|
Name |
Accession |
Description |
Interval |
E-value |
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
1-590 |
0e+00 |
|
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: 1142.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 1 MMRSHYCGQLNESLDGQEVTLCGWVHRRRDHGGVIFLDVRDREGLAQVVFDPDR-AETFAKADRVRSEFVVKITGKVRLR 79
Cdd:COG0173 1 MYRTHYCGELRESDVGQEVTLSGWVHRRRDHGGLIFIDLRDRYGITQVVFDPDDsAEAFEKAEKLRSEYVIAVTGKVRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 80 PEGARNPNMASGSIEVLGYELEVLNQAETPPFPLDEYSDVGEETRLRYRFIDLRRPEMAAKLKLRARITSSIRRYLDDNG 159
Cdd:COG0173 81 PEGTVNPKLPTGEIEVLASELEILNKAKTPPFQIDDDTDVSEELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDENG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 160 FLDVETPILGRPTPEGARDYLVPSRTYPGHFFALPQSPQLFKQLLMVAGFDRYYQIAKCFRDEDLRADRQPEFTQIDIET 239
Cdd:COG0173 161 FLEIETPILTKSTPEGARDYLVPSRVHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFRDEDLRADRQPEFTQLDIEM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 240 SFLDESDIIGITEKMVRQLFKEVLDVEFDE-FPHMPFEEAMRRYGSDKPDLRIPLELVDVADQLKEVEFKVFSGPANdPK 318
Cdd:COG0173 241 SFVDQEDVFELMEGLIRHLFKEVLGVELPTpFPRMTYAEAMERYGSDKPDLRFGLELVDVTDIFKDSGFKVFAGAAE-NG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 319 GRVAALRVPGAASMPRSQIDDYTKFVGIYGAKGLAYIKVNErakgvEGLQSPIVKFIPEANLNVILDRVGAVDGDIVFFG 398
Cdd:COG0173 320 GRVKAINVPGGASLSRKQIDELTEFAKQYGAKGLAYIKVNE-----DGLKSPIAKFLSEEELAAILERLGAKPGDLIFFV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 399 ADKAKIVCDALGALRIKVGHDLKLL-TREWAPMWVVDFPMFEENDD-GSLSALHHPFTSPKC-TPAELEANPGAALSRAY 475
Cdd:COG0173 395 ADKPKVVNKALGALRLKLGKELGLIdEDEFAFLWVVDFPLFEYDEEeGRWVAMHHPFTMPKDeDLDLLETDPGKVRAKAY 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 476 DMVLNGTELGGGSIRIHDKSMQQAVFRVLGIDEAEQEEKFGFLLDALKYGAPPHGGLAFGLDRLVMLMTGASSIREVIAF 555
Cdd:COG0173 475 DLVLNGYELGGGSIRIHDPELQEKVFELLGISEEEAEEKFGFLLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAF 554
|
570 580 590
....*....|....*....|....*....|....*
gi 15596160 556 PKTQSAGDVMTQAPGSVDGKALRELHIRLREQPKA 590
Cdd:COG0173 555 PKTQSAQDLMTGAPSEVDEKQLKELHIRLRPPEKK 589
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
1-588 |
0e+00 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 1126.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 1 MMRSHYCGQLNESLDGQEVTLCGWVHRRRDHGGVIFLDVRDREGLAQVVFDPDrAETFAKADRVRSEFVVKITGKVRLRP 80
Cdd:PRK00476 2 MMRTHYCGELRESHVGQTVTLCGWVHRRRDHGGLIFIDLRDREGIVQVVFDPD-AEAFEVAESLRSEYVIQVTGTVRARP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 81 EGARNPNMASGSIEVLGYELEVLNQAETPPFPLDEYSDVGEETRLRYRFIDLRRPEMAAKLKLRARITSSIRRYLDDNGF 160
Cdd:PRK00476 81 EGTVNPNLPTGEIEVLASELEVLNKSKTLPFPIDDEEDVSEELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDDNGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 161 LDVETPILGRPTPEGARDYLVPSRTYPGHFFALPQSPQLFKQLLMVAGFDRYYQIAKCFRDEDLRADRQPEFTQIDIETS 240
Cdd:PRK00476 161 LEIETPILTKSTPEGARDYLVPSRVHPGKFYALPQSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADRQPEFTQIDIEMS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 241 FLDESDIIGITEKMVRQLFKEVLDVEFDE-FPHMPFEEAMRRYGSDKPDLRIPLELVDVADQLKEVEFKVFSGPANDpKG 319
Cdd:PRK00476 241 FVTQEDVMALMEGLIRHVFKEVLGVDLPTpFPRMTYAEAMRRYGSDKPDLRFGLELVDVTDLFKDSGFKVFAGAAND-GG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 320 RVAALRVPG-AASMPRSQIDDYTKFVGIYGAKGLAYIKVNErakgvEGLQSPIVKFIPEANLNVILDRVGAVDGDIVFFG 398
Cdd:PRK00476 320 RVKAIRVPGgAAQLSRKQIDELTEFAKIYGAKGLAYIKVNE-----DGLKGPIAKFLSEEELAALLERTGAKDGDLIFFG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 399 ADKAKIVCDALGALRIKVGHDLKLL-TREWAPMWVVDFPMFEENDD-GSLSALHHPFTSPKCT--PAELEANPGAALSRA 474
Cdd:PRK00476 395 ADKAKVVNDALGALRLKLGKELGLIdEDKFAFLWVVDFPMFEYDEEeGRWVAAHHPFTMPKDEdlDELETTDPGKARAYA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 475 YDMVLNGTELGGGSIRIHDKSMQQAVFRVLGIDEAEQEEKFGFLLDALKYGAPPHGGLAFGLDRLVMLMTGASSIREVIA 554
Cdd:PRK00476 475 YDLVLNGYELGGGSIRIHRPEIQEKVFEILGISEEEAEEKFGFLLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIA 554
|
570 580 590
....*....|....*....|....*....|....
gi 15596160 555 FPKTQSAGDVMTQAPGSVDGKALRELHIRLREQP 588
Cdd:PRK00476 555 FPKTQSAQDLLTGAPSPVDEKQLRELGIRLRKKE 588
|
|
| aspS_bact |
TIGR00459 |
aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be ... |
2-583 |
0e+00 |
|
aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be discriminating (6.1.1.12) or nondiscriminating (6.1.1.23). In a multiple sequence alignment of representative asparaginyl-tRNA synthetases (asnS), archaeal/eukaryotic type aspartyl-tRNA synthetases (aspS_arch), and bacterial type aspartyl-tRNA synthetases (aspS_bact), there is a striking similarity between asnS and aspS_arch in gap pattern and in sequence, and a striking divergence of aspS_bact. Consequently, a separate model was built for each of the three groups. This model, aspS_bact, represents aspartyl-tRNA synthetases from the Bacteria and from mitochondria. In some species, this enzyme aminoacylates tRNA for both Asp and Asn; Asp-tRNA(asn) is subsequently transamidated to Asn-tRNA(asn). This model generates very low scores for the archaeal type of aspS and for asnS; scores between the trusted and noise cutoffs represent fragmentary sequences. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 211576 [Multi-domain] Cd Length: 583 Bit Score: 833.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 2 MRSHYCGQLNESLDGQEVTLCGWVHRRRDHGGVIFLDVRDREGLAQVVFDPDRAEtFAKADRVRSEFVVKITGKVRLRPE 81
Cdd:TIGR00459 1 MRTHYCGQLRTEHLGQTVTLAGWVNRRRDLGGLIFIDLRDRSGIVQVVCDPDADA-LKLAKGLRNEDVVQVKGKVSARPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 82 GARNPNMASGSIEVLGYELEVLNQAETPPFPLDEySDVGEETRLRYRFIDLRRPEMAAKLKLRARITSSIRRYLDDNGFL 161
Cdd:TIGR00459 80 GNINRNLDTGEIEILAESITLLNKSKTPPLIIEK-TDAEEEVRLKYRYLDLRRPEMQQRLKLRHKVTKAVRNFLDQQGFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 162 DVETPILGRPTPEGARDYLVPSRTYPGHFFALPQSPQLFKQLLMVAGFDRYYQIAKCFRDEDLRADRQPEFTQIDIETSF 241
Cdd:TIGR00459 159 EIETPMLTKSTPEGARDYLVPSRVHKGEFYALPQSPQLFKQLLMVSGVDRYYQIARCFRDEDLRADRQPEFTQIDMEMSF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 242 LDESDIIGITEKMVRQLFKEVLDVEFDE-FPHMPFEEAMRRYGSDKPDLRIPLELVDVADQLKEVEFKVFSGPANDpKGR 320
Cdd:TIGR00459 239 MTQEDVMELIEKLVSHVFLEVKGIDLKKpFPVMTYAEAMERYGSDKPDLRFPLELIDVTDLFKDSEFKVFSNLIND-GGR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 321 VAALRVPG-AASMPRSQIDDYTKFVGIYGAKGLAYIKVNERakgveGLQSPIVKFIPEANLNVILDRVGAVDGDIVFFGA 399
Cdd:TIGR00459 318 VKAIRVPGgWAELSRKSIKELRKFAKEYGAKGLAYLKVNED-----GINSPIKKFLDEKKGKILLERTDAQNGDILLFGA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 400 DKAKIVCDALGALRIKVGHDLKLLT-REWAPMWVVDFPMFEENDDGSLSALHHPFTSPK-CTPAELEANPGAALSRAYDM 477
Cdd:TIGR00459 393 GSKKIVLDALGALRLKLGKDLGLVDpDLFSFLWVVDFPMFEKDKEGRLCAAHHPFTMPKdEDLENLEAAPEEALAEAYDL 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 478 VLNGTELGGGSIRIHDKSMQQAVFRVLGIDEAEQEEKFGFLLDALKYGAPPHGGLAFGLDRLVMLMTGASSIREVIAFPK 557
Cdd:TIGR00459 473 VLNGVELGGGSIRIHDPEVQKKVFEILGIDPEEAREKFGFLLEAFKYGTPPHAGFALGLDRLMMLLTGTDNIRDVIAFPK 552
|
570 580
....*....|....*....|....*.
