|
Name |
Accession |
Description |
Interval |
E-value |
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
10-498 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 938.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 10 EDLNDQMLVRREKMENLREEGIDPFGKRFDRTHNSKELHDQFDQHSKEELNEMDLSASVAGRMMTKRGKGKAGFAHLQDR 89
Cdd:PRK00484 1 EELNEQIAVRREKLAELREQGIDPYPNKFERTHTAAELRAKYDDKEKEELEELEIEVSVAGRVMLKRVMGKASFATLQDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 90 EGQLQIYVRKDQVGDEAYEVFKHADLGDFFGVTGQIMKTDTGEVTVKAKTIVLLTKALRPLPDKYHGLTNIEQRYRQRYL 169
Cdd:PRK00484 81 SGRIQLYVSKDDVGEEALEAFKKLDLGDIIGVEGTLFKTKTGELSVKATELTLLTKSLRPLPDKFHGLTDVETRYRQRYV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 170 DLISNKDSFDRFMKRSQIISEIRRYLDGHGYVEVETPVLHNDAGGAAARPFITHHNALDMDLYLRIALELHLKRLIVGGM 249
Cdd:PRK00484 161 DLIVNPESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARPFITHHNALDIDLYLRIAPELYLKRLIVGGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 250 EKVYEIGRVFRNEGIDTTHNPEFTMLEAYTAYTDYKDVMDLTEGIIRNAADKVLGTTTITYDGQEVDLGSEFRRVHMVDA 329
Cdd:PRK00484 241 ERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTYQGTEIDFGPPFKRLTMVDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 330 IKEQTGVDFWkEMTVEEARTFAKEHNVEINNNMSVGHILNEFFETFVEETLKQPTFVYGHPVEVSPLAKKNPEDDRFTDR 409
Cdd:PRK00484 321 IKEYTGVDFD-DMTDEEARALAKELGIEVEKSWGLGKLINELFEEFVEPKLIQPTFITDYPVEISPLAKRHREDPGLTER 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 410 FELFIVGKEFANAFTELNDPIDQRERFEDQEKEREQGNDEAHGVDEDFIEALEYGLPPTGGLGIGIDRLVMLLTDAQSIR 489
Cdd:PRK00484 400 FELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIR 479
|
....*....
gi 486874386 490 DVLLFPTMR 498
Cdd:PRK00484 480 DVILFPLMR 488
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
1-498 |
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: 928.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 1 MADEQqahleDLNDQMLVRREKMENLREEGIDPFGKRFDRTHNSKELHDQFDQHSKEElnEMDLSASVAGRMMTKRGKGK 80
Cdd:COG1190 1 MSEEE-----DLNEQIRVRREKLEELREAGIDPYPNKFPRTHTAAEIREKYDELEAEE--ETGDEVSVAGRIMAKRDMGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 81 AGFAHLQDREGQLQIYVRKDQVGDEAYEVFKHADLGDFFGVTGQIMKTDTGEVTVKAKTIVLLTKALRPLPDKYHGLTNI 160
Cdd:COG1190 74 ASFADLQDGSGRIQLYLRRDELGEEAYELFKLLDLGDIVGVEGTVFRTKTGELSVKVEELTLLSKSLRPLPEKFHGLTDP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 161 EQRYRQRYLDLISNKDSFDRFMKRSQIISEIRRYLDGHGYVEVETPVLHNDAGGAAARPFITHHNALDMDLYLRIALELH 240
Cdd:COG1190 154 ETRYRQRYVDLIVNPEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 241 LKRLIVGGMEKVYEIGRVFRNEGIDTTHNPEFTMLEAYTAYTDYKDVMDLTEGIIRNAADKVLGTTTITYDGQEVDLGSE 320
Cdd:COG1190 234 LKRLIVGGFERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGTTKVTYQGQEIDLSPP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 321 FRRVHMVDAIKEQTGVDFWKEMTVEEARTFAKEHNVEINNNMSVGHILNEFFETFVEETLKQPTFVYGHPVEVSPLAKKN 400
Cdd:COG1190 314 WRRITMVEAIKEATGIDVTPLTDDEELRALAKELGIEVDPGWGRGKLIDELFEELVEPKLIQPTFVTDYPVEVSPLAKRH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 401 PEDDRFTDRFELFIVGKEFANAFTELNDPIDQRERFEDQEKEREQGNDEAHGVDEDFIEALEYGLPPTGGLGIGIDRLVM 480
Cdd:COG1190 394 RDDPGLTERFELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGLGIGIDRLVM 473
|
490
....*....|....*...
gi 486874386 481 LLTDAQSIRDVLLFPTMR 498
Cdd:COG1190 474 LLTDSPSIRDVILFPLMR 491
|
|
| lysS_bact |
TIGR00499 |
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ... |
11-498 |
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: 725.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 11 DLNDQMLVRREKMENLREEGIDPFGKRFDRTHNSKELHDQFDQHSKEELNEMDLSASVAGRMMTKRGKGKAGFAHLQDRE 90
Cdd:TIGR00499 1 ELNDQAQQRLEKLNRLRQTGNNPYLHKFERTHSAQEFQEKYADLSNEELKEKELKVSIAGRIKAIRSMGKATFITLQDES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 91 GQLQIYVRKDQVGDEAYEVFKH-ADLGDFFGVTGQIMKTDTGEVTVKAKTIVLLTKALRPLPDKYHGLTNIEQRYRQRYL 169
Cdd:TIGR00499 81 GQIQLYVNKNKLPEDFYEFDEYlLDLGDIIGVTGYPFKTKTGELSVKVTELQILTKCLQPLPDKWHGLTDQETRYRQRYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 170 DLISNKDSFDRFMKRSQIISEIRRYLDGHGYVEVETPVLHNDAGGAAARPFITHHNALDMDLYLRIALELHLKRLIVGGM 249
Cdd:TIGR00499 161 DLIVNPDVRQTFLKRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKPFITHHNALDMDLYLRIAPELYLKRLIVGGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 250 EKVYEIGRVFRNEGIDTTHNPEFTMLEAYTAYTDYKDVMDLTEGIIRNAADKVLGTTTITYDGQEVDLGSEFRRVHMVDA 329
Cdd:TIGR00499 241 EKVYEIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTFIINYNDLEIDLKPPWKRITMVDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 330 IKEQTGVDFWKEMTVEEARTFAKEHNVEI-NNNMSVGHILNEFFETFVEETLKQPTFVYGHPVEVSPLAKKNPEDDRFTD 408
Cdd:TIGR00499 321 LEMVTGIDFDILKDDETAKALAKEHGIEVaEDSLTLGHILNKFFEQFLEHTLIQPTFITHYPAEISPLAKRDPSNPEFTE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 409 RFELFIVGKEFANAFTELNDPIDQRERFEDQEKEREQGNDEAHGVDEDFIEALEYGLPPTGGLGIGIDRLVMLLTDAQSI 488
Cdd:TIGR00499 401 RFELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGIGIDRLVMLLTDAPSI 480
|
490
....*....|
gi 486874386 489 RDVLLFPTMR 498
Cdd:TIGR00499 481 RDVLLFPQLR 490
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
18-498 |
0e+00 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 650.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 18 VRREKMENLREEGIDPFGKRFDRTHNSKELHDQFDQHSKEELNEmDLSASVAGRMMTKRGKGKAGFAHLQDREGQLQIYV 97
Cdd:PLN02502 64 NRLKKVEALRAKGVEPYPYKFDVTHTAPELQEKYGSLENGEELE-DVSVSVAGRIMAKRAFGKLAFYDLRDDGGKIQLYA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 98 RKDQVGDEAYEVFK-HA--DLGDFFGVTGQIMKTDTGEVTVKAKTIVLLTKALRPLPDKYHGLTNIEQRYRQRYLDLISN 174
Cdd:PLN02502 143 DKKRLDLDEEEFEKlHSlvDRGDIVGVTGTPGKTKKGELSIFPTSFEVLTKCLLMLPDKYHGLTDQETRYRQRYLDLIAN 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 175 KDSFDRFMKRSQIISEIRRYLDGHGYVEVETPVLHNDAGGAAARPFITHHNALDMDLYLRIALELHLKRLIVGGMEKVYE 254
Cdd:PLN02502 223 PEVRDIFRTRAKIISYIRRFLDDRGFLEVETPMLNMIAGGAAARPFVTHHNDLNMDLYLRIATELHLKRLVVGGFERVYE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 255 IGRVFRNEGIDTTHNPEFTMLEAYTAYTDYKDVMDLTEGIIRNAADKVLGTTTITYDGQEVDLGSEFRRVHMVDAIKEQT 334
Cdd:PLN02502 303 IGRQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKELTGSYKIKYHGIEIDFTPPFRRISMISLVEEAT 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 335 GVDFWKEMTVEEARTFAKE----HNVEINNNMSVGHILNEFFETFVEETLKQPTFVYGHPVEVSPLAKKNPEDDRFTDRF 410
Cdd:PLN02502 383 GIDFPADLKSDEANAYLIAacekFDVKCPPPQTTGRLLNELFEEFLEETLVQPTFVLDHPVEMSPLAKPHRSKPGLTERF 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 411 ELFIVGKEFANAFTELNDPIDQRERFEDQEKEREQGNDEAHGVDEDFIEALEYGLPPTGGLGIGIDRLVMLLTDAQSIRD 490
Cdd:PLN02502 463 ELFINGRELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRLVMLLTDSASIRD 542
|
....*...
