|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
1-401 |
0e+00 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 650.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 1 MVKFAANINKESIVDVEGVVRKVNQKIGSCTQQdVELHVQKIYVISLAEPRLPLQLDDA-----VRPEAEGEEEGRATVN 75
Cdd:PLN02850 126 MVKYAKQLSRESVVDVEGVVSVPKKPVKGTTQQ-VEIQVRKIYCVSKALATLPFNVEDAarsesEIEKALQTGEQLVRVG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 76 QDTRLDNRVIDLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNNAYLAQSPQLYKQ 155
Cdd:PLN02850 205 QDTRLNNRVLDLRTPANQAIFRIQSQVCNLFREFLLSKGFVEIHTPKLIAGASEGGSAVFRLDYKGQPACLAQSPQLHKQ 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 156 MCICADFEKVFSIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYHEVMEEIADTMVQIFKGLQERFQTEIQTVNKQFPCE 235
Cdd:PLN02850 285 MAICGDFRRVFEIGPVFRAEDSFTHRHLCEFTGLDLEMEIKEHYSEVLDVVDELFVAIFDGLNERCKKELEAIREQYPFE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 236 PFKFLEPTLRLEYCEALAMLREAGVEMGDEDDLSTPNEKLLGHLVKEKYDTDFYILDKYPLAVRPFYTMPDPRNPKQSNS 315
Cdd:PLN02850 365 PLKYLPKTLRLTFAEGIQMLKEAGVEVDPLGDLNTESERKLGQLVKEKYGTDFYILHRYPLAVRPFYTMPCPDDPKYSNS 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 316 YDMFMRGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRD 395
Cdd:PLN02850 445 FDVFIRGEEIISGAQRVHDPELLEKRAEECGIDVKTISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPRD 524
|
....*.
gi 648216372 396 PKRLTP 401
Cdd:PLN02850 525 PQRLAP 530
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
74-397 |
8.87e-175 |
|
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: 490.16 E-value: 8.87e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 74 VNQDTRLDNRVIDLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNNAYLAQSPQLY 153
Cdd:cd00776 2 ANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 154 KQMCICAdFEKVFSIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYHEVMEEIADTMVQIFKGLQERFQTEIQTVNkQFP 233
Cdd:cd00776 82 KEMLIAA-LERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEDYNEVMDLIEELIKYIFKRVLERCAKELELVN-QLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 234 CEPFKFLEPTLRLEYCEALAMLREAGV--EMGDEDDLSTPNEKLLGhlvkEKYDTDFYILDKYPLAVRPFYTMPDPRNPK 311
Cdd:cd00776 160 RELLKPLEPFPRITYDEAIELLREKGVeeEVKWGEDLSTEHERLLG----EIVKGDPVFVTDYPKEIKPFYMKPDDDNPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 312 QSNSYDMFMRG-EEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTS 390
Cdd:cd00776 236 TVESFDLLMPGvGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAI 315
|
....*..
gi 648216372 391 MFPRDPK 397
Cdd:cd00776 316 LFPRDPK 322
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
1-401 |
3.17e-163 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 469.47 E-value: 3.17e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 1 MVKFAANINKESIVDVEGVVRKVNQKIGSCTQQDVELHVQKIYVISLAEPRLPLQLDDAvrpeAEGEEEGRATVNQDTRL 80
Cdd:PTZ00401 122 MIDFIGQIPTESIVDVEATVCKVEQPITSTSHSDIELKVKKIHTVTESLRTLPFTLEDA----SRKESDEGAKVNFDTRL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 81 DNRVIDLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNNAYLAQSPQLYKQMCICA 160
Cdd:PTZ00401 198 NSRWMDLRTPASGAIFRLQSRVCQYFRQFLIDSDFCEIHSPKIINAPSEGGANVFKLEYFNRFAYLAQSPQLYKQMVLQG 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 161 DFEKVFSIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYHEVMeeiaDTMVQIFKGLQERFQT---EIQTVNKQFPCEPF 237
Cdd:PTZ00401 278 DVPRVFEVGPVFRSENSNTHRHLTEFVGLDVEMRINEHYYEVL----DLAESLFNYIFERLAThtkELKAVCQQYPFEPL 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 238 KF------------------LEPT--------------LRLEYCEALAMLREAGVE-MGDEDDLSTPNEKLLGHLVKEKY 284
Cdd:PTZ00401 354 VWkltpermkelgvgvisegVEPTdkyqarvhnmdsrmLRINYMHCIELLNTVLEEkMAPTDDINTTNEKLLGKLVKERY 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 285 DTDFYILDKYPLAVRPFYTMPDPRNPKQSNSYDMFMRGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAP 364
Cdd:PTZ00401 434 GTDFFISDRFPSSARPFYTMECKDDERFTNSYDMFIRGEEISSGAQRIHDPDLLLARAKMLNVDLTPIKEYVDSFRLGAW 513
|
410 420 430
....*....|....*....|....*....|....*..
gi 648216372 365 PHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP 401
Cdd:PTZ00401 514 PHGGFGVGLERVVMLYLGLSNVRLASLFPRDPQRTTP 550
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
1-401 |
8.33e-157 |
|
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: 448.50 E-value: 8.33e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 1 MVKFAANINKESIVDVEGVVRkvnqkIGSCTQQDVELHVQKIYVISLAEPRLPLQLDDAVRPEAegeeegratvnqDTRL 80
Cdd:TIGR00458 55 LFKWAKKLNLESVVAVRGIVK-----IKEKAPGGFEIIPTKIEVINEAKEPLPLDPTEKVPAEL------------DTRL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 81 DNRVIDLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNNAYLAQSPQLYKQMCICA 160
Cdd:TIGR00458 118 DYRFLDLRRPTVQAIFRIRSGVLESVREFLAEEGFIEVHTPKLVASATEGGTELFPITYFEREAFLGQSPQLYKQQLMAA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 161 DFEKVFSIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHyHEVMEEIADTMVQIFKGLQERFQTEIQTVNKQFPCEPFKFl 240
Cdd:TIGR00458 198 GFERVYEIGPIFRAEEHNTHRHLNEATSIDIEMAFEDH-HDVMDILEELVVRVFEDVPERCAHQLETLEFKLEKPEGKF- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 241 eptLRLEYCEALAMLREAGVEMGDEDDLSTPNEKLLGhlvkEKYDTDFYILDkYPLAVRPFYTMPDPRNPKQSNSYDMFM 320
Cdd:TIGR00458 276 ---VRLTYDEAIEMANAKGVEIGWGEDLSTEAEKALG----EEMDGLYFITD-WPTEIRPFYTMPDEDNPEISKSFDLMY 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 321 RGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLT 400
Cdd:TIGR00458 348 RDLEISSGAQRIHLHDLLVERIKAKGLNPEGFKDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFPRDRKRLT 427
|
.
