|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
2-532 |
0e+00 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 1032.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 2 VGSEVLEECGEKISKKESKKRAAKLEKLLRkqeREEATSSSLSLEEEDESCSSNYGDVTTNELQSAVEGKELTDVSNLVE 81
Cdd:PLN02850 1 SSQEAVEESGEKISKKAAKKAAAKAEKLRR---EATAKAAAASLEDEDDPLASNYGDVPLEELQSKVTGREWTDVSDLGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 82 EIVGSEVSIRGRLHKNRLVGTKLFVILRESGFTVQCVVEETR--VGANMIKFVKQLSRESVVELIGVVSHPKKPLTGTTQ 159
Cdd:PLN02850 78 ELAGSEVLIRGRVHTIRGKGKSAFLVLRQSGFTVQCVVFVSEvtVSKGMVKYAKQLSRESVVDVEGVVSVPKKPVKGTTQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 160 QVEIHVRKMYCLSRSLPNLPLVVEDAARSESDIEKSGKDGKQAARVLQDTRLNNRVLDIRTPANQAIFRIQCQVQIAFRE 239
Cdd:PLN02850 158 QVEIQVRKIYCVSKALATLPFNVEDAARSESEIEKALQTGEQLVRVGQDTRLNNRVLDLRTPANQAIFRIQSQVCNLFRE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 240 YLQSKGFLEIHTPKLIAGSSEGGSAVFRLDYKGQPACLAQSPQLHKQMAICGDMRRVFEVGPVFRAEDSFTHRHLCEFVG 319
Cdd:PLN02850 238 FLLSKGFVEIHTPKLIAGASEGGSAVFRLDYKGQPACLAQSPQLHKQMAICGDFRRVFEIGPVFRAEDSFTHRHLCEFTG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 320 LDVEMEIRMHYSEIMDLVGELFPFIFTKIEERCPKELESVRKQYPFQSLKFLPQTLRLTFAEGIQMLKEAGEEVDPLGDL 399
Cdd:PLN02850 318 LDLEMEIKEHYSEVLDVVDELFVAIFDGLNERCKKELEAIREQYPFEPLKYLPKTLRLTFAEGIQMLKEAGVEVDPLGDL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 400 NTESERKLGQLVLEKYKTEFYMLHRYPSAVRPFYTMPYENDSNYSNSFDVFIRGEEIMSGAQRIHDPELLEKRARECGID 479
Cdd:PLN02850 398 NTESERKLGQLVKEKYGTDFYILHRYPLAVRPFYTMPCPDDPKYSNSFDVFIRGEEIISGAQRVHDPELLEKRAEECGID 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 22328958 480 VKTISTYIDAFRYGAPPHGGFGVGLERVVMLLCALNNIRKTSLFPRDSQRLTP 532
Cdd:PLN02850 478 VKTISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPRDPQRLAP 530
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
23-532 |
1.58e-167 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 485.65 E-value: 1.58e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 23 AAKLEKLLRKQEREEATSSSLSLEE-----EDESCSSNYGDV--TTNELQSAVEG-KELTDVSNLV-EEIVGSEVSIRGR 93
Cdd:PTZ00401 7 DAGAPAVEKKQSDKEARKAARLAEEkaraaEKAALVEKYKDVfgAAPMVQSTTYKsRTFIPVAVLSkPELVDKTVLIRAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 94 LHKNRLVGTKLFVILRESGFTVQCVVE-ETRVGANMIKFVKQLSRESVVELIGVVSHPKKPLTGTTQQ-VEIHVRKMYCL 171
Cdd:PTZ00401 87 VSTTRKKGKMAFMVLRDGSDSVQAMAAvEGDVPKEMIDFIGQIPTESIVDVEATVCKVEQPITSTSHSdIELKVKKIHTV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 172 SRSLPNLPLVVEDAARSESDieksgkdgkQAARVLQDTRLNNRVLDIRTPANQAIFRIQCQVQIAFREYLQSKGFLEIHT 251
Cdd:PTZ00401 167 TESLRTLPFTLEDASRKESD---------EGAKVNFDTRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLIDSDFCEIHS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 252 PKLIAGSSEGGSAVFRLDYKGQPACLAQSPQLHKQMAICGDMRRVFEVGPVFRAEDSFTHRHLCEFVGLDVEMEIRMHYS 331
Cdd:PTZ00401 238 PKIINAPSEGGANVFKLEYFNRFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNTHRHLTEFVGLDVEMRINEHYY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 332 EIMDLVGELFPFIFTKIEERCpKELESVRKQYPFQSL--KFLPQT------------------------------LRLTF 379
Cdd:PTZ00401 318 EVLDLAESLFNYIFERLATHT-KELKAVCQQYPFEPLvwKLTPERmkelgvgvisegveptdkyqarvhnmdsrmLRINY 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 380 AEGIQMLKEAGEE-VDPLGDLNTESERKLGQLVLEKYKTEFYMLHRYPSAVRPFYTMPYENDSNYSNSFDVFIRGEEIMS 458
Cdd:PTZ00401 397 MHCIELLNTVLEEkMAPTDDINTTNEKLLGKLVKERYGTDFFISDRFPSSARPFYTMECKDDERFTNSYDMFIRGEEISS 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22328958 459 GAQRIHDPELLEKRARECGIDVKTISTYIDAFRYGAPPHGGFGVGLERVVMLLCALNNIRKTSLFPRDSQRLTP 532
Cdd:PTZ00401 477 GAQRIHDPDLLLARAKMLNVDLTPIKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFPRDPQRTTP 550
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
76-532 |
5.40e-159 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 459.66 E-value: 5.40e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 76 VSNLVEEIVGSEVSIRGRLHKNRLVGTKLFVILRE-SGFtVQCVVEETRVgANMIKFVKQLSRESVVELIGVVSHPKKPL 154
Cdd:PRK05159 7 TSELTPELDGEEVTLAGWVHEIRDLGGIAFLILRDrSGI-IQVVVKKKVD-EELFETIKKLKRESVVSVTGTVKANPKAP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 155 TGttqqVEIHVRKMYCLSRSLPNLPLvvedaarsesDIEKSGKDgkqaarVLqDTRLNNRVLDIRTPANQAIFRIQCQVQ 234
Cdd:PRK05159 85 GG----VEVIPEEIEVLNKAEEPLPL----------DISGKVLA------EL-DTRLDNRFLDLRRPRVRAIFKIRSEVL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 235 IAFREYLQSKGFLEIHTPKLIAGSSEGGSAVFRLDYKGQPACLAQSPQLHKQMAICGDMRRVFEVGPVFRAEDSFTHRHL 314
Cdd:PRK05159 144 RAFREFLYENGFTEIFTPKIVASGTEGGAELFPIDYFEKEAYLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSRHL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 315 CEFVGLDVEME-IRMHYsEIMDLVGELFPFIFTKIEERCPKELESVRKQYPFQSLKFLpqtlRLTFAEGIQMLKEAGEEV 393
Cdd:PRK05159 224 NEYTSIDVEMGfIDDHE-DVMDLLENLLRYMYEDVAENCEKELELLGIELPVPETPIP----RITYDEAIEILKSKGNEI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 394 DPLGDLNTESERKLGQLVLEKYKTEFYMLHRYPSAVRPFYTMPYENDSNYSNSFDVFIRGEEIMSGAQRIHDPELLEKRA 473
Cdd:PRK05159 299 SWGDDLDTEGERLLGEYVKEEYGSDFYFITDYPSEKRPFYTMPDEDDPEISKSFDLLFRGLEITSGGQRIHRYDMLVESI 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 22328958 474 RECGIDVKTISTYIDAFRYGAPPHGGFGVGLERVVMLLCALNNIRKTSLFPRDSQRLTP 532
Cdd:PRK05159 379 KEKGLNPESFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFPRDRHRLTP 437
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
207-528 |
1.19e-158 |
|
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: 454.33 E-value: 1.19e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 207 QDTRLNNRVLDIRTPANQAIFRIQCQVQIAFREYLQSKGFLEIHTPKLIAGSSEGGSAVFRLDYKGQPACLAQSPQLHKQ 286
Cdd:cd00776 4 LETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQLYKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 287 MAICGdMRRVFEVGPVFRAEDSFTHRHLCEFVGLDVEMEIRMHYSEIMDLVGELFPFIFTKIEERCPKELESVrKQYPFQ 366
Cdd:cd00776 84 MLIAA-LERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEDYNEVMDLIEELIKYIFKRVLERCAKELELV-NQLNRE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 367 SLKFLPQTLRLTFAEGIQMLKEAG--EEVDPLGDLNTESERKLGqlvlEKYKTEFYMLHRYPSAVRPFYTMPYENDSNYS 444
Cdd:cd00776 162 LLKPLEPFPRITYDEAIELLREKGveEEVKWGEDLSTEHERLLG----EIVKGDPVFVTDYPKEIKPFYMKPDDDNPETV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 445 NSFDVFIRG-EEIMSGAQRIHDPELLEKRARECGIDVKTISTYIDAFRYGAPPHGGFGVGLERVVMLLCALNNIRKTSLF 523
Cdd:cd00776 238 ESFDLLMPGvGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILF 317
|
....*
gi 22328958 524 PRDSQ 528
Cdd:cd00776 318 PRDPK 322
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
74-532 |
1.19e-154 |
|
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: 448.35 E-value: 1.19e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 74 TDVSNLVEEIVGSEVSIRGRLHKNRLVGTKLFVILRESGFTVQCVVEETRVGAnmIKFVKQLSRESVVELIG-VVSHPKK 152
Cdd:COG0017 3 TYIKDLLPEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKLEN--FEEAKKLTTESSVEVTGtVVESPRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 153 PltgttQQVEIHVRKMYCLSRSLPNLPLVVedaarSESDIEksgkdgkqaarvlqdTRLNNRVLDIRTPANQAIFRIQCQ 232
