|
Name |
Accession |
Description |
Interval |
E-value |
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
7-595 |
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: 1157.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 7 LKRTHYCGELREKNINEEVVLMGWVQKKRNLGGLVFVDLRDTSGLCQIVFDTDVDKEAFEKAEKLGAEFVIAVKGKVCER 86
Cdd:COG0173 1 MYRTHYCGELRESDVGQEVTLSGWVHRRRDHGGLIFIDLRDRYGITQVVFDPDDSAEAFEKAEKLRSEYVIAVTGKVRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 87 Q--SKNPNMPTGDIEIFATELRLLNKSETPPIYIKDDDDVSEALRLKYRYLDLRKPSMQRNLKLRHKVMNITRNYLSNNR 164
Cdd:COG0173 81 PegTVNPKLPTGEIEVLASELEILNKAKTPPFQIDDDTDVSEELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDENG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 165 FCEIETPFLIAPTPEGARDYLVPSRVNPGKFYALPQSPQLYKQLLMVSGMDRYFQIVKCFRDEDLRADRQPEFTQIDCEM 244
Cdd:COG0173 161 FLEIETPILTKSTPEGARDYLVPSRVHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFRDEDLRADRQPEFTQLDIEM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 245 SFVEQEDVMSMIEGLLEAIFKEVLDVELALPLPKMTYAEAMSKYGSDKPDTRFGYELTDISDVVCNCGFKVFADATQPGK 324
Cdd:COG0173 241 SFVDQEDVFELMEGLIRHLFKEVLGVELPTPFPRMTYAEAMERYGSDKPDLRFGLELVDVTDIFKDSGFKVFAGAAENGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 325 SVRGINVKGKAdDFTRKQISSLEEHAKTYRAKGLAWMKVGQEGVTSPIAKFFNEEEMNAILTRMNAEVGDLLLFVADKNS 404
Cdd:COG0173 321 RVKAINVPGGA-SLSRKQIDELTEFAKQYGAKGLAYIKVNEDGLKSPIAKFLSEEELAAILERLGAKPGDLIFFVADKPK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 405 IVFDALGQVRLEVANRLNLLDKNVYNLLWVTEFPVFEEDEETGTFSAMHHPFTSPMDEDLDKLEEgDKSSLRAKAYDIVL 484
Cdd:COG0173 400 VVNKALGALRLKLGKELGLIDEDEFAFLWVVDFPLFEYDEEEGRWVAMHHPFTMPKDEDLDLLET-DPGKVRAKAYDLVL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 485 NGYEIGGGSVRISNSDVQSRMFKALGFTEERANEKFGYLLEAFKYGTPPHAGLAFGLDRLVMLLAGTDNIREVIAFPKNQ 564
Cdd:COG0173 479 NGYELGGGSIRIHDPELQEKVFELLGISEEEAEEKFGFLLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFPKTQ 558
|
570 580 590
....*....|....*....|....*....|.
gi 490589120 565 NAVCPMTNAPTLAEDEQLEELSIKVDIKDNE 595
Cdd:COG0173 559 SAQDLMTGAPSEVDEKQLKELHIRLRPPEKK 589
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
6-593 |
0e+00 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 1129.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 6 GLKRTHYCGELREKNINEEVVLMGWVQKKRNLGGLVFVDLRDTSGLCQIVFDtdVDKEAFEKAEKLGAEFVIAVKGKVCE 85
Cdd:PRK00476 1 HMMRTHYCGELRESHVGQTVTLCGWVHRRRDHGGLIFIDLRDREGIVQVVFD--PDAEAFEVAESLRSEYVIQVTGTVRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 86 R--QSKNPNMPTGDIEIFATELRLLNKSETPPIYIKDDDDVSEALRLKYRYLDLRKPSMQRNLKLRHKVMNITRNYLSNN 163
Cdd:PRK00476 79 RpeGTVNPNLPTGEIEVLASELEVLNKSKTLPFPIDDEEDVSEELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDDN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 164 RFCEIETPFLIAPTPEGARDYLVPSRVNPGKFYALPQSPQLYKQLLMVSGMDRYFQIVKCFRDEDLRADRQPEFTQIDCE 243
Cdd:PRK00476 159 GFLEIETPILTKSTPEGARDYLVPSRVHPGKFYALPQSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADRQPEFTQIDIE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 244 MSFVEQEDVMSMIEGLLEAIFKEVLDVELALPLPKMTYAEAMSKYGSDKPDTRFGYELTDISDVVCNCGFKVFADATQPG 323
Cdd:PRK00476 239 MSFVTQEDVMALMEGLIRHVFKEVLGVDLPTPFPRMTYAEAMRRYGSDKPDLRFGLELVDVTDLFKDSGFKVFAGAANDG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 324 KSVRGINVKGKADDFTRKQISSLEEHAKTYRAKGLAWMKVGQEGVTSPIAKFFNEEEMNAILTRMNAEVGDLLLFVADKN 403
Cdd:PRK00476 319 GRVKAIRVPGGAAQLSRKQIDELTEFAKIYGAKGLAYIKVNEDGLKGPIAKFLSEEELAALLERTGAKDGDLIFFGADKA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 404 SIVFDALGQVRLEVANRLNLLDKNVYNLLWVTEFPVFEEDEETGTFSAMHHPFTSPMDEDLDKLEEGDKSSLRAKAYDIV 483
Cdd:PRK00476 399 KVVNDALGALRLKLGKELGLIDEDKFAFLWVVDFPMFEYDEEEGRWVAAHHPFTMPKDEDLDELETTDPGKARAYAYDLV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 484 LNGYEIGGGSVRISNSDVQSRMFKALGFTEERANEKFGYLLEAFKYGTPPHAGLAFGLDRLVMLLAGTDNIREVIAFPKN 563
Cdd:PRK00476 479 LNGYELGGGSIRIHRPEIQEKVFEILGISEEEAEEKFGFLLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFPKT 558
|
570 580 590
....*....|....*....|....*....|
gi 490589120 564 QNAVCPMTNAPTLAEDEQLEELSIKVDIKD 593
Cdd:PRK00476 559 QSAQDLLTGAPSPVDEKQLRELGIRLRKKE 588
|
|
| aspS_bact |
TIGR00459 |
aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be ... |
8-592 |
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: 802.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 8 KRTHYCGELREKNINEEVVLMGWVQKKRNLGGLVFVDLRDTSGLCQIVFDTDvdKEAFEKAEKLGAEFVIAVKGKVCER- 86
Cdd:TIGR00459 1 MRTHYCGQLRTEHLGQTVTLAGWVNRRRDLGGLIFIDLRDRSGIVQVVCDPD--ADALKLAKGLRNEDVVQVKGKVSARp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 87 -QSKNPNMPTGDIEIFATELRLLNKSETPPIYIkDDDDVSEALRLKYRYLDLRKPSMQRNLKLRHKVMNITRNYLSNNRF 165
Cdd:TIGR00459 79 eGNINRNLDTGEIEILAESITLLNKSKTPPLII-EKTDAEEEVRLKYRYLDLRRPEMQQRLKLRHKVTKAVRNFLDQQGF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 166 CEIETPFLIAPTPEGARDYLVPSRVNPGKFYALPQSPQLYKQLLMVSGMDRYFQIVKCFRDEDLRADRQPEFTQIDCEMS 245
Cdd:TIGR00459 158 LEIETPMLTKSTPEGARDYLVPSRVHKGEFYALPQSPQLFKQLLMVSGVDRYYQIARCFRDEDLRADRQPEFTQIDMEMS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 246 FVEQEDVMSMIEGLLEAIFKEVLDVELALPLPKMTYAEAMSKYGSDKPDTRFGYELTDISDVVCNCGFKVFADATQPGKS 325
Cdd:TIGR00459 238 FMTQEDVMELIEKLVSHVFLEVKGIDLKKPFPVMTYAEAMERYGSDKPDLRFPLELIDVTDLFKDSEFKVFSNLINDGGR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 326 VRGINVKGKADDFTRKQISSLEEHAKTYRAKGLAWMKVGQEGVTSPIAKFFNEEEMNAILTRMNAEVGDLLLFVADKNSI 405
Cdd:TIGR00459 318 VKAIRVPGGWAELSRKSIKELRKFAKEYGAKGLAYLKVNEDGINSPIKKFLDEKKGKILLERTDAQNGDILLFGAGSKKI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 406 VFDALGQVRLEVANRLNLLDKNVYNLLWVTEFPVFEEDEEtGTFSAMHHPFTSPMDEDLDKLEEgDKSSLRAKAYDIVLN 485
Cdd:TIGR00459 398 VLDALGALRLKLGKDLGLVDPDLFSFLWVVDFPMFEKDKE-GRLCAAHHPFTMPKDEDLENLEA-APEEALAEAYDLVLN 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 486 GYEIGGGSVRISNSDVQSRMFKALGFTEERANEKFGYLLEAFKYGTPPHAGLAFGLDRLVMLLAGTDNIREVIAFPKNQN 565
Cdd:TIGR00459 476 GVELGGGSIRIHDPEVQKKVFEILGIDPEEAREKFGFLLEAFKYGTPPHAGFALGLDRLMMLLTGTDNIRDVIAFPKTTA 555
|
570 580
....*....|....*....|....*..