gi 648216372 401 P 401
Cdd:TIGR00458 428 P 428
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
2-401 |
9.79e-156 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 446.17 E-value: 9.79e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 2 VKFAANINKESIVDVEGVVRKVNQKIGSctqqdVELHVQKIYVISLAEPRLPLQLDDAVRPEAegeeegratvnqDTRLD 81
Cdd:PRK05159 59 FETIKKLKRESVVSVTGTVKANPKAPGG-----VEVIPEEIEVLNKAEEPLPLDISGKVLAEL------------DTRLD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 82 NRVIDLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNNAYLAQSPQLYKQMCICAD 161
Cdd:PRK05159 122 NRFLDLRRPRVRAIFKIRSEVLRAFREFLYENGFTEIFTPKIVASGTEGGAELFPIDYFEKEAYLAQSPQLYKQMMVGAG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 162 FEKVFSIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYHEVMEEIADTMVQIFKGLQERFQTEIQTVNKQFPCEPfkflE 241
Cdd:PRK05159 202 FERVFEIGPVFRAEEHNTSRHLNEYTSIDVEMGFIDDHEDVMDLLENLLRYMYEDVAENCEKELELLGIELPVPE----T 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 242 PTLRLEYCEALAMLREAGVEMGDEDDLSTPNEKLLGHLVKEKYDTDFYILDKYPLAVRPFYTMPDPRNPKQSNSYDMFMR 321
Cdd:PRK05159 278 PIPRITYDEAIEILKSKGNEISWGDDLDTEGERLLGEYVKEEYGSDFYFITDYPSEKRPFYTMPDEDDPEISKSFDLLFR 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 322 GEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP 401
Cdd:PRK05159 358 GLEITSGGQRIHRYDMLVESIKEKGLNPESFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFPRDRHRLTP 437
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
5-401 |
9.82e-150 |
|
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: 430.63 E-value: 9.82e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 5 AANINKESIVDVEGVVRKVNQKigsctQQDVELHVQKIYVISLAEPRLPLQLDDAvrpeaegeeegratvNQDTRLDNRV 84
Cdd:COG0017 59 AKKLTTESSVEVTGTVVESPRA-----PQGVELQAEEIEVLGEADEPYPLQPKRH---------------SLEFLLDNRH 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 85 IDLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNNAYLAQSPQLYKQMCICAdFEK 164
Cdd:COG0017 119 LRLRTNRFGAIFRIRSELARAIREFFQERGFVEVHTPIITASATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMA-LEK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 165 VFSIGPVFRAEDSNTHRHLTEFVGLDIEMAFnYHYHEVMEEIADTMVQIFKGLQERFQTEIQTVN------KQFPCEPFK 238
Cdd:COG0017 198 VYTFGPTFRAEKSNTRRHLAEFWMIEPEMAF-ADLEDVMDLAEEMLKYIIKYVLENCPEELEFLGrdverlEKVPESPFP 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 239 fleptlRLEYCEALAMLREAGVEMGDEDDLSTPNEKLLGhlvkEKYDTDFYILDKYPLAVRPFYTMPDPRNPKQSNSYDM 318
Cdd:COG0017 277 ------RITYTEAIEILKKSGEKVEWGDDLGTEHERYLG----EEFFKKPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 319 FMRG-EEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPK 397
Cdd:COG0017 347 LAPGiGEIIGGSQREHRYDVLVERIKEKGLDPEDYEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPG 426
|
....
gi 648216372 398 RLTP 401
Cdd:COG0017 427 RLTP 430
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
75-396 |
6.21e-102 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 304.87 E-value: 6.21e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 75 NQDTRLDNRVIDLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNN--AYLAQSPQL 152
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGkfYALPQSPQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 153 YKQMCICADFEKVFSIGPVFRAEDSNTHRHLtEFVGLDIEMAFNyHYHEVMEEIADTMVQIFKGLQERFQTEIQTVNKQF 232
Cdd:pfam00152 81 YKQLLMVAGFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFV-DYEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 233 PcEPFKfleptlRLEYCEALAMLREAGVEMGDEDdLSTPNEKLLGHLVKEKYDTDFYILDKYPLAVRPFYTMPDPRNPKQ 312
Cdd:pfam00152 159 K-KPFP------RITYAEAIEKLNGKDVEELGYG-SDKPDLRFLLELVIDKNKFNPLWVTDFPAEHHPFTMPKDEDDPAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 313 SNSYDMFMRGEEILSGAQRIHDPQLLTERALHHGIDLEKIKA----YIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQ 388
Cdd:pfam00152 231 AEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDPEEAEEkfgfYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIRE 310
|
....*...
gi 648216372 389 TSMFPRDP 396
Cdd:pfam00152 311 VIAFPKTR 318
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
5-401 |
2.45e-74 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 238.47 E-value: 2.45e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 5 AANINKESIVDVEGVVRKVNQKigsctQQDVELHVQKIYVISLAEPRLPLQLDDAvrpeaegeeegratvNQDTRLDNRV 84
Cdd:PRK03932 62 IKKLTTGSSVIVTGTVVESPRA-----GQGYELQATKIEVIGEDPEDYPIQKKRH---------------SIEFLREIAH 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 85 IDLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVS---------YFKNNAYLAQSPQLYKQ 155
Cdd:PRK03932 122 LRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVDTPIITASDCEGAGELFRVTtldldfskdFFGKEAYLTVSGQLYAE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 156 MCICAdFEKVFSIGPVFRAEDSNTHRHLTEFVGLDIEMAFnYHYHEVMEeIADTMVQ-IFKGLQERFQTEIQTVNKQFPC 234
Cdd:PRK03932 202 AYAMA-LGKVYTFGPTFRAENSNTRRHLAEFWMIEPEMAF-ADLEDNMD-LAEEMLKyVVKYVLENCPDDLEFLNRRVDK 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 235 EPFKFLEPTL-----RLEYCEALAMLREAG------VEMGDedDLSTPNEKLLghlVKEKYDTDFYILDkYPLAVRPFYT 303
Cdd:PRK03932 279 GDIERLENFIespfpRITYTEAIEILQKSGkkfefpVEWGD--DLGSEHERYL---AEEHFKKPVFVTN-YPKDIKAFYM 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 304 MPDPRNpKQSNSYDMFMRG-EEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLG 382
Cdd:PRK03932 353 RLNPDG-KTVAAMDLLAPGiGEIIGGSQREERLDVLEARIKELGLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITG 431
|
410
....*....|....*....
