|
Name |
Accession |
Description |
Interval |
E-value |
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
4-494 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 820.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 4 NILEQQRIQKANELKNAGVNPYPHFLVKELSLADFKKKFSYiFDTENKRDESISSVISGRLKLLRIAGKSIFANIEDENE 83
Cdd:PRK00484 4 NEQIAVRREKLAELREQGIDPYPNKFERTHTAAELRAKYDD-KEKEELEELEIEVSVAGRVMLKRVMGKASFATLQDGSG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 84 NLQIYFSKDSLGEEKFNLFKKnLEVGDIILAKGFPFVTKTGEFSLHASEITLATKSIVPLPEKYHGLTDIEQRYRKRYVD 163
Cdd:PRK00484 83 RIQLYVSKDDVGEEALEAFKK-LDLGDIIGVEGTLFKTKTGELSVKATELTLLTKSLRPLPDKFHGLTDVETRYRQRYVD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 164 MIMNAEVRKDFLTRSKVVSLIRHFFEEKGFLEVETPMMHPIAGGANAKPFVTFHNSLGVERFLRIAPELYLKRLVVGGFE 243
Cdd:PRK00484 162 LIVNPESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARPFITHHNALDIDLYLRIAPELYLKRLIVGGFE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 244 AVFEINRCFRNEGMDLTHNPEFTTIEFYWAYHNYKDLMDLTEELFALLLEKLQLGKIIEFDGQKIDFSKPFERITYKDAL 323
Cdd:PRK00484 242 RVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTYQGTEIDFGPPFKRLTMVDAI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 324 KKYGALsDEIIENKDKILEKLKKDGFEANDKLDLGHLQAELFDNYVESKLIDPTFITDFPISISPLSRRSDKNSEIAERF 403
Cdd:PRK00484 322 KEYTGV-DFDDMTDEEARALAKELGIEVEKSWGLGKLINELFEEFVEPKLIQPTFITDYPVEISPLAKRHREDPGLTERF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 404 ELFVCGRELANGFNELNDPLDQYERFLKQIEAKNAGDEEACEMDEDFVNALGYGMPPTAGQGIGIDRLVMLLTNKKSIRD 483
Cdd:PRK00484 401 ELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRD 480
|
490
....*....|.
gi 488866119 484 VILFPAMRPLK 494
Cdd:PRK00484 481 VILFPLMRPEK 491
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
3-495 |
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: 798.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 3 DNILEQQRIQKANELKNAGVNPYPHFLVKELSLADFKKKFSyifDTENKRDESISSVISGRLKLLRIAGKSIFANIEDEN 82
Cdd:COG1190 7 LNEQIRVRREKLEELREAGIDPYPNKFPRTHTAAEIREKYD---ELEAEEETGDEVSVAGRIMAKRDMGKASFADLQDGS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 83 ENLQIYFSKDSLGEEKFNLFKKnLEVGDIILAKGFPFVTKTGEFSLHASEITLATKSIVPLPEKYHGLTDIEQRYRKRYV 162
Cdd:COG1190 84 GRIQLYLRRDELGEEAYELFKL-LDLGDIVGVEGTVFRTKTGELSVKVEELTLLSKSLRPLPEKFHGLTDPETRYRQRYV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 163 DMIMNAEVRKDFLTRSKVVSLIRHFFEEKGFLEVETPMMHPIAGGANAKPFVTFHNSLGVERFLRIAPELYLKRLVVGGF 242
Cdd:COG1190 163 DLIVNPEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 243 EAVFEINRCFRNEGMDLTHNPEFTTIEFYWAYHNYKDLMDLTEELFALLLEKLQLGKIIEFDGQKIDFSKPFERITYKDA 322
Cdd:COG1190 243 ERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGTTKVTYQGQEIDLSPPWRRITMVEA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 323 LKKYGALSDEIIENKDKILEKLKKDGFEANDKLDLGHLQAELFDNYVESKLIDPTFITDFPISISPLSRRSDKNSEIAER 402
Cdd:COG1190 323 IKEATGIDVTPLTDDEELRALAKELGIEVDPGWGRGKLIDELFEELVEPKLIQPTFVTDYPVEVSPLAKRHRDDPGLTER 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 403 FELFVCGRELANGFNELNDPLDQYERFLKQIEAKNAGDEEACEMDEDFVNALGYGMPPTAGQGIGIDRLVMLLTNKKSIR 482
Cdd:COG1190 403 FELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIR 482
|
490
....*....|...
gi 488866119 483 DVILFPAMRPLKS 495
Cdd:COG1190 483 DVILFPLMRPEKK 495
|
|
| lysS_bact |
TIGR00499 |
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ... |
8-494 |
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: 628.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 8 QQRIQKANELKNAGVNPYPHFLVKELSLADFKKKFSYIFDTENKrDESISSVISGRLKLLRIAGKSIFANIEDENENLQI 87
Cdd:TIGR00499 7 QQRLEKLNRLRQTGNNPYLHKFERTHSAQEFQEKYADLSNEELK-EKELKVSIAGRIKAIRSMGKATFITLQDESGQIQL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 88 YFSKDSLGEEKFNLFKKNLEVGDIILAKGFPFVTKTGEFSLHASEITLATKSIVPLPEKYHGLTDIEQRYRKRYVDMIMN 167
Cdd:TIGR00499 86 YVNKNKLPEDFYEFDEYLLDLGDIIGVTGYPFKTKTGELSVKVTELQILTKCLQPLPDKWHGLTDQETRYRQRYLDLIVN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 168 AEVRKDFLTRSKVVSLIRHFFEEKGFLEVETPMMHPIAGGANAKPFVTFHNSLGVERFLRIAPELYLKRLVVGGFEAVFE 247
Cdd:TIGR00499 166 PDVRQTFLKRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKPFITHHNALDMDLYLRIAPELYLKRLIVGGLEKVYE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 248 INRCFRNEGMDLTHNPEFTTIEFYWAYHNYKDLMDLTEELFALLLEKLQLGKIIEFDGQKIDFSKPFERITYKDALKKYG 327
Cdd:TIGR00499 246 IGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTFIINYNDLEIDLKPPWKRITMVDALEMVT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 328 ALSDEIIENKDKILEKLKKDGFE-ANDKLDLGHLQAELFDNYVESKLIDPTFITDFPISISPLSRRSDKNSEIAERFELF 406
Cdd:TIGR00499 326 GIDFDILKDDETAKALAKEHGIEvAEDSLTLGHILNKFFEQFLEHTLIQPTFITHYPAEISPLAKRDPSNPEFTERFELF 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 407 VCGRELANGFNELNDPLDQYERFLKQIEAKNAGDEEACEMDEDFVNALGYGMPPTAGQGIGIDRLVMLLTNKKSIRDVIL 486
Cdd:TIGR00499 406 IAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGIGIDRLVMLLTDAPSIRDVLL 485
|
....*...
gi 488866119 487 FPAMRPLK 494
Cdd:TIGR00499 486 FPQLRPQK 493
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
10-492 |
0e+00 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 613.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 10 RIQKANELKNAGVNPYPHFLVKELSLADFKKKFSYIFDTENKRDESISsvISGRLKLLRIAGKSIFANIEDENENLQIYF 89
Cdd:PLN02502 65 RLKKVEALRAKGVEPYPYKFDVTHTAPELQEKYGSLENGEELEDVSVS--VAGRIMAKRAFGKLAFYDLRDDGGKIQLYA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 90 SKDSLG--EEKFNLFKKNLEVGDIILAKGFPFVTKTGEFSLHASEITLATKSIVPLPEKYHGLTDIEQRYRKRYVDMIMN 167
Cdd:PLN02502 143 DKKRLDldEEEFEKLHSLVDRGDIVGVTGTPGKTKKGELSIFPTSFEVLTKCLLMLPDKYHGLTDQETRYRQRYLDLIAN 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 168 AEVRKDFLTRSKVVSLIRHFFEEKGFLEVETPMMHPIAGGANAKPFVTFHNSLGVERFLRIAPELYLKRLVVGGFEAVFE 247
Cdd:PLN02502 223 PEVRDIFRTRAKIISYIRRFLDDRGFLEVETPMLNMIAGGAAARPFVTHHNDLNMDLYLRIATELHLKRLVVGGFERVYE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 248 INRCFRNEGMDLTHNPEFTTIEFYWAYHNYKDLMDLTEELFALLLEKLQLGKIIEFDGQKIDFSKPFERITYKDALKKY- 326
Cdd:PLN02502 303 IGRQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKELTGSYKIKYHGIEIDFTPPFRRISMISLVEEAt 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 327 -----GALSDEiiENKDKILEKLKKDGFEANDKLDLGHLQAELFDNYVESKLIDPTFITDFPISISPLSRRSDKNSEIAE 401
Cdd:PLN02502 383 gidfpADLKSD--EANAYLIAACEKFDVKCPPPQTTGRLLNELFEEFLEETLVQPTFVLDHPVEMSPLAKPHRSKPGLTE 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 402 RFELFVCGRELANGFNELNDPLDQYERFLKQIEAKNAGDEEACEMDEDFVNALGYGMPPTAGQGIGIDRLVMLLTNKKSI 481
Cdd:PLN02502 461 RFELFINGRELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRLVMLLTDSASI 540
|
490
....*....|.
gi 488866119 482 RDVILFPAMRP 492
Cdd:PLN02502 541 RDVIAFPAMKP 551
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
167-492 |
0e+00 |
|
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a lysine to the 3' OH group of ribose of the appropriate tRNA. Its assignment to class II aaRS is based upon its structure and the presence of three characteristic sequence motifs in the core domain. It is found in eukaryotes as well as some prokaryotes and archaea. However, LysRS belongs to class I aaRS's in some prokaryotes and archaea. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate.