gi 15596160 558 TQSAGDVMTQAPGSVDGKALRELHIR 583
Cdd:TIGR00459 553 TTAAACLMTEAPSFIDEKQLEELSIK 578
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
3-589 |
0e+00 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 682.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 3 RSHYCGQLNESLDGQEVTLCGWVHRRRDHGGVIFLDVRDREGLAQVVFDPDRA-ETFAKADRVRSEFVVKITGKVRLRPE 81
Cdd:PLN02903 59 RSHLCGALSVNDVGSRVTLCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDEFpEAHRTANRLRNEYVVAVEGTVRSRPQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 82 GARNPNMASGSIEVLGYELEVLNQAETP-PFPL----DEYSDVGEETRLRYRFIDLRRPEMAAKLKLRARITSSIRRYL- 155
Cdd:PLN02903 139 ESPNKKMKTGSVEVVAESVDILNVVTKSlPFLVttadEQKDSIKEEVRLRYRVLDLRRPQMNANLRLRHRVVKLIRRYLe 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 156 DDNGFLDVETPILGRPTPEGARDYLVPSRTYPGHFFALPQSPQLFKQLLMVAGFDRYYQIAKCFRDEDLRADRQPEFTQI 235
Cdd:PLN02903 219 DVHGFVEIETPILSRSTPEGARDYLVPSRVQPGTFYALPQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEFTQL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 236 DIETSFLDESDIIGITEKMVRQLFKEVLDVEF-DEFPHMPFEEAMRRYGSDKPDLRIPLELVDVADQLKEVEFKVFSGPA 314
Cdd:PLN02903 299 DMELAFTPLEDMLKLNEDLIRQVFKEIKGVQLpNPFPRLTYAEAMSKYGSDKPDLRYGLELVDVSDVFAESSFKVFAGAL 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 315 NDpKGRVAALRVPGAASMPRSQI----DDYTKFVGiYGAKGLAYIKVNERAKgVEGLQSpIVKFIPEANLNVILDRVGAV 390
Cdd:PLN02903 379 ES-GGVVKAICVPDGKKISNNTAlkkgDIYNEAIK-SGAKGLAFLKVLDDGE-LEGIKA-LVESLSPEQAEQLLAACGAG 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 391 DGDIVFFGADKAKIVCDALGALRIKVGHDLKLLTR-EWAPMWVVDFPMFEENDD-GSLSALHHPFTSPKctPAELEANPG 468
Cdd:PLN02903 455 PGDLILFAAGPTSSVNKTLDRLRQFIAKTLDLIDPsRHSILWVTDFPMFEWNEDeQRLEALHHPFTAPN--PEDMGDLSS 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 469 A-ALsrAYDMVLNGTELGGGSIRIHDKSMQQAVFRVLGIDEAEQEEKFGFLLDALKYGAPPHGGLAFGLDRLVMLMTGAS 547
Cdd:PLN02903 533 ArAL--AYDMVYNGVEIGGGSLRIYRRDVQQKVLEAIGLSPEEAESKFGYLLEALDMGAPPHGGIAYGLDRLVMLLAGAK 610
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 15596160 548 SIREVIAFPKTQSAGDVMTQAPGSVDGKALRELHIRLREQPK 589
Cdd:PLN02903 611 SIRDVIAFPKTTTAQCALTRAPSEVDDKQLQDLSIASTAPPP 652
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
6-580 |
0e+00 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 545.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 6 YCGQLNESLDGQEVTLCGWVHRRRDHGGVIFLDVRDREGLAQVVFDPDRA--ETFAKADRVRSEFVVKITGKVRLRPEGA 83
Cdd:PRK12820 8 FCGHLSLDDTGREVCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFSPEAApaDVYELAASLRAEFCVALQGEVQKRLEET 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 84 RNPNMASGSIEVLGYELEVLNQAETPPFPLDEYS-----------DVGEETRLRYRFIDLRRPEMAAKLKLRARITSSIR 152
Cdd:PRK12820 88 ENPHIETGDIEVFVRELSILAASEALPFAISDKAmtagagsagadAVNEDLRLQYRYLDIRRPAMQDHLAKRHRIIKCAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 153 RYLDDNGFLDVETPILGRPTPEGARDYLVPSRTYPGHFFALPQSPQLFKQLLMVAGFDRYYQIAKCFRDEDLRADRQPEF 232
Cdd:PRK12820 168 DFLDSRGFLEIETPILTKSTPEGARDYLVPSRIHPKEFYALPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 233 TQIDIETSFLDESDIIGITEKMVRQLFkEVLDVEFDE-FPHMPFEEAMRRYGSDKPDLRIPLELVDVADQLKEVEFKVFS 311
Cdd:PRK12820 248 TQLDIEASFIDEEFIFELIEELTARMF-AIGGIALPRpFPRMPYAEAMDTTGSDRPDLRFDLKFADATDIFENTRYGIFK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 312 GPANDpKGRVAALRVPGAASMPRSQI--DDYTK-FVGIYGAKGLAYIKVNErakgvEGLQSPIVKFIPEANLNVILDRVG 388
Cdd:PRK12820 327 QILQR-GGRIKGINIKGQSEKLSKNVlqNEYAKeIAPSFGAKGMTWMRAEA-----GGLDSNIVQFFSADEKEALKRRFH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 389 AVDGDIVFFGADKA-KIVCDALGALRIKVGHDLKLLTRE-WAPMWVVDFPMFEENDDGSLSALHHPFTSPKCT---PAEL 463
Cdd:PRK12820 401 AEDGDVIIMIADAScAIVLSALGQLRLHLADRLGLIPEGvFHPLWITDFPLFEATDDGGVTSSHHPFTAPDREdfdPGDI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 464 EANPgAALSRAYDMVLNGTELGGGSIRIHDKSMQQAVFRVLGIDEAEQEEKFGFLLDALKYGAPPHGGLAFGLDRLVMLM 543
Cdd:PRK12820 481 EELL-DLRSRAYDLVVNGEELGGGSIRINDKDIQLRIFAALGLSEEDIEDKFGFFLRAFDFAAPPHGGIALGLDRVVSMI 559
|
570 580 590
....*....|....*....|....*....|....*..
gi 15596160 544 TGASSIREVIAFPKTQSAGDVMTQAPGSVDGKALREL 580
Cdd:PRK12820 560 LQTPSIREVIAFPKNRSAACPLTGAPSEVAQEQLAEL 596
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
141-560 |
6.25e-156 |
|
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: 448.18 E-value: 6.25e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 141 LKLRARITSSIRRYLDDNGFLDVETPILGRPTPEGARDYLVPSRTYPGHFFALPQSPQLFKQLLMVAGFDRYYQIAKCFR 220
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTPEGARDFLVPSRLHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 221 DEDLRADRQPEFTQIDIETSFLDESDIIGITEKMVRQLFKEVLDVEFDE-FPHMPFEEAMRRYGsdkpdlriplelvdva 299
Cdd:cd00777 81 DEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLGVELTTpFPRMTYAEAMERYG---------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 300 dqlkevefkvfsgpandpkgrvaalrvpgaasmprsqiddytkfvgiygakglayikvnerakgveglqspivkfipean 379
Cdd:cd00777 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 380 lnvildrvgavdgdivffgadkakivcdalgalrikvghdlklltreWAPMWVVDFPMFEENDD-GSLSALHHPFTSPKC 458
Cdd:cd00777 145 -----------------------------------------------FKFLWIVDFPLFEWDEEeGRLVSAHHPFTAPKE 177
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 459 -TPAELEANPGAALSRAYDMVLNGTELGGGSIRIHDKSMQQAVFRVLGIDEAEQEEKFGFLLDALKYGAPPHGGLAFGLD 537
Cdd:cd00777 178 eDLDLLEKDPEDARAQAYDLVLNGVELGGGSIRIHDPDIQEKVFEILGLSEEEAEEKFGFLLEAFKYGAPPHGGIALGLD 257
|
410 420
....*....|....*....|...
