|
Name |
Accession |
Description |
Interval |
E-value |
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
1-592 |
0e+00 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 1080.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 1 MLRTHLAGDLRADLAGSTVTLTGWVGRRRDHGGVIFIDMRDRSGYAQVVFR-NSEVAERAHHLRSEYCIQVTGVVEKRPE 79
Cdd:PRK00476 2 MMRTHYCGELRESHVGQTVTLCGWVHRRRDHGGLIFIDLRDREGIVQVVFDpDAEAFEVAESLRSEYVIQVTGTVRARPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 80 GSENPNLASGEIEVNVTELTILNESAALPFQLEDvgtSGTVGEEARLKYRYLDLRREGPAKIMRLRAAVNRAARKVLDSH 159
Cdd:PRK00476 82 GTVNPNLPTGEIEVLASELEVLNKSKTLPFPIDD---EEDVSEELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDDN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 160 DFTEIETPTLTRSTPEGARDFVVPARLKPGTFYALPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQPEFTQLDVE 239
Cdd:PRK00476 159 GFLEIETPILTKSTPEGARDYLVPSRVHPGKFYALPQSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADRQPEFTQIDIE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 240 MSFAEQDDVIALAEEILVAIFAEA-GVTVQTPIPRMTFKEAMEKYGSDKPDLRFDIPLVECTEFFKDTTFRVFQN----- 313
Cdd:PRK00476 239 MSFVTQEDVMALMEGLIRHVFKEVlGVDLPTPFPRMTYAEAMRRYGSDKPDLRFGLELVDVTDLFKDSGFKVFAGaandg 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 314 DYVGAVVMDGGASQP-RRQLDAWQDWARQRGAKGLAYILVGEDGtLGGPVAKNITDAEREGIAVHVGAKPGDCIFFAAGD 392
Cdd:PRK00476 319 GRVKAIRVPGGAAQLsRKQIDELTEFAKIYGAKGLAYIKVNEDG-LKGPIAKFLSEEELAALLERTGAKDGDLIFFGADK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 393 AKSSRALLGAARGEIAKKLGLIKEGDWAFTWVVDAPLFEPAADAtasgdvalghSQWTAVHHAFTSPKPEHMDTFDK-DP 471
Cdd:PRK00476 398 AKVVNDALGALRLKLGKELGLIDEDKFAFLWVVDFPMFEYDEEE----------GRWVAAHHPFTMPKDEDLDELETtDP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 472 GNALAYAYDIVCNGNEIGGGSIRIHRPDVQKRVFDVMGIGEEEAQEQFGFLLDAFQYGAPPHGGIAFGWDRIVSLLAGVD 551
Cdd:PRK00476 468 GKARAYAYDLVLNGYELGGGSIRIHRPEIQEKVFEILGISEEEAEEKFGFLLDALKYGAPPHGGIAFGLDRLVMLLAGAD 547
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 740843632 552 SIRDVIAFPKSGGGVDPLTDAPTPITAQQRKETGIDFKPKP 592
Cdd:PRK00476 548 SIRDVIAFPKTQSAQDLLTGAPSPVDEKQLRELGIRLRKKE 588
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
1-594 |
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: 1074.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 1 MLRTHLAGDLRADLAGSTVTLTGWVGRRRDHGGVIFIDMRDRSGYAQVVF---RNSEVAERAHHLRSEYCIQVTGVVEKR 77
Cdd:COG0173 1 MYRTHYCGELRESDVGQEVTLSGWVHRRRDHGGLIFIDLRDRYGITQVVFdpdDSAEAFEKAEKLRSEYVIAVTGKVRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 78 PEGSENPNLASGEIEVNVTELTILNESAALPFQLEDvgtSGTVGEEARLKYRYLDLRREGPAKIMRLRAAVNRAARKVLD 157
Cdd:COG0173 81 PEGTVNPKLPTGEIEVLASELEILNKAKTPPFQIDD---DTDVSEELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 158 SHDFTEIETPTLTRSTPEGARDFVVPARLKPGTFYALPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQPEFTQLD 237
Cdd:COG0173 158 ENGFLEIETPILTKSTPEGARDYLVPSRVHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFRDEDLRADRQPEFTQLD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 238 VEMSFAEQDDVIALAEEILVAIFAE-AGVTVQTPIPRMTFKEAMEKYGSDKPDLRFDIPLVECTEFFKDTTFRVFQN--- 313
Cdd:COG0173 238 IEMSFVDQEDVFELMEGLIRHLFKEvLGVELPTPFPRMTYAEAMERYGSDKPDLRFGLELVDVTDIFKDSGFKVFAGaae 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 314 --DYVGAVVMDGGASQPRRQLDAWQDWARQRGAKGLAYILVGEDGtLGGPVAKNITDAEREGIAVHVGAKPGDCIFFAAG 391
Cdd:COG0173 318 ngGRVKAINVPGGASLSRKQIDELTEFAKQYGAKGLAYIKVNEDG-LKSPIAKFLSEEELAAILERLGAKPGDLIFFVAD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 392 DAKSSRALLGAARGEIAKKLGLIKEGDWAFTWVVDAPLFEPAADAtasgdvalghSQWTAVHHAFTSPKPEHMDTFDKDP 471
Cdd:COG0173 397 KPKVVNKALGALRLKLGKELGLIDEDEFAFLWVVDFPLFEYDEEE----------GRWVAMHHPFTMPKDEDLDLLETDP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 472 GNALAYAYDIVCNGNEIGGGSIRIHRPDVQKRVFDVMGIGEEEAQEQFGFLLDAFQYGAPPHGGIAFGWDRIVSLLAGVD 551
Cdd:COG0173 467 GKVRAKAYDLVLNGYELGGGSIRIHDPELQEKVFELLGISEEEAEEKFGFLLEAFKYGAPPHGGIAFGLDRLVMLLAGED 546
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 740843632 552 SIRDVIAFPKSGGGVDPLTDAPTPITAQQRKETGIDFKPKPKQ 594
Cdd:COG0173 547 SIRDVIAFPKTQSAQDLMTGAPSEVDEKQLKELHIRLRPPEKK 589
|
|
| aspS_bact |
TIGR00459 |
aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be ... |
3-591 |
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: 723.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 3 RTHLAGDLRADLAGSTVTLTGWVGRRRDHGGVIFIDMRDRSGYAQVVFRNSEVA-ERAHHLRSEYCIQVTGVVEKRPEGS 81
Cdd:TIGR00459 2 RTHYCGQLRTEHLGQTVTLAGWVNRRRDLGGLIFIDLRDRSGIVQVVCDPDADAlKLAKGLRNEDVVQVKGKVSARPEGN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 82 ENPNLASGEIEVNVTELTILNESAALPFQLEDVGTSgtvgEEARLKYRYLDLRREGPAKIMRLRAAVNRAARKVLDSHDF 161
Cdd:TIGR00459 82 INRNLDTGEIEILAESITLLNKSKTPPLIIEKTDAE----EEVRLKYRYLDLRRPEMQQRLKLRHKVTKAVRNFLDQQGF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 162 TEIETPTLTRSTPEGARDFVVPARLKPGTFYALPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQPEFTQLDVEMS 241
Cdd:TIGR00459 158 LEIETPMLTKSTPEGARDYLVPSRVHKGEFYALPQSPQLFKQLLMVSGVDRYYQIARCFRDEDLRADRQPEFTQIDMEMS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 242 FAEQDDVIALAEEILVAIFAE-AGVTVQTPIPRMTFKEAMEKYGSDKPDLRFDIPLVECTEFFKDTTFRVFQN-----DY 315
Cdd:TIGR00459 238 FMTQEDVMELIEKLVSHVFLEvKGIDLKKPFPVMTYAEAMERYGSDKPDLRFPLELIDVTDLFKDSEFKVFSNlindgGR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 316 VGAV-VMDGGASQPRRQLDAWQDWARQRGAKGLAYILVGEDGTlGGPVAKNITDAEREGIAVHVGAKPGDCIFFAAGDAK 394
Cdd:TIGR00459 318 VKAIrVPGGWAELSRKSIKELRKFAKEYGAKGLAYLKVNEDGI-NSPIKKFLDEKKGKILLERTDAQNGDILLFGAGSKK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 395 SSRALLGAARGEIAKKLGLIKEGDWAFTWVVDAPLFEPAadatasgdvalGHSQWTAVHHAFTSPKPEHMDTFDKDPGNA 474
Cdd:TIGR00459 397 IVLDALGALRLKLGKDLGLVDPDLFSFLWVVDFPMFEKD-----------KEGRLCAAHHPFTMPKDEDLENLEAAPEEA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 475 LAYAYDIVCNGNEIGGGSIRIHRPDVQKRVFDVMGIGEEEAQEQFGFLLDAFQYGAPPHGGIAFGWDRIVSLLAGVDSIR 554
Cdd:TIGR00459 466 LAEAYDLVLNGVELGGGSIRIHDPEVQKKVFEILGIDPEEAREKFGFLLEAFKYGTPPHAGFALGLDRLMMLLTGTDNIR 545
|
570 580 590
....*....|....*....|....*....|....*..