gi 490589120 566 AVCPMTNAPTLAEDEQLEELSIKVDIK 592
Cdd:TIGR00459 556 AACLMTEAPSFIDEKQLEELSIKYVVK 582
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
2-591 |
0e+00 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 702.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 2 ETLKGLKRTHYCGELREKNINEEVVLMGWVQKKRNLGGLVFVDLRDTSGLCQIVFDTDVDKEAFEKAEKLGAEFVIAVKG 81
Cdd:PLN02903 52 SQLTWPSRSHLCGALSVNDVGSRVTLCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDEFPEAHRTANRLRNEYVVAVEG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 82 KVCERQSK--NPNMPTGDIEIFATELRLLNKSETP---PIYIKDD--DDVSEALRLKYRYLDLRKPSMQRNLKLRHKVMN 154
Cdd:PLN02903 132 TVRSRPQEspNKKMKTGSVEVVAESVDILNVVTKSlpfLVTTADEqkDSIKEEVRLRYRVLDLRRPQMNANLRLRHRVVK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 155 ITRNYLSNNR-FCEIETPFLIAPTPEGARDYLVPSRVNPGKFYALPQSPQLYKQLLMVSGMDRYFQIVKCFRDEDLRADR 233
Cdd:PLN02903 212 LIRRYLEDVHgFVEIETPILSRSTPEGARDYLVPSRVQPGTFYALPQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 234 QPEFTQIDCEMSFVEQEDVMSMIEGLLEAIFKEVLDVELALPLPKMTYAEAMSKYGSDKPDTRFGYELTDISDVVCNCGF 313
Cdd:PLN02903 292 QPEFTQLDMELAFTPLEDMLKLNEDLIRQVFKEIKGVQLPNPFPRLTYAEAMSKYGSDKPDLRYGLELVDVSDVFAESSF 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 314 KVFADATQPGKSVRGINVKG--KADDFTRKQISSLEEHAKTYRAKGLAWMKVGQEGVTSPIAKF---FNEEEMNAILTRM 388
Cdd:PLN02903 372 KVFAGALESGGVVKAICVPDgkKISNNTALKKGDIYNEAIKSGAKGLAFLKVLDDGELEGIKALvesLSPEQAEQLLAAC 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 389 NAEVGDLLLFVADKNSIVFDALGQVRLEVANRLNLLDKNVYNLLWVTEFPVFEEDEETGTFSAMHHPFTSPMDEDLdkle 468
Cdd:PLN02903 452 GAGPGDLILFAAGPTSSVNKTLDRLRQFIAKTLDLIDPSRHSILWVTDFPMFEWNEDEQRLEALHHPFTAPNPEDM---- 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 469 eGDKSSLRAKAYDIVLNGYEIGGGSVRISNSDVQSRMFKALGFTEERANEKFGYLLEAFKYGTPPHAGLAFGLDRLVMLL 548
Cdd:PLN02903 528 -GDLSSARALAYDMVYNGVEIGGGSLRIYRRDVQQKVLEAIGLSPEEAESKFGYLLEALDMGAPPHGGIAYGLDRLVMLL 606
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 490589120 549 AGTDNIREVIAFPKNQNAVCPMTNAPTLAEDEQLEELSIKVDI 591
Cdd:PLN02903 607 AGAKSIRDVIAFPKTTTAQCALTRAPSEVDDKQLQDLSIASTA 649
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
12-587 |
0e+00 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 634.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 12 YCGELREKNINEEVVLMGWVQKKRNLGGLVFVDLRDTSGLCQIVFDTD-VDKEAFEKAEKLGAEFVIAVKGKVCER--QS 88
Cdd:PRK12820 8 FCGHLSLDDTGREVCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFSPEaAPADVYELAASLRAEFCVALQGEVQKRleET 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 89 KNPNMPTGDIEIFATELRLLNKSETPPIYIKDD-----------DDVSEALRLKYRYLDLRKPSMQRNLKLRHKVMNITR 157
Cdd:PRK12820 88 ENPHIETGDIEVFVRELSILAASEALPFAISDKamtagagsagaDAVNEDLRLQYRYLDIRRPAMQDHLAKRHRIIKCAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 158 NYLSNNRFCEIETPFLIAPTPEGARDYLVPSRVNPGKFYALPQSPQLYKQLLMVSGMDRYFQIVKCFRDEDLRADRQPEF 237
Cdd:PRK12820 168 DFLDSRGFLEIETPILTKSTPEGARDYLVPSRIHPKEFYALPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 238 TQIDCEMSFVEQEDVMSMIEGLLEAIFkEVLDVELALPLPKMTYAEAMSKYGSDKPDTRFGYELTDISDVVCNCGFKVFA 317
Cdd:PRK12820 248 TQLDIEASFIDEEFIFELIEELTARMF-AIGGIALPRPFPRMPYAEAMDTTGSDRPDLRFDLKFADATDIFENTRYGIFK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 318 DATQPGKSVRGINVKGKADDFTRK--QISSLEEHAKTYRAKGLAWMKVGQEGVTSPIAKFFNEEEMNAILTRMNAEVGDL 395
Cdd:PRK12820 327 QILQRGGRIKGINIKGQSEKLSKNvlQNEYAKEIAPSFGAKGMTWMRAEAGGLDSNIVQFFSADEKEALKRRFHAEDGDV 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 396 LLFVADKN-SIVFDALGQVRLEVANRLNLLDKNVYNLLWVTEFPVFEEDEETGTFSAmHHPFTSPMDEDLDKLEEGDKSS 474
Cdd:PRK12820 407 IIMIADAScAIVLSALGQLRLHLADRLGLIPEGVFHPLWITDFPLFEATDDGGVTSS-HHPFTAPDREDFDPGDIEELLD 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 475 LRAKAYDIVLNGYEIGGGSVRISNSDVQSRMFKALGFTEERANEKFGYLLEAFKYGTPPHAGLAFGLDRLVMLLAGTDNI 554
Cdd:PRK12820 486 LRSRAYDLVVNGEELGGGSIRINDKDIQLRIFAALGLSEEDIEDKFGFFLRAFDFAAPPHGGIALGLDRVVSMILQTPSI 565
|
570 580 590
....*....|....*....|....*....|...
gi 490589120 555 REVIAFPKNQNAVCPMTNAPTLAEDEQLEELSI 587
Cdd:PRK12820 566 REVIAFPKNRSAACPLTGAPSEVAQEQLAELGL 598
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
146-565 |
1.13e-167 |
|
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: 477.84 E-value: 1.13e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 146 LKLRHKVMNITRNYLSNNRFCEIETPFLIAPTPEGARDYLVPSRVNPGKFYALPQSPQLYKQLLMVSGMDRYFQIVKCFR 225
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTPEGARDFLVPSRLHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 226 DEDLRADRQPEFTQIDCEMSFVEQEDVMSMIEGLLEAIFKEVLDVELALPLPKMTYAEAMSKYGsdkpdtrfgyeltdis 305
Cdd:cd00777 81 DEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLGVELTTPFPRMTYAEAMERYG---------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 306 dvvcncgfkvfadatqpgksvrginvkgkaddftrkqissleehaktyrakglawmkvgqegvtspiakffneeemnail 385
Cdd:cd00777 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 386 trmnaevgdlllfvadknsivfdalgqvrlevanrlnlldknvYNLLWVTEFPVFEEDEETGTFSAMHHPFTSPMDEDLD 465
Cdd:cd00777 145 -------------------------------------------FKFLWIVDFPLFEWDEEEGRLVSAHHPFTAPKEEDLD 181
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 466 KLEEgDKSSLRAKAYDIVLNGYEIGGGSVRISNSDVQSRMFKALGFTEERANEKFGYLLEAFKYGTPPHAGLAFGLDRLV 545
Cdd:cd00777 182 LLEK-DPEDARAQAYDLVLNGVELGGGSIRIHDPDIQEKVFEILGLSEEEAEEKFGFLLEAFKYGAPPHGGIALGLDRLV 260
|
410 420
....*....|....*....|
gi 490589120 546 MLLAGTDNIREVIAFPKNQN 565
Cdd:cd00777 261 MLLTGSESIRDVIAFPKTQN 280
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
125-564 |
2.72e-144 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 420.05 E-value: 2.72e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 125 SEALRLKYRYLDLRKPSMQRNLKLRHKVMNITRNYLSNNRFCEIETPFLI-APTPEGARDYLVPSRVNpGKFYALPQSPQ 203
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTkSATPEGARDFLVPSRAL-GKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 204 LYKQLLMVSGMDRYFQIVKCFRDEDLRADRQPEFTQIDCEMSFVEQEDVMSMIEGLLEAIFKEVL----------DVELA 273
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEgiakeleggtLLDLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 274 LPLPKMTYAEAMSK----------YGSDKPDTRFGYELTdisdvvcncgfkvfadatqpgksvrginvkgkaddftrkqi 343
Cdd:pfam00152 160 KPFPRITYAEAIEKlngkdveelgYGSDKPDLRFLLELV----------------------------------------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 344 ssleehaktyrakglawmkvgqegvtspiakffneeemnailtrmnaevgdlllfvadknsivfdalgqvrlevanrlnl 423
Cdd:pfam00152 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 424 LDKNVYNLLWVTEFPvfeedeetgtfsAMHHPFTSPMDEDLDKLeegdksslrAKAYDIVLNGYEIGGGSVRISNSDVQS 503
Cdd:pfam00152 199 IDKNKFNPLWVTDFP------------AEHHPFTMPKDEDDPAL---------AEAFDLVLNGVEIGGGSIRIHDPELQE 257
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490589120 504 RMFKALGFTEERANEKFGYLLEAFKYGTPPHAGLAFGLDRLVMLLAGTDNIREVIAFPKNQ 564
Cdd:pfam00152 258 ERFEEQGLDPEEAEEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAFPKTR 318
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
146-563 |
8.64e-87 |
|
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of class II aminoacyl-tRNA synthetases of the subgroup containing aspartyl, lysyl, and asparaginyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. Nearly all class II tRNA synthetases are dimers and enzymes in this subgroup are homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.
