|
Name |
Accession |
Description |
Interval |
E-value |
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
7-498 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 965.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 7 EELNDQLLVRREKLHNLREQGIDPFGKRFERTNATNDLLSLYGEFSKEELEEKEISVSIAGRIMTKRGKGKAGFAHIQDL 86
Cdd:PRK00484 1 EELNEQIAVRREKLAELREQGIDPYPNKFERTHTAAELRAKYDDKEKEELEELEIEVSVAGRVMLKRVMGKASFATLQDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 87 HGQVQIYVRKDAVGDEEYELFKTADLGDLVGIEGKVFKTNVGELSVKATGFTLLTKSLRPLPDKYHGLKDVEQRYRQRYL 166
Cdd:PRK00484 81 SGRIQLYVSKDDVGEEALEAFKKLDLGDIIGVEGTLFKTKTGELSVKATELTLLTKSLRPLPDKFHGLTDVETRYRQRYV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 167 DLITSMESRETFVTRSKIIREMRRYLDDNGYLEVETPMMHAIAGGASARPFITHHNALDMELYMRIAIELHLKRLIVGGL 246
Cdd:PRK00484 161 DLIVNPESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARPFITHHNALDIDLYLRIAPELYLKRLIVGGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 247 EKVYEIGRVFRNEGVSTRHNPEFTMIELYEAYADYKDIMKLTENMVAHIAKQVLGTTTIQYGDYEINLEPEWTRLHMVDA 326
Cdd:PRK00484 241 ERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTYQGTEIDFGPPFKRLTMVDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 327 IKEHSGADFWnPMSVEEARELAKEHNVEIKDTMEVGHIINEFFEQKVEDKLIQPTFIYGHPVEISPLAKKNDEDPRFTDR 406
Cdd:PRK00484 321 IKEYTGVDFD-DMTDEEARALAKELGIEVEKSWGLGKLINELFEEFVEPKLIQPTFITDYPVEISPLAKRHREDPGLTER 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 407 FELFIVAREHANAFTELNDPIDQKERFEAQLKEREQGNDEAHMMDDDYIEALEYGMPPTGGLGIGIDRLVMLLTNAPSIR 486
Cdd:PRK00484 400 FELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIR 479
|
490
....*....|..
gi 446291816 487 DVLLFPAMRHKQ 498
Cdd:PRK00484 480 DVILFPLMRPEK 491
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
5-499 |
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: 949.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 5 NHEELNDQLLVRREKLHNLREQGIDPFGKRFERTNATNDLLSLYGEFSKEELEEKEisVSIAGRIMTKRGKGKAGFAHIQ 84
Cdd:COG1190 3 EEEDLNEQIRVRREKLEELREAGIDPYPNKFPRTHTAAEIREKYDELEAEEETGDE--VSVAGRIMAKRDMGKASFADLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 85 DLHGQVQIYVRKDAVGDEEYELFKTADLGDLVGIEGKVFKTNVGELSVKATGFTLLTKSLRPLPDKYHGLKDVEQRYRQR 164
Cdd:COG1190 81 DGSGRIQLYLRRDELGEEAYELFKLLDLGDIVGVEGTVFRTKTGELSVKVEELTLLSKSLRPLPEKFHGLTDPETRYRQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 165 YLDLITSMESRETFVTRSKIIREMRRYLDDNGYLEVETPMMHAIAGGASARPFITHHNALDMELYMRIAIELHLKRLIVG 244
Cdd:COG1190 161 YVDLIVNPEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 245 GLEKVYEIGRVFRNEGVSTRHNPEFTMIELYEAYADYKDIMKLTENMVAHIAKQVLGTTTIQYGDYEINLEPEWTRLHMV 324
Cdd:COG1190 241 GFERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGTTKVTYQGQEIDLSPPWRRITMV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 325 DAIKEHSGADFWNPMSVEEARELAKEHNVEIKDTMEVGHIINEFFEQKVEDKLIQPTFIYGHPVEISPLAKKNDEDPRFT 404
Cdd:COG1190 321 EAIKEATGIDVTPLTDDEELRALAKELGIEVDPGWGRGKLIDELFEELVEPKLIQPTFVTDYPVEVSPLAKRHRDDPGLT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 405 DRFELFIVAREHANAFTELNDPIDQKERFEAQLKEREQGNDEAHMMDDDYIEALEYGMPPTGGLGIGIDRLVMLLTNAPS 484
Cdd:COG1190 401 ERFELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSPS 480
|
490
....*....|....*
gi 446291816 485 IRDVLLFPAMRHKQD 499
Cdd:COG1190 481 IRDVILFPLMRPEKK 495
|
|
| lysS_bact |
TIGR00499 |
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ... |
8-495 |
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: 763.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 8 ELNDQLLVRREKLHNLREQGIDPFGKRFERTNATNDLLSLYGEFSKEELEEKEISVSIAGRIMTKRGKGKAGFAHIQDLH 87
Cdd:TIGR00499 1 ELNDQAQQRLEKLNRLRQTGNNPYLHKFERTHSAQEFQEKYADLSNEELKEKELKVSIAGRIKAIRSMGKATFITLQDES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 88 GQVQIYVRKDAVGDEEYELFK-TADLGDLVGIEGKVFKTNVGELSVKATGFTLLTKSLRPLPDKYHGLKDVEQRYRQRYL 166
Cdd:TIGR00499 81 GQIQLYVNKNKLPEDFYEFDEyLLDLGDIIGVTGYPFKTKTGELSVKVTELQILTKCLQPLPDKWHGLTDQETRYRQRYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 167 DLITSMESRETFVTRSKIIREMRRYLDDNGYLEVETPMMHAIAGGASARPFITHHNALDMELYMRIAIELHLKRLIVGGL 246
Cdd:TIGR00499 161 DLIVNPDVRQTFLKRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKPFITHHNALDMDLYLRIAPELYLKRLIVGGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 247 EKVYEIGRVFRNEGVSTRHNPEFTMIELYEAYADYKDIMKLTENMVAHIAKQVLGTTTIQYGDYEINLEPEWTRLHMVDA 326
Cdd:TIGR00499 241 EKVYEIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTFIINYNDLEIDLKPPWKRITMVDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 327 IKEHSGADFWNPMSVEEARELAKEHNVEI-KDTMEVGHIINEFFEQKVEDKLIQPTFIYGHPVEISPLAKKNDEDPRFTD 405
Cdd:TIGR00499 321 LEMVTGIDFDILKDDETAKALAKEHGIEVaEDSLTLGHILNKFFEQFLEHTLIQPTFITHYPAEISPLAKRDPSNPEFTE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 406 RFELFIVAREHANAFTELNDPIDQKERFEAQLKEREQGNDEAHMMDDDYIEALEYGMPPTGGLGIGIDRLVMLLTNAPSI 485
Cdd:TIGR00499 401 RFELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGIGIDRLVMLLTDAPSI 480
|
490
....*....|
gi 446291816 486 RDVLLFPAMR 495
Cdd:TIGR00499 481 RDVLLFPQLR 490
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
15-498 |
0e+00 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 682.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 15 VRREKLHNLREQGIDPFGKRFERTNATNDLLSLYGEFSK-EELEEKeiSVSIAGRIMTKRGKGKAGFAHIQDLHGQVQIY 93
Cdd:PLN02502 64 NRLKKVEALRAKGVEPYPYKFDVTHTAPELQEKYGSLENgEELEDV--SVSVAGRIMAKRAFGKLAFYDLRDDGGKIQLY 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 94 VRKDAVGDEEYELFK---TADLGDLVGIEGKVFKTNVGELSVKATGFTLLTKSLRPLPDKYHGLKDVEQRYRQRYLDLIT 170
Cdd:PLN02502 142 ADKKRLDLDEEEFEKlhsLVDRGDIVGVTGTPGKTKKGELSIFPTSFEVLTKCLLMLPDKYHGLTDQETRYRQRYLDLIA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 171 SMESRETFVTRSKIIREMRRYLDDNGYLEVETPMMHAIAGGASARPFITHHNALDMELYMRIAIELHLKRLIVGGLEKVY 250
Cdd:PLN02502 222 NPEVRDIFRTRAKIISYIRRFLDDRGFLEVETPMLNMIAGGAAARPFVTHHNDLNMDLYLRIATELHLKRLVVGGFERVY 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 251 EIGRVFRNEGVSTRHNPEFTMIELYEAYADYKDIMKLTENMVAHIAKQVLGTTTIQYGDYEINLEPEWTRLHMVDAIKEH 330
Cdd:PLN02502 302 EIGRQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKELTGSYKIKYHGIEIDFTPPFRRISMISLVEEA 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 331 SGADFWNPMSVEEAR----ELAKEHNVEIKDTMEVGHIINEFFEQKVEDKLIQPTFIYGHPVEISPLAKKNDEDPRFTDR 406
Cdd:PLN02502 382 TGIDFPADLKSDEANayliAACEKFDVKCPPPQTTGRLLNELFEEFLEETLVQPTFVLDHPVEMSPLAKPHRSKPGLTER 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 407 FELFIVAREHANAFTELNDPIDQKERFEAQLKEREQGNDEAHMMDDDYIEALEYGMPPTGGLGIGIDRLVMLLTNAPSIR 486
Cdd:PLN02502 462 FELFINGRELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRLVMLLTDSASIR 541
|
490
....*....|..