gi 740843632 555 DVIAFPKSGGGVDPLTDAPTPITAQQRKETGIDFKPK 591
Cdd:TIGR00459 546 DVIAFPKTTAAACLMTEAPSFIDEKQLEELSIKYVVK 582
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
3-583 |
0e+00 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 644.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 3 RTHLAGDLRADLAGSTVTLTGWVGRRRDHGGVIFIDMRDRSGYAQVVFRN---SEVAERAHHLRSEYCIQVTGVVEKRPE 79
Cdd:PLN02903 59 RSHLCGALSVNDVGSRVTLCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPdefPEAHRTANRLRNEYVVAVEGTVRSRPQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 80 GSENPNLASGEIEVNVTELTILNE-SAALPFQLEDVGTS-GTVGEEARLKYRYLDLRREGPAKIMRLRAAVNRAARKVL- 156
Cdd:PLN02903 139 ESPNKKMKTGSVEVVAESVDILNVvTKSLPFLVTTADEQkDSIKEEVRLRYRVLDLRRPQMNANLRLRHRVVKLIRRYLe 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 157 DSHDFTEIETPTLTRSTPEGARDFVVPARLKPGTFYALPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQPEFTQL 236
Cdd:PLN02903 219 DVHGFVEIETPILSRSTPEGARDYLVPSRVQPGTFYALPQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEFTQL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 237 DVEMSFAEQDDVIALAEEILVAIFAE-AGVTVQTPIPRMTFKEAMEKYGSDKPDLRFDIPLVECTEFFKDTTFRVF---- 311
Cdd:PLN02903 299 DMELAFTPLEDMLKLNEDLIRQVFKEiKGVQLPNPFPRLTYAEAMSKYGSDKPDLRYGLELVDVSDVFAESSFKVFagal 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 312 -QNDYVGAVVMDGGASQPRRQL----DAWQDwARQRGAKGLAYILVGEDGTLGGPVA--KNITDAEREGIAVHVGAKPGD 384
Cdd:PLN02903 379 eSGGVVKAICVPDGKKISNNTAlkkgDIYNE-AIKSGAKGLAFLKVLDDGELEGIKAlvESLSPEQAEQLLAACGAGPGD 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 385 CIFFAAGDAKSSRALLGAARGEIAKKLGLIKEGDWAFTWVVDAPLFEPAADatasgdvalgHSQWTAVHHAFTSPKPEHM 464
Cdd:PLN02903 458 LILFAAGPTSSVNKTLDRLRQFIAKTLDLIDPSRHSILWVTDFPMFEWNED----------EQRLEALHHPFTAPNPEDM 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 465 DtfdkDPGNALAYAYDIVCNGNEIGGGSIRIHRPDVQKRVFDVMGIGEEEAQEQFGFLLDAFQYGAPPHGGIAFGWDRIV 544
Cdd:PLN02903 528 G----DLSSARALAYDMVYNGVEIGGGSLRIYRRDVQQKVLEAIGLSPEEAESKFGYLLEALDMGAPPHGGIAYGLDRLV 603
|
570 580 590
....*....|....*....|....*....|....*....
gi 740843632 545 SLLAGVDSIRDVIAFPKSGGGVDPLTDAPTPITAQQRKE 583
Cdd:PLN02903 604 MLLAGAKSIRDVIAFPKTTTAQCALTRAPSEVDDKQLQD 642
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
8-586 |
0e+00 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 534.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 8 GDLRADLAGSTVTLTGWVGRRRDHGGVIFIDMRDRSGYAQVVFR----NSEVAERAHHLRSEYCIQVTGVVEKRPEGSEN 83
Cdd:PRK12820 10 GHLSLDDTGREVCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFSpeaaPADVYELAASLRAEFCVALQGEVQKRLEETEN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 84 PNLASGEIEVNVTELTILNESAALPFQLED--------VGTSGTVGEEARLKYRYLDLRREGPAKIMRLRAAVNRAARKV 155
Cdd:PRK12820 90 PHIETGDIEVFVRELSILAASEALPFAISDkamtagagSAGADAVNEDLRLQYRYLDIRRPAMQDHLAKRHRIIKCARDF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 156 LDSHDFTEIETPTLTRSTPEGARDFVVPARLKPGTFYALPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQPEFTQ 235
Cdd:PRK12820 170 LDSRGFLEIETPILTKSTPEGARDYLVPSRIHPKEFYALPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEFTQ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 236 LDVEMSFAEQDDVIALAEEILVAIFAEAGVTVQTPIPRMTFKEAMEKYGSDKPDLRFDIPLVECTEFFKDTTFRVFQNdy 315
Cdd:PRK12820 250 LDIEASFIDEEFIFELIEELTARMFAIGGIALPRPFPRMPYAEAMDTTGSDRPDLRFDLKFADATDIFENTRYGIFKQ-- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 316 vgaVVMDGGA-------------SQPRRQLDAWQDWARQRGAKGLAYILVgEDGTLGGPVAKNITDAEREGIAVHVGAKP 382
Cdd:PRK12820 328 ---ILQRGGRikginikgqseklSKNVLQNEYAKEIAPSFGAKGMTWMRA-EAGGLDSNIVQFFSADEKEALKRRFHAED 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 383 GDCIFFAAgDAKSSRAL--LGAARGEIAKKLGLIKEGDWAFTWVVDAPLFEPAADATAsgdvalghsqwTAVHHAFTSPk 460
Cdd:PRK12820 404 GDVIIMIA-DASCAIVLsaLGQLRLHLADRLGLIPEGVFHPLWITDFPLFEATDDGGV-----------TSSHHPFTAP- 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 461 pehmDTFDKDPGNA------LAYAYDIVCNGNEIGGGSIRIHRPDVQKRVFDVMGIGEEEAQEQFGFLLDAFQYGAPPHG 534
Cdd:PRK12820 471 ----DREDFDPGDIeelldlRSRAYDLVVNGEELGGGSIRINDKDIQLRIFAALGLSEEDIEDKFGFFLRAFDFAAPPHG 546
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 740843632 535 GIAFGWDRIVSLLAGVDSIRDVIAFPKSGGGVDPLTDAPTPITAQQRKETGI 586
Cdd:PRK12820 547 GIALGLDRVVSMILQTPSIREVIAFPKNRSAACPLTGAPSEVAQEQLAELGL 598
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
142-563 |
7.10e-160 |
|
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: 458.58 E-value: 7.10e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 142 MRLRAAVNRAARKVLDSHDFTEIETPTLTRSTPEGARDFVVPARLKPGTFYALPQSPQLFKQLLMVAGMERYYQIARCYR 221
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTPEGARDFLVPSRLHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 222 DEDFRADRQPEFTQLDVEMSFAEQDDVIALAEEILVAIFAEA-GVTVQTPIPRMTFKEAMEKYGsdkpdlrfdiplvect 300
Cdd:cd00777 81 DEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVlGVELTTPFPRMTYAEAMERYG---------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 301 effkdttfrvfqndyvgavvmdggasqprrqldawqdwarqrgakglayilvgedgtlggpvaknitdaeregiavhvga 380
Cdd:cd00777 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 381 kpgdciffaagdakssrallgaargeiakklglikegdWAFTWVVDAPLFEPAADatasgdvalgHSQWTAVHHAFTSPK 460
Cdd:cd00777 145 --------------------------------------FKFLWIVDFPLFEWDEE----------EGRLVSAHHPFTAPK 176
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 461 PEHMDTFDKDPGNALAYAYDIVCNGNEIGGGSIRIHRPDVQKRVFDVMGIGEEEAQEQFGFLLDAFQYGAPPHGGIAFGW 540
Cdd:cd00777 177 EEDLDLLEKDPEDARAQAYDLVLNGVELGGGSIRIHDPDIQEKVFEILGLSEEEAEEKFGFLLEAFKYGAPPHGGIALGL 256
|
410 420
....*....|....*....|...