Pssm-ID: 238358 [Multi-domain] Cd Length: 269 Bit Score: 270.50 E-value: 8.64e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 146 LKLRHKVMNITRNYLSNNRFCEIETPFLIAPTP-EGARDYLVPSRVnPGKFYALPQSPQLYKQLLMVSGMDRYFQIVKCF 224
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGgAGARPFLVKYNA-LGLDYYLRISPQLFKKRLMVGGLDRVFEINRNF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 225 RDEDLRADRQPEFTQIDCEMSFVEQEDVMSMIEGLLEAIFKEVL----------DVELALPLPKMTYAEAMSKYGsdkpd 294
Cdd:cd00669 80 RNEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLgvtavtygfeLEDFGLPFPRLTYREALERYG----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 295 trfgyeltdisdvvcncgfkvfadatqpgksvrginvkgkaddftrkqissleehaktyrakglawmkvgqegvtspiak 374
Cdd:cd00669 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 375 ffneeemnailtrmnaevgdlllfvadknsivfdalgqvrlevanrlnlldknvyNLLWVTEFPVFeedeetgtfsaMHH 454
Cdd:cd00669 155 -------------------------------------------------------QPLFLTDYPAE-----------MHS 168
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 455 PFTSPMDEDldkleegdksSLRAKAYDIVLNGYEIGGGSVRISNSDVQSRMFKALGFTEERANEKFGYLLEAFKYGTPPH 534
Cdd:cd00669 169 PLASPHDVN----------PEIADAFDLFINGVEVGNGSSRLHDPDIQAEVFQEQGINKEAGMEYFEFYLKALEYGLPPH 238
|
410 420
....*....|....*....|....*....
gi 490589120 535 AGLAFGLDRLVMLLAGTDNIREVIAFPKN 563
Cdd:cd00669 239 GGLGIGIDRLIMLMTNSPTIREVIAFPKM 267
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
7-561 |
1.10e-86 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 276.30 E-value: 1.10e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 7 LKRTHYCGELREKNINEEVVLMGWVQKKRNLGGLVFVDLRDTSGLCQIVFDTDVDKEAFEKAEKLGAEFVIAVKGKVcer 86
Cdd:PRK05159 1 MMKRHLTSELTPELDGEEVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKVDEELFETIKKLKRESVVSVTGTV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 87 qSKNPNMPTGdIEIFATELRLLNKSETPP---IYIKDDDDVSeaLRLKYRYLDLRKPSMQRNLKLRHKVMNITRNYLSNN 163
Cdd:PRK05159 78 -KANPKAPGG-VEVIPEEIEVLNKAEEPLpldISGKVLAELD--TRLDNRFLDLRRPRVRAIFKIRSEVLRAFREFLYEN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 164 RFCEIETPFLIAPTPEG-----ARDYLvpsrvnpGKFYALPQSPQLYKQLLMVSGMDRYFQIVKCFRDEDLRADRQ-PEF 237
Cdd:PRK05159 154 GFTEIFTPKIVASGTEGgaelfPIDYF-------EKEAYLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSRHlNEY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 238 TQIDCEMSFVE-QEDVMSMIEGLLEAIFKEV----------LDVELALP---LPKMTYAEAMSKYGSDkpdtrfGYELTD 303
Cdd:PRK05159 227 TSIDVEMGFIDdHEDVMDLLENLLRYMYEDVaencekelelLGIELPVPetpIPRITYDEAIEILKSK------GNEISW 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 304 ISDvvcncgfkvfadatqpgksvrginvkgkaddftrkqISSLEEHAktyrakglawmkvgqegvtspIAKFFNEEEmna 383
Cdd:PRK05159 301 GDD------------------------------------LDTEGERL---------------------LGEYVKEEY--- 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 384 iltrmnaevGDLLLFvadknsivfdalgqvrlevanrlnlldknvynllwVTEFPvfeedeetgtfsAMHHPF-TSPMDE 462
Cdd:PRK05159 321 ---------GSDFYF-----------------------------------ITDYP------------SEKRPFyTMPDED 344
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 463 DldkleegdksSLRAKAYDIVLNGYEIGGGSVRISNSDVQSRMFKALGFteeraN-EKFGYLLEAFKYGTPPHAGLAFGL 541
Cdd:PRK05159 345 D----------PEISKSFDLLFRGLEITSGGQRIHRYDMLVESIKEKGL-----NpESFEFYLEAFKYGMPPHGGFGLGL 409
|
570 580
....*....|....*....|
gi 490589120 542 DRLVMLLAGTDNIREVIAFP 561
Cdd:PRK05159 410 ERLTMKLLGLENIREAVLFP 429
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
9-561 |
5.46e-74 |
|
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: 242.65 E-value: 5.46e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 9 RTHYCGELREKNINEEVVLMGWVQKKRNLGGLVFVDLRDTSGLCQIVFDTDvDKEAFEKAEKLGAEFVIAVKGKVcerqS 88
Cdd:COG0017 1 KRTYIKDLLPEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKD-KLENFEEAKKLTTESSVEVTGTV----V 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 89 KNPNMPTGdIEIFATELRLLNKS-ETPPIYIKdddDVSEALRLKYRYLDLRKPSMQRNLKLRHKVMNITRNYLSNNRFCE 167
Cdd:COG0017 76 ESPRAPQG-VELQAEEIEVLGEAdEPYPLQPK---RHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 168 IETPFLIAPTPEGAR-----DYLvpsrvnpGKFYALPQSPQLYKQlLMVSGMDRYFQIVKCFRDEDLRADRQ-PEFTQID 241
Cdd:COG0017 152 VHTPIITASATEGGGelfpvDYF-------GKEAYLTQSGQLYKE-ALAMALEKVYTFGPTFRAEKSNTRRHlAEFWMIE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 242 CEMSFVEQEDVMSMIEGLLEAIFKEVLD-----------------VELALPLPKMTYAEAMSKYGSDKPDTRFGyeltdi 304
Cdd:COG0017 224 PEMAFADLEDVMDLAEEMLKYIIKYVLEncpeeleflgrdverleKVPESPFPRITYTEAIEILKKSGEKVEWG------ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 305 sdvvcncgfkvfadatqpgksvrginvkgkaDDFtrkqiSSLEEHAktyrakglawmkvgqegvtspiakffneeemnai 384
Cdd:COG0017 298 -------------------------------DDL-----GTEHERY---------------------------------- 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 385 LTrmnAEVGDLLLFvadknsivfdalgqvrlevanrlnlldknvynllwVTEFPvfeedEETGTFSAMHHPftspmdedl 464
Cdd:COG0017 308 LG---EEFFKKPVF-----------------------------------VTDYP-----KEIKAFYMKPNP--------- 335
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 465 dklEEGDKSslraKAYDIVLNGY-EIGGGSVRISNSDVQSRMFKALGFTEeranEKFGYLLEAFKYGTPPHAGLAFGLDR 543
Cdd:COG0017 336 ---DDPKTV----AAFDLLAPGIgEIIGGSQREHRYDVLVERIKEKGLDP----EDYEWYLDLRRYGSVPHAGFGLGLER 404
|
570
....*....|....*...