gi 648216372 383 LHNVRQTSMFPRDPKRLTP 401
Cdd:PRK03932 432 LDNIRDVIPFPRTPGRAEF 450
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
2-401 |
2.01e-69 |
|
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: 225.72 E-value: 2.01e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 2 VKFAANINKESIVDVEGVVRKVNQKigsctQQDVELHVQKIYVISLAEPR-LPLQLDDavrpeaegeeegratvnQDTRL 80
Cdd:TIGR00457 61 FQLLKSLTTGSSVSVTGKVVESPGK-----GQPVELQVKKIEVVGEAEPDdYPLQKKE-----------------HSLEF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 81 --DNRVIDLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVS---------YFKNNAYLAQS 149
Cdd:TIGR00457 119 lrDIAHLRLRTNTLGAVMRVRNALSQAIHRYFQENGFTWVSPPILTSNDCEGAGELFRVStgnidfsqdFFGKEAYLTVS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 150 PQLYKQMCICAdFEKVFSIGPVFRAEDSNTHRHLTEFVGLDIEMAFnYHYHEVMEEIADTMVQIFKGLQERFQTEIQTVN 229
Cdd:TIGR00457 199 GQLYLETYALA-LSKVYTFGPTFRAEKSNTSRHLSEFWMIEPEMAF-ANLNDLLQLAETLIKYIIKAVLENCSQELKFLE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 230 KQFPCEPFKFLEPTL-----RLEYCEALAMLREAGVEMGDED----DLSTPNEKLLGhlvkEKYDTDFYILDKYPLAVRP 300
Cdd:TIGR00457 277 KNFDKDLIKRLENIInnkfaRITYTDAIEILKESDKNFEYEDfwgdDLQTEHERFLA----EEYFKPPVFVTNYPKDIKA 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 301 FYtMPDPRNPKQSNSYDMFMRG-EEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTML 379
Cdd:TIGR00457 353 FY-MKLNDDGKTVAAMDLLAPGiGEIIGGSEREDDLDKLENRMKEMGLDTDALNWYLDLRKYGSVPHSGFGLGFERLLAY 431
|
410 420
....*....|....*....|..
gi 648216372 380 FLGLHNVRQTSMFPRDPKRLTP 401
Cdd:TIGR00457 432 ITGLENIRDAIPFPRTPGNINF 453
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
96-395 |
1.10e-58 |
|
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: 192.31 E-value: 1.10e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 96 FRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFK--NNAYLAQSPQLYKQMCICADFEKVFSIGPVFR 173
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNAlgLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 174 AEDSNThRHLTEFVGLDIEMAFNyHYHEVMEEIADTMVQIFKGLQErfqteiqTVNKQFPCEPFKFLEPTLRLEYCEALA 253
Cdd:cd00669 81 NEDLRA-RHQPEFTMMDLEMAFA-DYEDVIELTERLVRHLAREVLG-------VTAVTYGFELEDFGLPFPRLTYREALE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 254 MLREagvemgdeddlstpnekllghlvkekydtdFYILDKYPLAVRPFYTMPDPRNPKQSNSYDMFMRGEEILSGAQRIH 333
Cdd:cd00669 152 RYGQ------------------------------PLFLTDYPAEMHSPLASPHDVNPEIADAFDLFINGVEVGNGSSRLH 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648216372 334 DPQLLTERALHHGID----LEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRD 395
Cdd:cd00669 202 DPDIQAEVFQEQGINkeagMEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKM 267
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
76-396 |
2.40e-50 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 172.51 E-value: 2.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 76 QDTRLDNRVIdLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPkIISA--------ASEGGANVFTVSYFKNNAYLA 147
Cdd:PRK06462 11 EEFLRMSWKH-ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPP-IISPstdplmglGSDLPVKQISIDFYGVEYYLA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 148 QSPQLYKQMCIcADFEKVFSIGPVFRAE--DSNTHRHLTEFVGLDIEMAfNYHYHEVMEEIADTMVQIFKGLQERFQTEI 225
Cdd:PRK06462 89 DSMILHKQLAL-RMLGKIFYLSPNFRLEpvDKDTGRHLYEFTQLDIEIE-GADLDEVMDLIEDLIKYLVKELLEEHEDEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 226 QTVNKQFPcepfKFLEPTLRLEYCEALAMLREAGVEMGDEDDLSTPNEKLLghlvKEKYDTDFYILDkYPLAVRPFYTMP 305
Cdd:PRK06462 167 EFFGRDLP----HLKRPFKRITHKEAVEILNEEGCRGIDLEELGSEGEKSL----SEHFEEPFWIID-IPKGSREFYDRE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 306 DPRNPKQSNSYDMFMR---GEeILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLG 382
Cdd:PRK06462 238 DPERPGVLRNYDLLLPegyGE-AVSGGEREYEYEEIVERIREHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICG 316
|
330
....*....|....
