|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
80-602 |
0e+00 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 938.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 80 DREAIRSIRLKKVEELRGQGLEPYAYKWEKSHSANQLQEIYKHLANGEESDNEIdcVSIAGRVVARRAFGKLAFLTLRDD 159
Cdd:PLN02502 57 DPTQYRANRLKKVEALRAKGVEPYPYKFDVTHTAPELQEKYGSLENGEELEDVS--VSVAGRIMAKRAFGKLAFYDLRDD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 160 SGTIQLYCEKERLSDDQ--FEQLKQFIDIGDILGASGSMKRTEKGELSICVNSFSILTKSLLPLPDKYHGLTDIDKRYRQ 237
Cdd:PLN02502 135 GGKIQLYADKKRLDLDEeeFEKLHSLVDRGDIVGVTGTPGKTKKGELSIFPTSFEVLTKCLLMLPDKYHGLTDQETRYRQ 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 238 RYVDMIANPEVADVFRRRAKIVSEIRKTVESFGYLEVETPVLQGAAGGAEARPFVTFHNSLGRDLYLRIATELHLKRMLV 317
Cdd:PLN02502 215 RYLDLIANPEVRDIFRTRAKIISYIRRFLDDRGFLEVETPMLNMIAGGAAARPFVTHHNDLNMDLYLRIATELHLKRLVV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 318 GGFEKVYEIGRIFRNEGISTRHNPEFTTIEMYEAYSDYHSMMDMAELIVTQCSMAVNGKLTIDYQGTEICLERPWRRETM 397
Cdd:PLN02502 295 GGFERVYEIGRQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKELTGSYKIKYHGIEIDFTPPFRRISM 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 398 HNLVKEITGINFSElgedlgNAKDTVLLALQDVLEPKDKSGIRACSSLGHLLNEIFEVVVEPKLVQPTFVLDYPIEISPL 477
Cdd:PLN02502 375 ISLVEEATGIDFPA------DLKSDEANAYLIAACEKFDVKCPPPQTTGRLLNELFEEFLEETLVQPTFVLDHPVEMSPL 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 478 AKPHRGNAGLTERFELFICGREMANAFSELTDPVDQRTRLEEQVRQHNAkraeavrespepnakkddddDESYEVTLDED 557
Cdd:PLN02502 449 AKPHRSKPGLTERFELFINGRELANAFSELTDPVDQRERFEEQVKQHNA--------------------GDDEAMALDED 508
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 15231261 558 FLTALEYGMPPASGMGLGIDRLVMLLTNSASIRDVIAFPVLKLQQ 602
Cdd:PLN02502 509 FCTALEYGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFPAMKPQD 553
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
80-599 |
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: 786.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 80 DREAIRSIRLKKVEELRGQGLEPYAYKWEKSHSANQLQEIYKHLANGEESDNEidcVSIAGRVVARRAFGKLAFLTLRDD 159
Cdd:COG1190 6 DLNEQIRVRREKLEELREAGIDPYPNKFPRTHTAAEIREKYDELEAEEETGDE---VSVAGRIMAKRDMGKASFADLQDG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 160 SGTIQLYCEKERLSDDQFEQLKQfIDIGDILGASGSMKRTEKGELSICVNSFSILTKSLLPLPDKYHGLTDIDKRYRQRY 239
Cdd:COG1190 83 SGRIQLYLRRDELGEEAYELFKL-LDLGDIVGVEGTVFRTKTGELSVKVEELTLLSKSLRPLPEKFHGLTDPETRYRQRY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 240 VDMIANPEVADVFRRRAKIVSEIRKTVESFGYLEVETPVLQGAAGGAEARPFVTFHNSLGRDLYLRIATELHLKRMLVGG 319
Cdd:COG1190 162 VDLIVNPEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 320 FEKVYEIGRIFRNEGISTRHNPEFTTIEMYEAYSDYHSMMDMAELIVTQCSMAVNGKLTIDYQGTEICLERPWRRETMHN 399
Cdd:COG1190 242 FERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGTTKVTYQGQEIDLSPPWRRITMVE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 400 LVKEITGINFSELgEDLGNAKDtVLLALQDVLEPKDksgiracsSLGHLLNEIFEVVVEPKLVQPTFVLDYPIEISPLAK 479
Cdd:COG1190 322 AIKEATGIDVTPL-TDDEELRA-LAKELGIEVDPGW--------GRGKLIDELFEELVEPKLIQPTFVTDYPVEVSPLAK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 480 PHRGNAGLTERFELFICGREMANAFSELTDPVDQRTRLEEQVRQhnakraeavrespepnakKDDDDDESYEvtLDEDFL 559
Cdd:COG1190 392 RHRDDPGLTERFELFIAGREIANAFSELNDPIDQRERFEEQLEL------------------KAAGDDEAMP--MDEDFL 451
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15231261 560 TALEYGMPPASGMGLGIDRLVMLLTNSASIRDVIAFPVLK 599
Cdd:COG1190 452 RALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFPLMR 491
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
87-599 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 778.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 87 IRLKKVEELRGQGLEPYAYKWEKSHSANQLQEIYKHLaNGEESDNEIDCVSIAGRVVARRAFGKLAFLTLRDDSGTIQLY 166
Cdd:PRK00484 9 VRREKLAELREQGIDPYPNKFERTHTAAELRAKYDDK-EKEELEELEIEVSVAGRVMLKRVMGKASFATLQDGSGRIQLY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 167 CEKERLSDDQFEQLKQfIDIGDILGASGSMKRTEKGELSICVNSFSILTKSLLPLPDKYHGLTDIDKRYRQRYVDMIANP 246
Cdd:PRK00484 88 VSKDDVGEEALEAFKK-LDLGDIIGVEGTLFKTKTGELSVKATELTLLTKSLRPLPDKFHGLTDVETRYRQRYVDLIVNP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 247 EVADVFRRRAKIVSEIRKTVESFGYLEVETPVLQGAAGGAEARPFVTFHNSLGRDLYLRIATELHLKRMLVGGFEKVYEI 326
Cdd:PRK00484 167 ESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARPFITHHNALDIDLYLRIAPELYLKRLIVGGFERVYEI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 327 GRIFRNEGISTRHNPEFTTIEMYEAYSDYHSMMDMAELIVTQCSMAVNGKLTIDYQGTEICLERPWRRETMHNLVKEITG 406
Cdd:PRK00484 247 GRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTYQGTEIDFGPPFKRLTMVDAIKEYTG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 407 INFSELGEDLgnakdtvLLALQDVLEPKdksgIRACSSLGHLLNEIFEVVVEPKLVQPTFVLDYPIEISPLAKPHRGNAG 486
Cdd:PRK00484 327 VDFDDMTDEE-------ARALAKELGIE----VEKSWGLGKLINELFEEFVEPKLIQPTFITDYPVEISPLAKRHREDPG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 487 LTERFELFICGREMANAFSELTDPVDQRTRLEEQVRQhnakraeavrespepnakKDDDDDESYEvtLDEDFLTALEYGM 566
Cdd:PRK00484 396 LTERFELFIGGREIANAFSELNDPIDQRERFEAQVEA------------------KEAGDDEAMF--MDEDFLRALEYGM 455
|
490 500 510
....*....|....*....|....*....|...