gi 490589120 544 LVMLLAGTDNIREVIAFP 561
Cdd:COG0017 405 LVMWLTGLENIREVIPFP 422
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
9-142 |
1.43e-72 |
|
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: 228.56 E-value: 1.43e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 9 RTHYCGELREKNINEEVVLMGWVQKKRNLGGLVFVDLRDTSGLCQIVFDTDvDKEAFEKAEKLGAEFVIAVKGKVCERQ- 87
Cdd:cd04317 1 RTHYCGELRESHVGQEVTLCGWVQRRRDHGGLIFIDLRDRYGIVQVVFDPE-EAPEFELAEKLRNESVIQVTGKVRARPe 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 490589120 88 -SKNPNMPTGDIEIFATELRLLNKSETPPIYIKDDDDVSEALRLKYRYLDLRKPSM 142
Cdd:cd04317 80 gTVNPKLPTGEIEVVASELEVLNKAKTLPFEIDDDVNVSEELRLKYRYLDLRRPKM 135
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
11-569 |
5.66e-67 |
|
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative asparaginyl-tRNA synthetases (asnS), archaeal/eukaryotic type aspartyl-tRNA synthetases (aspS_arch), and bacterial type aspartyl-tRNA synthetases (aspS_bact), there is a striking similarity between asnS and aspS_arch in gap pattern and in sequence, and a striking divergence of aspS_bact. Consequently, a separate model was built for each of the three groups. This model, aspS_arch, represents aspartyl-tRNA synthetases from the eukaryotic cytosol and from the Archaea. In some species, this enzyme aminoacylates tRNA for both Asp and Asn; Asp-tRNA(asn) is subsequently transamidated to Asn-tRNA(asn). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273087 [Multi-domain] Cd Length: 428 Bit Score: 224.32 E-value: 5.66e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 11 HYCGELREKNINEEVVLMGWVQKKRNLGGLVFVDLRDTSGLCQIVFDTD-VDKEAFEKAEKLGAEFVIAVKGKVcERQSK 89
Cdd:TIGR00458 1 VYSADIKPEMDGQEVTFMGWVHEIRDLGGLIFVLLRDREGLIQITAPAKkVSKNLFKWAKKLNLESVVAVRGIV-KIKEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 90 NPnmptGDIEIFATELRLLNKSETP-PIYIKDDDDVSEALRLKYRYLDLRKPSMQRNLKLRHKVMNITRNYLSNNRFCEI 168
Cdd:TIGR00458 80 AP----GGFEIIPTKIEVINEAKEPlPLDPTEKVPAELDTRLDYRFLDLRRPTVQAIFRIRSGVLESVREFLAEEGFIEV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 169 ETPFLIAPTPEGARDyLVPSRVNPGKFYaLPQSPQLYKQLLMVSGMDRYFQIVKCFRDEDLRADRQ-PEFTQIDCEMSFV 247
Cdd:TIGR00458 156 HTPKLVASATEGGTE-LFPITYFEREAF-LGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNTHRHlNEATSIDIEMAFE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 248 EQEDVMSMIEGLLEAIFKEV----------LDVELALP---LPKMTYAEAmskygsdkpdtrfgyeltdisdvvcncgfk 314
Cdd:TIGR00458 234 DHHDVMDILEELVVRVFEDVpercahqletLEFKLEKPegkFVRLTYDEA------------------------------ 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 315 vfadatqpgksVRGINVKGkaddftrKQISSLEEhaktyrakglawmkvgqegvTSPIAKFFNEEEMnailtrmnaevgD 394
Cdd:TIGR00458 284 -----------IEMANAKG-------VEIGWGED--------------------LSTEAEKALGEEM------------D 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 395 LLLFVADknsivfdalgqvrlevanrlnlldknvynllWVTEFpvfeedeetgtfsamhHPFTSPMDEDLDKleegdkss 474
Cdd:TIGR00458 314 GLYFITD-------------------------------WPTEI----------------RPFYTMPDEDNPE-------- 338
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 475 lRAKAYDIVLNGYEIGGGSVRISNSDVQSRMFKALGFTEeranEKFGYLLEAFKYGTPPHAGLAFGLDRLVMLLAGTDNI 554
Cdd:TIGR00458 339 -ISKSFDLMYRDLEISSGAQRIHLHDLLVERIKAKGLNP----EGFKDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNI 413
|
570
....*....|....*
gi 490589120 555 REVIAFPKNQNAVCP 569
Cdd:TIGR00458 414 REAVLFPRDRKRLTP 428
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
14-569 |
1.93e-43 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 162.95 E-value: 1.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 14 GELREKNINEEVVLMGWVQKKRNLGGLVFVDLRDTSGLCQIVF---DTDVDKEAFEKAEKLGAEFVIAVKGKVcerqsKN 90
Cdd:PLN02850 73 SDLGEELAGSEVLIRGRVHTIRGKGKSAFLVLRQSGFTVQCVVfvsEVTVSKGMVKYAKQLSRESVVDVEGVV-----SV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 91 PNMP----TGDIEIFATELRLLNKSETP-PIYIKD----DDDVSEA-------------LRLKYRYLDLRKPSMQRNLKL 148
Cdd:PLN02850 148 PKKPvkgtTQQVEIQVRKIYCVSKALATlPFNVEDaarsESEIEKAlqtgeqlvrvgqdTRLNNRVLDLRTPANQAIFRI 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 149 RHKVMNITRNYLSNNRFCEIETPFLIAPTPEGAR-----DYLvpsrvnpGKFYALPQSPQLYKQLLMVSGMDRYFQIVKC 223
Cdd:PLN02850 228 QSQVCNLFREFLLSKGFVEIHTPKLIAGASEGGSavfrlDYK-------GQPACLAQSPQLHKQMAICGDFRRVFEIGPV 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 224 FRDEDLRADRQ-PEFTQIDCEMSFVEQED-VMSMIEGLLEAIFkevldvelalplpkmtyaeamskygsDKPDTRFGYEL 301
Cdd:PLN02850 301 FRAEDSFTHRHlCEFTGLDLEMEIKEHYSeVLDVVDELFVAIF--------------------------DGLNERCKKEL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 302 TDIsdvvcncgfkvfadatqpgksvrginvkgkaddftRKQ--ISSLEEHAKTYRakgLAWmkvgQEGVtspiakffnee 379
Cdd:PLN02850 355 EAI-----------------------------------REQypFEPLKYLPKTLR---LTF----AEGI----------- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 380 emnailtRMNAEVGDLLlfvadknsivfDALGQVRLEVANRLNLLDKNVYNllwvTEFPVFEEdeetgtFSAMHHPF-TS 458
Cdd:PLN02850 382 -------QMLKEAGVEV-----------DPLGDLNTESERKLGQLVKEKYG----TDFYILHR------YPLAVRPFyTM 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 459 PMDEDldkleegdksSLRAKAYDIVLNGYEIGGGSVRISNSDvqsrmfkalgFTEERANEK------FGYLLEAFKYGTP 532
Cdd:PLN02850 434 PCPDD----------PKYSNSFDVFIRGEEIISGAQRVHDPE----------LLEKRAEECgidvktISTYIDSFRYGAP 493
|
570 580 590
....*....|....*....|....*....|....*..
gi 490589120 533 PHAGLAFGLDRLVMLLAGTDNIREVIAFPKNQNAVCP 569
Cdd:PLN02850 494 PHGGFGVGLERVVMLFCGLNNIRKTSLFPRDPQRLAP 530
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
123-562 |
1.06e-40 |
|
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: 150.41 E-value: 1.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 123 DVSEALRLKYRYLDLRKPSMQRNLKLRHKVMNITRNYLSNNRFCEIETPFLIAPTPEGardylvPSRVNPGKFYA----L 198
Cdd:cd00776 1 DANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEG------GAELFKVSYFGkpayL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 199 PQSPQLYKQlLMVSGMDRYFQIVKCFRDEDLRADRQ-PEFTQIDCEMSFVEQ-EDVMSMIEGLLEAIFKEVLD------- 269
Cdd:cd00776 75 AQSPQLYKE-MLIAALERVYEIGPVFRAEKSNTRRHlSEFWMLEAEMAFIEDyNEVMDLIEELIKYIFKRVLErcakele 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 270 ---------VELALPLPKMTYAEAMskygsdkpdtrfgyeltdisdvvcncgfKVFADATQPGKSVRGinvkgkaDDFTr 340
Cdd:cd00776 154 lvnqlnrelLKPLEPFPRITYDEAI----------------------------ELLREKGVEEEVKWG-------EDLS- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 341 kqisslEEHAKtyrakglawmkvgqegvtspiakffneeemnailtRMNAEVgdlllfvadKNSIVFdalgqvrlevanr 420
Cdd:cd00776 198 ------TEHER-----------------------------------LLGEIV---------KGDPVF------------- 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 421 lnlldknvynllwVTEFPVfeedeETgtfsamhHPFTSPMDEDLDKLeegdksslrAKAYDIVLNGY-EIGGGSVRISNS 499
Cdd:cd00776 215 -------------VTDYPK-----EI-------KPFYMKPDDDNPET---------VESFDLLMPGVgEIVGGSQRIHDY 260
