|
Name |
Accession |
Description |
Interval |
E-value |
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
4-435 |
0e+00 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 675.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 4 PLKRTLTRELPQH-EGQTVKLQGFVHARRDLGGVQFLVLRDVTGVTQCVGS---------GLTLPLAESSVEVVGKVKAH 73
Cdd:PRK05159 1 MMKRHLTSELTPElDGEEVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKkkvdeelfeTIKKLKRESVVSVTGTVKAN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 74 PKAPGGFEVQVEDFRVISAATEATPVEIPKMEWNVnPETMLDYRVVTVRGLKERAALKVQAELVDAFRAHLRGEGFTEIS 153
Cdd:PRK05159 81 PKAPGGVEVIPEEIEVLNKAEEPLPLDISGKVLAE-LDTRLDNRFLDLRRPRVRAIFKIRSEVLRAFREFLYENGFTEIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 154 TPKIVSAGAEGGANLFPIDYFGHPAYLAQSPQLYKQIMVGV-FERVFEVAAVYRAEEHATSRHLNEYLSLDVEMGFIEDE 232
Cdd:PRK05159 160 TPKIVASGTEGGAELFPIDYFEKEAYLAQSPQLYKQMMVGAgFERVFEIGPVFRAEEHNTSRHLNEYTSIDVEMGFIDDH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 233 EDVMGLENRLLASIMERLRATSQAEFELLGATIPDVPAHIPRITLMDARQLVTEKYGHPVGGKDLDPEAERLLSQHFAET 312
Cdd:PRK05159 240 EDVMDLLENLLRYMYEDVAENCEKELELLGIELPVPETPIPRITYDEAIEILKSKGNEISWGDDLDTEGERLLGEYVKEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 313 EGSDFVFVTKYPRAARPFYAHPelNEDgsvNGEVTRGFDLLFRGIEITSGGQRIHDYGMLMDSIAAYKLKPESLEGYTEV 392
Cdd:PRK05159 320 YGSDFYFITDYPSEKRPFYTMP--DED---DPEISKSFDLLFRGLEITSGGQRIHRYDMLVESIKEKGLNPESFEFYLEA 394
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 81858899 393 FKYGMPPHGGFAIGAERLTAKLLGIANVRYARAFPRDRHRLTP 435
Cdd:PRK05159 395 FKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFPRDRHRLTP 437
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
6-435 |
1.20e-178 |
|
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: 505.36 E-value: 1.20e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 6 KRTLTREL-PQHEGQTVKLQGFVHARRDLGGVQFLVLRDVTGVTQCV-----------GSGLTLplaESSVEVVGKVKAH 73
Cdd:COG0017 1 KRTYIKDLlPEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGFIQVVvkkdklenfeeAKKLTT---ESSVEVTGTVVES 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 74 PKAPGGFEVQVEDFRVISAATEATPVEIpkmeWNVNPETMLDYRVVTVRGLKERAALKVQAELVDAFRAHLRGEGFTEIS 153
Cdd:COG0017 78 PRAPQGVELQAEEIEVLGEADEPYPLQP----KRHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVEVH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 154 TPKIVSAGAEGGANLFPIDYFGHPAYLAQSPQLYKQIMVGVFERVFEVAAVYRAEEHATSRHLNEYLSLDVEMGFIeDEE 233
Cdd:COG0017 154 TPIITASATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMALEKVYTFGPTFRAEKSNTRRHLAEFWMIEPEMAFA-DLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 234 DVMGLENRLLASIMERLRATSQAEFELLG---ATIPDVP-AHIPRITLMDARQLVtEKYGHPV-GGKDLDPEAERLLSQH 308
Cdd:COG0017 233 DVMDLAEEMLKYIIKYVLENCPEELEFLGrdvERLEKVPeSPFPRITYTEAIEIL-KKSGEKVeWGDDLGTEHERYLGEE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 309 FaeteGSDFVFVTKYPRAARPFYAHPelNEDgsvNGEVTRGFDLLFRGI-EITSGGQRIHDYGMLMDSIAAYKLKPESLE 387
Cdd:COG0017 312 F----FKKPVFVTDYPKEIKAFYMKP--NPD---DPKTVAAFDLLAPGIgEIIGGSQREHRYDVLVERIKEKGLDPEDYE 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 81858899 388 GYTEVFKYGMPPHGGFAIGAERLTAKLLGIANVRYARAFPRDRHRLTP 435
Cdd:COG0017 383 WYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
107-431 |
2.52e-129 |
|
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: 376.14 E-value: 2.52e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 107 NVNPETMLDYRVVTVRGLKERAALKVQAELVDAFRAHLRGEGFTEISTPKIVSAGAEGGANLFPIDYFGHPAYLAQSPQL 186
Cdd:cd00776 1 DANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 187 YKQIMVGVFERVFEVAAVYRAEEHATSRHLNEYLSLDVEMGFIEDEEDVMGLENRLLASIMERLRATSQAEFEL---LGA 263
Cdd:cd00776 81 YKEMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEDYNEVMDLIEELIKYIFKRVLERCAKELELvnqLNR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 264 TIPDVPAHIPRITLMDARQLVTEKYGH--PVGGKDLDPEAERLLSQHFaeteGSDFVFVTKYPRAARPFYAHPelNEDgs 341
Cdd:cd00776 161 ELLKPLEPFPRITYDEAIELLREKGVEeeVKWGEDLSTEHERLLGEIV----KGDPVFVTDYPKEIKPFYMKP--DDD-- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 342 vNGEVTRGFDLLFRGI-EITSGGQRIHDYGMLMDSIAAYKLKPESLEGYTEVFKYGMPPHGGFAIGAERLTAKLLGIANV 420
Cdd:cd00776 233 -NPETVESFDLLMPGVgEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNI 311
|
330
....*....|.
gi 81858899 421 RYARAFPRDRH 431
Cdd:cd00776 312 REAILFPRDPK 322
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
14-435 |
6.76e-121 |
|
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: 358.75 E-value: 6.76e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 14 PQHEGQTVKLQGFVHARRDLGGVQFLVLRDVTGVTQcvgsgLTLPL---------------AESSVEVVGKVKAHPKAPG 78
Cdd:TIGR00458 8 PEMDGQEVTFMGWVHEIRDLGGLIFVLLRDREGLIQ-----ITAPAkkvsknlfkwakklnLESVVAVRGIVKIKEKAPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 79 GFEVQVEDFRVISAATEATPVEiPKMEWNVNPETMLDYRVVTVRGLKERAALKVQAELVDAFRAHLRGEGFTEISTPKIV 158
Cdd:TIGR00458 83 GFEIIPTKIEVINEAKEPLPLD-PTEKVPAELDTRLDYRFLDLRRPTVQAIFRIRSGVLESVREFLAEEGFIEVHTPKLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 159 SAGAEGGANLFPIDYFGHPAYLAQSPQLYKQI-MVGVFERVFEVAAVYRAEEHATSRHLNEYLSLDVEMGFiEDEEDVMG 237
Cdd:TIGR00458 162 ASATEGGTELFPITYFEREAFLGQSPQLYKQQlMAAGFERVYEIGPIFRAEEHNTHRHLNEATSIDIEMAF-EDHHDVMD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 238 LENRLLASIMERLRATSQAEFELLGATIPDVPAHIPRITLMDARQLVTEKyGHPVG-GKDLDPEAERLLsqhfAETEGSD 316
Cdd:TIGR00458 241 ILEELVVRVFEDVPERCAHQLETLEFKLEKPEGKFVRLTYDEAIEMANAK-GVEIGwGEDLSTEAEKAL----GEEMDGL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 317 FvFVTKYPRAARPFYAHPElnEDgsvNGEVTRGFDLLFRGIEITSGGQRIHDYGMLMDSIAAYKLKPESLEGYTEVFKYG 396
Cdd:TIGR00458 316 Y-FITDWPTEIRPFYTMPD--ED---NPEISKSFDLMYRDLEISSGAQRIHLHDLLVERIKAKGLNPEGFKDYLEAFSYG 389
|
410 420 430
....*....|....*....|....*....|....*....
