|
Name |
Accession |
Description |
Interval |
E-value |
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
7-496 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 921.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 7 EELNDQQIVRREKMAALREQGIDPFGKRFERTANSQELKDKYANLDKEQLHDKNETATIAGRLVTKRGKGKVGFAHLQDR 86
Cdd:PRK00484 1 EELNEQIAVRREKLAELREQGIDPYPNKFERTHTAAELRAKYDDKEKEELEELEIEVSVAGRVMLKRVMGKASFATLQDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 87 EGQIQIYVRKDAVGEENYEIFKKADLGDFLGVEGEVMRTDMGELSIKATHITHLSKALRPLPEKFHGLTDVETIYRKRYL 166
Cdd:PRK00484 81 SGRIQLYVSKDDVGEEALEAFKKLDLGDIIGVEGTLFKTKTGELSVKATELTLLTKSLRPLPDKFHGLTDVETRYRQRYV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 167 DLISNRESFERFVTRSKIISEIRRYLDQKGFLEVETPVLHNEAGGAAARPFITHHNAQNIDMVLRIATELHLKRLIVGGM 246
Cdd:PRK00484 161 DLIVNPESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARPFITHHNALDIDLYLRIAPELYLKRLIVGGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 247 ERVYEIGRIFRNEGMDATHNPEFTSIEVYQAYADFQDIMDLTEGIIQHAAKSVKGDGPVNYQGTEIKINEPFKRVHMVDA 326
Cdd:PRK00484 241 ERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTYQGTEIDFGPPFKRLTMVDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 327 IREITGVDFWqDMTLKEAKAIAAEKKVPVEKHYTeVGHIINAFFEEFVEETLIQPTFVYGHPVAVSPLAKKNPEDQRFTD 406
Cdd:PRK00484 321 IKEYTGVDFD-DMTDEEARALAKELGIEVEKSWG-LGKLINELFEEFVEPKLIQPTFITDYPVEISPLAKRHREDPGLTE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 407 RFELFIMTKEYGNAFTELNDPIDQLSRFEAQAKAKELGDDEATGIDYDYIEALEYGMPPTGGLGIGIDRLCMLLTDTTTI 486
Cdd:PRK00484 399 RFELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSPSI 478
|
490
....*....|
gi 446024607 487 RDVLLFPTMK 496
Cdd:PRK00484 479 RDVILFPLMR 488
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
1-496 |
0e+00 |
|
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: 889.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 1 MSTEhmEELNDQQIVRREKMAALREQGIDPFGKRFERTANSQELKDKYANLDKEqlHDKNETATIAGRLVTKRGKGKVGF 80
Cdd:COG1190 1 MSEE--EDLNEQIRVRREKLEELREAGIDPYPNKFPRTHTAAEIREKYDELEAE--EETGDEVSVAGRIMAKRDMGKASF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 81 AHLQDREGQIQIYVRKDAVGEENYEIFKKADLGDFLGVEGEVMRTDMGELSIKATHITHLSKALRPLPEKFHGLTDVETI 160
Cdd:COG1190 77 ADLQDGSGRIQLYLRRDELGEEAYELFKLLDLGDIVGVEGTVFRTKTGELSVKVEELTLLSKSLRPLPEKFHGLTDPETR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 161 YRKRYLDLISNRESFERFVTRSKIISEIRRYLDQKGFLEVETPVLHNEAGGAAARPFITHHNAQNIDMVLRIATELHLKR 240
Cdd:COG1190 157 YRQRYVDLIVNPEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 241 LIVGGMERVYEIGRIFRNEGMDATHNPEFTSIEVYQAYADFQDIMDLTEGIIQHAAKSVKGDGPVNYQGTEIKINEPFKR 320
Cdd:COG1190 237 LIVGGFERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGTTKVTYQGQEIDLSPPWRR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 321 VHMVDAIREITGVDFWQDMTLKEAKAIAAEKKVPVEKHYTeVGHIINAFFEEFVEETLIQPTFVYGHPVAVSPLAKKNPE 400
Cdd:COG1190 317 ITMVEAIKEATGIDVTPLTDDEELRALAKELGIEVDPGWG-RGKLIDELFEELVEPKLIQPTFVTDYPVEVSPLAKRHRD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 401 DQRFTDRFELFIMTKEYGNAFTELNDPIDQLSRFEAQAKAKELGDDEATGIDYDYIEALEYGMPPTGGLGIGIDRLCMLL 480
Cdd:COG1190 396 DPGLTERFELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGLGIGIDRLVMLL 475
|
490
....*....|....*.
gi 446024607 481 TDTTTIRDVLLFPTMK 496
Cdd:COG1190 476 TDSPSIRDVILFPLMR 491
|
|
| lysS_bact |
TIGR00499 |
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ... |
8-496 |
0e+00 |
|
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the lysyl-tRNA synthetases that are class II amino-acyl tRNA synthetases. It includes all eukaryotic and most bacterial examples of the enzyme, but not archaeal or spirochete forms. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273107 [Multi-domain] Cd Length: 493 Bit Score: 707.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 8 ELNDQQIVRREKMAALREQGIDPFGKRFERTANSQELKDKYANLDKEQLHDKNETATIAGRLVTKRGKGKVGFAHLQDRE 87
Cdd:TIGR00499 1 ELNDQAQQRLEKLNRLRQTGNNPYLHKFERTHSAQEFQEKYADLSNEELKEKELKVSIAGRIKAIRSMGKATFITLQDES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 88 GQIQIYVRKDAVGEENYEIFKK-ADLGDFLGVEGEVMRTDMGELSIKATHITHLSKALRPLPEKFHGLTDVETIYRKRYL 166
Cdd:TIGR00499 81 GQIQLYVNKNKLPEDFYEFDEYlLDLGDIIGVTGYPFKTKTGELSVKVTELQILTKCLQPLPDKWHGLTDQETRYRQRYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 167 DLISNRESFERFVTRSKIISEIRRYLDQKGFLEVETPVLHNEAGGAAARPFITHHNAQNIDMVLRIATELHLKRLIVGGM 246
Cdd:TIGR00499 161 DLIVNPDVRQTFLKRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKPFITHHNALDMDLYLRIAPELYLKRLIVGGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 247 ERVYEIGRIFRNEGMDATHNPEFTSIEVYQAYADFQDIMDLTEGIIQHAAKSVKGDGPVNYQGTEIKINEPFKRVHMVDA 326
Cdd:TIGR00499 241 EKVYEIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTFIINYNDLEIDLKPPWKRITMVDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 327 IREITGVDFWQDMTLKEAKAIAAEKKVPVEKHYTEVGHIINAFFEEFVEETLIQPTFVYGHPVAVSPLAKKNPEDQRFTD 406
Cdd:TIGR00499 321 LEMVTGIDFDILKDDETAKALAKEHGIEVAEDSLTLGHILNKFFEQFLEHTLIQPTFITHYPAEISPLAKRDPSNPEFTE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 407 RFELFIMTKEYGNAFTELNDPIDQLSRFEAQAKAKELGDDEATGIDYDYIEALEYGMPPTGGLGIGIDRLCMLLTDTTTI 486
Cdd:TIGR00499 401 RFELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGIGIDRLVMLLTDAPSI 480
|
490
....*....|
gi 446024607 487 RDVLLFPTMK 496
Cdd:TIGR00499 481 RDVLLFPQLR 490
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
7-496 |
0e+00 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 642.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 7 EELNDQQI--VRREKMAALREQGIDPFGKRFERTANSQELKDKYANLDKEQlHDKNETATIAGRLVTKRGKGKVGFAHLQ 84
Cdd:PLN02502 54 ETMDPTQYraNRLKKVEALRAKGVEPYPYKFDVTHTAPELQEKYGSLENGE-ELEDVSVSVAGRIMAKRAFGKLAFYDLR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 85 DREGQIQIYVRKDAVGEENyEIFKK----ADLGDFLGVEGEVMRTDMGELSIKATHITHLSKALRPLPEKFHGLTDVETI 160
Cdd:PLN02502 133 DDGGKIQLYADKKRLDLDE-EEFEKlhslVDRGDIVGVTGTPGKTKKGELSIFPTSFEVLTKCLLMLPDKYHGLTDQETR 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 161 YRKRYLDLISNRESFERFVTRSKIISEIRRYLDQKGFLEVETPVLHNEAGGAAARPFITHHNAQNIDMVLRIATELHLKR 240
Cdd:PLN02502 212 YRQRYLDLIANPEVRDIFRTRAKIISYIRRFLDDRGFLEVETPMLNMIAGGAAARPFVTHHNDLNMDLYLRIATELHLKR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 241 LIVGGMERVYEIGRIFRNEGMDATHNPEFTSIEVYQAYADFQDIMDLTEGIIQHAAKSVKGDGPVNYQGTEIKINEPFKR 320
Cdd:PLN02502 292 LVVGGFERVYEIGRQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKELTGSYKIKYHGIEIDFTPPFRR 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 321 VHMVDAIREITGVDFWQDMTLKEAKA--IAAEKK--VPVEKHYTeVGHIINAFFEEFVEETLIQPTFVYGHPVAVSPLAK 396
Cdd:PLN02502 372 ISMISLVEEATGIDFPADLKSDEANAylIAACEKfdVKCPPPQT-TGRLLNELFEEFLEETLVQPTFVLDHPVEMSPLAK 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 397 KNPEDQRFTDRFELFIMTKEYGNAFTELNDPIDQLSRFEAQAKAKELGDDEATGIDYDYIEALEYGMPPTGGLGIGIDRL 476
Cdd:PLN02502 451 PHRSKPGLTERFELFINGRELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRL 530
|
490 500
....*....|....*....|
gi 446024607 477 CMLLTDTTTIRDVLLFPTMK 496
Cdd:PLN02502 531 VMLLTDSASIRDVIAFPAMK 550
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
171-496 |
0e+00 |
|
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: 542.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 171 NRESFERFVTRSKIISEIRRYLDQKGFLEVETPVLHNEAGGAAARPFITHHNAQNIDMVLRIATELHLKRLIVGGMERVY 250
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 251 EIGRIFRNEGMDATHNPEFTSIEVYQAYADFQDIMDLTEGIIQHAAKSVKGDGPVNYQGTEIKINEPFKRVHMVDAIREI 330
Cdd:cd00775 81 EIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIEYGGKELDFTPPFKRVTMVDALKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 331 TGVDFW---QDMTLKEAKAIAAEKKVPVEKHYTeVGHIINAFFEEFVEETLIQPTFVYGHPVAVSPLAKKNPEDQRFTDR 407
Cdd:cd00775 161 TGIDFPeldLEQPEELAKLLAKLIKEKIEKPRT-LGKLLDKLFEEFVEPTLIQPTFIIDHPVEISPLAKRHRSNPGLTER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 408 FELFIMTKEYGNAFTELNDPIDQLSRFEAQAKAKELGDDEATGIDYDYIEALEYGMPPTGGLGIGIDRLCMLLTDTTTIR 487
Cdd:cd00775 240 FELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLTDSNSIR 319
|
....*....