gi 486874386 491 VLLFPTMR 498
Cdd:PLN02502 543 VIAFPAMK 550
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
174-498 |
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: 559.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 174 NKDSFDRFMKRSQIISEIRRYLDGHGYVEVETPVLHNDAGGAAARPFITHHNALDMDLYLRIALELHLKRLIVGGMEKVY 253
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 254 EIGRVFRNEGIDTTHNPEFTMLEAYTAYTDYKDVMDLTEGIIRNAADKVLGTTTITYDGQEVDLGSEFRRVHMVDAIKEQ 333
Cdd:cd00775 81 EIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIEYGGKELDFTPPFKRVTMVDALKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 334 TGVDFWK---EMTVEEARTFAKEHNVEINNNMSVGHILNEFFETFVEETLKQPTFVYGHPVEVSPLAKKNPEDDRFTDRF 410
Cdd:cd00775 161 TGIDFPEldlEQPEELAKLLAKLIKEKIEKPRTLGKLLDKLFEEFVEPTLIQPTFIIDHPVEISPLAKRHRSNPGLTERF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 411 ELFIVGKEFANAFTELNDPIDQRERFEDQEKEREQGNDEAHGVDEDFIEALEYGLPPTGGLGIGIDRLVMLLTDAQSIRD 490
Cdd:cd00775 241 ELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLTDSNSIRD 320
|
....*...
gi 486874386 491 VLLFPTMR 498
Cdd:cd00775 321 VILFPAMR 328
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
12-495 |
1.00e-174 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 520.29 E-value: 1.00e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 12 LNDQMLVRREKMENLREEGIDPFGKRFDRTHnskELHDQFDQHSKEELnemdlsaSVAGRMMTKRGKGKAGFAHLQDREG 91
Cdd:PRK02983 610 LPEQVRVRLAKLEALRAAGVDPYPVGVPPTH---TVAEALDAPTGEEV-------SVSGRVLRIRDYGGVLFADLRDWSG 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 92 QLQIYVRKDQVGDEAYEVFKHA-DLGDFFGVTGQIMKTDTGEVTVKAKTIVLLTKALRPLPDKYHGLTNIEQRYRQRYLD 170
Cdd:PRK02983 680 ELQVLLDASRLEQGSLADFRAAvDLGDLVEVTGTMGTSRNGTLSLLVTSWRLAGKCLRPLPDKWKGLTDPEARVRQRYLD 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 171 LISNKDSFDRFMKRSQIISEIRRYLDGHGYVEVETPVLHNDAGGAAARPFITHHNALDMDLYLRIALELHLKRLIVGGME 250
Cdd:PRK02983 760 LAVNPEARDLLRARSAVVRAVRETLVARGFLEVETPILQQVHGGANARPFVTHINAYDMDLYLRIAPELYLKRLCVGGVE 839
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 251 KVYEIGRVFRNEGIDTTHNPEFTMLEAYTAYTDYKDVMDLTEGIIRNAADKVLGTTTITYDG-----QEVDLGSEFRRVH 325
Cdd:PRK02983 840 RVFELGRNFRNEGVDATHNPEFTLLEAYQAHADYDTMRDLTRELIQNAAQAAHGAPVVMRPDgdgvlEPVDISGPWPVVT 919
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 326 MVDAIKEQTGVDFWKEMTVEEARTFAKEHNVEINNNMSVGHILNEFFETFVEETLKQPTFVYGHPVEVSPLAKKNPEDDR 405
Cdd:PRK02983 920 VHDAVSEALGEEIDPDTPLAELRKLCDAAGIPYRTDWDAGAVVLELYEHLVEDRTTFPTFYTDFPTSVSPLTRPHRSDPG 999
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 406 FTDRFELFIVGKEFANAFTELNDPIDQRERFEDQEKEREQGNDEAHGVDEDFIEALEYGLPPTGGLGIGIDRLVMLLTdA 485
Cdd:PRK02983 1000 LAERWDLVAWGVELGTAYSELTDPVEQRRRLTEQSLLAAGGDPEAMELDEDFLQALEYAMPPTGGLGMGVDRLVMLLT-G 1078
|
490
....*....|
gi 486874386 486 QSIRDVLLFP 495
Cdd:PRK02983 1079 RSIRETLPFP 1088
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
11-498 |
2.90e-170 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 489.57 E-value: 2.90e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 11 DLNDQMLVRREKMENLREEGIdPFGKRFDRTHNSKELHDQFDQHSKEELNEMDLSASVAGRMMTKRGKGKAGFAHLQDRE 90
Cdd:PRK12445 14 DFNDELRNRREKLAALRQQGV-AFPNDFRRDHTSDQLHEEFDAKDNQELESLNIEVSVAGRMMTRRIMGKASFVTLQDVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 91 GQLQIYVRKDQVGDEAY-EVFKHADLGDFFGVTGQIMKTDTGEVTVKAKTIVLLTKALRPLPDKYHGLTNIEQRYRQRYL 169
Cdd:PRK12445 93 GRIQLYVARDSLPEGVYnDQFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFHGLQDQEVRYRQRYL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 170 DLISNKDSFDRFMKRSQIISEIRRYLDGHGYVEVETPVLHNDAGGAAARPFITHHNALDMDLYLRIALELHLKRLIVGGM 249
Cdd:PRK12445 173 DLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 250 EKVYEIGRVFRNEGIDTTHNPEFTMLEAYTAYTDYKDVMDLTEGIIRNAADKVLGTTTITYDGQEVDLGSEFRRVHMVDA 329
Cdd:PRK12445 253 ERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFDFGKPFEKLTMREA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 330 IKE-QTGVDFWKEMTVEEARTFAKEHNVEINNNMSVGHILNEFFETFVEETLKQPTFVYGHPVEVSPLAKKNPEDDRFTD 408
Cdd:PRK12445 333 IKKyRPETDMADLDNFDAAKALAESIGITVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEITD 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 409 RFELFIVGKEFANAFTELNDPIDQRERFEDQEKEREQGNDEAHGVDEDFIEALEYGLPPTGGLGIGIDRLVMLLTDAQSI 488
Cdd:PRK12445 413 RFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTI 492
|
490
....*....|
gi 486874386 489 RDVLLFPTMR 498
Cdd:PRK12445 493 RDVILFPAMR 502
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
19-498 |
7.91e-134 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 399.38 E-value: 7.91e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 19 RREKMENLREEGIDPFGKRFDRTHNSKELHDQF-DQHSKEELNEMDLSasVAGRMMTKRGKG-KAGFAHLQDREGQLQI- 95
Cdd:PTZ00417 89 RSKFIQEQKAKGINPYPHKFERTITVPEFVEKYqDLASGEHLEDTILN--VTGRIMRVSASGqKLRFFDLVGDGAKIQVl 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 96 --YVRKDQVGDEAYEVFKHADLGDFFGVTGQIMKTDTGEVTVKAKTIVLLTKALRPLPDKYhGLTNIEQRYRQRYLDLIS 173
Cdd:PTZ00417 167 anFAFHDHTKSNFAECYDKIRRGDIVGIVGFPGKSKKGELSIFPKETIILSPCLHMLPMKY-GLKDTEIRYRQRYLDLMI 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 174 NKDSFDRFMKRSQIISEIRRYLDGHGYVEVETPVLHNDAGGAAARPFITHHNALDMDLYLRIALELHLKRLIVGGMEKVY 253
Cdd:PTZ00417 246 NESTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLVAGGANARPFITHHNDLDLDLYLRIATELPLKMLIVGGIDKVY 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 254 EIGRVFRNEGIDTTHNPEFTMLEAYTAYTDYKDVMDLTEGIIRNAADKVLGTTTITY--DGQ-----EVDLGSEFRRVHM 326
Cdd:PTZ00417 326 EIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHLFGTYKILYnkDGPekdpiEIDFTPPYPKVSI 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 327 VDAIKEQTGVD----FWKEMTVEEARTFAKEHNVEINNNMSVGHILNEFFETFVEETL-KQPTFVYGHPVEVSPLAKKNP 401
Cdd:PTZ00417 406 VEELEKLTNTKleqpFDSPETINKMINLIKENKIEMPNPPTAAKLLDQLASHFIENKYpNKPFFIIEHPQIMSPLAKYHR 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 402 EDDRFTDRFELFIVGKEFANAFTELNDPIDQRERFEDQEKEREQGNDEAHGVDEDFIEALEYGLPPTGGLGIGIDRLVML 481
Cdd:PTZ00417 486 SKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCTSLEYGLPPTGGLGLGIDRITMF 565
|
490
....*....|....*..
