPE----KFAFYLQAFKHGIPRHGGIGMGLERMTMKFCGLGNVKEATLFP 430
Cdd:cd00777 201 GVELGGGSIRI--HDpDIQEKVfEILGLSEEeaeeKFGFLLEAFKYGAPPHGGIALGLDRLVMLLTGSESIRDVIAFP 276
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
10-129 |
2.74e-28 |
|
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: 108.38 E-value: 2.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 10 SAHLETEVLIRASVDVARQQGKMAFFDFRDRSGAVQgVVFGK--PDVLEVAKELKQEYAVEVKGIVHKRPEKMVNANVQN 87
Cdd:cd04317 10 ESHVGQEVTLCGWVQRRRDHGGLIFIDLRDRYGIVQ-VVFDPeeAPEFELAEKLRNESVIQVTGKVRARPEGTVNPKLPT 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1083564008 88 GDIELEITGITIVNAAEPMPFDLDGDL--NLDTLLDNRPLTLRR 129
Cdd:cd04317 89 GEIEVVASELEVLNKAKTLPFEIDDDVnvSEELRLKYRYLDLRR 132
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
2-432 |
3.25e-28 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 117.78 E-value: 3.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 2 ERILIADLS-AHLETEVLIRASVDVARQQGKMAFFDFRDRSGAVQgVVFG----KPDVLEVAKELKQEYAVEVKGIVHKR 76
Cdd:PRK12820 5 DRSFCGHLSlDDTGREVCLAGWVDAFRDHGELLFIHLRDRNGFIQ-AVFSpeaaPADVYELAASLRAEFCVALQGEVQKR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 77 PEKMVNANVQNGDIELEITGITIVNAAEPMPFDLDGD-------------LNLDTLLDNRPLTLRRKRERAVFKVQATIT 143
Cdd:PRK12820 84 LEETENPHIETGDIEVFVRELSILAASEALPFAISDKamtagagsagadaVNEDLRLQYRYLDIRRPAMQDHLAKRHRII 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 144 KAWREYLDGEGFTEFQAPKLVGGDAEGGSEVFKVDYFDDKKAF-LATSPQLYKQ-MMVGVFERVYTIGQMFRAERSATTR 221
Cdd:PRK12820 164 KCARDFLDSRGFLEIETPILTKSTPEGARDYLVPSRIHPKEFYaLPQSPQLFKQlLMIAGFERYFQLARCFRDEDLRPNR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 222 H---------------------LSEISMMDFEMGHVT--------SYLDVIATVS------------------------G 248
Cdd:PRK12820 244 QpeftqldieasfideefifelIEELTARMFAIGGIAlprpfprmPYAEAMDTTGsdrpdlrfdlkfadatdifentryG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 249 LVKHITKR------------VEETCANELaflgaEKVLVPEVIPVLSLAEIHDIIQKETGVDKH-----AELDMEPEDER 311
Cdd:PRK12820 324 IFKQILQRggrikginikgqSEKLSKNVL-----QNEYAKEIAPSFGAKGMTWMRAEAGGLDSNivqffSADEKEALKRR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 312 FICE-------------------------YAAKNLG--SDFVF----VTQFP----------TAKRAFYTKANVENPE-- 348
Cdd:PRK12820 399 FHAEdgdviimiadascaivlsalgqlrlHLADRLGliPEGVFhplwITDFPlfeatddggvTSSHHPFTAPDREDFDpg 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 349 --------YSDSFDLLFRGLEMCSGAERISNHDDLVAKIASRGMDPE----KFAFYLQAFKHGIPRHGGIGMGLERMTMK 416
Cdd:PRK12820 479 dieelldlRSRAYDLVVNGEELGGGSIRINDKDIQLRIFAALGLSEEdiedKFGFFLRAFDFAAPPHGGIALGLDRVVSM 558
|
570
....*....|....*.