gi 446024607 488 DVLLFPTMK 496
Cdd:cd00775 320 DVILFPAMR 328
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
8-496 |
1.93e-159 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 462.22 E-value: 1.93e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 8 ELNDQQIVRREKMAALREQGIdPFGKRFERTANSQELKDKYANLDKEQLHDKNETATIAGRLVTKRGKGKVGFAHLQDRE 87
Cdd:PRK12445 14 DFNDELRNRREKLAALRQQGV-AFPNDFRRDHTSDQLHEEFDAKDNQELESLNIEVSVAGRMMTRRIMGKASFVTLQDVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 88 GQIQIYVRKDAVGEENY-EIFKKADLGDFLGVEGEVMRTDMGELSIKATHITHLSKALRPLPEKFHGLTDVETIYRKRYL 166
Cdd:PRK12445 93 GRIQLYVARDSLPEGVYnDQFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFHGLQDQEVRYRQRYL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 167 DLISNRESFERFVTRSKIISEIRRYLDQKGFLEVETPVLHNEAGGAAARPFITHHNAQNIDMVLRIATELHLKRLIVGGM 246
Cdd:PRK12445 173 DLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 247 ERVYEIGRIFRNEGMDATHNPEFTSIEVYQAYADFQDIMDLTEGIIQHAAKSVKGDGPVNYQGTEIKINEPFKRVHMVDA 326
Cdd:PRK12445 253 ERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFDFGKPFEKLTMREA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 327 IREITGVDFWQDM-TLKEAKAIAAEKKVPVEKHYTeVGHIINAFFEEFVEETLIQPTFVYGHPVAVSPLAKKNPEDQRFT 405
Cdd:PRK12445 333 IKKYRPETDMADLdNFDAAKALAESIGITVEKSWG-LGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEIT 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 406 DRFELFIMTKEYGNAFTELNDPIDQLSRFEAQAKAKELGDDEATGIDYDYIEALEYGMPPTGGLGIGIDRLCMLLTDTTT 485
Cdd:PRK12445 412 DRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHT 491
|
490
....*....|.
gi 446024607 486 IRDVLLFPTMK 496
Cdd:PRK12445 492 IRDVILFPAMR 502
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
9-496 |
4.34e-159 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 479.85 E-value: 4.34e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 9 LNDQQIVRREKMAALREQGIDPFGKRFERTANSQELKDkyanldkeqlHDKNETATIAGRLVTKRGKGKVGFAHLQDREG 88
Cdd:PRK02983 610 LPEQVRVRLAKLEALRAAGVDPYPVGVPPTHTVAEALD----------APTGEEVSVSGRVLRIRDYGGVLFADLRDWSG 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 89 QIQIYVRKDAVGEENYEIFKKA-DLGDFLGVEGEVMRTDMGELSIKATHITHLSKALRPLPEKFHGLTDVETIYRKRYLD 167
Cdd:PRK02983 680 ELQVLLDASRLEQGSLADFRAAvDLGDLVEVTGTMGTSRNGTLSLLVTSWRLAGKCLRPLPDKWKGLTDPEARVRQRYLD 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 168 LISNRESFERFVTRSKIISEIRRYLDQKGFLEVETPVLHNEAGGAAARPFITHHNAQNIDMVLRIATELHLKRLIVGGME 247
Cdd:PRK02983 760 LAVNPEARDLLRARSAVVRAVRETLVARGFLEVETPILQQVHGGANARPFVTHINAYDMDLYLRIAPELYLKRLCVGGVE 839
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 248 RVYEIGRIFRNEGMDATHNPEFTSIEVYQAYADFQDIMDLTEGIIQHAAKSVKG-------DGPVNYQGTEIKINEPFKR 320
Cdd:PRK02983 840 RVFELGRNFRNEGVDATHNPEFTLLEAYQAHADYDTMRDLTRELIQNAAQAAHGapvvmrpDGDGVLEPVDISGPWPVVT 919
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 321 VHmvDAIREITGVDFWQDMTLKEAKAIAAEKKVPVEKHYTEvGHIINAFFEEFVEETLIQPTFVYGHPVAVSPLAKKNPE 400
Cdd:PRK02983 920 VH--DAVSEALGEEIDPDTPLAELRKLCDAAGIPYRTDWDA-GAVVLELYEHLVEDRTTFPTFYTDFPTSVSPLTRPHRS 996
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 401 DQRFTDRFELFIMTKEYGNAFTELNDPIDQLSRFEAQAKAKELGDDEATGIDYDYIEALEYGMPPTGGLGIGIDRLCMLL 480
Cdd:PRK02983 997 DPGLAERWDLVAWGVELGTAYSELTDPVEQRRRLTEQSLLAAGGDPEAMELDEDFLQALEYAMPPTGGLGMGVDRLVMLL 1076
|
490
....*....|....*.