Pssm-ID: 238398 [Multi-domain] Cd Length: 329 Bit Score: 542.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 167 NAEVRKDFLTRSKVVSLIRHFFEEKGFLEVETPMMHPIAGGANAKPFVTFHNSLGVERFLRIAPELYLKRLVVGGFEAVF 246
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 247 EINRCFRNEGMDLTHNPEFTTIEFYWAYHNYKDLMDLTEELFALLLEKLQLGKIIEFDGQKIDFSKPFERITYKDALKKY 326
Cdd:cd00775 81 EIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIEYGGKELDFTPPFKRVTMVDALKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 327 G-----ALSDEIIENKDKILEKLKKDGFEanDKLDLGHLQAELFDNYVESKLIDPTFITDFPISISPLSRRSDKNSEIAE 401
Cdd:cd00775 161 TgidfpELDLEQPEELAKLLAKLIKEKIE--KPRTLGKLLDKLFEEFVEPTLIQPTFIIDHPVEISPLAKRHRSNPGLTE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 402 RFELFVCGRELANGFNELNDPLDQYERFLKQIEAKNAGDEEACEMDEDFVNALGYGMPPTAGQGIGIDRLVMLLTNKKSI 481
Cdd:cd00775 239 RFELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLTDSNSI 318
|
330
....*....|.
gi 488866119 482 RDVILFPAMRP 492
Cdd:cd00775 319 RDVILFPAMRP 329
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
46-494 |
9.41e-158 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 457.99 E-value: 9.41e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 46 FDTENKRDE---SISSVISGRLKLLRIAGKSIFANIEDENENLQIYFSKDSLGEEKFNLFKKNLEVGDIILAKGFPFVTK 122
Cdd:PRK12445 53 FDAKDNQELeslNIEVSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEGVYNDQFKKWDLGDIIGARGTLFKTQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 123 TGEFSLHASEITLATKSIVPLPEKYHGLTDIEQRYRKRYVDMIMNAEVRKDFLTRSKVVSLIRHFFEEKGFLEVETPMMH 202
Cdd:PRK12445 133 TGELSIHCTELRLLTKALRPLPDKFHGLQDQEVRYRQRYLDLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 203 PIAGGANAKPFVTFHNSLGVERFLRIAPELYLKRLVVGGFEAVFEINRCFRNEGMDLTHNPEFTTIEFYWAYHNYKDLMD 282
Cdd:PRK12445 213 VIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 283 LTEELFALLLEKLQLGKIIEFDGQKIDFSKPFERITYKDALKKYGALSDEI-IENKDKILEKLKKDGFEANDKLDLGHLQ 361
Cdd:PRK12445 293 LTESLFRTLAQEVLGTTKVTYGEHVFDFGKPFEKLTMREAIKKYRPETDMAdLDNFDAAKALAESIGITVEKSWGLGRIV 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 362 AELFDNYVESKLIDPTFITDFPISISPLSRRSDKNSEIAERFELFVCGRELANGFNELNDPLDQYERFLKQIEAKNAGDE 441
Cdd:PRK12445 373 TEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDD 452
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 488866119 442 EACEMDEDFVNALGYGMPPTAGQGIGIDRLVMLLTNKKSIRDVILFPAMRPLK 494
Cdd:PRK12445 453 EAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFPAMRPQK 505
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
7-492 |
8.50e-147 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 448.26 E-value: 8.50e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 7 EQQ--RIQKANELKNAGVNPYPHFLVKELSLADfkkkfsyifDTENKRDESISsvISGRLKLLRIAGKSIFANIEDENEN 84
Cdd:PRK02983 612 EQVrvRLAKLEALRAAGVDPYPVGVPPTHTVAE---------ALDAPTGEEVS--VSGRVLRIRDYGGVLFADLRDWSGE 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 85 LQIYFSKDSLGEEKFNLFKKNLEVGDIILAKGFPFVTKTGEFSLHASEITLATKSIVPLPEKYHGLTDIEQRYRKRYVDM 164
Cdd:PRK02983 681 LQVLLDASRLEQGSLADFRAAVDLGDLVEVTGTMGTSRNGTLSLLVTSWRLAGKCLRPLPDKWKGLTDPEARVRQRYLDL 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 165 IMNAEVRKDFLTRSKVVSLIRHFFEEKGFLEVETPMMHPIAGGANAKPFVTFHNSLGVERFLRIAPELYLKRLVVGGFEA 244
Cdd:PRK02983 761 AVNPEARDLLRARSAVVRAVRETLVARGFLEVETPILQQVHGGANARPFVTHINAYDMDLYLRIAPELYLKRLCVGGVER 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 245 VFEINRCFRNEGMDLTHNPEFTTIEFYWAYHNYKDLMDLTEELF-----ALLLEKLQLGKIIEFDGQKIDFSKPFERITY 319
Cdd:PRK02983 841 VFELGRNFRNEGVDATHNPEFTLLEAYQAHADYDTMRDLTRELIqnaaqAAHGAPVVMRPDGDGVLEPVDISGPWPVVTV 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 320 KDALKKygALSDEIieNKDKILEKLKK----DGFEANDKLDLGHLQAELFDNYVESKLIDPTFITDFPISISPLSR--RS 393
Cdd:PRK02983 921 HDAVSE--ALGEEI--DPDTPLAELRKlcdaAGIPYRTDWDAGAVVLELYEHLVEDRTTFPTFYTDFPTSVSPLTRphRS 996
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 394 DKNseIAERFELFVCGRELANGFNELNDPLDQYERFLKQIEAKNAGDEEACEMDEDFVNALGYGMPPTAGQGIGIDRLVM 473
Cdd:PRK02983 997 DPG--LAERWDLVAWGVELGTAYSELTDPVEQRRRLTEQSLLAAGGDPEAMELDEDFLQALEYAMPPTGGLGMGVDRLVM 1074
|
490
....*....|....*....
gi 488866119 474 LLTNkKSIRDVILFPAMRP 492
Cdd:PRK02983 1075 LLTG-RSIRETLPFPLVKP 1092
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
8-492 |
1.17e-124 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 376.27 E-value: 1.17e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 8 QQRIQKANELKNAGVNPYPHFLVKELSLADFKKKFSYIFDTENKRDESISsvISGRLKLLRIAGKSI-FANIEDENENLQ 86
Cdd:PTZ00417 87 ENRSKFIQEQKAKGINPYPHKFERTITVPEFVEKYQDLASGEHLEDTILN--VTGRIMRVSASGQKLrFFDLVGDGAKIQ 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 87 IYFSKDSLGEEKFNLFK--KNLEVGDIILAKGFPFVTKTGEFSLHASEITLATKSIVPLPEKYhGLTDIEQRYRKRYVDM 164
Cdd:PTZ00417 165 VLANFAFHDHTKSNFAEcyDKIRRGDIVGIVGFPGKSKKGELSIFPKETIILSPCLHMLPMKY-GLKDTEIRYRQRYLDL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 165 IMNAEVRKDFLTRSKVVSLIRHFFEEKGFLEVETPMMHPIAGGANAKPFVTFHNSLGVERFLRIAPELYLKRLVVGGFEA 244
Cdd:PTZ00417 244 MINESTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLVAGGANARPFITHHNDLDLDLYLRIATELPLKMLIVGGIDK 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 245 VFEINRCFRNEGMDLTHNPEFTTIEFYWAYHNYKDLMDLTEELFALLLEKLqLG--KII------EFDGQKIDFSKPFER 316
Cdd:PTZ00417 324 VYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHL-FGtyKILynkdgpEKDPIEIDFTPPYPK 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 317 ITYKDALKKygaLSDEIIENK-------DKILEKLKKDGFEANDKLDLGHLQAELFDNYVESKLID-PTFITDFPISISP 388
Cdd:PTZ00417 403 VSIVEELEK---LTNTKLEQPfdspetiNKMINLIKENKIEMPNPPTAAKLLDQLASHFIENKYPNkPFFIIEHPQIMSP 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 389 LSRRSDKNSEIAERFELFVCGRELANGFNELNDPLDQYERFLKQIEAKNAGDEEACEMDEDFVNALGYGMPPTAGQGIGI 468
Cdd:PTZ00417 480 LAKYHRSKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCTSLEYGLPPTGGLGLGI 559
|
490 500
....*....|....*....|....
