|
Name |
Accession |
Description |
Interval |
E-value |
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
5-592 |
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: 1188.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 5 YRTVQCGEVGLEQVGQEVILNGWVQKRRDLGGVIFIDFRDRTGILQIVFNPEHNKNAWEVADKVRSEYVLAVKGTVVKRA 84
Cdd:COG0173 2 YRTHYCGELRESDVGQEVTLSGWVHRRRDHGGLIFIDLRDRYGITQVVFDPDDSAEAFEKAEKLRSEYVIAVTGKVRARP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 85 PEAVNPKLKTGEVEVIVSEIIILNDAKTPPFQIEDDIDVDEQVRLKYRYLDLRRPEMQRSLILRSKAAKAFRDFLDEKGF 164
Cdd:COG0173 82 EGTVNPKLPTGEIEVLASELEILNKAKTPPFQIDDDTDVSEELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDENGF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 165 VEVETPMLTKSTPEGAREYLVPSRVHPGEFFVLPQSPQLFKQLLMVSGMERYYQIARCFRDEDLRADRQPEFTQVDIETS 244
Cdd:COG0173 162 LEIETPILTKSTPEGARDYLVPSRVHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFRDEDLRADRQPEFTQLDIEMS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 245 FLSMEELLPMMEEMIAHVFKTTIGVDVPRPFPRLTYAEAMARYGSDKPDVRFGMELTDVSDLVATSDFKVFASVVSGGGQ 324
Cdd:COG0173 242 FVDQEDVFELMEGLIRHLFKEVLGVELPTPFPRMTYAEAMERYGSDKPDLRFGLELVDVTDIFKDSGFKVFAGAAENGGR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 325 VKAINAKGCGHYSRKEADDLGKFASRYGAKGLAWMGFKDGEVKGPIAKFFGEAEINSLKERLAVEEGDLLLFVADKPKVV 404
Cdd:COG0173 322 VKAINVPGGASLSRKQIDELTEFAKQYGAKGLAYIKVNEDGLKSPIAKFLSEEELAAILERLGAKPGDLIFFVADKPKVV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 405 ADALGALRSKLGAELGLIDHSQFAFLWVVDFPLVEWDEESQRYLALHHPFTRPKDEDLHLLESDPGQVRAQAYDMVLNGY 484
Cdd:COG0173 402 NKALGALRLKLGKELGLIDEDEFAFLWVVDFPLFEYDEEEGRWVAMHHPFTMPKDEDLDLLETDPGKVRAKAYDLVLNGY 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 485 ELGGGSMRIYKRDVQEKMFRTLGLTEEEAKQKFGFLLDAFDFGTPPHGGIALGLDRLIMLLAGRSNLREVIAFPKTASAS 564
Cdd:COG0173 482 ELGGGSIRIHDPELQEKVFELLGISEEEAEEKFGFLLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFPKTQSAQ 561
|
570 580
....*....|....*....|....*...
gi 686452888 565 DLMVDAPGPVDDKQLAELNIMTTVKDEE 592
Cdd:COG0173 562 DLMTGAPSEVDEKQLKELHIRLRPPEKK 589
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
5-590 |
0e+00 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 1140.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 5 YRTVQCGEVGLEQVGQEVILNGWVQKRRDLGGVIFIDFRDRTGILQIVFNPEhnKNAWEVADKVRSEYVLAVKGTVVKRA 84
Cdd:PRK00476 3 MRTHYCGELRESHVGQTVTLCGWVHRRRDHGGLIFIDLRDREGIVQVVFDPD--AEAFEVAESLRSEYVIQVTGTVRARP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 85 PEAVNPKLKTGEVEVIVSEIIILNDAKTPPFQIEDDIDVDEQVRLKYRYLDLRRPEMQRSLILRSKAAKAFRDFLDEKGF 164
Cdd:PRK00476 81 EGTVNPNLPTGEIEVLASELEVLNKSKTLPFPIDDEEDVSEELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDDNGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 165 VEVETPMLTKSTPEGAREYLVPSRVHPGEFFVLPQSPQLFKQLLMVSGMERYYQIARCFRDEDLRADRQPEFTQVDIETS 244
Cdd:PRK00476 161 LEIETPILTKSTPEGARDYLVPSRVHPGKFYALPQSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADRQPEFTQIDIEMS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 245 FLSMEELLPMMEEMIAHVFKTTIGVDVPRPFPRLTYAEAMARYGSDKPDVRFGMELTDVSDLVATSDFKVFASVVSGGGQ 324
Cdd:PRK00476 241 FVTQEDVMALMEGLIRHVFKEVLGVDLPTPFPRMTYAEAMRRYGSDKPDLRFGLELVDVTDLFKDSGFKVFAGAANDGGR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 325 VKAINAKGCG-HYSRKEADDLGKFASRYGAKGLAWMGFKDGEVKGPIAKFFGEAEINSLKERLAVEEGDLLLFVADKPKV 403
Cdd:PRK00476 321 VKAIRVPGGAaQLSRKQIDELTEFAKIYGAKGLAYIKVNEDGLKGPIAKFLSEEELAALLERTGAKDGDLIFFGADKAKV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 404 VADALGALRSKLGAELGLIDHSQFAFLWVVDFPLVEWDEESQRYLALHHPFTRPKDEDLHLLE-SDPGQVRAQAYDMVLN 482
Cdd:PRK00476 401 VNDALGALRLKLGKELGLIDEDKFAFLWVVDFPMFEYDEEEGRWVAAHHPFTMPKDEDLDELEtTDPGKARAYAYDLVLN 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 483 GYELGGGSMRIYKRDVQEKMFRTLGLTEEEAKQKFGFLLDAFDFGTPPHGGIALGLDRLIMLLAGRSNLREVIAFPKTAS 562
Cdd:PRK00476 481 GYELGGGSIRIHRPEIQEKVFEILGISEEEAEEKFGFLLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFPKTQS 560
|
570 580
....*....|....*....|....*...
gi 686452888 563 ASDLMVDAPGPVDDKQLAELNIMTTVKD 590
Cdd:PRK00476 561 AQDLLTGAPSPVDEKQLRELGIRLRKKE 588
|
|
| aspS_bact |
TIGR00459 |
aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be ... |
6-589 |
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: 858.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 6 RTVQCGEVGLEQVGQEVILNGWVQKRRDLGGVIFIDFRDRTGILQIVFNPEhnKNAWEVADKVRSEYVLAVKGTVVKRAP 85
Cdd:TIGR00459 2 RTHYCGQLRTEHLGQTVTLAGWVNRRRDLGGLIFIDLRDRSGIVQVVCDPD--ADALKLAKGLRNEDVVQVKGKVSARPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 86 EAVNPKLKTGEVEVIVSEIIILNDAKTPPFQIEDDiDVDEQVRLKYRYLDLRRPEMQRSLILRSKAAKAFRDFLDEKGFV 165
Cdd:TIGR00459 80 GNINRNLDTGEIEILAESITLLNKSKTPPLIIEKT-DAEEEVRLKYRYLDLRRPEMQQRLKLRHKVTKAVRNFLDQQGFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 166 EVETPMLTKSTPEGAREYLVPSRVHPGEFFVLPQSPQLFKQLLMVSGMERYYQIARCFRDEDLRADRQPEFTQVDIETSF 245
Cdd:TIGR00459 159 EIETPMLTKSTPEGARDYLVPSRVHKGEFYALPQSPQLFKQLLMVSGVDRYYQIARCFRDEDLRADRQPEFTQIDMEMSF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 246 LSMEELLPMMEEMIAHVFKTTIGVDVPRPFPRLTYAEAMARYGSDKPDVRFGMELTDVSDLVATSDFKVFASVVSGGGQV 325
Cdd:TIGR00459 239 MTQEDVMELIEKLVSHVFLEVKGIDLKKPFPVMTYAEAMERYGSDKPDLRFPLELIDVTDLFKDSEFKVFSNLINDGGRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 326 KAINAKG-CGHYSRKEADDLGKFASRYGAKGLAWMGFKDGEVKGPIAKFFGEAEINSLKERLAVEEGDLLLFVADKPKVV 404
Cdd:TIGR00459 319 KAIRVPGgWAELSRKSIKELRKFAKEYGAKGLAYLKVNEDGINSPIKKFLDEKKGKILLERTDAQNGDILLFGAGSKKIV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 405 ADALGALRSKLGAELGLIDHSQFAFLWVVDFPLVEWDEEsQRYLALHHPFTRPKDEDLHLLESDPGQVRAQAYDMVLNGY 484
Cdd:TIGR00459 399 LDALGALRLKLGKDLGLVDPDLFSFLWVVDFPMFEKDKE-GRLCAAHHPFTMPKDEDLENLEAAPEEALAEAYDLVLNGV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 485 ELGGGSMRIYKRDVQEKMFRTLGLTEEEAKQKFGFLLDAFDFGTPPHGGIALGLDRLIMLLAGRSNLREVIAFPKTASAS 564