gi 446024607 481 TDtTTIRDVLLFPTMK 496
Cdd:PRK02983 1077 TG-RSIRETLPFPLVK 1091
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
24-496 |
2.76e-126 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 380.12 E-value: 2.76e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 24 REQGIDPFGKRFERTANSQELKDKYANLDKEQlHDKNETATIAGRLVTKRGKG-KVGFAHLQDREGQIQI---YVRKDAV 99
Cdd:PTZ00417 97 KAKGINPYPHKFERTITVPEFVEKYQDLASGE-HLEDTILNVTGRIMRVSASGqKLRFFDLVGDGAKIQVlanFAFHDHT 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 100 GEENYEIFKKADLGDFLGVEGEVMRTDMGELSIKATHITHLSKALRPLPEKFhGLTDVETIYRKRYLDLISNRESFERFV 179
Cdd:PTZ00417 176 KSNFAECYDKIRRGDIVGIVGFPGKSKKGELSIFPKETIILSPCLHMLPMKY-GLKDTEIRYRQRYLDLMINESTRSTFI 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 180 TRSKIISEIRRYLDQKGFLEVETPVLHNEAGGAAARPFITHHNAQNIDMVLRIATELHLKRLIVGGMERVYEIGRIFRNE 259
Cdd:PTZ00417 255 TRTKIINYLRNFLNDRGFIEVETPTMNLVAGGANARPFITHHNDLDLDLYLRIATELPLKMLIVGGIDKVYEIGKVFRNE 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 260 GMDATHNPEFTSIEVYQAYADFQDIMDLTE----GIIQHAAKSVK----GDGPVNyQGTEIKINEPFKRVHMVDAIREIT 331
Cdd:PTZ00417 335 GIDNTHNPEFTSCEFYWAYADFYDLIKWSEdffsQLVMHLFGTYKilynKDGPEK-DPIEIDFTPPYPKVSIVEELEKLT 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 332 GVDFWQDM----TLKEAKAIAAEKKVPVEKHYTeVGHIINAFFEEFVEETLI-QPTFVYGHPVAVSPLAKKNPEDQRFTD 406
Cdd:PTZ00417 414 NTKLEQPFdspeTINKMINLIKENKIEMPNPPT-AAKLLDQLASHFIENKYPnKPFFIIEHPQIMSPLAKYHRSKPGLTE 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 407 RFELFIMTKEYGNAFTELNDPIDQLSRFEAQAKAKELGDDEATGIDYDYIEALEYGMPPTGGLGIGIDRLCMLLTDTTTI 486
Cdd:PTZ00417 493 RLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCTSLEYGLPPTGGLGLGIDRITMFLTNKNCI 572
|
490
....*....|
gi 446024607 487 RDVLLFPTMK 496
Cdd:PTZ00417 573 KDVILFPTMR 582
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
35-496 |
5.55e-118 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 361.27 E-value: 5.55e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 35 FERTANSQELKDKYANLDKEQlHDKNETATIAGRLVTKRGKGKVGFAHLQDREGQIQIYVRkdaVGEEnyeiFKKADL-- 112
Cdd:PTZ00385 83 FRGITPISEVRERYGYLASGD-RAAQATVRVAGRVTSVRDIGKIIFVTIRSNGNELQVVGQ---VGEH----FTREDLkk 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 113 -------GDFLGVEGEVMRTDMGELSIKATHITHLS------KALRPLPEKFHGLTDVETIYRKRYLDLISNRESFERFV 179
Cdd:PTZ00385 155 lkvslrvGDIIGADGVPCRMQRGELSVAASRMLILSpyvctdQVVCPNLRGFTVLQDNDVKYRYRFTDMMTNPCVIETIK 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 180 TRSKIISEIRRYLDQKGFLEVETPVLHNEAGGAAARPFITHHNAQNIDMVLRIATELHLKRLIVGGMERVYEIGRIFRNE 259
Cdd:PTZ00385 235 KRHVMLQALRDYFNERNFVEVETPVLHTVASGANAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERIYEIGKVFRNE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 260 GMDATHNPEFTSIEVYQAYADFQDIMDLTEGIIQHAAKSVKGDG-----PVNYQGT--EIKINEPFKRVHMVDAIREITG 332
Cdd:PTZ00385 315 DADRSHNPEFTSCEFYAAYHTYEDLMPMTEDIFRQLAMRVNGTTvvqiyPENAHGNpvTVDLGKPFRRVSVYDEIQRMSG 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 333 VDFWQDMTLKEAKAIAAEKKVPVeKHYTEVGHIINA--FFEE----FVEETLIQPTFVYGHPVAVSPLAKKNPEDQRFTD 406
Cdd:PTZ00385 395 VEFPPPNELNTPKGIAYMSVVML-RYNIPLPPVRTAakMFEKlidfFITDRVVEPTFVMDHPLFMSPLAKEQVSRPGLAE 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 407 RFELFIMTKEYGNAFTELNDPIDQLSRFEAQAKAKELGDDEATGIDYDYIEALEYGMPPTGGLGIGIDRLCMLLTDTTTI 486
Cdd:PTZ00385 474 RFELFVNGIEYCNAYSELNDPHEQYHRFQQQLVDRQGGDEEAMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNI 553
|
490
....*....|
gi 446024607 487 RDVLLFPTMK 496
Cdd:PTZ00385 554 RDGIIFPLLR 563
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
156-496 |
3.06e-116 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 344.93 E-value: 3.06e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 156 DVETIYRKRYLDLiSNRESFERFVTRSKIISEIRRYLDQKGFLEVETPVLHNEAGGAAARPFITHHNAQNIDMVLRIATE 235
Cdd:pfam00152 1 DEETRLKYRYLDL-RRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 236 LHLKRLIVGGMERVYEIGRIFRNEGMDATHNPEFTSIEVYQAYADFQDIMDLTEGIIQHAAKSVKGDGPVNYQGTEIKIN 315
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 316 EPFKRVHMVDAIREITGVDF--WQDMTLKEAKAIAAEKKVPVEKHytevghiinaffeefveetliQPTFVYGHPVAVSP 393
Cdd:pfam00152 160 KPFPRITYAEAIEKLNGKDVeeLGYGSDKPDLRFLLELVIDKNKF---------------------NPLWVTDFPAEHHP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 394 LAKKNPED-QRFTDRFELFIMTKEYGNAFTELNDPIDQLSRFEAQAKAKElgddEATGIDYDYIEALEYGMPPTGGLGIG 472
Cdd:pfam00152 219 FTMPKDEDdPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDPE----EAEEKFGFYLDALKYGAPPHGGLGIG 294
|
330 340
....*....|....*....|....
gi 446024607 473 IDRLCMLLTDTTTIRDVLLFPTMK 496
Cdd:pfam00152 295 LDRLVMLLTGLESIREVIAFPKTR 318
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
178-496 |
2.28e-93 |
|
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: 284.37 E-value: 2.28e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 178 FVTRSKIISEIRRYLDQKGFLEVETPVLHNEAGGAAARPFITHHNAQNIDMVLRIATELHLKRLIVGGMERVYEIGRIFR 257
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 258 NEGMDATHNPEFTSIEVYQAYADFQDIMDLTEGIIQHAAKSVKGDGPVNYQGTEIKINEPFKRVHMVDAIreitgvdfwq 337
Cdd:cd00669 81 NEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYGFELEDFGLPFPRLTYREAL---------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 338 dmtlkeakaiaaekkvpvekhytevghiinaffeefveETLIQPTFVYGHPV-AVSPLAKKNPEDQRFTDRFELFIMTKE 416
Cdd:cd00669 151 --------------------------------------ERYGQPLFLTDYPAeMHSPLASPHDVNPEIADAFDLFINGVE 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 417 YGNAFTELNDPIDQLSRFEAQAKAKELGDDEatgiDYDYIEALEYGMPPTGGLGIGIDRLCMLLTDTTTIRDVLLFPTMK 496
Cdd:cd00669 193 VGNGSSRLHDPDIQAEVFQEQGINKEAGMEY----FEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKMR 268
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
174-490 |
1.01e-68 |
|
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441870 [Multi-domain] Cd Length: 309 Bit Score: 222.29 E-value: 1.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 174 SFERFVTRSKIISEIRRYLDQKGFLEVETPVLhNEAGGAAA--RPFIT---HHNAQNIDMVLRIATELHLKRLIVGGMER 248
Cdd:COG2269 2 SREALRARARLLAAIRAFFAERGVLEVETPAL-SVAPGTDPhlDSFATefiGPDGGGRPLYLHTSPEFAMKRLLAAGSGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 249 VYEIGRIFRNEGMDATHNPEFTSIEVYQAYADFQDIMDLTEGIIQHAAKSVKgdgpvnyqgteikiNEPFKRVHMVDAIR 328
Cdd:COG2269 81 IYQIAKVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAAG--------------FAPAERLSYQEAFL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 329 EITGVDFWQdMTLKEAKAIAAEKKVPVEKHYTEVGhIINAFFEEFVEETLIQ--PTFVYGHPVAVSPLAKKNPEDQRFTD 406
Cdd:COG2269 147 RYLGIDPLT-ADLDELAAAAAAAGLRVADDDDRDD-LLDLLLSERVEPQLGRdrPTFLYDYPASQAALARISPDDPRVAE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 407 RFELFIMTKEYGNAFTELNDPIDQLSRFEA-QAKAKELGDDEATgIDYDYIEALEYGMPPTGGLGIGIDRLCMLLTDTTT 485
Cdd:COG2269 225 RFELYACGVELANGFHELTDAAEQRRRFEAdNAERERLGLPPYP-IDERFLAALAAGLPDCSGVALGFDRLLMLALGAER 303
|
....*
gi 446024607 486 IRDVL 490
Cdd:COG2269 304 IDDVL 308
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
191-490 |
1.21e-57 |
|
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: 192.77 E-value: 1.21e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 191 YLDQKGFLEVETPVLHNeAGGAAA--RPFITH---HNAQNIDMVLRIATELHLKRLIVGGMERVYEIGRIFRNEGMDATH 265
Cdd:TIGR00462 1 FFAERGVLEVETPLLSP-APVTDPhlDAFATEfvgPDGQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 266 NPEFTSIEVYQAYADFQDIMDLTEGIIQHAAKsvkgdgpvnyqgteiKINEPFKRVHMVDAIREITGVDFWQDmTLKEAK 345
Cdd:TIGR00462 80 NPEFTMLEWYRPGFDYHDLMDEVEALLQELLG---------------DPFAPAERLSYQEAFLRYAGIDPLTA-SLAELQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 346 AIAAEKKV--PVEKHYTEVghiinaFFEEFVE--ETLI---QPTFVYGHPVAVSPLAKKNPEDQRFTDRFELFIMTKEYG 418
Cdd:TIGR00462 144 AAAAAHGIraSEEDDRDDL------LDLLFSEkvEPHLgfgRPTFLYDYPASQAALARISPDDPRVAERFELYIKGLELA 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446024607 419 NAFTELNDPIDQLSRFEAQAKAKELGDDEATGIDYDYIEALEYGMPPTGGLGIGIDRLCMLLTDTTTIRDVL 490
Cdd:TIGR00462 218 NGFHELTDAAEQRRRFEADNALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDVL 289
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
174-489 |
7.18e-54 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 183.21 E-value: 7.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 174 SFERFVTRSKIISEIRRYLDQKGFLEVETPVL--------HNEaggaaarPFITH----HNAQNIDMVLRIATELHLKRL 241
Cdd:PRK09350 1 SIPNLLKRAKIIAEIRRFFADRGVLEVETPILsqatvtdiHLV-------PFETRfvgpGASQGKTLWLMTSPEYHMKRL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 242 IVGGMERVYEIGRIFRNEGMDATHNPEFTSIEVYQAYADFQDIMDLTEGIIQHAAKSvkgdgpvnyqgteikinEPFKRV 321
Cdd:PRK09350 74 LAAGSGPIFQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDC-----------------EPAESL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 322 HMVDAIREITGVDfwqdmTLKEAKAIAAEKKvpvEKHytevgHIINAFFEEFVEETLIQ---------------PTFVYG 386
Cdd:PRK09350 137 SYQQAFLRYLGID-----PLSADKTQLREVA---AKL-----GLSNIADEEEDRDTLLQllftfgvepnigkekPTFVYH 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 387 HPVAVSPLAKKNPEDQRFTDRFELFIMTKEYGNAFTELNDPIDQLSRFE---AQAKAKELGDDEatgIDYDYIEALEYGM 463
Cdd:PRK09350 204 FPASQAALAKISTEDHRVAERFEVYFKGIELANGFHELTDAREQRQRFEqdnRKRAARGLPQQP---IDENLIAALEAGL 280
|
330 340
....*....|....*....|....*.