gi 15231261 567 PPASGMGLGIDRLVMLLTNSASIRDVIAFPVLK 599
Cdd:PRK00484 456 PPTGGLGIGIDRLVMLLTDSPSIRDVILFPLMR 488
|
|
| lysS_bact |
TIGR00499 |
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ... |
88-601 |
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: 645.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 88 RLKKVEELRGQGLEPYAYKWEKSHSANQLQEIYKHLANGEESDNEIdCVSIAGRVVARRAFGKLAFLTLRDDSGTIQLYC 167
Cdd:TIGR00499 9 RLEKLNRLRQTGNNPYLHKFERTHSAQEFQEKYADLSNEELKEKEL-KVSIAGRIKAIRSMGKATFITLQDESGQIQLYV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 168 EKERLSDDQFEQLKQFIDIGDILGASGSMKRTEKGELSICVNSFSILTKSLLPLPDKYHGLTDIDKRYRQRYVDMIANPE 247
Cdd:TIGR00499 88 NKNKLPEDFYEFDEYLLDLGDIIGVTGYPFKTKTGELSVKVTELQILTKCLQPLPDKWHGLTDQETRYRQRYLDLIVNPD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 248 VADVFRRRAKIVSEIRKTVESFGYLEVETPVLQGAAGGAEARPFVTFHNSLGRDLYLRIATELHLKRMLVGGFEKVYEIG 327
Cdd:TIGR00499 168 VRQTFLKRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKPFITHHNALDMDLYLRIAPELYLKRLIVGGLEKVYEIG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 328 RIFRNEGISTRHNPEFTTIEMYEAYSDYHSMMDMAELIVTQCSMAVNGKLTIDYQGTEICLERPWRRETMHNLVKEITGI 407
Cdd:TIGR00499 248 RVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTFIINYNDLEIDLKPPWKRITMVDALEMVTGI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 408 NFSELgEDLGNAKdtvLLALQDVLEPKDKsgiraCSSLGHLLNEIFEVVVEPKLVQPTFVLDYPIEISPLAKPHRGNAGL 487
Cdd:TIGR00499 328 DFDIL-KDDETAK---ALAKEHGIEVAED-----SLTLGHILNKFFEQFLEHTLIQPTFITHYPAEISPLAKRDPSNPEF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 488 TERFELFICGREMANAFSELTDPVDQRTRLEEQVRQhnakraeavrespepnakKDDDDDESYEVtlDEDFLTALEYGMP 567
Cdd:TIGR00499 399 TERFELFIAGKEIANAYSELNDPLDQRERFEQQLAE------------------KEAGDDEAQLV--DEDFVEALEYGMP 458
|
490 500 510
....*....|....*....|....*....|....
gi 15231261 568 PASGMGLGIDRLVMLLTNSASIRDVIAFPVLKLQ 601
Cdd:TIGR00499 459 PTGGLGIGIDRLVMLLTDAPSIRDVLLFPQLRPQ 492
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
245-599 |
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: 543.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 245 NPEVADVFRRRAKIVSEIRKTVESFGYLEVETPVLQGAAGGAEARPFVTFHNSLGRDLYLRIATELHLKRMLVGGFEKVY 324
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 325 EIGRIFRNEGISTRHNPEFTTIEMYEAYSDYHSMMDMAELIVTQCSMAVNGKLTIDYQGTEICLERPWRRETMHNLVKEI 404
Cdd:cd00775 81 EIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIEYGGKELDFTPPFKRVTMVDALKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 405 TGINFSElgedlgnakdTVLLALQDVLEPKDKSGIRACS---SLGHLLNEIFEVVVEPKLVQPTFVLDYPIEISPLAKPH 481
Cdd:cd00775 161 TGIDFPE----------LDLEQPEELAKLLAKLIKEKIEkprTLGKLLDKLFEEFVEPTLIQPTFIIDHPVEISPLAKRH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 482 RGNAGLTERFELFICGREMANAFSELTDPVDQRTRLEEQVRQHNAKRAEAvrespepnakkdddddesyeVTLDEDFLTA 561
Cdd:cd00775 231 RSNPGLTERFELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEA--------------------MMMDEDFVTA 290
|
330 340 350
....*....|....*....|....*....|....*...