gi 81858899 397 MPPHGGFAIGAERLTAKLLGIANVRYARAFPRDRHRLTP 435
Cdd:TIGR00458 390 MPPHAGWGLGAERFVMFLLGLKNIREAVLFPRDRKRLTP 428
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
14-435 |
3.76e-98 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 303.55 E-value: 3.76e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 14 PQHEGQTVKLQGFVHARRDLGGVQFLVLRDVTGVTQCV--------GSGL-----TLPlAESSVEVVGKVKaHPKAP--- 77
Cdd:PLN02850 77 EELAGSEVLIRGRVHTIRGKGKSAFLVLRQSGFTVQCVvfvsevtvSKGMvkyakQLS-RESVVDVEGVVS-VPKKPvkg 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 78 --GGFEVQVEDFRVISAATEATPVEI-----PKMEWN-----------VNPETMLDYRVVTVRGLKERAALKVQAELVDA 139
Cdd:PLN02850 155 ttQQVEIQVRKIYCVSKALATLPFNVedaarSESEIEkalqtgeqlvrVGQDTRLNNRVLDLRTPANQAIFRIQSQVCNL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 140 FRAHLRGEGFTEISTPKIVSAGAEGGANLFPIDYFGHPAYLAQSPQLYKQIMV-GVFERVFEVAAVYRAEEHATSRHLNE 218
Cdd:PLN02850 235 FREFLLSKGFVEIHTPKLIAGASEGGSAVFRLDYKGQPACLAQSPQLHKQMAIcGDFRRVFEIGPVFRAEDSFTHRHLCE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 219 YLSLDVEMGFIEDEEDVMGLENRLLASIMERLRATSQAEFELLGATIP-DVPAHIP---RITLMDARQLVTEK--YGHPV 292
Cdd:PLN02850 315 FTGLDLEMEIKEHYSEVLDVVDELFVAIFDGLNERCKKELEAIREQYPfEPLKYLPktlRLTFAEGIQMLKEAgvEVDPL 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 293 GgkDLDPEAERLLSQHFAETEGSDFVFVTKYPRAARPFYAHPELNedgsvNGEVTRGFDLLFRGIEITSGGQRIHDYGML 372
Cdd:PLN02850 395 G--DLNTESERKLGQLVKEKYGTDFYILHRYPLAVRPFYTMPCPD-----DPKYSNSFDVFIRGEEIISGAQRVHDPELL 467
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81858899 373 MDSIAAYKLKPESLEGYTEVFKYGMPPHGGFAIGAERLTAKLLGIANVRYARAFPRDRHRLTP 435
Cdd:PLN02850 468 EKRAEECGIDVKTISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPRDPQRLAP 530
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
109-430 |
1.45e-95 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 289.85 E-value: 1.45e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 109 NPETMLDYRVVTVRGLKERAALKVQAELVDAFRAHLRGEGFTEISTPKIVSAGAEGGANLFPI------DYFghpaYLAQ 182
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVpsralgKFY----ALPQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 183 SPQLYKQI-MVGVFERVFEVAAVYRAEEHATSRHLnEYLSLDVEMGFIeDEEDVMGLENRLLASIMERLRATSQaefELL 261
Cdd:pfam00152 77 SPQLYKQLlMVAGFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFV-DYEDVMDLTEELIKEIFKEVEGIAK---ELE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 262 GATIPDVPAHIPRITLMDARQLVTEKYGHPvGGKDLDPEAERLLSQHFAETEGSDFVFVTKYPRAARPFYAHPELNEDGs 341
Cdd:pfam00152 152 GGTLLDLKKPFPRITYAEAIEKLNGKDVEE-LGYGSDKPDLRFLLELVIDKNKFNPLWVTDFPAEHHPFTMPKDEDDPA- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 342 vngeVTRGFDLLFRGIEITSGGQRIHDYGMLMDSIAAYKLKP----ESLEGYTEVFKYGMPPHGGFAIGAERLTAKLLGI 417
Cdd:pfam00152 230 ----LAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDPeeaeEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGL 305
|
330
....*....|...
gi 81858899 418 ANVRYARAFPRDR 430
Cdd:pfam00152 306 ESIREVIAFPKTR 318
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
6-435 |
5.48e-82 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 259.27 E-value: 5.48e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 6 KRTLTREL--PQHEGQTVKLQGFVHARRDLGGVQFLVLRDVTGVTQCVG------------SGLTLplaESSVEVVGKVK 71
Cdd:PRK03932 2 MRVSIKDIlkGKYVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVvkdngeeyfeeiKKLTT---GSSVIVTGTVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 72 AHPKAPGGFEVQVEDFRVISAATEATPveIPKMEWNVnpETMLDYRVVTVRGLKERAALKVQAELVDAFRAHLRGEGFTE 151
Cdd:PRK03932 79 ESPRAGQGYELQATKIEVIGEDPEDYP--IQKKRHSI--EFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 152 ISTPKIVSAGAEGGANLFPI---------DYFGHPAYLAQSPQLYKQIMVGVFERVFEVAAVYRAEEHATSRHLNEYLSL 222
Cdd:PRK03932 155 VDTPIITASDCEGAGELFRVttldldfskDFFGKEAYLTVSGQLYAEAYAMALGKVYTFGPTFRAENSNTRRHLAEFWMI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 223 DVEMGFIeDEEDVMGLENRLLASIMERLRATSQAEFELLGATIPD---------VPAHIPRITLMDARQLVTE---KYGH 290
Cdd:PRK03932 235 EPEMAFA-DLEDNMDLAEEMLKYVVKYVLENCPDDLEFLNRRVDKgdierlenfIESPFPRITYTEAIEILQKsgkKFEF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 291 PVG-GKDLDPEAERLLS-QHFAETegsdfVFVTKYPRAARPFYAHPelNEDGsvngEVTRGFDLLFRGI-EITSGGQRIH 367
Cdd:PRK03932 314 PVEwGDDLGSEHERYLAeEHFKKP-----VFVTNYPKDIKAFYMRL--NPDG----KTVAAMDLLAPGIgEIIGGSQREE 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81858899 368 DYGMLMDSIAAYKLKPESLEGYTEVFKYGMPPHGGFAIGAERLTAKLLGIANVRYARAFPRDRHRLTP 435
Cdd:PRK03932 383 RLDVLEARIKELGLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
14-435 |
7.50e-69 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 227.95 E-value: 7.50e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 14 PQHEGQTVKLQGFVHARRDLGGVQFLVLRDVTGVTQCVGSGL------------TLPlAESSVEVVGKV--KAHP---KA 76
Cdd:PTZ00401 74 PELVDKTVLIRARVSTTRKKGKMAFMVLRDGSDSVQAMAAVEgdvpkemidfigQIP-TESIVDVEATVckVEQPitsTS 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 77 PGGFEVQVEDFRVISAATEATPVEIPKME-------WNVNPETMLDYRVVTVRGLKERAALKVQAELVDAFRAHLRGEGF 149
Cdd:PTZ00401 153 HSDIELKVKKIHTVTESLRTLPFTLEDASrkesdegAKVNFDTRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLIDSDF 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 150 TEISTPKIVSAGAEGGANLFPIDYFGHPAYLAQSPQLYKQIMV-GVFERVFEVAAVYRAEEHATSRHLNEYLSLDVEMGF 228
Cdd:PTZ00401 233 CEIHSPKIINAPSEGGANVFKLEYFNRFAYLAQSPQLYKQMVLqGDVPRVFEVGPVFRSENSNTHRHLTEFVGLDVEMRI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 229 IEDEEDVMGLENRLLASIMERLrATSQAEFELLGATIPDVP--------------------------AHIPRITLMDARQ 282
Cdd:PTZ00401 313 NEHYYEVLDLAESLFNYIFERL-ATHTKELKAVCQQYPFEPlvwkltpermkelgvgvisegveptdKYQARVHNMDSRM 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 283 L-------------VTEKYGHPVggKDLDPEAERLLSQHFAETEGSDFVFVTKYPRAARPFYAHPELNEDgsvngEVTRG 349
Cdd:PTZ00401 392 LrinymhciellntVLEEKMAPT--DDINTTNEKLLGKLVKERYGTDFFISDRFPSSARPFYTMECKDDE-----RFTNS 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 350 FDLLFRGIEITSGGQRIHDYGMLMDSIAAYKLKPESLEGYTEVFKYGMPPHGGFAIGAERLTAKLLGIANVRYARAFPRD 429
Cdd:PTZ00401 465 YDMFIRGEEISSGAQRIHDPDLLLARAKMLNVDLTPIKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFPRD 544
|
....*.