gi 446024607 464 PPTGGLGIGIDRLCMLLTDTTTIRDV 489
Cdd:PRK09350 281 PDCSGVALGVDRLIMLALGAESISEV 306
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
64-168 |
1.62e-53 |
|
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: 175.74 E-value: 1.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 64 TIAGRLVTKRGKGKVGFAHLQDREGQIQIYVRKDAVGEENYEIFKKA-DLGDFLGVEGEVMRTDMGELSIKATHITHLSK 142
Cdd:cd04322 3 SVAGRIMSKRGSGKLSFADLQDESGKIQVYVNKDDLGEEEFEDFKKLlDLGDIIGVTGTPFKTKTGELSIFVKEFTLLSK 82
|
90 100
....*....|....*....|....*.
gi 446024607 143 ALRPLPEKFHGLTDVETIYRKRYLDL 168
Cdd:cd04322 83 SLRPLPEKFHGLTDVETRYRQRYLDL 108
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
60-493 |
2.36e-47 |
|
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: 169.46 E-value: 2.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 60 NETATIAGRLVTKRGKGKVGFAHLQDREGQIQIYVRKDAVgeENYEIFKKADLGDFLGVEGEVMRTDM--GELSIKATHI 137
Cdd:COG0017 14 GQEVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKL--ENFEEAKKLTTESSVEVTGTVVESPRapQGVELQAEEI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 138 THLSKALRPLP--EKFHGLtdvETIYRKRYLDLISNRESfERFVTRSKIISEIRRYLDQKGFLEVETPVLhneaGGAAAR 215
Cdd:COG0017 92 EVLGEADEPYPlqPKRHSL---EFLLDNRHLRLRTNRFG-AIFRIRSELARAIREFFQERGFVEVHTPII----TASATE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 216 PfithhnaqnidmvlriATEL----------HL-------KRLIVGGMERVYEIGRIFRNEGMDAT-HNPEFTSIEVYQA 277
Cdd:COG0017 164 G----------------GGELfpvdyfgkeaYLtqsgqlyKEALAMALEKVYTFGPTFRAEKSNTRrHLAEFWMIEPEMA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 278 YADFQDIMDLTEGIIQHAAKSVKGDGP-------VNYQGTEIKINEPFKRVHMVDAIreitgvdfwqdmtlkeakAIAAE 350
Cdd:COG0017 228 FADLEDVMDLAEEMLKYIIKYVLENCPeeleflgRDVERLEKVPESPFPRITYTEAI------------------EILKK 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 351 KKVPVE-------KHYTEVGhiinaffEEFVEEtliqPTFVYGHPVAVSPL-AKKNPEDQRFTDRFELfiMTKEYGnaft 422
Cdd:COG0017 290 SGEKVEwgddlgtEHERYLG-------EEFFKK----PVFVTDYPKEIKAFyMKPNPDDPKTVAAFDL--LAPGIG---- 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446024607 423 EL------NDPIDQLsrfeaQAKAKELGDDEAtgiDYD-YIEALEYGMPPTGGLGIGIDRLCMLLTDTTTIRDVLLFP 493
Cdd:COG0017 353 EIiggsqrEHRYDVL-----VERIKEKGLDPE---DYEwYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFP 422
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
57-493 |
1.06e-44 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 162.67 E-value: 1.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 57 HDKNETATIAGRLVTKRGKGKVGFAHLQDREGQIQIYVRKDAVgEENYEIFKKADLGDFLGVEGEVMRTDM--GELSIKA 134
Cdd:PRK05159 13 ELDGEEVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKVD-EELFETIKKLKRESVVSVTGTVKANPKapGGVEVIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 135 THITHLSKALRPLPEKFHG--LTDVETIYRKRYLDLISNRESfERFVTRSKIISEIRRYLDQKGFLEVETPVLHNEA--G 210
Cdd:PRK05159 92 EEIEVLNKAEEPLPLDISGkvLAELDTRLDNRFLDLRRPRVR-AIFKIRSEVLRAFREFLYENGFTEIFTPKIVASGteG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 211 GAAARPfITHHN-----AQnidmvlriATELHlKRLIVG-GMERVYEIGRIFRNEGMDAT-HNPEFTSIEVYQAYAD-FQ 282
Cdd:PRK05159 171 GAELFP-IDYFEkeaylAQ--------SPQLY-KQMMVGaGFERVFEIGPVFRAEEHNTSrHLNEYTSIDVEMGFIDdHE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 283 DIMDLTEGIIQHAAKSVKGDGP--VNYQGTEIKINE-PFKRVhmvdaireitgvdfwqdmTLKEAKAIAAEKKVPVEKHY 359
Cdd:PRK05159 241 DVMDLLENLLRYMYEDVAENCEkeLELLGIELPVPEtPIPRI------------------TYDEAIEILKSKGNEISWGD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 360 ---TEVGHIINaffEEFVEETLIQPTFVYGHPVAVSPL-AKKNPEDQRFTDRFELFIMTKEYGNAFTELNDPIDQLSRFE 435
Cdd:PRK05159 303 dldTEGERLLG---EYVKEEYGSDFYFITDYPSEKRPFyTMPDEDDPEISKSFDLLFRGLEITSGGQRIHRYDMLVESIK 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446024607 436 AQakakelgddeatGIDYD----YIEALEYGMPPTGGLGIGIDRLCMLLTDTTTIRDVLLFP 493
Cdd:PRK05159 380 EK------------GLNPEsfefYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFP 429
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
50-493 |
4.16e-40 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 152.53 E-value: 4.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 50 NLDKEQLhdkNETATIAGRLVTKRGKGKVGFAHLQDREGQIQIYVRKDAvgeenyEIFKKAD-LG--DFLGVEGEV---- 122
Cdd:PRK00476 10 ELRESHV---GQTVTLCGWVHRRRDHGGLIFIDLRDREGIVQVVFDPDA------EAFEVAEsLRseYVIQVTGTVrarp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 123 -------MRTdmGELSIKATHITHLSKAlRPLPekFH--GLTDV--ETIYRKRYLDLisnR--ESFERFVTRSKIISEIR 189
Cdd:PRK00476 81 egtvnpnLPT--GEIEVLASELEVLNKS-KTLP--FPidDEEDVseELRLKYRYLDL---RrpEMQKNLKLRSKVTSAIR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 190 RYLDQKGFLEVETPVLhneagGAA----ARPFI----THHN-----AQnidmvlriATELhLKRLI-VGGMERVYEIGRI 255
Cdd:PRK00476 153 NFLDDNGFLEIETPIL-----TKStpegARDYLvpsrVHPGkfyalPQ--------SPQL-FKQLLmVAGFDRYYQIARC 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 256 FRNEGMDATHNPEFTSIEVYQAYADFQDIMDLTEGIIQHAAKSVKGdgpvnyqgteIKINEPFKRVHMVDAIR------- 328
Cdd:PRK00476 219 FRDEDLRADRQPEFTQIDIEMSFVTQEDVMALMEGLIRHVFKEVLG----------VDLPTPFPRMTYAEAMRrygsdkp 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 329 ------EITGV-DFWQDMTLKE-AKAIAAEKKV---PVE-----------KHYTEVGHIINA------------------ 368
Cdd:PRK00476 289 dlrfglELVDVtDLFKDSGFKVfAGAANDGGRVkaiRVPggaaqlsrkqiDELTEFAKIYGAkglayikvnedglkgpia 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 369 -FFEEFVEETLIQPT---------FVYGHPVAVS------------------------------PLAKKNPEDQRFTDRF 408
Cdd:PRK00476 369 kFLSEEELAALLERTgakdgdlifFGADKAKVVNdalgalrlklgkelglidedkfaflwvvdfPMFEYDEEEGRWVAAH 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 409 ELFIMTKEYGNAFTELNDPIDQLS--------------------RFEAQAKAKE---LGDDEAT---GIdydYIEALEYG 462
Cdd:PRK00476 449 HPFTMPKDEDLDELETTDPGKARAyaydlvlngyelgggsirihRPEIQEKVFEilgISEEEAEekfGF---LLDALKYG 525
|
570 580 590
....*....|....*....|....*....|.