gi 15231261 562 LEYGMPPASGMGLGIDRLVMLLTNSASIRDVIAFPVLK 599
Cdd:cd00775 291 LEYGMPPTGGLGIGIDRLVMLLTDSNSIRDVILFPAMR 328
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
87-602 |
7.78e-163 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 493.71 E-value: 7.78e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 87 IRLKKVEELRGQGLEPYAYKWEKSHSANQlqeiykhlANGEESDNEidcVSIAGRVVARRAFGKLAFLTLRDDSGTIQLY 166
Cdd:PRK02983 616 VRLAKLEALRAAGVDPYPVGVPPTHTVAE--------ALDAPTGEE---VSVSGRVLRIRDYGGVLFADLRDWSGELQVL 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 167 CEKERLSDDQFEQLKQFIDIGDILGASGSMKRTEKGELSICVNSFSILTKSLLPLPDKYHGLTDIDKRYRQRYVDMIANP 246
Cdd:PRK02983 685 LDASRLEQGSLADFRAAVDLGDLVEVTGTMGTSRNGTLSLLVTSWRLAGKCLRPLPDKWKGLTDPEARVRQRYLDLAVNP 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 247 EVADVFRRRAKIVSEIRKTVESFGYLEVETPVLQGAAGGAEARPFVTFHNSLGRDLYLRIATELHLKRMLVGGFEKVYEI 326
Cdd:PRK02983 765 EARDLLRARSAVVRAVRETLVARGFLEVETPILQQVHGGANARPFVTHINAYDMDLYLRIAPELYLKRLCVGGVERVFEL 844
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 327 GRIFRNEGISTRHNPEFTTIEMYEAYSDYHSMMDMAELIVTQCSMAVNGKLTIDYQGTEICLER-----PWRRETMHNLV 401
Cdd:PRK02983 845 GRNFRNEGVDATHNPEFTLLEAYQAHADYDTMRDLTRELIQNAAQAAHGAPVVMRPDGDGVLEPvdisgPWPVVTVHDAV 924
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 402 KEitginfsELGEDLGnaKDTVLLALQDVLepkDKSGIRACS--SLGHLLNEIFEVVVEPKLVQPTFVLDYPIEISPLAK 479
Cdd:PRK02983 925 SE-------ALGEEID--PDTPLAELRKLC---DAAGIPYRTdwDAGAVVLELYEHLVEDRTTFPTFYTDFPTSVSPLTR 992
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 480 PHRGNAGLTERFELFICGREMANAFSELTDPVDQRTRLEEQvrqhnAKRAEAvrespepnakkddDDDESYEvtLDEDFL 559
Cdd:PRK02983 993 PHRSDPGLAERWDLVAWGVELGTAYSELTDPVEQRRRLTEQ-----SLLAAG-------------GDPEAME--LDEDFL 1052
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 15231261 560 TALEYGMPPASGMGLGIDRLVMLLTNsASIRDVIAFPVLKLQQ 602
Cdd:PRK02983 1053 QALEYAMPPTGGLGMGVDRLVMLLTG-RSIRETLPFPLVKPRQ 1094
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
88-602 |
4.11e-138 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 411.76 E-value: 4.11e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 88 RLKKVEELRGQGLePYAYKWEKSHSANQLQEIYKHLANGEESDNEIDcVSIAGRVVARRAFGKLAFLTLRDDSGTIQLYC 167
Cdd:PRK12445 22 RREKLAALRQQGV-AFPNDFRRDHTSDQLHEEFDAKDNQELESLNIE-VSVAGRMMTRRIMGKASFVTLQDVGGRIQLYV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 168 EKERLSDDQF-EQLKQFiDIGDILGASGSMKRTEKGELSICVNSFSILTKSLLPLPDKYHGLTDIDKRYRQRYVDMIANP 246
Cdd:PRK12445 100 ARDSLPEGVYnDQFKKW-DLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFHGLQDQEVRYRQRYLDLIAND 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 247 EVADVFRRRAKIVSEIRKTVESFGYLEVETPVLQGAAGGAEARPFVTFHNSLGRDLYLRIATELHLKRMLVGGFEKVYEI 326
Cdd:PRK12445 179 KSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGFERVFEI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 327 GRIFRNEGISTRHNPEFTTIEMYEAYSDYHSMMDMAELIVTQCSMAVNGKLTIDYQGTEICLERPWRRETMHNLVKEI-T 405
Cdd:PRK12445 259 NRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFDFGKPFEKLTMREAIKKYrP 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 406 GINFSelgeDLGNAKDTVLLAlqdvlepkDKSGIRACSS--LGHLLNEIFEVVVEPKLVQPTFVLDYPIEISPLAKPHRG 483
Cdd:PRK12445 339 ETDMA----DLDNFDAAKALA--------ESIGITVEKSwgLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDV 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 484 NAGLTERFELFICGREMANAFSELTDPVDQRTRLEEQVrqhnakraeavrespepNAKKDDDDDESYevtLDEDFLTALE 563
Cdd:PRK12445 407 NPEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQV-----------------NAKAAGDDEAMF---YDEDYVTALE 466
|
490 500 510
....*....|....*....|....*....|....*....