gi 81858899 430 RHRLTP 435
Cdd:PTZ00401 545 PQRTTP 550
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
130-430 |
2.03e-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: 184.60 E-value: 2.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 130 LKVQAELVDAFRAHLRGEGFTEISTPKIVSAGAEGGANLFPIDYF--GHPAYLAQSPQLYKQI-MVGVFERVFEVAAVYR 206
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNalGLDYYLRISPQLFKKRlMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 207 AEeHATSRHLNEYLSLDVEMGFIeDEEDVMGLENRLLASIMERLRATSQAEfelLGATIPDVPAHIPRITLMDArqlvTE 286
Cdd:cd00669 81 NE-DLRARHQPEFTMMDLEMAFA-DYEDVIELTERLVRHLAREVLGVTAVT---YGFELEDFGLPFPRLTYREA----LE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 287 KYGHPVggkdldpeaerllsqhfaetegsdfvFVTKYPRAARPFYAHPElnedgSVNGEVTRGFDLLFRGIEITSGGQRI 366
Cdd:cd00669 152 RYGQPL--------------------------FLTDYPAEMHSPLASPH-----DVNPEIADAFDLFINGVEVGNGSSRL 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81858899 367 HDYGMLMDSIAAYKLKPE----SLEGYTEVFKYGMPPHGGFAIGAERLTAKLLGIANVRYARAFPRDR 430
Cdd:cd00669 201 HDPDIQAEVFQEQGINKEagmeYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKMR 268
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
127-428 |
1.43e-53 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 181.76 E-value: 1.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 127 RAALKVQAELVDAFRAHLRGEGFTEISTP---KIVSAGAEGGANL----FPIDYFGHPAYLAQSPQLYKQIMVGVFERVF 199
Cdd:PRK06462 27 RKVLKVQSSILRYTREFLDGRGFVEVLPPiisPSTDPLMGLGSDLpvkqISIDFYGVEYYLADSMILHKQLALRMLGKIF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 200 EVAAVYRAE--EHATSRHLNEYLSLDVEMGFiEDEEDVMGLENRLLASIMERLRATSQAEFELLGATIPDVPAHIPRITL 277
Cdd:PRK06462 107 YLSPNFRLEpvDKDTGRHLYEFTQLDIEIEG-ADLDEVMDLIEDLIKYLVKELLEEHEDELEFFGRDLPHLKRPFKRITH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 278 MDARQLVTEKYGHPVGGKDLDPEAERLLSQHFAETegsdfVFVTKYPRAARPFYAHPELNEDGsvngeVTRGFDLLF-RG 356
Cdd:PRK06462 186 KEAVEILNEEGCRGIDLEELGSEGEKSLSEHFEEP-----FWIIDIPKGSREFYDREDPERPG-----VLRNYDLLLpEG 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81858899 357 I-EITSGGQRIHDYGMLMDSIAAYKLKPESLEGYTEVFKYGMPPHGGFAIGAERLTAKLLGIANVRYARAFPR 428
Cdd:PRK06462 256 YgEAVSGGEREYEYEEIVERIREHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQPFPR 328
|
|
| aspS_bact |
TIGR00459 |
aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be ... |
16-431 |
1.19e-43 |
|
aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be discriminating (6.1.1.12) or nondiscriminating (6.1.1.23). 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_bact, represents aspartyl-tRNA synthetases from the Bacteria and from mitochondria. In some species, this enzyme aminoacylates tRNA for both Asp and Asn; Asp-tRNA(asn) is subsequently transamidated to Asn-tRNA(asn). This model generates very low scores for the archaeal type of aspS and for asnS; scores between the trusted and noise cutoffs represent fragmentary sequences. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 211576 [Multi-domain] Cd Length: 583 Bit Score: 161.06 E-value: 1.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 16 HEGQTVKLQGFVHARRDLGGVQFLVLRDVTGVTQ--CVGSGLTLPLA-----ESSVEVVGKVKAHPK-------APGGFE 81
Cdd:TIGR00459 13 HLGQTVTLAGWVNRRRDLGGLIFIDLRDRSGIVQvvCDPDADALKLAkglrnEDVVQVKGKVSARPEgninrnlDTGEIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 82 VQVEDFRVISAAtEATPVEIPKMewNVNPETMLDYRVVTVRGLKERAALKVQAELVDAFRAHLRGEGFTEISTPKIVSAG 161
Cdd:TIGR00459 93 ILAESITLLNKS-KTPPLIIEKT--DAEEEVRLKYRYLDLRRPEMQQRLKLRHKVTKAVRNFLDQQGFLEIETPMLTKST 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 162 AEGGAN-LFPIDYFGHPAY-LAQSPQLYKQI-MVGVFERVFEVAAVYRAEEHATSRHlNEYLSLDVEMGFIeDEEDVMGL 238
Cdd:TIGR00459 170 PEGARDyLVPSRVHKGEFYaLPQSPQLFKQLlMVSGVDRYYQIARCFRDEDLRADRQ-PEFTQIDMEMSFM-TQEDVMEL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 239 ENRLLASI---------------------MER-------LRA-------------TSQAEFELL--------GATIPDVP 269
Cdd:TIGR00459 248 IEKLVSHVflevkgidlkkpfpvmtyaeaMERygsdkpdLRFplelidvtdlfkdSEFKVFSNLindggrvkAIRVPGGW 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 270 AHIPRITLMDARQLVTEkYG---------------HPVGgKDLDPEAERLLSQHFAETEGS------------------- 315
Cdd:TIGR00459 328 AELSRKSIKELRKFAKE-YGakglaylkvnedginSPIK-KFLDEKKGKILLERTDAQNGDillfgagskkivldalgal 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 316 ----------------DFVFVTKYP-----------RAARPFYA-HPELNEDGSVNGE--VTRGFDLLFRGIEITSGGQR 365
Cdd:TIGR00459 406 rlklgkdlglvdpdlfSFLWVVDFPmfekdkegrlcAAHHPFTMpKDEDLENLEAAPEeaLAEAYDLVLNGVELGGGSIR 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 366 IHDYGMLMDSIAAYKLKPESLE---GYT-EVFKYGMPPHGGFAIGAERLTAKLLGIANVRYARAFPRDRH 431
Cdd:TIGR00459 486 IHDPEVQKKVFEILGIDPEEARekfGFLlEAFKYGTPPHAGFALGLDRLMMLLTGTDNIRDVIAFPKTTA 555
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
5-427 |
3.93e-38 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 145.60 E-value: 3.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 5 LKRT-----LTRElpqHEGQTVKLQGFVHARRDLGGVQFLVLRDVTGVTQCV--GSGLTLPLA-----ESSVEVVGKVKA 72
Cdd:PRK00476 2 MMRThycgeLRES---HVGQTVTLCGWVHRRRDHGGLIFIDLRDREGIVQVVfdPDAEAFEVAeslrsEYVIQVTGTVRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 73 HPK-------APGGFEVQVEDFRVISAAtEATPVEIpKMEWNVNPETMLDYRVVTVRGLKERAALKVQAELVDAFRAHLR 145
Cdd:PRK00476 79 RPEgtvnpnlPTGEIEVLASELEVLNKS-KTLPFPI-DDEEDVSEELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 146 GEGFTEISTPKIVSAGAEgGANlfpiDY----------FghpaY-LAQSPQLYKQI-MVGVFERVFEVAAVYRAEEhatS 213
Cdd:PRK00476 157 DNGFLEIETPILTKSTPE-GAR----DYlvpsrvhpgkF----YaLPQSPQLFKQLlMVAGFDRYYQIARCFRDED---L 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 214 R--HLNEYLSLDVEMGFIeDEEDVMGLENRLLASIMErlratsqaefELLGAtipDVPAHIPRITLMDA----------- 280
Cdd:PRK00476 225 RadRQPEFTQIDIEMSFV-TQEDVMALMEGLIRHVFK----------EVLGV---DLPTPFPRMTYAEAmrrygsdkpdl 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 281 R-----QLVTE---------------------------------------------KYGHP------VGGKDL------- 297
Cdd:PRK00476 291 RfglelVDVTDlfkdsgfkvfagaandggrvkairvpggaaqlsrkqideltefakIYGAKglayikVNEDGLkgpiakf 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 298 --DPEAERLLSQHFAEtEGsDFVF--------VTKYPRAAR-----------------------PFYahpELNEDG---- 340
Cdd:PRK00476 371 lsEEELAALLERTGAK-DG-DLIFfgadkakvVNDALGALRlklgkelglidedkfaflwvvdfPMF---EYDEEEgrwv 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 341 -------SVNGE-------------VTRGFDLLFRGIEITSGGQRIHDYGM--LMDSIAayKLKPESLE---GY-TEVFK 394
Cdd:PRK00476 446 aahhpftMPKDEdldelettdpgkaRAYAYDLVLNGYELGGGSIRIHRPEIqeKVFEIL--GISEEEAEekfGFlLDALK 523
|
570 580 590
....*....|....*....|....*....|...