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490589120 500 DVQSRMFKALGFTEeranEKFGYLLEAFKYGTPPHAGLAFGLDRLVMLLAGTDNIREVIAFPK 562
Cdd:cd00776 261 DELEERIKEHGLDP----ESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFPR 319
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
8-561 |
4.51e-34 |
|
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: 135.55 E-value: 4.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 8 KRTHYCGELREK--------NINEEVVLMGWVQKKRNLGGLVFVDLRDTSGLCQIVFDTD-VDKEAFEKAEKLGAEFVIA 78
Cdd:COG1190 34 PRTHTAAEIREKydeleaeeETGDEVSVAGRIMAKRDMGKASFADLQDGSGRIQLYLRRDeLGEEAYELFKLLDLGDIVG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 79 VKGKVceRQSKnpnmpTGDIEIFATELRLLNKSETPP--IY--IKDDDdvseaLRLKYRYLDL--RKPSMQRnLKLRHKV 152
Cdd:COG1190 114 VEGTV--FRTK-----TGELSVKVEELTLLSKSLRPLpeKFhgLTDPE-----TRYRQRYVDLivNPEVRET-FRKRSKI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 153 MNITRNYLSNNRFCEIETPFLiAPTPEGA-------------RD-YLvpsRVnpgkfyalpqSPQLY-KQLLmVSGMDRY 217
Cdd:COG1190 181 IRAIRRFLDERGFLEVETPML-QPIAGGAaarpfithhnaldMDlYL---RI----------APELYlKRLI-VGGFERV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 218 FQIVKCFRDEDLRADRQPEFTQIDCEMSFVEQEDVMSMIEGLLEAIFKEVL----------DVELALPLPKMTYAEAMSK 287
Cdd:COG1190 246 FEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLgttkvtyqgqEIDLSPPWRRITMVEAIKE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 288 YGsdkpdtrfGYELTDISDvvcncgfkvfadatqpgksvrginvkgkaDDFTRKQISSLEEHAKTYRAKGlawmKVgqeg 367
Cdd:COG1190 326 AT--------GIDVTPLTD-----------------------------DEELRALAKELGIEVDPGWGRG----KL---- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 368 vtspIAKFFneEEmnailtrmnaevgdlllFVADKnsivfdalgqvrlevanrlnlldknvynlLW----VTEFPVfeed 443
Cdd:COG1190 361 ----IDELF--EE-----------------LVEPK-----------------------------LIqptfVTDYPV---- 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 444 eETgtfSamhhPFTSPMDEDLDKLEegdksslrakAYDIVLNGYEIGggsvrisNS-------DVQSRMFKALGftEERA 516
Cdd:COG1190 385 -EV---S----PLAKRHRDDPGLTE----------RFELFIAGREIA-------NAfselndpIDQRERFEEQL--ELKA 437
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 490589120 517 N---------EKFgylLEAFKYGTPPHAGLAFGLDRLVMLLAGTDNIREVIAFP 561
Cdd:COG1190 438 AgddeampmdEDF---LRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 488
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
8-561 |
4.90e-34 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 135.22 E-value: 4.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 8 KRTHYCGELREK----------NINEEVVLMGWVQKKRNLGGLVFVDLRDTSGLCQIVFDTD-VDKEAFEKAEKLGAEFV 76
Cdd:PRK00484 30 ERTHTAAELRAKyddkekeeleELEIEVSVAGRVMLKRVMGKASFATLQDGSGRIQLYVSKDdVGEEALEAFKKLDLGDI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 77 IAVKGKVceRQSKnpnmpTGDIEIFATELRLLNKSETP-PIyiKDDDDVSEALRLKYRYLDL-RKPSMQRNLKLRHKVMN 154
Cdd:PRK00484 110 IGVEGTL--FKTK-----TGELSVKATELTLLTKSLRPlPD--KFHGLTDVETRYRQRYVDLiVNPESRETFRKRSKIIS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 155 ITRNYLSNNRFCEIETPFLiAPTPEG--AR---------D---YLvpsRVnpgkfyalpqSPQLY-KQLLmVSGMDRYFQ 219
Cdd:PRK00484 181 AIRRFLDNRGFLEVETPML-QPIAGGaaARpfithhnalDidlYL---RI----------APELYlKRLI-VGGFERVYE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 220 IVKCFRDEDLRADRQPEFTQIDCEMSFVEQEDVMSMIEGLLEAIFKEVL----------DVELALPLPKMTYAEAMSKYG 289
Cdd:PRK00484 246 IGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLgttkvtyqgtEIDFGPPFKRLTMVDAIKEYT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 290 sdkpdtrfgyeltdisdvvcncgfkvfadatqpgksvrGINVKGKADDFTRKQISSLEEHAKTYRAKGlawmKVgqegvt 369
Cdd:PRK00484 326 --------------------------------------GVDFDDMTDEEARALAKELGIEVEKSWGLG----KL------ 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 370 spIAKFFNEeemnailtrmnaevgdlllFVADKnsivfdalgqvrlevanrlnlldknvynlLW----VTEFPVfeedeE 445
Cdd:PRK00484 358 --INELFEE-------------------FVEPK-----------------------------LIqptfITDYPV-----E 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 446 TgtfSamhhPFTSPMDEDLDKLEegdksslrakAYDIVLNGYEIGGGSVRISNSDVQSRMF------KALGftEERAN-- 517
Cdd:PRK00484 383 I---S----PLAKRHREDPGLTE----------RFELFIGGREIANAFSELNDPIDQRERFeaqveaKEAG--DDEAMfm 443
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 490589120 518 -EKFgylLEAFKYGTPPHAGLAFGLDRLVMLLAGTDNIREVIAFP 561
Cdd:PRK00484 444 dEDF---LRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
24-110 |
1.63e-32 |
|
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: 119.98 E-value: 1.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 24 EVVLMGWVQKKRNLGGLVFVDLRDTSGLCQIVFDTDVDKEAFEKAEKLGAEFVIAVKGKVCERqsKNPNMPTGDIEIFAT 103
Cdd:cd04100 1 EVTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEELGEFFEEAEKLRTESVVGVTGTVVKR--PEGNLATGEIELQAE 78
|
....*..
gi 490589120 104 ELRLLNK 110
Cdd:cd04100 79 ELEVLSK 85
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
16-561 |
2.32e-30 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 124.06 E-value: 2.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 16 LREKNINEEVVLMGWVQKKRNLGGLVFVDLRDTSGLCQIVFDTDVDKEAFEKAEKLGAEFVIAVKGKVcerqSKNPNMPT 95
Cdd:PRK03932 10 LKGKYVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDNGEEYFEEIKKLTTGSSVIVTGTV----VESPRAGQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 96 GdIEIFATELRLL-NKSETPPIYIKDDDDvsEALRlKYRYLDLRKPSMQRNLKLRHKVMNITRNYLSNNRFCEIETPFLI 174
Cdd:PRK03932 86 G-YELQATKIEVIgEDPEDYPIQKKRHSI--EFLR-EIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVDTPIIT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 175 APTPEGA--------------RDYLvpsrvnpGKFYALPQSPQLYKQLLMVSgmdryFQIVKC----FRDEDLRADRQ-P 235
Cdd:PRK03932 162 ASDCEGAgelfrvttldldfsKDFF-------GKEAYLTVSGQLYAEAYAMA-----LGKVYTfgptFRAENSNTRRHlA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 236 EFTQIDCEMSFVEQEDVMSMIEGLLEAIFKEVLDvelalplpkmtyaeamskygsdkpdtrfgyeltdisdvvcNCgfkv 315
Cdd:PRK03932 230 EFWMIEPEMAFADLEDNMDLAEEMLKYVVKYVLE----------------------------------------NC---- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 316 fadatqpgksvrginvkgkADDFtrkqissleehaktyrakglawmkvgqegvtspiaKFFNEEEMNAILTRmnaevgdl 395
Cdd:PRK03932 266 -------------------PDDL-----------------------------------EFLNRRVDKGDIER-------- 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 396 LLFVADKNsivFdalgqVRLEVANRLNLLDKNVYNLlwvtEFPV-----FEEDEEtgTFSAMHHpFTSP----------- 459
Cdd:PRK03932 284 LENFIESP---F-----PRITYTEAIEILQKSGKKF----EFPVewgddLGSEHE--RYLAEEH-FKKPvfvtnypkdik 348
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 460 ---MdedldKLEEGDKsslRAKAYDIVLNGY-EIGGGSVRISNSDV-QSRMfKALGFTEeranEKFGYLLEAFKYGTPPH 534
Cdd:PRK03932 349 afyM-----RLNPDGK---TVAAMDLLAPGIgEIIGGSQREERLDVlEARI-KELGLNK----EDYWWYLDLRRYGSVPH 415
|
570 580
....*....|....*....|....*..