Cdd:TIGR00459 478 ELGGGSIRIHDPEVQKKVFEILGIDPEEAREKFGFLLEAFKYGTPPHAGFALGLDRLMMLLTGTDNIRDVIAFPKTTAAA 557
|
570 580
....*....|....*....|....*
gi 686452888 565 DLMVDAPGPVDDKQLAELNIMTTVK 589
Cdd:TIGR00459 558 CLMTEAPSFIDEKQLEELSIKYVVK 582
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
1-588 |
0e+00 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 745.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 1 MSWQYRTVQCGEVGLEQVGQEVILNGWVQKRRDLGGVIFIDFRDRTGILQIVFNPEHNKNAWEVADKVRSEYVLAVKGTV 80
Cdd:PLN02903 54 LTWPSRSHLCGALSVNDVGSRVTLCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDEFPEAHRTANRLRNEYVVAVEGTV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 81 VKRAPEAVNPKLKTGEVEVIVSEIIILNDAKTP-PFQI----EDDIDVDEQVRLKYRYLDLRRPEMQRSLILRSKAAKAF 155
Cdd:PLN02903 134 RSRPQESPNKKMKTGSVEVVAESVDILNVVTKSlPFLVttadEQKDSIKEEVRLRYRVLDLRRPQMNANLRLRHRVVKLI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 156 RDFL-DEKGFVEVETPMLTKSTPEGAREYLVPSRVHPGEFFVLPQSPQLFKQLLMVSGMERYYQIARCFRDEDLRADRQP 234
Cdd:PLN02903 214 RRYLeDVHGFVEIETPILSRSTPEGARDYLVPSRVQPGTFYALPQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQP 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 235 EFTQVDIETSFLSMEELLPMMEEMIAHVFKTTIGVDVPRPFPRLTYAEAMARYGSDKPDVRFGMELTDVSDLVATSDFKV 314
Cdd:PLN02903 294 EFTQLDMELAFTPLEDMLKLNEDLIRQVFKEIKGVQLPNPFPRLTYAEAMSKYGSDKPDLRYGLELVDVSDVFAESSFKV 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 315 FASVVSGGGQVKAINA-KGCGHYS--RKEADDLGKFASRYGAKGLAWMGF-KDGEVKGPIAKFFGEAEINS--LKERLAV 388
Cdd:PLN02903 374 FAGALESGGVVKAICVpDGKKISNntALKKGDIYNEAIKSGAKGLAFLKVlDDGELEGIKALVESLSPEQAeqLLAACGA 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 389 EEGDLLLFVADKPKVVADALGALRSKLGAELGLIDHSQFAFLWVVDFPLVEWDEESQRYLALHHPFTRPKDEDLhlleSD 468
Cdd:PLN02903 454 GPGDLILFAAGPTSSVNKTLDRLRQFIAKTLDLIDPSRHSILWVTDFPMFEWNEDEQRLEALHHPFTAPNPEDM----GD 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 469 PGQVRAQAYDMVLNGYELGGGSMRIYKRDVQEKMFRTLGLTEEEAKQKFGFLLDAFDFGTPPHGGIALGLDRLIMLLAGR 548
Cdd:PLN02903 530 LSSARALAYDMVYNGVEIGGGSLRIYRRDVQQKVLEAIGLSPEEAESKFGYLLEALDMGAPPHGGIAYGLDRLVMLLAGA 609
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 686452888 549 SNLREVIAFPKTASASDLMVDAPGPVDDKQLAELNIMTTV 588
Cdd:PLN02903 610 KSIRDVIAFPKTTTAQCALTRAPSEVDDKQLQDLSIASTA 649
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
10-585 |
0e+00 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 632.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 10 CGEVGLEQVGQEVILNGWVQKRRDLGGVIFIDFRDRTGILQIVFNPEH-NKNAWEVADKVRSEYVLAVKGTVVKRAPEAV 88
Cdd:PRK12820 9 CGHLSLDDTGREVCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFSPEAaPADVYELAASLRAEFCVALQGEVQKRLEETE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 89 NPKLKTGEVEVIVSEIIILNDAKTPPFQIEDDI-----------DVDEQVRLKYRYLDLRRPEMQRSLILRSKAAKAFRD 157
Cdd:PRK12820 89 NPHIETGDIEVFVRELSILAASEALPFAISDKAmtagagsagadAVNEDLRLQYRYLDIRRPAMQDHLAKRHRIIKCARD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 158 FLDEKGFVEVETPMLTKSTPEGAREYLVPSRVHPGEFFVLPQSPQLFKQLLMVSGMERYYQIARCFRDEDLRADRQPEFT 237
Cdd:PRK12820 169 FLDSRGFLEIETPILTKSTPEGARDYLVPSRIHPKEFYALPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEFT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 238 QVDIETSFLSMEELLPMMEEMIAHVFKTTiGVDVPRPFPRLTYAEAMARYGSDKPDVRFGMELTDVSDLVATSDFKVFAS 317
Cdd:PRK12820 249 QLDIEASFIDEEFIFELIEELTARMFAIG-GIALPRPFPRMPYAEAMDTTGSDRPDLRFDLKFADATDIFENTRYGIFKQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 318 VVSGGGQVKAINAKGCGHYSRK---EADDLGKFASRYGAKGLAWMGFKDGEVKGPIAKFFGEAEINSLKERLAVEEGDLL 394
Cdd:PRK12820 328 ILQRGGRIKGINIKGQSEKLSKnvlQNEYAKEIAPSFGAKGMTWMRAEAGGLDSNIVQFFSADEKEALKRRFHAEDGDVI 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 395 LFVADKP-KVVADALGALRSKLGAELGLIDHSQFAFLWVVDFPLVEWDEESQrYLALHHPFTRPKDEDLhllesDPGQV- 472
Cdd:PRK12820 408 IMIADAScAIVLSALGQLRLHLADRLGLIPEGVFHPLWITDFPLFEATDDGG-VTSSHHPFTAPDREDF-----DPGDIe 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 473 -----RAQAYDMVLNGYELGGGSMRIYKRDVQEKMFRTLGLTEEEAKQKFGFLLDAFDFGTPPHGGIALGLDRLIMLLAG 547
Cdd:PRK12820 482 elldlRSRAYDLVVNGEELGGGSIRINDKDIQLRIFAALGLSEEDIEDKFGFFLRAFDFAAPPHGGIALGLDRVVSMILQ 561
|
570 580 590
....*....|....*....|....*....|....*...
gi 686452888 548 RSNLREVIAFPKTASASDLMVDAPGPVDDKQLAELNIM 585
Cdd:PRK12820 562 TPSIREVIAFPKNRSAACPLTGAPSEVAQEQLAELGLL 599
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
145-562 |
2.68e-169 |
|
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: 482.07 E-value: 2.68e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 145 LILRSKAAKAFRDFLDEKGFVEVETPMLTKSTPEGAREYLVPSRVHPGEFFVLPQSPQLFKQLLMVSGMERYYQIARCFR 224
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTPEGARDFLVPSRLHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 225 DEDLRADRQPEFTQVDIETSFLSMEELLPMMEEMIAHVFKTTIGVDVPRPFPRLTYAEAMARYGsdkpdvrfgmeltdvs 304
Cdd:cd00777 81 DEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLGVELTTPFPRMTYAEAMERYG---------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 305 dlvatsdfkvfasvvsgggqvkainakgcghysrkeaddlgkfasrygakglawmgfkdgevkgpiakffgeaeinslke 384
Cdd:cd00777 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 385 rlaveegdlllfvadkpkvvadalgalrsklgaelglidhsqFAFLWVVDFPLVEWDEESQRYLALHHPFTRPKDEDLHL 464
Cdd:cd00777 145 ------------------------------------------FKFLWIVDFPLFEWDEEEGRLVSAHHPFTAPKEEDLDL 182
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 465 LESDPGQVRAQAYDMVLNGYELGGGSMRIYKRDVQEKMFRTLGLTEEEAKQKFGFLLDAFDFGTPPHGGIALGLDRLIML 544
Cdd:cd00777 183 LEKDPEDARAQAYDLVLNGVELGGGSIRIHDPDIQEKVFEILGLSEEEAEEKFGFLLEAFKYGAPPHGGIALGLDRLVML 262
|
410
....*....|....*...