gi 488866119 469 DRLVMLLTNKKSIRDVILFPAMRP 492
Cdd:PTZ00417 560 DRITMFLTNKNCIKDVILFPTMRP 583
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
34-491 |
6.36e-121 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 368.98 E-value: 6.36e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 34 SLADFKKKFSYIFDTEnkRDESISSVISGRLKLLRIAGKSIFANIEDENENLQI------YFSKDSLGEekfnlFKKNLE 107
Cdd:PTZ00385 88 PISEVRERYGYLASGD--RAAQATVRVAGRVTSVRDIGKIIFVTIRSNGNELQVvgqvgeHFTREDLKK-----LKVSLR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 108 VGDIILAKGFPFVTKTGEFSLHASEITLAT------KSIVPLPEKYHGLTDIEQRYRKRYVDMIMNAEVRKDFLTRSKVV 181
Cdd:PTZ00385 161 VGDIIGADGVPCRMQRGELSVAASRMLILSpyvctdQVVCPNLRGFTVLQDNDVKYRYRFTDMMTNPCVIETIKKRHVML 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 182 SLIRHFFEEKGFLEVETPMMHPIAGGANAKPFVTFHNSLGVERFLRIAPELYLKRLVVGGFEAVFEINRCFRNEGMDLTH 261
Cdd:PTZ00385 241 QALRDYFNERNFVEVETPVLHTVASGANAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSH 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 262 NPEFTTIEFYWAYHNYKDLMDLTEELFALLLEKLQLGKIIEFDGQK-------IDFSKPFERITYKDALKKYGALS---- 330
Cdd:PTZ00385 321 NPEFTSCEFYAAYHTYEDLMPMTEDIFRQLAMRVNGTTVVQIYPENahgnpvtVDLGKPFRRVSVYDEIQRMSGVEfppp 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 331 DEIieNKDKILEKLKKDGFEANDKLDLGHLQAELFDN----YVESKLIDPTFITDFPISISPLSRRSDKNSEIAERFELF 406
Cdd:PTZ00385 401 NEL--NTPKGIAYMSVVMLRYNIPLPPVRTAAKMFEKlidfFITDRVVEPTFVMDHPLFMSPLAKEQVSRPGLAERFELF 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 407 VCGRELANGFNELNDPLDQYERFLKQIEAKNAGDEEACEMDEDFVNALGYGMPPTAGQGIGIDRLVMLLTNKKSIRDVIL 486
Cdd:PTZ00385 479 VNGIEYCNAYSELNDPHEQYHRFQQQLVDRQGGDEEAMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGII 558
|
....*
gi 488866119 487 FPAMR 491
Cdd:PTZ00385 559 FPLLR 563
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
152-491 |
2.69e-118 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 350.33 E-value: 2.69e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 152 DIEQRYRKRYVDMiMNAEVRKDFLTRSKVVSLIRHFFEEKGFLEVETPMMHPIAGGANAKPFVTFHNSLGVERFLRIAPE 231
Cdd:pfam00152 1 DEETRLKYRYLDL-RRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 232 LYLKRLVVGGFEAVFEINRCFRNEGMDLTHNPEFTTIEFYWAYHNYKDLMDLTEELFALLLEKLQLGKIIEFDGQKIDFS 311
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 312 KPFERITYKDALKKYgalsdeiienkdkiLEKLKKDGFEANDKLDLGHLQAELFDNYVesklIDPTFITDFPISISPLSR 391
Cdd:pfam00152 160 KPFPRITYAEAIEKL--------------NGKDVEELGYGSDKPDLRFLLELVIDKNK----FNPLWVTDFPAEHHPFTM 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 392 RSDKN-SEIAERFELFVCGRELANGFNELNDPLDQYERFLKQIEAKnagdEEACEMDEDFVNALGYGMPPTAGQGIGIDR 470
Cdd:pfam00152 222 PKDEDdPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDP----EEAEEKFGFYLDALKYGAPPHGGLGIGLDR 297
|
330 340
....*....|....*....|.
gi 488866119 471 LVMLLTNKKSIRDVILFPAMR 491
Cdd:pfam00152 298 LVMLLTGLESIREVIAFPKTR 318
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
174-492 |
1.94e-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: 300.16 E-value: 1.94e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 174 FLTRSKVVSLIRHFFEEKGFLEVETPMMHPIAGGANAKPFVTFHNSLGVERFLRIAPELYLKRLVVGGFEAVFEINRCFR 253
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 254 NEGMDLTHNPEFTTIEFYWAYHNYKDLMDLTEELFALLLEKLQLGKIIEFDGQKIDFSKPFERITYKDALKKYGAlsdei 333
Cdd:cd00669 81 NEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYGFELEDFGLPFPRLTYREALERYGQ----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 334 ienkdkileklkkdgfeandkldlghlqaelfdnyvesklidPTFITDFPI-SISPLSRRSDKNSEIAERFELFVCGREL 412
Cdd:cd00669 156 ------------------------------------------PLFLTDYPAeMHSPLASPHDVNPEIADAFDLFINGVEV 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 413 ANGFNELNDPLDQYERFLKQIEAKnagdEEACEMDEDFVNALGYGMPPTAGQGIGIDRLVMLLTNKKSIRDVILFPAMRP 492
Cdd:cd00669 194 GNGSSRLHDPDIQAEVFQEQGINK----EAGMEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKMRR 269
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
175-485 |
6.01e-80 |
|
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: 251.56 E-value: 6.01e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 175 LTRSKVVSLIRHFFEEKGFLEVETPMMHPiAGG--ANAKPFVT---FHNSLGVERFLRIAPELYLKRLVVGGFEAVFEIN 249
Cdd:COG2269 7 RARARLLAAIRAFFAERGVLEVETPALSV-APGtdPHLDSFATefiGPDGGGRPLYLHTSPEFAMKRLLAAGSGPIYQIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 250 RCFRNEGMDLTHNPEFTTIEFYWAYHNYKDLMDLTEELFALLLEKLQlgkiiefdgqkidfSKPFERITYKDALKKYGAL 329
Cdd:COG2269 86 KVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAAG--------------FAPAERLSYQEAFLRYLGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 330 sDEIIENKDKILEKLKKDGFEA------NDKLDLghlqaeLFDNYVESKL-ID-PTFITDFPISISPLSRRSDKNSEIAE 401
Cdd:COG2269 152 -DPLTADLDELAAAAAAAGLRVaddddrDDLLDL------LLSERVEPQLgRDrPTFLYDYPASQAALARISPDDPRVAE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 402 RFELFVCGRELANGFNELNDPLDQYERFLKQIEAKNAGDEEACEMDEDFVNALGYGMPPTAGQGIGIDRLVMLLTNKKSI 481
Cdd:COG2269 225 RFELYACGVELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALGAERI 304
|
....
gi 488866119 482 RDVI 485
Cdd:COG2269 305 DDVL 308
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
187-485 |
8.23e-80 |
|
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: 250.55 E-value: 8.23e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 187 FFEEKGFLEVETPMMHPiAGG--ANAKPF-VTFHNSLGVER--FLRIAPELYLKRLVVGGFEAVFEINRCFRNEGMDLTH 261
Cdd:TIGR00462 1 FFAERGVLEVETPLLSP-APVtdPHLDAFaTEFVGPDGQGRplYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 262 NPEFTTIEFYWAYHNYKDLMDLTEELFALLLEklqlgkiiefdgqkiDFSKPFERITYKDALKKYGALsDEIIENKDKIL 341
Cdd:TIGR00462 80 NPEFTMLEWYRPGFDYHDLMDEVEALLQELLG---------------DPFAPAERLSYQEAFLRYAGI-DPLTASLAELQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 342 EKLKKDGFEANDKLDLGHLQAELFDNYVESKL-ID-PTFITDFPISISPLSRRSDKNSEIAERFELFVCGRELANGFNEL 419
Cdd:TIGR00462 144 AAAAAHGIRASEEDDRDDLLDLLFSEKVEPHLgFGrPTFLYDYPASQAALARISPDDPRVAERFELYIKGLELANGFHEL 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488866119 420 NDPLDQYERFLKQIEAKNAGDEEACEMDEDFVNALGYGMPPTAGQGIGIDRLVMLLTNKKSIRDVI 485
Cdd:TIGR00462 224 TDAAEQRRRFEADNALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDVL 289
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
172-484 |
7.03e-66 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 215.18 E-value: 7.03e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 172 KDFLTRSKVVSLIRHFFEEKGFLEVETPMM-HPIAGGANAKPFVTFHNSLGVER----FLRIAPELYLKRLVVGGFEAVF 246
Cdd:PRK09350 3 PNLLKRAKIIAEIRRFFADRGVLEVETPILsQATVTDIHLVPFETRFVGPGASQgktlWLMTSPEYHMKRLLAAGSGPIF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 247 EINRCFRNEGMDLTHNPEFTTIEFYWAYHNYKDLMDLTEELFallleklqlgkiiefdgQKIDFSKPFERITYKDALKKY 326
Cdd:PRK09350 83 QICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLL-----------------QQVLDCEPAESLSYQQAFLRY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 327 GALsDEIIENKDKILEKLKKDGF--EANDKLDLGHLQAELFDNYVESKL--IDPTFITDFPISISPLSRRSDKNSEIAER 402
Cdd:PRK09350 146 LGI-DPLSADKTQLREVAAKLGLsnIADEEEDRDTLLQLLFTFGVEPNIgkEKPTFVYHFPASQAALAKISTEDHRVAER 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 403 FELFVCGRELANGFNELNDPLDQYERFLKQIEAKNAGDEEACEMDEDFVNALGYGMPPTAGQGIGIDRLVMLLTNKKSIR 482
Cdd:PRK09350 225 FEVYFKGIELANGFHELTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCSGVALGVDRLIMLALGAESIS 304
|
..