Cdd:COG0017 81 P-----QGVELQAEEIEVLGEADEPYPLQP-----KRHSLE---------------FLLDNRHLRLRTNRFGAIFRIRSE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 233 VQIAFREYLQSKGFLEIHTPKLIAGSSEGGSAVFRLDYKGQPACLAQSPQLHKQMAICGdMRRVFEVGPVFRAEDSFTHR 312
Cdd:COG0017 136 LARAIREFFQERGFVEVHTPIITASATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMA-LEKVYTFGPTFRAEKSNTRR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 313 HLCEFVGLDVEMEIrMHYSEIMDLVGELFPFIFTKIEERCPKELESVRKQypFQSLKFLPQT--LRLTFAEGIQMLKEAG 390
Cdd:COG0017 215 HLAEFWMIEPEMAF-ADLEDVMDLAEEMLKYIIKYVLENCPEELEFLGRD--VERLEKVPESpfPRITYTEAIEILKKSG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 391 EEVDPLGDLNTESERKLGqlvlEKYKTEFYMLHRYPSAVRPFYTMPYENDSNYSNSFDVFIRG-EEIMSGAQRIHDPELL 469
Cdd:COG0017 292 EKVEWGDDLGTEHERYLG----EEFFKKPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAPGiGEIIGGSQREHRYDVL 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22328958 470 EKRARECGIDVKTISTYIDAFRYGAPPHGGFGVGLERVVMLLCALNNIRKTSLFPRDSQRLTP 532
Cdd:COG0017 368 VERIKEKGLDPEDYEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
78-532 |
2.59e-140 |
|
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: 411.91 E-value: 2.59e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 78 NLVEEIVGSEVSIRGRLHKNRLVGTKLFVILRESGFTVQCVVEETRVGANMIKFVKQLSRESVVELIGVVSHPKKpltgT 157
Cdd:TIGR00458 5 DIKPEMDGQEVTFMGWVHEIRDLGGLIFVLLRDREGLIQITAPAKKVSKNLFKWAKKLNLESVVAVRGIVKIKEK----A 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 158 TQQVEIHVRKMYCLSRSLPNLPLVVEDAARSESDieksgkdgkqaarvlqdTRLNNRVLDIRTPANQAIFRIQCQVQIAF 237
Cdd:TIGR00458 81 PGGFEIIPTKIEVINEAKEPLPLDPTEKVPAELD-----------------TRLDYRFLDLRRPTVQAIFRIRSGVLESV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 238 REYLQSKGFLEIHTPKLIAGSSEGGSAVFRLDYKGQPACLAQSPQLHKQMAICGDMRRVFEVGPVFRAEDSFTHRHLCEF 317
Cdd:TIGR00458 144 REFLAEEGFIEVHTPKLVASATEGGTELFPITYFEREAFLGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNTHRHLNEA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 318 VGLDVEMEIRMHySEIMDLVGELFPFIFTKIEERCPKELESVRKQYPFQSLKFlpqtLRLTFAEGIQMLKEAGEEVDPLG 397
Cdd:TIGR00458 224 TSIDIEMAFEDH-HDVMDILEELVVRVFEDVPERCAHQLETLEFKLEKPEGKF----VRLTYDEAIEMANAKGVEIGWGE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 398 DLNTESERKLGqlvlEKYKTEFYMLHrYPSAVRPFYTMPYENDSNYSNSFDVFIRGEEIMSGAQRIHDPELLEKRARECG 477
Cdd:TIGR00458 299 DLSTEAEKALG----EEMDGLYFITD-WPTEIRPFYTMPDEDNPEISKSFDLMYRDLEISSGAQRIHLHDLLVERIKAKG 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 22328958 478 IDVKTISTYIDAFRYGAPPHGGFGVGLERVVMLLCALNNIRKTSLFPRDSQRLTP 532
Cdd:TIGR00458 374 LNPEGFKDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFPRDRKRLTP 428
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
207-527 |
3.03e-97 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 297.55 E-value: 3.03e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 207 QDTRLNNRVLDIRTPANQAIFRIQCQVQIAFREYLQSKGFLEIHTPKLIAGSSEGGSAVFRL--DYKGQPACLAQSPQLH 284
Cdd:pfam00152 2 EETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVpsRALGKFYALPQSPQLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 285 KQMAICGDMRRVFEVGPVFRAEDSFTHRHLcEFVGLDVEMEIrMHYSEIMDLVGELFPFIFTKIEErCPKELESvrkqyp 364
Cdd:pfam00152 82 KQLLMVAGFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSF-VDYEDVMDLTEELIKEIFKEVEG-IAKELEG------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 365 FQSLKFLPQTLRLTFAEGIQMLKEAGEEvDPLGDLNTESERKLGQLVLEKYKTEFYMLHRYPSAVRPFYTMPYENDSNYS 444
Cdd:pfam00152 153 GTLLDLKKPFPRITYAEAIEKLNGKDVE-ELGYGSDKPDLRFLLELVIDKNKFNPLWVTDFPAEHHPFTMPKDEDDPALA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 445 NSFDVFIRGEEIMSGAQRIHDPELLEKRARECGIDVKTIST----YIDAFRYGAPPHGGFGVGLERVVMLLCALNNIRKT 520
Cdd:pfam00152 232 EAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDPEEAEEkfgfYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREV 311
|
....*..
gi 22328958 521 SLFPRDS 527
Cdd:pfam00152 312 IAFPKTR 318
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
79-532 |
2.16e-74 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 242.71 E-value: 2.16e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 79 LVEEIVGSEVSIRGRLHKNRLVGTKLFVILRESGFTVQCVVEETRVGANMiKFVKQLSRESVVELIG-VVSHPKKPltgt 157
Cdd:PRK03932 10 LKGKYVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDNGEEYF-EEIKKLTTGSSVIVTGtVVESPRAG---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 158 tQQVEIHVRKMYCLSRSLPNLPLvvedaarsesdieksgkdgkQAARVLQDTRLNNRVLDIRTPANQAIFRIQCQVQIAF 237
Cdd:PRK03932 85 -QGYELQATKIEVIGEDPEDYPI--------------------QKKRHSIEFLREIAHLRPRTNKFGAVMRIRNTLAQAI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 238 REYLQSKGFLEIHTPKLIAGSSEGGSAVFRL---------DYKGQPACLAQSPQLHKQMAICGdMRRVFEVGPVFRAEDS 308
Cdd:PRK03932 144 HEFFNENGFVWVDTPIITASDCEGAGELFRVttldldfskDFFGKEAYLTVSGQLYAEAYAMA-LGKVYTFGPTFRAENS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 309 FTHRHLCEFVGLDVEMEIrMHYSEIMDLVGELFPFIFTKIEERCPKELESVRKQYPFQSLKFLPQTL-----RLTFAEGI 383
Cdd:PRK03932 223 NTRRHLAEFWMIEPEMAF-ADLEDNMDLAEEMLKYVVKYVLENCPDDLEFLNRRVDKGDIERLENFIespfpRITYTEAI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 384 QMLKEAGEEVDPL---G-DLNTESERklgQLVLEKYKTEFyMLHRYPSAVRPFYtMPYENDSNYSNSFDVFIRG-EEIMS 458
Cdd:PRK03932 302 EILQKSGKKFEFPvewGdDLGSEHER---YLAEEHFKKPV-FVTNYPKDIKAFY-MRLNPDGKTVAAMDLLAPGiGEIIG 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22328958 459 GAQRIHDPELLEKRARECGIDVKTISTYIDAFRYGAPPHGGFGVGLERVVMLLCALNNIRKTSLFPRDSQRLTP 532
Cdd:PRK03932 377 GSQREERLDVLEARIKELGLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
75-532 |
5.74e-71 |
|
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: 233.81 E-value: 5.74e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 75 DVSNLVEEIVGSEVSIRGRLHKNRLVGTKLFVILRE--SGFTVQCVVEETrVGANMIKFVKQLSRESVVELIG-VVSHPK 151
Cdd:TIGR00457 6 DLLQQVYKFVGDEVTVSGWVRTKRSSKKIIFLELNDgsSLGPIQAVINGE-DNPYLFQLLKSLTTGSSVSVTGkVVESPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 152 KPltgttQQVEIHVRKMYCLSRSLP-NLPLvvedaarsesdieksgkdgkQAARVLQDTRLNNRVLDIRTPANQAIFRIQ 230
Cdd:TIGR00457 85 KG-----QPVELQVKKIEVVGEAEPdDYPL--------------------QKKEHSLEFLRDIAHLRLRTNTLGAVMRVR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 231 CQVQIAFREYLQSKGFLEIHTPKLIAGSSEGGSAVFRL---------DYKGQPACLAQSPQLHKQMAICGdMRRVFEVGP 301
Cdd:TIGR00457 140 NALSQAIHRYFQENGFTWVSPPILTSNDCEGAGELFRVstgnidfsqDFFGKEAYLTVSGQLYLETYALA-LSKVYTFGP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 302 VFRAEDSFTHRHLCEFVGLDVEMEIrMHYSEIMDLVGELFPFIFTKIEERCPKELESVRKQYPFQSLKFLPQTL-----R 376
Cdd:TIGR00457 219 TFRAEKSNTSRHLSEFWMIEPEMAF-ANLNDLLQLAETLIKYIIKAVLENCSQELKFLEKNFDKDLIKRLENIInnkfaR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 377 LTFAEGIQMLKEAGE--EVDPL-G-DLNTESERKLGqlvlEKYKTEFYMLHRYPSAVRPFYtMPYENDSNYSNSFDVFIR 452
Cdd:TIGR00457 298 ITYTDAIEILKESDKnfEYEDFwGdDLQTEHERFLA----EEYFKPPVFVTNYPKDIKAFY-MKLNDDGKTVAAMDLLAP 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 453 G-EEIMSGAQRIHDPELLEKRARECGIDVKTISTYIDAFRYGAPPHGGFGVGLERVVMLLCALNNIRKTSLFPRDSQRLT 531
Cdd:TIGR00457 373 GiGEIIGGSEREDDLDKLENRMKEMGLDTDALNWYLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGNIN 452
|
.