gi 486874386 482 LTDAQSIRDVLLFPTMR 498
Cdd:PTZ00417 566 LTNKNCIKDVILFPTMR 582
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
159-498 |
4.49e-121 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 357.26 E-value: 4.49e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 159 NIEQRYRQRYLDLiSNKDSFDRFMKRSQIISEIRRYLDGHGYVEVETPVLHNDAGGAAARPFITHHNALDMDLYLRIALE 238
Cdd:pfam00152 1 DEETRLKYRYLDL-RRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 239 LHLKRLIVGGMEKVYEIGRVFRNEGIDTTHNPEFTMLEAYTAYTDYKDVMDLTEGIIRNAADKVLGTTTITYDGQEVDLG 318
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 319 SEFRRVHMVDAIKEQTGVDF--WKEMTVEEARTFAKEHNVEINNNmsvghilneffetfveetlkQPTFVYGHPVEVSPL 396
Cdd:pfam00152 160 KPFPRITYAEAIEKLNGKDVeeLGYGSDKPDLRFLLELVIDKNKF--------------------NPLWVTDFPAEHHPF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 397 AKKNPEDD-RFTDRFELFIVGKEFANAFTELNDPIDQRERFEDQEKEREqgndEAHGVDEDFIEALEYGLPPTGGLGIGI 475
Cdd:pfam00152 220 TMPKDEDDpALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDPE----EAEEKFGFYLDALKYGAPPHGGLGIGL 295
|
330 340
....*....|....*....|...
gi 486874386 476 DRLVMLLTDAQSIRDVLLFPTMR 498
Cdd:pfam00152 296 DRLVMLLTGLESIREVIAFPKTR 318
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
61-498 |
9.45e-119 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 363.20 E-value: 9.45e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 61 EMDLSASVAGRMMTKRGKGKAGFAHLQDREGQLQIYVrkdQVGdeayEVFKHADL---------GDFFGVTGQIMKTDTG 131
Cdd:PTZ00385 105 AAQATVRVAGRVTSVRDIGKIIFVTIRSNGNELQVVG---QVG----EHFTREDLkklkvslrvGDIIGADGVPCRMQRG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 132 EVTVKAKTIVLLT------KALRPLPDKYHGLTNIEQRYRQRYLDLISNKDSFDRFMKRSQIISEIRRYLDGHGYVEVET 205
Cdd:PTZ00385 178 ELSVAASRMLILSpyvctdQVVCPNLRGFTVLQDNDVKYRYRFTDMMTNPCVIETIKKRHVMLQALRDYFNERNFVEVET 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 206 PVLHNDAGGAAARPFITHHNALDMDLYLRIALELHLKRLIVGGMEKVYEIGRVFRNEGIDTTHNPEFTMLEAYTAYTDYK 285
Cdd:PTZ00385 258 PVLHTVASGANAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTSCEFYAAYHTYE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 286 DVMDLTEGIIRNAADKVLGTTTITYDGQ-------EVDLGSEFRRVHMVDAIKEQTGVDFWKEMTVEEARTFAK------ 352
Cdd:PTZ00385 338 DLMPMTEDIFRQLAMRVNGTTVVQIYPEnahgnpvTVDLGKPFRRVSVYDEIQRMSGVEFPPPNELNTPKGIAYmsvvml 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 353 EHNVEINNNMSVGHILNEFFETFVEETLKQPTFVYGHPVEVSPLAKKNPEDDRFTDRFELFIVGKEFANAFTELNDPIDQ 432
Cdd:PTZ00385 418 RYNIPLPPVRTAAKMFEKLIDFFITDRVVEPTFVMDHPLFMSPLAKEQVSRPGLAERFELFVNGIEYCNAYSELNDPHEQ 497
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 486874386 433 RERFEDQEKEREQGNDEAHGVDEDFIEALEYGLPPTGGLGIGIDRLVMLLTDAQSIRDVLLFPTMR 498
Cdd:PTZ00385 498 YHRFQQQLVDRQGGDEEAMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFPLLR 563
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
181-498 |
9.22e-99 |
|
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: 298.62 E-value: 9.22e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 181 FMKRSQIISEIRRYLDGHGYVEVETPVLHNDAGGAAARPFITHHNALDMDLYLRIALELHLKRLIVGGMEKVYEIGRVFR 260
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 261 NEGIDTTHNPEFTMLEAYTAYTDYKDVMDLTEGIIRNAADKVLGTTTITYDGQEVDLGSEFRRVHMVDAIkeqtgvdfwk 340
Cdd:cd00669 81 NEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYGFELEDFGLPFPRLTYREAL---------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 341 emtveeartfakehnveinnnmsvghilneffetfveETLKQPTFVYGHPVE-VSPLAKKNPEDDRFTDRFELFIVGKEF 419
Cdd:cd00669 151 -------------------------------------ERYGQPLFLTDYPAEmHSPLASPHDVNPEIADAFDLFINGVEV 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 420 ANAFTELNDPIDQRERFedqekeREQGNDEAHGV--DEDFIEALEYGLPPTGGLGIGIDRLVMLLTDAQSIRDVLLFPTM 497
Cdd:cd00669 194 GNGSSRLHDPDIQAEVF------QEQGINKEAGMeyFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKM 267
|
.
gi 486874386 498 R 498
Cdd:cd00669 268 R 268
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
176-492 |
1.74e-82 |
|
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: 258.11 E-value: 1.74e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 176 DSFDRFMKRSQIISEIRRYLDGHGYVEVETPVLHNDAGGAAA-RPFIT---HHNALDMDLYLRIALELHLKRLIVGGMEK 251
Cdd:COG2269 1 ASREALRARARLLAAIRAFFAERGVLEVETPALSVAPGTDPHlDSFATefiGPDGGGRPLYLHTSPEFAMKRLLAAGSGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 252 VYEIGRVFRNEGIDTTHNPEFTMLEAYTAYTDYKDVMDLTEGIIRNAADKVLGTttitydgqevdlgsEFRRVHMVDAIK 331
Cdd:COG2269 81 IYQIAKVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAAGFA--------------PAERLSYQEAFL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 332 EQTGVDFWkEMTVEEARTFAKEHNVEINNNMSVGHILNEFFETFVEETLKQ--PTFVYGHPVEVSPLAKKNPEDDRFTDR 409
Cdd:COG2269 147 RYLGIDPL-TADLDELAAAAAAAGLRVADDDDRDDLLDLLLSERVEPQLGRdrPTFLYDYPASQAALARISPDDPRVAER 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 410 FELFIVGKEFANAFTELNDPIDQRERFEDQEKEREQGNDEAHGVDEDFIEALEYGLPPTGGLGIGIDRLVMLLTDAQSIR 489
Cdd:COG2269 226 FELYACGVELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALGAERID 305
|
...