gi 648216372 383 LHNVRQTSMFPRDP 396
Cdd:PRK06462 317 LRHIREVQPFPRVP 330
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
5-393 |
7.07e-44 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 160.62 E-value: 7.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 5 AANINKESIVDVEGVVRK-----VNQKIGSctqQDVELHVQKIYVISLAEPrLPLQLDDavrpeaegeeegRATVNQDTR 79
Cdd:PRK00476 61 AESLRSEYVIQVTGTVRArpegtVNPNLPT---GEIEVLASELEVLNKSKT-LPFPIDD------------EEDVSEELR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 80 LDNRVIDLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPkIISAASEGGANVFTV-S-YFKNNAY-LAQSPQLYKQM 156
Cdd:PRK00476 125 LKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDDNGFLEIETP-ILTKSTPEGARDYLVpSrVHPGKFYaLPQSPQLFKQL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 157 CICADFEKVFSIGPVFRAEDSNTHRhLTEFVGLDIEMAFnYHYHEVMEEIADTMVQIFKGL--------------QE--- 219
Cdd:PRK00476 204 LMVAGFDRYYQIARCFRDEDLRADR-QPEFTQIDIEMSF-VTQEDVMALMEGLIRHVFKEVlgvdlptpfprmtyAEamr 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 220 ---------RFQTEIQTVNKQFPCEPFK-FLEPT--------LRLEYC-------------------------------- 249
Cdd:PRK00476 282 rygsdkpdlRFGLELVDVTDLFKDSGFKvFAGAAndggrvkaIRVPGGaaqlsrkqideltefakiygakglayikvned 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 250 ------------EALAMLREA-GVEMGD-----EDDLSTPNE----------KLLGHLVKEKYD----TDFyildkyPL- 296
Cdd:PRK00476 362 glkgpiakflseEELAALLERtGAKDGDliffgADKAKVVNDalgalrlklgKELGLIDEDKFAflwvVDF------PMf 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 297 -----AVR------PFyTMPDP--------RNPKQ--SNSYDMFMRGEEILSGAQRIHDPQLLtERALHH-GIDLEKIKA 354
Cdd:PRK00476 436 eydeeEGRwvaahhPF-TMPKDedldeletTDPGKarAYAYDLVLNGYELGGGSIRIHRPEIQ-EKVFEIlGISEEEAEE 513
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 648216372 355 ----YIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 393
Cdd:PRK00476 514 kfgfLLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
96-393 |
5.14e-41 |
|
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. AspRS is a homodimer, which attaches a specific amino acid to the 3' OH group of ribose of the appropriate tRNA. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. AspRS in this family differ from those found in the AsxRS family by a GAD insert in the core domain.
Pssm-ID: 238400 [Multi-domain] Cd Length: 280 Bit Score: 146.18 E-value: 5.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 96 FRLQSGICHLFRETLINKGFVEIQTPkIISAASEGGANVFTVSY--FKNNAY-LAQSPQLYKQMCICADFEKVFSIGPVF 172
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETP-ILTKSTPEGARDFLVPSrlHPGKFYaLPQSPQLFKQLLMVSGFDRYFQIARCF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 173 RAEDSNTHRHlTEFVGLDIEMAFnYHYHEVMEEIADTMVQIFKglqERFQTEIQTvnkqfpcePFKfleptlRLEYCEAL 252
Cdd:cd00777 80 RDEDLRADRQ-PEFTQIDIEMSF-VDQEDIMSLIEGLLKYVFK---EVLGVELTT--------PFP------RMTYAEAM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 253 amlreagvemgdeddlstpnekllghlvkEKYDTDF-YILD-----------KYPLAVRPFyTMPDP-------RNPKQ- 312
Cdd:cd00777 141 -----------------------------ERYGFKFlWIVDfplfewdeeegRLVSAHHPF-TAPKEedldlleKDPEDa 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 313 -SNSYDMFMRGEEILSGAQRIHDPQlLTERALHH-GIDLEKIKA----YIDSFRFGAPPHAGGGIGLERVTMLFLGLHNV 386
Cdd:cd00777 191 rAQAYDLVLNGVELGGGSIRIHDPD-IQEKVFEIlGLSEEEAEEkfgfLLEAFKYGAPPHGGIALGLDRLVMLLTGSESI 269
|
....*..
gi 648216372 387 RQTSMFP 393
Cdd:cd00777 270 RDVIAFP 276
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
5-393 |
2.34e-40 |
|
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: 150.92 E-value: 2.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 5 AANINKESIVDVEGVVRK-----VNQKI--GsctqqDVELHVQKIYVISLAEPrLPLQLDDAVRpeaegeeegratVNQD 77
Cdd:COG0173 62 AEKLRSEYVIAVTGKVRArpegtVNPKLptG-----EIEVLASELEILNKAKT-PPFQIDDDTD------------VSEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 78 TRLDNRVIDLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPkIISAASEGGANVFTV-------SYFknnAyLAQSP 150
Cdd:COG0173 124 LRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDENGFLEIETP-ILTKSTPEGARDYLVpsrvhpgKFY---A-LPQSP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 151 QLYKQMCICADFEKVFSIGPVFRAEDSNTHRHLtEFVGLDIEMAF---NyhyhEVMEEIADTMVQIFKGL---------- 217
Cdd:COG0173 199 QLFKQLLMVSGFDRYFQIARCFRDEDLRADRQP-EFTQLDIEMSFvdqE----DVFELMEGLIRHLFKEVlgvelptpfp 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 218 ----QE------------RFQTEIQTVNKQFPCEPFK-FLEPT--------LRLEYC----------------------- 249
Cdd:COG0173 274 rmtyAEamerygsdkpdlRFGLELVDVTDIFKDSGFKvFAGAAenggrvkaINVPGGaslsrkqideltefakqygakgl 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 250 --------------------EALAMLREA-GVEMGD-----EDDLSTPNE----------KLLGHLVKEKYD----TDFy 289
Cdd:COG0173 354 ayikvnedglkspiakflseEELAAILERlGAKPGDliffvADKPKVVNKalgalrlklgKELGLIDEDEFAflwvVDF- 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 290 ildkyPL-----------AVR-PFyTMPDP-------RNPKQ--SNSYDMFMRGEEILSGAQRIHDPQLLtERALHH-GI 347
Cdd:COG0173 433 -----PLfeydeeegrwvAMHhPF-TMPKDedldlleTDPGKvrAKAYDLVLNGYELGGGSIRIHDPELQ-EKVFELlGI 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 648216372 348 DLEKIKA----YIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 393
Cdd:COG0173 506 SEEEAEEkfgfLLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
14-396 |
7.94e-30 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 120.85 E-value: 7.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 14 VDVEGVVRKvnqkiGSCTQQDVELHVQKIYVISLAEPRLPLQlddavrpeaegeeegRATVNQDTRLDNRVIDLRTSTSQ 93
Cdd:PLN02603 164 VLVQGTVVS-----SQGGKQKVELKVSKIVVVGKSDPSYPIQ---------------KKRVSREFLRTKAHLRPRTNTFG 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 94 AVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVS------------------------------YFKNN 143
Cdd:PLN02603 224 AVARVRNALAYATHKFFQENGFVWVSSPIITASDCEGAGEQFCVTtlipnsaenggslvddipktkdglidwsqdFFGKP 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 144 AYLAQSPQLYKQMCICAdFEKVFSIGPVFRAEDSNTHRHLTEFVGLDIEMAF--------------NYHYHEVMEEIADT 209
Cdd:PLN02603 304 AFLTVSGQLNGETYATA-LSDVYTFGPTFRAENSNTSRHLAEFWMIEPELAFadlnddmacataylQYVVKYILENCKED 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 210 M----VQIFKGLQERFQteiQTVNKQFpcepfkfleptLRLEYCEALAMLREAG------VEMGDedDLSTPNEKllgHL 279
Cdd:PLN02603 383 MeffnTWIEKGIIDRLS---DVVEKNF-----------VQLSYTDAIELLLKAKkkfefpVKWGL--DLQSEHER---YI 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 280 VKEKYDTDFYILDKYPLAVRPFYtMPDPRNPKQSNSYDMFM-RGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDS 358
Cdd:PLN02603 444 TEEAFGGRPVIIRDYPKEIKAFY-MRENDDGKTVAAMDMLVpRVGELIGGSQREERLEYLEARLDELKLNKESYWWYLDL 522
|
410 420 430
....*....|....*....|....*....|....*...