gi 81858899 395 YGMPPHGGFAIGAERLTAKLLGIANVRYARAFP 427
Cdd:PRK00476 524 YGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
5-289 |
6.28e-35 |
|
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439943 [Multi-domain] Cd Length: 589 Bit Score: 136.67 E-value: 6.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 5 LKRTLT----RElpQHEGQTVKLQGFVHARRDLGGVQFLVLRDVTGVTQCV----GSGLTLPLA-----ESSVEVVGKVK 71
Cdd:COG0173 1 MYRTHYcgelRE--SDVGQEVTLSGWVHRRRDHGGLIFIDLRDRYGITQVVfdpdDSAEAFEKAeklrsEYVIAVTGKVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 72 AHPK-------APGGFEVQVEDFRVISAAtEATPVEIPKMEwNVNPETMLDYRVVTVRGLKERAALKVQAELVDAFRAHL 144
Cdd:COG0173 79 ARPEgtvnpklPTGEIEVLASELEILNKA-KTPPFQIDDDT-DVSEELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 145 RGEGFTEISTPkIVSAGAEGGANlfpiDY----------FghpaY-LAQSPQLYKQI-MVGVFERVFEVAAVYRAEEHAT 212
Cdd:COG0173 157 DENGFLEIETP-ILTKSTPEGAR----DYlvpsrvhpgkF----YaLPQSPQLFKQLlMVSGFDRYFQIARCFRDEDLRA 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81858899 213 SRHLnEYLSLDVEMGFIeDEEDVMGLENRLLASIMErlratsqaefELLGAtipDVPAHIPRITLMDArqlvTEKYG 289
Cdd:COG0173 228 DRQP-EFTQLDIEMSFV-DQEDVFELMEGLIRHLFK----------EVLGV---ELPTPFPRMTYAEA----MERYG 285
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
130-427 |
6.20e-33 |
|
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: 125.38 E-value: 6.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 130 LKVQAELVDAFRAHLRGEGFTEISTPkIVSAGAEGGANLFPIDYFGHP--AY-LAQSPQLYKQI-MVGVFERVFEVAAVY 205
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETP-ILTKSTPEGARDFLVPSRLHPgkFYaLPQSPQLFKQLlMVSGFDRYFQIARCF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 206 RAEEHATSRHlNEYLSLDVEMGFIeDEEDVMGLENRLLASIMERLRatsqaefellgatIPDVPAHIPRITLMDArqlvT 285
Cdd:cd00777 80 RDEDLRADRQ-PEFTQIDIEMSFV-DQEDIMSLIEGLLKYVFKEVL-------------GVELTTPFPRMTYAEA----M 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 286 EKYGH--------PVggKDLDPEAERLLSQHfaetegsdfvfvtkypraaRPFYA-HPELNEDGSVNGEVTRG--FDLLF 354
Cdd:cd00777 141 ERYGFkflwivdfPL--FEWDEEEGRLVSAH-------------------HPFTApKEEDLDLLEKDPEDARAqaYDLVL 199
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81858899 355 RGIEITSGGQRIHDYGMLMDSIAAYKLKPESLE----GYTEVFKYGMPPHGGFAIGAERLTAKLLGIANVRYARAFP 427
Cdd:cd00777 200 NGVELGGGSIRIHDPDIQEKVFEILGLSEEEAEekfgFLLEAFKYGAPPHGGIALGLDRLVMLLTGSESIRDVIAFP 276
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
18-428 |
7.48e-28 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 116.43 E-value: 7.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 18 GQTVKLQGFVHARRDLGGVQFLVLRDVTGVTQCVGSGLTLPLAESS---------VEVVGKVKAHP-KAP------GGFE 81
Cdd:PLN02903 72 GSRVTLCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDEFPEAHRTanrlrneyvVAVEGTVRSRPqESPnkkmktGSVE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 82 VQVEDFRVISAATEATPVEIPKMEWN---VNPETMLDYRVVTVRGLKERAALKVQAELVDAFRAHLRG-EGFTEISTPkI 157
Cdd:PLN02903 152 VVAESVDILNVVTKSLPFLVTTADEQkdsIKEEVRLRYRVLDLRRPQMNANLRLRHRVVKLIRRYLEDvHGFVEIETP-I 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 158 VSAGAEGGANLFPIDYFGHPA---YLAQSPQLYKQ-IMVGVFERVFEVAAVYRAEEHATSRHlNEYLSLDVEMGFIeDEE 233
Cdd:PLN02903 231 LSRSTPEGARDYLVPSRVQPGtfyALPQSPQLFKQmLMVSGFDRYYQIARCFRDEDLRADRQ-PEFTQLDMELAFT-PLE 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 234 DVMGLENRLLASIMErlratsqaefELLGATIPDvPahIPRITLMDArqlvTEKYGH----------------------- 290
Cdd:PLN02903 309 DMLKLNEDLIRQVFK----------EIKGVQLPN-P--FPRLTYAEA----MSKYGSdkpdlryglelvdvsdvfaessf 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 291 ------------------PVGGK-------------------------------------------DLDPE-AERLLS-- 306
Cdd:PLN02903 372 kvfagalesggvvkaicvPDGKKisnntalkkgdiyneaiksgakglaflkvlddgelegikalveSLSPEqAEQLLAac 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 307 --------------------------QHFAETEG------SDFVFVTKYPR------------AARPFYA-HPELNEDgs 341
Cdd:PLN02903 452 gagpgdlilfaagptssvnktldrlrQFIAKTLDlidpsrHSILWVTDFPMfewnedeqrleaLHHPFTApNPEDMGD-- 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 342 VNGEVTRGFDLLFRGIEITSGGQRIHDYGMLMDSIAAYKLKPESLE---GY-TEVFKYGMPPHGGFAIGAERLTAKLLGI 417
Cdd:PLN02903 530 LSSARALAYDMVYNGVEIGGGSLRIYRRDVQQKVLEAIGLSPEEAEskfGYlLEALDMGAPPHGGIAYGLDRLVMLLAGA 609
|
570
....*....|.