gi 446291816 487 DVLLFPAMRHKQ 498
Cdd:PLN02502 542 DVIAFPAMKPQD 553
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
173-495 |
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: 581.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 173 ESRETFVTRSKIIREMRRYLDDNGYLEVETPMMHAIAGGASARPFITHHNALDMELYMRIAIELHLKRLIVGGLEKVYEI 252
Cdd:cd00775 3 EVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVYEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 253 GRVFRNEGVSTRHNPEFTMIELYEAYADYKDIMKLTENMVAHIAKQVLGTTTIQYGDYEINLEPEWTRLHMVDAIKEHSG 332
Cdd:cd00775 83 GRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIEYGGKELDFTPPFKRVTMVDALKEKTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 333 ADFWNPmSVEEARELAKEHNVEIKDTME----VGHIINEFFEQKVEDKLIQPTFIYGHPVEISPLAKKNDEDPRFTDRFE 408
Cdd:cd00775 163 IDFPEL-DLEQPEELAKLLAKLIKEKIEkprtLGKLLDKLFEEFVEPTLIQPTFIIDHPVEISPLAKRHRSNPGLTERFE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 409 LFIVAREHANAFTELNDPIDQKERFEAQLKEREQGNDEAHMMDDDYIEALEYGMPPTGGLGIGIDRLVMLLTNAPSIRDV 488
Cdd:cd00775 242 LFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLTDSNSIRDV 321
|
....*..
gi 446291816 489 LLFPAMR 495
Cdd:cd00775 322 ILFPAMR 328
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
8-498 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 516.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 8 ELNDQLLVRREKLHNLREQGIdPFGKRFERTNATNDLLSLYGEFSKEELEEKEISVSIAGRIMTKRGKGKAGFAHIQDLH 87
Cdd:PRK12445 14 DFNDELRNRREKLAALRQQGV-AFPNDFRRDHTSDQLHEEFDAKDNQELESLNIEVSVAGRMMTRRIMGKASFVTLQDVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 88 GQVQIYVRKDAVGDEEY-ELFKTADLGDLVGIEGKVFKTNVGELSVKATGFTLLTKSLRPLPDKYHGLKDVEQRYRQRYL 166
Cdd:PRK12445 93 GRIQLYVARDSLPEGVYnDQFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFHGLQDQEVRYRQRYL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 167 DLITSMESRETFVTRSKIIREMRRYLDDNGYLEVETPMMHAIAGGASARPFITHHNALDMELYMRIAIELHLKRLIVGGL 246
Cdd:PRK12445 173 DLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 247 EKVYEIGRVFRNEGVSTRHNPEFTMIELYEAYADYKDIMKLTENMVAHIAKQVLGTTTIQYGDYEINLEPEWTRLHMVDA 326
Cdd:PRK12445 253 ERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFDFGKPFEKLTMREA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 327 IKEHS-GADFWNPMSVEEARELAKEHNVEIKDTMEVGHIINEFFEQKVEDKLIQPTFIYGHPVEISPLAKKNDEDPRFTD 405
Cdd:PRK12445 333 IKKYRpETDMADLDNFDAAKALAESIGITVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEITD 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 406 RFELFIVAREHANAFTELNDPIDQKERFEAQLKEREQGNDEAHMMDDDYIEALEYGMPPTGGLGIGIDRLVMLLTNAPSI 485
Cdd:PRK12445 413 RFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTI 492
|
490
....*....|...
gi 446291816 486 RDVLLFPAMRHKQ 498
Cdd:PRK12445 493 RDVILFPAMRPQK 505
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
9-495 |
2.30e-165 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 496.41 E-value: 2.30e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 9 LNDQLLVRREKLHNLREQGIDPFGKRFERTNATNDLL-SLYGEfskeeleekeiSVSIAGRIMTKRGKGKAGFAHIQDLH 87
Cdd:PRK02983 610 LPEQVRVRLAKLEALRAAGVDPYPVGVPPTHTVAEALdAPTGE-----------EVSVSGRVLRIRDYGGVLFADLRDWS 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 88 GQVQIYVRKDAVGDEEYELFKTA-DLGDLVGIEGKVFKTNVGELSVKATGFTLLTKSLRPLPDKYHGLKDVEQRYRQRYL 166
Cdd:PRK02983 679 GELQVLLDASRLEQGSLADFRAAvDLGDLVEVTGTMGTSRNGTLSLLVTSWRLAGKCLRPLPDKWKGLTDPEARVRQRYL 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 167 DLITSMESRETFVTRSKIIREMRRYLDDNGYLEVETPMMHAIAGGASARPFITHHNALDMELYMRIAIELHLKRLIVGGL 246
Cdd:PRK02983 759 DLAVNPEARDLLRARSAVVRAVRETLVARGFLEVETPILQQVHGGANARPFVTHINAYDMDLYLRIAPELYLKRLCVGGV 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 247 EKVYEIGRVFRNEGVSTRHNPEFTMIELYEAYADYKDIMKLTENMVAHIAKQVLGTTTIQYGDYEINLEP-----EWTRL 321
Cdd:PRK02983 839 ERVFELGRNFRNEGVDATHNPEFTLLEAYQAHADYDTMRDLTRELIQNAAQAAHGAPVVMRPDGDGVLEPvdisgPWPVV 918
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 322 HMVDAIKEHSGADFWNPMSVEEARELAKEHNVEIKDTMEVGHIINEFFEQKVEDKLIQPTFIYGHPVEISPLAKKNDEDP 401
Cdd:PRK02983 919 TVHDAVSEALGEEIDPDTPLAELRKLCDAAGIPYRTDWDAGAVVLELYEHLVEDRTTFPTFYTDFPTSVSPLTRPHRSDP 998
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 402 RFTDRFELFIVAREHANAFTELNDPIDQKERFEAQLKEREQGNDEAHMMDDDYIEALEYGMPPTGGLGIGIDRLVMLLTN 481
Cdd:PRK02983 999 GLAERWDLVAWGVELGTAYSELTDPVEQRRRLTEQSLLAAGGDPEAMELDEDFLQALEYAMPPTGGLGMGVDRLVMLLTG 1078
|
490
....*....|....
gi 446291816 482 ApSIRDVLLFPAMR 495
Cdd:PRK02983 1079 R-SIRETLPFPLVK 1091
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
16-495 |
1.00e-141 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 419.80 E-value: 1.00e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 16 RREKLHNLREQGIDPFGKRFERTNATNDLLSLYGEF-SKEELEEKEISVSiaGRIMTKRGKG-KAGFAHIQDLHGQVQI- 92
Cdd:PTZ00417 89 RSKFIQEQKAKGINPYPHKFERTITVPEFVEKYQDLaSGEHLEDTILNVT--GRIMRVSASGqKLRFFDLVGDGAKIQVl 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 93 --YVRKDAVGDEEYELFKTADLGDLVGIEGKVFKTNVGELSVKATGFTLLTKSLRPLPDKYhGLKDVEQRYRQRYLDLIT 170
Cdd:PTZ00417 167 anFAFHDHTKSNFAECYDKIRRGDIVGIVGFPGKSKKGELSIFPKETIILSPCLHMLPMKY-GLKDTEIRYRQRYLDLMI 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 171 SMESRETFVTRSKIIREMRRYLDDNGYLEVETPMMHAIAGGASARPFITHHNALDMELYMRIAIELHLKRLIVGGLEKVY 250
Cdd:PTZ00417 246 NESTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLVAGGANARPFITHHNDLDLDLYLRIATELPLKMLIVGGIDKVY 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 251 EIGRVFRNEGVSTRHNPEFTMIELYEAYADYKDIMKLTENMVAHIAKQVLGTTTIQYGD-------YEINLEPEWTRLHM 323
Cdd:PTZ00417 326 EIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHLFGTYKILYNKdgpekdpIEIDFTPPYPKVSI 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 324 VDAIKEHSGAD----FWNPMSVEEARELAKEHNVEIKDTMEVGHIINEFFEQKVEDKLI-QPTFIYGHPVEISPLAKKND 398
Cdd:PTZ00417 406 VEELEKLTNTKleqpFDSPETINKMINLIKENKIEMPNPPTAAKLLDQLASHFIENKYPnKPFFIIEHPQIMSPLAKYHR 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 399 EDPRFTDRFELFIVAREHANAFTELNDPIDQKERFEAQLKEREQGNDEAHMMDDDYIEALEYGMPPTGGLGIGIDRLVML 478
Cdd:PTZ00417 486 SKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCTSLEYGLPPTGGLGLGIDRITMF 565
|
490
....*....|....*..