gi 486874386 490 DVL 492
Cdd:COG2269 306 DVL 308
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
194-492 |
2.00e-71 |
|
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: 228.59 E-value: 2.00e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 194 YLDGHGYVEVETPVLhNDAGGAAA--RPFITH---HNALDMDLYLRIALELHLKRLIVGGMEKVYEIGRVFRNEGIDTTH 268
Cdd:TIGR00462 1 FFAERGVLEVETPLL-SPAPVTDPhlDAFATEfvgPDGQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 269 NPEFTMLEAYTAYTDYKDVMDLTEGIIRNAADkvlgtttitydgqevDLGSEFRRVHMVDAIKEQTGVDFWKEmTVEEAR 348
Cdd:TIGR00462 80 NPEFTMLEWYRPGFDYHDLMDEVEALLQELLG---------------DPFAPAERLSYQEAFLRYAGIDPLTA-SLAELQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 349 TFAKEHNVEINNNMSVGHILNEFFETFVEETLKQ--PTFVYGHPVEVSPLAKKNPEDDRFTDRFELFIVGKEFANAFTEL 426
Cdd:TIGR00462 144 AAAAAHGIRASEEDDRDDLLDLLFSEKVEPHLGFgrPTFLYDYPASQAALARISPDDPRVAERFELYIKGLELANGFHEL 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 486874386 427 NDPIDQRERFEDQEKEREQGNDEAHGVDEDFIEALEYGLPPTGGLGIGIDRLVMLLTDAQSIRDVL 492
Cdd:TIGR00462 224 TDAAEQRRRFEADNALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDVL 289
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
181-491 |
1.35e-61 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 203.62 E-value: 1.35e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 181 FMKRSQIISEIRRYLDGHGYVEVETPVLhNDAGGAAAR--PFITHHNALD----MDLYLRIALELHLKRLIVGGMEKVYE 254
Cdd:PRK09350 5 LLKRAKIIAEIRRFFADRGVLEVETPIL-SQATVTDIHlvPFETRFVGPGasqgKTLWLMTSPEYHMKRLLAAGSGPIFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 255 IGRVFRNEGIDTTHNPEFTMLEAYTAYTDYKDVMDLTEGIIRNAADkVLGTTTITYdgQEVdlgseFRRVHMVDAIKEQt 334
Cdd:PRK09350 84 ICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLD-CEPAESLSY--QQA-----FLRYLGIDPLSAD- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 335 gvdfwKEMTVEEARTFAKEHNVEINNNMSVghILNEFFETFVEETLKQ--PTFVYGHPVEVSPLAKKNPEDDRFTDRFEL 412
Cdd:PRK09350 155 -----KTQLREVAAKLGLSNIADEEEDRDT--LLQLLFTFGVEPNIGKekPTFVYHFPASQAALAKISTEDHRVAERFEV 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 486874386 413 FIVGKEFANAFTELNDPIDQRERFEDQEKEREQGNDEAHGVDEDFIEALEYGLPPTGGLGIGIDRLVMLLTDAQSIRDV 491
Cdd:PRK09350 228 YFKGIELANGFHELTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCSGVALGVDRLIMLALGAESISEV 306
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
67-171 |
7.70e-54 |
|
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: 176.51 E-value: 7.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 67 SVAGRMMTKRGKGKAGFAHLQDREGQLQIYVRKDQVGDEAYEVFKHA-DLGDFFGVTGQIMKTDTGEVTVKAKTIVLLTK 145
Cdd:cd04322 3 SVAGRIMSKRGSGKLSFADLQDESGKIQVYVNKDDLGEEEFEDFKKLlDLGDIIGVTGTPFKTKTGELSIFVKEFTLLSK 82
|
90 100
....*....|....*....|....*.
gi 486874386 146 ALRPLPDKYHGLTNIEQRYRQRYLDL 171
Cdd:cd04322 83 SLRPLPEKFHGLTDVETRYRQRYLDL 108
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
68-498 |
3.42e-43 |
|
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: 158.29 E-value: 3.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 68 VAGRMMTKRGKGKAGFAHLQDREGQLQIYVRKDQVgdEAYEVFKHADLGDFFGVTGQIMKTDT--GEVTVKAKTIVLLTK 145
Cdd:COG0017 19 VAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKL--ENFEEAKKLTTESSVEVTGTVVESPRapQGVELQAEEIEVLGE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 146 ALRPLP-DKY-HGLtniEQRYRQRYLDLISNKdsFDRFMK-RSQIISEIRRYLDGHGYVEVETPVL-HNDAGGAAarpfi 221
Cdd:COG0017 97 ADEPYPlQPKrHSL---EFLLDNRHLRLRTNR--FGAIFRiRSELARAIREFFQERGFVEVHTPIItASATEGGG----- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 222 thhnalDM---D-------------LYLRIAlelhlkrliVGGMEKVYEIGRVFRNEGIDTT-HNPEFTMLEAYTAYTDY 284
Cdd:COG0017 167 ------ELfpvDyfgkeayltqsgqLYKEAL---------AMALEKVYTFGPTFRAEKSNTRrHLAEFWMIEPEMAFADL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 285 KDVMDLTEGIIRNAADKV-------LGTTTITYDGQEVDLGSEFRRVHMVDAIK--EQTGVDF-WKEmtveearTFAKEH 354
Cdd:COG0017 232 EDVMDLAEEMLKYIIKYVlencpeeLEFLGRDVERLEKVPESPFPRITYTEAIEilKKSGEKVeWGD-------DLGTEH 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 355 nveinnnmsvghilneffETF-VEETLKQPTFVYGHPVEVSPL-AKKNPEDDRFTDRFELF------IVGkefanaftel 426
Cdd:COG0017 305 ------------------ERYlGEEFFKKPVFVTDYPKEIKAFyMKPNPDDPKTVAAFDLLapgigeIIG---------- 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 486874386 427 ndpIDQRE-RFEDQEKE-REQGNDEahgvdEDF---IEALEYGLPPTGGLGIGIDRLVMLLTDAQSIRDVLLFPTMR 498
Cdd:COG0017 357 ---GSQREhRYDVLVERiKEKGLDP-----EDYewyLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDP 425
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
54-495 |
1.01e-37 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 143.41 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 54 HSKEELNEMDLS-ASVAGRMMTKRGKGKAGFAHLQDREGQLQIYVRKDQVgDEAYEVFKHADLGDFFGVTGQIMKTDT-- 130
Cdd:PRK05159 6 LTSELTPELDGEeVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKVD-EELFETIKKLKRESVVSVTGTVKANPKap 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 131 GEVTVKAKTIVLLTKALRPLPDKYHG--LTNIEQRYRQRYLDLiSNKDSFDRFMKRSQIISEIRRYLDGHGYVEVETPVL 208
Cdd:PRK05159 85 GGVEVIPEEIEVLNKAEEPLPLDISGkvLAELDTRLDNRFLDL-RRPRVRAIFKIRSEVLRAFREFLYENGFTEIFTPKI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 209 HNDA--GGAAARPfITHhnaLDMDLYLRIALELHlKRLIVG-GMEKVYEIGRVFRNEGIDTT-HNPEFTMLEAYTAYTD- 283
Cdd:PRK05159 164 VASGteGGAELFP-IDY---FEKEAYLAQSPQLY-KQMMVGaGFERVFEIGPVFRAEEHNTSrHLNEYTSIDVEMGFIDd 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 284 YKDVMDLTEGIIRNAADKVLGTTTITYDGQEVDLG---SEFRRVHMVDAIK--EQTGVDF-WKE-MTVEEARTFAKehnv 356
Cdd:PRK05159 239 HEDVMDLLENLLRYMYEDVAENCEKELELLGIELPvpeTPIPRITYDEAIEilKSKGNEIsWGDdLDTEGERLLGE---- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 357 einnnmsvgHILNEFFETFVeetlkqptFVYGHPVEVSPL-AKKNPEDDRFTDRFELFIVGKEFANAftelndpiDQRE- 434
Cdd:PRK05159 315 ---------YVKEEYGSDFY--------FITDYPSEKRPFyTMPDEDDPEISKSFDLLFRGLEITSG--------GQRIh 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 486874386 435 RFEDQEKE-REQGNDEahgvdEDF---IEALEYGLPPTGGLGIGIDRLVMLLTDAQSIRDVLLFP 495
Cdd:PRK05159 370 RYDMLVESiKEKGLNP-----ESFefyLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFP 429
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
159-495 |
5.96e-35 |
|
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: 133.08 E-value: 5.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 159 NIEQRYRQRYLDLISNKdsFDRFMK-RSQIISEIRRYLDGHGYVEVETPVL-HNDA-GGAAARPFithhNALDMDLYLRI 235
Cdd:cd00776 3 NLETLLDNRHLDLRTPK--VQAIFRiRSEVLRAFREFLRENGFTEVHTPKItSTDTeGGAELFKV----SYFGKPAYLAQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 236 ALELHLKRLIvGGMEKVYEIGRVFRNEGIDTT-HNPEFTMLEAYTAY-TDYKDVMDLTEGIIRNAADKVLgtttityDGQ 313
Cdd:cd00776 77 SPQLYKEMLI-AALERVYEIGPVFRAEKSNTRrHLSEFWMLEAEMAFiEDYNEVMDLIEELIKYIFKRVL-------ERC 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 314 EVDLgsEFRRVHMVDAIKEQTGvdfWKEMTVEEARTFAKEHNVEinNNMSVGHILNEFFETFVEETLKQ-PTFVYGHPVE 392
Cdd:cd00776 149 AKEL--ELVNQLNRELLKPLEP---FPRITYDEAIELLREKGVE--EEVKWGEDLSTEHERLLGEIVKGdPVFVTDYPKE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 393 VSPL-AKKNPEDDRFTDRFELFIVGK-EFANAFTELNDPIDQRERFEDqekereqgndeaHGVD----EDFIEALEYGLP 466
Cdd:cd00776 222 IKPFyMKPDDDNPETVESFDLLMPGVgEIVGGSQRIHDYDELEERIKE------------HGLDpesfEWYLDLRKYGMP 289
|
330 340
....*....|....*....|....*....