gi 488866119 483 DV 484
Cdd:PRK09350 305 EV 306
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
60-164 |
1.79e-49 |
|
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: 164.96 E-value: 1.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 60 ISGRLKLLRIAGKSIFANIEDENENLQIYFSKDSLGEEKFNLFKKNLEVGDIILAKGFPFVTKTGEFSLHASEITLATKS 139
Cdd:cd04322 4 VAGRIMSKRGSGKLSFADLQDESGKIQVYVNKDDLGEEEFEDFKKLLDLGDIIGVTGTPFKTKTGELSIFVKEFTLLSKS 83
|
90 100
....*....|....*....|....*
gi 488866119 140 IVPLPEKYHGLTDIEQRYRKRYVDM 164
Cdd:cd04322 84 LRPLPEKFHGLTDVETRYRQRYLDL 108
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
59-488 |
1.03e-43 |
|
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: 159.99 E-value: 1.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 59 VISGRLKLLRIAGKSIFANIEDENENLQIYFSKDSLGEEKFNLFKKnLEVGDIILAKGFPFVTKT--GEFSLHASEITLA 136
Cdd:TIGR00458 16 TFMGWVHEIRDLGGLIFVLLRDREGLIQITAPAKKVSKNLFKWAKK-LNLESVVAVRGIVKIKEKapGGFEIIPTKIEVI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 137 TKSIVPLP----EKYHGltDIEQRYRKRYVDMiMNAEVRKDFLTRSKVVSLIRHFFEEKGFLEVETPMM--HPIAGGANA 210
Cdd:TIGR00458 95 NEAKEPLPldptEKVPA--ELDTRLDYRFLDL-RRPTVQAIFRIRSGVLESVREFLAEEGFIEVHTPKLvaSATEGGTEL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 211 KPFVTFHNslgvERFLRIAPELYLKRLVVGGFEAVFEINRCFRNEGMDLT-HNPEFTTIEFYWAYHNYKDLMDLTEELFA 289
Cdd:TIGR00458 172 FPITYFER----EAFLGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNTHrHLNEATSIDIEMAFEDHHDVMDILEELVV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 290 LLLEKLQLGKIIEFDGQKIDFSKP---FERITYKDALKKYGALSDEIIENKDKILEKLKKDGfeandkldlghlqaELFD 366
Cdd:TIGR00458 248 RVFEDVPERCAHQLETLEFKLEKPegkFVRLTYDEAIEMANAKGVEIGWGEDLSTEAEKALG--------------EEMD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 367 NYVesklidptFITDFPISISPLSRRSD-KNSEIAERFELFVCGRELANGFNELNDpldqYERFLKQIEAKNAGDEEAce 445
Cdd:TIGR00458 314 GLY--------FITDWPTEIRPFYTMPDeDNPEISKSFDLMYRDLEISSGAQRIHL----HDLLVERIKAKGLNPEGF-- 379
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 488866119 446 mdEDFVNALGYGMPPTAGQGIGIDRLVMLLTNKKSIRDVILFP 488
Cdd:TIGR00458 380 --KDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFP 420
|
|
| aspS_bact |
TIGR00459 |
aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be ... |
59-488 |
3.51e-42 |
|
aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be discriminating (6.1.1.12) or nondiscriminating (6.1.1.23). In a multiple sequence alignment of representative asparaginyl-tRNA synthetases (asnS), archaeal/eukaryotic type aspartyl-tRNA synthetases (aspS_arch), and bacterial type aspartyl-tRNA synthetases (aspS_bact), there is a striking similarity between asnS and aspS_arch in gap pattern and in sequence, and a striking divergence of aspS_bact. Consequently, a separate model was built for each of the three groups. This model, aspS_bact, represents aspartyl-tRNA synthetases from the Bacteria and from mitochondria. In some species, this enzyme aminoacylates tRNA for both Asp and Asn; Asp-tRNA(asn) is subsequently transamidated to Asn-tRNA(asn). This model generates very low scores for the archaeal type of aspS and for asnS; scores between the trusted and noise cutoffs represent fragmentary sequences. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 211576 [Multi-domain] Cd Length: 583 Bit Score: 158.36 E-value: 3.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 59 VISGRLKLLRIAGKSIFANIEDENENLQIYFSKDSLGEEKFnlfkKNLEVGDIILAKGFPFVT---------KTGEFSLH 129
Cdd:TIGR00459 19 TLAGWVNRRRDLGGLIFIDLRDRSGIVQVVCDPDADALKLA----KGLRNEDVVQVKGKVSARpegninrnlDTGEIEIL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 130 ASEITLATKSIVPLPEKYHGLTDIEQRYRKRYVDMiMNAEVRKDFLTRSKVVSLIRHFFEEKGFLEVETPMMhpiaggAN 209
Cdd:TIGR00459 95 AESITLLNKSKTPPLIIEKTDAEEEVRLKYRYLDL-RRPEMQQRLKLRHKVTKAVRNFLDQQGFLEIETPML------TK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 210 AKPfvtfhnsLGVERFL---RI----------APELYLKRLVVGGFEAVFEINRCFRNEGMDLTHNPEFTTIEFYWAYHN 276
Cdd:TIGR00459 168 STP-------EGARDYLvpsRVhkgefyalpqSPQLFKQLLMVSGVDRYYQIARCFRDEDLRADRQPEFTQIDMEMSFMT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 277 YKDLMDLTEELFALLLEKLqlgkiiefdgQKIDFSKPFERITYKDALKKYGA------LSDEIIENKD-------KILEK 343
Cdd:TIGR00459 241 QEDVMELIEKLVSHVFLEV----------KGIDLKKPFPVMTYAEAMERYGSdkpdlrFPLELIDVTDlfkdsefKVFSN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 344 LKKDG-------------FEANDKLD----------------------------------------LGHLQAELFD---- 366
Cdd:TIGR00459 311 LINDGgrvkairvpggwaELSRKSIKelrkfakeygakglaylkvnedginspikkfldekkgkilLERTDAQNGDillf 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 367 -----------------------NYVESKLIDPTFITDFPI--------------------SISPLSRRSDKNSEIAERF 403
Cdd:TIGR00459 391 gagskkivldalgalrlklgkdlGLVDPDLFSFLWVVDFPMfekdkegrlcaahhpftmpkDEDLENLEAAPEEALAEAY 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 404 ELFVCGRELANGFNELNDPLDQYERFlkqiEAKNAGDEEACEMDEDFVNALGYGMPPTAGQGIGIDRLVMLLTNKKSIRD 483
Cdd:TIGR00459 471 DLVLNGVELGGGSIRIHDPEVQKKVF----EILGIDPEEAREKFGFLLEAFKYGTPPHAGFALGLDRLMMLLTGTDNIRD 546
|
....*
gi 488866119 484 VILFP 488
Cdd:TIGR00459 547 VIAFP 551
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
59-488 |
1.08e-39 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 148.80 E-value: 1.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 59 VISGRLKLLRIAGKSIFANIEDENENLQIYFSKDSLgEEKFNLFKKnLEVGDIILAKG---FPFVTKTGeFSLHASEITL 135
Cdd:PRK05159 20 TLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKVD-EELFETIKK-LKRESVVSVTGtvkANPKAPGG-VEVIPEEIEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 136 ATKSIVPLPEKYHG--LTDIEQRYRKRYVDmIMNAEVRKDFLTRSKVVSLIRHFFEEKGFLEVETPMMhpIA----GGAN 209
Cdd:PRK05159 97 LNKAEEPLPLDISGkvLAELDTRLDNRFLD-LRRPRVRAIFKIRSEVLRAFREFLYENGFTEIFTPKI--VAsgteGGAE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 210 AKPFVTFHNslgvERFLRIAPELYLKRLVVGGFEAVFEINRCFRNEGMDLT-HNPEFTTIEFYWAY-HNYKDLMDLTEEL 287
Cdd:PRK05159 174 LFPIDYFEK----EAYLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSrHLNEYTSIDVEMGFiDDHEDVMDLLENL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 288 FALLLEKLQLGKIIEFDGQKIDF---SKPFERITYKDALkkygalsdeiienkdkilEKLKKDGFEANDKLDLGHLQAEL 364
Cdd:PRK05159 250 LRYMYEDVAENCEKELELLGIELpvpETPIPRITYDEAI------------------EILKSKGNEISWGDDLDTEGERL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 365 FDNYV-ESKLIDPTFITDFPISISPL-SRRSDKNSEIAERFELFVCGRELANGFNELNDpldqYERFLKQIEAKNagdee 442
Cdd:PRK05159 312 LGEYVkEEYGSDFYFITDYPSEKRPFyTMPDEDDPEISKSFDLLFRGLEITSGGQRIHR----YDMLVESIKEKG----- 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 488866119 443 aceMD-EDF---VNALGYGMPPTAGQGIGIDRLVMLLTNKKSIRDVILFP 488
Cdd:PRK05159 383 ---LNpESFefyLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFP 429
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
177-488 |
1.71e-37 |
|
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: 140.01 E-value: 1.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 177 RSKVVSLIRHFFEEKGFLEVETPMMhpIA----GGANAKPFVTFhnslGVERFLRIAPELYlKRLVVGGFEAVFEINRCF 252
Cdd:cd00776 27 RSEVLRAFREFLRENGFTEVHTPKI--TStdteGGAELFKVSYF----GKPAYLAQSPQLY-KEMLIAALERVYEIGPVF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 253 RNEGMDLT-HNPEFTTIEFYWAY-HNYKDLMDLTEEL----FALLLEK----LQLGKIIEFDGQKidFSKPFERITYKDA 322
Cdd:cd00776 100 RAEKSNTRrHLSEFWMLEAEMAFiEDYNEVMDLIEELikyiFKRVLERcakeLELVNQLNRELLK--PLEPFPRITYDEA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 323 LKkygalsdeiienkdkILEKlKKDGFEANDKLDLGHLQAELFDNYVESkliDPTFITDFPISISPL-SRRSDKNSEIAE 401
Cdd:cd00776 178 IE---------------LLRE-KGVEEEVKWGEDLSTEHERLLGEIVKG---DPVFVTDYPKEIKPFyMKPDDDNPETVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 402 RFELFVCGR-ELANGFNELNDpldqYERFLKQIEAKNAGDEEAcemdEDFVNALGYGMPPTAGQGIGIDRLVMLLTNKKS 480
Cdd:cd00776 239 SFDLLMPGVgEIVGGSQRIHD----YDELEERIKEHGLDPESF----EWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDN 310
|
....*...