gi 22328958 532 P 532
Cdd:TIGR00457 453 F 453
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
227-526 |
5.14e-54 |
|
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: 183.45 E-value: 5.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 227 FRIQCQVQIAFREYLQSKGFLEIHTPKLIAGSSEGGSAVFRLDY--KGQPACLAQSPQLHKQMAICGDMRRVFEVGPVFR 304
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYnaLGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 305 AEDSfTHRHLCEFVGLDVEMEIrMHYSEIMDLVGELFPFIFTKIeercpkeLESVRKQYPFQSLKFLPQTLRLTFAEGIq 384
Cdd:cd00669 81 NEDL-RARHQPEFTMMDLEMAF-ADYEDVIELTERLVRHLAREV-------LGVTAVTYGFELEDFGLPFPRLTYREAL- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 385 mlkeageevdplgdlnteseRKLGQlvlekykteFYMLHRYPSAVRPFYTMPYENDSNYSNSFDVFIRGEEIMSGAQRIH 464
Cdd:cd00669 151 --------------------ERYGQ---------PLFLTDYPAEMHSPLASPHDVNPEIADAFDLFINGVEVGNGSSRLH 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22328958 465 DPELLEKRARECGID----VKTISTYIDAFRYGAPPHGGFGVGLERVVMLLCALNNIRKTSLFPRD 526
Cdd:cd00669 202 DPDIQAEVFQEQGINkeagMEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKM 267
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
81-524 |
4.28e-48 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 175.64 E-value: 4.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 81 EEIVGSEVSIRGRLHKNRLVGTKLFVILRE-SGfTVQCVVEETrvgANMIKFVKQLSRESVVELIGVVSH-------PKK 152
Cdd:PRK00476 13 ESHVGQTVTLCGWVHRRRDHGGLIFIDLRDrEG-IVQVVFDPD---AEAFEVAESLRSEYVIQVTGTVRArpegtvnPNL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 153 PlTGttqQVEIHVRKMYCLSRSLPnLPLVVEDaarsESDieksgkdgkqaarVLQDTRLNNRVLDIRTPANQAIFRIQCQ 232
Cdd:PRK00476 89 P-TG---EIEVLASELEVLNKSKT-LPFPIDD----EED-------------VSEELRLKYRYLDLRRPEMQKNLKLRSK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 233 VQIAFREYLQSKGFLEIHTPKLIAGSSEGgsAvfRlDY-------KGQPACLAQSPQLHKQMAICGDMRRVFEVGPVFRA 305
Cdd:PRK00476 147 VTSAIRNFLDDNGFLEIETPILTKSTPEG--A--R-DYlvpsrvhPGKFYALPQSPQLFKQLLMVAGFDRYYQIARCFRD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 306 EDSFTHRHLcEFVGLDVEM------EI-------------------------RMHYSEIM--------DL--------VG 338
Cdd:PRK00476 222 EDLRADRQP-EFTQIDIEMsfvtqeDVmalmeglirhvfkevlgvdlptpfpRMTYAEAMrrygsdkpDLrfglelvdVT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 339 ELF---PF-IFTKIEE--------RCP-----------KELESVRKQYPFQSL---------------KFLPQtlrltfa 380
Cdd:PRK00476 301 DLFkdsGFkVFAGAANdggrvkaiRVPggaaqlsrkqiDELTEFAKIYGAKGLayikvnedglkgpiaKFLSE------- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 381 EGIQMLKE-------------AGEE---VDPLGDLNTESERKLGQLVLEKYK----TEFYMLH------RYPSAVRPFyT 434
Cdd:PRK00476 374 EELAALLErtgakdgdliffgADKAkvvNDALGALRLKLGKELGLIDEDKFAflwvVDFPMFEydeeegRWVAAHHPF-T 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 435 MPYENDSNY----------SNSFDVFIRGEEIMSGAQRIHDPELLEKRARECGIDVKTIST----YIDAFRYGAPPHGGF 500
Cdd:PRK00476 453 MPKDEDLDElettdpgkarAYAYDLVLNGYELGGGSIRIHRPEIQEKVFEILGISEEEAEEkfgfLLDALKYGAPPHGGI 532
|
570 580
....*....|....*....|....
gi 22328958 501 GVGLERVVMLLCALNNIRKTSLFP 524
Cdd:PRK00476 533 AFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
197-525 |
1.38e-47 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 168.27 E-value: 1.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 197 KDGKQAARVLQDTRLNNRVLdIRTPANQAIFRIQCQVQIAFREYLQSKGFLEIHTP-------KLIAGSSEGGSAVFRLD 269
Cdd:PRK06462 1 KDLERYPKEYEEFLRMSWKH-ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPiispstdPLMGLGSDLPVKQISID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 270 YKGQPACLAQSPQLHKQMAIcGDMRRVFEVGPVFRAE--DSFTHRHLCEFVGLDVEMEiRMHYSEIMDLVGELFPFIFTK 347
Cdd:PRK06462 80 FYGVEYYLADSMILHKQLAL-RMLGKIFYLSPNFRLEpvDKDTGRHLYEFTQLDIEIE-GADLDEVMDLIEDLIKYLVKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 348 IEERCPKELESVRKQYPFQSLKFLpqtlRLTFAEGIQMLKEAGEEVDPLGDLNTESERKLgqlvlEKYKTEFYMLHRYPS 427
Cdd:PRK06462 158 LLEEHEDELEFFGRDLPHLKRPFK----RITHKEAVEILNEEGCRGIDLEELGSEGEKSL-----SEHFEEPFWIIDIPK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 428 AVRPFYTMPYENDSNYSNSFDVFIR---GEeIMSGAQRIHDPELLEKRARECGIDVKTISTYIDAFRYGAPPHGGFGVGL 504
Cdd:PRK06462 229 GSREFYDREDPERPGVLRNYDLLLPegyGE-AVSGGEREYEYEEIVERIREHGVDPEKYKWYLEMAKEGPLPSAGFGIGV 307
|
330 340
....*....|....*....|.