gi 15596160 538 RLVMLMTGASSIREVIAFPKTQS 560
Cdd:cd00777 258 RLVMLLTGSESIRDVIAFPKTQN 280
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
120-559 |
1.08e-141 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 413.11 E-value: 1.08e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 120 GEETRLRYRFIDLRRPEMAAKLKLRARITSSIRRYLDDNGFLDVETPILGR-PTPEGARDYLVPSRTYpGHFFALPQSPQ 198
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKsATPEGARDFLVPSRAL-GKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 199 LFKQLLMVAGFDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFLDESDIIGITEKMVRQLFKEVLDVEFDE--------- 269
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELeggtlldlk 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 270 --FPHMPFEEAMRR----------YGSDKPDLRIPLELVDVADqlkevefkvfsgpandpkgrvaalrvpgaasmprsqi 337
Cdd:pfam00152 160 kpFPRITYAEAIEKlngkdveelgYGSDKPDLRFLLELVIDKN------------------------------------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 338 ddytkfvgiygakglayikvnerakgveglqspivkfipeanlnvildrvgavdgdivffgadkakivcdalgalrikvg 417
Cdd:pfam00152 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 418 hdlklltrEWAPMWVVDFPmfeenddgslsALHHPFTSPKCtpaelEANPgaALSRAYDMVLNGTELGGGSIRIHDKSMQ 497
Cdd:pfam00152 203 --------KFNPLWVTDFP-----------AEHHPFTMPKD-----EDDP--ALAEAFDLVLNGVEIGGGSIRIHDPELQ 256
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596160 498 QAVFRVLGIDEAEQEEKFGFLLDALKYGAPPHGGLAFGLDRLVMLMTGASSIREVIAFPKTQ 559
Cdd:pfam00152 257 EERFEEQGLDPEEAEEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAFPKTR 318
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
1-556 |
1.67e-91 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 288.63 E-value: 1.67e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 1 MMRSHYCGQLNESLDGQEVTLCGWVHRRRDHGGVIFLDVRDREGLAQVVFDPDR-AETFAKADRVRSEFVVKITGKVRlr 79
Cdd:PRK05159 1 MMKRHLTSELTPELDGEEVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKVdEELFETIKKLKRESVVSVTGTVK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 80 pegaRNPNmASGSIEVLGYELEVLNQAETPPfPLDEYSDVGEE--TRLRYRFIDLRRPEMAAKLKLRARITSSIRRYLDD 157
Cdd:PRK05159 79 ----ANPK-APGGVEVIPEEIEVLNKAEEPL-PLDISGKVLAEldTRLDNRFLDLRRPRVRAIFKIRSEVLRAFREFLYE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 158 NGFLDVETP-ILGRPTPEGARdyLVPSrTYPGHFFALPQSPQLFKQLLMVAGFDRYYQIAKCFRDEDLRADRQ-PEFTQI 235
Cdd:PRK05159 153 NGFTEIFTPkIVASGTEGGAE--LFPI-DYFEKEAYLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSRHlNEYTSI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 236 DIETSFLD-ESDIIGITEKMVRQLFKEV----------LDVEF----DEFPHMPFEEAMRRygsdkpdlriplelvdVAD 300
Cdd:PRK05159 230 DVEMGFIDdHEDVMDLLENLLRYMYEDVaencekelelLGIELpvpeTPIPRITYDEAIEI----------------LKS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 301 QLKEVEFkvfsGPANDPKGRVAalrvpgaasmprsqiddytkfvgiygakglayikVNERAKGVEGlqspivkfipeanl 380
Cdd:PRK05159 294 KGNEISW----GDDLDTEGERL----------------------------------LGEYVKEEYG-------------- 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 381 nvildrvgavdGDIVFfgadkakivcdalgalrikvghdlklltrewapmwVVDFPMfeenddgslSAlhHPF-TSPKct 459
Cdd:PRK05159 322 -----------SDFYF-----------------------------------ITDYPS---------EK--RPFyTMPD-- 342
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 460 paelEANPGaaLSRAYDMVLNGTELGGGSIRIHDKSMQQAVFRVLGIDeaeqEEKFGFLLDALKYGAPPHGGLAFGLDRL 539
Cdd:PRK05159 343 ----EDDPE--ISKSFDLLFRGLEITSGGQRIHRYDMLVESIKEKGLN----PESFEFYLEAFKYGMPPHGGFGLGLERL 412
|
570
....*....|....*..
gi 15596160 540 VMLMTGASSIREVIAFP 556
Cdd:PRK05159 413 TMKLLGLENIREAVLFP 429
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
141-558 |
1.24e-87 |
|
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: 272.81 E-value: 1.24e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 141 LKLRARITSSIRRYLDDNGFLDVETPILGRPTP-EGARDYLVPSRTyPGHFFALPQSPQLFKQLLMVAGFDRYYQIAKCF 219
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGgAGARPFLVKYNA-LGLDYYLRISPQLFKKRLMVGGLDRVFEINRNF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 220 RDEDLRADRQPEFTQIDIETSFLDESDIIGITEKMVRQLFKEVLDVEFDE-----------FPHMPFEEAMRRYGsdkpd 288
Cdd:cd00669 80 RNEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTygfeledfglpFPRLTYREALERYG----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 289 lriplelvdvadqlkevefkvfsgpandpkgrvaalrvpgaasmprsqiddytkfvgiygakglayikvnerakgveglq 368
Cdd:cd00669 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 369 spivkfipeanlnvildrvgavdgdivffgadkakivcdalgalrikvghdlklltrewAPMWVVDFPMFeenddgslsa 448
Cdd:cd00669 155 -----------------------------------------------------------QPLFLTDYPAE---------- 165
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 449 LHHPFTSPKctpaelEANPgaALSRAYDMVLNGTELGGGSIRIHDKSMQQAVFRVLGIDEAEQEEKFGFLLDALKYGAPP 528
Cdd:cd00669 166 MHSPLASPH------DVNP--EIADAFDLFINGVEVGNGSSRLHDPDIQAEVFQEQGINKEAGMEYFEFYLKALEYGLPP 237
|
410 420 430
....*....|....*....|....*....|
gi 15596160 529 HGGLAFGLDRLVMLMTGASSIREVIAFPKT 558
Cdd:cd00669 238 HGGLGIGIDRLIMLMTNSPTIREVIAFPKM 267
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
3-558 |
6.24e-78 |
|
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: 253.05 E-value: 6.24e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 3 RSHYCGQLNESLDGQEVTLCGWVHRRRDHGGVIFLDVRDREGLAQVVFDPDRAETFAKADRVRSEFVVKITGKVRLRPEg 82
Cdd:COG0017 1 KRTYIKDLLPEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKLENFEEAKKLTTESSVEVTGTVVESPR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 83 arnpnmASGSIEVLGYELEVLNQAETpPFPLDEySDVGEETRLRYRFIDLRRPEMAAKLKLRARITSSIRRYLDDNGFLD 162
Cdd:COG0017 80 ------APQGVELQAEEIEVLGEADE-PYPLQP-KRHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 163 VETPILgrpTP---EGArdylvpSRTYPGHFFA----LPQSPQLFKQlLMVAGFDRYYQIAKCFRDEDLRADRQ-PEFTQ 234
Cdd:COG0017 152 VHTPII---TAsatEGG------GELFPVDYFGkeayLTQSGQLYKE-ALAMALEKVYTFGPTFRAEKSNTRRHlAEFWM 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 235 IDIETSFLDESDIIGITEKMVRQLFKEVLDvefdefphmpfeeamrrygsdkpdlriplelvDVADQLKEVEFkvfsgpa 314
Cdd:COG0017 222 IEPEMAFADLEDVMDLAEEMLKYIIKYVLE--------------------------------NCPEELEFLGR------- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 315 ndpkgRVAALRVPGAASMPRsqIdDYTKFVGIYGAKGLAyikvnerakgveglqspivkfipeanlnvildrvgavdgdi 394
Cdd:COG0017 263 -----DVERLEKVPESPFPR--I-TYTEAIEILKKSGEK----------------------------------------- 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 395 VFFGADkakivcdaLGAlrikvgHDLKLLTrEWA---PMWVVDFPM----F--EENDDGslsalhhpftsPKctpaelea 465
Cdd:COG0017 294 VEWGDD--------LGT------EHERYLG-EEFfkkPVFVTDYPKeikaFymKPNPDD-----------PK-------- 339
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 466 npgaaLSRAYDMVLNGT-ELGGGSIRIHDKSMQQAVFRVLGIDeaeqEEKFGFLLDALKYGAPPHGGLAFGLDRLVMLMT 544
Cdd:COG0017 340 -----TVAAFDLLAPGIgEIIGGSQREHRYDVLVERIKEKGLD----PEDYEWYLDLRRYGSVPHAGFGLGLERLVMWLT 410
|
570
....*....|....