gi 648216372 359 FRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDP 396
Cdd:PLN02603 523 RRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFPRVP 560
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
1-58 |
1.08e-27 |
|
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: 105.34 E-value: 1.08e-27
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 648216372 1 MVKFAANINKESIVDVEGVVRKVNQKIGSCTQQDVELHVQKIYVISLAEPRLPLQLDD 58
Cdd:cd04320 45 MVKWAGSLSKESIVDVEGTVKKPEEPIKSCTQQDVELHIEKIYVVSEAAEPLPFQLED 102
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
5-394 |
4.32e-27 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 113.34 E-value: 4.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 5 AANINKESIVDVEGVVRK-----VNQKIGSCTQQDVELHVQKIYVISLAEPRLPLQLDDAvrpeaegeeegRATVNQDTR 79
Cdd:PLN02903 118 ANRLRNEYVVAVEGTVRSrpqesPNKKMKTGSVEVVAESVDILNVVTKSLPFLVTTADEQ-----------KDSIKEEVR 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 80 LDNRVIDLRTSTSQAVFRLQSGICHLFRETLINK-GFVEIQTPKIISAASEGGANVFTVSYFKNNAYLA--QSPQLYKQM 156
Cdd:PLN02903 187 LRYRVLDLRRPQMNANLRLRHRVVKLIRRYLEDVhGFVEIETPILSRSTPEGARDYLVPSRVQPGTFYAlpQSPQLFKQM 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 157 CICADFEKVFSIGPVFRAEDSNTHRHlTEFVGLDIEMAFNyHYHEVMEEIADTMVQIFK---GLQ--------------- 218
Cdd:PLN02903 267 LMVSGFDRYYQIARCFRDEDLRADRQ-PEFTQLDMELAFT-PLEDMLKLNEDLIRQVFKeikGVQlpnpfprltyaeams 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 219 --------ERFQTEIQTVNKQFPCEPFKFLE-------------------------------------------PTLR-- 245
Cdd:PLN02903 345 kygsdkpdLRYGLELVDVSDVFAESSFKVFAgalesggvvkaicvpdgkkisnntalkkgdiyneaiksgakglAFLKvl 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 246 ----LEYCEAL----------AMLREAGVEMGD-----EDDLSTPNEKL--LGHLVKEKYD------------TDFYILD 292
Cdd:PLN02903 425 ddgeLEGIKALveslspeqaeQLLAACGAGPGDlilfaAGPTSSVNKTLdrLRQFIAKTLDlidpsrhsilwvTDFPMFE 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 293 KYPLAVR------PFyTMPDPRNPKQSNS-----YDMFMRGEEILSGAQRIH--DPQLLTERALhhGIDLE----KIKAY 355
Cdd:PLN02903 505 WNEDEQRlealhhPF-TAPNPEDMGDLSSaralaYDMVYNGVEIGGGSLRIYrrDVQQKVLEAI--GLSPEeaesKFGYL 581
|
490 500 510
....*....|....*....|....*....|....*....
gi 648216372 356 IDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPR 394
Cdd:PLN02903 582 LEALDMGAPPHGGIAYGLDRLVMLLAGAKSIRDVIAFPK 620
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
75-393 |
1.79e-26 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 111.66 E-value: 1.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 75 NQDTRLDNRVIDLRTSTSQ-AVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNNA--YLAQSPQ 151
Cdd:PTZ00385 211 DNDVKYRYRFTDMMTNPCViETIKKRHVMLQALRDYFNERNFVEVETPVLHTVASGANAKSFVTHHNANAMdlFLRVAPE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 152 LYKQMCICADFEKVFSIGPVFRAEDSNtHRHLTEFVGLDIEMAfnYH-YHEVMEEIADTMVQIFKGLQERFQTEIQTVNK 230
Cdd:PTZ00385 291 LHLKQCIVGGMERIYEIGKVFRNEDAD-RSHNPEFTSCEFYAA--YHtYEDLMPMTEDIFRQLAMRVNGTTVVQIYPENA 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 231 QFPCEPFKFLEPTLRLEYCEALAmlREAGVEMGDEDDLSTPNEKLLGHLVKEKYDT----------------DFYILDKy 294
Cdd:PTZ00385 368 HGNPVTVDLGKPFRRVSVYDEIQ--RMSGVEFPPPNELNTPKGIAYMSVVMLRYNIplppvrtaakmfekliDFFITDR- 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 295 plAVRPFYTMPDP-----------RNPKQSNSYDMFMRGEEILSGAQRIHDP--------QLLTERalhHGIDLEKI--- 352
Cdd:PTZ00385 445 --VVEPTFVMDHPlfmsplakeqvSRPGLAERFELFVNGIEYCNAYSELNDPheqyhrfqQQLVDR---QGGDEEAMpld 519
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 648216372 353 KAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 393
Cdd:PTZ00385 520 ETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFP 560
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
3-401 |
5.00e-25 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 107.38 E-value: 5.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 3 KFAANINKESIVDVEGVVRKVNQKIGS--CTQQDVELHVQKIYVISLAEPrLPLQLDDAVRPEAEGEEEGRAtVNQDTRL 80