gi 22328958 505 ERVVMLLCALNNIRKTSLFPR 525
Cdd:PRK06462 308 ERLTRYICGLRHIREVQPFPR 328
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
79-524 |
2.15e-43 |
|
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: 162.48 E-value: 2.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 79 LVEEIVGSEVSIRGRLHKNRLVGTKLFVILRE-SGFTvQCVVEETRvGANMIKFVKQLSRESVVELIGVVSH-------P 150
Cdd:COG0173 10 LRESDVGQEVTLSGWVHRRRDHGGLIFIDLRDrYGIT-QVVFDPDD-SAEAFEKAEKLRSEYVIAVTGKVRArpegtvnP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 151 KKPlTGttqQVEIHVRKMYCLSRSLPnLPLVVEDaarsesDIEksgkdgkqaarVLQDTRLNNRVLDIRTPANQAIFRIQ 230
Cdd:COG0173 88 KLP-TG---EIEVLASELEILNKAKT-PPFQIDD------DTD-----------VSEELRLKYRYLDLRRPEMQKNLILR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 231 CQVQIAFREYLQSKGFLEIHTPKLIAGSSEGgsAvfRlDY-------KGQPACLAQSPQLHKQMAICGDMRRVFEVGPVF 303
Cdd:COG0173 146 HKVTKAIRNYLDENGFLEIETPILTKSTPEG--A--R-DYlvpsrvhPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 304 RAEDS-------FTH---------------------RHLC-EFVGLDVEMEI-RMHYSEIM--------DL--------V 337
Cdd:COG0173 221 RDEDLradrqpeFTQldiemsfvdqedvfelmegliRHLFkEVLGVELPTPFpRMTYAEAMerygsdkpDLrfglelvdV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 338 GELF---PF-IFTKIEE--------RCPK----------ELESVRKQY-------------PFQS--LKFLPQtlrltfa 380
Cdd:COG0173 301 TDIFkdsGFkVFAGAAEnggrvkaiNVPGgaslsrkqidELTEFAKQYgakglayikvnedGLKSpiAKFLSE------- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 381 EGIQMLKEAGEEVDplGDL-------NTESERKLGQLVLE-----------KYK----TEFYML------HRYPSAVRPF 432
Cdd:COG0173 374 EELAAILERLGAKP--GDLiffvadkPKVVNKALGALRLKlgkelglidedEFAflwvVDFPLFeydeeeGRWVAMHHPF 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 433 yTMPYEND-----SN----YSNSFDVFIRGEEIMSGAQRIHDPELLEKRARECGIDVKTIST----YIDAFRYGAPPHGG 499
Cdd:COG0173 452 -TMPKDEDldlleTDpgkvRAKAYDLVLNGYELGGGSIRIHDPELQEKVFELLGISEEEAEEkfgfLLEAFKYGAPPHGG 530
|
570 580
....*....|....*....|....*
gi 22328958 500 FGVGLERVVMLLCALNNIRKTSLFP 524
Cdd:COG0173 531 IAFGLDRLVMLLAGEDSIRDVIAFP 555
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
227-528 |
7.32e-42 |
|
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: 151.19 E-value: 7.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 227 FRIQCQVQIAFREYLQSKGFLEIHTPKLIAgSSEGGSAVF----RLdYKGQPACLAQSPQLHKQMAICGDMRRVFEVGPV 302
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTK-STPEGARDFlvpsRL-HPGKFYALPQSPQLFKQLLMVSGFDRYFQIARC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 303 FRAEDSFTHRHlCEFVGLDVEMEIrMHYSEIMDLVGELFPFIFtkieercpKELESVRKQYPFQslkflpqtlRLTFAEG 382
Cdd:cd00777 79 FRDEDLRADRQ-PEFTQIDIEMSF-VDQEDIMSLIEGLLKYVF--------KEVLGVELTTPFP---------RMTYAEA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 383 IQmlkEAGEE----VD-PLGDLNTESERklgqlvlekyktefymlhrYPSAVRPFyTMPYENDSNY---------SNSFD 448
Cdd:cd00777 140 ME---RYGFKflwiVDfPLFEWDEEEGR-------------------LVSAHHPF-TAPKEEDLDLlekdpedarAQAYD 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 449 VFIRGEEIMSGAQRIHDPELLEKRARECGIDVKTIST----YIDAFRYGAPPHGGFGVGLERVVMLLCALNNIRKTSLFP 524
Cdd:cd00777 197 LVLNGVELGGGSIRIHDPDIQEKVFEILGLSEEEAEEkfgfLLEAFKYGAPPHGGIALGLDRLVMLLTGSESIRDVIAFP 276
|
....
gi 22328958 525 RDSQ 528
Cdd:cd00777 277 KTQN 280
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
87-184 |
1.24e-35 |
|
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: 128.45 E-value: 1.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 87 EVSIRGRLHKNRLVGTKL-FVILRESGFTVQCVVE--ETRVGANMIKFVKQLSRESVVELIGVVSHPKKPLTGTTQQ-VE 162
Cdd:cd04320 1 EVLIRARVHTSRAQGAKLaFLVLRQQGYTIQGVLAasAEGVSKQMVKWAGSLSKESIVDVEGTVKKPEEPIKSCTQQdVE 80
|
90 100
....*....|....*....|..
gi 22328958 163 IHVRKMYCLSRSLPNLPLVVED 184
Cdd:cd04320 81 LHIEKIYVVSEAAEPLPFQLED 102
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
84-525 |
6.33e-34 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 135.49 E-value: 6.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 84 VGSEVSIRGRLHKNRLVGTKLFVILRESGF--TVQCVVEETRVGANMIKFVKQLSRESVVeLIGVVSHPKkpltGTTQQV 161
Cdd:PLN02603 106 VGKTLNVMGWVRTLRAQSSVTFIEVNDGSClsNMQCVMTPDAEGYDQVESGLITTGASVL-VQGTVVSSQ----GGKQKV 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 162 EIHVRKMYCLSRSLPNLPlvvedaarsesdIEKsgkdgKQAARVLQDTRLNNRVldiRTPANQAIFRIQCQVQIAFREYL 241
Cdd:PLN02603 181 ELKVSKIVVVGKSDPSYP------------IQK-----KRVSREFLRTKAHLRP---RTNTFGAVARVRNALAYATHKFF 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 242 QSKGFLEIHTP-----------------KLIAGSSE-GGSAVFRL------------DYKGQPACLAQSPQLHKQMAICG 291
Cdd:PLN02603 241 QENGFVWVSSPiitasdcegageqfcvtTLIPNSAEnGGSLVDDIpktkdglidwsqDFFGKPAFLTVSGQLNGETYATA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 292 dMRRVFEVGPVFRAEDSFTHRHLCEF---------VGLDVEMEIRMHYSE-----IMDLVGELFPFIFTKIEERCPKELE 357
Cdd:PLN02603 321 -LSDVYTFGPTFRAENSNTSRHLAEFwmiepelafADLNDDMACATAYLQyvvkyILENCKEDMEFFNTWIEKGIIDRLS 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 358 SVRKQypfqslkflpQTLRLTFAEGIQMLKEAGEEVD-PLG---DLNTESERKLGQlvlEKYKTEFYMLHRYPSAVRPFY 433
Cdd:PLN02603 400 DVVEK----------NFVQLSYTDAIELLLKAKKKFEfPVKwglDLQSEHERYITE---EAFGGRPVIIRDYPKEIKAFY 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 434 tMPYENDSNYSNSFDVFI-RGEEIMSGAQRIHDPELLEKRARECGIDVKTISTYIDAFRYGAPPHGGFGVGLERVVMLLC 512
Cdd:PLN02603 467 -MRENDDGKTVAAMDMLVpRVGELIGGSQREERLEYLEARLDELKLNKESYWWYLDLRRYGSVPHAGFGLGFERLVQFAT 545
|
490
....*....|...
gi 22328958 513 ALNNIRKTSLFPR 525
Cdd:PLN02603 546 GIDNIRDAIPFPR 558
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
78-532 |
1.61e-30 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 126.25 E-value: 1.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 78 NLVEEIVGSEVSIRGRLHKNRLVGTKLFVILRESGFTVQCVVEETRVGANMIKFVKQLSRESVVELIGVVshpKKPLTGT 157
Cdd:PRK12820 11 HLSLDDTGREVCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFSPEAAPADVYELAASLRAEFCVALQGEV---QKRLEET 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 158 ------TQQVEIHVRKMYCLSRSLPnLPLVVEDAARSesdiekSGKDGKQAARVLQDTRLNNRVLDIRTPANQAIFRIQC 231
Cdd:PRK12820 88 enphieTGDIEVFVRELSILAASEA-LPFAISDKAMT------AGAGSAGADAVNEDLRLQYRYLDIRRPAMQDHLAKRH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 232 QVQIAFREYLQSKGFLEIHTPKLIAGSSEGGSavfrlDY----KGQPA---CLAQSPQLHKQMAICGDMRRVFEVGPVFR 304
Cdd:PRK12820 161 RIIKCARDFLDSRGFLEIETPILTKSTPEGAR-----DYlvpsRIHPKefyALPQSPQLFKQLLMIAGFERYFQLARCFR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 305 AEDSFTHRHlCEFVGLDVEMEI------------------------------RMHYSEIMDLVGE-----LFPFIFTKIE 349
Cdd:PRK12820 236 DEDLRPNRQ-PEFTQLDIEASFideefifelieeltarmfaiggialprpfpRMPYAEAMDTTGSdrpdlRFDLKFADAT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 350 ERCPKELESVRKQ------------YPFQSLKFLPQTLRLTFAEGIQ----------MLKEAGEEVDPLGDLNTESERK- 406
Cdd:PRK12820 315 DIFENTRYGIFKQilqrggrikginIKGQSEKLSKNVLQNEYAKEIApsfgakgmtwMRAEAGGLDSNIVQFFSADEKEa 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 407 ---------------------------LGQLVLE---------------KYKTEFYMLHR-----YPSAVRPFyTMPYEN 439
Cdd:PRK12820 395 lkrrfhaedgdviimiadascaivlsaLGQLRLHladrlglipegvfhpLWITDFPLFEAtddggVTSSHHPF-TAPDRE 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 440 D----------SNYSNSFDVFIRGEEIMSGAQRIHDPELLEKRARECGIDVKTIST----YIDAFRYGAPPHGGFGVGLE 505
Cdd:PRK12820 474 DfdpgdieellDLRSRAYDLVVNGEELGGGSIRINDKDIQLRIFAALGLSEEDIEDkfgfFLRAFDFAAPPHGGIALGLD 553
|
570 580
....*....|....*....|....*..