gi 15231261 564 YGMPPASGMGLGIDRLVMLLTNSASIRDVIAFPVLKLQQ 602
Cdd:PRK12445 467 YGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFPAMRPQK 505
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
80-599 |
2.41e-119 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 368.59 E-value: 2.41e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 80 DREAIRSIRLKKVEELRGQGLEPYAYK-WEKSHSANQLQEIYKHLANGEESDNEIdcVSIAGRVVARRAFGKLAFLTLRD 158
Cdd:PTZ00385 55 KASATKTVTQEASRAPRSKLDLPAAYSsFRGITPISEVRERYGYLASGDRAAQAT--VRVAGRVTSVRDIGKIIFVTIRS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 159 DSGTIQLYCE-KERLSDDQFEQLKQFIDIGDILGASGSMKRTEKGELSICVNSFSILT------KSLLPLPDKYHGLTDI 231
Cdd:PTZ00385 133 NGNELQVVGQvGEHFTREDLKKLKVSLRVGDIIGADGVPCRMQRGELSVAASRMLILSpyvctdQVVCPNLRGFTVLQDN 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 232 DKRYRQRYVDMIANPEVADVFRRRAKIVSEIRKTVESFGYLEVETPVLQGAAGGAEARPFVTFHNSLGRDLYLRIATELH 311
Cdd:PTZ00385 213 DVKYRYRFTDMMTNPCVIETIKKRHVMLQALRDYFNERNFVEVETPVLHTVASGANAKSFVTHHNANAMDLFLRVAPELH 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 312 LKRMLVGGFEKVYEIGRIFRNEGISTRHNPEFTTIEMYEAYSDYHSMMDMAELIVTQCSMAVNGKLTIDYQ-------GT 384
Cdd:PTZ00385 293 LKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTSCEFYAAYHTYEDLMPMTEDIFRQLAMRVNGTTVVQIYpenahgnPV 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 385 EICLERPWRRETMHNLVKEITGINF---SELGEDLGNAKDTVLLALQDVLEPkdksgirACSSLGHLLNEIFEVVVEPKL 461
Cdd:PTZ00385 373 TVDLGKPFRRVSVYDEIQRMSGVEFpppNELNTPKGIAYMSVVMLRYNIPLP-------PVRTAAKMFEKLIDFFITDRV 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 462 VQPTFVLDYPIEISPLAKPHRGNAGLTERFELFICGREMANAFSELTDPVDQRTRLEEQVRQHNAKRAEAvrespepnak 541
Cdd:PTZ00385 446 VEPTFVMDHPLFMSPLAKEQVSRPGLAERFELFVNGIEYCNAYSELNDPHEQYHRFQQQLVDRQGGDEEA---------- 515
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15231261 542 kdddddesyeVTLDEDFLTALEYGMPPASGMGLGIDRLVMLLTNSASIRDVIAFPVLK 599
Cdd:PTZ00385 516 ----------MPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFPLLR 563
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
88-599 |
2.82e-116 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 358.17 E-value: 2.82e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 88 RLKKVEELRGQGLEPYAYKWEKSHSANQLQEIYKHLANGEESDNEIdcVSIAGRVVARRAFG-KLAFLTLRDDSGTIQLY 166
Cdd:PTZ00417 89 RSKFIQEQKAKGINPYPHKFERTITVPEFVEKYQDLASGEHLEDTI--LNVTGRIMRVSASGqKLRFFDLVGDGAKIQVL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 167 CEK--ERLSDDQFEQLKQFIDIGDILGASGSMKRTEKGELSICVNSFSILTKSLLPLPDKYhGLTDIDKRYRQRYVDMIA 244
Cdd:PTZ00417 167 ANFafHDHTKSNFAECYDKIRRGDIVGIVGFPGKSKKGELSIFPKETIILSPCLHMLPMKY-GLKDTEIRYRQRYLDLMI 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 245 NPEVADVFRRRAKIVSEIRKTVESFGYLEVETPVLQGAAGGAEARPFVTFHNSLGRDLYLRIATELHLKRMLVGGFEKVY 324
Cdd:PTZ00417 246 NESTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLVAGGANARPFITHHNDLDLDLYLRIATELPLKMLIVGGIDKVY 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 325 EIGRIFRNEGISTRHNPEFTTIEMYEAYSDYHSMMDMAELIVTQCSMAVNGKLTIDY-------QGTEICLERPWRRETm 397
Cdd:PTZ00417 326 EIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHLFGTYKILYnkdgpekDPIEIDFTPPYPKVS- 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 398 hnLVKEITGINFSELgEDLGNAKDTVLLALQDVLEpkDKSGIRACSSLGHLLNEIFEVVVEPKLV-QPTFVLDYPIEISP 476
Cdd:PTZ00417 405 --IVEELEKLTNTKL-EQPFDSPETINKMINLIKE--NKIEMPNPPTAAKLLDQLASHFIENKYPnKPFFIIEHPQIMSP 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 477 LAKPHRGNAGLTERFELFICGREMANAFSELTDPVDQRTRLEEQvrqhnakraeavrespepnaKKDDDDDESYEVTLDE 556
Cdd:PTZ00417 480 LAKYHRSKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQ--------------------QKDREKGDAEAFQFDA 539
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 15231261 557 DFLTALEYGMPPASGMGLGIDRLVMLLTNSASIRDVIAFPVLK 599
Cdd:PTZ00417 540 AFCTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFPTMR 582
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
230-599 |
8.42e-106 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 321.82 E-value: 8.42e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 230 DIDKRYRQRYVDMIaNPEVADVFRRRAKIVSEIRKTVESFGYLEVETPVLQGAAGGAEARPFVTFHNSLGRDLYLRIATE 309
Cdd:pfam00152 1 DEETRLKYRYLDLR-RPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 310 LHLKRMLVGGFEKVYEIGRIFRNEGISTRHNPEFTTIEMYEAYSDYHSMMDMAELIVTQCSMAVNGKLTIDYQGTEICLE 389
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 390 RPWRRETMHNLVKEITGINFSELGEDLgnakdtvllalqdvlepkDKSGIRAcsslghllneIFEVVVEPKLVQPTFVLD 469
Cdd:pfam00152 160 KPFPRITYAEAIEKLNGKDVEELGYGS------------------DKPDLRF----------LLELVIDKNKFNPLWVTD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 470 YPIEISPLAKPHRGN-AGLTERFELFICGREMANAFSELTDPVDQRTRLEEQVrqhnakraeavrESPEPNAKKddddde 548
Cdd:pfam00152 212 FPAEHHPFTMPKDEDdPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQG------------LDPEEAEEK------ 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 15231261 549 syevtlDEDFLTALEYGMPPASGMGLGIDRLVMLLTNSASIRDVIAFPVLK 599
Cdd:pfam00152 274 ------FGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAFPKTR 318
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
252-599 |
2.59e-83 |
|
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: 262.03 E-value: 2.59e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 252 FRRRAKIVSEIRKTVESFGYLEVETPVLQGAAGGAEARPFVTFHNSLGRDLYLRIATELHLKRMLVGGFEKVYEIGRIFR 331
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 332 NEGISTRHNPEFTTIEMYEAYSDYHSMMDMAELIVTQCSMAVNGKLTIDYQGTEICLERPWRRETMHNLVKeitginfse 411
Cdd:cd00669 81 NEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYGFELEDFGLPFPRLTYREALE--------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 412 lgedlgnakdtvllalqdvlepkdksgiracsslghllneifevvvepKLVQPTFVLDYPIEI-SPLAKPHRGNAGLTER 490
Cdd:cd00669 152 ------------------------------------------------RYGQPLFLTDYPAEMhSPLASPHDVNPEIADA 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 491 FELFICGREMANAFSELTDPVDQRTRLEEQVRQHnakraEAVRESpepnakkdddddesyevtlDEDFLTALEYGMPPAS 570
Cdd:cd00669 184 FDLFINGVEVGNGSSRLHDPDIQAEVFQEQGINK-----EAGMEY-------------------FEFYLKALEYGLPPHG 239
|
330 340
....*....|....*....|....*....