gi 15596160 545 GASSIREVIAFPKT 558
Cdd:COG0017 411 GLENIREVIPFPRD 424
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
3-137 |
6.57e-77 |
|
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: 239.73 E-value: 6.57e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 3 RSHYCGQLNESLDGQEVTLCGWVHRRRDHGGVIFLDVRDREGLAQVVFDPDRAETFAKADRVRSEFVVKITGKVRLRPEG 82
Cdd:cd04317 1 RTHYCGELRESHVGQEVTLCGWVQRRRDHGGLIFIDLRDRYGIVQVVFDPEEAPEFELAEKLRNESVIQVTGKVRARPEG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 15596160 83 ARNPNMASGSIEVLGYELEVLNQAETPPFPLDEYSDVGEETRLRYRFIDLRRPEM 137
Cdd:cd04317 81 TVNPKLPTGEIEVVASELEVLNKAKTLPFEIDDDVNVSEELRLKYRYLDLRRPKM 135
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
118-558 |
5.72e-45 |
|
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: 161.97 E-value: 5.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 118 DVGEETRLRYRFIDLRRPEMAAKLKLRARITSSIRRYLDDNGFLDVETPILGRPTPEGardylvPSRTYPGHFFA----L 193
Cdd:cd00776 1 DANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEG------GAELFKVSYFGkpayL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 194 PQSPQLFKQlLMVAGFDRYYQIAKCFRDEDLRADRQ-PEFTQIDIETSFL-DESDIIGITEKMVRQLFKEVLDVEFDEfp 271
Cdd:cd00776 75 AQSPQLYKE-MLIAALERVYEIGPVFRAEKSNTRRHlSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAKE-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 272 hmpfEEAMRRYGSDKPDLRIPlelvdvadqlkeveFKVFSgpandpkgrvaalrvpgaasmprsqiddYTKFVGIYGAKG 351
Cdd:cd00776 152 ----LELVNQLNRELLKPLEP--------------FPRIT----------------------------YDEAIELLREKG 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 352 layiKVNERAKGvEGLQSPIVKFIpeanlnvildrVGAVDGDIVFfgadkakivcdalgalrikvghdlklltrewapmw 431
Cdd:cd00776 186 ----VEEEVKWG-EDLSTEHERLL-----------GEIVKGDPVF----------------------------------- 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 432 VVDFPmfeenddgslsALHHPFTSPKCtpaelEANPGaaLSRAYDMVLNGT-ELGGGSIRIHDKSMQQAVFRVLGIDeae 510
Cdd:cd00776 215 VTDYP-----------KEIKPFYMKPD-----DDNPE--TVESFDLLMPGVgEIVGGSQRIHDYDELEERIKEHGLD--- 273
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 15596160 511 qEEKFGFLLDALKYGAPPHGGLAFGLDRLVMLMTGASSIREVIAFPKT 558
Cdd:cd00776 274 -PESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFPRD 320
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
3-556 |
9.55e-40 |
|
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: 151.73 E-value: 9.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 3 RSHYCGQL--------NESLDGQEVTLCGWVHRRRDHGGVIFLDVRDREGLAQVVFDPDR-----AETFAKADRvrSEFV 69
Cdd:COG1190 35 RTHTAAEIrekydeleAEEETGDEVSVAGRIMAKRDMGKASFADLQDGSGRIQLYLRRDElgeeaYELFKLLDL--GDIV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 70 VkITGKV-RLRpegarnpnmaSGSIEVLGYELEVLNQAETPPfPlDEY---SDVgeETRLRYRFIDL-RRPEMAAKLKLR 144
Cdd:COG1190 113 G-VEGTVfRTK----------TGELSVKVEELTLLSKSLRPL-P-EKFhglTDP--ETRYRQRYVDLiVNPEVRETFRKR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 145 ARITSSIRRYLDDNGFLDVETPILGrPTPEGA--RdylvPSRTypgHFFALPQ------SPQLF-KQLLmVAGFDRYYQI 215
Cdd:COG1190 178 SKIIRAIRRFLDERGFLEVETPMLQ-PIAGGAaaR----PFIT---HHNALDMdlylriAPELYlKRLI-VGGFERVFEI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 216 AKCFRDEDLRADRQPEFTQIDIETSFLDESDIIGITEKMVRQLFKEVL--------DVEFD---EFPHMPFEEAMRRYGS 284
Cdd:COG1190 249 GRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLgttkvtyqGQEIDlspPWRRITMVEAIKEATG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 285 dkpdlriplelVDVaDQLKEVEFkvfsgpandpkgrvaalrvpgaasmprsqiddytkfvgiygAKGLAyikvneRAKGV 364
Cdd:COG1190 329 -----------IDV-TPLTDDEE-----------------------------------------LRALA------KELGI 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 365 EglqspiVKfiPEANLNVILDrvgavdgdiVFFGAdkakivcdalgalriKVGHDLklltreWAPMWVVDFPmfeenddg 444
Cdd:COG1190 350 E------VD--PGWGRGKLID---------ELFEE---------------LVEPKL------IQPTFVTDYP-------- 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 445 slsalhhPFTSPKCTPAEleANPGaaLSRAYDMVLNGTELGGG-S-----IRIHDKSMQQAVFRVLGIDEAEQ-EEKFgf 517
Cdd:COG1190 384 -------VEVSPLAKRHR--DDPG--LTERFELFIAGREIANAfSelndpIDQRERFEEQLELKAAGDDEAMPmDEDF-- 450
|
570 580 590
....*....|....*....|....*....|....*....
gi 15596160 518 lLDALKYGAPPHGGLAFGLDRLVMLMTGASSIREVIAFP 556
Cdd:COG1190 451 -LRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 488
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
3-556 |
8.48e-37 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 144.36 E-value: 8.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 3 RSHYCGQLNE---------SLDGQEVTLCGWVHRRRDHGGVIFLDVRDREGLAQVVFDPDRA----ETFAK-ADRVRSEF 68
Cdd:PLN02502 86 VTHTAPELQEkygslengeELEDVSVSVAGRIMAKRAFGKLAFYDLRDDGGKIQLYADKKRLdldeEEFEKlHSLVDRGD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 69 VVKITGKVRlRPEgarnpnmaSGSIEVLGYELEVLnqaeTP---PFPlDEYS---DVgeETRLRYRFIDL-RRPEMAAKL 141
Cdd:PLN02502 166 IVGVTGTPG-KTK--------KGELSIFPTSFEVL----TKcllMLP-DKYHgltDQ--ETRYRQRYLDLiANPEVRDIF 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 142 KLRARITSSIRRYLDDNGFLDVETPIL-GRPTPEGARdylvPSRTYP---GHFFALPQSPQLFKQLLMVAGFDRYYQIAK 217
Cdd:PLN02502 230 RTRAKIISYIRRFLDDRGFLEVETPMLnMIAGGAAAR----PFVTHHndlNMDLYLRIATELHLKRLVVGGFERVYEIGR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 218 CFRDEDLRADRQPEFTQIDIETSFLDESDIIGITEKMVRQLFKEVldvefdefphmpFEEAMRRYGSDKPDLRIPLELVD 297
Cdd:PLN02502 306 QFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKEL------------TGSYKIKYHGIEIDFTPPFRRIS 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 298 VADQLKEvefkvfsgpandpkgrVAALRVPGAASMPRSqiddytkfvgiygakglayikvneRAKGVEGLQSPIVKFIPE 377
Cdd:PLN02502 374 MISLVEE----------------ATGIDFPADLKSDEA------------------------NAYLIAACEKFDVKCPPP 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 378 ANLNVILDRVgavdgdivfFGAdkakiVCDAlgalrikvghdlKLLTrewaPMWVVDFPmfEEnddgsLSALHHPFTSpk 457
Cdd:PLN02502 414 QTTGRLLNEL---------FEE-----FLEE------------TLVQ----PTFVLDHP--VE-----MSPLAKPHRS-- 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 458 ctpaeleaNPGaaLSRAYDMVLNGTELGGGSIRIHDKSMQ------QAVFRVLGIDEA-EQEEKFgflLDALKYGAPPHG 530
Cdd:PLN02502 455 --------KPG--LTERFELFINGRELANAFSELTDPVDQrerfeeQVKQHNAGDDEAmALDEDF---CTALEYGLPPTG 521
|
570 580
....*....|....*....|....*.
gi 15596160 531 GLAFGLDRLVMLMTGASSIREVIAFP 556
Cdd:PLN02502 522 GWGLGIDRLVMLLTDSASIRDVIAFP 547
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
3-556 |
2.67e-36 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 141.77 E-value: 2.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 3 RSHYCGQLNESLDGQE----------VTLCGWVHRRRDHGGVIFLDVRDREGLAQVVFDPDR-----AETFAKADRvrSE 67
Cdd:PRK00484 31 RTHTAAELRAKYDDKEkeeleeleieVSVAGRVMLKRVMGKASFATLQDGSGRIQLYVSKDDvgeeaLEAFKKLDL--GD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 68 FVVkITGKVrlrpegarnpnMASG----SIEVLgyELEVLNQAETP-PFPLDEYSDVgeETRLRYRFIDL-RRPEMAAKL 141
Cdd:PRK00484 109 IIG-VEGTL-----------FKTKtgelSVKAT--ELTLLTKSLRPlPDKFHGLTDV--ETRYRQRYVDLiVNPESRETF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 142 KLRARITSSIRRYLDDNGFLDVETPILgRPTPEG--ARdylvPSRTypgHFFALPQ------SPQLF-KQLLmVAGFDRY 212
Cdd:PRK00484 173 RKRSKIISAIRRFLDNRGFLEVETPML-QPIAGGaaAR----PFIT---HHNALDIdlylriAPELYlKRLI-VGGFERV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 213 YQIAKCFRDEDLRADRQPEFTQIDIETSFLDESDIIGITEKMVRQLFKEVL--------DVEFD---EFPHMPFEEAMRR 281
Cdd:PRK00484 244 YEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLgttkvtyqGTEIDfgpPFKRLTMVDAIKE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 282 YGSDKPDLRIPLELVDVADQLKeVEFKVFSGpandpKGRVaalrvpgaasmprsqiddytkfvgiygakglayikVNEra 361
Cdd:PRK00484 324 YTGVDFDDMTDEEARALAKELG-IEVEKSWG-----LGKL-----------------------------------INE-- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 362 kgveglqspivkfipeanlnvildrvgavdgdivFFGAdkakivcdalgalriKVGHDLklltreWAPMWVVDFPmfEEn 441
Cdd:PRK00484 361 ----------------------------------LFEE---------------FVEPKL------IQPTFITDYP--VE- 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 442 ddgslsalhhpfTSPKCTPaeLEANPGaaLSRAYDMVLNGTELGGG------SIRIHDKSMQQAVFRVLGIDEAEQ-EEK 514
Cdd:PRK00484 383 ------------ISPLAKR--HREDPG--LTERFELFIGGREIANAfselndPIDQRERFEAQVEAKEAGDDEAMFmDED 446
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 15596160 515 FgflLDALKYGAPPHGGLAFGLDRLVMLMTGASSIREVIAFP 556
Cdd:PRK00484 447 F---LRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| GAD |
pfam02938 |
GAD domain; This domain is found in some members of the GatB and aspartyl tRNA synthetases. |
310-409 |
1.31e-34 |
|
GAD domain; This domain is found in some members of the GatB and aspartyl tRNA synthetases.