gi 1083564008 417 FCGLGNVKEATLFPRD 432
Cdd:PRK12820 559 ILQTPSIREVIAFPKN 574
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
23-437 |
2.82e-24 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 105.46 E-value: 2.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 23 VDVARQQGK--MAFFDFRDRSGAVQGVVFGKPDVLEVAKELKQEYAVEVKGIVHKRPEkmvnANVQNGDIELEITGITIV 100
Cdd:PLN02221 59 VKTGREQGKgtFAFLEVNDGSCPANLQVMVDSSLYDLSTLVATGTCVTVDGVLKVPPE----GKGTKQKIELSVEKVIDV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 101 NAAEPMPFDL-DGDLNLDTLLDNRPLTLRRKRERAVFKVQATITKAWREYLDGEGFTEFQAPKLVGGDAEGGSEVF---- 175
Cdd:PLN02221 135 GTVDPTKYPLpKTKLTLEFLRDVLHLRSRTNSISAVARIRNALAFATHSFFQEHSFLYIHTPIITTSDCEGAGEMFqvtt 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 --------------------------------------------------------------------------------
Cdd:PLN02221 215 linyterleqdlidnpppteadveaarlivkergevvaqlkaakaskeeitaavaelkiakeslahieersklkpglpkk 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 176 --KVDYFDD---KKAFLATSPQLYKQMMVGVFERVYTIGQMFRAERSATTRHLSEISMMDFEMGhVTSYLDVIATVSGLV 250
Cdd:PLN02221 295 dgKIDYSKDffgRQAFLTVSGQLQVETYACALSSVYTFGPTFRAENSHTSRHLAEFWMVEPEIA-FADLEDDMNCAEAYV 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 251 KHITKRVEETCANELAFLGA------------------EKVLVPEVIPVLSLAeihdiIQKETGVDKHAE--LDMEPEDE 310
Cdd:PLN02221 374 KYMCKWLLDKCFDDMELMAKnfdsgcidrlrmvastpfGRITYTEAIELLEEA-----VAKGKEFDNNVEwgIDLASEHE 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 311 RFICEYAAKNLgsdfVFVTQFPTAKRAFYTKANvENPEYSDSFDLLFRGL-EMCSGAERISNHDDLVAKIASRGMDPEKF 389
Cdd:PLN02221 449 RYLTEVLFQKP----LIVYNYPKGIKAFYMRLN-DDEKTVAAMDVLVPKVgELIGGSQREERYDVIKQRIEEMGLPIEPY 523
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1083564008 390 AFYLQAFKHGIPRHGGIGMGLERMTMKFCGLGNVKEATLFPRDMNRID 437
Cdd:PLN02221 524 EWYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPRYPGKAD 571
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
175-431 |
3.41e-24 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 105.11 E-value: 3.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 175 FKVDYFDdKKAFLATSPQLYKQMMVGVFERVYTIGQMFRAERSATTRHLSEISMMDFEMGHVTSYlDVIATVSGLVKHIT 254
Cdd:PTZ00425 317 YKKDFFS-KQAFLTVSGQLSLENLCSSMGDVYTFGPTFRAENSHTSRHLAEFWMIEPEIAFADLY-DNMELAESYIKYCI 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 255 KRVEETCANELAFL--GAEKVLVPEVIPVL--SLAEIH-----DIIQKETG---VDKHAELDMEPEDERFICEYAAKNLg 322
Cdd:PTZ00425 395 GYVLNNNFDDIYYFeeNVETGLISRLKNILdeDFAKITytnviDLLQPYSDsfeVPVKWGMDLQSEHERFVAEQIFKKP- 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 323 sdfVFVTQFPTAKRAFYTKANvENPEYSDSFDLLFRGL-EMCSGAERISNHDDLVAKIASRGMDPEKFAFYLQAFKHGIP 401
Cdd:PTZ00425 474 ---VIVYNYPKDLKAFYMKLN-EDQKTVAAMDVLVPKIgEVIGGSQREDNLERLDKMIKEKKLNMESYWWYRQLRKFGSH 549
|
250 260 270
....*....|....*....|....*....|
gi 1083564008 402 RHGGIGMGLERMTMKFCGLGNVKEATLFPR 431
Cdd:PTZ00425 550 PHAGFGLGFERLIMLVTGVDNIKDTIPFPR 579
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