gi 15231261 571 GMGLGIDRLVMLLTNSASIRDVIAFPVLK 599
Cdd:cd00669 240 GLGIGIDRLIMLMTNSPTIREVIAFPKMR 268
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
253-594 |
7.22e-78 |
|
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: 7.22e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 253 RRRAKIVSEIRKTVESFGYLEVETPVLQgAAGGAEA--RPFVT---FHNSLGRDLYLRIATELHLKRMLVGGFEKVYEIG 327
Cdd:COG2269 7 RARARLLAAIRAFFAERGVLEVETPALS-VAPGTDPhlDSFATefiGPDGGGRPLYLHTSPEFAMKRLLAAGSGPIYQIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 328 RIFRNEGISTRHNPEFTTIEMYEAYSDYHSMMD-MAELI--VTQCSmavngkltidyqgteicLERPWRRETMHNLVKEI 404
Cdd:COG2269 86 KVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDeVEALLqlVLGAA-----------------GFAPAERLSYQEAFLRY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 405 TGINFSELGEDlgnakdtvllALQDVLEpkdKSGIRACSSLGH--LLNEIFEVVVEPKLVQ--PTFVLDYPIEISPLAKP 480
Cdd:COG2269 149 LGIDPLTADLD----------ELAAAAA---AAGLRVADDDDRddLLDLLLSERVEPQLGRdrPTFLYDYPASQAALARI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 481 HRGNAGLTERFELFICGREMANAFSELTDPVDQRTRLEEQvrqhNAKRAEAVRESPEpnakkdddddesyevtLDEDFLT 560
Cdd:COG2269 216 SPDDPRVAERFELYACGVELANGFHELTDAAEQRRRFEAD----NAERERLGLPPYP----------------IDERFLA 275
|
330 340 350
....*....|....*....|....*....|....
gi 15231261 561 ALEYGMPPASGMGLGIDRLVMLLTNSASIRDVIA 594
Cdd:COG2269 276 ALAAGLPDCSGVALGFDRLLMLALGAERIDDVLA 309
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
270-594 |
5.90e-75 |
|
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: 240.92 E-value: 5.90e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 270 GYLEVETPVLQgAAGGAEA--RPF-VTFHNSLG--RDLYLRIATELHLKRMLVGGFEKVYEIGRIFRNEGISTRHNPEFT 344
Cdd:TIGR00462 6 GVLEVETPLLS-PAPVTDPhlDAFaTEFVGPDGqgRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRHNPEFT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 345 TIEMYEAYSDYHSMMDMAELIVTQCSMAvngkltidyqgteicLERPWRRETMHNLVKEITGInfselgeDLGNAKDTvl 424
Cdd:TIGR00462 85 MLEWYRPGFDYHDLMDEVEALLQELLGD---------------PFAPAERLSYQEAFLRYAGI-------DPLTASLA-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 425 lALQDVLEPKdksGIRAcsSLGHLLNEIFEVV----VEPKLVQ--PTFVLDYPIEISPLAKPHRGNAGLTERFELFICGR 498
Cdd:TIGR00462 141 -ELQAAAAAH---GIRA--SEEDDRDDLLDLLfsekVEPHLGFgrPTFLYDYPASQAALARISPDDPRVAERFELYIKGL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 499 EMANAFSELTDPVDQRTRLEEQvrqhNAKRAEAVRESPEpnakkdddddesyevtLDEDFLTALEYGMPPASGMGLGIDR 578
Cdd:TIGR00462 215 ELANGFHELTDAAEQRRRFEAD----NALRKALGLPRYP----------------LDERFLAALEAGLPECSGVALGVDR 274
|
330
....*....|....*.