gi 740843632 541 DRIVSLLAGVDSIRDVIAFPKSG 563
Cdd:cd00777 257 DRLVMLLTGSESIRDVIAFPKTQ 279
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
121-561 |
1.32e-135 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 398.48 E-value: 1.32e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 121 GEEARLKYRYLDLRREGPAKIMRLRAAVNRAARKVLDSHDFTEIETPTLTRS-TPEGARDFVVPARLKpGTFYALPQSPQ 199
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSaTPEGARDFLVPSRAL-GKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 200 LFKQLLMVAGMERYYQIARCYRDEDFRADRQPEFTQLDVEMSFAEQDDVIALAEEILVAIFAEA-----------GVTVQ 268
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVegiakeleggtLLDLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 269 TPIPRMTFKEAMEK----------YGSDKPDLRFDIPLVecteffkdttfrvfqndyvgavvmdggasqprrqldawqdw 338
Cdd:pfam00152 160 KPFPRITYAEAIEKlngkdveelgYGSDKPDLRFLLELV----------------------------------------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 339 arqrgakglayilvgedgtlggpvaknitdaeregiavhvgakpgdciffaagdakssrallgaargeiakklglIKEGD 418
Cdd:pfam00152 199 ---------------------------------------------------------------------------IDKNK 203
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 419 WAFTWVVDAPlfepaadatasgdvalghsqwtAVHHAFTSPKPEHmdtfdkdpGNALAYAYDIVCNGNEIGGGSIRIHRP 498
Cdd:pfam00152 204 FNPLWVTDFP----------------------AEHHPFTMPKDED--------DPALAEAFDLVLNGVEIGGGSIRIHDP 253
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740843632 499 DVQKRVFDVMGIGEEEAQEQFGFLLDAFQYGAPPHGGIAFGWDRIVSLLAGVDSIRDVIAFPK 561
Cdd:pfam00152 254 ELQEERFEEQGLDPEEAEEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAFPK 316
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
1-560 |
1.06e-75 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 247.80 E-value: 1.06e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 1 MLRTHLAGDLRADLAGSTVTLTGWVGRRRDHGGVIFIDMRDRSGYAQVVFRNSEVAE---RAHHLRSEYCIQVTGVVEkr 77
Cdd:PRK05159 1 MMKRHLTSELTPELDGEEVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKVDEElfeTIKKLKRESVVSVTGTVK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 78 pegsENPNlASGEIEVNVTELTILNESAA-LPFQledvgTSGTVGEE--ARLKYRYLDLRREGPAKIMRLRAAVNRAARK 154
Cdd:PRK05159 79 ----ANPK-APGGVEVIPEEIEVLNKAEEpLPLD-----ISGKVLAEldTRLDNRFLDLRRPRVRAIFKIRSEVLRAFRE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 155 VLDSHDFTEIETPTLTRSTPEGArdfvvpARLKPGTFYA----LPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQ 230
Cdd:PRK05159 149 FLYENGFTEIFTPKIVASGTEGG------AELFPIDYFEkeayLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSRH 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 231 -PEFTQLDVEMSFAEQD-DVIALAEEILVAIFAEA-----------GVT---VQTPIPRMTFKEAMEKygsdkpdlrfdi 294
Cdd:PRK05159 223 lNEYTSIDVEMGFIDDHeDVMDLLENLLRYMYEDVaencekelellGIElpvPETPIPRITYDEAIEI------------ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 295 plvecteffkdttfrvfqndyvgavvmdggasqprrqldawqdwARQRGAKglayILVGEDgtLGgpvakniTDAERegi 374
Cdd:PRK05159 291 --------------------------------------------LKSKGNE----ISWGDD--LD-------TEGER--- 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 375 avhvgakpgdciffaagdakssrallgaARGEIAKklgliKEGDWAFTWVVDAPlfepaadatasgdvalghsqwtavhh 454
Cdd:PRK05159 311 ----------------------------LLGEYVK-----EEYGSDFYFITDYP-------------------------- 331
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 455 afTSPKPehMDTFDKDPGNALAYAYDIVCNGNEIGGGSIRIHRPDVQKRVFDVMGigeeEAQEQFGFLLDAFQYGAPPHG 534
Cdd:PRK05159 332 --SEKRP--FYTMPDEDDPEISKSFDLLFRGLEITSGGQRIHRYDMLVESIKEKG----LNPESFEFYLEAFKYGMPPHG 403
|
570 580
....*....|....*....|....*.
gi 740843632 535 GIAFGWDRIVSLLAGVDSIRDVIAFP 560
Cdd:PRK05159 404 GFGLGLERLTMKLLGLENIREAVLFP 429
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
142-563 |
2.47e-72 |
|
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: 233.52 E-value: 2.47e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 142 MRLRAAVNRAARKVLDSHDFTEIETPTLTRSTP-EGARDFVVPARlKPGTFYALPQSPQLFKQLLMVAGMERYYQIARCY 220
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGgAGARPFLVKYN-ALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 221 RDEDFRADRQPEFTQLDVEMSFAEQDDVIALAEEILVAIFAEA-GVTVQT----------PIPRMTFKEAMEKYGsdkpd 289
Cdd:cd00669 80 RNEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVlGVTAVTygfeledfglPFPRLTYREALERYG----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 290 lrfdiplvecteffkdttfrvfqndyvgavvmdggasqprrqldawqdwarqrgakglayilvgedgtlggpvaknitda 369
Cdd:cd00669 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 370 eregiavhvgakpgdciffaagdakssrallgaargeiakklglikegdwAFTWVVDAPLFepaadatasgdvalghsqw 449
Cdd:cd00669 155 --------------------------------------------------QPLFLTDYPAE------------------- 165
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 450 taVHHAFTSPKPEHmdtfdkdpgNALAYAYDIVCNGNEIGGGSIRIHRPDVQKRVFDVMGIGEEEAQEQFGFLLDAFQYG 529
Cdd:cd00669 166 --MHSPLASPHDVN---------PEIADAFDLFINGVEVGNGSSRLHDPDIQAEVFQEQGINKEAGMEYFEFYLKALEYG 234
|
410 420 430
....*....|....*....|....*....|....
gi 740843632 530 APPHGGIAFGWDRIVSLLAGVDSIRDVIAFPKSG 563
Cdd:cd00669 235 LPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKMR 268
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
3-560 |
9.69e-70 |
|
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: 231.86 E-value: 9.69e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 3 RTHLAGDLRADLAGSTVTLTGWVGRRRDHGGVIFIDMRDRSGYAQVVFRNSEVA--ERAHHLRSEYCIQVTGVVEKRPEg 80
Cdd:COG0017 1 KRTYIKDLLPEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKLEnfEEAKKLTTESSVEVTGTVVESPR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 81 senpnlASGEIEVNVTELTILNESAA-LPFQLEDVGTsgtvgeEARLKYRYLDLRREGPAKIMRLRAAVNRAARKVLDSH 159
Cdd:COG0017 80 ------APQGVELQAEEIEVLGEADEpYPLQPKRHSL------EFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQER 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 160 DFTEIETPTLTRSTPEGARD-FVVparlkpgTFYA----LPQSPQLFKQlLMVAGMERYYQIARCYRDEDFRADRQ-PEF 233
Cdd:COG0017 148 GFVEVHTPIITASATEGGGElFPV-------DYFGkeayLTQSGQLYKE-ALAMALEKVYTFGPTFRAEKSNTRRHlAEF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 234 TQLDVEMSFAEQDDVIALAEEILVAIFAEAG------------------VTVQTPIPRMTFKEAMEKYGSDKPDLRFdip 295
Cdd:COG0017 220 WMIEPEMAFADLEDVMDLAEEMLKYIIKYVLencpeeleflgrdverleKVPESPFPRITYTEAIEILKKSGEKVEW--- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 296 lvecteffkdttfrvfqndyvgavvmdggasqprrqldawqdwarqrgakglayilvGEDgtLGgpvakniTDAEREgIA 375
Cdd:COG0017 297 ---------------------------------------------------------GDD--LG-------TEHERY-LG 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 376 VHVGAKPgdcIFfaagdakssrallgaargeiakklglikegdwaftwVVDAPlfepaadatasgdvalghsqwtavhha 455
Cdd:COG0017 310 EEFFKKP---VF------------------------------------VTDYP--------------------------- 323
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 456 fTSPKPEHMDTFDKDPGnaLAYAYDIVCNG-NEIGGGSIRIHRPDVQKRVFDVMGIGEEEaqeqFGFLLDAFQYGAPPHG 534
Cdd:COG0017 324 -KEIKAFYMKPNPDDPK--TVAAFDLLAPGiGEIIGGSQREHRYDVLVERIKEKGLDPED----YEWYLDLRRYGSVPHA 396
|
570 580
....*....|....*....|....*.