Cdd:PRK12820 63 ELAASLRAEFCVALQGEVQKRLEETENphIETGDIEVFVRELSILAASEA-LPFAISDKAMTAGAGSAGADA-VNEDLRL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 81 DNRVIDLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNNAY--LAQSPQLYKQMCI 158
Cdd:PRK12820 141 QYRYLDIRRPAMQDHLAKRHRIIKCARDFLDSRGFLEIETPILTKSTPEGARDYLVPSRIHPKEFyaLPQSPQLFKQLLM 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 159 CADFEKVFSIGPVFRAEDSNTHRHlTEFVGLDIEMAF------------------------------NYHYHEVME---- 204
Cdd:PRK12820 221 IAGFERYFQLARCFRDEDLRPNRQ-PEFTQLDIEASFideefifelieeltarmfaiggialprpfpRMPYAEAMDttgs 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 205 ------------EIAD----TMVQIFKGLQERfQTEIQTVNKQFPCEpfKFLEPTLRLEYCEALA----------MLREA 258
Cdd:PRK12820 300 drpdlrfdlkfaDATDifenTRYGIFKQILQR-GGRIKGINIKGQSE--KLSKNVLQNEYAKEIApsfgakgmtwMRAEA 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 259 G------VEMGDEDDLstpnEKLLGHLVKEKYDTDFYILDK----------------------------YPLAVRPF--- 301
Cdd:PRK12820 377 GgldsniVQFFSADEK----EALKRRFHAEDGDVIIMIADAscaivlsalgqlrlhladrlglipegvfHPLWITDFplf 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 302 --------------YTMP-----DPRNPK-----QSNSYDMFMRGEEILSGAQRIHDP--QLLTERALhhGIDLEKIKA- 354
Cdd:PRK12820 453 eatddggvtsshhpFTAPdredfDPGDIEelldlRSRAYDLVVNGEELGGGSIRINDKdiQLRIFAAL--GLSEEDIEDk 530
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 648216372 355 ---YIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP 401
Cdd:PRK12820 531 fgfFLRAFDFAAPPHGGIALGLDRVVSMILQTPSIREVIAFPKNRSAACP 580
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
135-398 |
1.06e-24 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 105.85 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 135 FTVSYFKNNAYLAQSPQLYKQMCICAdFEKVFSIGPVFRAEDSNTHRHLTEFVGLDIEMAFNyHYHEVMEeIADTMVQ-I 213
Cdd:PLN02221 300 YSKDFFGRQAFLTVSGQLQVETYACA-LSSVYTFGPTFRAENSHTSRHLAEFWMVEPEIAFA-DLEDDMN-CAEAYVKyM 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 214 FKGLQERFQTEIQTVNKQFPCEPFKFLE-----PTLRLEYCEALAMLREAgVEMGDE--------DDLSTPNEKLLGHLV 280
Cdd:PLN02221 377 CKWLLDKCFDDMELMAKNFDSGCIDRLRmvastPFGRITYTEAIELLEEA-VAKGKEfdnnvewgIDLASEHERYLTEVL 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 281 KEKYdtdfYILDKYPLAVRPFYtMPDPRNPKQSNSYDMFM-RGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSF 359
Cdd:PLN02221 456 FQKP----LIVYNYPKGIKAFY-MRLNDDEKTVAAMDVLVpKVGELIGGSQREERYDVIKQRIEEMGLPIEPYEWYLDLR 530
|
250 260 270
....*....|....*....|....*....|....*....
gi 648216372 360 RFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKR 398
Cdd:PLN02221 531 RYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPRYPGK 569
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
75-393 |
7.71e-24 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 103.22 E-value: 7.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 75 NQDTRLDNRVIDL-RTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSY--FKNNAYLAQSPQ 151
Cdd:PRK12445 162 DQEVRYRQRYLDLiANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHnaLDLDMYLRIAPE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 152 LYKQMCICADFEKVFSIGPVFRAEDSNThRHLTEFVGLDIEMAFNyHYHEVMEeiadTMVQIFKGLQerfQTEIQTVNKQ 231
Cdd:PRK12445 242 LYLKRLVVGGFERVFEINRNFRNEGISV-RHNPEFTMMELYMAYA-DYHDLIE----LTESLFRTLA---QEVLGTTKVT 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 232 FPCEPFKFLEPTLRLEYCEALAMLREAgVEMGDEDDLSTPN----------EKL--LGHLVKEKYD-------TDFYILD 292
Cdd:PRK12445 313 YGEHVFDFGKPFEKLTMREAIKKYRPE-TDMADLDNFDAAKalaesigitvEKSwgLGRIVTEIFDevaeahlIQPTFIT 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 293 KYPLAVRPFYTMPDPrNPKQSNSYDMFMRGEEILSGAQRIHDPQLLTER------ALHHGIDLEKI--KAYIDSFRFGAP 364
Cdd:PRK12445 392 EYPAEVSPLARRNDV-NPEITDRFEFFIGGREIGNGFSELNDAEDQAERfqeqvnAKAAGDDEAMFydEDYVTALEYGLP 470
|
330 340
....*....|....*....|....*....