gi 686452888 545 LAGRSNLREVIAFPKTAS 562
Cdd:cd00777 263 LTGSESIRDVIAFPKTQN 280
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
124-560 |
6.91e-145 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 421.59 E-value: 6.91e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 124 DEQVRLKYRYLDLRRPEMQRSLILRSKAAKAFRDFLDEKGFVEVETPMLTKS-TPEGAREYLVPSRVHpGEFFVLPQSPQ 202
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSaTPEGARDFLVPSRAL-GKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 203 LFKQLLMVSGMERYYQIARCFRDEDLRADRQPEFTQVDIETSFLSMEELLPMMEEMIAHVFKTTIGV----------DVP 272
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIakeleggtllDLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 273 RPFPRLTYAEAMAR----------YGSDKPDVRFGMELTdvsdlvatsdfkvfasvvsgggqvkainakgcghysrkead 342
Cdd:pfam00152 160 KPFPRITYAEAIEKlngkdveelgYGSDKPDLRFLLELV----------------------------------------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 343 dlgkfasrygakglawmgfkdgevkgpiakffgeaeinslkerlaveegdlllfvadkpkvvadalgalrsklgaelglI 422
Cdd:pfam00152 199 -------------------------------------------------------------------------------I 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 423 DHSQFAFLWVVDFPlvewdeesqrylALHHPFTRPKDEDLHllesdpgqVRAQAYDMVLNGYELGGGSMRIYKRDVQEKM 502
Cdd:pfam00152 200 DKNKFNPLWVTDFP------------AEHHPFTMPKDEDDP--------ALAEAFDLVLNGVEIGGGSIRIHDPELQEER 259
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 686452888 503 FRTLGLTEEEAKQKFGFLLDAFDFGTPPHGGIALGLDRLIMLLAGRSNLREVIAFPKT 560
Cdd:pfam00152 260 FEEQGLDPEEAEEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAFPKT 317
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
5-558 |
7.90e-90 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 284.39 E-value: 7.90e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 5 YRTVQCGEVGLEQVGQEVILNGWVQKRRDLGGVIFIDFRDRTGILQIVFNPEHNKNAWEVADKVRSEYVLAVKGTVVKra 84
Cdd:PRK05159 2 MKRHLTSELTPELDGEEVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKVDEELFETIKKLKRESVVSVTGTVKA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 85 peavNPKLKTGeVEVIVSEIIILNDAKTP-PFQIEDDIDVDEQVRLKYRYLDLRRPEMQRSLILRSKAAKAFRDFLDEKG 163
Cdd:PRK05159 80 ----NPKAPGG-VEVIPEEIEVLNKAEEPlPLDISGKVLAELDTRLDNRFLDLRRPRVRAIFKIRSEVLRAFREFLYENG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 164 FVEVETPMLTKSTPEGAREylvpsrVHPGEFF----VLPQSPQLFKQLLMVSGMERYYQIARCFRDEDLRADRQ-PEFTQ 238
Cdd:PRK05159 155 FTEIFTPKIVASGTEGGAE------LFPIDYFekeaYLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSRHlNEYTS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 239 VDIETSFL-SMEELLPMMEEMIAHVFKT----------TIGVDVPRP---FPRLTYAEAMARygsdkpdvrfgmeltdvs 304
Cdd:PRK05159 229 IDVEMGFIdDHEDVMDLLENLLRYMYEDvaencekeleLLGIELPVPetpIPRITYDEAIEI------------------ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 305 dlvatsdfkvfasvvsgggqvkaINAKGcghYSRKEADDLGKFASRYgakglawmgfkdgevkgpIAKFFGEaeinslke 384
Cdd:PRK05159 291 -----------------------LKSKG---NEISWGDDLDTEGERL------------------LGEYVKE-------- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 385 rlavEEGDLLLFVADKPKvvadalgALRsklgaelglidhsqfaflwvvdfplvewdeesqrylalhhPF-TRPKDEDLH 463
Cdd:PRK05159 319 ----EYGSDFYFITDYPS-------EKR----------------------------------------PFyTMPDEDDPE 347
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 464 LLESdpgqvraqaYDMVLNGYELGGGSMRIYKRDVQEKMFRTLGLTEEeakqKFGFLLDAFDFGTPPHGGIALGLDRLIM 543
Cdd:PRK05159 348 ISKS---------FDLLFRGLEITSGGQRIHRYDMLVESIKEKGLNPE----SFEFYLEAFKYGMPPHGGFGLGLERLTM 414
|
570
....*....|....*
gi 686452888 544 LLAGRSNLREVIAFP 558
Cdd:PRK05159 415 KLLGLENIREAVLFP 429
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
6-560 |
3.57e-84 |
|
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: 269.23 E-value: 3.57e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 6 RTVQCGEVGLEQVGQEVILNGWVQKRRDLGGVIFIDFRDRTGILQIVFNPEHNKNaWEVADKVRSEYVLAVKGTVVKrap 85
Cdd:COG0017 1 KRTYIKDLLPEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKLEN-FEEAKKLTTESSVEVTGTVVE--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 86 eavNPKLKTGeVEVIVSEIIILNDAKTP-PFQIED-DIDvdeqVRLKYRYLDLRRPEMQRSLILRSKAAKAFRDFLDEKG 163
Cdd:COG0017 77 ---SPRAPQG-VELQAEEIEVLGEADEPyPLQPKRhSLE----FLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 164 FVEVETPMLTKSTPEGAREylvpsrVHPGEFF----VLPQSPQLFKQlLMVSGMERYYQIARCFRDEDLRADRQ-PEFTQ 238
Cdd:COG0017 149 FVEVHTPIITASATEGGGE------LFPVDYFgkeaYLTQSGQLYKE-ALAMALEKVYTFGPTFRAEKSNTRRHlAEFWM 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 239 VDIETSFLSMEELLPMMEEMIAHVFKT----------TIGVDVPR-------PFPRLTYAEAMARYGSDKPDVRFGmelt 301
Cdd:COG0017 222 IEPEMAFADLEDVMDLAEEMLKYIIKYvlencpeeleFLGRDVERlekvpesPFPRITYTEAIEILKKSGEKVEWG---- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 302 dvsdlvatsdfkvfasvvsgggqvkainakgcghysrkeaDDLGKFASRYgakglawmgfkdgevkgpiakffgeaeins 381
Cdd:COG0017 298 ----------------------------------------DDLGTEHERY------------------------------ 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 382 lkerLAVEEGDLLLFVADKPKvvadalgALRsklgaelglidhsqfaflwvvdfplvewdeesqrylalhhPF-TRPKDE 460
Cdd:COG0017 308 ----LGEEFFKKPVFVTDYPK-------EIK----------------------------------------AFyMKPNPD 336
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 461 dlhllesDPGQVRaqAYDMVLNGY-ELGGGSMRIYKRDVQEKMFRTLGLTEEEakqkFGFLLDAFDFGTPPHGGIALGLD 539
Cdd:COG0017 337 -------DPKTVA--AFDLLAPGIgEIIGGSQREHRYDVLVERIKEKGLDPED----YEWYLDLRRYGSVPHAGFGLGLE 403
|
570 580
....*....|....*....|.
gi 686452888 540 RLIMLLAGRSNLREVIAFPKT 560
Cdd:COG0017 404 RLVMWLTGLENIREVIPFPRD 424
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
145-560 |
2.13e-83 |
|
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: 262.03 E-value: 2.13e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 145 LILRSKAAKAFRDFLDEKGFVEVETPMLTKSTP-EGAREYLVPSRvHPGEFFVLPQSPQLFKQLLMVSGMERYYQIARCF 223
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGgAGARPFLVKYN-ALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 224 RDEDLRADRQPEFTQVDIETSFLSMEELLPMMEEMIAHVFKTTIGV----------DVPRPFPRLTYAEAMARYGsdkpd 293
Cdd:cd00669 80 RNEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVtavtygfeleDFGLPFPRLTYREALERYG----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 294 vrfgmeltdvsdlvatsdfkvfasvvsgggqvkainakgcghysrkeaddlgkfasrygakglawmgfkdgevkgpiakf 373
Cdd:cd00669 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 374 fgeaeinslkerlaveegdlllfvadkpkvvadalgalrsklgaelglidhsqfAFLWVVDFPLVewdeesqrylaLHHP 453
Cdd:cd00669 155 ------------------------------------------------------QPLFLTDYPAE-----------MHSP 169
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 454 FTRPKDEDlhllesdpgQVRAQAYDMVLNGYELGGGSMRIYKRDVQEKMFRTLGLTEEEAKQKFGFLLDAFDFGTPPHGG 533
Cdd:cd00669 170 LASPHDVN---------PEIADAFDLFINGVEVGNGSSRLHDPDIQAEVFQEQGINKEAGMEYFEFYLKALEYGLPPHGG 240
|
410 420
....*....|....*....|....*..