gi 81858899 418 ANVRYARAFPR 428
Cdd:PLN02903 610 KSIRDVIAFPK 620
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
18-428 |
2.81e-27 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 114.30 E-value: 2.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 18 GQTVKLQGFVHARRDLGGVQFLVLRDVTGVT--QCV-----------GSGLTLPLAesSVEVVGKVKAHPKAPGGFEVQV 84
Cdd:PLN02603 107 GKTLNVMGWVRTLRAQSSVTFIEVNDGSCLSnmQCVmtpdaegydqvESGLITTGA--SVLVQGTVVSSQGGKQKVELKV 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 85 EDFRVISAATEATPVEIPKmewnVNPETMLdyrvvTVRGLKER-----AALKVQAELVDAFRAHLRGEGFTEISTPKIVS 159
Cdd:PLN02603 185 SKIVVVGKSDPSYPIQKKR----VSREFLR-----TKAHLRPRtntfgAVARVRNALAYATHKFFQENGFVWVSSPIITA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 160 AGAEGGANLFPI------------------------------DYFGHPAYLAQSPQLYKQIMVGVFERVFEVAAVYRAEE 209
Cdd:PLN02603 256 SDCEGAGEQFCVttlipnsaenggslvddipktkdglidwsqDFFGKPAFLTVSGQLNGETYATALSDVYTFGPTFRAEN 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 210 HATSRHLNEYLSLDVEMGFiEDEEDVMGLENRLLASIMERLRATSQAEFELLGATIPD---------VPAHIPRITLMDA 280
Cdd:PLN02603 336 SNTSRHLAEFWMIEPELAF-ADLNDDMACATAYLQYVVKYILENCKEDMEFFNTWIEKgiidrlsdvVEKNFVQLSYTDA 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 281 RQLV---TEKYGHPVG-GKDLDPEAERLLSQhfaETEGSDFVFVTKYPRAARPFYAHPelNEDGsvngEVTRGFDLLF-R 355
Cdd:PLN02603 415 IELLlkaKKKFEFPVKwGLDLQSEHERYITE---EAFGGRPVIIRDYPKEIKAFYMRE--NDDG----KTVAAMDMLVpR 485
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81858899 356 GIEITSGGQRIHDYGMLMDSIAAYKLKPESLEGYTEVFKYGMPPHGGFAIGAERLTAKLLGIANVRYARAFPR 428
Cdd:PLN02603 486 VGELIGGSQREERLEYLEARLDELKLNKESYWWYLDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFPR 558
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
14-435 |
2.51e-25 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 108.92 E-value: 2.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 14 PQHEGQTVKLQGFVHARRDLGGVQFLVLRDVTGVTQCVGSGLTLPL----------AESSVEVVGKVKAHPKA------- 76
Cdd:PRK12820 14 LDDTGREVCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFSPEAAPAdvyelaaslrAEFCVALQGEVQKRLEEtenphie 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 77 PGGFEVQVEDFRVISaATEATPVEIPKMEW----------NVNPETMLDYRVVTVRGLKERAALKVQAELVDAFRAHLRG 146
Cdd:PRK12820 94 TGDIEVFVRELSILA-ASEALPFAISDKAMtagagsagadAVNEDLRLQYRYLDIRRPAMQDHLAKRHRIIKCARDFLDS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 147 EGFTEISTPKIVSAGAEGG------ANLFPIDYFGHPaylaQSPQLYKQ-IMVGVFERVFEVAAVYRAEEHATSRHlNEY 219
Cdd:PRK12820 173 RGFLEIETPILTKSTPEGArdylvpSRIHPKEFYALP----QSPQLFKQlLMIAGFERYFQLARCFRDEDLRPNRQ-PEF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 220 LSLDVEMGFIeDEEDVMGLENRLLASIMER---------LRATSQAEFELLGATIPDVPAHIPRITLMDA---------R 281
Cdd:PRK12820 248 TQLDIEASFI-DEEFIFELIEELTARMFAIggialprpfPRMPYAEAMDTTGSDRPDLRFDLKFADATDIfentrygifK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 282 QLVteKYGHPVGGKDLDPEAERL-----------------------------------LSQHFAETEGSDF--------- 317
Cdd:PRK12820 327 QIL--QRGGRIKGINIKGQSEKLsknvlqneyakeiapsfgakgmtwmraeaggldsnIVQFFSADEKEALkrrfhaedg 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 318 ---------------------------------------VFVTKYP-----------RAARPFYAHPELNED-GSVNGEV 346
Cdd:PRK12820 405 dviimiadascaivlsalgqlrlhladrlglipegvfhpLWITDFPlfeatddggvtSSHHPFTAPDREDFDpGDIEELL 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 347 ---TRGFDLLFRGIEITSGGQRIHDYGMLMDSIAAYKLKPESLEG----YTEVFKYGMPPHGGFAIGAERLTAKLLGIAN 419
Cdd:PRK12820 485 dlrSRAYDLVVNGEELGGGSIRINDKDIQLRIFAALGLSEEDIEDkfgfFLRAFDFAAPPHGGIALGLDRVVSMILQTPS 564
|
570
....*....|....*.
gi 81858899 420 VRYARAFPRDRHRLTP 435
Cdd:PRK12820 565 IREVIAFPKNRSAACP 580
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
115-428 |
4.27e-21 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 95.86 E-value: 4.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 115 DYRVVTvrglKERAALKVQAELVDAFRAHLRGEGFTEISTPKIVSAGAEGGANL--FPIDYFGHPAYLAQSPQLYKQIMV 192
Cdd:PTZ00425 265 DYRAIP----RVNKKNKKGEKREDILNTCNANNNNGNSSSSNAVSSPAYPDQYLidYKKDFFSKQAFLTVSGQLSLENLC 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 193 GVFERVFEVAAVYRAEEHATSRHLNEYLSLDVEMGFIE----------------------DEEDVMGLENRLLASIMERL 250
Cdd:PTZ00425 341 SSMGDVYTFGPTFRAENSHTSRHLAEFWMIEPEIAFADlydnmelaesyikycigyvlnnNFDDIYYFEENVETGLISRL 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 251 RATSQAEFellgatipdvpAHIPRITLMDARQLVTEKYGHPVG-GKDLDPEAERLLSQHFAETEgsdfVFVTKYPRAARP 329
Cdd:PTZ00425 421 KNILDEDF-----------AKITYTNVIDLLQPYSDSFEVPVKwGMDLQSEHERFVAEQIFKKP----VIVYNYPKDLKA 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 330 FYAhpELNEDGsvngEVTRGFDLLFRGI-EITSGGQRIHDYGMLMDSIAAYKLKPESLEGYTEVFKYGMPPHGGFAIGAE 408
Cdd:PTZ00425 486 FYM--KLNEDQ----KTVAAMDVLVPKIgEVIGGSQREDNLERLDKMIKEKKLNMESYWWYRQLRKFGSHPHAGFGLGFE 559
|
330 340
....*....|....*....|
gi 81858899 409 RLTAKLLGIANVRYARAFPR 428
Cdd:PTZ00425 560 RLIMLVTGVDNIKDTIPFPR 579
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
172-428 |
3.27e-20 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 93.13 E-value: 3.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 172 DYFGHPAYLAQSPQLYKQIMVGVFERVFEVAAVYRAEEHATSRHLNEYLSLDVEMGFIEDEEDV---------------- 235
Cdd:PLN02221 303 DFFGRQAFLTVSGQLQVETYACALSSVYTFGPTFRAENSHTSRHLAEFWMVEPEIAFADLEDDMncaeayvkymckwlld 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 236 -----MGLENRLLAS-IMERLRATSQAEFEllgatipdvpahipRITLMDARQLVTEKYGhpvGGKDLDPEAE---RLLS 306
Cdd:PLN02221 383 kcfddMELMAKNFDSgCIDRLRMVASTPFG--------------RITYTEAIELLEEAVA---KGKEFDNNVEwgiDLAS 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 307 QH---FAETEGSDFVFVTKYPRAARPFYAhpELNEDGsvngEVTRGFDLLFRGI-EITSGGQRIHDYGMLMDSIAAYKLK 382
Cdd:PLN02221 446 EHeryLTEVLFQKPLIVYNYPKGIKAFYM--RLNDDE----KTVAAMDVLVPKVgELIGGSQREERYDVIKQRIEEMGLP 519
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 81858899 383 PESLEGYTEVFKYGMPPHGGFAIGAERLTAKLLGIANVRYARAFPR 428
Cdd:PLN02221 520 IEPYEWYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPR 565
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
20-91 |
1.02e-19 |
|
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. Class 2b aaRSs include the homodimeric aspartyl-, asparaginyl-, and lysyl-tRNA synthetases (AspRS, AsnRS, and LysRS). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Included in this group are archeal and archeal-like AspRSs which are non-discriminating and can charge both tRNAAsp and tRNAAsn. E. coli cells have two isoforms of LysRSs (LysS and LysU) encoded by two distinct genes, which are differentially regulated. The cytoplasmic and the mitochondrial isoforms of human LysRS are encoded by a single gene. Yeast cytoplasmic and mitochondrial LysRSs participate in mitochondrial import of cytoplasmic tRNAlysCUU. In addition to their housekeeping role, human LysRS may function as a signaling molecule that activates immune cells. Tomato LysRS may participate in a process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging. AsnRS is immunodominant antigen of the filarial nematode Brugia malayai and is of interest as a target for anti-parasitic drug design. Human AsnRS has been shown to be a pro-inflammatory chemokine which interacts with CCR3 chemokine receptors on T cells, immature dendritic cells and macrophages.