gi 648216372 365 PHAGGGIGLERVTMLFLGLHNVRQTSMFP 393
Cdd:PRK12445 471 PTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
84-396 |
3.97e-23 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 101.25 E-value: 3.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 84 VIDLRTSTSQAVfrlqsgicHLFRETlinKGFVEIQTPKIISAASEGGANVFTVS------------------------- 138
Cdd:PTZ00425 214 VIRIRNALAIAT--------HLFFQS---RGFLYIHTPLITTSDCEGGGEMFTVTtllgedadyraiprvnkknkkgekr 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 139 --------------------------------------YFKNNAYLAQSPQLYKQMcICADFEKVFSIGPVFRAEDSNTH 180
Cdd:PTZ00425 283 edilntcnannnngnssssnavsspaypdqylidykkdFFSKQAFLTVSGQLSLEN-LCSSMGDVYTFGPTFRAENSHTS 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 181 RHLTEFVGLDIEMAFNYHYHEVmeEIADTMVQIFKG--LQERFQtEIQTVNKQFPCEPFKFLEPTL-----RLEYCEALA 253
Cdd:PTZ00425 362 RHLAEFWMIEPEIAFADLYDNM--ELAESYIKYCIGyvLNNNFD-DIYYFEENVETGLISRLKNILdedfaKITYTNVID 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 254 MLR------EAGVEMGDedDLSTPNEKLlghlVKEKYDTDFYILDKYPLAVRPFYtMPDPRNPKQSNSYDMFM-RGEEIL 326
Cdd:PTZ00425 439 LLQpysdsfEVPVKWGM--DLQSEHERF----VAEQIFKKPVIVYNYPKDLKAFY-MKLNEDQKTVAAMDVLVpKIGEVI 511
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 327 SGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDP 396
Cdd:PTZ00425 512 GGSQREDNLERLDKMIKEKKLNMESYWWYRQLRKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFPRYP 581
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
95-393 |
1.29e-22 |
|
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: 97.27 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 95 VFRLQSGICHLFRETLINKGFVEIQTPKIISAAseGGANV--FTVSY--FKNNAYLAQSPQLYKQMCICADFEKVFSIGP 170
Cdd:cd00775 7 TFIVRSKIISYIRKFLDDRGFLEVETPMLQPIA--GGAAArpFITHHnaLDMDLYLRIAPELYLKRLIVGGFERVYEIGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 171 VFRAEDSNThRHLTEFVGLDIEMAfnYH-YHEVM---EEIADTMVQ-IFKGLQERFQTEIQTVNKqfpcePFKfleptlR 245
Cdd:cd00775 85 NFRNEGIDL-THNPEFTMIEFYEA--YAdYNDMMdltEDLFSGLVKkINGKTKIEYGGKELDFTP-----PFK------R 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 246 LEYCEALAmlREAGVEMGDEDDLSTPN-EKLLGHLVKEKYD---TDFYILDK------------------YPLAVRPFyT 303
Cdd:cd00775 151 VTMVDALK--EKTGIDFPELDLEQPEElAKLLAKLIKEKIEkprTLGKLLDKlfeefveptliqptfiidHPVEISPL-A 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 304 MPDPRNPKQSNSYDMFMRGEEILSGAQRIHDPQLLTER-----ALHHGIDLEKI---KAYIDSFRFGAPPHAGGGIGLER 375
Cdd:cd00775 228 KRHRSNPGLTERFELFICGKEIANAYTELNDPFDQRERfeeqaKQKEAGDDEAMmmdEDFVTALEYGMPPTGGLGIGIDR 307
|
330
....*....|....*...
gi 648216372 376 VTMLFLGLHNVRQTSMFP 393
Cdd:cd00775 308 LVMLLTDSNSIRDVILFP 325
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
135-394 |
1.23e-20 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 93.78 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 135 FTVSYFKNNAYLAQSPQLYKQMCICAdFEKVFSIGPVFRAEDSNTHRHLTEFVGLDIEMAFNyHYHEVMEEIADTMVQIF 214
Cdd:PLN02532 363 FSKDFFSRPTYLTVSGRLHLESYACA-LGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAFS-ELEDAMNCAEDYFKFLC 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 215 KGLQERFQTEIQTVNKQFPCEPFKFLE-----PTLRLEYCEALAMLREA---GVEMGDEDDLSTPNEKLlGHLVKEKYDT 286
Cdd:PLN02532 441 KWVLENCSEDMKFVSKRIDKTISTRLEaiissSLQRISYTEAVDLLKQAtdkKFETKPEWGIALTTEHL-SYLADEIYKK 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 287 DFYILDkYPLAVRPFYTMPDpRNPKQSNSYDMFM-RGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPP 365
Cdd:PLN02532 520 PVIIYN-YPKELKPFYVRLN-DDGKTVAAFDLVVpKVGTVITGSQNEERMDILNARIEELGLPREQYEWYLDLRRHGTVK 597
|
250 260
....*....|....*....|....*....
gi 648216372 366 HAGGGIGLERVTMLFLGLHNVRQTSMFPR 394
Cdd:PLN02532 598 HSGFSLGFELMVLFATGLPDVRDAIPFPR 626
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
75-393 |
1.17e-18 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 87.74 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 75 NQDTRLDNRVIDLRTSTSQA-VFRLQSGICHLFRETLINKGFVEIQTPKIISAAseGGANVFTVSYFKN----NAYLAQS 149
Cdd:PLN02502 207 DQETRYRQRYLDLIANPEVRdIFRTRAKIISYIRRFLDDRGFLEVETPMLNMIA--GGAAARPFVTHHNdlnmDLYLRIA 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 150 PQLYKQMCICADFEKVFSIGPVFRAEDSNThRHLTEFVGLDIEMAFNyHYHEVM---EEIADTMV-QIFKGLQERFQ-TE 224
Cdd:PLN02502 285 TELHLKRLVVGGFERVYEIGRQFRNEGIST-RHNPEFTTCEFYQAYA-DYNDMMeltEEMVSGMVkELTGSYKIKYHgIE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 225 IQTVnkqfpcEPFK------FLEPTLRLEYCEAL--AMLREAGVEMGDEDDLSTPN--------EKLLGHLVKEKYDTDF 288
Cdd:PLN02502 363 IDFT------PPFRrismisLVEEATGIDFPADLksDEANAYLIAACEKFDVKCPPpqttgrllNELFEEFLEETLVQPT 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 289 YILDkYPLAVRPFyTMPDPRNPKQSNSYDMFMRGEEILSGAQRIHDP----QLLTERALHHGIDLEKIKAYIDSF----R 360
Cdd:PLN02502 437 FVLD-HPVEMSPL-AKPHRSKPGLTERFELFINGRELANAFSELTDPvdqrERFEEQVKQHNAGDDEAMALDEDFctalE 514
|
330 340 350
....*....|....*....|....*....|...
gi 648216372 361 FGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 393
Cdd:PLN02502 515 YGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFP 547
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
75-393 |
1.52e-18 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 87.37 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 75 NQDTRLDNRVIDLRTS-TSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAAseGGANVFTVSYFKN----NAYLAQS 149
Cdd:PTZ00417 231 DTEIRYRQRYLDLMINeSTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLVA--GGANARPFITHHNdldlDLYLRIA 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 150 PQLYKQMCICADFEKVFSIGPVFRAED-SNTHRhlTEFVGLDIEMAFNyHYHEVMEEIADTMVQIFKGLqerFQTEIQTV 228
Cdd:PTZ00417 309 TELPLKMLIVGGIDKVYEIGKVFRNEGiDNTHN--PEFTSCEFYWAYA-DFYDLIKWSEDFFSQLVMHL---FGTYKILY 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 229 NKQFP-CEPFK--FLEPTLRLEYCEALAMLREAGVE--------------MGDEDDLSTPN--------EKLLGHLVKEK 283
Cdd:PTZ00417 383 NKDGPeKDPIEidFTPPYPKVSIVEELEKLTNTKLEqpfdspetinkminLIKENKIEMPNpptaakllDQLASHFIENK 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 284 Y-DTDFYILDkYPLAVRPFYTMPDPRnPKQSNSYDMFMRGEEILSGAQRIHDPQLLTERALHHGIDLEKIKA-------- 354
Cdd:PTZ00417 463 YpNKPFFIIE-HPQIMSPLAKYHRSK-PGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAeafqfdaa 540
|
330 340 350
....*....|....*....|....*....|....*....