gi 446024607 463 MPPTGGLGIGIDRLCMLLTDTTTIRDVLLFP 493
Cdd:PRK00476 526 APPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
47-493 |
2.78e-38 |
|
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: 144.97 E-value: 2.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 47 KYANLDKEQLHDKnetATIAGRLVTKRGKGKVGFAHLQDREGQIQIYVRKDAVGEENYEIFKKADLGDFLGVEGEVMRTD 126
Cdd:TIGR00458 2 YSADIKPEMDGQE---VTFMGWVHEIRDLGGLIFVLLRDREGLIQITAPAKKVSKNLFKWAKKLNLESVVAVRGIVKIKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 127 --MGELSIKATHITHLSKALRPLP----EKFHGltDVETIYRKRYLDLISNRESfERFVTRSKIISEIRRYLDQKGFLEV 200
Cdd:TIGR00458 79 kaPGGFEIIPTKIEVINEAKEPLPldptEKVPA--ELDTRLDYRFLDLRRPTVQ-AIFRIRSGVLESVREFLAEEGFIEV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 201 ETPVLHNEA--GGAAARPfITHHNAQnidMVLRIATELHLKRLIVGGMERVYEIGRIFRNEGMDAT-HNPEFTSIEVYQA 277
Cdd:TIGR00458 156 HTPKLVASAteGGTELFP-ITYFERE---AFLGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNTHrHLNEATSIDIEMA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 278 YADFQDIMDLTEGIIQHAAKSVKGDGPVNYQGTEIKI---NEPFKRVhmvdaireitgvdfwqdmTLKEAKAIAAEKKVP 354
Cdd:TIGR00458 232 FEDHHDVMDILEELVVRVFEDVPERCAHQLETLEFKLekpEGKFVRL------------------TYDEAIEMANAKGVE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 355 VEKhytevGHIINAFFEEFVEETLIQPTFVYGHPVAVSPLAKKNPEDQ-RFTDRFELFIMTKEYGNAFTElndpIDQLSR 433
Cdd:TIGR00458 294 IGW-----GEDLSTEAEKALGEEMDGLYFITDWPTEIRPFYTMPDEDNpEISKSFDLMYRDLEISSGAQR----IHLHDL 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 434 FEAQAKAKELGDDEATgidyDYIEALEYGMPPTGGLGIGIDRLCMLLTDTTTIRDVLLFP 493
Cdd:TIGR00458 365 LVERIKAKGLNPEGFK----DYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFP 420
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
60-493 |
2.11e-35 |
|
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: 138.98 E-value: 2.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 60 NETATIAGRLVTKRGKGKVGFAHLQDREGQIQIYVRKDavgeENYEIFKKAD-LG--DFLGVEGEV-----------MRT 125
Cdd:COG0173 16 GQEVTLSGWVHRRRDHGGLIFIDLRDRYGITQVVFDPD----DSAEAFEKAEkLRseYVIAVTGKVrarpegtvnpkLPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 126 dmGELSIKATHITHLSKAlRPLPEKFHGLTDV--ETIYRKRYLDLisNRES-FERFVTRSKIISEIRRYLDQKGFLEVET 202
Cdd:COG0173 92 --GEIEVLASELEILNKA-KTPPFQIDDDTDVseELRLKYRYLDL--RRPEmQKNLILRHKVTKAIRNYLDENGFLEIET 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 203 PVLhneagGAA----ARPFI----THHN-----AQnidmvlriATELhLKRLI-VGGMERVYEIGRIFRNEGMDATHNPE 268
Cdd:COG0173 167 PIL-----TKStpegARDYLvpsrVHPGkfyalPQ--------SPQL-FKQLLmVSGFDRYFQIARCFRDEDLRADRQPE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 269 FTSIEVYQAYADFQDIMDLTEGIIQHAAKSVKGdgpvnyqgteIKINEPFKRVHMVDAIREiTGVD-----FwqDMTLKE 343
Cdd:COG0173 233 FTQLDIEMSFVDQEDVFELMEGLIRHLFKEVLG----------VELPTPFPRMTYAEAMER-YGSDkpdlrF--GLELVD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 344 AKAIAAEK--KV---PVEKH---------------------YTEVGHIINA-------------------FFEEFVEETL 378
Cdd:COG0173 300 VTDIFKDSgfKVfagAAENGgrvkainvpggaslsrkqideLTEFAKQYGAkglayikvnedglkspiakFLSEEELAAI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 379 IQPT---------FVYGHPVAVSP--------LAKK----NPEDQRF---TDrFELFIMTKEYG------NAFTELNDP- 427
Cdd:COG0173 380 LERLgakpgdlifFVADKPKVVNKalgalrlkLGKElgliDEDEFAFlwvVD-FPLFEYDEEEGrwvamhHPFTMPKDEd 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 428 IDQLSRFEAQAKAK---------ELG-------DDE-------ATGIDYDY--------IEALEYGMPPTGGLGIGIDRL 476
Cdd:COG0173 459 LDLLETDPGKVRAKaydlvlngyELGggsirihDPElqekvfeLLGISEEEaeekfgflLEAFKYGAPPHGGIAFGLDRL 538
|
570
....*....|....*..
gi 446024607 477 CMLLTDTTTIRDVLLFP 493
Cdd:COG0173 539 VMLLAGEDSIRDVIAFP 555
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
178-493 |
8.83e-34 |
|
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: 128.85 E-value: 8.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 178 FVTRSKIISEIRRYLDQKGFLEVETPVLhNEAGGAAARPFIthhnaqnidmvlrIATELH-------------LKRLI-V 243
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPIL-TKSTPEGARDFL-------------VPSRLHpgkfyalpqspqlFKQLLmV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 244 GGMERVYEIGRIFRNEGMDATHNPEFTSIEVYQAYADFQDIMDLTEGIIQHAAKSVKGdgpvnyqgteIKINEPFKRVHM 323
Cdd:cd00777 67 SGFDRYFQIARCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG----------VELTTPFPRMTY 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 324 VDAIREItGVDF-W-QDMTLKEakaiaaekKVPVEKHYTEVGHIinafFEEFVEETLiqptfvyghpvavsPLAKKNPED 401
Cdd:cd00777 137 AEAMERY-GFKFlWiVDFPLFE--------WDEEEGRLVSAHHP----FTAPKEEDL--------------DLLEKDPED 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 402 QRfTDRFELFIMTKEYGNAFTELNDPIDQLSRFEAQAKAKELGDDEATGIdydyIEALEYGMPPTGGLGIGIDRLCMLLT 481
Cdd:cd00777 190 AR-AQAYDLVLNGVELGGGSIRIHDPDIQEKVFEILGLSEEEAEEKFGFL----LEAFKYGAPPHGGIALGLDRLVMLLT 264
|
330
....*....|..