Pssm-ID: 239766 [Multi-domain] Cd Length: 85 Bit Score: 83.00 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 20 TVKLQGFVHARRDLGGVQFLVLRDVTGVTQCVGSGLTLPLA---------ESSVEVVGKVKAHPK---APGGFEVQVEDF 87
Cdd:cd04100 1 EVTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEELGEFfeeaeklrtESVVGVTGTVVKRPEgnlATGEIELQAEEL 80
|
....
gi 81858899 88 RVIS 91
Cdd:cd04100 81 EVLS 84
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
16-117 |
2.33e-19 |
|
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: 83.72 E-value: 2.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 16 HEGQTVKLQGFVHARRDLGGVQFLVLRDVTGVTQCV---GSGLTLPLA-----ESSVEVVGKVKAHPK-------APGGF 80
Cdd:cd04317 12 HVGQEVTLCGWVQRRRDHGGLIFIDLRDRYGIVQVVfdpEEAPEFELAeklrnESVIQVTGKVRARPEgtvnpklPTGEI 91
|
90 100 110
....*....|....*....|....*....|....*..
gi 81858899 81 EVQVEDFRVISAAtEATPVEIPKmEWNVNPETMLDYR 117
Cdd:cd04317 92 EVVASELEVLNKA-KTLPFEIDD-DVNVSEELRLKYR 126
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
169-430 |
6.63e-19 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 89.16 E-value: 6.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 169 FPIDYFGHPAYLAQSPQLYKQIMVGVFERVFEVAAVYRAEEHATSRHLNEYLSLDVEMGFIEDE---------------- 232
Cdd:PLN02532 363 FSKDFFSRPTYLTVSGRLHLESYACALGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAFSELEdamncaedyfkflckw 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 233 ------EDVMGLENRLLASIMERLRATSQAEFEllgatipdvpahipRITLMDA----RQLVTEKY-GHPVGGKDLDPEA 301
Cdd:PLN02532 443 vlencsEDMKFVSKRIDKTISTRLEAIISSSLQ--------------RISYTEAvdllKQATDKKFeTKPEWGIALTTEH 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 302 ERLLSQHFAETEgsdfVFVTKYPRAARPFYAhpELNEDgsvnGEVTRGFDLLF--RGIEITsGGQRIHDYGMLMDSIAAY 379
Cdd:PLN02532 509 LSYLADEIYKKP----VIIYNYPKELKPFYV--RLNDD----GKTVAAFDLVVpkVGTVIT-GSQNEERMDILNARIEEL 577
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 81858899 380 KLKPESLEGYTEVFKYGMPPHGGFAIGAERLTAKLLGIANVRYARAFPRDR 430
Cdd:PLN02532 578 GLPREQYEWYLDLRRHGTVKHSGFSLGFELMVLFATGLPDVRDAIPFPRSW 628
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
14-101 |
2.71e-18 |
|
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: 80.05 E-value: 2.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 14 PQHEGQTVKLQGFVHARRDLGGVQFLVLRDVTGVTQCV-------------GSGLTlplAESSVEVVGKVKAHPKAPGGF 80
Cdd:cd04316 8 PELDGEEVTVAGWVHEIRDLGGIKFVILRDREGIVQVTapkkkvdkelfktVRKLS---RESVISVTGTVKAEPKAPNGV 84
|
90 100
....*....|....*....|.
gi 81858899 81 EVQVEDFRVISAATEATPVEI 101
Cdd:cd04316 85 EIIPEEIEVLSEAKTPLPLDP 105
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
20-91 |
1.55e-17 |
|
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and Saccharomyces cerevisiae cytoplasmic asparaginyl-tRNA synthetase (AsnRS), in Brugia malayai AsnRs and, in various putative bacterial AsnRSs. This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. AsnRS is immunodominant antigen of the filarial nematode B. malayai and of interest as a target for anti-parasitic drug design. Human AsnRS has been shown to be a pro-inflammatory chemokine which interacts with CCR3 chemokine receptors on T cells, immature dendritic cells and macrophages.
Pssm-ID: 239818 [Multi-domain] Cd Length: 84 Bit Score: 76.89 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 20 TVKLQGFVHARRDLGGVQFLVLRDVTGVTQCVGSG---------LTLPLaESSVEVVGKVKAHPK---APGGFEVQVEDF 87
Cdd:cd04323 1 RVKVFGWVHRLRSQKKLMFLVLRDGTGFLQCVLSKklvtefydaKSLTQ-ESSVEVTGEVKEDPRakqAPGGYELQVDYL 79
|
....
gi 81858899 88 RVIS 91
Cdd:cd04323 80 EIIG 83
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
127-427 |
6.00e-17 |
|
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: 81.48 E-value: 6.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 127 RAALKVQAELVDAFRAHLRGEGFTEISTPkIVSAGAeGGANLFP-IDY---FGHPAYLAQSPQLY-KQIMVGVFERVFEV 201
Cdd:cd00775 5 RQTFIVRSKIISYIRKFLDDRGFLEVETP-MLQPIA-GGAAARPfITHhnaLDMDLYLRIAPELYlKRLIVGGFERVYEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 202 AAVYRaEEHATSRHLNEYLSLDVEMGFIeDEEDVMGLENRLLASIMERLRATSQAEFellGATIPDVPAHIPRITLMDAr 281
Cdd:cd00775 83 GRNFR-NEGIDLTHNPEFTMIEFYEAYA-DYNDMMDLTEDLFSGLVKKINGKTKIEY---GGKELDFTPPFKRVTMVDA- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 282 qlVTEKYGHPVGGKDL--DPEAERLLSQHFAETEG-------------SDFV--------FVTKYPRAARPFY-AHPEln 337
Cdd:cd00775 157 --LKEKTGIDFPELDLeqPEELAKLLAKLIKEKIEkprtlgklldklfEEFVeptliqptFIIDHPVEISPLAkRHRS-- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 338 edgsvNGEVTRGFDLLFRGIEITSG----------------GQRIHDYG----MLMDsiaayklkpeslEGYTEVFKYGM 397
Cdd:cd00775 233 -----NPGLTERFELFICGKEIANAytelndpfdqrerfeeQAKQKEAGddeaMMMD------------EDFVTALEYGM 295
|
330 340 350
....*....|....*....|....*....|
gi 81858899 398 PPHGGFAIGAERLTAKLLGIANVRYARAFP 427
Cdd:cd00775 296 PPTGGLGIGIDRLVMLLTDSNSIRDVILFP 325
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
21-430 |
6.33e-17 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 82.80 E-value: 6.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 21 VKLQGFVHARRDLGGVQFLVLRDVTGVTQCVGSGLTLPLAESSVE---------VVGKVKAHPKAPGGFEVQVEDFRVIS 91
Cdd:PRK12445 68 VSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEGVYNDQfkkwdlgdiIGARGTLFKTQTGELSIHCTELRLLT 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 92 AATEATPVEIPKMEwnvNPETMLDYRVVT-VRGLKERAALKVQAELVDAFRAHLRGEGFTEISTP--KIVSAGAEGGANL 168
Cdd:PRK12445 148 KALRPLPDKFHGLQ---DQEVRYRQRYLDlIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPmmQVIPGGASARPFI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 169 FPIDYFGHPAYLAQSPQLY-KQIMVGVFERVFEVAAVYRaEEHATSRHLNEYLSLDVEMGFiEDEEDVMGLENRLLASIM 247
Cdd:PRK12445 225 THHNALDLDMYLRIAPELYlKRLVVGGFERVFEINRNFR-NEGISVRHNPEFTMMELYMAY-ADYHDLIELTESLFRTLA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 248 ERLRATSQAEFellGATIPDVPAHIPRITLMDArqlvTEKYGHPVGGKDLD------PEAE-------------RLLSQH 308
Cdd:PRK12445 303 QEVLGTTKVTY---GEHVFDFGKPFEKLTMREA----IKKYRPETDMADLDnfdaakALAEsigitvekswglgRIVTEI 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 309 FAETEGSDFV---FVTKYPRAARPfyahpeLNEDGSVNGEVTRGFDLLFRGIEITSGGQRIHDY----GMLMDSIAAYKL 381
Cdd:PRK12445 376 FDEVAEAHLIqptFITEYPAEVSP------LARRNDVNPEITDRFEFFIGGREIGNGFSELNDAedqaERFQEQVNAKAA 449
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 81858899 382 KPESL----EGYTEVFKYGMPPHGGFAIGAERLTAKLLGIANVRYARAFPRDR 430
Cdd:PRK12445 450 GDDEAmfydEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFPAMR 502
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
21-117 |
1.22e-15 |
|
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: 72.17 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 21 VKLQGFVHARRDLGGVQFLVLRDVTGVTQCVGSGLTLPLA---------ESSVEVVGKVKAHPKAPGGFEVQVEDFRVIS 91
Cdd:cd04319 2 VTLAGWVYRKREVGKKAFIVLRDSTGIVQAVFSKDLNEEAyreakkvgiESSVIVEGAVKADPRAPGGAEVHGEKLEIIQ 81
|
90 100
....*....|....*....|....*.
gi 81858899 92 AateATPVEIPKmewNVNPETMLDYR 117
Cdd:cd04319 82 N---VEFFPITE---DASDEFLLDVR 101
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
139-410 |
1.04e-13 |
|
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.