gi 686452888 534 IALGLDRLIMLLAGRSNLREVIAFPKT 560
Cdd:cd00669 241 LGIGIDRLIMLMTNSPTIREVIAFPKM 267
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
6-141 |
6.15e-76 |
|
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: 237.42 E-value: 6.15e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 6 RTVQCGEVGLEQVGQEVILNGWVQKRRDLGGVIFIDFRDRTGILQIVFNPEhNKNAWEVADKVRSEYVLAVKGTVVKRAP 85
Cdd:cd04317 1 RTHYCGELRESHVGQEVTLCGWVQRRRDHGGLIFIDLRDRYGIVQVVFDPE-EAPEFELAEKLRNESVIQVTGKVRARPE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 686452888 86 EAVNPKLKTGEVEVIVSEIIILNDAKTPPFQIEDDIDVDEQVRLKYRYLDLRRPEM 141
Cdd:cd04317 80 GTVNPKLPTGEIEVVASELEVLNKAKTLPFEIDDDVNVSEELRLKYRYLDLRRPKM 135
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
122-560 |
8.93e-47 |
|
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: 166.97 E-value: 8.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 122 DVDEQVRLKYRYLDLRRPEMQRSLILRSKAAKAFRDFLDEKGFVEVETPMLTKSTPEGareylvPSRVHPGEFF----VL 197
Cdd:cd00776 1 DANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEG------GAELFKVSYFgkpaYL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 198 PQSPQLFKQlLMVSGMERYYQIARCFRDEDLRADRQ-PEFTQVDIETSFL-SMEELLPMMEEMIAHVFKT---------- 265
Cdd:cd00776 75 AQSPQLYKE-MLIAALERVYEIGPVFRAEKSNTRRHlSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRvlercakele 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 266 TIGVD------VPRPFPRLTYAEAmarygsdkpdvrfgmeltdvsdlvatsdfkvfasvvsgggqVKAINAKGcGHYSRK 339
Cdd:cd00776 154 LVNQLnrellkPLEPFPRITYDEA-----------------------------------------IELLREKG-VEEEVK 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 340 EADDLGkfasrygakglawmgfKDGEvkgpiaKFFGEaeinslkerlaveegdlllFVADKPKVvadalgalrsklgael 419
Cdd:cd00776 192 WGEDLS----------------TEHE------RLLGE-------------------IVKGDPVF---------------- 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 420 glidhsqfaflwVVDFPLvewdeeSQRylalhhPF-TRPKDEDLHLLESdpgqvraqaYDMVLNGY-ELGGGSMRIYKRD 497
Cdd:cd00776 215 ------------VTDYPK------EIK------PFyMKPDDDNPETVES---------FDLLMPGVgEIVGGSQRIHDYD 261
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 686452888 498 VQEKMFRTLGLTEEEakqkFGFLLDAFDFGTPPHGGIALGLDRLIMLLAGRSNLREVIAFPKT 560
Cdd:cd00776 262 ELEERIKEHGLDPES----FEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFPRD 320
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
16-558 |
1.13e-36 |
|
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: 142.87 E-value: 1.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 16 EQVGQEVILNGWVQKRRDLGGVIFIDFRDRTGILQIVFNPEH-NKNAWEVADKVRSEYVLAVKGTVVKRapeavnpklKT 94
Cdd:COG1190 53 EETGDEVSVAGRIMAKRDMGKASFADLQDGSGRIQLYLRRDElGEEAYELFKLLDLGDIVGVEGTVFRT---------KT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 95 GEVEVIVSEIIILndAKT---PPFQIEDDIDVDEQVRlkYRYLDL-RRPEMQRSLILRSKAAKAFRDFLDEKGFVEVETP 170
Cdd:COG1190 124 GELSVKVEELTLL--SKSlrpLPEKFHGLTDPETRYR--QRYVDLiVNPEVRETFRKRSKIIRAIRRFLDERGFLEVETP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 171 MLTkSTPEGA-------------RE-YLvpsRVhpgeffvlpqSPQLF-KQLLmVSGMERYYQIARCFRDEDLRADRQPE 235
Cdd:COG1190 200 MLQ-PIAGGAaarpfithhnaldMDlYL---RI----------APELYlKRLI-VGGFERVFEIGRNFRNEGIDTTHNPE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 236 FTQVDIETSFLSMEELLPMMEEMIAHVFKTTIG----------VDVPRPFPRLTYAEAMARYGsdkpDVRFgMELTDVSD 305
Cdd:COG1190 265 FTMLELYQAYADYNDMMDLTEELIREAAEAVLGttkvtyqgqeIDLSPPWRRITMVEAIKEAT----GIDV-TPLTDDEE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 306 LvatsdfkvfasvvsgggqvkainakgcghysRKEADDLG-KFASRYGAkglawmgfkdGEVkgpIAKFFGEaeinslke 384
Cdd:COG1190 340 L-------------------------------RALAKELGiEVDPGWGR----------GKL---IDELFEE-------- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 385 rlaveegdlllFVADKpkvvadalgalrsklgaelgLIdhsQFAFlwVVDFPLvewdEESqrylalhhPFTRPKDEdlhl 464
Cdd:COG1190 368 -----------LVEPK--------------------LI---QPTF--VTDYPV----EVS--------PLAKRHRD---- 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 465 lesDPGQVraQAYDMVLNGYELGGGsmriYKR----DVQEKMFrtlgltEEEAKQK-------------FgflLDAFDFG 527
Cdd:COG1190 396 ---DPGLT--ERFELFIAGREIANA----FSElndpIDQRERF------EEQLELKaagddeampmdedF---LRALEYG 457
|
570 580 590
....*....|....*....|....*....|.
gi 686452888 528 TPPHGGIALGLDRLIMLLAGRSNLREVIAFP 558
Cdd:COG1190 458 MPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 488
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
15-558 |
9.99e-35 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 137.53 E-value: 9.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 15 LEQVGQEVILNGWVQKRRDLGGVIFIDFRDRTGILQIVFN----PEHNKNAW---EVADkvrseyVLAVKGTVVKRapea 87
Cdd:PRK00484 50 LEELEIEVSVAGRVMLKRVMGKASFATLQDGSGRIQLYVSkddvGEEALEAFkklDLGD------IIGVEGTLFKT---- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 88 vnpklKTGEVEVIVSEIIILNDAKTPP---FqiedDIDVDEQVRLKYRYLDL-RRPEMQRSLILRSKAAKAFRDFLDEKG 163
Cdd:PRK00484 120 -----KTGELSVKATELTLLTKSLRPLpdkF----HGLTDVETRYRQRYVDLiVNPESRETFRKRSKIISAIRRFLDNRG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 164 FVEVETPMLtKSTPEG--ARE------------YLvpsRVhpgeffvlpqSPQLF-KQLLmVSGMERYYQIARCFRDEDL 228
Cdd:PRK00484 191 FLEVETPML-QPIAGGaaARPfithhnaldidlYL---RI----------APELYlKRLI-VGGFERVYEIGRNFRNEGI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 229 RADRQPEFTQVDIETSFLSMEELLPMMEEMIAHVFKTTIG----------VDVPRPFPRLTYAEAMARYGsdkpdvrfGM 298
Cdd:PRK00484 256 DTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGttkvtyqgteIDFGPPFKRLTMVDAIKEYT--------GV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 299 ELTDVSDlvatsdfkvfasvvsgggqvkainakgcghysrkeaDDLGKFASRYGAKGLAWMGFkdGEVkgpIAKFFGEae 378
Cdd:PRK00484 328 DFDDMTD------------------------------------EEARALAKELGIEVEKSWGL--GKL---INELFEE-- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 379 inslkerlaveegdlllFVADKpkvvadalgalrsklgaelgLIdhsQFAFlwVVDFPLvewdEESqrylalhhPFTRPK 458
Cdd:PRK00484 365 -----------------FVEPK--------------------LI---QPTF--ITDYPV----EIS--------PLAKRH 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 459 DEDLHLLEsdpgqvRAQAYdmvLNGYELGGGsmriYKR--D--VQEKMFrtlgltEEEAKQK-------------FgflL 521
Cdd:PRK00484 391 REDPGLTE------RFELF---IGGREIANA----FSElnDpiDQRERF------EAQVEAKeagddeamfmdedF---L 448
|
570 580 590
....*....|....*....|....*....|....*..
gi 686452888 522 DAFDFGTPPHGGIALGLDRLIMLLAGRSNLREVIAFP 558
Cdd:PRK00484 449 RALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
16-560 |
1.99e-34 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 135.62 E-value: 1.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 16 EQVGQEVILNGWVQKRRDLGGVIFIDFRDRTGILQIVFNPEHNKNAWEVADKVRSEYVLAVKGTVVK--RAPeavnpklk 93
Cdd:PRK03932 13 KYVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDNGEEYFEEIKKLTTGSSVIVTGTVVEspRAG-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 94 tGEVEVIVSEIIIL-NDAKTPPFQiEDDIDVDeqVRLKYRYLDLRRPEMQRSLILRSKAAKAFRDFLDEKGFVEVETPML 172
Cdd:PRK03932 85 -QGYELQATKIEVIgEDPEDYPIQ-KKRHSIE--FLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVDTPII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 173 TKSTPEGAreylvpsrvhpGEFFVLPQSPQLFKQ-------LLMVSG---MERY-------YQIARCFRDEDLRADRQ-P 234
Cdd:PRK03932 161 TASDCEGA-----------GELFRVTTLDLDFSKdffgkeaYLTVSGqlyAEAYamalgkvYTFGPTFRAENSNTRRHlA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 235 EFTQVDIETSFLSMEELLPMMEEMIAHVFKTTI---------------GVDVPR-------PFPRLTYAEAMarygsdkp 292
Cdd:PRK03932 230 EFWMIEPEMAFADLEDNMDLAEEMLKYVVKYVLencpddleflnrrvdKGDIERlenfiesPFPRITYTEAI-------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 293 dvrfgmeltdvsDLVATSDFKvFASVVSGGgqvkainakgcghysrkeaDDLGKFASRYgakgLAwmgfkDGEVKGPIak 372
Cdd:PRK03932 302 ------------EILQKSGKK-FEFPVEWG-------------------DDLGSEHERY----LA-----EEHFKKPV-- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 373 ffgeaeinslkerlaveegdlllFVADKPKVVadalgalrsKlgaelglidhsqfAFlwvvdfplvewdeesqrYLalhh 452
Cdd:PRK03932 339 -----------------------FVTNYPKDI---------K-------------AF-----------------YM---- 352
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 453 pftRPKDEdlhllesdpGQVRAqAYDMVLNGY-ELGGGSMRIYKRDVQEKMFRTLGLTEEEakqkFGFLLDAFDFGTPPH 531
Cdd:PRK03932 353 ---RLNPD---------GKTVA-AMDLLAPGIgEIIGGSQREERLDVLEARIKELGLNKED----YWWYLDLRRYGSVPH 415
|
570 580
....*....|....*....|....*....
gi 686452888 532 GGIALGLDRLIMLLAGRSNLREVIAFPKT 560
Cdd:PRK03932 416 SGFGLGFERLVAYITGLDNIRDVIPFPRT 444
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
21-108 |
6.81e-33 |
|
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: 120.75 E-value: 6.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 21 EVILNGWVQKRRDLGGVIFIDFRDRTGILQIVFNPEHNKNAWEVADKVRSEYVLAVKGTVVKRAPeavnPKLKTGEVEVI 100
Cdd:cd04100 1 EVTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEELGEFFEEAEKLRTESVVGVTGTVVKRPE----GNLATGEIELQ 76
|
....*...