gi 488866119 481 IRDVILFP 488
Cdd:cd00776 311 IREAILFP 318
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
59-491 |
1.75e-35 |
|
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: 137.11 E-value: 1.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 59 VISGRLKLLRIAGKSIFANIEDENENLQIYFSKDSLgeEKFNLFKKnLEVGDIILAKGFpfVTKT----GEFSLHASEIT 134
Cdd:COG0017 18 TVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKL--ENFEEAKK-LTTESSVEVTGT--VVESprapQGVELQAEEIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 135 LATKSIVPLP--EKYHGLtdiEQRYRKRYVDmIMNAEVRKDFLTRSKVVSLIRHFFEEKGFLEVETPMMHPIA--GGANA 210
Cdd:COG0017 93 VLGEADEPYPlqPKRHSL---EFLLDNRHLR-LRTNRFGAIFRIRSELARAIREFFQERGFVEVHTPIITASAteGGGEL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 211 KPfVTFHnslGVERFLRIAPELYlKRLVVGGFEAVFEINRCFRNEGMDLT-HNPEFTTIEFYWAYHNYKDLMDLTEELFA 289
Cdd:COG0017 169 FP-VDYF---GKEAYLTQSGQLY-KEALAMALEKVYTFGPTFRAEKSNTRrHLAEFWMIEPEMAFADLEDVMDLAEEMLK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 290 LLLEKL--QLGKIIEFDGQKIDF-----SKPFERITYKDALkkygalsdeiienkdkilEKLKKDGFEANDKLDLG--HL 360
Cdd:COG0017 244 YIIKYVleNCPEELEFLGRDVERlekvpESPFPRITYTEAI------------------EILKKSGEKVEWGDDLGteHE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 361 QA---ELFDnyveskliDPTFITDFPISISPL-SRRSDKNSEIAERFELfvcgreLANGFNEL---NDPLDQYERFLKQI 433
Cdd:COG0017 306 RYlgeEFFK--------KPVFVTDYPKEIKAFyMKPNPDDPKTVAAFDL------LAPGIGEIiggSQREHRYDVLVERI 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488866119 434 EAKNagdeeaceMDED----FVNALGYGMPPTAGQGIGIDRLVMLLTNKKSIRDVILFPAMR 491
Cdd:COG0017 372 KEKG--------LDPEdyewYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDP 425
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
174-488 |
6.41e-35 |
|
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: 131.93 E-value: 6.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 174 FLTRSKVVSLIRHFFEEKGFLEVETPMM-HPIAGGAnaKPFVTfHNSLGVERF--LRIAPELYLKRLVVGGFEAVFEINR 250
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILtKSTPEGA--RDFLV-PSRLHPGKFyaLPQSPQLFKQLLMVSGFDRYFQIAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 251 CFRNEGMDLTHNPEFTTIEFYWAYHNYKDLMDLTEELFALLLEKLqLGKIIEfdgqkidfsKPFERITYKDALKKYGALS 330
Cdd:cd00777 78 CFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEV-LGVELT---------TPFPRMTYAEAMERYGFKF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 331 DEIIEnkdkiLEKLKKDgfEANDKLDLGHlqaELFDNYVESKLidPTFitdfpisisplsrRSDKNSEIAERFELFVCGR 410
Cdd:cd00777 148 LWIVD-----FPLFEWD--EEEGRLVSAH---HPFTAPKEEDL--DLL-------------EKDPEDARAQAYDLVLNGV 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488866119 411 ELANGFNELNDPLDQyERFLKQIeakNAGDEEACEMDEDFVNALGYGMPPTAGQGIGIDRLVMLLTNKKSIRDVILFP 488
Cdd:cd00777 203 ELGGGSIRIHDPDIQ-EKVFEIL---GLSEEEAEEKFGFLLEAFKYGAPPHGGIALGLDRLVMLLTGSESIRDVIAFP 276
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
122-488 |
5.08e-33 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 132.50 E-value: 5.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 122 KTGEFSLHASEITLATKSIV-PLPEKYHGLTDIEQRYRKRYVDMiMNAEVRKDFLTRSKVVSLIRHFFEEKGFLEVETPM 200
Cdd:PRK00476 89 PTGEIEVLASELEVLNKSKTlPFPIDDEEDVSEELRLKYRYLDL-RRPEMQKNLKLRSKVTSAIRNFLDDNGFLEIETPI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 201 M---HPiaGGAnakpfvtfhnslgveR-FL---RI----------APELYLKRLVVGGFEAVFEINRCFRNEgmDLTHN- 262
Cdd:PRK00476 168 LtksTP--EGA---------------RdYLvpsRVhpgkfyalpqSPQLFKQLLMVAGFDRYYQIARCFRDE--DLRADr 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 263 -PEFTTIEFYWAYHNYKDLMDLTEELFALLLEKLqLGkiiefdgqkIDFSKPFERITYKDALKKYGalSD--------EI 333
Cdd:PRK00476 229 qPEFTQIDIEMSFVTQEDVMALMEGLIRHVFKEV-LG---------VDLPTPFPRMTYAEAMRRYG--SDkpdlrfglEL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 334 I----------------------------------------------------------------------------ENK 337
Cdd:PRK00476 297 VdvtdlfkdsgfkvfagaandggrvkairvpggaaqlsrkqideltefakiygakglayikvnedglkgpiakflseEEL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 338 DKILEKLK-KDG---FEANDKLD-----LGHLQAELFDnyvESKLID-----PTFITDFPI------------------- 384
Cdd:PRK00476 377 AALLERTGaKDGdliFFGADKAKvvndaLGALRLKLGK---ELGLIDedkfaFLWVVDFPMfeydeeegrwvaahhpftm 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 385 ---SISPLSRRSDKNSEIAERFELfVCgrelaNGFnEL-------NDPLDQYERFlkqiEAKNAGDEEAcemDEDF---V 451
Cdd:PRK00476 454 pkdEDLDELETTDPGKARAYAYDL-VL-----NGY-ELgggsiriHRPEIQEKVF----EILGISEEEA---EEKFgflL 519
|
490 500 510
....*....|....*....|....*....|....*..