gi 740843632 535 GIAFGWDRIVSLLAGVDSIRDVIAFP 560
Cdd:COG0017 397 GFGLGLERLVMWLTGLENIREVIPFP 422
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
3-136 |
1.25e-66 |
|
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: 213.54 E-value: 1.25e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 3 RTHLAGDLRADLAGSTVTLTGWVGRRRDHGGVIFIDMRDRSGYAQVVFR--NSEVAERAHHLRSEYCIQVTGVVEKRPEG 80
Cdd:cd04317 1 RTHYCGELRESHVGQEVTLCGWVQRRRDHGGLIFIDLRDRYGIVQVVFDpeEAPEFELAEKLRNESVIQVTGKVRARPEG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 740843632 81 SENPNLASGEIEVNVTELTILNESAALPFQLEDvgtSGTVGEEARLKYRYLDLRRE 136
Cdd:cd04317 81 TVNPKLPTGEIEVVASELEVLNKAKTLPFEIDD---DVNVSEELRLKYRYLDLRRP 133
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
120-561 |
4.47e-42 |
|
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: 154.26 E-value: 4.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 120 VGEEARLKYRYLDLRREGPAKIMRLRAAVNRAARKVLDSHDFTEIETPTLTRSTPEGardfvvPARLKPGTFYA----LP 195
Cdd:cd00776 2 ANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEG------GAELFKVSYFGkpayLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 196 QSPQLFKQlLMVAGMERYYQIARCYRDEDFRADRQ-PEFTQLDVEMSFAEQ-DDVIALAEEILVAIFAeagvTVQTpipr 273
Cdd:cd00776 76 QSPQLYKE-MLIAALERVYEIGPVFRAEKSNTRRHlSEFWMLEAEMAFIEDyNEVMDLIEELIKYIFK----RVLE---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 274 mTFKEAMEKYGSDKPDlrfdiPLVECTEFfkdttfrvfqndyvgavvmdggasqPRRQLDAWQDWARQRGAKglAYILVG 353
Cdd:cd00776 147 -RCAKELELVNQLNRE-----LLKPLEPF-------------------------PRITYDEAIELLREKGVE--EEVKWG 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 354 EDgtLGgpvakniTDAEREgIAVHVGAKPgdcIFfaagdakssrallgaargeiakklglikegdwaftwVVDAPLfepa 433
Cdd:cd00776 194 ED--LS-------TEHERL-LGEIVKGDP---VF------------------------------------VTDYPK---- 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 434 adatasgdvalghsqwtavhhaftSPKPEHMDTFDKDPGnaLAYAYD-IVCNGNEIGGGSIRIHRPDVQKRVFDVMGIGE 512
Cdd:cd00776 221 ------------------------EIKPFYMKPDDDNPE--TVESFDlLMPGVGEIVGGSQRIHDYDELEERIKEHGLDP 274
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 740843632 513 EEaqeqFGFLLDAFQYGAPPHGGIAFGWDRIVSLLAGVDSIRDVIAFPK 561
Cdd:cd00776 275 ES----FEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFPR 319
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
8-573 |
3.47e-38 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 148.32 E-value: 3.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 8 GDLRADLAGSTVTLTGWVGRRRDHGGVIFIDMRDRSGYAQVVFRNSEVAERAHHLR------SEYCIQVTGVV---EKRP 78
Cdd:PLN02850 73 SDLGEELAGSEVLIRGRVHTIRGKGKSAFLVLRQSGFTVQCVVFVSEVTVSKGMVKyakqlsRESVVDVEGVVsvpKKPV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 79 EGsenpnlASGEIEVNVTELTILNES-AALPFQLEDVGTS--------------GTVGEEARLKYRYLDLRREGPAKIMR 143
Cdd:PLN02850 153 KG------TTQQVEIQVRKIYCVSKAlATLPFNVEDAARSeseiekalqtgeqlVRVGQDTRLNNRVLDLRTPANQAIFR 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 144 LRAAVNRAARKVLDSHDFTEIETPTLTRSTPEGARD------FVVPArlkpgtfyALPQSPQLFKQLLMVAGMERYYQIA 217
Cdd:PLN02850 227 IQSQVCNLFREFLLSKGFVEIHTPKLIAGASEGGSAvfrldyKGQPA--------CLAQSPQLHKQMAICGDFRRVFEIG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 218 RCYRDEDFRADRQ-PEFTQLDVEMSFAEQ-DDVIALAEEILVAIFaeagvtvqtpiprmtfkeamekygsdkpdlrfdip 295
Cdd:PLN02850 299 PVFRAEDSFTHRHlCEFTGLDLEMEIKEHySEVLDVVDELFVAIF----------------------------------- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 296 lvecteffkdttfrvfqndyvgavvmDGGASQPRRQLDAwqdWARQRGAKGLAYIlvgeDGTLggpvakNITDAerEGIA 375
Cdd:PLN02850 344 --------------------------DGLNERCKKELEA---IREQYPFEPLKYL----PKTL------RLTFA--EGIQ 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 376 vhvgakpgdcIFFAAGDAKSSralLGAARGEIAKKLG-LIKEgdwaftwvvdaplfepaadaTASGDVALGHSQWTAVHH 454
Cdd:PLN02850 383 ----------MLKEAGVEVDP---LGDLNTESERKLGqLVKE--------------------KYGTDFYILHRYPLAVRP 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 455 AFTSPKPEhmdtfdkDPgnALAYAYDIVCNGNEIGGGSIRIHRPDVQKRVFDVMGIGEEEAQEqfgfLLDAFQYGAPPHG 534
Cdd:PLN02850 430 FYTMPCPD-------DP--KYSNSFDVFIRGEEIISGAQRVHDPELLEKRAEECGIDVKTIST----YIDSFRYGAPPHG 496
|
570 580 590
....*....|....*....|....*....|....*....
gi 740843632 535 GIAFGWDRIVSLLAGVDSIRDVIAFPKsgggvDPLTDAP 573
Cdd:PLN02850 497 GFGVGLERVVMLFCGLNNIRKTSLFPR-----DPQRLAP 530
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
3-560 |
1.17e-37 |
|
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: 145.95 E-value: 1.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 3 RTHLAGDLRADLA--------GSTVTLTGWVGRRRDHGGVIFIDMRDRSGYAQVVFRNSEVAERAHHLRSEY----CIQV 70
Cdd:COG1190 35 RTHTAAEIREKYDeleaeeetGDEVSVAGRIMAKRDMGKASFADLQDGSGRIQLYLRRDELGEEAYELFKLLdlgdIVGV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 71 TGVV--EKRpegsenpnlasGEIEVNVTELTILNES-AALP---FQLEDVgtsgtvgeEARLKYRYLDL-RREGPAKIMR 143
Cdd:COG1190 115 EGTVfrTKT-----------GELSVKVEELTLLSKSlRPLPekfHGLTDP--------ETRYRQRYVDLiVNPEVRETFR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 144 LRAAVNRAARKVLDSHDFTEIETPTLTrSTPEGA--RDFVvparlkpgTFY-ALPQ------SPQLF-KQLLmVAGMERY 213
Cdd:COG1190 176 KRSKIIRAIRRFLDERGFLEVETPMLQ-PIAGGAaaRPFI--------THHnALDMdlylriAPELYlKRLI-VGGFERV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 214 YQIARCYRDEDfrADRQ--PEFTQLDVEMSFAEQDDVIALAEEILVAIFAEAG----VTVQ-------TPIPRMTFKEAM 280
Cdd:COG1190 246 FEIGRNFRNEG--IDTThnPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLgttkVTYQgqeidlsPPWRRITMVEAI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 281 EKYGSdkpdlrfdiplvecTEFFKDTTFrvfqndyvgavvmdggasqprrqldawqDWARQRgakglayilvgedgtlgg 360
Cdd:COG1190 324 KEATG--------------IDVTPLTDD----------------------------EELRAL------------------ 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 361 pvaknitdAEREGIAVHVGAKPGDCI--FFaagDAKssrallgaargeIAKKLglikegdWAFTWVVDAPlfepaadata 438
Cdd:COG1190 344 --------AKELGIEVDPGWGRGKLIdeLF---EEL------------VEPKL-------IQPTFVTDYP---------- 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 439 sgdvalghsqwtavhhAFTSP--KPeHmdtfDKDPGnaLAYAYDIVCNGNEIGGGSIRIHRPDVQKRVF----DVMGIGE 512
Cdd:COG1190 384 ----------------VEVSPlaKR-H----RDDPG--LTERFELFIAGREIANAFSELNDPIDQRERFeeqlELKAAGD 440
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 740843632 513 EEAQ---EQFgflLDAFQYGAPPHGGIAFGWDRIVSLLAGVDSIRDVIAFP 560
Cdd:COG1190 441 DEAMpmdEDF---LRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 488
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
18-103 |
4.16e-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: 116.13 E-value: 4.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 18 TVTLTGWVGRRRDHGGVIFIDMRDRSGYAQVVFR---NSEVAERAHHLRSEYCIQVTGVVEKRPEGsenpNLASGEIEVN 94
Cdd:cd04100 1 EVTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNkeeLGEFFEEAEKLRTESVVGVTGTVVKRPEG----NLATGEIELQ 76
|
....*....