gi 486874386 467 PTGGLGIGIDRLVMLLTDAQSIRDVLLFP 495
Cdd:cd00776 290 PHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
181-495 |
1.27e-32 |
|
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: 125.77 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 181 FMKRSQIISEIRRYLDGHGYVEVETPVLHNDA-GGAaaRPFI----THHN---ALDM--DLYLRIalelhlkrLIVGGME 250
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTpEGA--RDFLvpsrLHPGkfyALPQspQLFKQL--------LMVSGFD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 251 KVYEIGRVFRNEGIDTTHNPEFTMLEAYTAYTDYKDVMDLTEGIIRNAADKVLGtttitydgqeVDLGSEFRRVHMVDAI 330
Cdd:cd00777 71 RYFQIARCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG----------VELTTPFPRMTYAEAM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 331 kEQTGVDF-WkemtVEEARTFakEHNVEINNNMSVGHIlnefFETFVEETLkqptfvyghpvevsPLAKKNPEDDRfTDR 409
Cdd:cd00777 141 -ERYGFKFlW----IVDFPLF--EWDEEEGRLVSAHHP----FTAPKEEDL--------------DLLEKDPEDAR-AQA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 410 FELFIVGKEFANAFTELNDPIDQRERFEDQEKEREQGNDE-AHgvdedFIEALEYGLPPTGGLGIGIDRLVMLLTDAQSI 488
Cdd:cd00777 195 YDLVLNGVELGGGSIRIHDPDIQEKVFEILGLSEEEAEEKfGF-----LLEAFKYGAPPHGGIALGLDRLVMLLTGSESI 269
|
....*..
gi 486874386 489 RDVLLFP 495
Cdd:cd00777 270 RDVIAFP 276
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
58-495 |
4.28e-31 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 126.72 E-value: 4.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 58 ELNEMDLSASV--AGRMMTKRGKGKAGFAHLQDREGQLQIYVRKDQvgdeayEVFKHAD-LGDFF--GVTGQIMKTD--- 129
Cdd:PRK00476 10 ELRESHVGQTVtlCGWVHRRRDHGGLIFIDLRDREGIVQVVFDPDA------EAFEVAEsLRSEYviQVTGTVRARPegt 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 130 ------TGEVTVKAKTIVLLTKA--LrPLPDKYHGLTNIEQRYRQRYLDLISNKdSFDRFMKRSQIISEIRRYLDGHGYV 201
Cdd:PRK00476 84 vnpnlpTGEIEVLASELEVLNKSktL-PFPIDDEEDVSEELRLKYRYLDLRRPE-MQKNLKLRSKVTSAIRNFLDDNGFL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 202 EVETPVLhndagGAA----ARPFI----THHNaldmDLYlriAL----ELhLKRLI-VGGMEKVYEIGRVFRNEGIDTTH 268
Cdd:PRK00476 162 EIETPIL-----TKStpegARDYLvpsrVHPG----KFY---ALpqspQL-FKQLLmVAGFDRYYQIARCFRDEDLRADR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 269 NPEFTMLEAYTAYTDYKDVMDLTEGIIRNAADKVLGTT------TITYD---------------GQE-VDLGSEFRRVH- 325
Cdd:PRK00476 229 QPEFTQIDIEMSFVTQEDVMALMEGLIRHVFKEVLGVDlptpfpRMTYAeamrrygsdkpdlrfGLElVDVTDLFKDSGf 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 326 -----------MVDAIKEQTGVDFWKEMTVEEARTFAKEHN------VEINNNMSVGHILNeFFETFVEETLKQPT---- 384
Cdd:PRK00476 309 kvfagaandggRVKAIRVPGGAAQLSRKQIDELTEFAKIYGakglayIKVNEDGLKGPIAK-FLSEEELAALLERTgakd 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 385 -----FVYGHPVEVS------------------------------PLAKKNPEDDR-------FT-------DRFELFIV 415
Cdd:PRK00476 388 gdlifFGADKAKVVNdalgalrlklgkelglidedkfaflwvvdfPMFEYDEEEGRwvaahhpFTmpkdedlDELETTDP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 416 GKEFANAF------TEL-------NDPIDQRERFE----DQEKEREQgndeahgvdedF---IEALEYGLPPTGGLGIGI 475
Cdd:PRK00476 468 GKARAYAYdlvlngYELgggsiriHRPEIQEKVFEilgiSEEEAEEK-----------FgflLDALKYGAPPHGGIAFGL 536
|
570 580
....*....|....*....|
gi 486874386 476 DRLVMLLTDAQSIRDVLLFP 495
Cdd:PRK00476 537 DRLVMLLAGADSIRDVIAFP 556
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
58-495 |
7.09e-25 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 108.34 E-value: 7.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 58 ELNEMDLSASV--AGRMMTKRGKGKAGFAHLQDREGQLQIyVRKDQVGDEAYEVFKHADLGDFFGVTGQIM--------- 126
Cdd:PLN02903 65 ALSVNDVGSRVtlCGWVDLHRDMGGLTFLDVRDHTGIVQV-VTLPDEFPEAHRTANRLRNEYVVAVEGTVRsrpqespnk 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 127 KTDTGEVTVKAKTIVLLTKALRPLP------DKYHGLTNIEQRYRQRYLDLISNKDSFDrFMKRSQIISEIRRYL-DGHG 199
Cdd:PLN02903 144 KMKTGSVEVVAESVDILNVVTKSLPflvttaDEQKDSIKEEVRLRYRVLDLRRPQMNAN-LRLRHRVVKLIRRYLeDVHG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 200 YVEVETPVLHNDAGgAAARPFITHHNALDMDLY-LRIALELHLKRLIVGGMEKVYEIGRVFRNEGIDTTHNPEFTMLEAY 278
Cdd:PLN02903 223 FVEIETPILSRSTP-EGARDYLVPSRVQPGTFYaLPQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEFTQLDME 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 279 TAYTDYKDVMDLTEGIIRNAADKVLGtttitydgqeVDLGSEFRRVHMVDAIkEQTGVD-----FWKEMT-VEEA----- 347
Cdd:PLN02903 302 LAFTPLEDMLKLNEDLIRQVFKEIKG----------VQLPNPFPRLTYAEAM-SKYGSDkpdlrYGLELVdVSDVfaess 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 348 -RTFA---------KEHNV----EINNN--MSVGHILNEFF---------------------------------ETFVEE 378
Cdd:PLN02903 371 fKVFAgalesggvvKAICVpdgkKISNNtaLKKGDIYNEAIksgakglaflkvlddgelegikalveslspeqaEQLLAA 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 379 TLKQP----TFVYGHPVEVS------------------------------PLAKKNPEDDRFTDRFELFI-----VGKEF 419
Cdd:PLN02903 451 CGAGPgdliLFAAGPTSSVNktldrlrqfiaktldlidpsrhsilwvtdfPMFEWNEDEQRLEALHHPFTapnpeDMGDL 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 420 ANAFTELNDP-------------IDQRERfedQEKEREQGNDEAHGVDEDF---IEALEYGLPPTGGLGIGIDRLVMLLT 483
Cdd:PLN02903 531 SSARALAYDMvyngveigggslrIYRRDV---QQKVLEAIGLSPEEAESKFgylLEALDMGAPPHGGIAYGLDRLVMLLA 607
|
570
....*....|..