gi 488866119 452 NALGYGMPPTAGQGIGIDRLVMLLTNKKSIRDVILFP 488
Cdd:PRK00476 520 DALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
122-488 |
6.34e-30 |
|
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: 123.18 E-value: 6.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 122 KTGEFSLHASEITLATKSIV-PLPEKYHGLTDIEQRYRKRYVDMiMNAEVRKDFLTRSKVVSLIRHFFEEKGFLEVETPM 200
Cdd:COG0173 90 PTGEIEVLASELEILNKAKTpPFQIDDDTDVSEELRLKYRYLDL-RRPEMQKNLILRHKVTKAIRNYLDENGFLEIETPI 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 201 MhpIAG---GAnakpfvtfhnslgveR-FL---RI----------APELYLKRLVVGGFEAVFEINRCFRNEgmDLTHN- 262
Cdd:COG0173 169 L--TKStpeGA---------------RdYLvpsRVhpgkfyalpqSPQLFKQLLMVSGFDRYFQIARCFRDE--DLRADr 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 263 -PEFTTIEFYWAYHNYKDLMDLTEELFALLLEKLqLGkiiefdgqkIDFSKPFERITYKDALKKYGalSD--------EI 333
Cdd:COG0173 230 qPEFTQLDIEMSFVDQEDVFELMEGLIRHLFKEV-LG---------VELPTPFPRMTYAEAMERYG--SDkpdlrfglEL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 334 I---------------------------------------------------------------------------ENKD 338
Cdd:COG0173 298 VdvtdifkdsgfkvfagaaenggrvkainvpggaslsrkqideltefakqygakglayikvnedglkspiakflseEELA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 339 KILEKLK-KDG----FEAnDKLD-----LGHLQAELFDnyvESKLID-----PTFITDFPisispLSRRSDKNSEIA--- 400
Cdd:COG0173 378 AILERLGaKPGdlifFVA-DKPKvvnkaLGALRLKLGK---ELGLIDedefaFLWVVDFP-----LFEYDEEEGRWVamh 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 401 --------ERFELF--------------VCgrelaNGfNEL-------NDPLDQYERFlkqiEAKNAGDEEAcemDEDF- 450
Cdd:COG0173 449 hpftmpkdEDLDLLetdpgkvrakaydlVL-----NG-YELgggsiriHDPELQEKVF----ELLGISEEEA---EEKFg 515
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 488866119 451 --VNALGYGMPPTAGQGIGIDRLVMLLTNKKSIRDVILFP 488
Cdd:COG0173 516 flLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
60-491 |
4.65e-24 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 105.84 E-value: 4.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 60 ISGRLKLLRIAGKSIFANIEDENENLQIYFSKDSLGEEKFNLfKKNLEVGDIILAKGF----------PFVtKTGEFSLH 129
Cdd:PRK12820 23 LAGWVDAFRDHGELLFIHLRDRNGFIQAVFSPEAAPADVYEL-AASLRAEFCVALQGEvqkrleetenPHI-ETGDIEVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 130 ASEITLATKSIV---PLPEKY-----------HGLTDIEQRYRkrYVDmIMNAEVRKDFLTRSKVVSLIRHFFEEKGFLE 195
Cdd:PRK12820 101 VRELSILAASEAlpfAISDKAmtagagsagadAVNEDLRLQYR--YLD-IRRPAMQDHLAKRHRIIKCARDFLDSRGFLE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 196 VETPMMhPIAGGANAKPFVTFHNSLGVERF-LRIAPELYLKRLVVGGFEAVFEINRCFRNEGMDLTHNPEFTTIEFYWAY 274
Cdd:PRK12820 178 IETPIL-TKSTPEGARDYLVPSRIHPKEFYaLPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEFTQLDIEASF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 275 HNYKDLMDLTEELFAllleklqlgKIIEFDGqkIDFSKPFERITYKDALKKYG------------ALSDEIIENK----- 337
Cdd:PRK12820 257 IDEEFIFELIEELTA---------RMFAIGG--IALPRPFPRMPYAEAMDTTGsdrpdlrfdlkfADATDIFENTrygif 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 338 DKIL---------------EKLKKD---------------------------GFEAN-------DKLD------------ 356
Cdd:PRK12820 326 KQILqrggrikginikgqsEKLSKNvlqneyakeiapsfgakgmtwmraeagGLDSNivqffsaDEKEalkrrfhaedgd 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 357 ----------------LGHLQAELFD--NYVESKLIDPTFITDFPI-----------SISPLS---RRSDKNSEIAE--- 401
Cdd:PRK12820 406 viimiadascaivlsaLGQLRLHLADrlGLIPEGVFHPLWITDFPLfeatddggvtsSHHPFTapdREDFDPGDIEElld 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 402 ----RFELFVCGRELANGFNELNDPLDQYERFlkqiEAKNAGDEEACEMDEDFVNALGYGMPPTAGQGIGIDRLVMLLTN 477
Cdd:PRK12820 486 lrsrAYDLVVNGEELGGGSIRINDKDIQLRIF----AALGLSEEDIEDKFGFFLRAFDFAAPPHGGIALGLDRVVSMILQ 561
|
570
....*....|....
gi 488866119 478 KKSIRDVILFPAMR 491
Cdd:PRK12820 562 TPSIREVIAFPKNR 575
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
60-488 |
8.55e-24 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 104.87 E-value: 8.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 60 ISGRLKLLRIAGKSIFANIEDENENLQIYFSKDSLGEEKFNLfkKNLEVGDIILAKGF----PFV-----TKTGEFSLHA 130
Cdd:PLN02903 77 LCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDEFPEAHRTA--NRLRNEYVVAVEGTvrsrPQEspnkkMKTGSVEVVA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 131 SEITLATKSIVPLPEKYHGLTDI------EQRYRKRYVDM---IMNAEVRkdflTRSKVVSLIRHFFEEK-GFLEVETPM 200
Cdd:PLN02903 155 ESVDILNVVTKSLPFLVTTADEQkdsikeEVRLRYRVLDLrrpQMNANLR----LRHRVVKLIRRYLEDVhGFVEIETPI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 201 M-HPIAGGANAKPfVTFHNSLGVERFLRIAPELYLKRLVVGGFEAVFEINRCFRNEGMDLTHNPEFTTIEFYWAYHNYKD 279
Cdd:PLN02903 231 LsRSTPEGARDYL-VPSRVQPGTFYALPQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEFTQLDMELAFTPLED 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 280 LMDLTEELFALLLEKlqlgkiiefdGQKIDFSKPFERITYKDALKKYGA-------------LSDEIIE----------- 335
Cdd:PLN02903 310 MLKLNEDLIRQVFKE----------IKGVQLPNPFPRLTYAEAMSKYGSdkpdlryglelvdVSDVFAEssfkvfagale 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 336 ------------NKDKILEKLKKDGFEANDK-------------LDLGHL-------------QAE-------------- 363
Cdd:PLN02903 380 sggvvkaicvpdGKKISNNTALKKGDIYNEAiksgakglaflkvLDDGELegikalveslspeQAEqllaacgagpgdli 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 364 LFDN---------------YV--ESKLIDPT-----FITDFPI-SISPLSRR----------------SDKNSEIAERFE 404
Cdd:PLN02903 460 LFAAgptssvnktldrlrqFIakTLDLIDPSrhsilWVTDFPMfEWNEDEQRlealhhpftapnpedmGDLSSARALAYD 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 405 LFVCGRELANGfnelndPLDQYERFLKQ--IEAKNAGDEEACEMDEDFVNALGYGMPPTAGQGIGIDRLVMLLTNKKSIR 482
Cdd:PLN02903 540 MVYNGVEIGGG------SLRIYRRDVQQkvLEAIGLSPEEAESKFGYLLEALDMGAPPHGGIAYGLDRLVMLLAGAKSIR 613
|
....*.
gi 488866119 483 DVILFP 488
Cdd:PLN02903 614 DVIAFP 619
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
165-488 |
2.33e-19 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 88.92 E-value: 2.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 165 IMNAEVRKDFLTRSKVVSLIRHFFEEKGFLEVETPMMHPIA-----GGANAKPFVTFHNSLGVERFLRIAPELYlKRLVV 239
Cdd:PRK06462 21 ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIISPSTdplmgLGSDLPVKQISIDFYGVEYYLADSMILH-KQLAL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 240 GGFEAVFEINRCFRNEGMD---LTHNPEFTTIEFYWAYHNYKDLMDLTEELFALLLEKLQ---LGKIIEFDGQKIDFSKP 313
Cdd:PRK06462 100 RMLGKIFYLSPNFRLEPVDkdtGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLeehEDELEFFGRDLPHLKRP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 314 FERITYKDALKkygALSDEIIENKDKilEKLKKDGfEAndkldlghLQAELFDNyvesklidPTFITDFPISISPLSRRS 393
Cdd:PRK06462 180 FKRITHKEAVE---ILNEEGCRGIDL--EELGSEG-EK--------SLSEHFEE--------PFWIIDIPKGSREFYDRE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 394 DKNSE-IAERFELFvcgreLANGFNEL---NDPLDQYERFLKQIeaKNAG-DEEA----CEMDEDfvnalgyGMPPTAGQ 464
Cdd:PRK06462 238 DPERPgVLRNYDLL-----LPEGYGEAvsgGEREYEYEEIVERI--REHGvDPEKykwyLEMAKE-------GPLPSAGF 303
|
330 340
....*....|....*....|....