gi 446024607 482 DTTTIRDVLLFP 493
Cdd:cd00777 265 GSESIRDVIAFP 276
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
156-493 |
5.50e-31 |
|
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: 122.29 E-value: 5.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 156 DVETIYRKRYLDLISNRESfERFVTRSKIISEIRRYLDQKGFLEVETPVLHNEA--GGAAARPFithhNAQNIDMVLRIA 233
Cdd:cd00776 3 NLETLLDNRHLDLRTPKVQ-AIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDteGGAELFKV----SYFGKPAYLAQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 234 TELHLKRLIvGGMERVYEIGRIFRNEGMDAT-HNPEFTSIEVYQAYA-DFQDIMDLTEGIIQHAAKSVKGDGP-----VN 306
Cdd:cd00776 78 PQLYKEMLI-AALERVYEIGPVFRAEKSNTRrHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAkelelVN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 307 YQGTEIKI-NEPFKRvhmvdaireitgvdfwqdMTLKEAKAIAAEKKVPVEKHYTEVghiINAFFEEFVEETLIQ-PTFV 384
Cdd:cd00776 157 QLNRELLKpLEPFPR------------------ITYDEAIELLREKGVEEEVKWGED---LSTEHERLLGEIVKGdPVFV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 385 YGHPVAVSPL-AKKNPEDQRFTDRFELFImtKEYGnaftEL-------NDPiDQLsrfeaQAKAKELGDDEAtgiDYD-Y 455
Cdd:cd00776 216 TDYPKEIKPFyMKPDDDNPETVESFDLLM--PGVG----EIvggsqriHDY-DEL-----EERIKEHGLDPE---SFEwY 280
|
330 340 350
....*....|....*....|....*....|....*...
gi 446024607 456 IEALEYGMPPTGGLGIGIDRLCMLLTDTTTIRDVLLFP 493
Cdd:cd00776 281 LDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
58-493 |
3.04e-25 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 109.49 E-value: 3.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 58 DKNETATIAGRLVTKRGKGKVGFAHLQDREGQIQIYVRKDAVgEENYEIFKKADLGDFLGVEGEV-----------MRTd 126
Cdd:PLN02903 70 DVGSRVTLCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDEF-PEAHRTANRLRNEYVVAVEGTVrsrpqespnkkMKT- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 127 mGELSIKATHITHLSKALRPLPEKFHGLTDV------ETIYRKRYLDLisNRESFER-FVTRSKIISEIRRYL-DQKGFL 198
Cdd:PLN02903 148 -GSVEVVAESVDILNVVTKSLPFLVTTADEQkdsikeEVRLRYRVLDL--RRPQMNAnLRLRHRVVKLIRRYLeDVHGFV 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 199 EVETPVLhNEAGGAAARPFITHHNAQNIDM-VLRIATELHLKRLIVGGMERVYEIGRIFRNEGMDATHNPEFTSIEVYQA 277
Cdd:PLN02903 225 EIETPIL-SRSTPEGARDYLVPSRVQPGTFyALPQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEFTQLDMELA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 278 YADFQDIMDLTEGIIQHAAKSVKGdgpvnyqgteIKINEPFKRVHMVDAIREITG--VDFWQDMTLKEAKAIAAE----- 350
Cdd:PLN02903 304 FTPLEDMLKLNEDLIRQVFKEIKG----------VQLPNPFPRLTYAEAMSKYGSdkPDLRYGLELVDVSDVFAEssfkv 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 351 -----------KKVPV---EKHYTEV----GHIIN----------AFF-----------------------EEFVEETLI 379
Cdd:PLN02903 374 fagalesggvvKAICVpdgKKISNNTalkkGDIYNeaiksgakglAFLkvlddgelegikalveslspeqaEQLLAACGA 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 380 QP----TFVYGHPVAVS------------------------------PLAKKNPEDQRFtdrfelfimtKEYGNAFTELN 425
Cdd:PLN02903 454 GPgdliLFAAGPTSSVNktldrlrqfiaktldlidpsrhsilwvtdfPMFEWNEDEQRL----------EALHHPFTAPN 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 426 -DPIDQLS------------------------RFEAQAKAKE---LGDDEATGiDYDYI-EALEYGMPPTGGLGIGIDRL 476
Cdd:PLN02903 524 pEDMGDLSsaralaydmvyngveigggslriyRRDVQQKVLEaigLSPEEAES-KFGYLlEALDMGAPPHGGIAYGLDRL 602
|
570
....*....|....*..
gi 446024607 477 CMLLTDTTTIRDVLLFP 493
Cdd:PLN02903 603 VMLLAGAKSIRDVIAFP 619
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
12-493 |
1.24e-23 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 103.92 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 12 QQIVRREKMAALREQGIDPFGKR--FERTANSQELKDKYANLDKEQLHDKneTATIAGRLVTKRGKGKVGFAHLQDREGQ 89
Cdd:PTZ00401 30 EEKARAAEKAALVEKYKDVFGAApmVQSTTYKSRTFIPVAVLSKPELVDK--TVLIRARVSTTRKKGKMAFMVLRDGSDS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 90 IQIYVrkdAVGEEnyeifKKADLGDFLG----------------VEGEVMRTDMGELSIKATHITHLSKALRPLP----- 148
Cdd:PTZ00401 108 VQAMA---AVEGD-----VPKEMIDFIGqiptesivdveatvckVEQPITSTSHSDIELKVKKIHTVTESLRTLPftled 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 149 ----EKFHGL-TDVETIYRKRYLDLISNrESFERFVTRSKIISEIRRYLDQKGFLEVETPVLHNEAGGAAARPFITHHNa 223
Cdd:PTZ00401 180 asrkESDEGAkVNFDTRLNSRWMDLRTP-ASGAIFRLQSRVCQYFRQFLIDSDFCEIHSPKIINAPSEGGANVFKLEYF- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 224 qNIDMVLRIATELHLKRLIVGGMERVYEIGRIFRNEGMDA-THNPEFTSIEVYQAYAD-FQDIMDLTEGIIQHAAKSVKG 301
Cdd:PTZ00401 258 -NRFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNThRHLTEFVGLDVEMRINEhYYEVLDLAESLFNYIFERLAT 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 302 DgpvNYQGTEIKINEPFKRVhmvdaireitgvdFWQdMTLKEAKAIA----AEKKVPVEK---------------HYTEV 362
Cdd:PTZ00401 337 H---TKELKAVCQQYPFEPL-------------VWK-LTPERMKELGvgviSEGVEPTDKyqarvhnmdsrmlriNYMHC 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 363 GHIINAFFEEFVEET-------------LIQPTfvYG--------HPVAVSPL-AKKNPEDQRFTDRFELFIMTKEYGNA 420
Cdd:PTZ00401 400 IELLNTVLEEKMAPTddinttnekllgkLVKER--YGtdffisdrFPSSARPFyTMECKDDERFTNSYDMFIRGEEISSG 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446024607 421 FTELNDPIDQLSRfeaqakAKELGDDeATGIDyDYIEALEYGMPPTGGLGIGIDRLCMLLTDTTTIRDVLLFP 493
Cdd:PTZ00401 478 AQRIHDPDLLLAR------AKMLNVD-LTPIK-EYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFP 542
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
1-493 |
9.13e-21 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 95.16 E-value: 9.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 1 MSTEHMEELNDQQIVRREKMAALR-EQGIDPFGKRFERTANSQE---LKDKYANLDKEQLHDK----------------- 59
Cdd:PLN02850 1 SSQEAVEESGEKISKKAAKKAAAKaEKLRREATAKAAAASLEDEddpLASNYGDVPLEELQSKvtgrewtdvsdlgeela 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 60 NETATIAGRLVTKRGKGKVGFAHLQDREGQIQ--IYVRKDAVGEENYEIFKKADLGDFLGVEGEVMR--------TDMGE 129
Cdd:PLN02850 81 GSEVLIRGRVHTIRGKGKSAFLVLRQSGFTVQcvVFVSEVTVSKGMVKYAKQLSRESVVDVEGVVSVpkkpvkgtTQQVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 130 LSIKATHIthLSKALRPLP-----------EKFHGLTDVETIYR--------KRYLDL--ISNRESFErfvTRSKIISEI 188
Cdd:PLN02850 161 IQVRKIYC--VSKALATLPfnvedaarsesEIEKALQTGEQLVRvgqdtrlnNRVLDLrtPANQAIFR---IQSQVCNLF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 189 RRYLDQKGFLEVETPVLHNEA--GGAAArpFITHHNAQniDMVLRIATELHLKRLIVGGMERVYEIGRIFRNEGmDATHN 266
Cdd:PLN02850 236 REFLLSKGFVEIHTPKLIAGAseGGSAV--FRLDYKGQ--PACLAQSPQLHKQMAICGDFRRVFEIGPVFRAED-SFTHR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 267 P--EFTSIEVYQAYAD-FQDIMDLTEGIIQHAAKSV-----KGDGPVN--YQGTEIKINEPFKRVHMVDAIREI----TG 332
Cdd:PLN02850 311 HlcEFTGLDLEMEIKEhYSEVLDVVDELFVAIFDGLnerckKELEAIReqYPFEPLKYLPKTLRLTFAEGIQMLkeagVE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 333 VDFWQDMTLKEAKAIAaekKVPVEKHYTEvghiinaFFeefveetliqptFVYGHPVAVSPL-AKKNPEDQRFTDRFELF 411
Cdd:PLN02850 391 VDPLGDLNTESERKLG---QLVKEKYGTD-------FY------------ILHRYPLAVRPFyTMPCPDDPKYSNSFDVF 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 412 IMTKEYGNAFTELNDPiDQLSRfeaqaKAKELGDDEATGidYDYIEALEYGMPPTGGLGIGIDRLCMLLTDTTTIRDVLL 491
Cdd:PLN02850 449 IRGEEIISGAQRVHDP-ELLEK-----RAEECGIDVKTI--STYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSL 520
|
..