Pssm-ID: 397199 [Multi-domain] Cd Length: 94 Bit Score: 125.84 E-value: 1.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 310 FSGPANdPKGRVAALRVPGAASMPRSQIDDYTKFVGIYGAKGLAYIKVNErakgvEGLQSPIVKFIPEANLNVILDRVGA 389
Cdd:pfam02938 1 FSEALK-SGGSVKALRVPGAAGLSRKEIDELERFAKEYGAKGLAWIKVEG-----GGHTGPIAKFLTEEEVEKLLEAVGA 74
|
90 100
....*....|....*....|
gi 15596160 390 VDGDIVFFGADKAKIVCDAL 409
Cdd:pfam02938 75 EDGDALLFVADKKKTVNKAL 94
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
10-558 |
2.59e-33 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 132.54 E-value: 2.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 10 LNESLDGQEVTLCGWVHRRRDHGGVIFLDVRDREGLAQ-VVFDPDRAETFAKADRVRSEFVVKITGKVRLRPEgarnpnm 88
Cdd:PRK03932 10 LKGKYVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFKQlQVVKDNGEEYFEEIKKLTTGSSVIVTGTVVESPR------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 89 ASGSIEVLGYELEVLnQAETPPFPL--DEYSDvgeETRLRYRFIDLRRPEMAAKLKLRARITSSIRRYLDDNGFLDVETP 166
Cdd:PRK03932 83 AGQGYELQATKIEVI-GEDPEDYPIqkKRHSI---EFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVDTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 167 ILGRPTPEGARD-YLVPSR--TYPGHFFA----LPQSPQLFKQLLMVAgFDRYYQIAKCFRDEDLRADRQ-PEFTQIDIE 238
Cdd:PRK03932 159 IITASDCEGAGElFRVTTLdlDFSKDFFGkeayLTVSGQLYAEAYAMA-LGKVYTFGPTFRAENSNTRRHlAEFWMIEPE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 239 TSFLDESDIIGITEKMVRQLFKEVL-----DVEFdefphmpFEEamrrygsdkpdlRIPLELVDVADQLKEVEFKvfsgp 313
Cdd:PRK03932 238 MAFADLEDNMDLAEEMLKYVVKYVLencpdDLEF-------LNR------------RVDKGDIERLENFIESPFP----- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 314 andpkgRVaalrvpgaasmprsqidDYTkfvgiygakglayikvneraKGVEGLQSPIVKFIpeanlnvildrvgavdgD 393
Cdd:PRK03932 294 ------RI-----------------TYT--------------------EAIEILQKSGKKFE-----------------F 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 394 IVFFGADkakivcdaLGAlrikvGHDlKLLTREW--APMWVVDFP-------MfEENDDGSLSAlhhpftspkctpaele 464
Cdd:PRK03932 314 PVEWGDD--------LGS-----EHE-RYLAEEHfkKPVFVTNYPkdikafyM-RLNPDGKTVA---------------- 362
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 465 anpgaalsrAYDMVLNGT-ELGGGSIRIHDKSMQQAVFRVLGIDeaeqEEKFGFLLDALKYGAPPHGGLAFGLDRLVMLM 543
Cdd:PRK03932 363 ---------AMDLLAPGIgEIIGGSQREERLDVLEARIKELGLN----KEDYWWYLDLRRYGSVPHSGFGLGFERLVAYI 429
|
570
....*....|....*
gi 15596160 544 TGASSIREVIAFPKT 558
Cdd:PRK03932 430 TGLDNIRDVIPFPRT 444
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
8-557 |
7.77e-33 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 132.52 E-value: 7.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 8 GQLNESLDGQEVTLCGWVHRRRDHGGVIFLDVRDREGLAQVVFDPDRAETFAK----ADRVRSEFVVKITGKVRLRPEGA 83
Cdd:PLN02850 73 SDLGEELAGSEVLIRGRVHTIRGKGKSAFLVLRQSGFTVQCVVFVSEVTVSKGmvkyAKQLSRESVVDVEGVVSVPKKPV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 84 RNpnmASGSIEVLGYELEVLNQAETP-PFPLD-----------------EYSDVGEETRLRYRFIDLRRPEMAAKLKLRA 145
Cdd:PLN02850 153 KG---TTQQVEIQVRKIYCVSKALATlPFNVEdaarseseiekalqtgeQLVRVGQDTRLNNRVLDLRTPANQAIFRIQS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 146 RITSSIRRYLDDNGFLDVETPILGRPTPEGARDylVPSRTYPGHFFALPQSPQLFKQLLMVAGFDRYYQIAKCFRDEDLR 225
Cdd:PLN02850 230 QVCNLFREFLLSKGFVEIHTPKLIAGASEGGSA--VFRLDYKGQPACLAQSPQLHKQMAICGDFRRVFEIGPVFRAEDSF 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 226 ADRQ-PEFTQIDIETSfldesdiigitekmVRQLFKEVLDVEFDEFPHMpFEEAMRRYGSdkpdlriplELVDVADQLke 304
Cdd:PLN02850 308 THRHlCEFTGLDLEME--------------IKEHYSEVLDVVDELFVAI-FDGLNERCKK---------ELEAIREQY-- 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 305 vefkvfsgPANDPKGRVAALRvpgaasmprsqiddytkfvgiygakgLAYikvnerAKGVEGLQSPIVKFIPEANLNVIL 384
Cdd:PLN02850 362 --------PFEPLKYLPKTLR--------------------------LTF------AEGIQMLKEAGVEVDPLGDLNTES 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 385 DRvgavdgdivffgadkakivcdALGAL-RIKVGHDLKLLTRewapmwvvdFPmfeenddgslSALhHPFTSPKCtpael 463
Cdd:PLN02850 402 ER---------------------KLGQLvKEKYGTDFYILHR---------YP----------LAV-RPFYTMPC----- 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 464 EANPgaALSRAYDMVLNGTELGGGSIRIHDKSMQQAVFRVLGIDeaeqEEKFGFLLDALKYGAPPHGGLAFGLDRLVMLM 543
Cdd:PLN02850 436 PDDP--KYSNSFDVFIRGEEIISGAQRVHDPELLEKRAEECGID----VKTISTYIDSFRYGAPPHGGFGVGLERVVMLF 509
|
570
....*....|....
gi 15596160 544 TGASSIREVIAFPK 557
Cdd:PLN02850 510 CGLNNIRKTSLFPR 523
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
135-556 |
4.84e-31 |
|
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: 123.46 E-value: 4.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 135 PEMAAKLKLRARITSSIRRYLDDNGFLDVETPILgRPTPEGARdylvpSRTYPGHFFALPQ------SPQLFKQLLMVAG 208
Cdd:cd00775 2 EEVRQTFIVRSKIISYIRKFLDDRGFLEVETPML-QPIAGGAA-----ARPFITHHNALDMdlylriAPELYLKRLIVGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 209 FDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFLDESDIIGITEKMVRQLFKEVldvefdefpHMPFEeamRRYGSDKPD 288
Cdd:cd00775 76 FERVYEIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKI---------NGKTK---IEYGGKELD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 289 LRIPLELVDVADQLKEVEFKVFSGPANDpkgrvaalrvpgaasmprsQIDDYTKFVGIYGAKglayikvnerakgveglq 368
Cdd:cd00775 144 FTPPFKRVTMVDALKEKTGIDFPELDLE-------------------QPEELAKLLAKLIKE------------------ 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 369 spivKFIPEANLNVILDRVgavdgdivfFGadkakivcdalgalrIKVGHDLklltreWAPMWVVDFPMfeenddgSLSA 448
Cdd:cd00775 187 ----KIEKPRTLGKLLDKL---------FE---------------EFVEPTL------IQPTFIIDHPV-------EISP 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 449 L--HHPftspkctpaeleANPGaaLSRAYDMVLNGTELGGGSIRIHD------KSMQQAVFRVLGIDEA-EQEEKFgflL 519
Cdd:cd00775 226 LakRHR------------SNPG--LTERFELFICGKEIANAYTELNDpfdqreRFEEQAKQKEAGDDEAmMMDEDF---V 288
|
410 420 430
....*....|....*....|....*....|....*..
gi 15596160 520 DALKYGAPPHGGLAFGLDRLVMLMTGASSIREVIAFP 556
Cdd:cd00775 289 TALEYGMPPTGGLGIGIDRLVMLLTDSNSIRDVILFP 325
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
18-105 |
5.24e-31 |
|
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: 115.74 E-value: 5.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 18 EVTLCGWVHRRRDHGGVIFLDVRDREGLAQVVFDPDRA-ETFAKADRVRSEFVVKITGKVRLRPEGarnpNMASGSIEVL 96
Cdd:cd04100 1 EVTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEELgEFFEEAEKLRTESVVGVTGTVVKRPEG----NLATGEIELQ 76
|
....*....