gi 22328958 506 RVVMLLCALNNIRKTSLFPRDSQRLTP 532
Cdd:PRK12820 554 RVVSMILQTPSIREVIAFPKNRSAACP 580
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
269-525 |
1.21e-29 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 122.80 E-value: 1.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 269 DYKGQPACLAQSPQLHKQMAICGdMRRVFEVGPVFRAEDSFTHRHLCEFVGLDVE-----MEIRMHYSE---------IM 334
Cdd:PLN02221 303 DFFGRQAFLTVSGQLQVETYACA-LSSVYTFGPTFRAENSHTSRHLAEFWMVEPEiafadLEDDMNCAEayvkymckwLL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 335 DLVGELFPFIFTKIEERCPKELESVRKQyPFQslkflpqtlRLTFAEGIQMLKEA---GEEVD---PLG-DLNTESERKL 407
Cdd:PLN02221 382 DKCFDDMELMAKNFDSGCIDRLRMVAST-PFG---------RITYTEAIELLEEAvakGKEFDnnvEWGiDLASEHERYL 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 408 GQLVLEKYktefYMLHRYPSAVRPFYtMPYENDSNYSNSFDVFI-RGEEIMSGAQRIHDPELLEKRARECGIDVKTISTY 486
Cdd:PLN02221 452 TEVLFQKP----LIVYNYPKGIKAFY-MRLNDDEKTVAAMDVLVpKVGELIGGSQREERYDVIKQRIEEMGLPIEPYEWY 526
|
250 260 270
....*....|....*....|....*....|....*....
gi 22328958 487 IDAFRYGAPPHGGFGVGLERVVMLLCALNNIRKTSLFPR 525
Cdd:PLN02221 527 LDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPR 565
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
84-528 |
8.33e-29 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 120.66 E-value: 8.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 84 VGSEVSIRGRLHKNRLVGTKLFVILRESGFTVQcVVEETRVGANMIKFVKQLSRESVVELIGVV-SHPKKPLTGT--TQQ 160
Cdd:PLN02903 71 VGSRVTLCGWVDLHRDMGGLTFLDVRDHTGIVQ-VVTLPDEFPEAHRTANRLRNEYVVAVEGTVrSRPQESPNKKmkTGS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 161 VEIHVRKMYCLSRSLPNLPLVVEDAARSESDIEksgkdgkqaarvlQDTRLNNRVLDIRTPANQAIFRIQCQVQIAFREY 240
Cdd:PLN02903 150 VEVVAESVDILNVVTKSLPFLVTTADEQKDSIK-------------EEVRLRYRVLDLRRPQMNANLRLRHRVVKLIRRY 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 241 LQSK-GFLEIHTPKLIAGSSEGGsavfrLDY----KGQPA---CLAQSPQLHKQMAICGDMRRVFEVGPVFRAEDSFTHR 312
Cdd:PLN02903 217 LEDVhGFVEIETPILSRSTPEGA-----RDYlvpsRVQPGtfyALPQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 313 HlCEFVGLDVEM---------------------EI----------RMHYSEIMDLVGELFPFIFTKIEErcpKELESVRK 361
Cdd:PLN02903 292 Q-PEFTQLDMELaftpledmlklnedlirqvfkEIkgvqlpnpfpRLTYAEAMSKYGSDKPDLRYGLEL---VDVSDVFA 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 362 QYPFQ------------------------SLKFLP------QTLR-----LTFA--------EGIQMLKEA--GEEVDPL 396
Cdd:PLN02903 368 ESSFKvfagalesggvvkaicvpdgkkisNNTALKkgdiynEAIKsgakgLAFLkvlddgelEGIKALVESlsPEQAEQL 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 397 --------GDL------NTESERK----LGQLVLEKYK------------TEFYML------HRYPSAVRPFyTMPYEND 440
Cdd:PLN02903 448 laacgagpGDLilfaagPTSSVNKtldrLRQFIAKTLDlidpsrhsilwvTDFPMFewnedeQRLEALHHPF-TAPNPED 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 441 S-NYSN----SFDVFIRGEEIMSGAQRIHDPELLEKRARECGIDVKTIST----YIDAFRYGAPPHGGFGVGLERVVMLL 511
Cdd:PLN02903 527 MgDLSSaralAYDMVYNGVEIGGGSLRIYRRDVQQKVLEAIGLSPEEAESkfgyLLEALDMGAPPHGGIAYGLDRLVMLL 606
|
570
....*....|....*..
gi 22328958 512 CALNNIRKTSLFPRDSQ 528
Cdd:PLN02903 607 AGAKSIRDVIAFPKTTT 623
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
58-524 |
1.55e-27 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 115.93 E-value: 1.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 58 DVTTNELQSAVEGKELTDVSNLveeivGSEVSIRGRLHKNRLVGTKLFVILRESGFTVQCVVEETRVGANMikFVKQLSR 137
Cdd:PRK12445 43 DHTSDQLHEEFDAKDNQELESL-----NIEVSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEGV--YNDQFKK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 138 ESVVELIGVVSHPKKPLTGttqQVEIHVRKMYCLSRSLPNLPlvveDAARSESDieksgkdgkqaarvlQDTRLNNRVLD 217
Cdd:PRK12445 116 WDLGDIIGARGTLFKTQTG---ELSIHCTELRLLTKALRPLP----DKFHGLQD---------------QEVRYRQRYLD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 218 -IRTPANQAIFRIQCQVQIAFREYLQSKGFLEIHTP--KLIAGSSEGGSAVFRLDYKGQPACLAQSPQLHKQMAICGDMR 294
Cdd:PRK12445 174 lIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPmmQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGFE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 295 RVFEVGPVFRAEdSFTHRHLCEFVgldvEMEIRMHYSEIMDLVgELFPFIFTKIEERCpkeLESVRKQYPFQSLKFLPQT 374
Cdd:PRK12445 254 RVFEINRNFRNE-GISVRHNPEFT----MMELYMAYADYHDLI-ELTESLFRTLAQEV---LGTTKVTYGEHVFDFGKPF 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 375 LRLTFAEGIQMLK-----------EAGEEVDPLGDLNTESERKLGQLVLEKYK--TEFYMLH-----RYPSAVRPfytMP 436
Cdd:PRK12445 325 EKLTMREAIKKYRpetdmadldnfDAAKALAESIGITVEKSWGLGRIVTEIFDevAEAHLIQptfitEYPAEVSP---LA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 437 YENDSN--YSNSFDVFIRGEEIMSGAQRIHDPELLEKR------ARECGIDVKTI--STYIDAFRYGAPPHGGFGVGLER 506
Cdd:PRK12445 402 RRNDVNpeITDRFEFFIGGREIGNGFSELNDAEDQAERfqeqvnAKAAGDDEAMFydEDYVTALEYGLPPTAGLGIGIDR 481
|
490
....*....|....*...