gi 740843632 95 VTELTILNE 103
Cdd:cd04100 77 AEELEVLSK 85
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
3-560 |
4.25e-30 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 124.05 E-value: 4.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 3 RTHLAGDLRA----------DLAGSTVTLTGWVGRRRDHGGVIFIDMRDRSGYAQVVFRNSEVAERAHHLRSEY----CI 68
Cdd:PRK00484 31 RTHTAAELRAkyddkekeelEELEIEVSVAGRVMLKRVMGKASFATLQDGSGRIQLYVSKDDVGEEALEAFKKLdlgdII 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 69 QVTGVV--EKRpegsenpnlasGEIEVNVTELTILNES-AALP--FQ-LEDVgtsgtvgeEARLKYRYLDL-RREGPAKI 141
Cdd:PRK00484 111 GVEGTLfkTKT-----------GELSVKATELTLLTKSlRPLPdkFHgLTDV--------ETRYRQRYVDLiVNPESRET 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 142 MRLRAAVNRAARKVLDSHDFTEIETPTLtRSTPEG--ARDFVvparlkpgTFY-ALPQ------SPQLF-KQLLmVAGME 211
Cdd:PRK00484 172 FRKRSKIISAIRRFLDNRGFLEVETPML-QPIAGGaaARPFI--------THHnALDIdlylriAPELYlKRLI-VGGFE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 212 RYYQIARCYRDEDfrADRQ--PEFTQLDVEMSFAEQDDVIALAEEILVAIFAEA---------GVTV--QTPIPRMTFKE 278
Cdd:PRK00484 242 RVYEIGRNFRNEG--IDTRhnPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVlgttkvtyqGTEIdfGPPFKRLTMVD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 279 AMEKY-GSDkpdlrFDIPLVEcteffkdttfrvfqndyvgavvmdggasqprrqldawqdwarqrgakglayilvgedgt 357
Cdd:PRK00484 320 AIKEYtGVD-----FDDMTDE----------------------------------------------------------- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 358 lggpVAKNItdAEREGIAVHVGAKPGDCI--FFaagdakssrallgaarGEIA-KKLglikegdWAFTWVVDAPLfEpaa 434
Cdd:PRK00484 336 ----EARAL--AKELGIEVEKSWGLGKLIneLF----------------EEFVePKL-------IQPTFITDYPV-E--- 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 435 datasgdvalghsqwtavhhafTSP--KPeHmdtfDKDPGnaLAYAYDIVCNGNEIGGGSIRIHRPDVQKRVF------- 505
Cdd:PRK00484 383 ----------------------ISPlaKR-H----REDPG--LTERFELFIGGREIANAFSELNDPIDQRERFeaqveak 433
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 740843632 506 DVmgiGEEEAQ---EQFgflLDAFQYGAPPHGGIAFGWDRIVSLLAGVDSIRDVIAFP 560
Cdd:PRK00484 434 EA---GDDEAMfmdEDF---LRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
3-560 |
2.02e-27 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 118.14 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 3 RTHLAGDLRADLAGSTVTLTGWVGRRRDHGGVIFIDMRDRSGYAQVVFRNSEVAERAHHLRSEYC-----IQVTG-VVEK 76
Cdd:PRK02983 638 PTHTVAEALDAPTGEEVSVSGRVLRIRDYGGVLFADLRDWSGELQVLLDASRLEQGSLADFRAAVdlgdlVEVTGtMGTS 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 77 RpegsenpnlaSGEIEVNVTELTILNES-AALPFQledvgTSGTVGEEARLKYRYLDLRREGPAK-IMRLRAAVNRAARK 154
Cdd:PRK02983 718 R----------NGTLSLLVTSWRLAGKClRPLPDK-----WKGLTDPEARVRQRYLDLAVNPEARdLLRARSAVVRAVRE 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 155 VLDSHDFTEIETPTLtrSTPEG---ARDFVVPARLKPGTFYaLPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQP 231
Cdd:PRK02983 783 TLVARGFLEVETPIL--QQVHGganARPFVTHINAYDMDLY-LRIAPELYLKRLCVGGVERVFELGRNFRNEGVDATHNP 859
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 232 EFTQLDVEMSFAEQDDVIALAEEILVAifaeagvtvqtpiprmtfkEAMEKYGSdkpdlrfdiplvecteffkdttfrvf 311
Cdd:PRK02983 860 EFTLLEAYQAHADYDTMRDLTRELIQN-------------------AAQAAHGA-------------------------- 894
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 312 qndyvgAVVMDGGASQPRRQLDAWQDWaRQRGAKGLAYILVGEDGTLGGPVAKNITDAEREGIAVHVgakpgdciffaag 391
Cdd:PRK02983 895 ------PVVMRPDGDGVLEPVDISGPW-PVVTVHDAVSEALGEEIDPDTPLAELRKLCDAAGIPYRT------------- 954
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 392 dakssrallGAARGEIAKKL--GLIKEGDWAFTWVVDAPlfepaadatasgdvalghsqwtavhhAFTSPKP-EHMDtfd 468
Cdd:PRK02983 955 ---------DWDAGAVVLELyeHLVEDRTTFPTFYTDFP--------------------------TSVSPLTrPHRS--- 996
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 469 kDPGnaLAYAYDIVCNGNEIGGGSIRIHRPDVQKRVFDVMGI----GEEEAQEQFGFLLDAFQYGAPPHGGIAFGWDRIV 544
Cdd:PRK02983 997 -DPG--LAERWDLVAWGVELGTAYSELTDPVEQRRRLTEQSLlaagGDPEAMELDEDFLQALEYAMPPTGGLGMGVDRLV 1073
|
570
....*....|....*.
gi 740843632 545 SLLAGVdSIRDVIAFP 560
Cdd:PRK02983 1074 MLLTGR-SIRETLPFP 1088
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
1-560 |
1.19e-25 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 110.20 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 1 MLRTHLAGDLRADLAGSTVTLTGWVGRRRDHGGVIFIDMRDRSGYAQVVF---RNSEVAERAHHLRSEYCIQVTGVVEKR 77
Cdd:PRK03932 1 MMRVSIKDILKGKYVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVvkdNGEEYFEEIKKLTTGSSVIVTGTVVES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 78 PEgsenpnlASGEIEVNVTELTILNESAA-LPFQLEDVGTsgtvgeEARLKYRYLDLRREGPAKIMRLRAAVNRAARKVL 156
Cdd:PRK03932 81 PR-------AGQGYELQATKIEVIGEDPEdYPIQKKRHSI------EFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 157 DSHDFTEIETPTLTRSTPEGARD-FVVPARLKPGT--FYA----LPQSPQLFKQLLMVAgMERYYQIARCYRDEDFRADR 229
Cdd:PRK03932 148 NENGFVWVDTPIITASDCEGAGElFRVTTLDLDFSkdFFGkeayLTVSGQLYAEAYAMA-LGKVYTFGPTFRAENSNTRR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 230 Q-PEFTQLDVEMSFAEQDDVIALAEEILVAIfaeagvtvqtpiprmtFKEAMEKygsDKPDLRF-----DIPLVECTEFF 303
Cdd:PRK03932 227 HlAEFWMIEPEMAFADLEDNMDLAEEMLKYV----------------VKYVLEN---CPDDLEFlnrrvDKGDIERLENF 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 304 KDTTF-RVfqnDYVGAVVMdggasqprrqldawqdwARQRGAKGLAYILVGEDgtLGgpvaknitdAEREgiavhvgakp 382
Cdd:PRK03932 288 IESPFpRI---TYTEAIEI-----------------LQKSGKKFEFPVEWGDD--LG---------SEHE---------- 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 383 gdciffaagdakssRALlgaargeiAKKlglikegdwaftwVVDAPLFepaadatasgdvalghsqwtaVHHAFTSPKPE 462
Cdd:PRK03932 327 --------------RYL--------AEE-------------HFKKPVF---------------------VTNYPKDIKAF 350
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 463 HMdtfDKDPGNALAYAYDIVCNG-NEIGGGSIRIHRPDVQKRVFDVMGIGEEEaqeqFGFLLDAFQYGAPPHGGIAFGWD 541
Cdd:PRK03932 351 YM---RLNPDGKTVAAMDLLAPGiGEIIGGSQREERLDVLEARIKELGLNKED----YWWYLDLRRYGSVPHSGFGLGFE 423
|
570
....*....|....*....
gi 740843632 542 RIVSLLAGVDSIRDVIAFP 560
Cdd:PRK03932 424 RLVAYITGLDNIRDVIPFP 442
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
11-568 |
9.22e-24 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 105.46 E-value: 9.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 11 RADLAGSTVTLTGWVGRRRDHGGVIFIDMRDRSGYAQVVFRNS-----EVAERAHHLRSEYCIQVTGVVEKrpegSENP- 84
Cdd:PTZ00401 73 KPELVDKTVLIRARVSTTRKKGKMAFMVLRDGSDSVQAMAAVEgdvpkEMIDFIGQIPTESIVDVEATVCK----VEQPi 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 85 -NLASGEIEVNVTELTILNES-AALPFQLEDVGTSGT-----VGEEARLKYRYLDLRREGPAKIMRLRAAVNRAARKVLD 157
Cdd:PTZ00401 149 tSTSHSDIELKVKKIHTVTESlRTLPFTLEDASRKESdegakVNFDTRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLI 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 158 SHDFTEIETPTLTRSTPEGARDFvvparLKPGTF---YALPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQ-PEF 233
Cdd:PTZ00401 229 DSDFCEIHSPKIINAPSEGGANV-----FKLEYFnrfAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNTHRHlTEF 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 234 TQLDVEMSFAEQ-DDVIALAEEILVAIFAE--------AGVTVQTPIPRMTFK---EAMEKYGsdkpdlrfdiplvecte 301
Cdd:PTZ00401 304 VGLDVEMRINEHyYEVLDLAESLFNYIFERlathtkelKAVCQQYPFEPLVWKltpERMKELG----------------- 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 302 ffkdttfrvfqndyVGAVvmdggaSQPRRQLDAWQDWARQRGAKGLAYilvgedgtlggpvakNITDA-EREGIAVHVGA 380
Cdd:PTZ00401 367 --------------VGVI------SEGVEPTDKYQARVHNMDSRMLRI---------------NYMHCiELLNTVLEEKM 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 381 KPGDCIffaagdAKSSRALLGAargeiakklgLIKEGDWAFTWVVDapLFEpaadatasgdvalghsqwTAVHHAFTSPK 460
Cdd:PTZ00401 412 APTDDI------NTTNEKLLGK----------LVKERYGTDFFISD--RFP------------------SSARPFYTMEC 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 461 PEhmdtfDKDPGNalayAYDIVCNGNEIGGGSIRIHRPDVQKRVFDVMGIGEEEAQEqfgfLLDAFQYGAPPHGGIAFGW 540
Cdd:PTZ00401 456 KD-----DERFTN----SYDMFIRGEEISSGAQRIHDPDLLLARAKMLNVDLTPIKE----YVDSFRLGAWPHGGFGVGL 522
|
570 580
....*....|....*....|....*...