gi 15596160 97 GYELEVLNQ 105
Cdd:cd04100 77 AEELEVLSK 85
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
3-556 |
2.42e-30 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 127.00 E-value: 2.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 3 RSHYCGQLNESLDGQEVTLCGWVHRRRDHGGVIFLDVRDREGLAQVVFDPDRAETFAKADRvRSEF----VVKITGKVrl 78
Cdd:PRK02983 638 PTHTVAEALDAPTGEEVSVSGRVLRIRDYGGVLFADLRDWSGELQVLLDASRLEQGSLADF-RAAVdlgdLVEVTGTM-- 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 79 rpeGARNpnmaSGSIEVLGYELEVLNQAETP-PFPLDEYSDVgeETRLRYRFIDLR-RPEMAAKLKLRARITSSIRRYLD 156
Cdd:PRK02983 715 ---GTSR----NGTLSLLVTSWRLAGKCLRPlPDKWKGLTDP--EARVRQRYLDLAvNPEARDLLRARSAVVRAVRETLV 785
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 157 DNGFLDVETPILgrPTPEG---ARDYLVPSRTYPGHFFaLPQSPQLFKQLLMVAGFDRYYQIAKCFRDEDLRADRQPEFT 233
Cdd:PRK02983 786 ARGFLEVETPIL--QQVHGganARPFVTHINAYDMDLY-LRIAPELYLKRLCVGGVERVFELGRNFRNEGVDATHNPEFT 862
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 234 QIDIETSFLDESDIIGITEKMVRqlfkevldvefdefphmpfEEAMRRYGSD---KPDLRIPLELVDVADqlkevEFKVf 310
Cdd:PRK02983 863 LLEAYQAHADYDTMRDLTRELIQ-------------------NAAQAAHGAPvvmRPDGDGVLEPVDISG-----PWPV- 917
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 311 sgpandpkgrvaalrvpgaasmprsqiddytkfVGIYGAkglayikVNErAKGVEglqspIVKFIPEANLNVILDRVG-A 389
Cdd:PRK02983 918 ---------------------------------VTVHDA-------VSE-ALGEE-----IDPDTPLAELRKLCDAAGiP 951
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 390 VDgdivfFGADKAKIVCDALGALrikVGHdlklltREWAPMWVVDFPMfeenddgSLSalhhPFTSPKctpaelEANPGa 469
Cdd:PRK02983 952 YR-----TDWDAGAVVLELYEHL---VED------RTTFPTFYTDFPT-------SVS----PLTRPH------RSDPG- 999
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 470 aLSRAYDMVLNGTELGGG----------SIRIHDKSMQQAvfrvlGID-EA-EQEEKFgflLDALKYGAPPHGGLAFGLD 537
Cdd:PRK02983 1000 -LAERWDLVAWGVELGTAyseltdpveqRRRLTEQSLLAA-----GGDpEAmELDEDF---LQALEYAMPPTGGLGMGVD 1070
|
570
....*....|....*....
gi 15596160 538 RLVMLMTGAsSIREVIAFP 556
Cdd:PRK02983 1071 RLVMLLTGR-SIRETLPFP 1088
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
5-114 |
6.13e-27 |
|
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: 105.09 E-value: 6.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 5 HYCGQLNESLDGQEVTLCGWVHRRRDHGGVIFLDVRDREGLAQVVF--DPDRAETFAKADRVRSEFVVKITGKVRLRPEg 82
Cdd:cd04316 1 HYSAEITPELDGEEVTVAGWVHEIRDLGGIKFVILRDREGIVQVTApkKKVDKELFKTVRKLSRESVISVTGTVKAEPK- 79
|
90 100 110
....*....|....*....|....*....|..
gi 15596160 83 arnpnmASGSIEVLGYELEVLNQAETPPfPLD 114
Cdd:cd04316 80 ------APNGVEIIPEEIEVLSEAKTPL-PLD 104
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
19-556 |
1.10e-25 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 111.66 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 19 VTLCGWVHRRRDHGGVIFLDVRDREGLAQVVFDPdrAETFAKADRVRSEFVVKITGKVRLRPEGARnpnMASGSIEVLGY 98
Cdd:PTZ00385 110 VRVAGRVTSVRDIGKIIFVTIRSNGNELQVVGQV--GEHFTREDLKKLKVSLRVGDIIGADGVPCR---MQRGELSVAAS 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 99 ELEVL------NQAETPP---FPLDEYSDVgeetRLRYRFIDL-RRPEMAAKLKLRARITSSIRRYLDDNGFLDVETPIL 168
Cdd:PTZ00385 185 RMLILspyvctDQVVCPNlrgFTVLQDNDV----KYRYRFTDMmTNPCVIETIKKRHVMLQALRDYFNERNFVEVETPVL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 169 GR-PTPEGARDYLVPSRTYPGHFFaLPQSPQLFKQLLMVAGFDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFLDESDI 247
Cdd:PTZ00385 261 HTvASGANAKSFVTHHNANAMDLF-LRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTSCEFYAAYHTYEDL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 248 IGITEKMVRQLF-----KEVLDVEFDEFPHMPFEeamrrygsdkPDLRIPLELVDVADQLKE---VEFKvfsgPANDpkg 319
Cdd:PTZ00385 340 MPMTEDIFRQLAmrvngTTVVQIYPENAHGNPVT----------VDLGKPFRRVSVYDEIQRmsgVEFP----PPNE--- 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 320 rvaaLRVPgaasmprsqiddytkfvgiygaKGLAYikvnerakgveglqspivkfipeanLNVILDRVgavdgDIVFFGA 399
Cdd:PTZ00385 403 ----LNTP----------------------KGIAY-------------------------MSVVMLRY-----NIPLPPV 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 400 DKAKIVCDALgalrikvgHDLKLLTREWAPMWVVDFPMfeenddgslsalhhpFTSPkcTPAELEANPGaaLSRAYDMVL 479
Cdd:PTZ00385 427 RTAAKMFEKL--------IDFFITDRVVEPTFVMDHPL---------------FMSP--LAKEQVSRPG--LAERFELFV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 480 NGTELGGGSIRIHD------KSMQQAVFRVLGIDEA-EQEEKFgflLDALKYGAPPHGGLAFGLDRLVMLMTGASSIREV 552
Cdd:PTZ00385 480 NGIEYCNAYSELNDpheqyhRFQQQLVDRQGGDEEAmPLDETF---LKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDG 556
|
....
gi 15596160 553 IAFP 556
Cdd:PTZ00385 557 IIFP 560
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
90-557 |
1.15e-25 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 111.24 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 90 SGSIEVLGYELEVLNQAETppfplDEYSDVGEETRLRYRFIDLRRPEMAAKLKLRARITSSIRRYLDDNGFLDVETP-IL 168
Cdd:PTZ00401 167 TESLRTLPFTLEDASRKES-----DEGAKVNFDTRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLIDSDFCEIHSPkII 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 169 GRPTPEGARDYLVpsrTYPGHFFALPQSPQLFKQLLMVAGFDRYYQIAKCFRDEDLRADRQ-PEFTQIDIETSfldesdi 247
Cdd:PTZ00401 242 NAPSEGGANVFKL---EYFNRFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNTHRHlTEFVGLDVEMR------- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 248 igitekmVRQLFKEVLDVEFDEFPHMpFEEAMRRYGSDKPDLRI----PLELVDVADQLKEVEFKVFSG---PANDPKGR 320
Cdd:PTZ00401 312 -------INEHYYEVLDLAESLFNYI-FERLATHTKELKAVCQQypfePLVWKLTPERMKELGVGVISEgvePTDKYQAR 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 321 VAALrvpgaasmprsqiddytkfvgiygakGLAYIKVNerakgveglqspivkfIPE--ANLNVILDRVGAVDGDIvffG 398
Cdd:PTZ00401 384 VHNM--------------------------DSRMLRIN----------------YMHciELLNTVLEEKMAPTDDI---N 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 399 ADKAKIvcdaLGAL-RIKVGHDLKLLTRewapmwvvdFPmfeenddgslsALHHPFTSPKCTPAELEANpgaalsrAYDM 477
Cdd:PTZ00401 419 TTNEKL----LGKLvKERYGTDFFISDR---------FP-----------SSARPFYTMECKDDERFTN-------SYDM 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 478 VLNGTELGGGSIRIHDKSMQQAVFRVLGIDEAEQEEkfgfLLDALKYGAPPHGGLAFGLDRLVMLMTGASSIREVIAFPK 557
Cdd:PTZ00401 468 FIRGEEISSGAQRIHDPDLLLARAKMLNVDLTPIKE----YVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFPR 543
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
3-556 |
1.23e-22 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 101.68 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 3 RSHYCGQLNESLDGQ----------EVTLCGWVHRRRDHGGVIFLDVRDREGLAQVVFDPDRAETFAKADRVRSEFVVKI 72
Cdd:PRK12445 42 RDHTSDQLHEEFDAKdnqeleslniEVSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEGVYNDQFKKWDLGDI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 73 TGkvrlrpegARNP--NMASGSIEVLGYELEVLNQAeTPPFPLDEYSDVGEETRLRYRFIDLRRPEMAAK-LKLRARITS 149
Cdd:PRK12445 122 IG--------ARGTlfKTQTGELSIHCTELRLLTKA-LRPLPDKFHGLQDQEVRYRQRYLDLIANDKSRQtFVVRSKILA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 150 SIRRYLDDNGFLDVETPILgRPTPEGARdylvpSRTYPGHFFALPQ------SPQLFKQLLMVAGFDRYYQIAKCFRDED 223
Cdd:PRK12445 193 AIRQFMVARGFMEVETPMM-QVIPGGAS-----ARPFITHHNALDLdmylriAPELYLKRLVVGGFERVFEINRNFRNEG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 224 LRADRQPEFTQIDIETSFLDESDIIGITEKMVRQLFKEVLDVEfdEFPhmpfeeamrrYGSDKPDLRIPLELVDVADQLK 303
Cdd:PRK12445 267 ISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTT--KVT----------YGEHVFDFGKPFEKLTMREAIK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 304 EVEfkvfsgpandpkgrvaalrvpgaasmPRSQIDDYTKFvgiYGAKGLAY---IKVnERAKGVEGLQSPIVKFIPEANL 380
Cdd:PRK12445 335 KYR--------------------------PETDMADLDNF---DAAKALAEsigITV-EKSWGLGRIVTEIFDEVAEAHL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 381 nvildrvgavdgdivffgadkakivcdalgalrikvghdlklltreWAPMWVVDFPmfeenddgslsalhhpftsPKCTP 460
Cdd:PRK12445 385 ----------------------------------------------IQPTFITEYP-------------------AEVSP 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 461 AELEANPGAALSRAYDMVLNGTELGGGSIRIHDKSMQQAVF------RVLGIDEAE-QEEKFgflLDALKYGAPPHGGLA 533
Cdd:PRK12445 400 LARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAERFqeqvnaKAAGDDEAMfYDEDY---VTALEYGLPPTAGLG 476
|
570 580
....*....|....*....|...