gi 22328958 507 VVMLLCALNNIRKTSLFP 524
Cdd:PRK12445 482 MIMLFTNSHTIRDVILFP 499
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
225-525 |
1.34e-26 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 113.58 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 225 AIFRIQCQVQIAFREYLQSKGFLEIHTPKLIAGSSEGGSAVFR------------------------------------- 267
Cdd:PTZ00425 213 SVIRIRNALAIATHLFFQSRGFLYIHTPLITTSDCEGGGEMFTvttllgedadyraiprvnkknkkgekredilntcnan 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 268 ----------------------LDYK----GQPACLAQSPQLHKQmAICGDMRRVFEVGPVFRAEDSFTHRHLCEFVGLD 321
Cdd:PTZ00425 293 nnngnssssnavsspaypdqylIDYKkdffSKQAFLTVSGQLSLE-NLCSSMGDVYTFGPTFRAENSHTSRHLAEFWMIE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 322 VE---------MEIRMHYseIMDLVGELFPFIFTKI---EERCPKELESVRKQYPFQSLKflpqtlRLTFAEGIQMLKEA 389
Cdd:PTZ00425 372 PEiafadlydnMELAESY--IKYCIGYVLNNNFDDIyyfEENVETGLISRLKNILDEDFA------KITYTNVIDLLQPY 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 390 GEEVD-PLG---DLNTESERKLGQLVLEKYktefYMLHRYPSAVRPFYtMPYENDSNYSNSFDVFI-RGEEIMSGAQRIH 464
Cdd:PTZ00425 444 SDSFEvPVKwgmDLQSEHERFVAEQIFKKP----VIVYNYPKDLKAFY-MKLNEDQKTVAAMDVLVpKIGEVIGGSQRED 518
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22328958 465 DPELLEKRARECGIDVKTISTYIDAFRYGAPPHGGFGVGLERVVMLLCALNNIRKTSLFPR 525
Cdd:PTZ00425 519 NLERLDKMIKEKKLNMESYWWYRQLRKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFPR 579
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
60-524 |
1.45e-26 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 113.55 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 60 TTNELQsavegKELTDVSNlVEEIVGSEVSIRGRLHKNRLVGTKLFVILRESGFTVQCVVEETRVGANMIKFVKQLSRES 139
Cdd:PLN02502 89 TAPELQ-----EKYGSLEN-GEELEDVSVSVAGRIMAKRAFGKLAFYDLRDDGGKIQLYADKKRLDLDEEEFEKLHSLVD 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 140 VVELIGVVSHPKKPLTGttqQVEIHVRKMYCLSRSLPNLPLvvedaarsesdiEKSG-KDgkqaarvlQDTRLNNRVLD- 217
Cdd:PLN02502 163 RGDIVGVTGTPGKTKKG---ELSIFPTSFEVLTKCLLMLPD------------KYHGlTD--------QETRYRQRYLDl 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 218 IRTPANQAIFRIQCQVQIAFREYLQSKGFLEIHTPKL--IAGSSEGGSAVFRLDYKGQPACLAQSPQLHKQMAICGDMRR 295
Cdd:PLN02502 220 IANPEVRDIFRTRAKIISYIRRFLDDRGFLEVETPMLnmIAGGAAARPFVTHHNDLNMDLYLRIATELHLKRLVVGGFER 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 296 VFEVGPVFRAEDSFThRHLCEFVglDVEM-EIRMHYSEIMDLVGELFpfiftkieERCPKEL-ESVRKQYPFQSLKFLPQ 373
Cdd:PLN02502 300 VYEIGRQFRNEGIST-RHNPEFT--TCEFyQAYADYNDMMELTEEMV--------SGMVKELtGSYKIKYHGIEIDFTPP 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 374 TLRLTFAEGiqmLKEAGEEVDPlGDLNTESERKLGQLVLEKYKTEF-------YMLHRY------PSAVRPFYTM----- 435
Cdd:PLN02502 369 FRRISMISL---VEEATGIDFP-ADLKSDEANAYLIAACEKFDVKCpppqttgRLLNELfeefleETLVQPTFVLdhpve 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 436 ------PYENDSNYSNSFDVFIRGEEIMSGAQRIHDP----ELLEKRAR--------ECGIDvktiSTYIDAFRYGAPPH 497
Cdd:PLN02502 445 msplakPHRSKPGLTERFELFINGRELANAFSELTDPvdqrERFEEQVKqhnagddeAMALD----EDFCTALEYGLPPT 520
|
490 500
....*....|....*....|....*..
gi 22328958 498 GGFGVGLERVVMLLCALNNIRKTSLFP 524
Cdd:PLN02502 521 GGWGLGIDRLVMLLTDSASIRDVIAFP 547
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
238-524 |
1.21e-25 |
|
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a lysine to the 3' OH group of ribose of the appropriate tRNA. Its assignment to class II aaRS is based upon its structure and the presence of three characteristic sequence motifs in the core domain. It is found in eukaryotes as well as some prokaryotes and archaea. However, LysRS belongs to class I aaRS's in some prokaryotes and archaea. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate.
Pssm-ID: 238398 [Multi-domain] Cd Length: 329 Bit Score: 107.67 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 238 REYLQSKGFLEIHTPKL--IAGsseGGSA--------VFRLDYKgqpacLAQSPQLHKQMAICGDMRRVFEVGPVFRAEd 307
Cdd:cd00775 19 RKFLDDRGFLEVETPMLqpIAG---GAAArpfithhnALDMDLY-----LRIAPELYLKRLIVGGFERVYEIGRNFRNE- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 308 SFTHRHLCEFvgldVEMEIRMHYS---EIMDLVGELFPFIFTKIeercpkeLESVRKQYPFQSLKFLPQTLRLTFAEGIQ 384
Cdd:cd00775 90 GIDLTHNPEF----TMIEFYEAYAdynDMMDLTEDLFSGLVKKI-------NGKTKIEYGGKELDFTPPFKRVTMVDALK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 385 mlKEAGEEVDPLGDLNTESERK---------------LGQL---VLEKYKTEFYM----LHRYPSAVRPFyTMPYENDSN 442
Cdd:cd00775 159 --EKTGIDFPELDLEQPEELAKllaklikekiekprtLGKLldkLFEEFVEPTLIqptfIIDHPVEISPL-AKRHRSNPG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 443 YSNSFDVFIRGEEIMSGAQRIHDPE------LLEKRARECG------IDvktiSTYIDAFRYGAPPHGGFGVGLERVVML 510
Cdd:cd00775 236 LTERFELFICGKEIANAYTELNDPFdqrerfEEQAKQKEAGddeammMD----EDFVTALEYGMPPTGGLGIGIDRLVML 311
|
330
....*....|....
gi 22328958 511 LCALNNIRKTSLFP 524
Cdd:cd00775 312 LTDSNSIRDVILFP 325
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
253-527 |
1.12e-24 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 108.03 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 253 KLIAGSSEGGSAV-FRLDYKGQPACLAQSPQLHKQMAICGdMRRVFEVGPVFRAEDSFTHRHLCEFVGLDVEMEirmhYS 331
Cdd:PLN02532 349 KLKTGTSVKADKLsFSKDFFSRPTYLTVSGRLHLESYACA-LGNVYTFGPRFRADRIDSARHLAEMWMVEVEMA----FS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 332 EI---MDLVGELFPFIFTKIEERCPKELESVRKQYPFQSLKFLPQTL-----RLTFAEGIQMLKEAgeeVDPLGDLNTE- 402
Cdd:PLN02532 424 ELedaMNCAEDYFKFLCKWVLENCSEDMKFVSKRIDKTISTRLEAIIssslqRISYTEAVDLLKQA---TDKKFETKPEw 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 403 ----SERKLGQLVLEKYKTEFyMLHRYPSAVRPFYtMPYENDSNYSNSFDVFI-RGEEIMSGAQRIHDPELLEKRARECG 477
Cdd:PLN02532 501 gialTTEHLSYLADEIYKKPV-IIYNYPKELKPFY-VRLNDDGKTVAAFDLVVpKVGTVITGSQNEERMDILNARIEELG 578
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 22328958 478 IDVKTISTYIDAFRYGAPPHGGFGVGLERVVMLLCALNNIRKTSLFPRDS 527
Cdd:PLN02532 579 LPREQYEWYLDLRRHGTVKHSGFSLGFELMVLFATGLPDVRDAIPFPRSW 628
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
60-524 |
3.18e-24 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 105.94 E-value: 3.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 60 TTNELQSAVEGKELTDVSNLVEEivgseVSIRGRLHKNRLVGTKLFVILRESGFTVQCVVEETRVGANMIKFVKQlsres 139
Cdd:PRK00484 34 TAAELRAKYDDKEKEELEELEIE-----VSVAGRVMLKRVMGKASFATLQDGSGRIQLYVSKDDVGEEALEAFKK----- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 140 vVEL---IGVVSHPKKPLTGttqQVEIHVRKMYCLSRSLPNLPlvveDAARSESDIEKsgkdgkqaaRVLQdtrlnnRVL 216
Cdd:PRK00484 104 -LDLgdiIGVEGTLFKTKTG---ELSVKATELTLLTKSLRPLP----DKFHGLTDVET---------RYRQ------RYV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 217 D-IRTPANQAIFRIQCQVQIAFREYLQSKGFLEIHTPKL--IAGsseGGSAvfR--------LDykgQPACLAQSPQLHK 285
Cdd:PRK00484 161 DlIVNPESRETFRKRSKIISAIRRFLDNRGFLEVETPMLqpIAG---GAAA--RpfithhnaLD---IDLYLRIAPELYL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 286 QMAICGDMRRVFEVGPVFRAEDSFThRHLCEFvgldVEMEIRMHYS---EIMDLVGELFPFIFTKIeercpkeLESVRKQ 362
Cdd:PRK00484 233 KRLIVGGFERVYEIGRNFRNEGIDT-RHNPEF----TMLEFYQAYAdynDMMDLTEELIRHLAQAV-------LGTTKVT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 363 YPFQSLKFLPQTLRLTFAEGIQmlKEAGEEVDPLGD-----------LNTESERKLGQLVLEKY--KTE-------FYMl 422
Cdd:PRK00484 301 YQGTEIDFGPPFKRLTMVDAIK--EYTGVDFDDMTDeearalakelgIEVEKSWGLGKLINELFeeFVEpkliqptFIT- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 423 hRYPSAVRPFyTMPYENDSNYSNSFDVFIRGEEIMSGAQRIHDP----ELLEKRARE--------CGIDVktisTYIDAF 490
Cdd:PRK00484 378 -DYPVEISPL-AKRHREDPGLTERFELFIGGREIANAFSELNDPidqrERFEAQVEAkeagddeaMFMDE----DFLRAL 451
|
490 500 510
....*....|....*....|....*....|....