133-430 |
1.47e-23 |
|
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: 100.74 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 133 RAVFKVQATITKAWREYLDGEGFTEFQAPKL--VGGDAEggSEVFKVDYFD-DKKAFLATSPQLY-KQMMVGVFERVYTI 208
Cdd:cd00775 5 RQTFIVRSKIISYIRKFLDDRGFLEVETPMLqpIAGGAA--ARPFITHHNAlDMDLYLRIAPELYlKRLIVGGFERVYEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 209 GQMFRAErSATTRHLSEISMMDFEMGHvTSYLDVIATVSGLVKHITKRVeetcanelafLGAEKVLVPEVIPVLS----L 284
Cdd:cd00775 83 GRNFRNE-GIDLTHNPEFTMIEFYEAY-ADYNDMMDLTEDLFSGLVKKI----------NGKTKIEYGGKELDFTppfkR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 285 AEIHDIIQKETGVDKHAELDMEPEDERFICEYAAK--------------NLGSDFV--------FVTQFPTAKRAFyTKA 342
Cdd:cd00775 151 VTMVDALKEKTGIDFPELDLEQPEELAKLLAKLIKekiekprtlgklldKLFEEFVeptliqptFIIDHPVEISPL-AKR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 343 NVENPEYSDSFDLLFRGLEMCSGAERISNHDD----LVAKIASRGMDPEKFAF----YLQAFKHGIPRHGGIGMGLERMT 414
Cdd:cd00775 230 HRSNPGLTERFELFICGKEIANAYTELNDPFDqrerFEEQAKQKEAGDDEAMMmdedFVTALEYGMPPTGGLGIGIDRLV 309
|
330
....*....|....*.
gi 1083564008 415 MKFCGLGNVKEATLFP 430
Cdd:cd00775 310 MLLTDSNSIRDVILFP 325
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
11-430 |
5.24e-21 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 95.13 E-value: 5.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 11 AHLETEVLIRASVDVARQQGKMAFFDFRDRSGAVQgvVFGKPDVLEVAKELKQEYAVEVKGIVHKRPEKMvnaNVQNGDI 90
Cdd:PRK12445 62 ESLNIEVSVAGRMMTRRIMGKASFVTLQDVGGRIQ--LYVARDSLPEGVYNDQFKKWDLGDIIGARGTLF---KTQTGEL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 91 ELEITGITIVNAA-EPMPFDLDGDLNLDTLLDNRPLTL-RRKRERAVFKVQATITKAWREYLDGEGFTEFQAP--KLVGG 166
Cdd:PRK12445 137 SIHCTELRLLTKAlRPLPDKFHGLQDQEVRYRQRYLDLiANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPmmQVIPG 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 167 DAEGGSEVFKVDYFDdKKAFLATSPQLY-KQMMVGVFERVYTIGQMFRAErSATTRHLSEISMMDFEMGHvTSYLDVIAT 245
Cdd:PRK12445 217 GASARPFITHHNALD-LDMYLRIAPELYlKRLVVGGFERVFEINRNFRNE-GISVRHNPEFTMMELYMAY-ADYHDLIEL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 246 VSGLVKHITKRV----EETCANELAFLGA--EKVLVPEVI----PVLSLAEIHDI-----IQKETGVDKHAELDMEPEDE 310
Cdd:PRK12445 294 TESLFRTLAQEVlgttKVTYGEHVFDFGKpfEKLTMREAIkkyrPETDMADLDNFdaakaLAESIGITVEKSWGLGRIVT 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 311 RFICEYAAKNLGSDfVFVTQFPtAKRAFYTKANVENPEYSDSFDLLFRGLEMCSGAERISNHDDLVAKI-----ASRGMD 385
Cdd:PRK12445 374 EIFDEVAEAHLIQP-TFITEYP-AEVSPLARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAERFqeqvnAKAAGD 451
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1083564008 386 PEKFAF---YLQAFKHGIPRHGGIGMGLERMTMKFCGLGNVKEATLFP 430
Cdd:PRK12445 452 DEAMFYdedYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
5-430 |
8.18e-21 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 94.39 E-value: 8.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 5 LIADLSA---HLETEVLIRASVDVA--------RQQGKMAFFDFRDRSGAVQgvVFGKPDvlEVAKELKQEYA------- 66