gi 446024607 492 FP 493
Cdd:PLN02850 521 FP 522
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
56-493 |
1.78e-19 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 91.59 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 56 LHDKNETATIAGRLVTKRGKGKVGFAHLQDREGQIQIYVRKDAVGEENYEIFKKADLGDFLGVEGEVMR---------TD 126
Cdd:PRK12820 14 LDDTGREVCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFSPEAAPADVYELAASLRAEFCVALQGEVQKrleetenphIE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 127 MGELSIKATHITHLSKALR---PLPEKF-----------HGLTDVETIYRkrYLDLisNRESFER-FVTRSKIISEIRRY 191
Cdd:PRK12820 94 TGDIEVFVRELSILAASEAlpfAISDKAmtagagsagadAVNEDLRLQYR--YLDI--RRPAMQDhLAKRHRIIKCARDF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 192 LDQKGFLEVETPVLhNEAGGAAARPFITHHNAQNIDM-VLRIATELHLKRLIVGGMERVYEIGRIFRNEGMDATHNPEFT 270
Cdd:PRK12820 170 LDSRGFLEIETPIL-TKSTPEGARDYLVPSRIHPKEFyALPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEFT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 271 SIEVYQAYADFQDIMDLTEGII--------------------QHAAKSVKGDGP-------------------------- 304
Cdd:PRK12820 249 QLDIEASFIDEEFIFELIEELTarmfaiggialprpfprmpyAEAMDTTGSDRPdlrfdlkfadatdifentrygifkqi 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 305 ---------VNYQGTEIKINepfKRVHMVDAIREITGVDFWQDMTLKEAKAIAAEKKVPVEKHYTEVGHIINAFFEE--- 372
Cdd:PRK12820 329 lqrggrikgINIKGQSEKLS---KNVLQNEYAKEIAPSFGAKGMTWMRAEAGGLDSNIVQFFSADEKEALKRRFHAEdgd 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 373 -----------FVEETLIQ------------PTFVYgHPVAVSPLAKKNPEDQR--------FT--DR------------ 407
Cdd:PRK12820 406 viimiadascaIVLSALGQlrlhladrlgliPEGVF-HPLWITDFPLFEATDDGgvtsshhpFTapDRedfdpgdieell 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 408 ------FELFIMTKEYGNAFTELNDPIDQLSRFEAQAKAKELGDDEaTGIdydYIEALEYGMPPTGGLGIGIDRLCMLLT 481
Cdd:PRK12820 485 dlrsraYDLVVNGEELGGGSIRINDKDIQLRIFAALGLSEEDIEDK-FGF---FLRAFDFAAPPHGGIALGLDRVVSMIL 560
|
570
....*....|..
gi 446024607 482 DTTTIRDVLLFP 493
Cdd:PRK12820 561 QTPSIREVIAFP 572
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
64-142 |
1.29e-17 |
|
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: 77.61 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 64 TIAGRLVTKRGKGKVGFAHLQDREGQIQIYVRKDAVGEEnYEIFKKADLGDFLGVEGEVMRTD-----MGELSIKATHIT 138
Cdd:cd04100 3 TLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEELGEF-FEEAEKLRTESVVGVTGTVVKRPegnlaTGEIELQAEELE 81
|
....
gi 446024607 139 HLSK 142
Cdd:cd04100 82 VLSK 85
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
53-495 |
1.00e-16 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 82.46 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 53 KEQLHDK--NETATIAGRLVTKRGKGKVGFAHLQDREGQIQIYVRKDAvGEENYEIFKKADLGDFLGVEGEVmRTDMG-- 128
Cdd:PRK03932 7 KDILKGKyvGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDN-GEEYFEEIKKLTTGSSVIVTGTV-VESPRag 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 129 ---ELSIKATHITHLSKALRPLPEKFHGLtdvETIYRKRYLDLISNREsFERFVTRSKIISEIRRYLDQKGFLEVETPVL 205
Cdd:PRK03932 85 qgyELQATKIEVIGEDPEDYPIQKKRHSI---EFLREIAHLRPRTNKF-GAVMRIRNTLAQAIHEFFNENGFVWVDTPII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 206 HNEAGGAAARPF--ITHHNAQNIDMVLRIAT-----ELHLKRLIVgGMERVYEIGRIFRNEGMDAT-HNPEFTSIEVYQA 277
Cdd:PRK03932 161 TASDCEGAGELFrvTTLDLDFSKDFFGKEAYltvsgQLYAEAYAM-ALGKVYTFGPTFRAENSNTRrHLAEFWMIEPEMA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 278 YADFQDIMDLTEGIIQHAAKSVkgdgpVNYQGTEIKINEPFKRVHMVDAIREITGVDFWQdMTLKEAKAIAAEKKVPVEk 357
Cdd:PRK03932 240 FADLEDNMDLAEEMLKYVVKYV-----LENCPDDLEFLNRRVDKGDIERLENFIESPFPR-ITYTEAIEILQKSGKKFE- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 358 HYTEVGHIINAFFEEFVEETLIQ-PTFVYGHPVAVSPL-AKKNPED--------------------QRfTDRFELFImtk 415
Cdd:PRK03932 313 FPVEWGDDLGSEHERYLAEEHFKkPVFVTNYPKDIKAFyMRLNPDGktvaamdllapgigeiiggsQR-EERLDVLE--- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 416 eygnaftelndpidqlsrfeaqAKAKELGDDEAtgiDYD-YIEALEYGMPPTGGLGIGIDRLCMLLTDTTTIRDVLLFPT 494
Cdd:PRK03932 389 ----------------------ARIKELGLNKE---DYWwYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPR 443
|
.
gi 446024607 495 M 495
Cdd:PRK03932 444 T 444
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
180-283 |
1.12e-15 |
|
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.
Pssm-ID: 238391 [Multi-domain] Cd Length: 211 Bit Score: 76.00 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 180 TRSKIISEIRRYLDQKGFLEVETPVLHNEAGGAAAR----PFITHHNAQNIDMVLRIATELHLKRLIVG----GMERVYE 251
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGhepkDLLPVGAENEEDLYLRPTLEPGLVRLFVShirkLPLRLAE 80
|
90 100 110
....*....|....*....|....*....|....
gi 446024607 252 IGRIFRNEG--MDATHNPEFTSIEVYQAYADFQD 283
Cdd:cd00768 81 IGPAFRNEGgrRGLRRVREFTQLEGEVFGEDGEE 114
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
64-140 |
1.27e-15 |
|
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: 71.50 E-value: 1.27e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446024607 64 TIAGRLVTK-RGKGKVGFAHLQDREGQIQIYVRKdavgEENYEIFKKADLGDFLGVEGEVMRTDMGELSIKATHITHL 140
Cdd:pfam01336 2 TVAGRVTSIrRSGGKLLFLTLRDGTGSIQVVVFK----EEAEKLAKKLKEGDVVRVTGKVKKRKGGELELVVEEIELL 75
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
169-493 |
8.84e-15 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 75.44 E-value: 8.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 169 ISNRESFERFVTRSKIISEIRRYLDQKGFLEVETPVL--------HNEAGGAAARPFIthhNAQNIDMVLRIATELHlKR 240
Cdd:PRK06462 21 ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIIspstdplmGLGSDLPVKQISI---DFYGVEYYLADSMILH-KQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 241 LIVGGMERVYEIGRIFRNEGMDA---THNPEFTSIEVYQAYADFQDIMDLTEGIIQHAAKSV--KGDGPVNYQGTEI-KI 314
Cdd:PRK06462 97 LALRMLGKIFYLSPNFRLEPVDKdtgRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELleEHEDELEFFGRDLpHL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 315 NEPFKRvhmvdaireitgvdfwqdMTLKEAKAIaAEKKVPVEKHYTEvghiINAFFEEFVEETLIQPTFVYGHPVAVSPL 394
Cdd:PRK06462 177 KRPFKR------------------ITHKEAVEI-LNEEGCRGIDLEE----LGSEGEKSLSEHFEEPFWIIDIPKGSREF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 395 AKKnpEDQRFTDRFELF--IMTKEYGNAFT------ELNdpidqlsrfEAQAKAKELGDDEAtgiDYD-YIEALEYGMPP 465
Cdd:PRK06462 234 YDR--EDPERPGVLRNYdlLLPEGYGEAVSggereyEYE---------EIVERIREHGVDPE---KYKwYLEMAKEGPLP 299
|
330 340
....*....|....*....|....*...