gi 686452888 101 VSEIIILN 108
Cdd:cd04100 77 AEELEVLS 84
|
|
| GAD |
pfam02938 |
GAD domain; This domain is found in some members of the GatB and aspartyl tRNA synthetases. |
315-408 |
1.76e-30 |
|
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: 114.67 E-value: 1.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 315 FASVVSGGGQVKAINAKGCGHYSRKEADDLGKFASRYGAKGLAWMGFKDGEVKGPIAKFFGEAEINSLKERLAVEEGDLL 394
Cdd:pfam02938 1 FSEALKSGGSVKALRVPGAAGLSRKEIDELERFAKEYGAKGLAWIKVEGGGHTGPIAKFLTEEEVEKLLEAVGAEDGDAL 80
|
90
....*....|....
gi 686452888 395 LFVADKPKVVADAL 408
Cdd:pfam02938 81 LFVADKKKTVNKAL 94
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
8-559 |
1.88e-30 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 125.59 E-value: 1.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 8 VQCGEVGLEQVGQEVILNGWVQKRRDLGGVIFIDFRDRTGILQIVF---NPEHNKNAWEVADKVRSEYVLAVKGtVVKRA 84
Cdd:PLN02850 70 TDVSDLGEELAGSEVLIRGRVHTIRGKGKSAFLVLRQSGFTVQCVVfvsEVTVSKGMVKYAKQLSRESVVDVEG-VVSVP 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 85 PEAVnpKLKTGEVEVIVSEIIILNDAKTP-PFQIED------DIDVDEQV-----------RLKYRYLDLRRPEMQRSLI 146
Cdd:PLN02850 149 KKPV--KGTTQQVEIQVRKIYCVSKALATlPFNVEDaarsesEIEKALQTgeqlvrvgqdtRLNNRVLDLRTPANQAIFR 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 147 LRSKAAKAFRDFLDEKGFVEVETPMLTKSTPEGAreylvpSRVHPGEFF----VLPQSPQLFKQLLMVSGMERYYQIARC 222
Cdd:PLN02850 227 IQSQVCNLFREFLLSKGFVEIHTPKLIAGASEGG------SAVFRLDYKgqpaCLAQSPQLHKQMAICGDFRRVFEIGPV 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 223 FRDEDLRADRQ-PEFTQVDIEtsflsME------ELLPMMEEMIAHVFkttigvdvprpfprltyaeamarygsDKPDVR 295
Cdd:PLN02850 301 FRAEDSFTHRHlCEFTGLDLE-----MEikehysEVLDVVDELFVAIF--------------------------DGLNER 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 296 FGMELtdvsdlvatsdfkvfasvvsgggqvKAINakgcghySRKEADDLgkfasRYGAKGLawmgfkdgevkgpiakffg 375
Cdd:PLN02850 350 CKKEL-------------------------EAIR-------EQYPFEPL-----KYLPKTL------------------- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 376 eaeinslkeRLAVEEGDLLLFVADkpkVVADALGALRSKLGAELGLIDHSQFAflwvVDFPLVEwdeesqRYLALHHPF- 454
Cdd:PLN02850 374 ---------RLTFAEGIQMLKEAG---VEVDPLGDLNTESERKLGQLVKEKYG----TDFYILH------RYPLAVRPFy 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 455 TRPKDEDLHLLESdpgqvraqaYDMVLNGYELGGGSMRIYKRDVQEKMFRTLGLTEEEAKQkfgfLLDAFDFGTPPHGGI 534
Cdd:PLN02850 432 TMPCPDDPKYSNS---------FDVFIRGEEIISGAQRVHDPELLEKRAEECGIDVKTIST----YIDSFRYGAPPHGGF 498
|
570 580
....*....|....*....|....*
gi 686452888 535 ALGLDRLIMLLAGRSNLREVIAFPK 559
Cdd:PLN02850 499 GVGLERVVMLFCGLNNIRKTSLFPR 523
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
6-558 |
1.00e-26 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 115.83 E-value: 1.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 6 RTVQCGEVGLEQVGQEVILNGWVQKRRDLGGVIFIDFRDRTGILQIVFN----PEHNKNAW----EVADKVrseyvlAVK 77
Cdd:PRK02983 638 PTHTVAEALDAPTGEEVSVSGRVLRIRDYGGVLFADLRDWSGELQVLLDasrlEQGSLADFraavDLGDLV------EVT 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 78 GTVVKRapeavnpklKTGEVEVIVSEIIILNDAKTPpfqIEDDID--VDEQVRLKYRYLDLR-RPEMQRSLILRSKAAKA 154
Cdd:PRK02983 712 GTMGTS---------RNGTLSLLVTSWRLAGKCLRP---LPDKWKglTDPEARVRQRYLDLAvNPEARDLLRARSAVVRA 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 155 FRDFLDEKGFVEVETPMLtkstpegareylvpSRVHPG---EFFV-----------LPQSPQLFKQLLMVSGMERYYQIA 220
Cdd:PRK02983 780 VRETLVARGFLEVETPIL--------------QQVHGGanaRPFVthinaydmdlyLRIAPELYLKRLCVGGVERVFELG 845
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 221 RCFRDEDLRADRQPEFTQVDIETSFLSMEELLPMMEEMIAHVfkttigvdvprpfprltyaeAMARYGSD---KPDVRFG 297
Cdd:PRK02983 846 RNFRNEGVDATHNPEFTLLEAYQAHADYDTMRDLTRELIQNA--------------------AQAAHGAPvvmRPDGDGV 905
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 298 MELTDVSDL--VATsdfkVFASVVSGGGQvkAINAKGcghysrkEADDLGKFASRYGAKGLAWMGfkdgevkgpiakffg 375
Cdd:PRK02983 906 LEPVDISGPwpVVT----VHDAVSEALGE--EIDPDT-------PLAELRKLCDAAGIPYRTDWD--------------- 957
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 376 eaeinslkerlaveEGDLLLfvadkpkvvadalgalrsklgaEL--GLIDHSQFAFLWVVDFPLvewdEESqrylalhhP 453
Cdd:PRK02983 958 --------------AGAVVL----------------------ELyeHLVEDRTTFPTFYTDFPT----SVS--------P 989
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 454 FTRPkdedlHllESDPGQvrAQAYDMVLNGYELGGGsmriY---------KRDVQEKMFRTLGLTEE--EAKQKFgflLD 522
Cdd:PRK02983 990 LTRP-----H--RSDPGL--AERWDLVAWGVELGTA----YseltdpveqRRRLTEQSLLAAGGDPEamELDEDF---LQ 1053
|
570 580 590
....*....|....*....|....*....|....*.
gi 686452888 523 AFDFGTPPHGGIALGLDRLIMLLAGRSnLREVIAFP 558
Cdd:PRK02983 1054 ALEYAMPPTGGLGMGVDRLVMLLTGRS-IRETLPFP 1088
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
16-559 |
2.01e-25 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 110.47 E-value: 2.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 16 EQVGQEVILNGWVQKRRDLGGVIFIDFRDRTGILQIVFNPEHN--KNAWEVADKVRSEYVLAVKGTVVKrapeAVNPKLK 93
Cdd:PTZ00401 75 ELVDKTVLIRARVSTTRKKGKMAFMVLRDGSDSVQAMAAVEGDvpKEMIDFIGQIPTESIVDVEATVCK----VEQPITS 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 94 TG--EVEVIVSEIIILNDA-KTPPFQIED--------DIDVDEQVRLKYRYLDLRRPEMQRSLILRSKAAKAFRDFLDEK 162
Cdd:PTZ00401 151 TShsDIELKVKKIHTVTESlRTLPFTLEDasrkesdeGAKVNFDTRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLIDS 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 163 GFVEVETPMLTKSTPEGAreylvpSRVHPGEFF----VLPQSPQLFKQLLMVSGMERYYQIARCFRDEDLRADRQ-PEFT 237
Cdd:PTZ00401 231 DFCEIHSPKIINAPSEGG------ANVFKLEYFnrfaYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNTHRHlTEFV 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 238 QVDIETSFLS-MEELLPMMEEMIAHVFKTTIG-----VDVPR--PFPRLTY---AEAMARYGsdkpdvrfgmeLTDVSDL 306
Cdd:PTZ00401 305 GLDVEMRINEhYYEVLDLAESLFNYIFERLAThtkelKAVCQqyPFEPLVWkltPERMKELG-----------VGVISEG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 307 VATSDfKVFASVVSGGGQVKAINAKGCghysrkeaddlgkfasrygakglawmgfkdgevkgpIAkffgeaeinslkerl 386
Cdd:PTZ00401 374 VEPTD-KYQARVHNMDSRMLRINYMHC------------------------------------IE--------------- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 387 aveegdLLLFVADKPKVVADALGALRSKLgaeLGLIDHSQFAflwvVDFPLvewdeeSQRYLALHHPF-TRPKDEDLHLL 465
Cdd:PTZ00401 402 ------LLNTVLEEKMAPTDDINTTNEKL---LGKLVKERYG----TDFFI------SDRFPSSARPFyTMECKDDERFT 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 466 ESdpgqvraqaYDMVLNGYELGGGSMRIYKRDVQEKMFRTLGLTEEEAKQkfgfLLDAFDFGTPPHGGIALGLDRLIMLL 545
Cdd:PTZ00401 463 NS---------YDMFIRGEEISSGAQRIHDPDLLLARAKMLNVDLTPIKE----YVDSFRLGAWPHGGFGVGLERVVMLY 529
|
570
....*....|....