Cdd:PRK00484 34 TAAELRAkydDKEKEELEELEIEVSvagrvmlkRVMGKASFATLQDGSGRIQ--LYVSKD--DVGEEALEAFKkldlgdi 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 67 VEVKGIVHKrpekmvnanVQNGDIELEITGITIVNAA-EPMPFDLDGDLNLDTlldnrpltlR-RKRE---------RAV 135
Cdd:PRK00484 110 IGVEGTLFK---------TKTGELSVKATELTLLTKSlRPLPDKFHGLTDVET---------RyRQRYvdlivnpesRET 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 136 FKVQATITKAWREYLDGEGFTEFQAPKL--VGGDAEGGSEVFKVDYFDdKKAFLATSPQLY-KQMMVGVFERVYTIGQMF 212
Cdd:PRK00484 172 FRKRSKIISAIRRFLDNRGFLEVETPMLqpIAGGAAARPFITHHNALD-IDLYLRIAPELYlKRLIVGGFERVYEIGRNF 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 213 RAErSATTRHLSEISMMDFEMGHVTsYLDVIATVSGLVKHITKRVeetcanelafLGAEKVLVPEVipVLSLAE------ 286
Cdd:PRK00484 251 RNE-GIDTRHNPEFTMLEFYQAYAD-YNDMMDLTEELIRHLAQAV----------LGTTKVTYQGT--EIDFGPpfkrlt 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 287 IHDIIQKETGVDkhaeLDMEPEDErfiCEYAAKNLGSD-----------------FV--------FVTQFPT-----AKR 336
Cdd:PRK00484 317 MVDAIKEYTGVD----FDDMTDEE---ARALAKELGIEvekswglgklinelfeeFVepkliqptFITDYPVeisplAKR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 337 afytkaNVENPEYSDSFDLLFRGLEMCSG----------AERisnhddLVAKIASRGM-DPEKFAF---YLQAFKHGIPR 402
Cdd:PRK00484 390 ------HREDPGLTERFELFIGGREIANAfselndpidqRER------FEAQVEAKEAgDDEAMFMdedFLRALEYGMPP 457
|
490 500
....*....|....*....|....*...
gi 1083564008 403 HGGIGMGLERMTMKFCGLGNVKEATLFP 430
Cdd:PRK00484 458 TGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
159-431 |
2.31e-19 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 90.70 E-value: 2.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 159 QAPKLVGGDAEGGSEV-FKVDYFDdKKAFLATSPQLYKQMMVGVFERVYTIGQMFRAERSATTRHLSEISMMDFEMGhVT 237
Cdd:PLN02532 346 AKEKLKTGTSVKADKLsFSKDFFS-RPTYLTVSGRLHLESYACALGNVYTFGPRFRADRIDSARHLAEMWMVEVEMA-FS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 238 SYLDVIATVSGLVKHITKRVEETCANELAFLGAE---------KVLVPEVIPVLSLAEIHDIIQKETgvDKHAELDME-- 306
Cdd:PLN02532 424 ELEDAMNCAEDYFKFLCKWVLENCSEDMKFVSKRidktistrlEAIISSSLQRISYTEAVDLLKQAT--DKKFETKPEwg 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 307 ----PEDErficEYAAKNLGSDFVFVTQFPTAKRAFYTKANvENPEYSDSFDLLF-RGLEMCSGAERISNHDDLVAKIAS 381
Cdd:PLN02532 502 ialtTEHL----SYLADEIYKKPVIIYNYPKELKPFYVRLN-DDGKTVAAFDLVVpKVGTVITGSQNEERMDILNARIEE 576
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1083564008 382 RGMDPEKFAFYLQAFKHGIPRHGGIGMGLERMTMKFCGLGNVKEATLFPR 431
Cdd:PLN02532 577 LGLPREQYEWYLDLRRHGTVKHSGFSLGFELMVLFATGLPDVRDAIPFPR 626
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
11-430 |
3.25e-18 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 86.97 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 11 AHLET-EVLIRASVDVA------RQQGKMAFFDFRDRSGAVQgVVFGKPDVLEVAKELKQeyavevkgivhkrpekmVNA 83