gi 446291816 479 LTNAPSIRDVLLFPAMR 495
Cdd:PTZ00417 566 LTNKNCIKDVILFPTMR 582
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
156-495 |
1.60e-119 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 353.41 E-value: 1.60e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 156 DVEQRYRQRYLDLITSmESRETFVTRSKIIREMRRYLDDNGYLEVETPMMHAIAGGASARPFITHHNALDMELYMRIAIE 235
Cdd:pfam00152 1 DEETRLKYRYLDLRRP-KMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 236 LHLKRLIVGGLEKVYEIGRVFRNEGVSTRHNPEFTMIELYEAYADYKDIMKLTENMVAHIAKQVLGTTTIQYGDYEINLE 315
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 316 PEWTRLHMVDAIKEHSGADfwnpmsVEEARE-LAKEHnveIKDTMEVGHIINEFfeqkvedkliQPTFIYGHPVEISPLA 394
Cdd:pfam00152 160 KPFPRITYAEAIEKLNGKD------VEELGYgSDKPD---LRFLLELVIDKNKF----------NPLWVTDFPAEHHPFT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 395 KKNDED-PRFTDRFELFIVAREHANAFTELNDPIDQKERFEAQLKEREqgndEAHMMDDDYIEALEYGMPPTGGLGIGID 473
Cdd:pfam00152 221 MPKDEDdPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDPE----EAEEKFGFYLDALKYGAPPHGGLGIGLD 296
|
330 340
....*....|....*....|..
gi 446291816 474 RLVMLLTNAPSIRDVLLFPAMR 495
Cdd:pfam00152 297 RLVMLLTGLESIREVIAFPKTR 318
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
35-496 |
3.60e-117 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 358.96 E-value: 3.60e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 35 FERTNATNDLLSLYGEFSKEElEEKEISVSIAGRIMTKRGKGKAGFAHIQ----DLhgQVQIYVRKDAVGDEEYELFKTA 110
Cdd:PTZ00385 83 FRGITPISEVRERYGYLASGD-RAAQATVRVAGRVTSVRDIGKIIFVTIRsngnEL--QVVGQVGEHFTREDLKKLKVSL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 111 DLGDLVGIEGKVFKTNVGELSVKATGFTLLT------KSLRPLPDKYHGLKDVEQRYRQRYLDLITSMESRETFVTRSKI 184
Cdd:PTZ00385 160 RVGDIIGADGVPCRMQRGELSVAASRMLILSpyvctdQVVCPNLRGFTVLQDNDVKYRYRFTDMMTNPCVIETIKKRHVM 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 185 IREMRRYLDDNGYLEVETPMMHAIAGGASARPFITHHNALDMELYMRIAIELHLKRLIVGGLEKVYEIGRVFRNEGVSTR 264
Cdd:PTZ00385 240 LQALRDYFNERNFVEVETPVLHTVASGANAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRS 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 265 HNPEFTMIELYEAYADYKDIMKLTENMVAHIAKQVLGTTTIQ------YGD-YEINLEPEWTRLHMVDAIKEHSGADFWN 337
Cdd:PTZ00385 320 HNPEFTSCEFYAAYHTYEDLMPMTEDIFRQLAMRVNGTTVVQiypenaHGNpVTVDLGKPFRRVSVYDEIQRMSGVEFPP 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 338 PMSVEEARELAK------EHNVEIKDTMEVGHIINEFFEQKVEDKLIQPTFIYGHPVEISPLAKKNDEDPRFTDRFELFI 411
Cdd:PTZ00385 400 PNELNTPKGIAYmsvvmlRYNIPLPPVRTAAKMFEKLIDFFITDRVVEPTFVMDHPLFMSPLAKEQVSRPGLAERFELFV 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 412 VAREHANAFTELNDPIDQKERFEAQLKEREQGNDEAHMMDDDYIEALEYGMPPTGGLGIGIDRLVMLLTNAPSIRDVLLF 491
Cdd:PTZ00385 480 NGIEYCNAYSELNDPHEQYHRFQQQLVDRQGGDEEAMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIF 559
|
....*
gi 446291816 492 PAMRH 496
Cdd:PTZ00385 560 PLLRQ 564
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
178-495 |
1.27e-102 |
|
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: 308.25 E-value: 1.27e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 178 FVTRSKIIREMRRYLDDNGYLEVETPMMHAIAGGASARPFITHHNALDMELYMRIAIELHLKRLIVGGLEKVYEIGRVFR 257
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 258 NEGVSTRHNPEFTMIELYEAYADYKDIMKLTENMVAHIAKQVLGTTTIQYGDYEINLEPEWTRLHMVDAIKehsgadfwn 337
Cdd:cd00669 81 NEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYGFELEDFGLPFPRLTYREALE--------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 338 pmsveearelakehnveikdtmevghiineffeqkvedKLIQPTFIYGHPVEI-SPLAKKNDEDPRFTDRFELFIVAREH 416
Cdd:cd00669 152 --------------------------------------RYGQPLFLTDYPAEMhSPLASPHDVNPEIADAFDLFINGVEV 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 417 ANAFTELNDPIDQKERFeaqlkeREQGNDEAHMM--DDDYIEALEYGMPPTGGLGIGIDRLVMLLTNAPSIRDVLLFPAM 494
Cdd:cd00669 194 GNGSSRLHDPDIQAEVF------QEQGINKEAGMeyFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKM 267
|
.