gi 446024607 466 TGGLGIGIDRLCMLLTDTTTIRDVLLFP 493
Cdd:PRK06462 300 SAGFGIGVERLTRYICGLRHIREVQPFP 327
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
34-493 |
1.06e-12 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 70.44 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 34 RFERTANSQELKDKYANldkeqlhdknETATIAG--RLVTKRGKGKVGFAHLQDREGQIQIYVRKDAvGEENYEIFKKAD 111
Cdd:PTZ00425 65 KSEKEFNDNSRKNKYID----------QIITVCGwsKAVRKQGGGRFCFVNLNDGSCHLNLQIIVDQ-SIENYEKLLKCG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 112 LGDFLGVEGEVMRTDMG------------ELSIKATHI-------THLSKALRPLPEKFHGltdvetiyrKRYLDLISNR 172
Cdd:PTZ00425 134 VGCCFRFTGKLIISPVQnenkkgllkenvELALKDNSIhnfeiygENLDPQKYPLSKKNHG---------KEFLREVAHL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 173 ESFERFVT-----RSKIISEIRRYLDQKGFLEVETPV-----------------LHNEAGGAAARPFI------------ 218
Cdd:PTZ00425 205 RPRSYFISsviriRNALAIATHLFFQSRGFLYIHTPLittsdcegggemftvttLLGEDADYRAIPRVnkknkkgekred 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 219 ---THHNAQN--------------------ID---------MVLRIATELHLKRLiVGGMERVYEIGRIFRNEGMDAT-H 265
Cdd:PTZ00425 285 ilnTCNANNNngnssssnavsspaypdqylIDykkdffskqAFLTVSGQLSLENL-CSSMGDVYTFGPTFRAENSHTSrH 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 266 NPEFTSIEVYQAYADFQDIMDLTEGIIQHAAKSVkgdgpVNYQGTEIKINEPFKRVHMVDAIREITGVDFWQdMTLKEAK 345
Cdd:PTZ00425 364 LAEFWMIEPEIAFADLYDNMELAESYIKYCIGYV-----LNNNFDDIYYFEENVETGLISRLKNILDEDFAK-ITYTNVI 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 346 AI----AAEKKVPVEkhyteVGHIINAFFEEFVEETLIQ-PTFVYGHPVAVSPLAKKNPEDQRFTDRFELFI--MTKEYG 418
Cdd:PTZ00425 438 DLlqpySDSFEVPVK-----WGMDLQSEHERFVAEQIFKkPVIVYNYPKDLKAFYMKLNEDQKTVAAMDVLVpkIGEVIG 512
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446024607 419 NAFTElndpiDQLSRFEAQAKAKELGDDEAtgidYDYIEALEYGMPPTGGLGIGIDRLCMLLTDTTTIRDVLLFP 493
Cdd:PTZ00425 513 GSQRE-----DNLERLDKMIKEKKLNMESY----WWYRQLRKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFP 578
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
58-168 |
3.72e-08 |
|
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: 52.14 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 58 DKNETATIAGRLVTKRGKGKVGFAHLQDREGQIQIYVRkdavgEENYEIFKKAD---LGDFLGVEGEV-----------M 123
Cdd:cd04317 12 HVGQEVTLCGWVQRRRDHGGLIFIDLRDRYGIVQVVFD-----PEEAPEFELAEklrNESVIQVTGKVrarpegtvnpkL 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 446024607 124 RTdmGELSIKATHITHLSKAlRPLPekF----HGLTDVETIYRKRYLDL 168
Cdd:cd04317 87 PT--GEIEVVASELEVLNKA-KTLP--FeiddDVNVSEELRLKYRYLDL 130
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
61-148 |
7.93e-08 |
|
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: 50.39 E-value: 7.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 61 ETATIAGRLVTKRGKGKVGFAHLQDREGQIQIYVRKDAVGEENYEIFKKADLGDFLGVEGEVMRTDM--GELSIKATHIT 138
Cdd:cd04316 13 EEVTVAGWVHEIRDLGGIKFVILRDREGIVQVTAPKKKVDKELFKTVRKLSRESVISVTGTVKAEPKapNGVEIIPEEIE 92
|
90
....*....|
gi 446024607 139 HLSKALRPLP 148
Cdd:cd04316 93 VLSEAKTPLP 102
|
|
| pheS |
TIGR00468 |
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ... |
183-273 |
3.90e-06 |
|
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are heterodimeric, with 2 alpha (pheS) and 2 beta (pheT) subunits. This model describes the alpha subunit, which shows some similarity to class II aminoacyl-tRNA ligases. Mitochondrial phenylalanyl-tRNA synthetase is a single polypeptide chain, active as a monomer, and similar to this chain rather than to the beta chain, but excluded from this model. An interesting feature of the alignment of all sequences captured by this model is a deep split between non-spirochete bacterial examples and all other examples; supporting this split is a relative deletion of about 50 residues in the former set between two motifs well conserved throughout the alignment. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273095 [Multi-domain] Cd Length: 293 Bit Score: 48.46 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 183 KIISEIRRYLDQKGFLEVETPVLHNEAGGAAARPFITHHNAQNI--------DMVLRI---ATELHLKRLIVGGMERVYE 251
Cdd:TIGR00468 76 RVIDEIRDIFLGLGFTEETGPEVETDFWNFDALNIPQDHPARDMqdtfyikdRLLLRThttAVQLRTMEEQEKPPIRIFS 155
|
90 100
....*....|....*....|..
gi 446024607 252 IGRIFRNEGMDATHNPEFTSIE 273
Cdd:TIGR00468 156 PGRVFRNDTVDATHLPEFHQVE 177
|
|
| PheRS_alpha_core |
cd00496 |
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ... |
182-273 |
5.10e-04 |
|
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure and the presence of three characteristic sequence motifs. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. While class II aaRSs generally aminoacylate the 3'-OH 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. PheRS is an alpha-2/ beta-2 tetramer.
Pssm-ID: 238277 [Multi-domain] Cd Length: 218 Bit Score: 41.38 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446024607 182 SKIISEIRRYLDQKGFLEVETPVLHNEAGGAAARPFITHHNAQNI----------DMVLRIATELHLKRLIVGGME--RV 249
Cdd:cd00496 4 NKVIEEIEDIFVSMGFTEVEGPEVETDFYNFDALNIPQDHPARDMqdtfyindpaRLLLRTHTSAVQARALAKLKPpiRI 83
|
90 100
....*....|....*....|....
gi 446024607 250 YEIGRIFRNEGMDATHNPEFTSIE 273
Cdd:cd00496 84 FSIGRVYRNDEIDATHLPEFHQIE 107
|
|
| PTZ00326 |
PTZ00326 |
phenylalanyl-tRNA synthetase alpha chain; Provisional |
219-273 |
1.69e-03 |
|
phenylalanyl-tRNA synthetase alpha chain; Provisional
Pssm-ID: 240361 [Multi-domain] Cd Length: 494 Bit Score: 40.72 E-value: 1.69e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 446024607 219 THHNAQNIDMVLRIATELHLKRLIVGGmeRVYEIGRIFRNEGMDATHNPEFTSIE 273
Cdd:PTZ00326 332 THTTAVSARMLYKLAQEYKKTGPFKPK--KYFSIDRVFRNETLDATHLAEFHQVE 384
|
|
| PLN02853 |
PLN02853 |
Probable phenylalanyl-tRNA synthetase alpha chain |
248-273 |
2.30e-03 |
|
Probable phenylalanyl-tRNA synthetase alpha chain
Pssm-ID: 215458 [Multi-domain] Cd Length: 492 Bit Score: 40.43 E-value: 2.30e-03
10 20
....*....|....*....|....*.
gi 446024607 248 RVYEIGRIFRNEGMDATHNPEFTSIE 273
Cdd:PLN02853 344 RYFSIDRVFRNEAVDRTHLAEFHQVE 369
|
|
| tRNA-synt_2d |
pfam01409 |
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ... |
248-273 |
4.39e-03 |
|
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only phenylalanyl-tRNA synthetases. This is the core catalytic domain.
Pssm-ID: 396130 [Multi-domain] Cd Length: 245 Bit Score: 38.72 E-value: 4.39e-03
10 20
....*....|....*....|....*.
gi 446024607 248 RVYEIGRIFRNEGMDATHNPEFTSIE 273
Cdd:pfam01409 104 KIFSIGRVFRRDQVDATHLPEFHQVE 129
|
|
| |