gi 648216372 355 YIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 393
Cdd:PTZ00417 541 FCTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFP 579
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
75-393 |
1.05e-16 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 82.32 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 75 NQDTRLDNRVIDLRTST-SQAVFRLQSGICHLFRETLINKGFVEIQTPkiISAASEGGANV--FTVSYfknNAY-----L 146
Cdd:PRK02983 748 DPEARVRQRYLDLAVNPeARDLLRARSAVVRAVRETLVARGFLEVETP--ILQQVHGGANArpFVTHI---NAYdmdlyL 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 147 AQSPQLY-KQMCIcADFEKVFSIGPVFRAE--------------------DSNTHRHLTEfvGLDIEMAFNYH------- 198
Cdd:PRK02983 823 RIAPELYlKRLCV-GGVERVFELGRNFRNEgvdathnpeftlleayqahaDYDTMRDLTR--ELIQNAAQAAHgapvvmr 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 199 -YHEVMEEIAD-----TMVQIFKGLQERFQTEIQtvnkqfPCEPFkflePTLRlEYCEAlamlreAGVEMGDEDDLSTPN 272
Cdd:PRK02983 900 pDGDGVLEPVDisgpwPVVTVHDAVSEALGEEID------PDTPL----AELR-KLCDA------AGIPYRTDWDAGAVV 962
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 273 EKLLGHLVkEKYDTD--FYIldKYPLAVRPFyTMPDPRNPKQSNSYDMFMRGEEILSGAQRIHDP----QLLTERAL-HH 345
Cdd:PRK02983 963 LELYEHLV-EDRTTFptFYT--DFPTSVSPL-TRPHRSDPGLAERWDLVAWGVELGTAYSELTDPveqrRRLTEQSLlAA 1038
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 648216372 346 GIDLEKI---KAYIDSFRFGAPPHAGGGIGLERVTMLFLGLhNVRQTSMFP 393
Cdd:PRK02983 1039 GGDPEAMeldEDFLQALEYAMPPTGGLGMGVDRLVMLLTGR-SIRETLPFP 1088
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
75-393 |
6.79e-15 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 75.90 E-value: 6.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 75 NQDTRLDNRVIDLRTS-TSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAAseGGANV--FTVSYfknNA-----YL 146
Cdd:PRK00484 150 DVETRYRQRYVDLIVNpESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIA--GGAAArpFITHH---NAldidlYL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 147 AQSPQLYKQMCICADFEKVFSIGPVFRAEDSNThRHLTEFVGLDIEMAfnYH-YHEVM---EE-IADTMVQIFKGLQERF 221
Cdd:PRK00484 225 RIAPELYLKRLIVGGFERVYEIGRNFRNEGIDT-RHNPEFTMLEFYQA--YAdYNDMMdltEElIRHLAQAVLGTTKVTY 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 222 Q-TEIqTVNKQFPCEPFK----------FLEPTLRleycEALAMLREAGVEMGDEDDLSTPNEKLLGHLVKEKYDTDFYI 290
Cdd:PRK00484 302 QgTEI-DFGPPFKRLTMVdaikeytgvdFDDMTDE----EARALAKELGIEVEKSWGLGKLINELFEEFVEPKLIQPTFI 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 291 LDkYPLAVRPFyTMPDPRNPKQSNSYDMFMRGEEILSG----------AQRIHDpQLLtERAL----HHGIDLEkikaYI 356
Cdd:PRK00484 377 TD-YPVEISPL-AKRHREDPGLTERFELFIGGREIANAfselndpidqRERFEA-QVE-AKEAgddeAMFMDED----FL 448
|
330 340 350
....*....|....*....|....*....|....*..
gi 648216372 357 DSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 393
Cdd:PRK00484 449 RALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
106-208 |
2.59e-09 |
|
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: 56.74 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 106 FRETLINKGFVEIQTPKIISAASEGGAN------VFTVSYFKNNAYLAQSPQLYKQM----CICADFEKVFSIGPVFRAE 175
Cdd:cd00768 9 LRRFMAELGFQEVETPIVEREPLLEKAGhepkdlLPVGAENEEDLYLRPTLEPGLVRlfvsHIRKLPLRLAEIGPAFRNE 88
|
90 100 110
....*....|....*....|....*....|....*....
gi 648216372 176 DSNTH-RHLTEFVGLDIEMAF-----NYHYHEVMEEIAD 208
Cdd:cd00768 89 GGRRGlRRVREFTQLEGEVFGedgeeASEFEELIELTEE 127
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
3-88 |
5.77e-08 |
|
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: 51.37 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216372 3 KFAANINKESIVDVEGVVRK-----VNQKIGSctqQDVELHVQKIYVISLAEPrLPLQLDDAVRpeaegeeegratVNQD 77
Cdd:cd04317 57 ELAEKLRNESVIQVTGKVRArpegtVNPKLPT---GEIEVVASELEVLNKAKT-LPFEIDDDVN------------VSEE 120
|
90
....*....|.
gi 648216372 78 TRLDNRVIDLR 88
Cdd:cd04317 121 LRLKYRYLDLR 131
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
1-46 |
2.65e-07 |
|
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: 47.95 E-value: 2.65e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 648216372 1 MVKFAANINKESIVDVEGVVRKVnqKIGSCTQQDVELHVQKIYVIS 46
Cdd:cd04100 41 FFEEAEKLRTESVVGVTGTVVKR--PEGNLATGEIELQAEELEVLS 84
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
1-54 |
3.79e-03 |
|
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: 36.91 E-value: 3.79e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 648216372 1 MVKFAANINKESIVDVEGVVRKVNQKIGsctqqDVELHVQKIYVISLAEPRLPL 54
Cdd:cd04316 55 LFKTVRKLSRESVISVTGTVKAEPKAPN-----GVEIIPEEIEVLSEAKTPLPL 103
|
|
| |