gi 486874386 484 DAQSIRDVLLFP 495
Cdd:PLN02903 608 GAKSIRDVIAFP 619
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
83-495 |
3.53e-24 |
|
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: 105.85 E-value: 3.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 83 FAHLQDREGQLQIYVRKDqVGDEAYEVFKHadLGDFF--GVTGQIMKTD---------TGEVTVKAKTIVLLTKAlRPLP 151
Cdd:COG0173 36 FIDLRDRYGITQVVFDPD-DSAEAFEKAEK--LRSEYviAVTGKVRARPegtvnpklpTGEIEVLASELEILNKA-KTPP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 152 ----DkyHGLTNIEQRYRQRYLDLiSNKDSFDRFMKRSQIISEIRRYLDGHGYVEVETPVLhndagGAA----ARpfith 223
Cdd:COG0173 112 fqidD--DTDVSEELRLKYRYLDL-RRPEMQKNLILRHKVTKAIRNYLDENGFLEIETPIL-----TKStpegAR----- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 224 hnalDmdlYL---RI------AL----ELhLKRLI-VGGMEKVYEIGRVFRNEGIDTTHNPEFTMLEAYTAYTDYKDVMD 289
Cdd:COG0173 179 ----D---YLvpsRVhpgkfyALpqspQL-FKQLLmVSGFDRYFQIARCFRDEDLRADRQPEFTQLDIEMSFVDQEDVFE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 290 LTEGIIRNAADKVLGTT------TITYD---------------GQE-VDLGSEFRrvhmvdaikeqtGVDFwkemtveea 347
Cdd:COG0173 251 LMEGLIRHLFKEVLGVElptpfpRMTYAeamerygsdkpdlrfGLElVDVTDIFK------------DSGF--------- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 348 RTFAKehnvEINNNMSVGHI---------------LNEFFETF----------VEETLKqptfvyghpvevSPLAKKNPE 402
Cdd:COG0173 310 KVFAG----AAENGGRVKAInvpggaslsrkqideLTEFAKQYgakglayikvNEDGLK------------SPIAKFLSE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 403 DDR--FTDRFE-------LFIVGK-EFANAF---------TELNdPIDQRER----------FE-DQEKER--------- 443
Cdd:COG0173 374 EELaaILERLGakpgdliFFVADKpKVVNKAlgalrlklgKELG-LIDEDEFaflwvvdfplFEyDEEEGRwvamhhpft 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 444 -EQGNDEA------------------------------H------------GVDED--------FIEALEYGLPPTGGLG 472
Cdd:COG0173 453 mPKDEDLDlletdpgkvrakaydlvlngyelgggsiriHdpelqekvfellGISEEeaeekfgfLLEAFKYGAPPHGGIA 532
|
570 580
....*....|....*....|...
gi 486874386 473 IGIDRLVMLLTDAQSIRDVLLFP 495
Cdd:COG0173 533 FGLDRLVMLLAGEDSIRDVIAFP 555
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
184-495 |
5.89e-22 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 96.63 E-value: 5.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 184 RSQIISEIRRYLDGHGYVEVETPVL--------HNDAGGAAARPFIthhNALDMDLYLRIALELHlKRLIVGGMEKVYEI 255
Cdd:PRK06462 33 QSSILRYTREFLDGRGFVEVLPPIIspstdplmGLGSDLPVKQISI---DFYGVEYYLADSMILH-KQLALRMLGKIFYL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 256 GRVFRNEGIDT---THNPEFTMLEAYTAYTDYKDVMDLTEGIIRNAADKVLGTttitYDGQEVDLGSEFRRVHmvdaike 332
Cdd:PRK06462 109 SPNFRLEPVDKdtgRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEE----HEDELEFFGRDLPHLK------- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 333 qtgVDFwKEMTVEEARTFAKEHNVEINNNMSvghiLNEFFETFVEETLKQPTFVYGHPVEVSPL-AKKNPEDDRFTDRFE 411
Cdd:PRK06462 178 ---RPF-KRITHKEAVEILNEEGCRGIDLEE----LGSEGEKSLSEHFEEPFWIIDIPKGSREFyDREDPERPGVLRNYD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 412 LFIvgkefANAFTELndpIDQRERFED----QEKEREQGNDEAHGvdEDFIEALEYGLPPTGGLGIGIDRLVMLLTDAQS 487
Cdd:PRK06462 250 LLL-----PEGYGEA---VSGGEREYEyeeiVERIREHGVDPEKY--KWYLEMAKEGPLPSAGFGIGVERLTRYICGLRH 319
|
....*...
gi 486874386 488 IRDVLLFP 495
Cdd:PRK06462 320 IREVQPFP 327
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
55-495 |
1.99e-21 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 97.37 E-value: 1.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 55 SKEELneMDLSASVAGRMMTKRGKGKAGFAHLQDREGQLQIYVRK---------DQVGDEAYEVFKHADlGDFFGVTGQI 125
Cdd:PTZ00401 72 SKPEL--VDKTVLIRARVSTTRKKGKMAFMVLRDGSDSVQAMAAVegdvpkemiDFIGQIPTESIVDVE-ATVCKVEQPI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 126 MKTDTGEVTVKAKTIVLLTKALRPLP----------DKYHGLTNIEQRYRQRYLDLISNKdSFDRFMKRSQIISEIRRYL 195
Cdd:PTZ00401 149 TSTSHSDIELKVKKIHTVTESLRTLPftledasrkeSDEGAKVNFDTRLNSRWMDLRTPA-SGAIFRLQSRVCQYFRQFL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 196 DGHGYVEVETPVLHNDAGGAAARPFITHHnaLDMDLYLRIALELHLKRLIVGGMEKVYEIGRVFRNEGIDT-THNPEFTM 274
Cdd:PTZ00401 228 IDSDFCEIHSPKIINAPSEGGANVFKLEY--FNRFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNThRHLTEFVG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 275 LEAYTAYTD-YKDVMDLTEGIIRNAADKVLGTTtitydGQEVDLGSEFRRVHMV-----DAIKEqTGVDFWKEMTVEEAR 348
Cdd:PTZ00401 306 LDVEMRINEhYYEVLDLAESLFNYIFERLATHT-----KELKAVCQQYPFEPLVwkltpERMKE-LGVGVISEGVEPTDK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 349 TFAKEHNVEIN----NNMSVGHILNEFFET------------------FVEETLKQPTFVYGH-PVEVSPL-AKKNPEDD 404
Cdd:PTZ00401 380 YQARVHNMDSRmlriNYMHCIELLNTVLEEkmaptddinttnekllgkLVKERYGTDFFISDRfPSSARPFyTMECKDDE 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 405 RFTDRFELFIVGKEFANAFTELNDPidqrerfeDQEKEREQGNDEAHGVDEDFIEALEYGLPPTGGLGIGIDRLVMLLTD 484
Cdd:PTZ00401 460 RFTNSYDMFIRGEEISSGAQRIHDP--------DLLLARAKMLNVDLTPIKEYVDSFRLGAWPHGGFGVGLERVVMLYLG 531
|
490
....*....|.