Pssm-ID: 238391 [Multi-domain] Cd Length: 211 Bit Score: 69.84 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 139 AFRAHLRGEGFTEISTPKIVSAGAEGGANLFPID------YFGHPAYLAQSPQLYKQIMVG-----VFERVFEVAAVYRA 207
Cdd:cd00768 8 KLRRFMAELGFQEVETPIVEREPLLEKAGHEPKDllpvgaENEEDLYLRPTLEPGLVRLFVshirkLPLRLAEIGPAFRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 208 EE-HATSRHLNEYLSLDVEMgFIEDEEDVMGLENrlLASIMERLratsqaeFELLGATIPdvpahipritlmdarqlvte 286
Cdd:cd00768 88 EGgRRGLRRVREFTQLEGEV-FGEDGEEASEFEE--LIELTEEL-------LRALGIKLD-------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 287 kyghpvggkdldpeaerllsqhfaetegsdFVFVTKYPRAARPfyahpelnedgsvnGEVTRGFDLLF-----RGIEITS 361
Cdd:cd00768 138 ------------------------------IVFVEKTPGEFSP--------------GGAGPGFEIEVdhpegRGLEIGS 173
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 81858899 362 GGQRIHDYGMLMDSIAayklkpeslegYTEVFKYGMPPHGGFAIGAERL 410
Cdd:cd00768 174 GGYRQDEQARAADLYF-----------LDEALEYRYPPTIGFGLGLERL 211
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
8-427 |
3.11e-12 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 68.84 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 8 TLTRELPQHEGQTVKLQGFVHARRDLGGVQFLVLRDVTGVTQCVGSGLTLPLAESS-----------VEVVGKVKAHPKa 76
Cdd:PRK02983 641 TVAEALDAPTGEEVSVSGRVLRIRDYGGVLFADLRDWSGELQVLLDASRLEQGSLAdfraavdlgdlVEVTGTMGTSRN- 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 77 pGGFEVQVEDFRVisAATEATPveIPKmEWN--VNPETMLDYRVVTVRGLKE-RAALKVQAELVDAFRAHLRGEGFTEIS 153
Cdd:PRK02983 720 -GTLSLLVTSWRL--AGKCLRP--LPD-KWKglTDPEARVRQRYLDLAVNPEaRDLLRARSAVVRAVRETLVARGFLEVE 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 154 TPkIVSAgAEGGANLFP----IDYFGHPAYLAQSPQLY-KQIMVGVFERVFEVAAVYRAE-----------------EHA 211
Cdd:PRK02983 794 TP-ILQQ-VHGGANARPfvthINAYDMDLYLRIAPELYlKRLCVGGVERVFELGRNFRNEgvdathnpeftlleayqAHA 871
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 212 ---TSRHLNEYLSLDV------EMGFIEDEEDVMGLENRLLASImeRLRATSQAEFELLGATI-PDVP----------AH 271
Cdd:PRK02983 872 dydTMRDLTRELIQNAaqaahgAPVVMRPDGDGVLEPVDISGPW--PVVTVHDAVSEALGEEIdPDTPlaelrklcdaAG 949
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 272 IPRITLMDARQLVTEKYGHPVGGKDLDPeaerllsqhfaetegsdfVFVTKYPRA----ARPFYAHPELNEDgsvngevt 347
Cdd:PRK02983 950 IPYRTDWDAGAVVLELYEHLVEDRTTFP------------------TFYTDFPTSvsplTRPHRSDPGLAER-------- 1003
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 348 rgFDLLFRGIEITSGgqrihdYGMLMD-----------SIAAYKLKPESL---EGYTEVFKYGMPPHGGFAIGAERLTAK 413
Cdd:PRK02983 1004 --WDLVAWGVELGTA------YSELTDpveqrrrlteqSLLAAGGDPEAMeldEDFLQALEYAMPPTGGLGMGVDRLVML 1075
|
490
....*....|....
gi 81858899 414 LLGiANVRYARAFP 427
Cdd:PRK02983 1076 LTG-RSIRETLPFP 1088
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
127-427 |
7.95e-12 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 66.94 E-value: 7.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 127 RAALKVQAELVDAFRAHLRGEGFTEISTPkiVSAGAEGGANLFPIDYFgHPA-----YLAQSPQLY-KQIMVGVFERVFE 200
Cdd:PLN02502 226 RDIFRTRAKIISYIRRFLDDRGFLEVETP--MLNMIAGGAAARPFVTH-HNDlnmdlYLRIATELHlKRLVVGGFERVYE 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 201 VAAVYRaEEHATSRHLNEYLSLDVEMGFiEDEEDVMGLENRLLASIMERLRATSQAEFellGATIPDVPAHIPRITLMDa 280
Cdd:PLN02502 303 IGRQFR-NEGISTRHNPEFTTCEFYQAY-ADYNDMMELTEEMVSGMVKELTGSYKIKY---HGIEIDFTPPFRRISMIS- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 281 rqLVTEKYGHPVGGKDLDPEAE---------------------RLLSQ---HFAETEGSDFVFVTKYPRA----ARPFYA 332
Cdd:PLN02502 377 --LVEEATGIDFPADLKSDEANayliaacekfdvkcpppqttgRLLNElfeEFLEETLVQPTFVLDHPVEmsplAKPHRS 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 333 HPELNE--DGSVNG--------EVTRGFDLLFRGIEITSGGQRIHDYGMLMDsiaayklkpeslEGYTEVFKYGMPPHGG 402
Cdd:PLN02502 455 KPGLTErfELFINGrelanafsELTDPVDQRERFEEQVKQHNAGDDEAMALD------------EDFCTALEYGLPPTGG 522
|
330 340
....*....|....*....|....*
gi 81858899 403 FAIGAERLTAKLLGIANVRYARAFP 427
Cdd:PLN02502 523 WGLGIDRLVMLLTDSASIRDVIAFP 547
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
17-421 |
1.03e-10 |
|
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA synthetase (class II) is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440803 [Multi-domain] Cd Length: 495 Bit Score: 63.51 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 17 EGQTVKLQGFVHARRDLGGVQFLVLRDVTGVTQC------VGSGLtlpLAESS-------VEVVGKVkahpkapggF--- 80
Cdd:COG1190 55 TGDEVSVAGRIMAKRDMGKASFADLQDGSGRIQLylrrdeLGEEA---YELFKlldlgdiVGVEGTV---------Frtk 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 81 --E--VQVEDFRVISAA--------TEATPVE----------IpkmewnVNPETmldyrvvtvrglkeRAALKVQAELVD 138
Cdd:COG1190 123 tgElsVKVEELTLLSKSlrplpekfHGLTDPEtryrqryvdlI------VNPEV--------------RETFRKRSKIIR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 139 AFRAHLRGEGFTEISTPkIVSAGAeGGANLFP----IDYFGHPAYLAQSPQLY-KQIMVGVFERVFEVAAVYRaEEHATS 213
Cdd:COG1190 183 AIRRFLDERGFLEVETP-MLQPIA-GGAAARPfithHNALDMDLYLRIAPELYlKRLIVGGFERVFEIGRNFR-NEGIDT 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 214 RHLNEYLSLDVEMGFiEDEEDVMGLENRLLASIMERLRATSQAEFEllGATIpDVPAHIPRITLMDArqlVTEKYGHPVG 293
Cdd:COG1190 260 THNPEFTMLELYQAY-ADYNDMMDLTEELIREAAEAVLGTTKVTYQ--GQEI-DLSPPWRRITMVEA---IKEATGIDVT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 294 GKDLDPEAERLLSQHFAETEGSD------------FV--------FVTKYPRA----ARPfyaHPElnedgsvNGEVTRG 349
Cdd:COG1190 333 PLTDDEELRALAKELGIEVDPGWgrgklidelfeeLVepkliqptFVTDYPVEvsplAKR---HRD-------DPGLTER 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 350 FDLLFRGIEITSG--------GQR--------IHDYG----MLMDS--IAAyklkpesLEgytevfkYGMPPHGGFAIGA 407
Cdd:COG1190 403 FELFIAGREIANAfselndpiDQRerfeeqleLKAAGddeaMPMDEdfLRA-------LE-------YGMPPTGGLGIGI 468
|
490
....*....|....