gi 22328958 491 RYGAPPHGGFGVGLERVVMLLCALNNIRKTSLFP 524
Cdd:PRK00484 452 EYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
81-524 |
7.77e-24 |
|
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: 104.73 E-value: 7.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 81 EEIVGSEVSIRGRLHKNRLVGTKLFVILRESGFTVQCVVEETRVGANMIKFVKQLSRESVVELIGVVshpkkpltGTTQQ 160
Cdd:COG1190 52 EEETGDEVSVAGRIMAKRDMGKASFADLQDGSGRIQLYLRRDELGEEAYELFKLLDLGDIVGVEGTV--------FRTKT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 161 VE--IHVRKMYCLSRSLPNLPlvvedaarsesdiEK-SG-KDgkqaarvlQDTRLNNRVLD-IRTPANQAIFRIQCQVQI 235
Cdd:COG1190 124 GElsVKVEELTLLSKSLRPLP-------------EKfHGlTD--------PETRYRQRYVDlIVNPEVRETFRKRSKIIR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 236 AFREYLQSKGFLEIHTPKL--IAGsseGGSAvfR--------LDykgQPACLAQSPQLHKQMAICGDMRRVFEVGPVFRA 305
Cdd:COG1190 183 AIRRFLDERGFLEVETPMLqpIAG---GAAA--RpfithhnaLD---MDLYLRIAPELYLKRLIVGGFERVFEIGRNFRN 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 306 EDSfTHRHLCEFvgldVEMEIRMHYS---EIMDLVGELFPFIFTKIeercpkeLESVRKQYPFQSLKFLPQTLRLTFAEG 382
Cdd:COG1190 255 EGI-DTTHNPEF----TMLELYQAYAdynDMMDLTEELIREAAEAV-------LGTTKVTYQGQEIDLSPPWRRITMVEA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 383 IqmLKEAGEEVDPLGDLNT------------ESERKLGQLVLE--KYKTE-------FYMLhrYPSAVRPFyTMPYENDS 441
Cdd:COG1190 323 I--KEATGIDVTPLTDDEElralakelgievDPGWGRGKLIDElfEELVEpkliqptFVTD--YPVEVSPL-AKRHRDDP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 442 NYSNSFDVFIRGEEIMSGAQRIHDPELLEKR------ARECG--------IDvktistYIDAFRYGAPPHGGFGVGLERV 507
Cdd:COG1190 398 GLTERFELFIAGREIANAFSELNDPIDQRERfeeqleLKAAGddeampmdED------FLRALEYGMPPTGGLGIGIDRL 471
|
490
....*....|....*..
gi 22328958 508 VMLLCALNNIRKTSLFP 524
Cdd:COG1190 472 VMLLTDSPSIRDVILFP 488
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
88-524 |
1.78e-21 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 98.18 E-value: 1.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 88 VSIRGRLHKNRLVGTKLFVILRESGFTVQCVVEetrVGANMIK-FVKQLSRE-SVVELIGVVSHPKKPLTGttqQVEIHV 165
Cdd:PTZ00385 110 VRVAGRVTSVRDIGKIIFVTIRSNGNELQVVGQ---VGEHFTReDLKKLKVSlRVGDIIGADGVPCRMQRG---ELSVAA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 166 RKMYCLSrslpnlPLVVEDAARSESdieksgkdgKQAARVLQDT--RLNNRVLDIRT-PANQAIFRIQCQVQIAFREYLQ 242
Cdd:PTZ00385 184 SRMLILS------PYVCTDQVVCPN---------LRGFTVLQDNdvKYRYRFTDMMTnPCVIETIKKRHVMLQALRDYFN 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 243 SKGFLEIHTPKL--IAGSSEGGSAVFRLDYKGQPACLAQSPQLHKQMAICGDMRRVFEVGPVFRAEDSfTHRHLCEFVgl 320
Cdd:PTZ00385 249 ERNFVEVETPVLhtVASGANAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDA-DRSHNPEFT-- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 321 DVEMEIRMH-YSEIMDLVGELFPFIFTKIEERCPKELESVRKQYPFQSLKFLPQTLRLTFAEGIQmlKEAGEEVDPLGDL 399
Cdd:PTZ00385 326 SCEFYAAYHtYEDLMPMTEDIFRQLAMRVNGTTVVQIYPENAHGNPVTVDLGKPFRRVSVYDEIQ--RMSGVEFPPPNEL 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 400 NTESERKLGQLVLEKYKT----------------EFYMLHRY--PSAV--RPFYTMPYENDS----NYSNSFDVFIRGEE 455
Cdd:PTZ00385 404 NTPKGIAYMSVVMLRYNIplppvrtaakmfekliDFFITDRVvePTFVmdHPLFMSPLAKEQvsrpGLAERFELFVNGIE 483
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22328958 456 IMSGAQRIHDPELLEKRARECGID--------VKTISTYIDAFRYGAPPHGGFGVGLERVVMLLCALNNIRKTSLFP 524
Cdd:PTZ00385 484 YCNAYSELNDPHEQYHRFQQQLVDrqggdeeaMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFP 560
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
81-524 |
1.01e-17 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 86.22 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 81 EEIVGSEVSIRGRLHKNRLVGTKL-FVILRESGFTVQCVVEETRVGANMIKFVKQLSRESVVELIGVVSHPKKPLTGttq 159
Cdd:PTZ00417 128 EHLEDTILNVTGRIMRVSASGQKLrFFDLVGDGAKIQVLANFAFHDHTKSNFAECYDKIRRGDIVGIVGFPGKSKKG--- 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 160 QVEIHVRKMYCLSRSLPNLPLvvedaarsesdieKSGkdgkqaarvLQDT--RLNNRVLDIRTPAN-QAIFRIQCQVQIA 236
Cdd:PTZ00417 205 ELSIFPKETIILSPCLHMLPM-------------KYG---------LKDTeiRYRQRYLDLMINEStRSTFITRTKIINY 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 237 FREYLQSKGFLEIHTP--KLIAGSSEGGSAVFRLDYKGQPACLAQSPQLHKQMAICGDMRRVFEVGPVFRAED------- 307
Cdd:PTZ00417 263 LRNFLNDRGFIEVETPtmNLVAGGANARPFITHHNDLDLDLYLRIATELPLKMLIVGGIDKVYEIGKVFRNEGidnthnp 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 308 SFTHrhlCEFVGLDVEMEIRMHYSE--IMDLVGELF-----------------------PFIFTKIEERCPKeLESVRKQ 362
Cdd:PTZ00417 343 EFTS---CEFYWAYADFYDLIKWSEdfFSQLVMHLFgtykilynkdgpekdpieidftpPYPKVSIVEELEK-LTNTKLE 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 363 YPFQSlkflPQTLRltfaEGIQMLKEAGEEVDplgdlNTESERKL-----GQLVLEKYKTEFYMLHRYPSAVRPFYTMpY 437
Cdd:PTZ00417 419 QPFDS----PETIN----KMINLIKENKIEMP-----NPPTAAKLldqlaSHFIENKYPNKPFFIIEHPQIMSPLAKY-H 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 438 ENDSNYSNSFDVFIRGEEIMSGAQRIHDPE------LLEKRARECGiDVKTI---STYIDAFRYGAPPHGGFGVGLERVV 508
Cdd:PTZ00417 485 RSKPGLTERLEMFICGKEVLNAYTELNDPFkqkecfSAQQKDREKG-DAEAFqfdAAFCTSLEYGLPPTGGLGLGIDRIT 563
|
490
....*....|....*.