gi 15231261 579 LVMLLTNSASIRDVIA 594
Cdd:TIGR00462 275 LLMLALGADSIDDVLA 290
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
242-592 |
6.07e-56 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 191.30 E-value: 6.07e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 242 MIANpevadvFRRRAKIVSEIRKTVESFGYLEVETPVLQGAAG-GAEARPFVTFHNSLGRD----LYLRIATELHLKRML 316
Cdd:PRK09350 1 SIPN------LLKRAKIIAEIRRFFADRGVLEVETPILSQATVtDIHLVPFETRFVGPGASqgktLWLMTSPEYHMKRLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 317 VGGFEKVYEIGRIFRNEGISTRHNPEFTTIEMYEAYSDYHSMMDMAELIVTQCSmavngkltidyqgteICleRPWRRET 396
Cdd:PRK09350 75 AAGSGPIFQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVL---------------DC--EPAESLS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 397 MHNLVKEITGINfsELGEDLGNakdtvllaLQDVLEPKDKSGIRA-CSSLGHLLNEIFEVVVEPKLVQ--PTFVLDYPIE 473
Cdd:PRK09350 138 YQQAFLRYLGID--PLSADKTQ--------LREVAAKLGLSNIADeEEDRDTLLQLLFTFGVEPNIGKekPTFVYHFPAS 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 474 ISPLAKPHRGNAGLTERFELFICGREMANAFSELTDPVDQRTRLEeqvrQHNAKRAEavRESPepnakkdddddesyEVT 553
Cdd:PRK09350 208 QAALAKISTEDHRVAERFEVYFKGIELANGFHELTDAREQRQRFE----QDNRKRAA--RGLP--------------QQP 267
|
330 340 350
....*....|....*....|....*....|....*....
gi 15231261 554 LDEDFLTALEYGMPPASGMGLGIDRLVMLLTNSASIRDV 592
Cdd:PRK09350 268 IDENLIAALEAGLPDCSGVALGVDRLIMLALGAESISEV 306
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
136-242 |
1.22e-52 |
|
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These enzymes are homodimeric class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Included in this group are E. coli LysS and LysU. These two isoforms of LysRS are encoded by distinct genes which are differently regulated. Eukaryotes contain 2 sets of aaRSs, both of which encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Saccharomyces cerevisiae cytoplasmic and mitochondrial LysRSs have been shown to participate in the mitochondrial import of the only nuclear-encoded tRNA of S. cerevisiae (tRNAlysCUU). The gene for human LysRS encodes both the cytoplasmic and the mitochondrial isoforms of LysRS. In addition to their housekeeping role, human lysRS may function as a signaling molecule that activates immune cells and tomato LysRS may participate in a root-specific process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging.
Pssm-ID: 239817 [Multi-domain] Cd Length: 108 Bit Score: 175.36 E-value: 1.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 136 VSIAGRVVARRAFGKLAFLTLRDDSGTIQLYCEKERLSDDQFEQLKQFIDIGDILGASGSMKRTEKGELSICVNSFSILT 215
Cdd:cd04322 2 VSVAGRIMSKRGSGKLSFADLQDESGKIQVYVNKDDLGEEEFEDFKKLLDLGDIIGVTGTPFKTKTGELSIFVKEFTLLS 81
|
90 100
....*....|....*....|....*..
gi 15231261 216 KSLLPLPDKYHGLTDIDKRYRQRYVDM 242
Cdd:cd04322 82 KSLRPLPEKFHGLTDVETRYRQRYLDL 108
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
118-596 |
4.02e-43 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 160.36 E-value: 4.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 118 EIYKHLaNGEEsdneidcVSIAGRVVARRAFGKLAFLTLRDDSGTIQLYCEKERlSDDQFEQLKQfIDIGDILGASGSMK 197
Cdd:PRK05159 9 ELTPEL-DGEE-------VTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKV-DEELFETIKK-LKRESVVSVTGTVK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 198 RTEK--GELSICVNSFSILTKSLLPLPDKYHG--LTDIDKRYRQRYVDmIANPEVADVFRRRAKIVSEIRKTVESFGYLE 273
Cdd:PRK05159 79 ANPKapGGVEVIPEEIEVLNKAEEPLPLDISGkvLAELDTRLDNRFLD-LRRPRVRAIFKIRSEVLRAFREFLYENGFTE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 274 VETP--VLQGAAGGAEARPFVTFhnslGRDLYLRIATELHlKRMLVG-GFEKVYEIGRIFRNEGIST-RHNPEFTTI--E 347
Cdd:PRK05159 158 IFTPkiVASGTEGGAELFPIDYF----EKEAYLAQSPQLY-KQMMVGaGFERVFEIGPVFRAEEHNTsRHLNEYTSIdvE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 348 MyeAYSD-YHSMMDMAELIVTQCSMAVNGKLTIDYQGTEICLERPwrretmhnlVKEITGINFSElgedlgnAKDtVLLA 426
Cdd:PRK05159 233 M--GFIDdHEDVMDLLENLLRYMYEDVAENCEKELELLGIELPVP---------ETPIPRITYDE-------AIE-ILKS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 427 LQDVLEPKDksgiracsSLG----HLLNEIFEVVVEPKLVqptFVLDYPIEISPL-AKPHRGNAGLTERFELFICGREMA 501
Cdd:PRK05159 294 KGNEISWGD--------DLDtegeRLLGEYVKEEYGSDFY---FITDYPSEKRPFyTMPDEDDPEISKSFDLLFRGLEIT 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 502 NAfseltdpvDQRT-RLEEQVRQHNAKraeavRESPepnakkdddddESYevtldEDFLTALEYGMPPASGMGLGIDRLV 580
Cdd:PRK05159 363 SG--------GQRIhRYDMLVESIKEK-----GLNP-----------ESF-----EFYLEAFKYGMPPHGGFGLGLERLT 413
|
490
....*....|....*.