gi 486874386 485 AQSIRDVLLFP 495
Cdd:PTZ00401 532 LSNVRLASLFP 542
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
68-497 |
2.30e-19 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 90.55 E-value: 2.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 68 VAGRMMTKRGKGKAGFAHLQDREGQLQIYVRKDQvGDEAYEVFKHADLGDFFGVTGQIMKTDT--GEVTVKAKTIVLLTK 145
Cdd:PRK03932 21 VRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDN-GEEYFEEIKKLTTGSSVIVTGTVVESPRagQGYELQATKIEVIGE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 146 ALR--PLPDKYHGltnIEQRYRQRYLDLISNKdsFDRFMK-RSQIISEIRRYLDGHGYVEVETPVL-HNDAGGAAARpFI 221
Cdd:PRK03932 100 DPEdyPIQKKRHS---IEFLREIAHLRPRTNK--FGAVMRiRNTLAQAIHEFFNENGFVWVDTPIItASDCEGAGEL-FR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 222 ThhNALDMDL---------YLRIALELHLKRLIVGgMEKVYEIGRVFRNEGIDTT-HNPEFTMLEAYTAYTDYKDVMDLT 291
Cdd:PRK03932 174 V--TTLDLDFskdffgkeaYLTVSGQLYAEAYAMA-LGKVYTFGPTFRAENSNTRrHLAEFWMIEPEMAFADLEDNMDLA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 292 EGIIRNAADKVLgtttityDGQEVDLgsEF--RRVHM--VDAIKEQTGVDFwKEMTVEEARTFAKEHNVEINNNMSVGHI 367
Cdd:PRK03932 251 EEMLKYVVKYVL-------ENCPDDL--EFlnRRVDKgdIERLENFIESPF-PRITYTEAIEILQKSGKKFEFPVEWGDD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 368 LNEFFETF-VEETLKQPTFVYGHPVEVSPLAKKNPEDDRFTDRFELF------IVGKEfanaftelndpidQRErfEDQE 440
Cdd:PRK03932 321 LGSEHERYlAEEHFKKPVFVTNYPKDIKAFYMRLNPDGKTVAAMDLLapgigeIIGGS-------------QRE--ERLD 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 486874386 441 K--EREqgndEAHGVDEdfiEALE-------YGLPPTGGLGIGIDRLVMLLTDAQSIRDVLLFPTM 497
Cdd:PRK03932 386 VleARI----KELGLNK---EDYWwyldlrrYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRT 444
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
68-498 |
4.71e-19 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 90.43 E-value: 4.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 68 VAGRMMTKRGKGKAGFAHLQDREGQLQIYVRKDQVGDEAYEVFKHADLGDFFGVTGQIMK---------TDTG--EVTVK 136
Cdd:PRK12820 23 LAGWVDAFRDHGELLFIHLRDRNGFIQAVFSPEAAPADVYELAASLRAEFCVALQGEVQKrleetenphIETGdiEVFVR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 137 AKTIVLLTKALrPLPDKYHGLT-----------NIEQRYRQRYLDlISNKDSFDRFMKRSQIISEIRRYLDGHGYVEVET 205
Cdd:PRK12820 103 ELSILAASEAL-PFAISDKAMTagagsagadavNEDLRLQYRYLD-IRRPAMQDHLAKRHRIIKCARDFLDSRGFLEIET 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 206 PVLhNDAGGAAARPFITHHNALDMDLY-LRIALELHLKRLIVGGMEKVYEIGRVFRNEGIDTTHNPEFTMLEAYTAYTDY 284
Cdd:PRK12820 181 PIL-TKSTPEGARDYLVPSRIHPKEFYaLPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEFTQLDIEASFIDE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 285 KDVMDLTEGII------------RNAADKVLGTTTITYDGQEVDLGSEFRRVHMVDaIKEQTGVDFWKEMTVEEAR---- 348
Cdd:PRK12820 260 EFIFELIEELTarmfaiggialpRPFPRMPYAEAMDTTGSDRPDLRFDLKFADATD-IFENTRYGIFKQILQRGGRikgi 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 349 ------------TFAKEHNVEINNNM----------SVGHILNEFFETFVEETLKQ------------------------ 382
Cdd:PRK12820 339 nikgqseklsknVLQNEYAKEIAPSFgakgmtwmraEAGGLDSNIVQFFSADEKEAlkrrfhaedgdviimiadascaiv 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 383 ------------------PTFVYgHPVEVSPLAKKNPEDDR--------FT--DR------------------FELFIVG 416
Cdd:PRK12820 419 lsalgqlrlhladrlgliPEGVF-HPLWITDFPLFEATDDGgvtsshhpFTapDRedfdpgdieelldlrsraYDLVVNG 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 417 KEFANAFTELNDPIDQRERFE-----DQEKEREQGNdeahgvdedFIEALEYGLPPTGGLGIGIDRLVMLLTDAQSIRDV 491
Cdd:PRK12820 498 EELGGGSIRINDKDIQLRIFAalglsEEDIEDKFGF---------FLRAFDFAAPPHGGIALGLDRVVSMILQTPSIREV 568
|
....*..
gi 486874386 492 LLFPTMR 498
Cdd:PRK12820 569 IAFPKNR 575
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
68-495 |
1.52e-18 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 88.22 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 68 VAGRMMTKRGKGKAGFAHLQDREGQLQ--IYVRKDQVGD------EAYEVFKHADLGDFFGVTGQIMKTDTGEVTVKAKT 139
Cdd:PLN02850 86 IRGRVHTIRGKGKSAFLVLRQSGFTVQcvVFVSEVTVSKgmvkyaKQLSRESVVDVEGVVSVPKKPVKGTTQQVEIQVRK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 140 IVLLTKALRPLP-------------------DKYHGLTNIEQRYRQRYLDL--ISNKDSFdRFmkRSQIISEIRRYLDGH 198
Cdd:PLN02850 166 IYCVSKALATLPfnvedaarseseiekalqtGEQLVRVGQDTRLNNRVLDLrtPANQAIF-RI--QSQVCNLFREFLLSK 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 199 GYVEVETPVLHNDA--GGAAArpFithhnALDmdlY------LRIALELHLKRLIVGGMEKVYEIGRVFRNEGIDT-THN 269
Cdd:PLN02850 243 GFVEIHTPKLIAGAseGGSAV--F-----RLD---YkgqpacLAQSPQLHKQMAICGDFRRVFEIGPVFRAEDSFThRHL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 270 PEFTMLEAYTAYTD-YKDVMDLTegiirnaaDKVLGTTtitYDGQEVDLGSEfrrvhmVDAIKEQTGVDFWK------EM 342
Cdd:PLN02850 313 CEFTGLDLEMEIKEhYSEVLDVV--------DELFVAI---FDGLNERCKKE------LEAIREQYPFEPLKylpktlRL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 343 TVEEARTFAKEHNVEIN--------NNMSVGHILNEFFET-FVeetlkqptFVYGHPVEVSPL-AKKNPEDDRFTDRFEL 412
Cdd:PLN02850 376 TFAEGIQMLKEAGVEVDplgdlnteSERKLGQLVKEKYGTdFY--------ILHRYPLAVRPFyTMPCPDDPKYSNSFDV 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 413 FIVGKEFANAFTELNDP--IDQRERfedqekereqgndeAHGVD----EDFIEALEYGLPPTGGLGIGIDRLVMLLTDAQ 486
Cdd:PLN02850 448 FIRGEEIISGAQRVHDPelLEKRAE--------------ECGIDvktiSTYIDSFRYGAPPHGGFGVGLERVVMLFCGLN 513
|
....*....