gi 446291816 495 R 495
Cdd:cd00669 268 R 268
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
174-489 |
5.87e-79 |
|
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: 248.87 E-value: 5.87e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 174 SRETFVTRSKIIREMRRYLDDNGYLEVETPMMhAIAGGASA--RPFIT---HHNALDMELYMRIAIELHLKRLIVGGLEK 248
Cdd:COG2269 2 SREALRARARLLAAIRAFFAERGVLEVETPAL-SVAPGTDPhlDSFATefiGPDGGGRPLYLHTSPEFAMKRLLAAGSGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 249 VYEIGRVFRNEGVSTRHNPEFTMIELYEAYADYKDIMKLTENMVAHIAKQVLgtttiqygdyeinlEPEWTRLHMVDAIK 328
Cdd:COG2269 81 IYQIAKVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAAG--------------FAPAERLSYQEAFL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 329 EHSGADfwnPM--SVEEARELAKEHNVEIKDTMEVGHIINEFFEQKVEDKLIQ--PTFIYGHPVEISPLAKKNDEDPRFT 404
Cdd:COG2269 147 RYLGID---PLtaDLDELAAAAAAAGLRVADDDDRDDLLDLLLSERVEPQLGRdrPTFLYDYPASQAALARISPDDPRVA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 405 DRFELFIVAREHANAFTELNDPIDQKERFEAQLKEREQGNDEAHMMDDDYIEALEYGMPPTGGLGIGIDRLVMLLTNAPS 484
Cdd:COG2269 224 ERFELYACGVELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALGAER 303
|
....*
gi 446291816 485 IRDVL 489
Cdd:COG2269 304 IDDVL 308
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
191-489 |
3.45e-70 |
|
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: 225.51 E-value: 3.45e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 191 YLDDNGYLEVETPMMhAIAGGASA--RPFITH---HNALDMELYMRIAIELHLKRLIVGGLEKVYEIGRVFRNEGVSTRH 265
Cdd:TIGR00462 1 FFAERGVLEVETPLL-SPAPVTDPhlDAFATEfvgPDGQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 266 NPEFTMIELYEAYADYKDIMKLTENMVAHIAKQvlgtttiqygdyeinLEPEWTRLHMVDAIKEHSGadfWNPM--SVEE 343
Cdd:TIGR00462 80 NPEFTMLEWYRPGFDYHDLMDEVEALLQELLGD---------------PFAPAERLSYQEAFLRYAG---IDPLtaSLAE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 344 ARELAKEHNVEIKDTMEVGHIINEFFEQKVEDKLIQ--PTFIYGHPVEISPLAKKNDEDPRFTDRFELFIVAREHANAFT 421
Cdd:TIGR00462 142 LQAAAAAHGIRASEEDDRDDLLDLLFSEKVEPHLGFgrPTFLYDYPASQAALARISPDDPRVAERFELYIKGLELANGFH 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446291816 422 ELNDPIDQKERFEAQLKEREQGNDEAHMMDDDYIEALEYGMPPTGGLGIGIDRLVMLLTNAPSIRDVL 489
Cdd:TIGR00462 222 ELTDAAEQRRRFEADNALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDVL 289
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
174-488 |
4.79e-63 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 207.47 E-value: 4.79e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 174 SRETFVTRSKIIREMRRYLDDNGYLEVETPMM-HAIAGGASARPFITHHNALDME----LYMRIAIELHLKRLIVGGLEK 248
Cdd:PRK09350 1 SIPNLLKRAKIIAEIRRFFADRGVLEVETPILsQATVTDIHLVPFETRFVGPGASqgktLWLMTSPEYHMKRLLAAGSGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 249 VYEIGRVFRNEGVSTRHNPEFTMIELYEAYADYKDIMKLTENmvahIAKQVLGTTTIQYGDYEinlepewtrlhmvDAIK 328
Cdd:PRK09350 81 IFQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDD----LLQQVLDCEPAESLSYQ-------------QAFL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 329 EHSGADfwnPMSVEEA--RELAKEHNVeikdtmevGHIINE----------FFEQKVEDKLIQ--PTFIYGHPVEISPLA 394
Cdd:PRK09350 144 RYLGID---PLSADKTqlREVAAKLGL--------SNIADEeedrdtllqlLFTFGVEPNIGKekPTFVYHFPASQAALA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 395 KKNDEDPRFTDRFELFIVAREHANAFTELNDPIDQKERFEAQLKEREQGNDEAHMMDDDYIEALEYGMPPTGGLGIGIDR 474
Cdd:PRK09350 213 KISTEDHRVAERFEVYFKGIELANGFHELTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCSGVALGVDR 292
|
330
....*....|....
gi 446291816 475 LVMLLTNAPSIRDV 488
Cdd:PRK09350 293 LIMLALGAESISEV 306
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
62-168 |
2.71e-57 |
|
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: 185.37 E-value: 2.71e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 62 SVSIAGRIMTKRGKGKAGFAHIQDLHGQVQIYVRKDAVGDEEYELFKTA-DLGDLVGIEGKVFKTNVGELSVKATGFTLL 140
Cdd:cd04322 1 EVSVAGRIMSKRGSGKLSFADLQDESGKIQVYVNKDDLGEEEFEDFKKLlDLGDIIGVTGTPFKTKTGELSIFVKEFTLL 80
|
90 100
....*....|....*....|....*...
gi 446291816 141 TKSLRPLPDKYHGLKDVEQRYRQRYLDL 168
Cdd:cd04322 81 SKSLRPLPEKFHGLTDVETRYRQRYLDL 108
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
63-496 |
2.01e-49 |
|
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: 175.24 E-value: 2.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 63 VSIAGRIMTKRGKGKAGFAHIQDLHGQVQIYVRKDAVgdEEYELFKTADLGDLVGIEGKVFKTN--VGELSVKATGFTLL 140
Cdd:COG0017 17 VTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKL--ENFEEAKKLTTESSVEVTGTVVESPraPQGVELQAEEIEVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 141 TKSLRPLP-DKY-HGLkdvEQRYRQRYLDLITSmESRETFVTRSKIIREMRRYLDDNGYLEVETPMMHAIA--GGAS--- 213
Cdd:COG0017 95 GEADEPYPlQPKrHSL---EFLLDNRHLRLRTN-RFGAIFRIRSELARAIREFFQERGFVEVHTPIITASAteGGGElfp 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 214 ----ARP-FITHHNALDMELYMriaielhlkrlivGGLEKVYEIGRVFRNEGVST-RHNPEFTMIELYEAYADYKDIMKL 287
Cdd:COG0017 171 vdyfGKEaYLTQSGQLYKEALA-------------MALEKVYTFGPTFRAEKSNTrRHLAEFWMIEPEMAFADLEDVMDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 288 TENMVAHIAKQVLgtttiQYGDYEIN-LEPEWTRLHMVdaIKehsgADFwnP-MSVEEARELAKEHNVEIKDTMEVG--- 362
Cdd:COG0017 238 AEEMLKYIIKYVL-----ENCPEELEfLGRDVERLEKV--PE----SPF--PrITYTEAIEILKKSGEKVEWGDDLGteh 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 363 -HIINEFFEQKvedkliqPTFIYGHPVEISPL-AKKNDEDPRFTDRFELF------IVA---REHanaftelndpidqke 431
Cdd:COG0017 305 eRYLGEEFFKK-------PVFVTDYPKEIKAFyMKPNPDDPKTVAAFDLLapgigeIIGgsqREH--------------- 362
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446291816 432 RFEaQLKER--EQGNDEAHMmdDDYIEALEYGMPPTGGLGIGIDRLVMLLTNAPSIRDVLLFPAMRH 496
Cdd:COG0017 363 RYD-VLVERikEKGLDPEDY--EWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPG 426
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
53-496 |
3.90e-44 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 161.13 E-value: 3.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 53 KEELEEKEisVSIAGRIMTKRGKGKAGFAHIQDLHGQVQIYVRKDAVgDEEYELFKTADLGDLVGIEGKVFKTNV--GEL 130
Cdd:PRK05159 11 TPELDGEE--VTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKVD-EELFETIKKLKRESVVSVTGTVKANPKapGGV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 131 SVKATGFTLLTKSLRPLPDKYHG--LKDVEQRYRQRYLDLiTSMESRETFVTRSKIIREMRRYLDDNGYLEVETPMMHAI 208
Cdd:PRK05159 88 EVIPEEIEVLNKAEEPLPLDISGkvLAELDTRLDNRFLDL-RRPRVRAIFKIRSEVLRAFREFLYENGFTEIFTPKIVAS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 209 A--GGASARPfITHhnaLDMELYMRIAIELHlKRLIVG-GLEKVYEIGRVFRNEGVST-RHNPEFTMIELYEAYAD-YKD 283
Cdd:PRK05159 167 GteGGAELFP-IDY---FEKEAYLAQSPQLY-KQMMVGaGFERVFEIGPVFRAEEHNTsRHLNEYTSIDVEMGFIDdHED 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 284 IMKLTENMVAHIAKQVLGTTTIQYGDYEINL---EPEWTRLHMvdaikehsgadfwnpmsvEEARELAKEHNVEIKDTME 360