gi 488866119 465 GIGIDRLVMLLTNKKSIRDVILFP 488
Cdd:PRK06462 304 GIGVERLTRYICGLRHIREVQPFP 327
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
59-488 |
1.36e-18 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 88.61 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 59 VISGRLKLLRIAGKSIFANIEDENENLQ-IYFSKDSLGEEKFNLFKKNLEVGDIILAKGF------PFVTKTGEFSLHAS 131
Cdd:PLN02850 85 LIRGRVHTIRGKGKSAFLVLRQSGFTVQcVVFVSEVTVSKGMVKYAKQLSRESVVDVEGVvsvpkkPVKGTTQQVEIQVR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 132 EITLATKSIVPLP-----------EKYHGLTDIEQ--------RYRKRYVDMIMNAEvRKDFLTRSKVVSLIRHFFEEKG 192
Cdd:PLN02850 165 KIYCVSKALATLPfnvedaarsesEIEKALQTGEQlvrvgqdtRLNNRVLDLRTPAN-QAIFRIQSQVCNLFREFLLSKG 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 193 FLEVETPMMhpIAGGANAKPFVTFHNSLGVERFLRIAPELYLKRLVVGGFEAVFEINRCFRNEGmDLTHNP--EFTTIEF 270
Cdd:PLN02850 244 FVEIHTPKL--IAGASEGGSAVFRLDYKGQPACLAQSPQLHKQMAICGDFRRVFEIGPVFRAED-SFTHRHlcEFTGLDL 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 271 YWAYH-NYKDLMDLTEELFALLLEKL--QLGKIIEfdgqKIDFSKPFERITYkdaLKKYGALSDEiienkdKILEKLKKD 347
Cdd:PLN02850 321 EMEIKeHYSEVLDVVDELFVAIFDGLneRCKKELE----AIREQYPFEPLKY---LPKTLRLTFA------EGIQMLKEA 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 348 GFEANDKLDLGHLQAELFDNYVESKLIDPTFITD-FPISISPLSRRSD-KNSEIAERFELFVCGRELANGFNELNDPldq 425
Cdd:PLN02850 388 GVEVDPLGDLNTESERKLGQLVKEKYGTDFYILHrYPLAVRPFYTMPCpDDPKYSNSFDVFIRGEEIISGAQRVHDP--- 464
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488866119 426 yeRFLKQIEaknagdeEACEMD----EDFVNALGYGMPPTAGQGIGIDRLVMLLTNKKSIRDVILFP 488
Cdd:PLN02850 465 --ELLEKRA-------EECGIDvktiSTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFP 522
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
121-488 |
2.75e-16 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 81.58 E-value: 2.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 121 TKTGEFSLHASEITLATKSIVPLP---------EKYHGL-TDIEQRYRKRYVDMIMNAEvRKDFLTRSKVVSLIRHFFEE 190
Cdd:PTZ00401 151 TSHSDIELKVKKIHTVTESLRTLPftledasrkESDEGAkVNFDTRLNSRWMDLRTPAS-GAIFRLQSRVCQYFRQFLID 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 191 KGFLEVETPMM--HPIAGGANAKPFVTFHNslgvERFLRIAPELYLKRLVVGGFEAVFEINRCFRNEGMDL-THNPEFT- 266
Cdd:PTZ00401 230 SDFCEIHSPKIinAPSEGGANVFKLEYFNR----FAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNThRHLTEFVg 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 267 -TIEFYWAYHnYKDLMDLTEELFALLLEKLQlGKIIEFDGQKIDFskPFERITYKDALKKYGALSDEIIENKDKILEKLK 345
Cdd:PTZ00401 306 lDVEMRINEH-YYEVLDLAESLFNYIFERLA-THTKELKAVCQQY--PFEPLVWKLTPERMKELGVGVISEGVEPTDKYQ 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 346 KDGFEANDK-LDLGHLQA-ELFDNYVESKLiDPT-----------------------FITD-FPISISPLSRRSDKNSE- 398
Cdd:PTZ00401 382 ARVHNMDSRmLRINYMHCiELLNTVLEEKM-APTddinttnekllgklvkerygtdfFISDrFPSSARPFYTMECKDDEr 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 399 IAERFELFVCGRELANGFNELNDPldqyERFLKQIEAKNAGDEEAcemdEDFVNALGYGMPPTAGQGIGIDRLVMLLTNK 478
Cdd:PTZ00401 461 FTNSYDMFIRGEEISSGAQRIHDP----DLLLARAKMLNVDLTPI----KEYVDSFRLGAWPHGGFGVGLERVVMLYLGL 532
|
410
....*....|
gi 488866119 479 KSIRDVILFP 488
Cdd:PTZ00401 533 SNVRLASLFP 542
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
176-297 |
5.41e-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: 76.77 E-value: 5.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 176 TRSKVVSLIRHFFEEKGFLEVETPMMHPIAGGANA----KPFVTFHNSLGVERFLRIAPELYLKRLVVG----GFEAVFE 247
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAghepKDLLPVGAENEEDLYLRPTLEPGLVRLFVShirkLPLRLAE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 488866119 248 INRCFRNEG--MDLTHNPEFTTIEFYWAY------HNYKDLMDLTEELFALLLEKLQL 297
Cdd:cd00768 81 IGPAFRNEGgrRGLRRVREFTQLEGEVFGedgeeaSEFEELIELTEELLRALGIKLDI 138
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
59-488 |
4.23e-12 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 67.83 E-value: 4.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 59 VISGRLKLLRIAGKSIFANIEDEN--ENLQIYFSKDslgEEKFNLFKKnLEVGDIILAKGFpfVTKT----GEFSLHASE 132
Cdd:PRK03932 20 TVRGWVRTKRDSGKIAFLQLRDGScfKQLQVVKDNG---EEYFEEIKK-LTTGSSVIVTGT--VVESpragQGYELQATK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 133 ITLATKSIV--PLPEKYHG---LTDIEQ-RYRKRyvdmIMNAEVRkdflTRSKVVSLIRHFFEEKGFLEVETPMMHPIAG 206
Cdd:PRK03932 94 IEVIGEDPEdyPIQKKRHSiefLREIAHlRPRTN----KFGAVMR----IRNTLAQAIHEFFNENGFVWVDTPIITASDC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 207 -GAnAKPFVTFHNSL-------GVERFLRIAPELYLKRLVVGgFEAVFEINRCFRNEGMDLT-HNPEFTTIEFYWAYHNY 277
Cdd:PRK03932 166 eGA-GELFRVTTLDLdfskdffGKEAYLTVSGQLYAEAYAMA-LGKVYTFGPTFRAENSNTRrHLAEFWMIEPEMAFADL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 278 KDLMDLTEEL----FALLLEKLQlgKIIEFDGQKIDF----------SKPFERITYKDALkkygalsdeiienkdKILEK 343
Cdd:PRK03932 244 EDNMDLAEEMlkyvVKYVLENCP--DDLEFLNRRVDKgdierlenfiESPFPRITYTEAI---------------EILQK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 344 LKKDgFEANDK--LDLG--H---LQAELFDNyvesklidPTFITDFPISISPLSRRSDKNSEIAERFELFVCG------- 409
Cdd:PRK03932 307 SGKK-FEFPVEwgDDLGseHeryLAEEHFKK--------PVFVTNYPKDIKAFYMRLNPDGKTVAAMDLLAPGigeiigg 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 410 --RElangfnelndplDQYERFLKQIEAKNagdeeaceMD-EDFVNALG---YGMPPTAGQGIGIDRLVMLLTNKKSIRD 483
Cdd:PRK03932 378 sqRE------------ERLDVLEARIKELG--------LNkEDYWWYLDlrrYGSVPHSGFGLGFERLVAYITGLDNIRD 437
|
....*
gi 488866119 484 VILFP 488
Cdd:PRK03932 438 VIPFP 442
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
59-135 |
5.66e-10 |
|
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: 55.70 E-value: 5.66e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488866119 59 VISGRL-KLLRIAGKSIFANIEDENENLQIYFSKDSLGEekfnlFKKNLEVGDIILAKGFPFVTKTGEFSLHASEITL 135
Cdd:pfam01336 2 TVAGRVtSIRRSGGKLLFLTLRDGTGSIQVVVFKEEAEK-----LAKKLKEGDVVRVTGKVKKRKGGELELVVEEIEL 74
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
220-497 |
2.76e-06 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 49.99 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 220 LGVERFLRIAPELYLKRLVVGgFEAVFEINRCFRNEGMDLT-HNPEFTTIEFYWAYHNYKDLMDLTEE----LFALLLEK 294
Cdd:PLN02221 305 FGRQAFLTVSGQLQVETYACA-LSSVYTFGPTFRAENSHTSrHLAEFWMVEPEIAFADLEDDMNCAEAyvkyMCKWLLDK 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 295 LQ-----LGKIIE---FDGQKIDFSKPFERITYKDALKkygalsdeiienkdkILEKLKKDGFEANDKLDLGHLQAELFD 366
Cdd:PLN02221 384 CFddmelMAKNFDsgcIDRLRMVASTPFGRITYTEAIE---------------LLEEAVAKGKEFDNNVEWGIDLASEHE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 367 NYVESKLID-PTFITDFPISISPLSRRSDKNSEIAERFELFV--CGRELANGFNElndplDQYERFLKQIEAKNAgdeeA 443
Cdd:PLN02221 449 RYLTEVLFQkPLIVYNYPKGIKAFYMRLNDDEKTVAAMDVLVpkVGELIGGSQRE-----ERYDVIKQRIEEMGL----P 519
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 488866119 444 CEMDEDFVNALGYGMPPTAGQGIGIDRLVMLLTNKKSIRDVILFPAMrPLKSEL 497
Cdd:PLN02221 520 IEPYEWYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPRY-PGKADL 572
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
245-488 |
2.04e-05 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 47.17 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 245 VFEINRCFRNEGMD-LTHNPEFTTIEFYWAYHNYKDLMDLTEELFALLLEKL--QLGKIIEFDGQKID----------FS 311
Cdd:PLN02532 392 VYTFGPRFRADRIDsARHLAEMWMVEVEMAFSELEDAMNCAEDYFKFLCKWVleNCSEDMKFVSKRIDktistrleaiIS 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 312 KPFERITYKDALKkygalsdeiienkdkILEKLKKDGFEAndKLDLG-HLQAELFDNYVESKLIDPTFITDFPISISPLS 390
Cdd:PLN02532 472 SSLQRISYTEAVD---------------LLKQATDKKFET--KPEWGiALTTEHLSYLADEIYKKPVIIYNYPKELKPFY 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 391 RRSDKNSEIAERFELFV-------CGRE-------LANGFNELNDPLDQYERFLkqieaknagdeeacemdedfvNALGY 456
Cdd:PLN02532 535 VRLNDDGKTVAAFDLVVpkvgtviTGSQneermdiLNARIEELGLPREQYEWYL---------------------DLRRH 593
|
250 260 270
....*....|....*....|....*....|..