gi 486874386 487 SIRDVLLFP 495
Cdd:PLN02850 514 NIRKTSLFP 522
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
184-296 |
2.38e-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: 80.62 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 184 RSQIISEIRRYLDGHGYVEVETPVLHNDAGGAAAR----PFITHHNALDMDLYLRIALELHLKRLIVG----GMEKVYEI 255
Cdd:cd00768 2 RSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGhepkDLLPVGAENEEDLYLRPTLEPGLVRLFVShirkLPLRLAEI 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 486874386 256 GRVFRNEGI--DTTHNPEFTMLEAYTAYTD------YKDVMDLTEGIIR 296
Cdd:cd00768 82 GPAFRNEGGrrGLRRVREFTQLEGEVFGEDgeeaseFEELIELTEELLR 130
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
232-495 |
4.20e-15 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 77.76 E-value: 4.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 232 YLRIALELHLKRLiVGGMEKVYEIGRVFRNEGIDTT-HNPEFTMLEAYTAYTDYKDVMDLTEGIIRNAADKVLGTT--TI 308
Cdd:PTZ00425 327 FLTVSGQLSLENL-CSSMGDVYTFGPTFRAENSHTSrHLAEFWMIEPEIAFADLYDNMELAESYIKYCIGYVLNNNfdDI 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 309 TYDGQEVDLGsefrrvhMVDAIKEQTGVDFWK---EMTVEEARTFAKEHNVEINNNMSvghiLNEFFETFV-EETLKQPT 384
Cdd:PTZ00425 406 YYFEENVETG-------LISRLKNILDEDFAKityTNVIDLLQPYSDSFEVPVKWGMD----LQSEHERFVaEQIFKKPV 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 385 FVYGHPVEVSPLAKKNPEDDRFTDRFELFI--VGKEFANAFTElndpiDQRERFEDQEKEREQgNDEAHGVdedFIEALE 462
Cdd:PTZ00425 475 IVYNYPKDLKAFYMKLNEDQKTVAAMDVLVpkIGEVIGGSQRE-----DNLERLDKMIKEKKL-NMESYWW---YRQLRK 545
|
250 260 270
....*....|....*....|....*....|...
gi 486874386 463 YGLPPTGGLGIGIDRLVMLLTDAQSIRDVLLFP 495
Cdd:PTZ00425 546 FGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFP 578
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
67-145 |
4.73e-15 |
|
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: 70.29 E-value: 4.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 67 SVAGRMMTKRGKGKAGFAHLQDREGQLQIYVRKDQVgDEAYEVFKHADLGDFFGVTGQIMKTD-----TGEVTVKAKTIV 141
Cdd:cd04100 3 TLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEEL-GEFFEEAEKLRTESVVGVTGTVVKRPegnlaTGEIELQAEELE 81
|
....
gi 486874386 142 LLTK 145
Cdd:cd04100 82 VLSK 85
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
67-143 |
4.41e-13 |
|
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: 64.18 E-value: 4.41e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 486874386 67 SVAGRMMTK-RGKGKAGFAHLQDREGQLQIYVRKDqvgdEAYEVFKHADLGDFFGVTGQIMKTDTGEVTVKAKTIVLL 143
Cdd:pfam01336 2 TVAGRVTSIrRSGGKLLFLTLRDGTGSIQVVVFKE----EAEKLAKKLKEGDVVRVTGKVKKRKGGELELVVEEIELL 75
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
249-495 |
2.01e-08 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 56.54 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 249 MEKVYEIGRVFRNEGIDTT-HNPEFTMLEAYTAYTDYKDVMDLTEGIIRNAADKVLGTTtitYDGQE-----VDLG---- 318
Cdd:PLN02221 326 LSSVYTFGPTFRAENSHTSrHLAEFWMVEPEIAFADLEDDMNCAEAYVKYMCKWLLDKC---FDDMElmaknFDSGcidr 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 319 ------SEFRRVHMVDAIKeqtgvdfwkemTVEEARTFAKEhnveINNNMSVGHILNEFFETFVEETL-KQPTFVYGHPV 391
Cdd:PLN02221 403 lrmvasTPFGRITYTEAIE-----------LLEEAVAKGKE----FDNNVEWGIDLASEHERYLTEVLfQKPLIVYNYPK 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 392 EVSPLAKKNPEDDRFTDRFELFI--VGKEFANAftelndpidQRERFEDQEKEREQGNDEAHGVDEDFIEALEYGLPPTG 469
Cdd:PLN02221 468 GIKAFYMRLNDDEKTVAAMDVLVpkVGELIGGS---------QREERYDVIKQRIEEMGLPIEPYEWYLDLRRYGTVKHC 538
|
250 260
....*....|....*....|....*.
gi 486874386 470 GLGIGIDRLVMLLTDAQSIRDVLLFP 495
Cdd:PLN02221 539 GFGLGFERMILFATGIDNIRDVIPFP 564
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
230-495 |
7.87e-08 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 54.88 E-value: 7.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 230 DLYLRIALELHLKRLiVGGMEKVYEIGRVFRNEGIDTT-HNPEFTMLEAYTAYTDYKDVMD--------LTEGIIRNAAD 300
Cdd:PLN02532 371 PTYLTVSGRLHLESY-ACALGNVYTFGPRFRADRIDSArHLAEMWMVEVEMAFSELEDAMNcaedyfkfLCKWVLENCSE 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 301 ------KVLGTTTITYdgQEVDLGSEFRRV---HMVDAIKEQTGVDFwkEMTVEEARTFAKEHnveinnnmsvghilnef 371
Cdd:PLN02532 450 dmkfvsKRIDKTISTR--LEAIISSSLQRIsytEAVDLLKQATDKKF--ETKPEWGIALTTEH----------------- 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 372 FETFVEETLKQPTFVYGHPVEVSPLAKKNPEDDRFTDRFEL-------FIVGKEFANAFTELNdpidqrERFEDQEKERE 444
Cdd:PLN02532 509 LSYLADEIYKKPVIIYNYPKELKPFYVRLNDDGKTVAAFDLvvpkvgtVITGSQNEERMDILN------ARIEELGLPRE 582
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 486874386 445 QGndeahgvdEDFIEALEYGLPPTGGLGIGIDRLVMLLTDAQSIRDVLLFP 495
Cdd:PLN02532 583 QY--------EWYLDLRRHGTVKHSGFSLGFELMVLFATGLPDVRDAIPFP 625
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
40-171 |
1.04e-06 |
|
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: 47.90 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 40 RTHNSKELhdqfdqhSKEELNEmdlSASVAGRMMTKRGKGKAGFAHLQDREGQLQIYVRKDQvgDEAYEVFKHADLGDFF 119
Cdd:cd04317 1 RTHYCGEL-------RESHVGQ---EVTLCGWVQRRRDHGGLIFIDLRDRYGIVQVVFDPEE--APEFELAEKLRNESVI 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 486874386 120 GVTGQIM---------KTDTGEVTVKAKTIVLLTKALR-PLPDKYHGLTNIEQRYRQRYLDL 171
Cdd:cd04317 69 QVTGKVRarpegtvnpKLPTGEIEVVASELEVLNKAKTlPFEIDDDVNVSEELRLKYRYLDL 130
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
68-152 |
3.53e-04 |
|
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: 39.99 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 68 VAGRMMTKRGKGKAGFAHLQDREGQLQIYVRKDQVGDEAYEVFKHADLGDFFGVTGQIMKTDT--GEVTVKAKTIVLLTK 145
Cdd:cd04316 17 VAGWVHEIRDLGGIKFVILRDREGIVQVTAPKKKVDKELFKTVRKLSRESVISVTGTVKAEPKapNGVEIIPEEIEVLSE 96
|
....*..
gi 486874386 146 ALRPLPD 152
Cdd:cd04316 97 AKTPLPL 103
|
|
| pheS |
PRK04172 |
phenylalanine--tRNA ligase subunit alpha; |
251-276 |
2.46e-03 |
|
phenylalanine--tRNA ligase subunit alpha;
Pssm-ID: 235239 [Multi-domain] Cd Length: 489 Bit Score: 40.20 E-value: 2.46e-03
10 20
....*....|....*....|....*.
gi 486874386 251 KVYEIGRVFRNEGIDTTHNPEFTMLE 276
Cdd:PRK04172 352 KYFSIGRVFRPDTIDATHLPEFYQLE 377
|
|
| PheRS_alpha_core |
cd00496 |
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ... |
185-277 |
6.43e-03 |
|
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: 38.30 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486874386 185 SQIISEIRRYLDGHGYVEVETPVLHNDAGGAAARPFITHHNALDM-DLY-----LRIALELH--------LKRLivGGME 250
Cdd:cd00496 4 NKVIEEIEDIFVSMGFTEVEGPEVETDFYNFDALNIPQDHPARDMqDTFyindpARLLLRTHtsavqaraLAKL--KPPI 81
|
90 100
....*....|....*....|....*..
gi 486874386 251 KVYEIGRVFRNEGIDTTHNPEFTMLEA 277
Cdd:cd00496 82 RIFSIGRVYRNDEIDATHLPEFHQIEG 108
|
|
| |