Cdd:PRK05159 242 VMDLLENLLRYMYEDVAENCEKELELLGIELpvpETPIPRITY------------------DEAIEILKSKGNEISWGDD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 361 VG----HIINEFFEQKVEDKLIqptFIYGHPVEISPL-AKKNDEDPRFTDRFELF-----IVA---REHanaftelndpi 427
Cdd:PRK05159 304 LDtegeRLLGEYVKEEYGSDFY---FITDYPSEKRPFyTMPDEDDPEISKSFDLLfrgleITSggqRIH----------- 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446291816 428 dQKERFEAQLKEReqGNDEAHMmdDDYIEALEYGMPPTGGLGIGIDRLVMLLTNAPSIRDVLLFPAMRH 496
Cdd:PRK05159 370 -RYDMLVESIKEK--GLNPESF--EFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFPRDRH 433
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
53-497 |
1.77e-41 |
|
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: 153.83 E-value: 1.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 53 KEELEEKEisVSIAGRIMTKRGKGKAGFAHIQDLHGQVQIYVRKDAVGDEEYELFKTADLGDLVGIEGKVFKTN--VGEL 130
Cdd:TIGR00458 7 KPEMDGQE--VTFMGWVHEIRDLGGLIFVLLRDREGLIQITAPAKKVSKNLFKWAKKLNLESVVAVRGIVKIKEkaPGGF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 131 SVKATGFTLLTKSLRPLP----DKYHGlkDVEQRYRQRYLDLITSmESRETFVTRSKIIREMRRYLDDNGYLEVETPMMH 206
Cdd:TIGR00458 85 EIIPTKIEVINEAKEPLPldptEKVPA--ELDTRLDYRFLDLRRP-TVQAIFRIRSGVLESVREFLAEEGFIEVHTPKLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 207 AIA--GGASARPfITHhnaLDMELYMRIAIELHLKRLIVGGLEKVYEIGRVFRNEGVST-RHNPEFTMIELYEAYADYKD 283
Cdd:TIGR00458 162 ASAteGGTELFP-ITY---FEREAFLGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNThRHLNEATSIDIEMAFEDHHD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 284 IMKLTENMVAHIAKQVLGTTTIQYGDYEINLEPEWTRLhmvdaikehsgadfwNPMSVEEARELAKEHNVEIKDtmevGH 363
Cdd:TIGR00458 238 VMDILEELVVRVFEDVPERCAHQLETLEFKLEKPEGKF---------------VRLTYDEAIEMANAKGVEIGW----GE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 364 IINEFFEQKVEDKLIQPTFIYGHPVEISPLAKKNDED-PRFTDRFELFIVAREHANAFTELNDPIDQKERFEAQLKEREQ 442
Cdd:TIGR00458 299 DLSTEAEKALGEEMDGLYFITDWPTEIRPFYTMPDEDnPEISKSFDLMYRDLEISSGAQRIHLHDLLVERIKAKGLNPEG 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 446291816 443 GndeahmmdDDYIEALEYGMPPTGGLGIGIDRLVMLLTNAPSIRDVLLFPAMRHK 497
Cdd:TIGR00458 379 F--------KDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFPRDRKR 425
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
156-492 |
1.34e-38 |
|
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: 143.09 E-value: 1.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 156 DVEQRYR--QRYLDLITSmESRETFVTRSKIIREMRRYLDDNGYLEVETPMMHAIA--GGASARPFithhNALDMELYMR 231
Cdd:cd00776 1 DANLETLldNRHLDLRTP-KVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDteGGAELFKV----SYFGKPAYLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 232 IAIELHLKRLIvGGLEKVYEIGRVFRNEGVST-RHNPEFTMIELYEAYA-DYKDIMKLTENMVAHIAKQVL------GTT 303
Cdd:cd00776 76 QSPQLYKEMLI-AALERVYEIGPVFRAEKSNTrRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLercakeLEL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 304 TIQYGDYEINLEPEWTRlhmvdaikehsgadfwnpMSVEEARELAKEHNV--EIKDTMEVGHIINEFFEQKVEDKLIqpt 381
Cdd:cd00776 155 VNQLNRELLKPLEPFPR------------------ITYDEAIELLREKGVeeEVKWGEDLSTEHERLLGEIVKGDPV--- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 382 FIYGHPVEISPL-AKKNDEDPRFTDRFELF------IVA---REHanaftelnDPIDQKERFEaqlkerEQGNDEAHMmd 451
Cdd:cd00776 214 FVTDYPKEIKPFyMKPDDDNPETVESFDLLmpgvgeIVGgsqRIH--------DYDELEERIK------EHGLDPESF-- 277
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 446291816 452 DDYIEALEYGMPPTGGLGIGIDRLVMLLTNAPSIRDVLLFP 492
Cdd:cd00776 278 EWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
178-492 |
4.52e-33 |
|
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: 126.92 E-value: 4.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 178 FVTRSKIIREMRRYLDDNGYLEVETPMMhaiagGAS----ARPFI----THHN---ALDM--ELYMRIaielhlkrLIVG 244
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPIL-----TKStpegARDFLvpsrLHPGkfyALPQspQLFKQL--------LMVS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 245 GLEKVYEIGRVFRNEGVSTRHNPEFTMIELYEAYADYKDIMKLTENMVAHIAKQVLGtttiqygdyeINLEPEWTRLHMV 324
Cdd:cd00777 68 GFDRYFQIARCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG----------VELTTPFPRMTYA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 325 DAIKEHSGADFWnpmsveearelakehnveikdtmevghiINEF--FEQKVEDKLIQPTFiygHPV-----EISPLAKKN 397
Cdd:cd00777 138 EAMERYGFKFLW----------------------------IVDFplFEWDEEEGRLVSAH---HPFtapkeEDLDLLEKD 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 398 DEDPRfTDRFELFIVAREHANAFTELNDPIDQKERFEAQLKEREQGNDE-AHMMdddyiEALEYGMPPTGGLGIGIDRLV 476
Cdd:cd00777 187 PEDAR-AQAYDLVLNGVELGGGSIRIHDPDIQEKVFEILGLSEEEAEEKfGFLL-----EAFKYGAPPHGGIALGLDRLV 260
|
330
....*....|....*.
gi 446291816 477 MLLTNAPSIRDVLLFP 492
Cdd:cd00777 261 MLLTGSESIRDVIAFP 276
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
49-492 |
6.48e-30 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 123.25 E-value: 6.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 49 GEFSKEELEEKeisVSIAGRIMTKRGKGKAGFAHIQDLHGQVQIyvrkdaVGDEEYELFKTAD-LG--DLVGIEGKV--- 122
Cdd:PRK00476 9 GELRESHVGQT---VTLCGWVHRRRDHGGLIFIDLRDREGIVQV------VFDPDAEAFEVAEsLRseYVIQVTGTVrar 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 123 --------FKTnvGELSVKATGFTLLTKSlRPLPDKYHGLKDV--EQRYRQRYLDLITSmESRETFVTRSKIIREMRRYL 192
Cdd:PRK00476 80 pegtvnpnLPT--GEIEVLASELEVLNKS-KTLPFPIDDEEDVseELRLKYRYLDLRRP-EMQKNLKLRSKVTSAIRNFL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 193 DDNGYLEVETPMMhaiagGAS----ARPFI----THHN---ALDM------ELYMriaielhlkrliVGGLEKVYEIGRV 255
Cdd:PRK00476 156 DDNGFLEIETPIL-----TKStpegARDYLvpsrVHPGkfyALPQspqlfkQLLM------------VAGFDRYYQIARC 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 256 FRNEGVSTRHNPEFTMIELYEAYADYKDIMKLTENMVAHIAKQVLGtttiqygdyeINLEPEWTRLHMVDAIKEHsGA-- 333
Cdd:PRK00476 219 FRDEDLRADRQPEFTQIDIEMSFVTQEDVMALMEGLIRHVFKEVLG----------VDLPTPFPRMTYAEAMRRY-GSdk 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 334 -DFWNPMSVEEARELAKEHNVEI-KDTMEVGHII--------NEFFEQKVEDKLIQPTFIYGHP------VE----ISPL 393
Cdd:PRK00476 288 pDLRFGLELVDVTDLFKDSGFKVfAGAANDGGRVkairvpggAAQLSRKQIDELTEFAKIYGAKglayikVNedglKGPI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 394 AKKNDEDPR--FTDRFE------LFIVA-------------REHA----------------------------------- 417
Cdd:PRK00476 368 AKFLSEEELaaLLERTGakdgdlIFFGAdkakvvndalgalRLKLgkelglidedkfaflwvvdfpmfeydeeegrwvaa 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 418 -NAFT----------ELNDPID---------------------------QKERFEA-QLKEREQGNDEAHMMDddyieAL 458
Cdd:PRK00476 448 hHPFTmpkdedldelETTDPGKarayaydlvlngyelgggsirihrpeiQEKVFEIlGISEEEAEEKFGFLLD-----AL 522
|
570 580 590
....*....|....*....|....*....|....