gi 740843632 541 DRIVSLLAGVDSIRDVIAFPKSGGGVDP 568
Cdd:PTZ00401 523 ERVVMLYLGLSNVRLASLFPRDPQRTTP 550
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
3-256 |
2.95e-20 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 94.67 E-value: 2.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 3 RTHLAGDLR---------ADLAGSTVTLTGWVGRRRDHGGVIFIDMRDRSGYAQVVF---RNSEVAERAHHLRSEY---- 66
Cdd:PLN02502 86 VTHTAPELQekygslengEELEDVSVSVAGRIMAKRAFGKLAFYDLRDDGGKIQLYAdkkRLDLDEEEFEKLHSLVdrgd 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 67 CIQVTGVVeKRPEgsenpnlaSGEIEVNVTELTILNESA-ALPFQ---LEDVGTsgtvgeeaRLKYRYLDL-RREGPAKI 141
Cdd:PLN02502 166 IVGVTGTP-GKTK--------KGELSIFPTSFEVLTKCLlMLPDKyhgLTDQET--------RYRQRYLDLiANPEVRDI 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 142 MRLRAAVNRAARKVLDSHDFTEIETPTLtRSTPEG--ARDFVvparlkpgTFY-------ALPQSPQLFKQLLMVAGMER 212
Cdd:PLN02502 229 FRTRAKIISYIRRFLDDRGFLEVETPML-NMIAGGaaARPFV--------THHndlnmdlYLRIATELHLKRLVVGGFER 299
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 740843632 213 YYQIARCYRDEDFRADRQPEFTQLDVEMSFAEQDDVIALAEEIL 256
Cdd:PLN02502 300 VYEIGRQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMV 343
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
5-560 |
5.01e-20 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 94.33 E-value: 5.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 5 HLAGDLRAdlAGSTVTLTGWVGRRRDHGGVIFIDMRDRSGYAQVVFRNSEVAERAHHLRSEYCIQVTGVVekrpeGSEN- 83
Cdd:PTZ00385 98 YLASGDRA--AQATVRVAGRVTSVRDIGKIIFVTIRSNGNELQVVGQVGEHFTREDLKKLKVSLRVGDII-----GADGv 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 84 P-NLASGEIEVNVTELTILNesaalPFQLEDV-------GTSGTVGEEARLKYRYLDLRrEGPAKI--MRLRAAVNRAAR 153
Cdd:PTZ00385 171 PcRMQRGELSVAASRMLILS-----PYVCTDQvvcpnlrGFTVLQDNDVKYRYRFTDMM-TNPCVIetIKKRHVMLQALR 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 154 KVLDSHDFTEIETPTL-TRSTPEGARDFVVPARLKPGTFYaLPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQPE 232
Cdd:PTZ00385 245 DYFNERNFVEVETPVLhTVASGANAKSFVTHHNANAMDLF-LRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 233 FTQLDVEMSFAEQDDVIALAEEILVAIFAEAGVTVQTPIprmtfkeamekygsdKPDLRFDIPL-VECTEFFKdttfRVF 311
Cdd:PTZ00385 324 FTSCEFYAAYHTYEDLMPMTEDIFRQLAMRVNGTTVVQI---------------YPENAHGNPVtVDLGKPFR----RVS 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 312 QNDYVGAvvMDGGASQPRRQLDAwqdwarqrgAKGLAY---ILVGEDGTLggPvaknitdaeregiAVHVGAKPGDCI-- 386
Cdd:PTZ00385 385 VYDEIQR--MSGVEFPPPNELNT---------PKGIAYmsvVMLRYNIPL--P-------------PVRTAAKMFEKLid 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 387 FFAagdakSSRALlgaargeiakklglikegdwAFTWVVDAPLF-EPAADATASgdvalghsqwtavhhaftspkpehmd 465
Cdd:PTZ00385 439 FFI-----TDRVV--------------------EPTFVMDHPLFmSPLAKEQVS-------------------------- 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 466 tfdkDPGnaLAYAYDIVCNGNEIGGGSIRIHRPD-----VQKRVFDVMGiGEEEAQEQFGFLLDAFQYGAPPHGGIAFGW 540
Cdd:PTZ00385 468 ----RPG--LAERFELFVNGIEYCNAYSELNDPHeqyhrFQQQLVDRQG-GDEEAMPLDETFLKSLQVGLPPTAGWGMGI 540
|
570 580
....*....|....*....|
gi 740843632 541 DRIVSLLAGVDSIRDVIAFP 560
Cdd:PTZ00385 541 DRALMLLTNSSNIRDGIIFP 560
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
19-101 |
6.50e-19 |
|
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: 81.13 E-value: 6.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 19 VTLTGWV-GRRRDHGGVIFIDMRDRSGYAQVVFRNSEVAERAHHLRSEYCIQVTGVVEKRPEgsenpnlasGEIEVNVTE 97
Cdd:pfam01336 1 VTVAGRVtSIRRSGGKLLFLTLRDGTGSIQVVVFKEEAEKLAKKLKEGDVVRVTGKVKKRKG---------GELELVVEE 71
|
....
gi 740843632 98 LTIL 101
Cdd:pfam01336 72 IELL 75
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
5-108 |
2.90e-18 |
|
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the homodimeric non-discriminating (ND) Pyrococcus kodakaraensis aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. P. kodakaraensis AspRS is a class 2b aaRS. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. P. kodakaraensis ND-AspRS can charge both tRNAAsp and tRNAAsn. Some of the enzymes in this group may be discriminating, based on the presence of homologs of asparaginyl-tRNA synthetase (AsnRS) in their completed genomes.
Pssm-ID: 239811 [Multi-domain] Cd Length: 108 Bit Score: 80.44 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 5 HLAGDLRADLAGSTVTLTGWVGRRRDHGGVIFIDMRDRSGYAQVVFR----NSEVAERAHHLRSEYCIQVTGVVEKRPEg 80
Cdd:cd04316 1 HYSAEITPELDGEEVTVAGWVHEIRDLGGIKFVILRDREGIVQVTAPkkkvDKELFKTVRKLSRESVISVTGTVKAEPK- 79
|
90 100
....*....|....*....|....*...
gi 740843632 81 senpnlASGEIEVNVTELTILNESAALP 108
Cdd:cd04316 80 ------APNGVEIIPEEIEVLSEAKTPL 101
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
143-560 |
6.05e-17 |
|
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a lysine to the 3' OH group of ribose of the appropriate tRNA. Its assignment to class II aaRS is based upon its structure and the presence of three characteristic sequence motifs in the core domain. It is found in eukaryotes as well as some prokaryotes and archaea. However, LysRS belongs to class I aaRS's in some prokaryotes and archaea. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate.