Cdd:PLN02502 98 GSLENgEELEDVSVSVAgrimakRAFGKLAFYDLRDDGGKIQ-LYADKKRLDLDEEEFEK-----------------LHS 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 84 NVQNGDI-------------ELEI--TGITIVN-AAEPMPFDLDGDLNLDTLLDNRPLTLRRKRE-RAVFKVQATITKAW 146
Cdd:PLN02502 160 LVDRGDIvgvtgtpgktkkgELSIfpTSFEVLTkCLLMLPDKYHGLTDQETRYRQRYLDLIANPEvRDIFRTRAKIISYI 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 147 REYLDGEGFTEFQAPKLVGgdAEGGSEV--FKVDYFD-DKKAFLATSPQLY-KQMMVGVFERVYTIGQMFRAErSATTRH 222
Cdd:PLN02502 240 RRFLDDRGFLEVETPMLNM--IAGGAAArpFVTHHNDlNMDLYLRIATELHlKRLVVGGFERVYEIGRQFRNE-GISTRH 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 223 LSEISMMDFEMghvtSYLDVIATVSGLVKHITKRVEETCanelaflGAEKVLVPEVI----PVLSLAEIHDIIQKETGVD 298
Cdd:PLN02502 317 NPEFTTCEFYQ----AYADYNDMMELTEEMVSGMVKELT-------GSYKIKYHGIEidftPPFRRISMISLVEEATGID 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 299 KHAELDmEPEDERF---ICEYAAKNLGS-------------DFV--------FVTQFPT-----AKRafytkaNVENPEY 349
Cdd:PLN02502 386 FPADLK-SDEANAYliaACEKFDVKCPPpqttgrllnelfeEFLeetlvqptFVLDHPVemsplAKP------HRSKPGL 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 350 SDSFDLLFRGLEMCSG------------------AERISNHDDLVAkiasrgMDpEKFafyLQAFKHGIPRHGGIGMGLE 411
Cdd:PLN02502 459 TERFELFINGRELANAfseltdpvdqrerfeeqvKQHNAGDDEAMA------LD-EDF---CTALEYGLPPTGGWGLGID 528
|
490
....*....|....*....
gi 1083564008 412 RMTMKFCGLGNVKEATLFP 430
Cdd:PLN02502 529 RLVMLLTDSASIRDVIAFP 547
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
16-101 |
5.73e-18 |
|
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. Class 2b aaRSs include the homodimeric aspartyl-, asparaginyl-, and lysyl-tRNA synthetases (AspRS, AsnRS, and LysRS). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Included in this group are archeal and archeal-like AspRSs which are non-discriminating and can charge both tRNAAsp and tRNAAsn. E. coli cells have two isoforms of LysRSs (LysS and LysU) encoded by two distinct genes, which are differentially regulated. The cytoplasmic and the mitochondrial isoforms of human LysRS are encoded by a single gene. Yeast cytoplasmic and mitochondrial LysRSs participate in mitochondrial import of cytoplasmic tRNAlysCUU. In addition to their housekeeping role, human LysRS may function as a signaling molecule that activates immune cells. Tomato LysRS may participate in a process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging. AsnRS is immunodominant antigen of the filarial nematode Brugia malayai and is of interest as a target for anti-parasitic drug design. Human AsnRS has been shown to be a pro-inflammatory chemokine which interacts with CCR3 chemokine receptors on T cells, immature dendritic cells and macrophages.
Pssm-ID: 239766 [Multi-domain] Cd Length: 85 Bit Score: 78.38 E-value: 5.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 16 EVLIRASVDVARQQGKMAFFDFRDRSGAVQGVVFGK--PDVLEVAKELKQEYAVEVKGIVHKRPEKmvnaNVQNGDIELE 93
Cdd:cd04100 1 EVTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEelGEFFEEAEKLRTESVVGVTGTVVKRPEG----NLATGEIELQ 76
|
....*...