gi 686452888 546 AGRSNLREVIAFPK 559
Cdd:PTZ00401 530 LGLSNVRLASLFPR 543
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
26-558 |
3.07e-25 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 110.51 E-value: 3.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 26 GWVQKRRDLGGVIFIDFRDRTGILQIVFNPEHNKNAwEVADKVRSEyvLAVkGTVVkrAPEAVNPKLKTGEVEVIVSEII 105
Cdd:PTZ00385 114 GRVTSVRDIGKIIFVTIRSNGNELQVVGQVGEHFTR-EDLKKLKVS--LRV-GDII--GADGVPCRMQRGELSVAASRML 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 106 ILNdaktpPFQIEDDIDV----------DEQVRLKYRYLDL-RRPEMQRSLILRSKAAKAFRDFLDEKGFVEVETPML-T 173
Cdd:PTZ00385 188 ILS-----PYVCTDQVVCpnlrgftvlqDNDVKYRYRFTDMmTNPCVIETIKKRHVMLQALRDYFNERNFVEVETPVLhT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 174 KSTPEGAREYLVPSRVHPGEFFvLPQSPQLFKQLLMVSGMERYYQIARCFRDEDLRADRQPEFTQVDIETSFLSMEELLP 253
Cdd:PTZ00385 263 VASGANAKSFVTHHNANAMDLF-LRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTSCEFYAAYHTYEDLMP 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 254 MMEEMIAHVFKTTIGVDVPRPFPRltyaeamaRYGSDKPDVRFGMELTDVSdlvatsdfkVFASVVSGGGqvkainakgc 333
Cdd:PTZ00385 342 MTEDIFRQLAMRVNGTTVVQIYPE--------NAHGNPVTVDLGKPFRRVS---------VYDEIQRMSG---------- 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 334 ghYSRKEADDLGKfasrygAKGLAWMgfkdgevkgpiAKFFGEAEINSLKERLAVEEGDLLL--FVADkpKVVADALgal 411
Cdd:PTZ00385 395 --VEFPPPNELNT------PKGIAYM-----------SVVMLRYNIPLPPVRTAAKMFEKLIdfFITD--RVVEPTF--- 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 412 rsklgaelgLIDHSQFAflwvvdFPLVEwdEESQRylalhhpftrpkdedlhllesdPGqvRAQAYDMVLNGYELGGGSM 491
Cdd:PTZ00385 451 ---------VMDHPLFM------SPLAK--EQVSR----------------------PG--LAERFELFVNGIEYCNAYS 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 686452888 492 RI------YKRDVQEKMFRTLGltEEEAKQKFGFLLDAFDFGTPPHGGIALGLDRLIMLLAGRSNLREVIAFP 558
Cdd:PTZ00385 490 ELndpheqYHRFQQQLVDRQGG--DEEAMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFP 560
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
139-558 |
1.35e-23 |
|
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: 101.89 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 139 PEMQRSLILRSKAAKAFRDFLDEKGFVEVETPMLtKSTPEG--AReylvPSRVHPGEFFV---LPQSPQLFKQLLMVSGM 213
Cdd:cd00775 2 EEVRQTFIVRSKIISYIRKFLDDRGFLEVETPML-QPIAGGaaAR----PFITHHNALDMdlyLRIAPELYLKRLIVGGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 214 ERYYQIARCFRDEDLRADRQPEFTQVDIETSFLSMEELLPMMEEMIAHVFKTTIG----------VDVPRPFPRLTYAEA 283
Cdd:cd00775 77 ERVYEIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGktkieyggkeLDFTPPFKRVTMVDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 284 MARYgsdkpdvrFGMELTDVSDlvatsdfkvfasvvsgggqvkainakgcghysrkeaddlgkFASRYGAKGLAWMgFKD 363
Cdd:cd00775 157 LKEK--------TGIDFPELDL-----------------------------------------EQPEELAKLLAKL-IKE 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 364 GEVKGP-----IAKFFGEaeinslkerlAVEEgdlllfvadkpkvvadalgalrsklgaelgliDHSQFAFlwVVDFPLv 438
Cdd:cd00775 187 KIEKPRtlgklLDKLFEE----------FVEP--------------------------------TLIQPTF--IIDHPV- 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 439 ewdEESqrylalhhPFTRPKDEDLHLLESdpgqvraqaYDMVLNGYELGGGSMRIYKRDVQEKMFrtlgltEEEAKQK-- 516
Cdd:cd00775 222 ---EIS--------PLAKRHRSNPGLTER---------FELFICGKEIANAYTELNDPFDQRERF------EEQAKQKea 275
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 686452888 517 -----------FgflLDAFDFGTPPHGGIALGLDRLIMLLAGRSNLREVIAFP 558
Cdd:cd00775 276 gddeammmdedF---VTALEYGMPPTGGLGIGIDRLVMLLTDSNSIRDVILFP 325
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
15-306 |
1.65e-23 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 104.37 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 15 LEQVGQEVILNGWVQKRRDLGGVIFIDFRDRTGILQI----------VFNPEHNKnaWEVADkvrseyVLAVKGTVVKRa 84
Cdd:PRK12445 61 LESLNIEVSVAGRMMTRRIMGKASFVTLQDVGGRIQLyvardslpegVYNDQFKK--WDLGD------IIGARGTLFKT- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 85 peavnpklKTGEVEVIVSEIIILNDAKTPpfqIEDDID--VDEQVRLKYRYLDLRRPEMQR-SLILRSKAAKAFRDFLDE 161
Cdd:PRK12445 132 --------QTGELSIHCTELRLLTKALRP---LPDKFHglQDQEVRYRQRYLDLIANDKSRqTFVVRSKILAAIRQFMVA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 162 KGFVEVETPMLtKSTPEGA--REYLVPSRVHPGEFFvLPQSPQLFKQLLMVSGMERYYQIARCFRDEDLRADRQPEFTQV 239
Cdd:PRK12445 201 RGFMEVETPMM-QVIPGGAsaRPFITHHNALDLDMY-LRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMM 278
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 686452888 240 DIETSFLSMEELLPMMEEMIAHVFKTTIG----------VDVPRPFPRLTYAEAMARYgsdKPDvrfgmelTDVSDL 306
Cdd:PRK12445 279 ELYMAYADYHDLIELTESLFRTLAQEVLGttkvtygehvFDFGKPFEKLTMREAIKKY---RPE-------TDMADL 345
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
4-558 |
2.21e-23 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 104.30 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 4 QYRTVQCGEvglEQVGQEVILNGWVQKRRDLGGVIFIDFRDRTGILQIVFNPEHNKNAWEVADKVRSEY----VLAVKGT 79
Cdd:PLN02502 96 KYGSLENGE---ELEDVSVSVAGRIMAKRAFGKLAFYDLRDDGGKIQLYADKKRLDLDEEEFEKLHSLVdrgdIVGVTGT 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 80 VvkrapeavnPKLKTGEVEVIVSEIIILNDA-KTPPFQIEDDIDVDEqvRLKYRYLDL-RRPEMQRSLILRSKAAKAFRD 157
Cdd:PLN02502 173 P---------GKTKKGELSIFPTSFEVLTKClLMLPDKYHGLTDQET--RYRQRYLDLiANPEVRDIFRTRAKIISYIRR 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 158 FLDEKGFVEVETPMLtKSTPEGA--ReylvPSRVHPGEF---FVLPQSPQLFKQLLMVSGMERYYQIARCFRDEDLRADR 232
Cdd:PLN02502 242 FLDDRGFLEVETPML-NMIAGGAaaR----PFVTHHNDLnmdLYLRIATELHLKRLVVGGFERVYEIGRQFRNEGISTRH 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 233 QPEFTQVDIETSFLSMEELLPMMEEMIAHVFKTTIG----------VDVPRPFPRLTYAEamarygsdkpDVRFGMELTD 302
Cdd:PLN02502 317 NPEFTTCEFYQAYADYNDMMELTEEMVSGMVKELTGsykikyhgieIDFTPPFRRISMIS----------LVEEATGIDF 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 303 VSDLvatsdfkvfasvvsgggqvkainakgcghysrkEADDLGKFASRYGAKGlawmgfkDGEVKGP------IAKFFGE 376
Cdd:PLN02502 387 PADL---------------------------------KSDEANAYLIAACEKF-------DVKCPPPqttgrlLNELFEE 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 377 aeinslkerlAVEEGdlLL---FVADKPKVVAdalgalrsklgaelglidhsqfaflwvvdfPLVEWdeesqrylalHhp 453
Cdd:PLN02502 427 ----------FLEET--LVqptFVLDHPVEMS------------------------------PLAKP----------H-- 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 454 ftrpkdedlhllESDPGQVraQAYDMVLNGYELGGGSMRIYKRDVQEKMFrtlgltEEEAKQK-----FGFLLD-----A 523
Cdd:PLN02502 453 ------------RSKPGLT--ERFELFINGRELANAFSELTDPVDQRERF------EEQVKQHnagddEAMALDedfctA 512
|
570 580 590
....*....|....*....|....*....|....*
gi 686452888 524 FDFGTPPHGGIALGLDRLIMLLAGRSNLREVIAFP 558
Cdd:PLN02502 513 LEYGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFP 547
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
11-114 |
2.48e-22 |
|
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: 91.99 E-value: 2.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 11 GEVGLEQVGQEVILNGWVQKRRDLGGVIFIDFRDRTGILQIVFN-PEHNKNAWEVADKVRSEYVLAVKGTVvkrapEAvN 89
Cdd:cd04316 4 AEITPELDGEEVTVAGWVHEIRDLGGIKFVILRDREGIVQVTAPkKKVDKELFKTVRKLSRESVISVTGTV-----KA-E 77
|
90 100
....*....|....*....|....*
gi 686452888 90 PKLKTGeVEVIVSEIIILNDAKTPP 114
Cdd:cd04316 78 PKAPNG-VEIIPEEIEVLSEAKTPL 101
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
124-283 |
1.67e-19 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 90.08 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 124 DEQVRLKYRYLDLRRPEMQRSLILRSKAAKAFRDFLDEKGFVEVETPMLTKSTPEGARE-----YLVPSRVHPGEFFVLP 198
Cdd:PRK06462 9 EYEEFLRMSWKHISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIISPSTDPLMGLgsdlpVKQISIDFYGVEYYLA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 199 QSPQLFKQlLMVSGMERYYQIARCFRDEDLRADRQP---EFTQVDIETSFLSMEELLPMMEEMIAHVFKT---------- 265
Cdd:PRK06462 89 DSMILHKQ-LALRMLGKIFYLSPNFRLEPVDKDTGRhlyEFTQLDIEIEGADLDEVMDLIEDLIKYLVKElleehedele 167
|
170 180
....*....|....*....|.