Pssm-ID: 238398 [Multi-domain] Cd Length: 329 Bit Score: 82.25 E-value: 6.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 143 RLRAAVNRAARKVLDSHDFTEIETPTLtRSTPEG--ARDFVvparlkpgTFYA-------LPQSPQLFKQLLMVAGMERY 213
Cdd:cd00775 9 IVRSKIISYIRKFLDDRGFLEVETPML-QPIAGGaaARPFI--------THHNaldmdlyLRIAPELYLKRLIVGGFERV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 214 YQIARCYRDEDFRADRQPEFTQLDVEMSFAEQDDVIALAEEILVAIfaeagvtvqtpiprmtfkeAMEKYGSDKPD---- 289
Cdd:cd00775 80 YEIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGL-------------------VKKINGKTKIEyggk 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 290 -LRFDIPlvectefFKDTTFRVFQNDYVGAVVMDGGASQPRrqldawqDWARQRGakglayilvgedgtlggpvaknitd 368
Cdd:cd00775 141 eLDFTPP-------FKRVTMVDALKEKTGIDFPELDLEQPE-------ELAKLLA------------------------- 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 369 aerEGIAVHVGAKPgdciffaagdakSSRALLGAARGEIAKKLgLIKEgdwafTWVVDAPlfepaadatasgdvalghsq 448
Cdd:cd00775 182 ---KLIKEKIEKPR------------TLGKLLDKLFEEFVEPT-LIQP-----TFIIDHP-------------------- 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 449 wtavhhAFTSP----KPEhmdtfdkDPGnaLAYAYDIVCNGNEIGGGSIRIHRPDVQKRVF-DVMGI---GEEEAQ---E 517
Cdd:cd00775 221 ------VEISPlakrHRS-------NPG--LTERFELFICGKEIANAYTELNDPFDQRERFeEQAKQkeaGDDEAMmmdE 285
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 740843632 518 QFgflLDAFQYGAPPHGGIAFGWDRIVSLLAGVDSIRDVIAFP 560
Cdd:cd00775 286 DF---VTALEYGMPPTGGLGIGIDRLVMLLTDSNSIRDVILFP 325
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
88-283 |
4.18e-16 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 81.26 E-value: 4.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 88 SGEIEVNVTELTILNES-AALPFQLEdvgtsGTVGEEARLKYRYLDL-RREGPAKIMRLRAAVNRAARKVLDSHDFTEIE 165
Cdd:PRK12445 133 TGELSIHCTELRLLTKAlRPLPDKFH-----GLQDQEVRYRQRYLDLiANDKSRQTFVVRSKILAAIRQFMVARGFMEVE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 166 TPTLtRSTPEGA--RDFVVPARLKPGTFYaLPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQPEFTQLDVEMSFA 243
Cdd:PRK12445 208 TPMM-QVIPGGAsaRPFITHHNALDLDMY-LRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYA 285
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 740843632 244 EQDDVIALAEEILVAIFAEAGVTVQT-----------PIPRMTFKEAMEKY 283
Cdd:PRK12445 286 DYHDLIELTESLFRTLAQEVLGTTKVtygehvfdfgkPFEKLTMREAIKKY 336
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
144-272 |
5.18e-15 |
|
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: 74.08 E-value: 5.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 144 LRAAVNRAARKVLDSHDFTEIETPTLTRSTPEGARDFVVPARLKP----GTFYALPQSPQLFKQLLMV----AGMERYYQ 215
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHEPKDLLPVgaenEEDLYLRPTLEPGLVRLFVshirKLPLRLAE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740843632 216 IARCYRDEDFRAD--RQPEFTQLDVEMSFAEQDD------VIALAEEILVAIFAEAGVTVQTPIP 272
Cdd:cd00768 81 IGPAFRNEGGRRGlrRVREFTQLEGEVFGEDGEEasefeeLIELTEELLRALGIKLDIVFVEKTP 145
|
|
| GAD |
pfam02938 |
GAD domain; This domain is found in some members of the GatB and aspartyl tRNA synthetases. |
316-395 |
9.03e-14 |
|
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: 67.29 E-value: 9.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 316 VGAVVMDGGASQPRRQLDAWQDWARQRGAKGLAYILVGEDGtLGGPVAKNITDAEREGIAVHVGAKPGDCIFFAAGDAKS 395
Cdd:pfam02938 11 VKALRVPGAAGLSRKEIDELERFAKEYGAKGLAWIKVEGGG-HTGPIAKFLTEEEVEKLLEAVGAEDGDALLFVADKKKT 89
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
123-281 |
3.15e-13 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 71.20 E-value: 3.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 123 EARLKYRYLDLRREGPAKIMRLRAAVNRAARKVLDSHDFTEIETPTLTRST----PEGARDFVVPARLK-PGTFYALPQS 197
Cdd:PRK06462 11 EEFLRMSWKHISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIISPSTdplmGLGSDLPVKQISIDfYGVEYYLADS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 198 PQLFKQLlMVAGMERYYQIARCYRDEDFRADRQP---EFTQLDVEMSFAEQDDVIALAEEILVAIFAEAGVT-------- 266
Cdd:PRK06462 91 MILHKQL-ALRMLGKIFYLSPNFRLEPVDKDTGRhlyEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEhedeleff 169
|
170 180
....*....|....*....|.
gi 740843632 267 ------VQTPIPRMTFKEAME 281
Cdd:PRK06462 170 grdlphLKRPFKRITHKEAVE 190
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
18-103 |
2.33e-11 |
|
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: 59.94 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 18 TVTLTGWVGRRRDHGGVIFIDMRDRSGYAQVVFRNSEVAE--RAHHLRSEYCIQVTGVVEKRPEGSENPnlasGEIEVNV 95
Cdd:cd04323 1 RVKVFGWVHRLRSQKKLMFLVLRDGTGFLQCVLSKKLVTEfyDAKSLTQESSVEVTGEVKEDPRAKQAP----GGYELQV 76
|
....*...
gi 740843632 96 TELTILNE 103
Cdd:cd04323 77 DYLEIIGE 84
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
123-560 |
1.41e-09 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 60.79 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 123 EARLKYRYLDLR-REGPAKIMRLRAAVNRAARKVLDSHDFTEIETPTLTR-STPEGARDFVVPARLKPGTFYaLPQSPQL 200
Cdd:PTZ00417 233 EIRYRQRYLDLMiNESTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLvAGGANARPFITHHNDLDLDLY-LRIATEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 201 FKQLLMVAGMERYYQIARCYRDEDFRADRQPEFTQLDVEMSFAEQDDVIALAEeilvaifaeagvtvqtpiprmtfkeam 280
Cdd:PTZ00417 312 PLKMLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSE--------------------------- 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 281 ekygsdkpdlrfdiplvectEFFKDTTFRVFqndyvgavvmdggasqprrqldawqdwarqrgakGLAYILVGEDGTLGG 360
Cdd:PTZ00417 365 --------------------DFFSQLVMHLF----------------------------------GTYKILYNKDGPEKD 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 361 PVAKNITDAEREGIAVHVGAKPGDCIFFAAGDAKSSrallgaargeIAKKLGLIKEGDWAFTwvvDAPLFEPAADATASG 440
Cdd:PTZ00417 391 PIEIDFTPPYPKVSIVEELEKLTNTKLEQPFDSPET----------INKMINLIKENKIEMP---NPPTAAKLLDQLASH 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 441 DVALGHSQ---WTAVHHAFTSPKPEHMDTfdkDPGnaLAYAYDIVCNGNEIGGGSIRIHRPDVQKRVFDVMGIGEEEAQE 517
Cdd:PTZ00417 458 FIENKYPNkpfFIIEHPQIMSPLAKYHRS---KPG--LTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDA 532
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 740843632 518 QfGFLLDA-----FQYGAPPHGGIAFGWDRIVSLLAGVDSIRDVIAFP 560
Cdd:PTZ00417 533 E-AFQFDAafctsLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFP 579
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
18-133 |
2.89e-09 |
|
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These enzymes are homodimeric class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Included in this group are E. coli LysS and LysU. These two isoforms of LysRS are encoded by distinct genes which are differently regulated. Eukaryotes contain 2 sets of aaRSs, both of which encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Saccharomyces cerevisiae cytoplasmic and mitochondrial LysRSs have been shown to participate in the mitochondrial import of the only nuclear-encoded tRNA of S. cerevisiae (tRNAlysCUU). The gene for human LysRS encodes both the cytoplasmic and the mitochondrial isoforms of LysRS. In addition to their housekeeping role, human lysRS may function as a signaling molecule that activates immune cells and tomato LysRS may participate in a root-specific process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging.