gi 15596160 534 FGLDRLVMLMTGASSIREVIAFP 556
Cdd:PRK12445 477 IGIDRMIMLFTNSHTIRDVILFP 499
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
143-272 |
1.69e-19 |
|
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: 87.17 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 143 LRARITSSIRRYLDDNGFLDVETPILGRPTPEGARD----YLVPSRTYPGHFFALPQSPQLFKQLLMV----AGFDRYYQ 214
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGhepkDLLPVGAENEEDLYLRPTLEPGLVRLFVshirKLPLRLAE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596160 215 IAKCFRDEDLRAD--RQPEFTQIDIETSFLDESDI------IGITEKMVRQLFKE-----VLDVEFDEFPH 272
Cdd:cd00768 81 IGPAFRNEGGRRGlrRVREFTQLEGEVFGEDGEEAsefeelIELTEELLRALGIKldivfVEKTPGEFSPG 151
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
122-561 |
2.21e-18 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 88.91 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 122 ETRLRYRFIDLRRPEMA-AKLKLRARITSSIRRYLDDNGFLDVETPILGR-PTPEGARDYLVPSRTYPGHFFaLPQSPQL 199
Cdd:PTZ00417 233 EIRYRQRYLDLMINESTrSTFITRTKIINYLRNFLNDRGFIEVETPTMNLvAGGANARPFITHHNDLDLDLY-LRIATEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 200 FKQLLMVAGFDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFLDESDIIGITEKMVRQLFKEVldvefdefphmpFEEAM 279
Cdd:PTZ00417 312 PLKMLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHL------------FGTYK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 280 RRYGSDKPDlRIPLEL--------VDVADQLKEVEFKVFSGPANDPkgrvaalrvpgaasmprsqiDDYTKFVGIygakg 351
Cdd:PTZ00417 380 ILYNKDGPE-KDPIEIdftppypkVSIVEELEKLTNTKLEQPFDSP--------------------ETINKMINL----- 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 352 layIKVNErakgVEgLQSPivkfiPEAnlnvildrvgavdgdivffgadkAKIVcDALGALRIKVGHDLKlltrewaPMW 431
Cdd:PTZ00417 434 ---IKENK----IE-MPNP-----PTA-----------------------AKLL-DQLASHFIENKYPNK-------PFF 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 432 VVDFPMFEenddgSLSALHHpftspkctpaelEANPGaaLSRAYDMVLNGTELGGGSIRIHDKSMQQAVFRVLGIDEaEQ 511
Cdd:PTZ00417 470 IIEHPQIM-----SPLAKYH------------RSKPG--LTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDR-EK 529
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 15596160 512 EEKFGFLLDA-----LKYGAPPHGGLAFGLDRLVMLMTGASSIREVIAFPKTQSA 561
Cdd:PTZ00417 530 GDAEAFQFDAafctsLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFPTMRPA 584
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
122-313 |
7.63e-18 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 85.07 E-value: 7.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 122 ETRLRYRFIDLRRPEMAAKLKLRARITSSIRRYLDDNGFLDVETPILGRPTPEGARD-----YLVPSRTYPGHFFALPQS 196
Cdd:PRK06462 11 EEFLRMSWKHISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIISPSTDPLMGLgsdlpVKQISIDFYGVEYYLADS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 197 PQLFKQLlMVAGFDRYYQIAKCFRDEDLRADRQP---EFTQIDIETSFLDESDIIGITEKMVRQLFKEVLDVEFDEFphm 273
Cdd:PRK06462 91 MILHKQL-ALRMLGKIFYLSPNFRLEPVDKDTGRhlyEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHEDEL--- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15596160 274 pfeeamRRYGSDKPDLRIPLELVDVADQLKEVEFKVFSGP 313
Cdd:PRK06462 167 ------EFFGRDLPHLKRPFKRITHKEAVEILNEEGCRGI 200
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
19-103 |
8.45e-16 |
|
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: 72.27 E-value: 8.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 19 VTLCGWVHR-RRDHGGVIFLDVRDREGLAQVVFDPDRAETFAKadRVRSEFVVKITGKVRLRPEgarnpnmasGSIEVLG 97
Cdd:pfam01336 1 VTVAGRVTSiRRSGGKLLFLTLRDGTGSIQVVVFKEEAEKLAK--KLKEGDVVRVTGKVKKRKG---------GELELVV 69
|
....*.
gi 15596160 98 YELEVL 103
Cdd:pfam01336 70 EEIELL 75
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
18-102 |
2.57e-14 |
|
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: 68.41 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 18 EVTLCGWVHRRRDHGGVIFLDVRDREGLAQVVFDPDRAETFAKADRVRSEFVVKITGKVRLRPEGARNPNmasgsievlG 97
Cdd:cd04323 1 RVKVFGWVHRLRSQKKLMFLVLRDGTGFLQCVLSKKLVTEFYDAKSLTQESSVEVTGEVKEDPRAKQAPG---------G 71
|
....*
gi 15596160 98 YELEV 102
Cdd:cd04323 72 YELQV 76
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
18-128 |
3.43e-12 |
|
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: 62.93 E-value: 3.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 18 EVTLCGWVHRRRDHGGVIFLDVRDREGLAQVVFDPDRA-ETFAKADRVRSEFVVKITGKVRLRPEgarnpnmASGSIEVL 96
Cdd:cd04319 1 KVTLAGWVYRKREVGKKAFIVLRDSTGIVQAVFSKDLNeEAYREAKKVGIESSVIVEGAVKADPR-------APGGAEVH 73
|
90 100 110
....*....|....*....|....*....|..
gi 15596160 97 GYELEVLNQAEtpPFPLDEysDVGEETRLRYR 128
Cdd:cd04319 74 GEKLEIIQNVE--FFPITE--DASDEFLLDVR 101
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
154-554 |
1.60e-11 |
|
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous to the C-terminal region of lysyl-tRNA synthetase (LysS). Multiple sequence alignment of these proteins with the homologous regions of collected LysS proteins shows that these proteins form a distinct set rather than just similar truncations of LysS. The protein is termed GenX after its designation in E. coli. Interestingly, genX often is located near a homolog of lysine-2,3-aminomutase. Its function is unknown. [Unknown function, General]
Pssm-ID: 273090 [Multi-domain] Cd Length: 290 Bit Score: 65.26 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 154 YLDDNGFLDVETPILGR-PTPEGARDYLVPSRTYPG----HFFaLPQSPQLF-KQLLmVAGFDRYYQIAKCFRDEDLRAD 227
Cdd:TIGR00462 1 FFAERGVLEVETPLLSPaPVTDPHLDAFATEFVGPDgqgrPLY-LQTSPEYAmKRLL-AAGSGPIFQICKVFRNGERGRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 228 RQPEFTQIDIETSFLDESDIIGITEkmvrQLFKEVLDVEFDEFPHMPFEEAMRRYgsdkpdLRIplelvdvadqlkevef 307
Cdd:TIGR00462 79 HNPEFTMLEWYRPGFDYHDLMDEVE----ALLQELLGDPFAPAERLSYQEAFLRY------AGI---------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 308 kvfsgpanDPkgrvaalrvpgaASMPRSQIDDYTKFVGIYGAkglayikvnerakgveglqspivkfiPEANLNVILDRV 387
Cdd:TIGR00462 133 --------DP------------LTASLAELQAAAAAHGIRAS--------------------------EEDDRDDLLDLL 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 388 gavdgdIVFfgadkakIVCDALGALRikvghdlklltrewaPMWVVDFPmfeenddGSLSALhhpftspkctpAEL-EAN 466
Cdd:TIGR00462 167 ------FSE-------KVEPHLGFGR---------------PTFLYDYP-------ASQAAL-----------ARIsPDD 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 467 PGAAlsRAYDMVLNGTELGGGsirihdksmqqavFRVLgIDEAEQEEKF------------------GFLLDALKYGAPP 528
Cdd:TIGR00462 201 PRVA--ERFELYIKGLELANG-------------FHEL-TDAAEQRRRFeadnalrkalglprypldERFLAALEAGLPE 264
|
410 420
....*....|....*....|....*.