gi 446291816 459 EYGMPPTGGLGIGIDRLVMLLTNAPSIRDVLLFP 492
Cdd:PRK00476 523 KYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
49-492 |
7.98e-25 |
|
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: 107.78 E-value: 7.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 49 GEFSKEELEEKeisVSIAGRIMTKRGKGKAGFAHIQDLHGQVQIYVRKDAVGdeeyELFKTADlgDL-----VGIEGKVF 123
Cdd:COG0173 8 GELRESDVGQE---VTLSGWVHRRRDHGGLIFIDLRDRYGITQVVFDPDDSA----EAFEKAE--KLrseyvIAVTGKVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 124 K-----------TnvGELSVKATGFTLLTKSlRPLPDKYHGLKDV--EQRYRQRYLDLITSmESRETFVTRSKIIREMRR 190
Cdd:COG0173 79 ArpegtvnpklpT--GEIEVLASELEILNKA-KTPPFQIDDDTDVseELRLKYRYLDLRRP-EMQKNLILRHKVTKAIRN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 191 YLDDNGYLEVETPMMhaiagGAS----ARPFI----THHN---ALDM--ELYmriaielhlKRLI-VGGLEKVYEIGRVF 256
Cdd:COG0173 155 YLDENGFLEIETPIL-----TKStpegARDYLvpsrVHPGkfyALPQspQLF---------KQLLmVSGFDRYFQIARCF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 257 RNEgvSTRHN--PEFTMIELYEAYADYKDIMKLTENMVAHIAKQVLGtttiqygdyeINLEPEWTR-------------- 320
Cdd:COG0173 221 RDE--DLRADrqPEFTQLDIEMSFVDQEDVFELMEGLIRHLFKEVLG----------VELPTPFPRmtyaeamerygsdk 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 321 ------LHMVD------------------------AIKEHSGADF---------------------WnpMSVEE------ 343
Cdd:COG0173 289 pdlrfgLELVDvtdifkdsgfkvfagaaenggrvkAINVPGGASLsrkqideltefakqygakglaY--IKVNEdglksp 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 344 -ARELAKEHNVEIKDTM--EVGHIIneFF----EQKVED-------------KLIQP-TFiygHPVEIS--PLAKKNDED 400
Cdd:COG0173 367 iAKFLSEEELAAILERLgaKPGDLI--FFvadkPKVVNKalgalrlklgkelGLIDEdEF---AFLWVVdfPLFEYDEEE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 401 PR-------FT----DRFELFIVAREHANAF--------TEL-------NDPIDQKERFEA-QLKEREQGNDEAHMMDdd 453
Cdd:COG0173 442 GRwvamhhpFTmpkdEDLDLLETDPGKVRAKaydlvlngYELgggsiriHDPELQEKVFELlGISEEEAEEKFGFLLE-- 519
|
570 580 590
....*....|....*....|....*....|....*....
gi 446291816 454 yieALEYGMPPTGGLGIGIDRLVMLLTNAPSIRDVLLFP 492
Cdd:COG0173 520 ---AFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
53-492 |
2.26e-24 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 106.33 E-value: 2.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 53 KEELEEKEisVSIAGRIMTKRGKGKAGFAHIQDLHGQVQ--IYVRKDAVGDEEYELFKTADLGDLVGIEGKV------FK 124
Cdd:PLN02850 76 GEELAGSE--VLIRGRVHTIRGKGKSAFLVLRQSGFTVQcvVFVSEVTVSKGMVKYAKQLSRESVVDVEGVVsvpkkpVK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 125 TNVGELSVKATGFTLLTKSLRPLP-----------DKYHGLKDVEQ--------RYRQRYLDLITSmESRETFVTRSKII 185
Cdd:PLN02850 154 GTTQQVEIQVRKIYCVSKALATLPfnvedaarsesEIEKALQTGEQlvrvgqdtRLNNRVLDLRTP-ANQAIFRIQSQVC 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 186 REMRRYLDDNGYLEVETPMMHAIA--GGASArpFITHHNALDMELYMriAIELHLKRLIVGGLEKVYEIGRVFRNEGVST 263
Cdd:PLN02850 233 NLFREFLLSKGFVEIHTPKLIAGAseGGSAV--FRLDYKGQPACLAQ--SPQLHKQMAICGDFRRVFEIGPVFRAEDSFT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 264 -RHNPEFTMIEL-YEAYADYKDIMKLTENMVAHI-------AKQVLGTTTIQYGDYEINLEPEWTRLHMvdaikehsgad 334
Cdd:PLN02850 309 hRHLCEFTGLDLeMEIKEHYSEVLDVVDELFVAIfdglnerCKKELEAIREQYPFEPLKYLPKTLRLTF----------- 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 335 fwnpmsvEEARELAKEHNVEIkDTMEvghIINEFFEQK----VEDKLIQPTFI-YGHPVEISPLAKKND-EDPRFTDRFE 408
Cdd:PLN02850 378 -------AEGIQMLKEAGVEV-DPLG---DLNTESERKlgqlVKEKYGTDFYIlHRYPLAVRPFYTMPCpDDPKYSNSFD 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 409 LFIVAREHANAFTELNDPIDQKERFEAQLKEREQGNDeahmmdddYIEALEYGMPPTGGLGIGIDRLVMLLTNAPSIRDV 488
Cdd:PLN02850 447 VFIRGEEIISGAQRVHDPELLEKRAEECGIDVKTIST--------YIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKT 518
|
....
gi 446291816 489 LLFP 492
Cdd:PLN02850 519 SLFP 522
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
51-492 |
1.03e-22 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 100.57 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 51 FSKEELEEKeisVSIAGRIMTKRGKGKAGFAHIQDLHGQVQIYVRKDAvGDEEYELFKTADLGDLVGIEGKVFKTN--VG 128
Cdd:PRK03932 10 LKGKYVGQE---VTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDN-GEEYFEEIKKLTTGSSVIVTGTVVESPraGQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 129 ELSVKATGFTLLTKSLR--PLPDKYHG---LKDVeqryrqRYLDLITSMESrETFVTRSKIIREMRRYLDDNGYLEVETP 203
Cdd:PRK03932 86 GYELQATKIEVIGEDPEdyPIQKKRHSiefLREI------AHLRPRTNKFG-AVMRIRNTLAQAIHEFFNENGFVWVDTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 204 MMHAIAGGASARPFITHHNALDME---------------LYMRIAIElhlkrlivgGLEKVYEIGRVFRNEGVST-RHNP 267
Cdd:PRK03932 159 IITASDCEGAGELFRVTTLDLDFSkdffgkeayltvsgqLYAEAYAM---------ALGKVYTFGPTFRAENSNTrRHLA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 268 EFTMIELYEAYADYKDIMKLTENMVAHIAKQVLGT---------TTIQYGDYEI---NLEPEWTRLHMVDAIK--EHSGA 333
Cdd:PRK03932 230 EFWMIEPEMAFADLEDNMDLAEEMLKYVVKYVLENcpddleflnRRVDKGDIERlenFIESPFPRITYTEAIEilQKSGK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 334 DFWNP------MSVEEARELAKEHnveikdtmevghiinefFEqkvedkliQPTFIYGHPVEISPLAKKNDEDPRftdrf 407
Cdd:PRK03932 310 KFEFPvewgddLGSEHERYLAEEH-----------------FK--------KPVFVTNYPKDIKAFYMRLNPDGK----- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 408 elfIVA-----------------REhanaftelndpidqkERFEaQLKER--EQGNDEAHMmdDDYIEALEYGMPPTGGL 468
Cdd:PRK03932 360 ---TVAamdllapgigeiiggsqRE---------------ERLD-VLEARikELGLNKEDY--WWYLDLRRYGSVPHSGF 418
|
490 500
....*....|....*....|....