gi 488866119 457 GMPPTAGQGIGIDRLVMLLTNKKSIRDVILFP 488
Cdd:PLN02532 594 GTVKHSGFSLGFELMVLFATGLPDVRDAIPFP 625
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
35-488 |
3.10e-05 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 46.51 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 35 LADFKKKFSyIFDTENKRDESISSV-----ISGRLKLLRIAGKSIFANIEDEN--ENLQIYFSKDSLGEEKFNlfKKNLE 107
Cdd:PLN02603 83 VGEFRKKLR-IADVKGGEDEGLARVgktlnVMGWVRTLRAQSSVTFIEVNDGSclSNMQCVMTPDAEGYDQVE--SGLIT 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 108 VGDIILAKGFPFVTKTGE--FSLHASEITLATKSIVPLPEKyhgltdiEQRYRKRYVDMIMNAEVRKDFL-----TRSKV 180
Cdd:PLN02603 160 TGASVLVQGTVVSSQGGKqkVELKVSKIVVVGKSDPSYPIQ-------KKRVSREFLRTKAHLRPRTNTFgavarVRNAL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 181 VSLIRHFFEEKGFLEVETPMMHPI-AGGANAKPFVT--------FHNSL-------------------GVERFLRIAPEL 232
Cdd:PLN02603 233 AYATHKFFQENGFVWVSSPIITASdCEGAGEQFCVTtlipnsaeNGGSLvddipktkdglidwsqdffGKPAFLTVSGQL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 233 YLKRLVVGgFEAVFEINRCFRNEGMDLT-HNPEFTTIEFYWAYHNYKDLMDLTEELFALLLEKlqlgkIIEFDGQKIDF- 310
Cdd:PLN02603 313 NGETYATA-LSDVYTFGPTFRAENSNTSrHLAEFWMIEPELAFADLNDDMACATAYLQYVVKY-----ILENCKEDMEFf 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 311 ----------------SKPFERITYKDALKkygalsdeiienkdkILEKLKKDgFEANDKLDLgHLQAElFDNYVESKLI 374
Cdd:PLN02603 387 ntwiekgiidrlsdvvEKNFVQLSYTDAIE---------------LLLKAKKK-FEFPVKWGL-DLQSE-HERYITEEAF 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 375 D--PTFITDFPISISPLSRRSDKNSEIAERFELFV--CGrELANGfnelndplDQYERFLKQIEAKNagDEEACEMDED- 449
Cdd:PLN02603 449 GgrPVIIRDYPKEIKAFYMRENDDGKTVAAMDMLVprVG-ELIGG--------SQREERLEYLEARL--DELKLNKESYw 517
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 488866119 450 -FVNALGYGMPPTAGQGIGIDRLVMLLTNKKSIRDVILFP 488
Cdd:PLN02603 518 wYLDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFP 557
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
223-488 |
6.17e-04 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 42.32 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 223 ERFLRIAPELYLKRLVvGGFEAVFEINRCFRNEGMDLT-HNPEFTTIEFYWAYHNYKDLMDLTEELFallleKLQLGKII 301
Cdd:PTZ00425 325 QAFLTVSGQLSLENLC-SSMGDVYTFGPTFRAENSHTSrHLAEFWMIEPEIAFADLYDNMELAESYI-----KYCIGYVL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 302 EFDGQKIDFskpFERITYKDALKKYGALSDE-----IIENKDKILEKLKkDGFEANDKLDLgHLQAElFDNYVESKLID- 375
Cdd:PTZ00425 399 NNNFDDIYY---FEENVETGLISRLKNILDEdfakiTYTNVIDLLQPYS-DSFEVPVKWGM-DLQSE-HERFVAEQIFKk 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488866119 376 PTFITDFPISISPLSRRSDKNSEIAERFELFVCGRELANGFNELNDPLDQYERFLKqieaknagdEEACEMDED--FVNA 453
Cdd:PTZ00425 473 PVIVYNYPKDLKAFYMKLNEDQKTVAAMDVLVPKIGEVIGGSQREDNLERLDKMIK---------EKKLNMESYwwYRQL 543
|
250 260 270
....*....|....*....|....*....|....*
gi 488866119 454 LGYGMPPTAGQGIGIDRLVMLLTNKKSIRDVILFP 488
Cdd:PTZ00425 544 RKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFP 578
|
|
| PheRS_alpha_core |
cd00496 |
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ... |
245-288 |
6.40e-04 |
|
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure and the presence of three characteristic sequence motifs. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. While class II aaRSs generally aminoacylate the 3'-OH ribose of the appropriate tRNA, PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. PheRS is an alpha-2/ beta-2 tetramer.
Pssm-ID: 238277 [Multi-domain] Cd Length: 218 Bit Score: 41.38 E-value: 6.40e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 488866119 245 VFEINRCFRNEGMDLTHNPEFTTIEFYWAYHN--YKDLMDLTEELF 288
Cdd:cd00496 83 IFSIGRVYRNDEIDATHLPEFHQIEGLVVDKGltFADLKGTLEEFA 128
|
|
| tRNA-synt_2d |
pfam01409 |
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ... |
245-294 |
2.58e-03 |
|
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only phenylalanyl-tRNA synthetases. This is the core catalytic domain.
Pssm-ID: 396130 [Multi-domain] Cd Length: 245 Bit Score: 39.49 E-value: 2.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 488866119 245 VFEINRCFRNEGMDLTHNPEFTTIEFYWAYHNY--KDLMDLTEELFALLLEK 294
Cdd:pfam01409 105 IFSIGRVFRRDQVDATHLPEFHQVEGLVVDENVtfADLKGVLEEFLRKFFGF 156
|
|
| AsnA |
cd00645 |
Asparagine synthetase (aspartate-ammonia ligase) (AsnA) catalyses the conversion of ... |
427-484 |
4.58e-03 |
|
Asparagine synthetase (aspartate-ammonia ligase) (AsnA) catalyses the conversion of L-aspartate to L-asparagine in the presence of ATP and ammonia. AsnA is a homodimeric enzyme which is structurally similiar to the catalytic core domain of class II aminoacyl-tRNA synthetases. Ammonia-dependent AsnA is not homologous to the glutamine-dependent asparagine synthetase AsnB.
Pssm-ID: 238350 Cd Length: 309 Bit Score: 39.25 E-value: 4.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 488866119 427 ERFLKQIEAKNAGDEEACEMDEDFVNALgygMPPTAGQGIGIDRLVMLLTNKKSIRDV 484
Cdd:cd00645 242 ESLQKQLKLAGDEDRLELPFHKMLLNGE---LPQTIGGGIGQSRLCMFLLQKAHIGEV 296
|
|
| PLN02853 |
PLN02853 |
Probable phenylalanyl-tRNA synthetase alpha chain |
234-269 |
9.46e-03 |
|
Probable phenylalanyl-tRNA synthetase alpha chain
Pssm-ID: 215458 [Multi-domain] Cd Length: 492 Bit Score: 38.50 E-value: 9.46e-03
10 20 30
....*....|....*....|....*....|....*...
gi 488866119 234 LKRLVVGGFEA--VFEINRCFRNEGMDLTHNPEFTTIE 269
Cdd:PLN02853 332 LYKLAQKGFKPkrYFSIDRVFRNEAVDRTHLAEFHQVE 369
|
|
| |