gi 15231261 581 MLLTNSASIRDVIAFP 596
Cdd:PRK05159 414 MKLLGLENIREAVLFP 429
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
118-596 |
9.43e-40 |
|
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: 150.59 E-value: 9.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 118 EIYKHLANGEesdneidcVSIAGRVVARRAFGKLAFLTLRDDSGTIQLYCEKERLsdDQFEQLKQfIDIGDILGASGSMK 197
Cdd:COG0017 7 DLLPEHVGQE--------VTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKL--ENFEEAKK-LTTESSVEVTGTVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 198 RTE--KGELSICVNSFSILTKSLLPLP-DKYHglTDIDKRYRQRYVDmIANPEVADVFRRRAKIVSEIRKTVESFGYLEV 274
Cdd:COG0017 76 ESPraPQGVELQAEEIEVLGEADEPYPlQPKR--HSLEFLLDNRHLR-LRTNRFGAIFRIRSELARAIREFFQERGFVEV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 275 ETPVLQGAA--GGAEARPfVTFHnslGRDLYLRIATELHlKRMLVGGFEKVYEIGRIFRNEGIST-RHNPEFTTIEMYEA 351
Cdd:COG0017 153 HTPIITASAteGGGELFP-VDYF---GKEAYLTQSGQLY-KEALAMALEKVYTFGPTFRAEKSNTrRHLAEFWMIEPEMA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 352 YSDYHSMMDMAELIVTQCSMAVNGK-------LTIDYQGTEICLERPWRRETMHNLVKEI--TGINFsELGEDLGNAKDT 422
Cdd:COG0017 228 FADLEDVMDLAEEMLKYIIKYVLENcpeelefLGRDVERLEKVPESPFPRITYTEAIEILkkSGEKV-EWGDDLGTEHER 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 423 VllalqdvlepkdksgiracsslghLLNEIFEvvvepklvQPTFVLDYPIEISPL-AKPHRGNAGLTERFELficgreMA 501
Cdd:COG0017 307 Y------------------------LGEEFFK--------KPVFVTDYPKEIKAFyMKPNPDDPKTVAAFDL------LA 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 502 NAFSELTDpVDQR-TRLEEQVrqhnaKRAEAVRESPepnakkdddddESYevtldEDFLTALEYGMPPASGMGLGIDRLV 580
Cdd:COG0017 349 PGIGEIIG-GSQReHRYDVLV-----ERIKEKGLDP-----------EDY-----EWYLDLRRYGSVPHAGFGLGLERLV 406
|
490
....*....|....*.
gi 15231261 581 MLLTNSASIRDVIAFP 596
Cdd:COG0017 407 MWLTGLENIREVIPFP 422
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
230-596 |
1.27e-29 |
|
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: 119.21 E-value: 1.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 230 DIDKRYRQRYVDmIANPEVADVFRRRAKIVSEIRKTVESFGYLEVETPVLQGAA--GGAEARPFVTFhnslGRDLYLRIA 307
Cdd:cd00776 3 NLETLLDNRHLD-LRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDteGGAELFKVSYF----GKPAYLAQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 308 TELHlKRMLVGGFEKVYEIGRIFRNEGIST-RHNPEFTTIEMYEAY-SDYHSMMDMAELIVTQCSMAVNGK----LTIDY 381
Cdd:cd00776 78 PQLY-KEMLIAALERVYEIGPVFRAEKSNTrRHLSEFWMLEAEMAFiEDYNEVMDLIEELIKYIFKRVLERcakeLELVN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 382 QGT--EICLERPWRRetmhnlvkeitgINFSELGEdlgnakdtVLLALQDVLEPKDKSGIRACSSLghLLNEIFEVVvep 459
Cdd:cd00776 157 QLNreLLKPLEPFPR------------ITYDEAIE--------LLREKGVEEEVKWGEDLSTEHER--LLGEIVKGD--- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 460 klvqPTFVLDYPIEISPL-AKPHRGNAGLTERFELFICGREmanafsELTD---PVDQRTRLEEQVRQHNakraeavres 535
Cdd:cd00776 212 ----PVFVTDYPKEIKPFyMKPDDDNPETVESFDLLMPGVG------EIVGgsqRIHDYDELEERIKEHG---------- 271
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231261 536 pepnakkddDDDESYEVTLDedfltALEYGMPPASGMGLGIDRLVMLLTNSASIRDVIAFP 596
Cdd:cd00776 272 ---------LDPESFEWYLD-----LRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
136-596 |
4.72e-22 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 100.83 E-value: 4.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 136 VSIAGRVVARRAFGKLAFLTLRDDSGTIQLYCEKERLSDDQFEQLKQFIDIGDILGASGSMKRT--------EKGELSIC 207
Cdd:PRK12820 21 VCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFSPEAAPADVYELAASLRAEFCVALQGEVQKRLeetenphiETGDIEVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 208 VNSFSILTKS-LLPLPDKYHGLT-----------DIDKRYRQRYVDmIANPEVADVFRRRAKIVSEIRKTVESFGYLEVE 275
Cdd:PRK12820 101 VRELSILAASeALPFAISDKAMTagagsagadavNEDLRLQYRYLD-IRRPAMQDHLAKRHRIIKCARDFLDSRGFLEIE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 276 TPVLQGAAGGAeARPFVTFHNSLGRDLY-LRIATELHLKRMLVGGFEKVYEIGRIFRNEGISTRHNPEFTTIEMYEAYSD 354
Cdd:PRK12820 180 TPILTKSTPEG-ARDYLVPSRIHPKEFYaLPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEFTQLDIEASFID 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 355 YHSMMDMAELIVTQCsMAVNGkltidyqgteICLERPWRR-------------------------------ETMHNLVKE 403
Cdd:PRK12820 259 EEFIFELIEELTARM-FAIGG----------IALPRPFPRmpyaeamdttgsdrpdlrfdlkfadatdifeNTRYGIFKQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 404 -------ITGINFSELGEDLGN-------AKDTV------------------------------LLALQDVLEPKDKSGI 439
Cdd:PRK12820 328 ilqrggrIKGINIKGQSEKLSKnvlqneyAKEIApsfgakgmtwmraeaggldsnivqffsadeKEALKRRFHAEDGDVI 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 440 -----RAC----SSLG----HLLNEIFevVVEPKLVQPTFVLDYPI-----------EISPLAKPHR---------GNAG 486
Cdd:PRK12820 408 imiadASCaivlSALGqlrlHLADRLG--LIPEGVFHPLWITDFPLfeatddggvtsSHHPFTAPDRedfdpgdieELLD 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 487 LTER-FELFICGREMANAfseltdpvdqRTRLEEQVRQHNAKRAEAVREspepnakKDDDDDESYevtldedFLTALEYG 565
Cdd:PRK12820 486 LRSRaYDLVVNGEELGGG----------SIRINDKDIQLRIFAALGLSE-------EDIEDKFGF-------FLRAFDFA 541
|
570 580 590
....*....|....*....|....*....|.