gi 446291816 469 GIGIDRLVMLLTNAPSIRDVLLFP 492
Cdd:PRK03932 419 GLGFERLVAYITGLDNIRDVIPFP 442
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
51-492 |
1.24e-21 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 98.14 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 51 FSKEELEEKeiSVSIAGRIMTKRGKGKAGFAHIQDLHGQVQIYVR-KDAVGDEEYELFKTADLGDLVGIEGKVFK----- 124
Cdd:PTZ00401 71 LSKPELVDK--TVLIRARVSTTRKKGKMAFMVLRDGSDSVQAMAAvEGDVPKEMIDFIGQIPTESIVDVEATVCKveqpi 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 125 --TNVGELSVKATGFTLLTKSLRPLP---------DKYHGLK-DVEQRYRQRYLDLITSmESRETFVTRSKIIREMRRYL 192
Cdd:PTZ00401 149 tsTSHSDIELKVKKIHTVTESLRTLPftledasrkESDEGAKvNFDTRLNSRWMDLRTP-ASGAIFRLQSRVCQYFRQFL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 193 DDNGYLEVETPMMHAIAGGASARPFITHHnaLDMELYMRIAIELHLKRLIVGGLEKVYEIGRVFRNEGVST-RHNPEFTM 271
Cdd:PTZ00401 228 IDSDFCEIHSPKIINAPSEGGANVFKLEY--FNRFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNThRHLTEFVG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 272 IELyEAYAD--YKDIMKLTENMVAHIAKQVLGTTT------IQYgDYE---INLEPEWTRLHMVDAIKEHSgadfwNPMS 340
Cdd:PTZ00401 306 LDV-EMRINehYYEVLDLAESLFNYIFERLATHTKelkavcQQY-PFEplvWKLTPERMKELGVGVISEGV-----EPTD 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 341 VEEARelakEHNVEIK----DTMEVGHIINEFFEQKVE-------------DKLIQPTfiYGHPVEIS---PLAKKN--- 397
Cdd:PTZ00401 379 KYQAR----VHNMDSRmlriNYMHCIELLNTVLEEKMAptddinttnekllGKLVKER--YGTDFFISdrfPSSARPfyt 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 398 ---DEDPRFTDRFELFIVAREHANAFTELNDPidqkerfeAQLKEREQGNDEAHMMDDDYIEALEYGMPPTGGLGIGIDR 474
Cdd:PTZ00401 453 mecKDDERFTNSYDMFIRGEEISSGAQRIHDP--------DLLLARAKMLNVDLTPIKEYVDSFRLGAWPHGGFGVGLER 524
|
490
....*....|....*...
gi 446291816 475 LVMLLTNAPSIRDVLLFP 492
Cdd:PTZ00401 525 VVMLYLGLSNVRLASLFP 542
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
169-492 |
3.00e-21 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 94.70 E-value: 3.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 169 ITSMESRETFVTRSKIIREMRRYLDDNGYLEVETPM--------MHAIAGGASARPFIthhNALDMELYMRIAIELHlKR 240
Cdd:PRK06462 21 ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIispstdplMGLGSDLPVKQISI---DFYGVEYYLADSMILH-KQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 241 LIVGGLEKVYEIGRVFRNEGV---STRHNPEFTMIELYEAYADYKDIMKLTENMVAHIAKQVLGTTTIQYGDYEINLePE 317
Cdd:PRK06462 97 LALRMLGKIFYLSPNFRLEPVdkdTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHEDELEFFGRDL-PH 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 318 WTRlhmvdaikehsgaDFWNpMSVEEARELAKEHNVEIKDTMEvghiINEFFEQKVEDKLIQPTFIYGHPVEISPLAKKN 397
Cdd:PRK06462 176 LKR-------------PFKR-ITHKEAVEILNEEGCRGIDLEE----LGSEGEKSLSEHFEEPFWIIDIPKGSREFYDRE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 398 DED-PRFTDRFELFIV----------AREHanaftELNDPIDqkerfeaqlKEREQGNDEAHMmdDDYIEALEYGMPPTG 466
Cdd:PRK06462 238 DPErPGVLRNYDLLLPegygeavsggEREY-----EYEEIVE---------RIREHGVDPEKY--KWYLEMAKEGPLPSA 301
|
330 340
....*....|....*....|....*.
gi 446291816 467 GLGIGIDRLVMLLTNAPSIRDVLLFP 492
Cdd:PRK06462 302 GFGIGVERLTRYICGLRHIREVQPFP 327
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
63-492 |
1.25e-20 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 95.24 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 63 VSIAGRIMTKRGKGKAGFAHIQDLHGQVQIYVRKDAVgDEEYELFKTADLGDLVGIEGKVF---------KTNVGELSVK 133
Cdd:PLN02903 75 VTLCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDEF-PEAHRTANRLRNEYVVAVEGTVRsrpqespnkKMKTGSVEVV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 134 ATGFTLLTKSLRPLP-------DKYHGLKDvEQRYRQRYLDLITSMESReTFVTRSKIIREMRRYL-DDNGYLEVETPMM 205
Cdd:PLN02903 154 AESVDILNVVTKSLPflvttadEQKDSIKE-EVRLRYRVLDLRRPQMNA-NLRLRHRVVKLIRRYLeDVHGFVEIETPIL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 206 haiaggasARPfiTHHNALDMELYMRI----------AIELHLKRLIVGGLEKVYEIGRVFRNEGVSTRHNPEFTMIELY 275
Cdd:PLN02903 232 --------SRS--TPEGARDYLVPSRVqpgtfyalpqSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEFTQLDME 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 276 EAYADYKDIMKLTENMVAHIAKQVLGTT----------------------TIQYGDYEINLEPEWTRLH----------- 322
Cdd:PLN02903 302 LAFTPLEDMLKLNEDLIRQVFKEIKGVQlpnpfprltyaeamskygsdkpDLRYGLELVDVSDVFAESSfkvfagalesg 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 323 -MVDAIKEHSGA-----------DFWNPMSVEEARELAKEhNVEIKDTMEVGHIINEFFEQKVEDKLIQPT--------- 381
Cdd:PLN02903 382 gVVKAICVPDGKkisnntalkkgDIYNEAIKSGAKGLAFL-KVLDDGELEGIKALVESLSPEQAEQLLAACgagpgdlil 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 382 FIYGHPVEIS------------------------------PLAKKNDEDPR-------FT----DRFELFIVARehANAF 420
Cdd:PLN02903 461 FAAGPTSSVNktldrlrqfiaktldlidpsrhsilwvtdfPMFEWNEDEQRlealhhpFTapnpEDMGDLSSAR--ALAY 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 421 TELNDPID-------------QKERFEA-QLKEREQGNDEAHMMdddyiEALEYGMPPTGGLGIGIDRLVMLLTNAPSIR 486
Cdd:PLN02903 539 DMVYNGVEigggslriyrrdvQQKVLEAiGLSPEEAESKFGYLL-----EALDMGAPPHGGIAYGLDRLVMLLAGAKSIR 613
|
....*.
gi 446291816 487 DVLLFP 492
Cdd:PLN02903 614 DVIAFP 619
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
63-495 |
6.25e-19 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 90.05 E-value: 6.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 63 VSIAGRIMTKRGKGKAGFAHIQDLHGQVQIYVRKDAVGDEEYELFKTADLGDLVGIEGKVFK---------TNVGELSVK 133
Cdd:PRK12820 21 VCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFSPEAAPADVYELAASLRAEFCVALQGEVQKrleetenphIETGDIEVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 134 ATGFTLLTKSLR---PLPDKY-----------HGLKDVEQRYRqrYLDLI-TSMEsrETFVTRSKIIREMRRYLDDNGYL 198
Cdd:PRK12820 101 VRELSILAASEAlpfAISDKAmtagagsagadAVNEDLRLQYR--YLDIRrPAMQ--DHLAKRHRIIKCARDFLDSRGFL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 199 EVETPMMhAIAGGASARPFITHHNALDMELY-MRIAIELHLKRLIVGGLEKVYEIGRVFRNEGVSTRHNPEFTMIELYEA 277
Cdd:PRK12820 177 EIETPIL-TKSTPEGARDYLVPSRIHPKEFYaLPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEFTQLDIEAS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 278 YADYKDIMKLTENMVAHIAK----------------QVLGTTTIQYGDYEINLEP-------EWTRLHMVDAIKEHSGAD 334
Cdd:PRK12820 256 FIDEEFIFELIEELTARMFAiggialprpfprmpyaEAMDTTGSDRPDLRFDLKFadatdifENTRYGIFKQILQRGGRI 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 335 ------------FWNPMSVEEARELAKEHNVEIKDTMEV------GHIINEFFEQKVE-----------DKLIQ------ 379
Cdd:PRK12820 336 kginikgqseklSKNVLQNEYAKEIAPSFGAKGMTWMRAeaggldSNIVQFFSADEKEalkrrfhaedgDVIIMiadasc 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 380 ---------------------PTFIYgHPVEIS--PLAKKNDED-----------PRFTD---------------RFELF 410
Cdd:PRK12820 416 aivlsalgqlrlhladrlgliPEGVF-HPLWITdfPLFEATDDGgvtsshhpftaPDREDfdpgdieelldlrsrAYDLV 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 411 IVAREHANAFTELNDPIDQKERFEA-QLKEREQGNDEAHmmdddYIEALEYGMPPTGGLGIGIDRLVMLLTNAPSIRDVL 489
Cdd:PRK12820 495 VNGEELGGGSIRINDKDIQLRIFAAlGLSEEDIEDKFGF-----FLRAFDFAAPPHGGIALGLDRVVSMILQTPSIREVI 569
|
....*.