gi 490589120 535 AGLAFGLDRLVMLLAGTDNIREVIAFP 561
Cdd:PRK03932 416 SGFGLGFERLVAYITGLDNIRDVIPFP 442
|
|
| GAD |
pfam02938 |
GAD domain; This domain is found in some members of the GatB and aspartyl tRNA synthetases. |
316-410 |
3.38e-28 |
|
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: 108.12 E-value: 3.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 316 FADATQPGKSVRGINVKGkADDFTRKQISSLEEHAKTYRAKGLAWMKVGQEGVTSPIAKFFNEEEMNAILTRMNAEVGDL 395
Cdd:pfam02938 1 FSEALKSGGSVKALRVPG-AAGLSRKEIDELERFAKEYGAKGLAWIKVEGGGHTGPIAKFLTEEEVEKLLEAVGAEDGDA 79
|
90
....*....|....*
gi 490589120 396 LLFVADKNSIVFDAL 410
Cdd:pfam02938 80 LLFVADKKKTVNKAL 94
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
17-569 |
3.57e-27 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 115.86 E-value: 3.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 17 REKNINEEVVLMGWVQKKRNLGGLVFVDLRDTSGLCQ--IVFDTDVDKEAFEKAEKLGAEFVIAVKGKVCERQSKNPNMP 94
Cdd:PTZ00401 73 KPELVDKTVLIRARVSTTRKKGKMAFMVLRDGSDSVQamAAVEGDVPKEMIDFIGQIPTESIVDVEATVCKVEQPITSTS 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 95 TGDIEIFATELRLLNKS-ETPPIYIKD-----DDD---VSEALRLKYRYLDLRKPSMQRNLKLRHKVMNITRNYLSNNRF 165
Cdd:PTZ00401 153 HSDIELKVKKIHTVTESlRTLPFTLEDasrkeSDEgakVNFDTRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLIDSDF 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 166 CEIETPFLIAPTPEGARDYLVPSRVNpgKFYALPQSPQLYKQLLMVSGMDRYFQIVKCFRDEDLRADRQ-PEFTQIDCEM 244
Cdd:PTZ00401 233 CEIHSPKIINAPSEGGANVFKLEYFN--RFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNTHRHlTEFVGLDVEM 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 245 SFVEQ-EDVMSMIEGLLEAIFKEVldvelalplpkMTYAEAMSKYGSDKPDTRFGYELTdiSDVVCNCGFKVFADATQPg 323
Cdd:PTZ00401 311 RINEHyYEVLDLAESLFNYIFERL-----------ATHTKELKAVCQQYPFEPLVWKLT--PERMKELGVGVISEGVEP- 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 324 ksvrginvkgkaddftrkqissleehAKTYRAKglawmkvgqegvtspiakffnEEEMNAILTRMN-AEVGDLLLFVADK 402
Cdd:PTZ00401 377 --------------------------TDKYQAR---------------------VHNMDSRMLRINyMHCIELLNTVLEE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 403 NSIVFDALGQVRLEVanrLNLLDKNVYNllwvTEFpvFEEDEetgtFSAMHHPF-TSPMDEDldkleegdksSLRAKAYD 481
Cdd:PTZ00401 410 KMAPTDDINTTNEKL---LGKLVKERYG----TDF--FISDR----FPSSARPFyTMECKDD----------ERFTNSYD 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 482 IVLNGYEIGGGSVRISNSDVQSRMFKALGFTEERANEkfgyLLEAFKYGTPPHAGLAFGLDRLVMLLAGTDNIREVIAFP 561
Cdd:PTZ00401 467 MFIRGEEISSGAQRIHDPDLLLARAKMLNVDLTPIKE----YVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFP 542
|
....*...
gi 490589120 562 KNQNAVCP 569
Cdd:PTZ00401 543 RDPQRTTP 550
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
11-126 |
1.16e-26 |
|
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: 104.32 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 11 HYCGELREKNINEEVVLMGWVQKKRNLGGLVFVDLRDTSGLCQIVFDTD-VDKEAFEKAEKLGAEFVIAVKGKVcERQSK 89
Cdd:cd04316 1 HYSAEITPELDGEEVTVAGWVHEIRDLGGIKFVILRDREGIVQVTAPKKkVDKELFKTVRKLSRESVISVTGTV-KAEPK 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 490589120 90 NPNmptgDIEIFATELRLLNKSETPPIyikddDDVSE 126
Cdd:cd04316 80 APN----GVEIIPEEIEVLSEAKTPLP-----LDPTG 107
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
19-561 |
3.09e-26 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 112.46 E-value: 3.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 19 KNINEEVVLMGWVQKKRNLGGLVFVDLRDTSGLCQIVFDTDVDKEAF--EKAEKLGAEFVIAVKGKVCERQsknpnmpTG 96
Cdd:PRK12445 62 ESLNIEVSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEGVynDQFKKWDLGDIIGARGTLFKTQ-------TG 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 97 DIEIFATELRLLNKSETP-PIYIKDDDDvsEALRLKYRYLDLRKPSMQRN-LKLRHKVMNITRNYLSNNRFCEIETPFL- 173
Cdd:PRK12445 135 ELSIHCTELRLLTKALRPlPDKFHGLQD--QEVRYRQRYLDLIANDKSRQtFVVRSKILAAIRQFMVARGFMEVETPMMq 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 174 IAPTPEGARDYLVPSRVNPGKFYaLPQSPQLYKQLLMVSGMDRYFQIVKCFRDEDLRADRQPEFTQIDCEMSFVEQEDVM 253
Cdd:PRK12445 213 VIPGGASARPFITHHNALDLDMY-LRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLI 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 254 SMIEGLLEAIFKEVLD----------VELALPLPKMTYAEAMSKYgsdKPDtrfgyelTDISDVvcncgfkvfadatqpg 323
Cdd:PRK12445 292 ELTESLFRTLAQEVLGttkvtygehvFDFGKPFEKLTMREAIKKY---RPE-------TDMADL---------------- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 324 ksvrginvkgkaDDFTrkqissleehaktyRAKGLAwmkvgqEGVTSPIAKFFNeeemnaiLTRMNAEVGDlllfvadkn 403
Cdd:PRK12445 346 ------------DNFD--------------AAKALA------ESIGITVEKSWG-------LGRIVTEIFD--------- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 404 sivfdalgqvrlEVAnrlnllDKNVYNLLWVTEFPVfeedeetgtfsamhhpFTSPMdedldkLEEGDKSSLRAKAYDIV 483
Cdd:PRK12445 378 ------------EVA------EAHLIQPTFITEYPA----------------EVSPL------ARRNDVNPEITDRFEFF 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 484 LNGYEIGGGSVRISNSDVQSRMFKALGFTEERANEKFGYLLE----AFKYGTPPHAGLAFGLDRLVMLLAGTDNIREVIA 559
Cdd:PRK12445 418 IGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEdyvtALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVIL 497
|
..
gi 490589120 560 FP 561
Cdd:PRK12445 498 FP 499
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
9-561 |
2.66e-24 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 107.00 E-value: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 9 RTHYCGELREK---------NINEEVVLMGWVQKKRNLGGLVFVDLRDTSGLCQIVFD---TDVDKEAFEKAE---KLGA 73
Cdd:PLN02502 86 VTHTAPELQEKygslengeeLEDVSVSVAGRIMAKRAFGKLAFYDLRDDGGKIQLYADkkrLDLDEEEFEKLHslvDRGD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 74 efVIAVKGKVceRQSKnpnmpTGDIEIFATELRLLNKSETP-PIYIKDDDDVSEalRLKYRYLDL-RKPSMQRNLKLRHK 151
Cdd:PLN02502 166 --IVGVTGTP--GKTK-----KGELSIFPTSFEVLTKCLLMlPDKYHGLTDQET--RYRQRYLDLiANPEVRDIFRTRAK 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 152 VMNITRNYLSNNRFCEIETPFL-IAPTPEGARDYLVPSRVNPGKFYaLPQSPQLYKQLLMVSGMDRYFQIVKCFRDEDLR 230
Cdd:PLN02502 235 IISYIRRFLDDRGFLEVETPMLnMIAGGAAARPFVTHHNDLNMDLY-LRIATELHLKRLVVGGFERVYEIGRQFRNEGIS 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 231 ADRQPEFTQIDCEMSFVEQEDVMSMIEGLLEAIFKEVldvelalplpkmtyaeamskYGSDKPDtrfgYELTDIsdvvcn 310
Cdd:PLN02502 314 TRHNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKEL--------------------TGSYKIK----YHGIEI------ 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 311 cgfkvfaDATQPgksvrginvkgkaddFTR-KQISSLEEHAKtyrakglawmkvgqegvtSPIAKFFNEEEMNAILtrmn 389
Cdd:PLN02502 364 -------DFTPP---------------FRRiSMISLVEEATG------------------IDFPADLKSDEANAYL---- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 390 aevgdlllfvadknsIVFDALGQVRLEVANRL-NLLDKnvynllwvtefpVFEEDEETG----TFsAMHHP-FTSPmded 463
Cdd:PLN02502 400 ---------------IAACEKFDVKCPPPQTTgRLLNE------------LFEEFLEETlvqpTF-VLDHPvEMSP---- 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 464 LDKLEegdksslRAKA-----YDIVLNGYEIGGGSVRISNSDVQSRMF------KALGFTEERA-NEKFgylLEAFKYGT 531
Cdd:PLN02502 448 LAKPH-------RSKPglterFELFINGRELANAFSELTDPVDQRERFeeqvkqHNAGDDEAMAlDEDF---CTALEYGL 517
|
570 580 590
....*....|....*....|....*....|
gi 490589120 532 PPHAGLAFGLDRLVMLLAGTDNIREVIAFP 561
Cdd:PLN02502 518 PPTGGWGLGIDRLVMLLTDSASIRDVIAFP 547
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
18-561 |
1.19e-23 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 105.50 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 18 EKNINEEVVLMGWVQKKRNLGGLVFVDLRDTSGLCQIVFDTDvdkEAF--EKAEKLGAEF----VIAVKGKVCErqsknp 91
Cdd:PTZ00385 103 DRAAQATVRVAGRVTSVRDIGKIIFVTIRSNGNELQVVGQVG---EHFtrEDLKKLKVSLrvgdIIGADGVPCR------ 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 92 nMPTGDIEIFATELRLLNksetpPIYIKD--------------DDDVsealRLKYRYLDL-RKPSMQRNLKLRHKVMNIT 156
Cdd:PTZ00385 174 -MQRGELSVAASRMLILS-----PYVCTDqvvcpnlrgftvlqDNDV----KYRYRFTDMmTNPCVIETIKKRHVMLQAL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 157 RNYLSNNRFCEIETPFL-IAPTPEGARDYLVPSRVNPGKFYaLPQSPQLYKQLLMVSGMDRYFQIVKCFRDEDLRADRQP 235
Cdd:PTZ00385 244 RDYFNERNFVEVETPVLhTVASGANAKSFVTHHNANAMDLF-LRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNP 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 236 EFTQIDCEMSFVEQEDVMSMIEGlleaIFKevldvELALPLPKMTYAEAMSKYGSDKPDTrfgyelTDIsdvvcncgfkv 315
Cdd:PTZ00385 323 EFTSCEFYAAYHTYEDLMPMTED----IFR-----QLAMRVNGTTVVQIYPENAHGNPVT------VDL----------- 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 316 fadatqpGKSVRGINVkgkADDFTRKQISSLEEHAKTYRAKGLAWmkvgqegvtspiakffneeeMNAILTRMNAEvgdl 395
Cdd:PTZ00385 377 -------GKPFRRVSV---YDEIQRMSGVEFPPPNELNTPKGIAY--------------------MSVVMLRYNIP---- 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 396 llfvadknsivfdaLGQVRLEVANRLNLLDknvynlLWVTEFPVfeedeeTGTFsAMHHP-FTSPMDEdldklEEGDKSS 474
Cdd:PTZ00385 423 --------------LPPVRTAAKMFEKLID------FFITDRVV------EPTF-VMDHPlFMSPLAK-----EQVSRPG 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 475 LrAKAYDIVLNGYEIGGGSVRISNSDVQSRMFKALGFTEERANEKFGYLLEAF----KYGTPPHAGLAFGLDRLVMLLAG 550
Cdd:PTZ00385 471 L-AERFELFVNGIEYCNAYSELNDPHEQYHRFQQQLVDRQGGDEEAMPLDETFlkslQVGLPPTAGWGMGIDRALMLLTN 549
|
570
....*....|.