gi 15596160 529 HGGLAFGLDRLVMLMTGASSIREVIA 554
Cdd:TIGR00462 265 CSGVALGVDRLLMLALGADSIDDVLA 290
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
137-552 |
1.91e-09 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 59.17 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 137 MAAKLKLRARITSSIRRYLDDNGFLDVETPILGRPT---------------PEGA---RDYLVPSRTYpgHffalpqspq 198
Cdd:PRK09350 1 SIPNLLKRAKIIAEIRRFFADRGVLEVETPILSQATvtdihlvpfetrfvgPGASqgkTLWLMTSPEY--H--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 199 lFKQLLmVAGFDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFLDESDIIgiteKMVRQLFKEVLDVEfdEFPHMPFEEA 278
Cdd:PRK09350 70 -MKRLL-AAGSGPIFQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLM----NEVDDLLQQVLDCE--PAESLSYQQA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 279 MRRY-GSDkpdlriPLElvdvAD--QLKEVEFKV-FSGPANDpkgrvaalrvpgaasmprsQIDDYTKFVGIYgakglay 354
Cdd:PRK09350 142 FLRYlGID------PLS----ADktQLREVAAKLgLSNIADE-------------------EEDRDTLLQLLF------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 355 ikvnerAKGVeglqspivkfipEANLnvildrvgavdgdivffGADKakivcdalgalrikvghdlklltrewaPMWVVD 434
Cdd:PRK09350 186 ------TFGV------------EPNI-----------------GKEK---------------------------PTFVYH 203
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 435 FPmfeenddGSLSALhhpftspkctpAELEANPGAALSRaYDMVLNGTELGGGSIRIHDKSMQQAVFrvlgIDEAEQEEK 514
Cdd:PRK09350 204 FP-------ASQAAL-----------AKISTEDHRVAER-FEVYFKGIELANGFHELTDAREQRQRF----EQDNRKRAA 260
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 15596160 515 FGF--------LLDALKYGAPPHGGLAFGLDRLVMLMTGASSIREV 552
Cdd:PRK09350 261 RGLpqqpidenLIAALEAGLPDCSGVALGVDRLIMLALGAESISEV 306
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
8-563 |
1.29e-08 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 57.68 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 8 GQLNESLD--GQEVTLCGWVHRRRDHGGVIFLDVRDREGLA--QVVFDPDrAETFakaDRVRSEFV-----VKITGKVRL 78
Cdd:PLN02603 97 GGEDEGLArvGKTLNVMGWVRTLRAQSSVTFIEVNDGSCLSnmQCVMTPD-AEGY---DQVESGLIttgasVLVQGTVVS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 79 RPEGARNPNMASGSIEVLGyelevlnqAETPPFPLdeysdvgEETRLRYRFIDLR---RPE---MAAKLKLRARITSSIR 152
Cdd:PLN02603 173 SQGGKQKVELKVSKIVVVG--------KSDPSYPI-------QKKRVSREFLRTKahlRPRtntFGAVARVRNALAYATH 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 153 RYLDDNGFLDVETPILGRPTPEGARDY-----LVPSRTYPGH-------------------FFALPQ----SPQLFKQLL 204
Cdd:PLN02603 238 KFFQENGFVWVSSPIITASDCEGAGEQfcvttLIPNSAENGGslvddipktkdglidwsqdFFGKPAfltvSGQLNGETY 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 205 MVAGFDrYYQIAKCFRDEDLRADRQ-PEFTQIDIETSFLDESDIIGITEKMVRQLFKEVLD--VEFDEFPHMPFEEAMRR 281
Cdd:PLN02603 318 ATALSD-VYTFGPTFRAENSNTSRHlAEFWMIEPELAFADLNDDMACATAYLQYVVKYILEncKEDMEFFNTWIEKGIID 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 282 YGSDKPDLR-IPLELVDVADQL----KEVEFKVFSGpandpkgrvaalrvpgaasmprsqIDdytkfvgiygakglayik 356
Cdd:PLN02603 397 RLSDVVEKNfVQLSYTDAIELLlkakKKFEFPVKWG------------------------LD------------------ 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 357 vnerakgvegLQSPIVKFIPEanlnvildrvgavdgdiVFFGAdkakivcdalgalrikvghdlklltrewAPMWVVDFP 436
Cdd:PLN02603 435 ----------LQSEHERYITE-----------------EAFGG----------------------------RPVIIRDYP 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 437 ------MFEENDDGSLSAlhhpftspkctpaeleanpgaalsrAYDMVLNGT-ELGGGSIRIHDKSMQQAVFRVLGIDEa 509
Cdd:PLN02603 460 keikafYMRENDDGKTVA-------------------------AMDMLVPRVgELIGGSQREERLEYLEARLDELKLNK- 513
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 15596160 510 eqeEKFGFLLDALKYGAPPHGGLAFGLDRLVMLMTGASSIREVIAFPKTQSAGD 563
Cdd:PLN02603 514 ---ESYWWYLDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFPRVPGSAE 564
|
|
| ScAspRS_mt_like_N |
cd04321 |
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
18-105 |
1.17e-07 |
|
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: 49.62 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 18 EVTLCGWVHRRRD-HGGVIFLDVRDREG-LAQVVfDPDRAETFAKADRVRSEFVVKITGKVRLRPEGARNPNmasGSIEV 95
Cdd:cd04321 1 KVTLNGWIDRKPRiVKKLSFADLRDPNGdIIQLV-STAKKDAFSLLKSITAESPVQVRGKLQLKEAKSSEKN---DEWEL 76
|
90
....*....|
gi 15596160 96 LGYELEVLNQ 105
Cdd:cd04321 77 VVDDIQTLNA 86
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
18-103 |
4.39e-06 |
|
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli asparaginyl-tRNA synthetase (AsnRS) and, in Arabidopsis thaliana and Saccharomyces cerevisiae mitochondrial (mt) AsnRS. This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. S. cerevisiae mtAsnRS can charge E.coli tRNA with asparagines. Mutations in the gene for S. cerevisiae mtAsnRS has been found to induce a "petite" phenotype typical for a mutation in a nuclear gene that results in a non-functioning mitochondrial protein synthesis system.
Pssm-ID: 239813 [Multi-domain] Cd Length: 82 Bit Score: 44.86 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 18 EVTLCGWVHRRRDHGGVIFLDVRD---REGLaQVVFDPDrAETFAKADRVRSEFVVKITGKVRLRPEgarnpnmASGSIE 94
Cdd:cd04318 1 EVTVNGWVRSVRDSKKISFIELNDgscLKNL-QVVVDKE-LTNFKEILKLSTGSSIRVEGVLVKSPG-------AKQPFE 71
|
....*....
gi 15596160 95 VLGYELEVL 103
Cdd:cd04318 72 LQAEKIEVL 80
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
523-557 |
7.83e-06 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 48.87 E-value: 7.83e-06
10 20 30
....*....|....*....|....*....|....*
gi 15596160 523 KYGAPPHGGLAFGLDRLVMLMTGASSIREVIAFPK 557
Cdd:PTZ00425 545 KFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFPR 579
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
483-564 |
6.77e-05 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 45.76 E-value: 6.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 483 ELGGGSIRIHDKSMQQAVFRVLGIdeaeQEEKFGFLLDALKYGAPPHGGLAFGLDRLVMLMTGASSIREVIAFPKTQSAG 562
Cdd:PLN02221 495 ELIGGSQREERYDVIKQRIEEMGL----PIEPYEWYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPRYPGKA 570
|
..
gi 15596160 563 DV 564
Cdd:PLN02221 571 DL 572
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
511-558 |
2.37e-04 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 44.09 E-value: 2.37e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 15596160 511 QEEKFGFLLDALKYGAPPHGGLAFGLDRLVMLMTGASSIREVIAFPKT 558
Cdd:PLN02532 580 PREQYEWYLDLRRHGTVKHSGFSLGFELMVLFATGLPDVRDAIPFPRS 627
|
|
| tRNA-synt_2d |
pfam01409 |
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ... |
211-271 |
4.12e-03 |
|
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only phenylalanyl-tRNA synthetases. This is the core catalytic domain.
Pssm-ID: 396130 [Multi-domain] Cd Length: 245 Bit Score: 39.10 E-value: 4.12e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596160 211 RYYQIAKCFRDEDLRADRQPEFTQI-----DIETSFldeSDIIGITEKMVRQLFKEVLDVEFDE--FP 271
Cdd:pfam01409 104 KIFSIGRVFRRDQVDATHLPEFHQVeglvvDENVTF---ADLKGVLEEFLRKFFGFEVKVRFRPsyFP 168
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
136-238 |
4.23e-03 |
|
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. It is responsible for the attachment of histidine to the 3' OH group of ribose of the appropriate tRNA. This domain 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. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ. HisZ along with HisG catalyze the first reaction in histidine biosynthesis. HisZ is found only in a subset of bacteria and differs from HisRS in lacking a C-terminal anti-codon binding domain.
Pssm-ID: 238396 [Multi-domain] Cd Length: 261 Bit Score: 39.12 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596160 136 EMAAKLKLRARITSSIRRYlddnGFLDVETPIL-------GRPTPE-----------GARDY-LVPSRTYP-GHFFAlpQ 195
Cdd:cd00773 1 EAALRRYIEDTLREVFERY----GYEEIDTPVFeytelflRKSGDEvskemyrfkdkGGRDLaLRPDLTAPvARAVA--E 74
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 15596160 196 SPQLFKQLLmvagfdRYYQIAKCFRDEDLRADRQPEFTQIDIE 238
Cdd:cd00773 75 NLLSLPLPL------KLYYIGPVFRYERPQKGRYREFYQVGVE 111
|
|
| |