Pssm-ID: 239817 [Multi-domain] Cd Length: 108 Bit Score: 54.79 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 18 TVTLTGWVGRRRDHGGVIFIDMRDRSGYAQVVFRNSEVAERAHHLRSEYC-----IQVTGVVEKrpegSEnpnlaSGEIE 92
Cdd:cd04322 1 EVSVAGRIMSKRGSGKLSFADLQDESGKIQVYVNKDDLGEEEFEDFKKLLdlgdiIGVTGTPFK----TK-----TGELS 71
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 740843632 93 VNVTELTILNES-AALPFQLedvgtSGTVGEEARLKYRYLDL 133
Cdd:cd04322 72 IFVKEFTLLSKSlRPLPEKF-----HGLTDVETRYRQRYLDL 108
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
12-567 |
3.19e-09 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 59.62 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 12 ADLAGSTVTLTGWV--GRRRDHGGVIFIDMRDRSGYAQV-VFRNSEVAERAHHLRSEYCIQVTGVVEKRPEGSENPNlas 88
Cdd:PLN02221 46 AGLAGQKVRIGGWVktGREQGKGTFAFLEVNDGSCPANLqVMVDSSLYDLSTLVATGTCVTVDGVLKVPPEGKGTKQ--- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 89 gEIEVNVTELTILNESAALPFQLEDVGTSgtvgEEARLKYRYLDLRREGPAKIMRLRAAVNRAARKVLDSHDFTEIETPT 168
Cdd:PLN02221 123 -KIELSVEKVIDVGTVDPTKYPLPKTKLT----LEFLRDVLHLRSRTNSISAVARIRNALAFATHSFFQEHSFLYIHTPI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 169 LTRSTPEGArdfvvparlkpgtfyalpqsPQLFKQLLMVAGMERYyqiarcyrDEDFRADRQPefTQLDVE---MSFAEQ 245
Cdd:PLN02221 198 ITTSDCEGA--------------------GEMFQVTTLINYTERL--------EQDLIDNPPP--TEADVEaarLIVKER 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 246 DDVIAlaeEILVAIFAEAGVTV---QTPIPRMTFKEAME----KYGSDKPDLRFDIplveCTEFFKDTTFRV-------- 310
Cdd:PLN02221 248 GEVVA---QLKAAKASKEEITAavaELKIAKESLAHIEErsklKPGLPKKDGKIDY----SKDFFGRQAFLTvsgqlqve 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 311 -----FQNDYVGAVVMDGGASQPRRQLDAWqdWARQrgaKGLAYILVGEDGTLGGPVAKNITD--AEREGIAVHVGAKpg 383
Cdd:PLN02221 321 tyacaLSSVYTFGPTFRAENSHTSRHLAEF--WMVE---PEIAFADLEDDMNCAEAYVKYMCKwlLDKCFDDMELMAK-- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 384 dciFFAAGDAKSSRALLGAARGEIA--KKLGLIKEGdwaftwVVDAPLFEPAADATAsgDVALGHSQWTAvHHAFTSP-- 459
Cdd:PLN02221 394 ---NFDSGCIDRLRMVASTPFGRITytEAIELLEEA------VAKGKEFDNNVEWGI--DLASEHERYLT-EVLFQKPli 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 460 ---KPEHMDTFD---KDPGNALAYAYDIVCNGNEIGGGSIRIHRPDVQKRVFDVMGIgeeeAQEQFGFLLDAFQYGAPPH 533
Cdd:PLN02221 462 vynYPKGIKAFYmrlNDDEKTVAAMDVLVPKVGELIGGSQREERYDVIKQRIEEMGL----PIEPYEWYLDLRRYGTVKH 537
|
570 580 590
....*....|....*....|....*....|....
gi 740843632 534 GGIAFGWDRIVSLLAGVDSIRDVIAFPKSGGGVD 567
Cdd:PLN02221 538 CGFGLGFERMILFATGIDNIRDVIPFPRYPGKAD 571
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
461-567 |
4.42e-09 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 59.22 E-value: 4.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 461 PEHMDTF---DKDPGNALAYAYDIVCNGNEIGGGSIRIHRPDVQKRVFDVMGIGeeeaQEQFGFLLDAFQYGAPPHGGIA 537
Cdd:PLN02603 459 PKEIKAFymrENDDGKTVAAMDMLVPRVGELIGGSQREERLEYLEARLDELKLN----KESYWWYLDLRRYGSVPHAGFG 534
|
90 100 110
....*....|....*....|....*....|
gi 740843632 538 FGWDRIVSLLAGVDSIRDVIAFPKSGGGVD 567
Cdd:PLN02603 535 LGFERLVQFATGIDNIRDAIPFPRVPGSAE 564
|
|
| ScAspRS_mt_like_N |
cd04321 |
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
19-103 |
4.55e-09 |
|
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: 53.48 E-value: 4.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 19 VTLTGWVGRRRD-HGGVIFIDMRDRSGYA-QVV-FRNSEVAERAHHLRSEYCIQVTGVV-EKRPEGSENPNlasgEIEVN 94
Cdd:cd04321 2 VTLNGWIDRKPRiVKKLSFADLRDPNGDIiQLVsTAKKDAFSLLKSITAESPVQVRGKLqLKEAKSSEKND----EWELV 77
|
....*....
gi 740843632 95 VTELTILNE 103
Cdd:cd04321 78 VDDIQTLNA 86
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
19-112 |
1.33e-07 |
|
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: 49.83 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 19 VTLTGWVGRRRDHGGVIFIDMRDRSGYAQVVF---RNSEVAERAHHLRSEYCIQVTGVVEKRPEGSENPNLASGEIEV-- 93
Cdd:cd04319 2 VTLAGWVYRKREVGKKAFIVLRDSTGIVQAVFskdLNEEAYREAKKVGIESSVIVEGAVKADPRAPGGAEVHGEKLEIiq 81
|
90
....*....|....*....
gi 740843632 94 NVTELTIlNESAALPFQLE 112
Cdd:cd04319 82 NVEFFPI-TEDASDEFLLD 99
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
160-283 |
4.81e-07 |
|
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: 51.78 E-value: 4.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 160 DFTEIETPTLTRST-PEG-----ARDFVVPARLKPgTFYaLPQSPQLF-KQLLmVAGMERYYQIARCYRDEDFRADRQPE 232
Cdd:TIGR00462 6 GVLEVETPLLSPAPvTDPhldafATEFVGPDGQGR-PLY-LQTSPEYAmKRLL-AAGSGPIFQICKVFRNGERGRRHNPE 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 740843632 233 FTQLD---VEMSFAE-QDDVIALAEEILVAIFAEAgvtvqtpiPRMTFKEAMEKY 283
Cdd:TIGR00462 83 FTMLEwyrPGFDYHDlMDEVEALLQELLGDPFAPA--------ERLSYQEAFLRY 129
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
142-256 |
1.36e-06 |
|
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: 49.91 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 142 MRLRAAVNRAARKVLDSHDFTEIETPT------LTRSTPEGAR------------------DFVVP-ARlkpgtFYAlpQ 196
Cdd:cd00773 2 AALRRYIEDTLREVFERYGYEEIDTPVfeytelFLRKSGDEVSkemyrfkdkggrdlalrpDLTAPvAR-----AVA--E 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740843632 197 SPQLFKQLLmvagmeRYYQIARCYRDEDFRADRQPEFTQLDVEM-------SFAEqddVIALAEEIL 256
Cdd:cd00773 75 NLLSLPLPL------KLYYIGPVFRYERPQKGRYREFYQVGVEIigsdsplADAE---VIALAVEIL 132
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
487-564 |
1.82e-06 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 50.79 E-value: 1.82e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740843632 487 EIGGGSiriHRPDVQKRVfDVMGIGEEEAQEQFGFLLDAFQYGAPPHGGIAFGWDRIVSLLAGVDSIRDVIAFPKSGG 564
Cdd:PTZ00425 509 EVIGGS---QREDNLERL-DKMIKEKKLNMESYWWYRQLRKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFPRYPG 582
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
18-101 |
2.92e-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: 45.63 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 18 TVTLTGWVGRRRDHGGVIFIDMRDRSGYA--QVVFRNS-EVAERAHHLRSEYCIQVTGVVEKRPEgsenpnlASGEIEVN 94
Cdd:cd04318 1 EVTVNGWVRSVRDSKKISFIELNDGSCLKnlQVVVDKElTNFKEILKLSTGSSIRVEGVLVKSPG-------AKQPFELQ 73
|
....*..
gi 740843632 95 VTELTIL 101
Cdd:cd04318 74 AEKIEVL 80
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
469-564 |
4.03e-04 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 43.32 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 469 KDPGNALAyAYDIVC-NGNEIGGGSIRIHRPDVQKRVFDVMGIgeeeAQEQFGFLLDAFQYGAPPHGGIAFGWDRIVSLL 547
Cdd:PLN02532 538 NDDGKTVA-AFDLVVpKVGTVITGSQNEERMDILNARIEELGL----PREQYEWYLDLRRHGTVKHSGFSLGFELMVLFA 612
|
90
....*....|....*..
gi 740843632 548 AGVDSIRDVIAFPKSGG 564
Cdd:PLN02532 613 TGLPDVRDAIPFPRSWG 629
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
521-556 |
4.31e-03 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 39.53 E-value: 4.31e-03
10 20 30
....*....|....*....|....*....|....*.
gi 740843632 521 FLLDAFQYGAPPHGGIAFGWDRIVSLLAGVDSIRDV 556
Cdd:PRK09350 271 NLIAALEAGLPDCSGVALGVDRLIMLALGAESISEV 306
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
18-113 |
6.68e-03 |
|
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces cerevisiae and human cytoplasmic aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis.
Pssm-ID: 239815 [Multi-domain] Cd Length: 102 Bit Score: 36.39 E-value: 6.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843632 18 TVTLTGWVGRRRDHGG-VIFIDMRDRSGYAQ-VVFRNSEVAER-----AHHLRSEYCIQVTGVVEKRPEGSENPNLAsgE 90
Cdd:cd04320 1 EVLIRARVHTSRAQGAkLAFLVLRQQGYTIQgVLAASAEGVSKqmvkwAGSLSKESIVDVEGTVKKPEEPIKSCTQQ--D 78
|
90 100
....*....|....*....|....
gi 740843632 91 IEVNVTELTILNESAA-LPFQLED 113
Cdd:cd04320 79 VELHIEKIYVVSEAAEpLPFQLED 102
|
|
| |