gi 490589120 551 TDNIREVIAFP 561
Cdd:PTZ00385 550 SSNIRDGIIFP 560
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
6-561 |
1.57e-23 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 105.82 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 6 GLKRTHYCGELREKNINEEVVLMGWVQKKRNLGGLVFVDLRDTSGLCQIVFDTDV----DKEAFEKAEKLGAefVIAVKG 81
Cdd:PRK02983 635 GVPPTHTVAEALDAPTGEEVSVSGRVLRIRDYGGVLFADLRDWSGELQVLLDASRleqgSLADFRAAVDLGD--LVEVTG 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 82 KVCerQSKNpnmptGDIEIFATELRLLNKSETP-PIYIKDDDDVsEAlRLKYRYLDLR-KPSMQRNLKLRHKVMNITRNY 159
Cdd:PRK02983 713 TMG--TSRN-----GTLSLLVTSWRLAGKCLRPlPDKWKGLTDP-EA-RVRQRYLDLAvNPEARDLLRARSAVVRAVRET 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 160 LSNNRFCEIETPFLiaPTPEG---ARDYLvpSRVNPgkfYALPQ----SPQLYKQLLMVSGMDRYFQIVKCFRDEDLRAD 232
Cdd:PRK02983 784 LVARGFLEVETPIL--QQVHGganARPFV--THINA---YDMDLylriAPELYLKRLCVGGVERVFELGRNFRNEGVDAT 856
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 233 RQPEFTQIDCEMSFveqEDVMSMIEGLLEAIfkevldvelalplpkmtYAEAMSKYGSD---KPDTRFGYELTDISDVvc 309
Cdd:PRK02983 857 HNPEFTLLEAYQAH---ADYDTMRDLTRELI-----------------QNAAQAAHGAPvvmRPDGDGVLEPVDISGP-- 914
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 310 ncgfkvfadatQPGKSVrginvkgkaddftrkqissleeHAKTYRAkglawmkVGQE-GVTSPIAKffneeemnailtrm 388
Cdd:PRK02983 915 -----------WPVVTV----------------------HDAVSEA-------LGEEiDPDTPLAE-------------- 940
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 389 naevgdlLLFVADKNSIVFDA---LGQVRLEVANRLnlldknvynllwV---TEFPVFEEDEETGtfsamhhpfTSPmde 462
Cdd:PRK02983 941 -------LRKLCDAAGIPYRTdwdAGAVVLELYEHL------------VedrTTFPTFYTDFPTS---------VSP--- 989
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 463 dldkLEEGDKSSLR-AKAYDIVLNGYEIGGGSVRISNSDVQSRMF-----KALGFTEE--RANEKFgylLEAFKYGTPPH 534
Cdd:PRK02983 990 ----LTRPHRSDPGlAERWDLVAWGVELGTAYSELTDPVEQRRRLteqslLAAGGDPEamELDEDF---LQALEYAMPPT 1062
|
570 580
....*....|....*....|....*..
gi 490589120 535 AGLAFGLDRLVMLLAGTdNIREVIAFP 561
Cdd:PRK02983 1063 GGLGMGVDRLVMLLTGR-SIRETLPFP 1088
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
146-561 |
1.48e-18 |
|
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: 86.87 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 146 LKLRHKVMNITRNYLSNNRFCEIETPFLiAPTPEG--ARDYLVPSRVNPGKFYaLPQSPQLYKQLLMVSGMDRYFQIVKC 223
Cdd:cd00775 8 FIVRSKIISYIRKFLDDRGFLEVETPML-QPIAGGaaARPFITHHNALDMDLY-LRIAPELYLKRLIVGGFERVYEIGRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 224 FRDEDLRADRQPEFTQIDCEMSFVEQEDVMSMIEGLLEAIFKEVL--------DVELAL--PLPKMTYAEAMSKYgsdkp 293
Cdd:cd00775 86 FRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINgktkieygGKELDFtpPFKRVTMVDALKEK----- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 294 dtrfgyeltdisdvvcncgfkvfadatqpgksvRGInvkgkadDFTRKQISSLEEHAKTYrakglawmkvgqegvtspia 373
Cdd:cd00775 161 ---------------------------------TGI-------DFPELDLEQPEELAKLL-------------------- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 374 kffneEEMNAILTRMNAEVGDLLLFVADKnsivfdalgqvrlevanrlnLLDKNVYNLLWVTEFPVfeedeETGTFSAMH 453
Cdd:cd00775 181 -----AKLIKEKIEKPRTLGKLLDKLFEE--------------------FVEPTLIQPTFIIDHPV-----EISPLAKRH 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 454 HpftspmdedldkleegDKSSLrAKAYDIVLNGYEIGGGSVRISNSDVQSRMF------KALGFTEERA-NEKFgylLEA 526
Cdd:cd00775 231 R----------------SNPGL-TERFELFICGKEIANAYTELNDPFDQRERFeeqakqKEAGDDEAMMmDEDF---VTA 290
|
410 420 430
....*....|....*....|....*....|....*
gi 490589120 527 FKYGTPPHAGLAFGLDRLVMLLAGTDNIREVIAFP 561
Cdd:cd00775 291 LEYGMPPTGGLGIGIDRLVMLLTDSNSIRDVILFP 325
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
148-276 |
9.82e-17 |
|
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: 79.08 E-value: 9.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 148 LRHKVMNITRNYLSNNRFCEIETPFLIAPTPEGARD----YLVPSRVNPGKFYALPQSPQLYKQLLMVS----GMDRYFQ 219
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGhepkDLLPVGAENEEDLYLRPTLEPGLVRLFVShirkLPLRLAE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 490589120 220 IVKCFRDEDLRAD--RQPEFTQIDCEMsFVEQEDVMSMIEGLLEAIFKEVLDVELALPL 276
Cdd:cd00768 81 IGPAFRNEGGRRGlrRVREFTQLEGEV-FGEDGEEASEFEELIELTEELLRALGIKLDI 138
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
137-303 |
3.64e-16 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 80.06 E-value: 3.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 137 LRKPSMQRNLKLRHKVMNITRNYLSNNRFCEIETPFLIAPTPEGARD-----YLVPSRVNPGKFYALPQSPQLYKQLlMV 211
Cdd:PRK06462 21 ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIISPSTDPLMGLgsdlpVKQISIDFYGVEYYLADSMILHKQL-AL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 212 SGMDRYFQIVKCFRDEDLRADRQP---EFTQIDCEMSFVEQEDVMSMIEGLLEAIFKEVLDV-------------ELALP 275
Cdd:PRK06462 100 RMLGKIFYLSPNFRLEPVDKDTGRhlyEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEhedeleffgrdlpHLKRP 179
|
170 180
....*....|....*....|....*...
gi 490589120 276 LPKMTYAEAMSKYGSDKPDTRFGYELTD 303
Cdd:PRK06462 180 FKRITHKEAVEILNEEGCRGIDLEELGS 207
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
24-135 |
4.54e-15 |
|
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: 71.02 E-value: 4.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 24 EVVLMGWVQKKRNLGGLVFVDLRDTSGLCQIVFDTDVDKEAFEKAEKLGAEFVIAVKGKVCErqskNPNMPTGdIEIFAT 103
Cdd:cd04319 1 KVTLAGWVYRKREVGKKAFIVLRDSTGIVQAVFSKDLNEEAYREAKKVGIESSVIVEGAVKA----DPRAPGG-AEVHGE 75
|
90 100 110
....*....|....*....|....*....|..