gi 1083564008 94 ITGITIVN 101
Cdd:cd04100 77 AEELEVLS 84
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
14-430 |
5.13e-17 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 83.54 E-value: 5.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 14 ETEVLIRAS--VDVARQQGKMAFFDFRDRSGAVQGVV-----FGKPDVLEVAKELKQEYAVEVKGIvhkrPEKMvnanvQ 86
Cdd:PTZ00385 105 AAQATVRVAgrVTSVRDIGKIIFVTIRSNGNELQVVGqvgehFTREDLKKLKVSLRVGDIIGADGV----PCRM-----Q 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 87 NGDIELEITGITIVNAAEPMPFDLDGDLNLDTLLDNRPLTLRRK-----RERAVF---KVQATITKAWREYLDGEGFTEF 158
Cdd:PTZ00385 176 RGELSVAASRMLILSPYVCTDQVVCPNLRGFTVLQDNDVKYRYRftdmmTNPCVIetiKKRHVMLQALRDYFNERNFVEV 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 159 QAPKL--VGGDAEGGSEVFKVDYfDDKKAFLATSPQLY-KQMMVGVFERVYTIGQMFRAErSATTRHLSEISMMDFEMGH 235
Cdd:PTZ00385 256 ETPVLhtVASGANAKSFVTHHNA-NAMDLFLRVAPELHlKQCIVGGMERIYEIGKVFRNE-DADRSHNPEFTSCEFYAAY 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 236 VTsYLDVIATVSGLVKHITKRVEETCANELAFLGAEKVLVP-EVIPVLSLAEIHDIIQKETGVdkhaelDMEPEDE---- 310
Cdd:PTZ00385 334 HT-YEDLMPMTEDIFRQLAMRVNGTTVVQIYPENAHGNPVTvDLGKPFRRVSVYDEIQRMSGV------EFPPPNElntp 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 311 RFICEYAAKNLGSDFvfvtQFP---TAKRAF---------------------------YTKANVENPEYSDSFDLLFRGL 360
Cdd:PTZ00385 407 KGIAYMSVVMLRYNI----PLPpvrTAAKMFeklidffitdrvveptfvmdhplfmspLAKEQVSRPGLAERFELFVNGI 482
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564008 361 EMCSGAERISNHDDLVAK-----IASRGMDPEKFAF---YLQAFKHGIPRHGGIGMGLERMTMKFCGLGNVKEATLFP 430
Cdd:PTZ00385 483 EYCNAYSELNDPHEQYHRfqqqlVDRQGGDEEAMPLdetFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFP 560
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
16-111 |
2.47e-13 |
|
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: 65.66 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 16 EVLIRASVDVARQQG-KMAFFDFRDRSGAVQGVVFGKPDV-----LEVAKELKQEYAVEVKGIVhKRPEKMVNANVQNgD 89
Cdd:cd04320 1 EVLIRARVHTSRAQGaKLAFLVLRQQGYTIQGVLAASAEGvskqmVKWAGSLSKESIVDVEGTV-KKPEEPIKSCTQQ-D 78
|
90 100
....*....|....*....|...
gi 1083564008 90 IELEITGI-TIVNAAEPMPFDLD 111
Cdd:cd04320 79 VELHIEKIyVVSEAAEPLPFQLE 101
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
17-100 |
1.96e-11 |
|
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: 59.56 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 17 VLIRASV-DVARQQGKMAFFDFRDRSGAVQGVVFgKPDVLEVAKELKQEYAVEVKGIVHKRPEkmvnanvqnGDIELEIT 95
Cdd:pfam01336 1 VTVAGRVtSIRRSGGKLLFLTLRDGTGSIQVVVF-KEEAEKLAKKLKEGDVVRVTGKVKKRKG---------GELELVVE 70
|
....*
gi 1083564008 96 GITIV 100
Cdd:pfam01336 71 EIELL 75
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
133-430 |
4.85e-10 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 61.56 E-value: 4.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 133 RAVFKVQATITKAWREYLDGEGFTEFQAP--KLVGGDAEggSEVFKVDYFD-DKKAFLATSPQL-YKQMMVGVFERVYTI 208