gi 446291816 490 LFPAMR 495
Cdd:PRK12820 570 AFPKNR 575
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
180-392 |
3.49e-16 |
|
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: 77.16 E-value: 3.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 180 TRSKIIREMRRYLDDNGYLEVETPMMHAIAGGASAR----PFITHHNALDMELYMRIAIELHLKRLIVGGL----EKVYE 251
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGhepkDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIrklpLRLAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 252 IGRVFRNEG--VSTRHNPEFTMIELYEAYAD------YKDIMKLTENMVAHIAkqVLGTTTIQYGDYEINLEPEWTRlhm 323
Cdd:cd00768 81 IGPAFRNEGgrRGLRRVREFTQLEGEVFGEDgeeaseFEELIELTEELLRALG--IKLDIVFVEKTPGEFSPGGAGP--- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446291816 324 vdaikehsGADFWNPMSVEEARELakehnveikdtmEVGHIINEFFEQKVEDKLIQPTFIYGHPVEISP 392
Cdd:cd00768 156 --------GFEIEVDHPEGRGLEI------------GSGGYRQDEQARAADLYFLDEALEYRYPPTIGF 204
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
63-140 |
1.80e-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: 71.11 E-value: 1.80e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446291816 63 VSIAGRIMTK-RGKGKAGFAHIQDLHGQVQIYVRKDAVgdeeYELFKTADLGDLVGIEGKVFKTNVGELSVKATGFTLL 140
Cdd:pfam01336 1 VTVAGRVTSIrRSGGKLLFLTLRDGTGSIQVVVFKEEA----EKLAKKLKEGDVVRVTGKVKKRKGGELELVVEEIELL 75
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
63-142 |
4.35e-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: 4.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 63 VSIAGRIMTKRGKGKAGFAHIQDLHGQVQIYVRKDaVGDEEYELFKTADLGDLVGIEGKVFKTN-----VGELSVKATGF 137
Cdd:cd04100 2 VTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKE-ELGEFFEEAEKLRTESVVGVTGTVVKRPegnlaTGEIELQAEEL 80
|
....*
gi 446291816 138 TLLTK 142
Cdd:cd04100 81 EVLSK 85
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
227-492 |
5.64e-13 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 71.21 E-value: 5.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 227 ELYMRIAIELHLKRLiVGGLEKVYEIGRVFRNEGVST-RHNPEFTMIELYEAYADYKDIMKLTENMVAHIAKQVLGTTTI 305
Cdd:PTZ00425 325 QAFLTVSGQLSLENL-CSSMGDVYTFGPTFRAENSHTsRHLAEFWMIEPEIAFADLYDNMELAESYIKYCIGYVLNNNFD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 306 QYGDYEINLEPewtrlHMVDAIKEHSGADFwNPMSVEEARELAKEHNVEIKDTMEVGHIINEFFEQKVEDKLIQ-PTFIY 384
Cdd:PTZ00425 404 DIYYFEENVET-----GLISRLKNILDEDF-AKITYTNVIDLLQPYSDSFEVPVKWGMDLQSEHERFVAEQIFKkPVIVY 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 385 GHPVEISPLAKKNDEDPRFTDRFELFIVAREHANAFTELNDPIdqkERFEAQLKEREQgNDEAHMMdddYIEALEYGMPP 464
Cdd:PTZ00425 478 NYPKDLKAFYMKLNEDQKTVAAMDVLVPKIGEVIGGSQREDNL---ERLDKMIKEKKL-NMESYWW---YRQLRKFGSHP 550
|
250 260
....*....|....*....|....*...
gi 446291816 465 TGGLGIGIDRLVMLLTNAPSIRDVLLFP 492
Cdd:PTZ00425 551 HAGFGLGFERLIMLVTGVDNIKDTIPFP 578
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
246-492 |
2.35e-11 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 66.15 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 246 LEKVYEIGRVFRNEGVST-RHNPEFTMIELYEAYADYKDIMKLTENMVAHIAKQVLGTTTiqygdYEINLEPEWTRLHMV 324
Cdd:PLN02603 321 LSDVYTFGPTFRAENSNTsRHLAEFWMIEPELAFADLNDDMACATAYLQYVVKYILENCK-----EDMEFFNTWIEKGII 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 325 DAIKEHSGADFWNpMSVEEARELAKEHNVEIKDTMEVGHIINEFFEQKVEDKLI--QPTFIYGHPVEISPLAKKNDEDPR 402
Cdd:PLN02603 396 DRLSDVVEKNFVQ-LSYTDAIELLLKAKKKFEFPVKWGLDLQSEHERYITEEAFggRPVIIRDYPKEIKAFYMRENDDGK 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 403 FTDRFELfIVARehanaFTELNDPIDQKERF---EAQLKEREQgNDEAHMMdddYIEALEYGMPPTGGLGIGIDRLVMLL 479
Cdd:PLN02603 475 TVAAMDM-LVPR-----VGELIGGSQREERLeylEARLDELKL-NKESYWW---YLDLRRYGSVPHAGFGLGFERLVQFA 544
|
250
....*....|...
gi 446291816 480 TNAPSIRDVLLFP 492
Cdd:PLN02603 545 TGIDNIRDAIPFP 557
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
246-499 |
8.73e-10 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 61.16 E-value: 8.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 246 LEKVYEIGRVFRNEGVST-RHNPEFTMIELYEAYADYKDIMKLTENMVAHIAKQVLGTTtiqYGDYEI---NLEPEWT-R 320
Cdd:PLN02221 326 LSSVYTFGPTFRAENSHTsRHLAEFWMVEPEIAFADLEDDMNCAEAYVKYMCKWLLDKC---FDDMELmakNFDSGCIdR 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 321 LHMVDAIKehsgadfWNPMSVEEARELAKE---HNVEIKDTMEVGHIINEFFEQKVEDKLIQ-PTFIYGHPVEISPLAKK 396
Cdd:PLN02221 403 LRMVASTP-------FGRITYTEAIELLEEavaKGKEFDNNVEWGIDLASEHERYLTEVLFQkPLIVYNYPKGIKAFYMR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 397 NDEDPRFTDRFELFIvarehaNAFTELNDPIDQKERFEAqLKEREQGNDEAHMMDDDYIEALEYGMPPTGGLGIGIDRLV 476
Cdd:PLN02221 476 LNDDEKTVAAMDVLV------PKVGELIGGSQREERYDV-IKQRIEEMGLPIEPYEWYLDLRRYGTVKHCGFGLGFERMI 548
|
250 260
....*....|....*....|...
gi 446291816 477 MLLTNAPSIRDVLLFPAMRHKQD 499
Cdd:PLN02221 549 LFATGIDNIRDVIPFPRYPGKAD 571
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
49-168 |
2.34e-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: 46.75 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 49 GEFSKEELEEKeisVSIAGRIMTKRGKGKAGFAHIQDLHGQVQIYVRKDAvgDEEYELFKTADLGDLVGIEGKVFK---- 124
Cdd:cd04317 6 GELRESHVGQE---VTLCGWVQRRRDHGGLIFIDLRDRYGIVQVVFDPEE--APEFELAEKLRNESVIQVTGKVRArpeg 80
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 446291816 125 -TN----VGELSVKATGFTLLTKSlRPLP----DKYHGLKDVEQRYrqRYLDL 168
Cdd:cd04317 81 tVNpklpTGEIEVVASELEVLNKA-KTLPfeidDDVNVSEELRLKY--RYLDL 130
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| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
53-149 |
8.15e-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: 38.84 E-value: 8.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291816 53 KEELEEKEisVSIAGRIMTKRGKGKAGFAHIQDLHGQVQIYVRKDAVGDEEYELFKTADLGDLVGIEGKVfktnvgELSV 132
Cdd:cd04316 7 TPELDGEE--VTVAGWVHEIRDLGGIKFVILRDREGIVQVTAPKKKVDKELFKTVRKLSRESVISVTGTV------KAEP 78
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90 100
....*....|....*....|....*
gi 446291816 133 KA-TGF-------TLLTKSLRPLPD 149
Cdd:cd04316 79 KApNGVeiipeeiEVLSEAKTPLPL 103
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