gi 490589120 104 ELRLLNKSETPPIyikdDDDVSEALRLKYRYL 135
Cdd:cd04319 76 KLEIIQNVEFFPI----TEDASDEFLLDVRHL 103
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
25-108 |
1.91e-14 |
|
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: 68.42 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 25 VVLMGWV-QKKRNLGGLVFVDLRDTSGLCQIVFDtdvDKEAFEKAEKLGAEFVIAVKGKVCERqsknpnmPTGDIEIFAT 103
Cdd:pfam01336 1 VTVAGRVtSIRRSGGKLLFLTLRDGTGSIQVVVF---KEEAEKLAKKLKEGDVVRVTGKVKKR-------KGGELELVVE 70
|
....*
gi 490589120 104 ELRLL 108
Cdd:pfam01336 71 EIELL 75
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
96-297 |
4.75e-11 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 65.42 E-value: 4.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 96 GDIEIFATELRLLNKS--ETPPIY-IKDDDdvseaLRLKYRYLDLR-KPSMQRNLKLRHKVMNITRNYLSNNRFCEIETP 171
Cdd:PTZ00417 204 GELSIFPKETIILSPClhMLPMKYgLKDTE-----IRYRQRYLDLMiNESTRSTFITRTKIINYLRNFLNDRGFIEVETP 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 172 FL-IAPTPEGARDYLVPSRVNPGKFYaLPQSPQLYKQLLMVSGMDRYFQIVKCFRDEDLRADRQPEFTQIDCEMSFVEQE 250
Cdd:PTZ00417 279 TMnLVAGGANARPFITHHNDLDLDLY-LRIATELPLKMLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFY 357
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490589120 251 DVMSMIEGLLEAIF-----------------KEVLDVELALPLPKMTYAEAMSKYGSDKPDTRF 297
Cdd:PTZ00417 358 DLIKWSEDFFSQLVmhlfgtykilynkdgpeKDPIEIDFTPPYPKVSIVEELEKLTNTKLEQPF 421
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
24-137 |
1.48e-10 |
|
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: 58.26 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 24 EVVLMGWVQKKRNLGGLVFVDLRDTSGLCQIVFD-TDVDKEAFEKAEK---LGAefVIAVKGKVceRQSKnpnmpTGDIE 99
Cdd:cd04322 1 EVSVAGRIMSKRGSGKLSFADLQDESGKIQVYVNkDDLGEEEFEDFKKlldLGD--IIGVTGTP--FKTK-----TGELS 71
|
90 100 110
....*....|....*....|....*....|....*....
gi 490589120 100 IFATELRLLNKSETP-PIYIKDDDDVseALRLKYRYLDL 137
Cdd:cd04322 72 IFVKEFTLLSKSLRPlPEKFHGLTDV--ETRYRQRYLDL 108
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
466-562 |
6.59e-10 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 61.96 E-value: 6.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 466 KLEEGDKSslrAKAYDIVLNGY-EIGGGSVRISNSDVQSRMFKalgftEERAN-EKFGYLLEAFKYGTPPHAGLAFGLDR 543
Cdd:PTZ00425 489 KLNEDQKT---VAAMDVLVPKIgEVIGGSQREDNLERLDKMIK-----EKKLNmESYWWYRQLRKFGSHPHAGFGLGFER 560
|
90
....*....|....*....
gi 490589120 544 LVMLLAGTDNIREVIAFPK 562
Cdd:PTZ00425 561 LIMLVTGVDNIKDTIPFPR 579
|
|
| ScAspRS_mt_like_N |
cd04321 |
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
24-109 |
1.44e-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: 55.02 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 24 EVVLMGWVQKKRNLGG-LVFVDLRDTSGLC-QIVfDTDvDKEAFEKAEKLGAEFVIAVKGKVCERQSKNpNMPTGDIEIF 101
Cdd:cd04321 1 KVTLNGWIDRKPRIVKkLSFADLRDPNGDIiQLV-STA-KKDAFSLLKSITAESPVQVRGKLQLKEAKS-SEKNDEWELV 77
|
....*...
gi 490589120 102 ATELRLLN 109
Cdd:cd04321 78 VDDIQTLN 85
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
24-108 |
7.13e-09 |
|
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: 53.01 E-value: 7.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 24 EVVLMGWVQKKRNLGGLVFVDLRDTSGLCQIVFDTDVDKEaFEKAEKLGAEFVIAVKGKVCERQsKNPNMPTGdIEIFAT 103
Cdd:cd04323 1 RVKVFGWVHRLRSQKKLMFLVLRDGTGFLQCVLSKKLVTE-FYDAKSLTQESSVEVTGEVKEDP-RAKQAPGG-YELQVD 77
|
....*
gi 490589120 104 ELRLL 108
Cdd:cd04323 78 YLEII 82
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
157-559 |
1.73e-08 |
|
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: 56.02 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 157 RNYLsnnrfcEIETPFLI-APTPEGARDYLVPSRVNPG----KFYaLPQSPQLY-KQLLmVSGMDRYFQIVKCFRDEDLR 230
Cdd:TIGR00462 5 RGVL------EVETPLLSpAPVTDPHLDAFATEFVGPDgqgrPLY-LQTSPEYAmKRLL-AAGSGPIFQICKVFRNGERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 231 ADRQPEFT-----QIDCEMsfveqEDVMSMIEGLLEAIFKEvldveLALPLPKMTYAEAMSKYGsdkpdtrfgyeltdis 305
Cdd:TIGR00462 77 RRHNPEFTmlewyRPGFDY-----HDLMDEVEALLQELLGD-----PFAPAERLSYQEAFLRYA---------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 306 dvvcncgfkvfadatqpgksvrGINVkgkaddftrkQISSLEEHAKTYRAKGLAWMkvgqegvtspiakffNEEEMNAIL 385
Cdd:TIGR00462 131 ----------------------GIDP----------LTASLAELQAAAAAHGIRAS---------------EEDDRDDLL 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 386 TrmnaevgdlLLFVadknSIVFDALGQVRLevanrlnlldknvynlLWVTEFPVFEedeetgtfSAmhhpftspmdedLD 465
Cdd:TIGR00462 164 D---------LLFS----EKVEPHLGFGRP----------------TFLYDYPASQ--------AA------------LA 194
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 466 KLEEGDKS-SLRAKAYdivLNGYEIGGGSVRISNSDVQSRMF-------KALGFTEERANEKFgylLEAFKYGTPPHAGL 537
Cdd:TIGR00462 195 RISPDDPRvAERFELY---IKGLELANGFHELTDAAEQRRRFeadnalrKALGLPRYPLDERF---LAALEAGLPECSGV 268
|
410 420
....*....|....*....|..
gi 490589120 538 AFGLDRLVMLLAGTDNIREVIA 559
Cdd:TIGR00462 269 ALGVDRLLMLALGADSIDDVLA 290
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
488-562 |
7.62e-08 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 55.36 E-value: 7.62e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490589120 488 EIGGGSVRISNSDV-QSRMfkalgfTEERAN-EKFGYLLEAFKYGTPPHAGLAFGLDRLVMLLAGTDNIREVIAFPK 562
Cdd:PLN02603 488 ELIGGSQREERLEYlEARL------DELKLNkESYWWYLDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFPR 558
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
488-562 |
1.71e-07 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 54.23 E-value: 1.71e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490589120 488 EIGGGSVRISNSDVQSRMFKALGFteerANEKFGYLLEAFKYGTPPHAGLAFGLDRLVMLLAGTDNIREVIAFPK 562
Cdd:PLN02221 495 ELIGGSQREERYDVIKQRIEEMGL----PIEPYEWYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPR 565
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
476-557 |
5.69e-07 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 51.47 E-value: 5.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 476 RAKAYDIVLNGYEIGGGSVRISNSDVQSRMFKAlgFTEERANEKFG------YLLEAFKYGTPPHAGLAFGLDRLVMLLA 549
Cdd:PRK09350 221 VAERFEVYFKGIELANGFHELTDAREQRQRFEQ--DNRKRAARGLPqqpideNLIAALEAGLPDCSGVALGVDRLIMLAL 298
|
....*...
gi 490589120 550 GTDNIREV 557
Cdd:PRK09350 299 GAESISEV 306
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
24-108 |
6.07e-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: 6.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 24 EVVLMGWVQKKRNLGGLVFVDLRDtsGLC----QIVFDTdvDKEAFEKAEKL--GAefVIAVKGKVCERQSKNpnmptGD 97
Cdd:cd04318 1 EVTVNGWVRSVRDSKKISFIELND--GSClknlQVVVDK--ELTNFKEILKLstGS--SIRVEGVLVKSPGAK-----QP 69
|
90
....*....|.
gi 490589120 98 IEIFATELRLL 108
Cdd:cd04318 70 FELQAEKIEVL 80
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
477-562 |
3.84e-04 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 43.32 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589120 477 AKAYDIVL-NGYEIGGGSVRISNSDVQSRMFKALGFTEEraneKFGYLLEAFKYGTPPHAGLAFGLDRLVMLLAGTDNIR 555
Cdd:PLN02532 544 VAAFDLVVpKVGTVITGSQNEERMDILNARIEELGLPRE----QYEWYLDLRRHGTVKHSGFSLGFELMVLFATGLPDVR 619
|
....*..
gi 490589120 556 EVIAFPK 562
Cdd:PLN02532 620 DAIPFPR 626
|
|
| |