Cdd:PTZ00417 250 RSTFITRTKIINYLRNFLNDRGFIEVETPtmNLVAGGAN--ARPFITHHNDlDLDLYLRIATELpLKMLIVGGIDKVYEI 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 209 GQMFRAERSATTrHLSEISMMDFEMGHvTSYLDVIA----TVSGLVKHI--------TKRVEETCANELAFLGA-EKVLV 275
Cdd:PTZ00417 328 GKVFRNEGIDNT-HNPEFTSCEFYWAY-ADFYDLIKwsedFFSQLVMHLfgtykilyNKDGPEKDPIEIDFTPPyPKVSI 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 276 PEVIPVLSLAEIHDIIQKETGVDKHAELDMEPEDERFICEYAAK---NLGSDFVfVTQFPtaKRAFYTkanVENPE---- 348
Cdd:PTZ00417 406 VEELEKLTNTKLEQPFDSPETINKMINLIKENKIEMPNPPTAAKlldQLASHFI-ENKYP--NKPFFI---IEHPQimsp 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 349 ---YSDSFDLLFRGLEM-CSGAERISNHDDL------------VAKIASRGmDPEKFAF---YLQAFKHGIPRHGGIGMG 409
Cdd:PTZ00417 480 lakYHRSKPGLTERLEMfICGKEVLNAYTELndpfkqkecfsaQQKDREKG-DAEAFQFdaaFCTSLEYGLPPTGGLGLG 558
|
330 340
....*....|....*....|.
gi 1083564008 410 LERMTMKFCGLGNVKEATLFP 430
Cdd:PTZ00417 559 IDRITMFLTNKNCIKDVILFP 579
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
142-413 |
5.80e-10 |
|
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: 59.05 E-value: 5.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 142 ITKAWREYLDGEGFTEFQAPKLVG-GDAEGGSEVFKVDYF----DDKKAFLATSPQLYK-QMMVGV----FERVYTIGQM 211
Cdd:cd00768 5 IEQKLRRFMAELGFQEVETPIVERePLLEKAGHEPKDLLPvgaeNEEDLYLRPTLEPGLvRLFVSHirklPLRLAEIGPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 212 FRAE-RSATTRHLSEISMMDFEMGHVTsyldviatvsglvkhitkrveetcanelaflGAEKVLVPEVIpvlSLAEihDI 290
Cdd:cd00768 85 FRNEgGRRGLRRVREFTQLEGEVFGED-------------------------------GEEASEFEELI---ELTE--EL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 291 IQKETGVDkhaeldmepederficeyaaknlgsDFVFVTQFPTAKRAfytkanvenPEYSDSFDLLF-----RGLEMCSG 365
Cdd:cd00768 129 LRALGIKL-------------------------DIVFVEKTPGEFSP---------GGAGPGFEIEVdhpegRGLEIGSG 174
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1083564008 366 AERISNHDDLVAKIasrgmdpekfaFYLQAFKHGIPRHGGIGMGLERM 413
Cdd:cd00768 175 GYRQDEQARAADLY-----------FLDEALEYRYPPTIGFGLGLERL 211
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
16-100 |
8.77e-09 |
|
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: 52.24 E-value: 8.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 16 EVLIRASVDVARQQGKMAFFDFRDRSGAVQGVVFGKpDVLE--VAKELKQEYAVEVKGIVHKRPEkmvnANVQNGDIELE 93
Cdd:cd04323 1 RVKVFGWVHRLRSQKKLMFLVLRDGTGFLQCVLSKK-LVTEfyDAKSLTQESSVEVTGEVKEDPR----AKQAPGGYELQ 75
|
....*..
gi 1083564008 94 ITGITIV 100
Cdd:cd04323 76 VDYLEII 82
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
16-125 |
8.77e-06 |
|
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: 44.44 E-value: 8.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 16 EVLIRASVDVARQQGKMAFFDFRDRSGAVQgVVFGK---PDVLEVAKELKQEYAVEVKGIVHKRPEKmvnanvqNGDIEL 92
Cdd:cd04319 1 KVTLAGWVYRKREVGKKAFIVLRDSTGIVQ-AVFSKdlnEEAYREAKKVGIESSVIVEGAVKADPRA-------PGGAEV 72
|
90 100 110
....*....|....*....|....*....|...