gi 81858899 408 ERLTAKLLGIANVR 421
Cdd:COG1190 469 DRLVMLLTDSPSIR 482
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
20-427 |
7.68e-10 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 60.82 E-value: 7.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 20 TVKLQGFVHARRDLGGVQFLVLR----DVTGVTQcVGSGLT---LPLAESSVEVvGKVKAHPKAP-----GGFEVQVEDF 87
Cdd:PTZ00385 109 TVRVAGRVTSVRDIGKIIFVTIRsngnELQVVGQ-VGEHFTredLKKLKVSLRV-GDIIGADGVPcrmqrGELSVAASRM 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 88 RVISAATEATPVEIPKME-WNVNPETMLDYRVVTVRGLKERA---ALKVQAELVDAFRAHLRGEGFTEISTPKIVSAGAE 163
Cdd:PTZ00385 187 LILSPYVCTDQVVCPNLRgFTVLQDNDVKYRYRFTDMMTNPCvieTIKKRHVMLQALRDYFNERNFVEVETPVLHTVASG 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 164 GGANLFPIDYFGHPA--YLAQSPQLY-KQIMVGVFERVFEVAAVYRAEEhATSRHLNEYLSLDVEMGFiEDEEDVMGLEN 240
Cdd:PTZ00385 267 ANAKSFVTHHNANAMdlFLRVAPELHlKQCIVGGMERIYEIGKVFRNED-ADRSHNPEFTSCEFYAAY-HTYEDLMPMTE 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 241 RLLASIMERLRATSQAEFELLGAT-IP---DVPAHIPRITLMDARQLVT-------EKYGHPVG---------GKDLDPE 300
Cdd:PTZ00385 345 DIFRQLAMRVNGTTVVQIYPENAHgNPvtvDLGKPFRRVSVYDEIQRMSgvefpppNELNTPKGiaymsvvmlRYNIPLP 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 301 AERLLSQHFAETegSDFvFVTKY---PRAA--RPFYAHPELNEDGSVNGEVTRgFDLLFRGIEITSGGQRIHD------- 368
Cdd:PTZ00385 425 PVRTAAKMFEKL--IDF-FITDRvvePTFVmdHPLFMSPLAKEQVSRPGLAER-FELFVNGIEYCNAYSELNDpheqyhr 500
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 369 -YGMLMDSIAAYKLKPESLEGYTEVFKYGMPPHGGFAIGAERLTAKLLGIANVRYARAFP 427
Cdd:PTZ00385 501 fQQQLVDRQGGDEEAMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFP 560
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
21-90 |
6.88e-09 |
|
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: 52.24 E-value: 6.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 21 VKLQGFVHA-RRDLGGVQFLVLRDVTGVTQCV---------GSGLTLplaESSVEVVGKVKAHPKapGGFEVQVEDFRVI 90
Cdd:pfam01336 1 VTVAGRVTSiRRSGGKLLFLTLRDGTGSIQVVvfkeeaeklAKKLKE---GDVVRVTGKVKKRKG--GELELVVEEIELL 75
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
108-410 |
1.87e-07 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 53.17 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 108 VNPETmldyrvvtvrglkeRAALKVQAELVDAFRAHLRGEGFTEISTPkIVSAGAeGGANLFP----IDYFGHPAYLAQS 183
Cdd:PRK00484 164 VNPES--------------RETFRKRSKIISAIRRFLDNRGFLEVETP-MLQPIA-GGAAARPfithHNALDIDLYLRIA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 184 PQLY-KQIMVGVFERVFEVAAVYRaEEHATSRHLNEYLSLDVEMGFiEDEEDVMGLENRLLASIMERLRATSQAEFEllG 262
Cdd:PRK00484 228 PELYlKRLIVGGFERVYEIGRNFR-NEGIDTRHNPEFTMLEFYQAY-ADYNDMMDLTEELIRHLAQAVLGTTKVTYQ--G 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 263 ATIpDVPAHIPRITLMDArqlVTEKYGHPVGGKDLDpEAERLLSQHFAETEGSD------------FV--------FVTK 322
Cdd:PRK00484 304 TEI-DFGPPFKRLTMVDA---IKEYTGVDFDDMTDE-EARALAKELGIEVEKSWglgklinelfeeFVepkliqptFITD 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 323 YPRAARPF-YAHPElnedgsvNGEVTRGFDLLFRGIEITSG----------GQRIH----------DYGMLMDsiaaykl 381
Cdd:PRK00484 379 YPVEISPLaKRHRE-------DPGLTERFELFIGGREIANAfselndpidqRERFEaqveakeagdDEAMFMD------- 444
|
330 340
....*....|....*....|....*....
gi 81858899 382 kpeslEGYTEVFKYGMPPHGGFAIGAERL 410
Cdd:PRK00484 445 -----EDFLRALEYGMPPTGGLGIGIDRL 468
|
|
| ScAspRS_mt_like_N |
cd04321 |
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
21-92 |
2.29e-06 |
|
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: 45.39 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 21 VKLQGFVHARRDLGG-VQFLVLRDVTG-VTQCVGSGLTLPL-------AESSVEVVGKVKAHPKAPGG----FEVQVEDF 87
Cdd:cd04321 2 VTLNGWIDRKPRIVKkLSFADLRDPNGdIIQLVSTAKKDAFsllksitAESPVQVRGKLQLKEAKSSEkndeWELVVDDI 81
|
....*
gi 81858899 88 RVISA 92
Cdd:cd04321 82 QTLNA 86
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
20-90 |
7.48e-06 |
|
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli asparaginyl-tRNA synthetase (AsnRS) and, in Arabidopsis thaliana and Saccharomyces cerevisiae mitochondrial (mt) AsnRS. This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. S. cerevisiae mtAsnRS can charge E.coli tRNA with asparagines. Mutations in the gene for S. cerevisiae mtAsnRS has been found to induce a "petite" phenotype typical for a mutation in a nuclear gene that results in a non-functioning mitochondrial protein synthesis system.
Pssm-ID: 239813 [Multi-domain] Cd Length: 82 Bit Score: 43.71 E-value: 7.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 20 TVKLQGFVHARRDLGGVQFLVLRDvtGVT----QCV----------GSGLTLPlaeSSVEVVGKVKAHPKAPGGFEVQVE 85
Cdd:cd04318 1 EVTVNGWVRSVRDSKKISFIELND--GSClknlQVVvdkeltnfkeILKLSTG---SSIRVEGVLVKSPGAKQPFELQAE 75
|
....*
gi 81858899 86 DFRVI 90
Cdd:cd04318 76 KIEVL 80
|
|
| RPA3 |
cd04479 |
RPA3: A subfamily of OB folds similar to human RPA3 (also called RPA14). RPA3 is the smallest ... |
4-73 |
2.83e-03 |
|
RPA3: A subfamily of OB folds similar to human RPA3 (also called RPA14). RPA3 is the smallest subunit of Replication protein A (RPA). RPA is a nuclear ssDNA binding protein (SSB) which appears to be involved in all aspects of DNA metabolism including replication, recombination, and repair. RPA also mediates specific interactions of various nuclear proteins. In animals, plants, and fungi, RPA is a heterotrimer with subunits of 70KDa (RPA1), 32kDa (RPA2), and 14 KDa (RPA3). RPA3 is believed to have a structural role in assembly of the RPA heterotrimer.
Pssm-ID: 239925 Cd Length: 101 Bit Score: 37.24 E-value: 2.83e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81858899 4 PLKRTLTRELPQHEGQTVKLQGFVHARRDlggvQFLVLRDVTGVTQCVGSGLTLPLAESS-VEVVGKVKAH 73
Cdd:cd04479 1 PTPRINGAMLSQFVGKTVRIVGKVEKVDG----DSLTLISSDGVNVTVELNRPLDLPISGyVEVIGKVSPD 67
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
20-98 |
3.62e-03 |
|
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: 36.77 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81858899 20 TVKLQGFVHARRDLGGVQ-FLVLRDVTGVTQCV---------------GSGLTLplaESSVEVVGKVKAHPK-----APG 78
Cdd:cd04320 1 EVLIRARVHTSRAQGAKLaFLVLRQQGYTIQGVlaasaegvskqmvkwAGSLSK---ESIVDVEGTVKKPEEpikscTQQ 77
|
90 100
....*....|....*....|
gi 81858899 79 GFEVQVEDFRVISAATEATP 98
Cdd:cd04320 78 DVELHIEKIYVVSEAAEPLP 97
|
|
| |