gi 686452888 266 TIGVDVP---RPFPRLTYAEA 283
Cdd:PRK06462 168 FFGRDLPhlkRPFKRITHKEA 188
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
147-263 |
3.99e-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: 86.02 E-value: 3.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 147 LRSKAAKAFRDFLDEKGFVEVETPMLTKSTPEGAR----EYLVPSRVHPGEFFVLPQSPQLFKQLLMVS----GMERYYQ 218
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAghepKDLLPVGAENEEDLYLRPTLEPGLVRLFVShirkLPLRLAE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 686452888 219 IARCFRDEDLRAD--RQPEFTQVDIETSFL------SMEELLPMMEEMIAHVF 263
Cdd:cd00768 81 IGPAFRNEGGRRGlrRVREFTQLEGEVFGEdgeeasEFEELIELTEELLRALG 133
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
39-291 |
1.47e-17 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 86.22 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 39 FIDFRDRTGILQIVFN---PEHNK-NAWEVADKVRSEYVLAVKGtvvkrapeaVNPKLKTGEVEVIVSEIIILNDA-KTP 113
Cdd:PTZ00417 153 FFDLVGDGAKIQVLANfafHDHTKsNFAECYDKIRRGDIVGIVG---------FPGKSKKGELSIFPKETIILSPClHML 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 114 PFQIEDDidvDEQVRLKYRYLDLRRPEMQRS-LILRSKAAKAFRDFLDEKGFVEVETPMLT-KSTPEGAREYLvpsrVHP 191
Cdd:PTZ00417 224 PMKYGLK---DTEIRYRQRYLDLMINESTRStFITRTKIINYLRNFLNDRGFIEVETPTMNlVAGGANARPFI----THH 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 192 GEF---FVLPQSPQLFKQLLMVSGMERYYQIARCFRDEDLRADRQPEFTQVDIETSFLSMEELLPMMEE----MIAHVFK 264
Cdd:PTZ00417 297 NDLdldLYLRIATELPLKMLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDffsqLVMHLFG 376
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 686452888 265 T-------------TIGVDVPRPFPRLTYAEAMARYGSDK 291
Cdd:PTZ00417 377 TykilynkdgpekdPIEIDFTPPYPKVSIVEELEKLTNTK 416
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
22-107 |
3.33e-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: 73.42 E-value: 3.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 22 VILNGWV-QKRRDLGGVIFIDFRDRTGILQIVFNPEhnkNAWEVADKVRSEYVLAVKGTVVKRapeavnpklKTGEVEVI 100
Cdd:pfam01336 1 VTVAGRVtSIRRSGGKLLFLTLRDGTGSIQVVVFKE---EAEKLAKKLKEGDVVRVTGKVKKR---------KGGELELV 68
|
....*..
gi 686452888 101 VSEIIIL 107
Cdd:pfam01336 69 VEEIELL 75
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
158-556 |
1.63e-14 |
|
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: 74.12 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 158 FLDEKGFVEVETPMLTKST-PEGAREYL---VPSRVHPGEFFVLPQSPQLF-KQLLmVSGMERYYQIARCFRDEDLRADR 232
Cdd:TIGR00462 1 FFAERGVLEVETPLLSPAPvTDPHLDAFateFVGPDGQGRPLYLQTSPEYAmKRLL-AAGSGPIFQICKVFRNGERGRRH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 233 QPEFTQVDIETSFLSMEELLPMMEEMIAHVFKttigvDVPRPFPRLTYAEAMARYgsdkpdVRFGMELTDVSDLVATSDF 312
Cdd:TIGR00462 80 NPEFTMLEWYRPGFDYHDLMDEVEALLQELLG-----DPFAPAERLSYQEAFLRY------AGIDPLTASLAELQAAAAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 313 KvfasvvsgggqvkainakgcGHYSRKEADDLGKFasrygakglawmgfkdgevkgpiakffgeaeinslkerlaveegD 392
Cdd:TIGR00462 149 H--------------------GIRASEEDDRDDLL--------------------------------------------D 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 393 LLLfvadkpkvvadaLGALRSKLGAElglidhsqfAFLWVVDFPlvewdeESQRYLAlhhpftRPKDEDLHLLEsdpgqv 472
Cdd:TIGR00462 165 LLF------------SEKVEPHLGFG---------RPTFLYDYP------ASQAALA------RISPDDPRVAE------ 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 473 RAQAYdmvLNGYELGGG----------SMRiYKRDVQEKmfRTLGLTEEEAKQKFgflLDAFDFGTPPHGGIALGLDRLI 542
Cdd:TIGR00462 206 RFELY---IKGLELANGfheltdaaeqRRR-FEADNALR--KALGLPRYPLDERF---LAALEAGLPECSGVALGVDRLL 276
|
410
....*....|....
gi 686452888 543 MLLAGRSNLREVIA 556
Cdd:TIGR00462 277 MLALGADSIDDVLA 290
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
14-566 |
2.69e-13 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 72.70 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 14 GLEQVGQEVILNGWVQKRRDLGGVIFIDFRDRTGI--LQIVFNPEHnknawEVADKVRSEYVLA-----VKGTVVkrapE 86
Cdd:PLN02603 102 GLARVGKTLNVMGWVRTLRAQSSVTFIEVNDGSCLsnMQCVMTPDA-----EGYDQVESGLITTgasvlVQGTVV----S 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 87 AVNPKLKtgeVEVIVSEIIILNDAKtPPFQIEDDIDVDEQVRLKyRYLDLRRPEMQRSLILRSKAAKAFRDFLDEKGFVE 166
Cdd:PLN02603 173 SQGGKQK---VELKVSKIVVVGKSD-PSYPIQKKRVSREFLRTK-AHLRPRTNTFGAVARVRNALAYATHKFFQENGFVW 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 167 VETPMLTKSTPEGAREylvpsrvhpgEFFV---LPQSPQLFKQLLmvsgmeryyqiarcfrdedlraDRQPEFT--QVDI 241
Cdd:PLN02603 248 VSSPIITASDCEGAGE----------QFCVttlIPNSAENGGSLV----------------------DDIPKTKdgLIDW 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 242 ETSFLSMEELLPMMEEMIAHvfkttigvdvprpfprlTYAEAMarygsdkpdvrfgmeltdvsdlvatSDFKVFasvvsg 321
Cdd:PLN02603 296 SQDFFGKPAFLTVSGQLNGE-----------------TYATAL-------------------------SDVYTF------ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 322 GGQVKAINAKGCGHysrkeaddLGKFasrygakglaWM-----GFKDGEVKGPIAKFFGEAEINSL----KERLA----- 387
Cdd:PLN02603 328 GPTFRAENSNTSRH--------LAEF----------WMiepelAFADLNDDMACATAYLQYVVKYIlencKEDMEffntw 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 388 VEEG--DLLLFVADKPKVVADALGALRSKLGAElglidhSQFaflwvvDFPlVEW----DEESQRYLALHHPFTRP---- 457
Cdd:PLN02603 390 IEKGiiDRLSDVVEKNFVQLSYTDAIELLLKAK------KKF------EFP-VKWgldlQSEHERYITEEAFGGRPviir 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 458 ---KD-EDLHLLESDPGQVRAqAYDMVLNGY-ELGGGSMRIYKRDVQEKMFRTLGLTeeeaKQKFGFLLDAFDFGTPPHG 532
Cdd:PLN02603 457 dypKEiKAFYMRENDDGKTVA-AMDMLVPRVgELIGGSQREERLEYLEARLDELKLN----KESYWWYLDLRRYGSVPHA 531
|
570 580 590
....*....|....*....|....*....|....
gi 686452888 533 GIALGLDRLIMLLAGRSNLREVIAFPKTASASDL 566
Cdd:PLN02603 532 GFGLGFERLVQFATGIDNIRDAIPFPRVPGSAEF 565
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
21-134 |
6.28e-11 |
|
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: 59.46 E-value: 6.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 21 EVILNGWVQKRRDLGGVIFIDFRDRTGILQIVFNPEHNKNAWEVADKVRSEYVLAVKGTVVK--RAPeavnpklktGEVE 98
Cdd:cd04319 1 KVTLAGWVYRKREVGKKAFIVLRDSTGIVQAVFSKDLNEEAYREAKKVGIESSVIVEGAVKAdpRAP---------GGAE 71
|
90 100 110
....*....|....*....|....*....|....*.