gi 22328958 509 MLLCALNNIRKTSLFP 524
Cdd:PTZ00417 564 MFLTNKNCIKDVILFP 579
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
80-524 |
7.44e-17 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 84.25 E-value: 7.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 80 VEEIVGSEVSIRGRLHKNRLVGTKLFVILRESGFTVQCVVEETRVGANMIK-FVKQLSRESVVELIGVVSHPKkplTGTt 158
Cdd:PRK02983 646 LDAPTGEEVSVSGRVLRIRDYGGVLFADLRDWSGELQVLLDASRLEQGSLAdFRAAVDLGDLVEVTGTMGTSR---NGT- 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 159 qqVEIHVRKMYCLSRSLPNLPlvveDAARSESDIEksgkdgkqaARVLQdtrlnnRVLDIRT-PANQAIFRIQCQVQIAF 237
Cdd:PRK02983 722 --LSLLVTSWRLAGKCLRPLP----DKWKGLTDPE---------ARVRQ------RYLDLAVnPEARDLLRARSAVVRAV 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 238 REYLQSKGFLEIHTPKL--IAGsseGGSA---VFRLDYKGQPACLAQSPQLH-KQMAIcGDMRRVFEVGPVFRAED-SFT 310
Cdd:PRK02983 781 RETLVARGFLEVETPILqqVHG---GANArpfVTHINAYDMDLYLRIAPELYlKRLCV-GGVERVFELGRNFRNEGvDAT 856
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 311 HRHlcEFVGLDVemeIRMH--YSEIMDLVGELF----------PFIFTKIEErcpKELESVRKQYPFqslkflPQtlrLT 378
Cdd:PRK02983 857 HNP--EFTLLEA---YQAHadYDTMRDLTRELIqnaaqaahgaPVVMRPDGD---GVLEPVDISGPW------PV---VT 919
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 379 FAEGIQmlkEA-GEEVDPlgDLNTESERKL--------------GQLVLEKY------KTE---FYMlhRYPSAVRPFyT 434
Cdd:PRK02983 920 VHDAVS---EAlGEEIDP--DTPLAELRKLcdaagipyrtdwdaGAVVLELYehlvedRTTfptFYT--DFPTSVSPL-T 991
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 435 MPYENDSNYSNSFDVFIRGEEIMSGAQRIHDPelLEKRAR-------ECGIDVKTIS---TYIDAFRYGAPPHGGFGVGL 504
Cdd:PRK02983 992 RPHRSDPGLAERWDLVAWGVELGTAYSELTDP--VEQRRRlteqsllAAGGDPEAMEldeDFLQALEYAMPPTGGLGMGV 1069
|
490 500
....*....|....*....|
gi 22328958 505 ERVVMLLCAlNNIRKTSLFP 524
Cdd:PRK02983 1070 DRLVMLLTG-RSIRETLPFP 1088
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
87-173 |
6.64e-16 |
|
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: 72.60 E-value: 6.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 87 EVSIRGRLHKNRLVGTKLFVILRESGFTVQCVVEETRVGaNMIKFVKQLSRESVVELIGVVSHPKKPlTGTTQQVEIHVR 166
Cdd:cd04100 1 EVTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEELG-EFFEEAEKLRTESVVGVTGTVVKRPEG-NLATGEIELQAE 78
|
....*..
gi 22328958 167 KMYCLSR 173
Cdd:cd04100 79 ELEVLSK 85
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
233-506 |
3.14e-12 |
|
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: 65.99 E-value: 3.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 233 VQIAFREYLQSKGFLEIHTPKLIAGSSEGGSA------VFRLDYKGQPACLAQSPQLHKQMAICGDMR----RVFEVGPV 302
Cdd:cd00768 5 IEQKLRRFMAELGFQEVETPIVEREPLLEKAGhepkdlLPVGAENEEDLYLRPTLEPGLVRLFVSHIRklplRLAEIGPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 303 FRAED-SFTHRHLCEFVGLDVEMeirmhyseimdlVGElfpfiftkieercpkelesvrkqyPFQSLKFLPQTLRLTFAe 381
Cdd:cd00768 85 FRNEGgRRGLRRVREFTQLEGEV------------FGE------------------------DGEEASEFEELIELTEE- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 382 giqMLKEAGEEVDPlgdlnteserklgqLVLEKYKTEFYMLHrypsavrpfytmpyendsnYSNSFDVFI-----RGEEI 456
Cdd:cd00768 128 ---LLRALGIKLDI--------------VFVEKTPGEFSPGG-------------------AGPGFEIEVdhpegRGLEI 171
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 22328958 457 MSGAQRIHDPELLEKRARecgidvktistYIDAFRYGAPPHGGFGVGLER 506
Cdd:cd00768 172 GSGGYRQDEQARAADLYF-----------LDEALEYRYPPTIGFGLGLER 210
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
81-180 |
3.83e-12 |
|
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: 62.72 E-value: 3.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 81 EEIVGSEVSIRGRLHKNRLVGTKLFVILRESGFTVQCVVEETRVGANMIKFVKQLSRESVVELIGVVSHPKKPLTGttqq 160
Cdd:cd04316 8 PELDGEEVTVAGWVHEIRDLGGIKFVILRDREGIVQVTAPKKKVDKELFKTVRKLSRESVISVTGTVKAEPKAPNG---- 83
|
90 100
....*....|....*....|
gi 22328958 161 VEIHVRKMYCLSRSLPNLPL 180
Cdd:cd04316 84 VEIIPEEIEVLSEAKTPLPL 103
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
77-221 |
1.84e-09 |
|
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: 55.99 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 77 SNLVEEIVGSEVSIRGRLHKNRLVGTKLFVILRESGFTVQCVVEETRvgANMIKFVKQLSRESVVELIGVVSH------- 149
Cdd:cd04317 6 GELRESHVGQEVTLCGWVQRRRDHGGLIFIDLRDRYGIVQVVFDPEE--APEFELAEKLRNESVIQVTGKVRArpegtvn 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22328958 150 PKKPltgtTQQVEIHVRKMYCLSRSlPNLPLVVEDAArSESDieksgkdgkqaarvlqDTRLNNRVLDIRTP 221
Cdd:cd04317 84 PKLP----TGEIEVVASELEVLNKA-KTLPFEIDDDV-NVSE----------------ELRLKYRYLDLRRP 133
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
88-171 |
7.81e-06 |
|
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: 43.76 E-value: 7.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 88 VSIRGRLH-KNRLVGTKLFVILR-ESGfTVQCVVEEtrvgANMIKFVKQLSRESVVELIGVVSHPKKPltgttqQVEIHV 165
Cdd:pfam01336 1 VTVAGRVTsIRRSGGKLLFLTLRdGTG-SIQVVVFK----EEAEKLAKKLKEGDVVRVTGKVKKRKGG------ELELVV 69
|
....*.
gi 22328958 166 RKMYCL 171
Cdd:pfam01336 70 EEIELL 75
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
87-168 |
1.19e-05 |
|
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus horikoshii AsnRS asparaginyl-tRNA synthetase (AsnRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The archeal enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose.
Pssm-ID: 239814 [Multi-domain] Cd Length: 103 Bit Score: 44.05 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 87 EVSIRGRLHKNRLVGTKLFVILRESGFTVQCVVEETrVGANMIKFVKQLSRESVVELIG-VVSHPKKPlTGttqqVEIHV 165
Cdd:cd04319 1 KVTLAGWVYRKREVGKKAFIVLRDSTGIVQAVFSKD-LNEEAYREAKKVGIESSVIVEGaVKADPRAP-GG----AEVHG 74
|
...
gi 22328958 166 RKM 168
Cdd:cd04319 75 EKL 77
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
87-166 |
1.36e-05 |
|
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: 43.38 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 87 EVSIRGRLHKNRLVGTKLFVILRESGFTVQCVVEETRVGANMIkfVKQLSRESVVELIGVVSHP---KKPLTGttqqVEI 163
Cdd:cd04323 1 RVKVFGWVHRLRSQKKLMFLVLRDGTGFLQCVLSKKLVTEFYD--AKSLTQESSVEVTGEVKEDpraKQAPGG----YEL 74
|
...
gi 22328958 164 HVR 166
Cdd:cd04323 75 QVD 77
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
238-518 |
2.91e-05 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 46.08 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 238 REYLQSKGFLEIHTPKLI-AGSSEGGSAVFRLDY------KGQPACLAQSPQLH-KQM--AICGDmrrVFEVGPVFRAED 307
Cdd:PRK09350 16 RRFFADRGVLEVETPILSqATVTDIHLVPFETRFvgpgasQGKTLWLMTSPEYHmKRLlaAGSGP---IFQICKSFRNEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 308 SfTHRHLCEFVGLDVemeIRMHYS--EIMDLVGELFPFIFtkieeRCpKELESVRKQYPFQslKFLpqtlrltfaegiqm 385
Cdd:PRK09350 93 A-GRYHNPEFTMLEW---YRPHYDmyRLMNEVDDLLQQVL-----DC-EPAESLSYQQAFL--RYL-------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 386 lkeageEVDPLGDLNT---ESERKLGQLVL----EKYKTEFYMLhrYPSAVRP---------FYTMPYE---------ND 440
Cdd:PRK09350 147 ------GIDPLSADKTqlrEVAAKLGLSNIadeeEDRDTLLQLL--FTFGVEPnigkekptfVYHFPASqaalakistED 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 441 SNYSNSFDVFIRGEEIMSGAQRIHDPELLEKR-------ARECGIDVKTISTY-IDAFRYGAPPHGGFGVGLERVVMLLC 512
Cdd:PRK09350 219 HRVAERFEVYFKGIELANGFHELTDAREQRQRfeqdnrkRAARGLPQQPIDENlIAALEAGLPDCSGVALGVDRLIMLAL 298
|
....*.
gi 22328958 513 ALNNIR 518
Cdd:PRK09350 299 GAESIS 304
|
|
| ScAspRS_mt_like_N |
cd04321 |
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
87-171 |
2.46e-03 |
|
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: 37.30 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328958 87 EVSIRGRLH-KNRLVGTKLFVILRES-GFTVQcVVEETRVGAnmIKFVKQLSRESVVELIGVVSHPKKPLTGTTQQVEIH 164
Cdd:cd04321 1 KVTLNGWIDrKPRIVKKLSFADLRDPnGDIIQ-LVSTAKKDA--FSLLKSITAESPVQVRGKLQLKEAKSSEKNDEWELV 77
|
....*..
gi 22328958 165 VRKMYCL 171
Cdd:cd04321 78 VDDIQTL 84
|
|
| |