gi 1083564008 93 EITGITIVNAAEPMPFDLDGDLNLdtLLDNRPL 125
Cdd:cd04319 73 HGEKLEIIQNVEFFPITEDASDEF--LLDVRHL 103
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
6-113 |
1.09e-05 |
|
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: 44.23 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 6 IADLSAHLE-TEVLIRASVDVARQQGKMAFFDFRDRSGAVQGVVFGK---PDVLEVAKELKQEYAVEVKGIVhKRPEKMV 81
Cdd:cd04316 3 SAEITPELDgEEVTVAGWVHEIRDLGGIKFVILRDREGIVQVTAPKKkvdKELFKTVRKLSRESVISVTGTV-KAEPKAP 81
|
90 100 110
....*....|....*....|....*....|...
gi 1083564008 82 NanvqngDIELEITGITIVNAAE-PMPFDLDGD 113
Cdd:cd04316 82 N------GVEIIPEEIEVLSEAKtPLPLDPTGK 108
|
|
| ScAspRS_mt_like_N |
cd04321 |
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
27-102 |
1.94e-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: 42.69 E-value: 1.94e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1083564008 27 RQQGKMAFFDFRDRSG-AVQGVVFGKPDVLEVAKELKQEYAVEVKGIVHKRPEKmvnANVQNGDIELEITGITIVNA 102
Cdd:cd04321 13 RIVKKLSFADLRDPNGdIIQLVSTAKKDAFSLLKSITAESPVQVRGKLQLKEAK---SSEKNDEWELVVDDIQTLNA 86
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
181-425 |
1.54e-04 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 43.38 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 181 DDKKAFLATSPQLY-KQMMVGVFERVYTIGQMFRAERSATtRHLSEISMMDFEMGHVtSYLDVIATVSGLVKHITKRVE- 258
Cdd:PRK09350 56 QGKTLWLMTSPEYHmKRLLAAGSGPIFQICKSFRNEEAGR-YHNPEFTMLEWYRPHY-DMYRLMNEVDDLLQQVLDCEPa 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 259 ETCANELAF--------LGAEKVLVPEVIPVLSLAEIHDIiqketgvdkhaELDMEPEDERFICEYAAKNLGSDF-VFVT 329
Cdd:PRK09350 134 ESLSYQQAFlrylgidpLSADKTQLREVAAKLGLSNIADE-----------EEDRDTLLQLLFTFGVEPNIGKEKpTFVY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564008 330 QFPtAKRAFYTKANVENPEYSDSFDLLFRGLEMCSGAERISNHDDLV-------AKIASRGMDPEKF-AFYLQAFKHGIP 401
Cdd:PRK09350 203 HFP-ASQAALAKISTEDHRVAERFEVYFKGIELANGFHELTDAREQRqrfeqdnRKRAARGLPQQPIdENLIAALEAGLP 281
|
250 260
....*....|....*....|....
gi 1083564008 402 RHGGIGMGLERMTMKFCGLGNVKE 425
Cdd:PRK09350 282 DCSGVALGVDRLIMLALGAESISE 305
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
27-75 |
4.02e-03 |
|
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These enzymes are homodimeric class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Included in this group are E. coli LysS and LysU. These two isoforms of LysRS are encoded by distinct genes which are differently regulated. Eukaryotes contain 2 sets of aaRSs, both of which encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Saccharomyces cerevisiae cytoplasmic and mitochondrial LysRSs have been shown to participate in the mitochondrial import of the only nuclear-encoded tRNA of S. cerevisiae (tRNAlysCUU). The gene for human LysRS encodes both the cytoplasmic and the mitochondrial isoforms of LysRS. In addition to their housekeeping role, human lysRS may function as a signaling molecule that activates immune cells and tomato LysRS may participate in a root-specific process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging.
Pssm-ID: 239817 [Multi-domain] Cd Length: 108 Bit Score: 36.69 E-value: 4.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1083564008 27 RQQGKMAFFDFRDRSGAVQgVVFGKPDVLEVAKELKQEYA-----VEVKGIVHK 75
Cdd:cd04322 12 RGSGKLSFADLQDESGKIQ-VYVNKDDLGEEEFEDFKKLLdlgdiIGVTGTPFK 64
|
|
| |