gi 686452888 99 VIVSEIIILNDAKtpPFQIEDdiDVDEQVRLKYRYL 134
Cdd:cd04319 72 VHGEKLEIIQNVE--FFPITE--DASDEFLLDVRHL 103
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
6-566 |
2.77e-10 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 63.09 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 6 RTVQC---GEVGLeqVGQEVILNGWVQKRRDLG--GVIFIDFRDRT--GILQIVFNPehnkNAWEVADKVRSEYVLAVKG 78
Cdd:PLN02221 36 RSILDrpdGGAGL--AGQKVRIGGWVKTGREQGkgTFAFLEVNDGScpANLQVMVDS----SLYDLSTLVATGTCVTVDG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 79 tVVKRAPEAVNPKLKtgeVEVIVSEIIILNDAKTPPFQIEDDIDVDEQVRlkyRYLDLRRPEMQRSLILRSKAAKAF--R 156
Cdd:PLN02221 110 -VLKVPPEGKGTKQK---IELSVEKVIDVGTVDPTKYPLPKTKLTLEFLR---DVLHLRSRTNSISAVARIRNALAFatH 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 157 DFLDEKGFVEVETPMLTKSTPEGAREylvpsrvhpgeffvlpqspqLFKQLLMVSGMERYyqiarcfrDEDLRADRQPef 236
Cdd:PLN02221 183 SFFQEHSFLYIHTPIITTSDCEGAGE--------------------MFQVTTLINYTERL--------EQDLIDNPPP-- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 237 TQVDIETSFLSMEELLPMMEEM-IAHVFKTTIGVDVPRpfprLTYAEAMARYGSDKPDVRFGMELTDvSDLVATSDFKVF 315
Cdd:PLN02221 233 TEADVEAARLIVKERGEVVAQLkAAKASKEEITAAVAE----LKIAKESLAHIEERSKLKPGLPKKD-GKIDYSKDFFGR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 316 ASVVSGGGQVKaINAKGCG----------------HYSRKEA---------------DDLgKFASRYGAKGLAWMGFKDG 364
Cdd:PLN02221 308 QAFLTVSGQLQ-VETYACAlssvytfgptfraensHTSRHLAefwmvepeiafadleDDM-NCAEAYVKYMCKWLLDKCF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 365 EVKGPIAKFFGEAEINSLK-------ERLAVEEGDLLLfvadkPKVVADalgalrsklGAELgliDHSqfaflwvvdfpl 437
Cdd:PLN02221 386 DDMELMAKNFDSGCIDRLRmvastpfGRITYTEAIELL-----EEAVAK---------GKEF---DNN------------ 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 438 VEWD----EESQRYLA---LHHP---FTRPKDEDLHLLESDPGQVRAQAYDMVLNGY-ELGGGSMRIYKRDVQEKMFRTL 506
Cdd:PLN02221 437 VEWGidlaSEHERYLTevlFQKPlivYNYPKGIKAFYMRLNDDEKTVAAMDVLVPKVgELIGGSQREERYDVIKQRIEEM 516
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 507 GLTEEeakqKFGFLLDAFDFGTPPHGGIALGLDRLIMLLAGRSNLREVIAFPKTASASDL 566
Cdd:PLN02221 517 GLPIE----PYEWYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPRYPGKADL 572
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
21-82 |
1.93e-08 |
|
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: 51.85 E-value: 1.93e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 686452888 21 EVILNGWVQKRRDLGGVIFIDFRDRTGILQIVFNPEhNKNAWEVADKVRSEYVLAVKGTVVK 82
Cdd:cd04323 1 RVKVFGWVHRLRSQKKLMFLVLRDGTGFLQCVLSKK-LVTEFYDAKSLTQESSVEVTGEVKE 61
|
|
| ScAspRS_mt_like_N |
cd04321 |
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
21-109 |
2.13e-08 |
|
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: 51.55 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 21 EVILNGWVQKRRDLGG-VIFIDFRDRTG-ILQIVFNPEHnkNAWEVADKVRSEYVLAVKGTVVKRAPeavNPKLKTGEVE 98
Cdd:cd04321 1 KVTLNGWIDRKPRIVKkLSFADLRDPNGdIIQLVSTAKK--DAFSLLKSITAESPVQVRGKLQLKEA---KSSEKNDEWE 75
|
90
....*....|.
gi 686452888 99 VIVSEIIILND 109
Cdd:cd04321 76 LVVDDIQTLNA 86
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
21-107 |
6.81e-07 |
|
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: 47.17 E-value: 6.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 21 EVILNGWVQKRRDLGGVIFIDFRDRTGI--LQIVFNPEhnKNAWEVADKVRSEYVLAVKGTVVKRAPeavnpklKTGEVE 98
Cdd:cd04318 1 EVTVNGWVRSVRDSKKISFIELNDGSCLknLQVVVDKE--LTNFKEILKLSTGSSIRVEGVLVKSPG-------AKQPFE 71
|
....*....
gi 686452888 99 VIVSEIIIL 107
Cdd:cd04318 72 LQAEKIEVL 80
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
438-559 |
9.44e-07 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 51.95 E-value: 9.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 438 VEW----DEESQRYLA---LHHP---FTRPKDEDLHLLESDPGQVRAQAYDMVLNGY-ELGGGSMRIYKRDVQEKMFRTL 506
Cdd:PTZ00425 451 VKWgmdlQSEHERFVAeqiFKKPvivYNYPKDLKAFYMKLNEDQKTVAAMDVLVPKIgEVIGGSQREDNLERLDKMIKEK 530
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 686452888 507 GLTEEEakqkFGFLLDAFDFGTPPHGGIALGLDRLIMLLAGRSNLREVIAFPK 559
Cdd:PTZ00425 531 KLNMES----YWWYRQLRKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFPR 579
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
21-136 |
1.69e-06 |
|
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: 46.70 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 21 EVILNGWVQKRRDLGGVIFIDFRDRTGILQIVFN-----PEHN---KNAWEVADkvrseyVLAVKGTVVKRapeavnpkl 92
Cdd:cd04322 1 EVSVAGRIMSKRGSGKLSFADLQDESGKIQVYVNkddlgEEEFedfKKLLDLGD------IIGVTGTPFKT--------- 65
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 686452888 93 KTGEVEVIVSEIIILndAKT---PPFQIEDDIDVDEQVRLkyRYLDL 136
Cdd:cd04322 66 KTGELSIFVKEFTLL--SKSlrpLPEKFHGLTDVETRYRQ--RYLDL 108
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
145-287 |
1.95e-06 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 49.93 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 145 LILRSKAAKAFRDFLDEKGFVEVETPMLTKSTpegareyLVPSRVHPGE-FFVLPQSPQLFKQLLMVS---GMERY---- 216
Cdd:PRK09350 5 LLKRAKIIAEIRRFFADRGVLEVETPILSQAT-------VTDIHLVPFEtRFVGPGASQGKTLWLMTSpeyHMKRLlaag 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 686452888 217 ----YQIARCFRDEDLRADRQPEFTQVDIETSFLSMEELLPMMEEMIAHVFKTtigvdvpRPFPRLTYAEAMARY 287
Cdd:PRK09350 78 sgpiFQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDC-------EPAESLSYQQAFLRY 145
|
|
| GatE |
COG2511 |
Archaeal Glu-tRNAGln amidotransferase subunit E, contains GAD domain [Translation, ribosomal ... |
302-410 |
7.15e-05 |
|
Archaeal Glu-tRNAGln amidotransferase subunit E, contains GAD domain [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442001 [Multi-domain] Cd Length: 630 Bit Score: 45.94 E-value: 7.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 302 DVSDLVATSDFKVFASVVSGGGQVKAINAKGCG-------HYSRKEADDLGKFASRYGAKGLawmgFKDGEVKGpiakfF 374
Cdd:COG2511 284 DVTDVFKDTKSKVIKKALKKGGKVLAVKLPGFAgllgreiQPGRRLGTELADYAKFWGVGGI----FHTDELPN-----Y 354
|
90 100 110
....*....|....*....|....*....|....*...
gi 686452888 375 G--EAEINSLKERLAVEEGDLLLFVADKPKVVADALGA 410
Cdd:COG2511 355 GitEEEVEALREALGAGEEDAFVIVADEEEKAKKALEA 392
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
474-560 |
2.12e-04 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 44.09 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 474 AQAYDMVL-NGYELGGGSMRIYKRDVQEKMFRTLGLTEEEakqkFGFLLDAFDFGTPPHGGIALGLDRLIMLLAGRSNLR 552
Cdd:PLN02532 544 VAAFDLVVpKVGTVITGSQNEERMDILNARIEELGLPREQ----YEWYLDLRRHGTVKHSGFSLGFELMVLFATGLPDVR 619
|
....*...
gi 686452888 553 EVIAFPKT 560
Cdd:PLN02532 620 DAIPFPRS 627
|
|
| PRK04028 |
PRK04028 |
Glu-tRNA(Gln) amidotransferase subunit GatE; |
299-410 |
1.24e-03 |
|
Glu-tRNA(Gln) amidotransferase subunit GatE;
Pssm-ID: 235205 [Multi-domain] Cd Length: 630 Bit Score: 41.73 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686452888 299 ELTDVSDLVATSDFKVFASVVSGGGQVKAINAKGC-GHYSR---------KEADDLGKfasRYGAKGLawmgFKDGEVKG 368
Cdd:PRK04028 280 EIVDVTELFKDTKSKIIKKALKKGGKVLAIKLPGFkGLLGReiqpgrrlgTELADYAK---AWGVGGI----FHTDELPA 352
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 686452888 369 piakfFG--EAEINSLKERLAVEEGDLLLFVADKPKVVADALGA 410
Cdd:PRK04028 353 -----YGitEEEVEALREALGAGENDAFILVADEEEKAEKALEA 391
|
|
| |