gi 15231261 566 MPPASGMGLGIDRLVMLLTNSASIRDVIAFP 596
Cdd:PRK12820 542 APPHGGIALGLDRVVSMILQTPSIREVIAFP 572
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
109-596 |
3.00e-20 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 94.75 E-value: 3.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 109 KSHSANQLQEiyKHLanGEEsdneidcVSIAGRVVARRAFGKLAFLTLRDDSGTIQLYCEKERLSDDQFEQLKQfidiGD 188
Cdd:PRK00476 4 RTHYCGELRE--SHV--GQT-------VTLCGWVHRRRDHGGLIFIDLRDREGIVQVVFDPDAEAFEVAESLRS----EY 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 189 ILGASGSM-KRTEK--------GELSICVNSFSILTKS-LLPLPDKYHGLTDIDKRYRQRYVDMiANPEVADVFRRRAKI 258
Cdd:PRK00476 69 VIQVTGTVrARPEGtvnpnlptGEIEVLASELEVLNKSkTLPFPIDDEEDVSEELRLKYRYLDL-RRPEMQKNLKLRSKV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 259 VSEIRKTVESFGYLEVETPVL-----QGAaggaearpfvtfhnslgRDlYL---RIatelH-------------LKRML- 316
Cdd:PRK00476 148 TSAIRNFLDDNGFLEIETPILtkstpEGA-----------------RD-YLvpsRV----HpgkfyalpqspqlFKQLLm 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 317 VGGFEKVYEIGRIFRNEGISTRHNPEFTTI--EMyeaysdyhSMMDMAELivtqcsMAVNGKLtidyqgteiclerpwrr 394
Cdd:PRK00476 206 VAGFDRYYQIARCFRDEDLRADRQPEFTQIdiEM--------SFVTQEDV------MALMEGL----------------- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 395 etMHNLVKEITGIN---------FSELGEDLGNAK-DT-VLLALQDVLE-------------PKDKSGIRAcsslghlln 450
Cdd:PRK00476 255 --IRHVFKEVLGVDlptpfprmtYAEAMRRYGSDKpDLrFGLELVDVTDlfkdsgfkvfagaANDGGRVKA--------- 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 451 eifeVVVEPKLVQPT---------FV-------LDYpIEI------SPLAK--PHRGNAGLTERFE-------LFICGRe 499
Cdd:PRK00476 324 ----IRVPGGAAQLSrkqidelteFAkiygakgLAY-IKVnedglkGPIAKflSEEELAALLERTGakdgdliFFGADK- 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 500 mANAFSELTDpvdqrtrleeQVRQHNAKRAEAVRES----------P--EPNAK--------------KDDDDDE----- 548
Cdd:PRK00476 398 -AKVVNDALG----------ALRLKLGKELGLIDEDkfaflwvvdfPmfEYDEEegrwvaahhpftmpKDEDLDElettd 466
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 549 -------SYEVTL----------------------------DED-------FLTALEYGMPPASGMGLGIDRLVMLLTNS 586
Cdd:PRK00476 467 pgkarayAYDLVLngyelgggsirihrpeiqekvfeilgisEEEaeekfgfLLDALKYGAPPHGGIAFGLDRLVMLLAGA 546
|
650
....*....|
gi 15231261 587 ASIRDVIAFP 596
Cdd:PRK00476 547 DSIRDVIAFP 556
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
126-596 |
1.73e-19 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 92.54 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 126 GEESDNEI-DCVSIAGRVVARRAFGKLAFLTLRDDSGTIQLYCEKERLSD--DQFEQLKQ--FIDIGDILGASGSM---K 197
Cdd:PLN02903 64 GALSVNDVgSRVTLCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDEFPEahRTANRLRNeyVVAVEGTVRSRPQEspnK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 198 RTEKGELSICVNSFSILTKSLLPLP------DKYHGLTDIDKRYRQRYVDMiANPEVADVFRRRAKIVSEIRKTVES-FG 270
Cdd:PLN02903 144 KMKTGSVEVVAESVDILNVVTKSLPflvttaDEQKDSIKEEVRLRYRVLDL-RRPQMNANLRLRHRVVKLIRRYLEDvHG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 271 YLEVETPVLQGAAGGAeARPFVTFHNSLGRDLYLRIATELHLKRML-VGGFEKVYEIGRIFRNEGISTRHNPEFTTIEMY 349
Cdd:PLN02903 223 FVEIETPILSRSTPEG-ARDYLVPSRVQPGTFYALPQSPQLFKQMLmVSGFDRYYQIARCFRDEDLRADRQPEFTQLDME 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 350 EAYSDYHSMMDMAELIVTQcsmavngkltIDYQGTEICLERPWRR----ETMH-------------------NLVKEITG 406
Cdd:PLN02903 302 LAFTPLEDMLKLNEDLIRQ----------VFKEIKGVQLPNPFPRltyaEAMSkygsdkpdlryglelvdvsDVFAESSF 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 407 INFSELGEDLGNAK-----------DTVLLALQDVLEPKDKSGIRACSSL-----GHL-----LNEIFEVVVEPKLVQPT 465
Cdd:PLN02903 372 KVFAGALESGGVVKaicvpdgkkisNNTALKKGDIYNEAIKSGAKGLAFLkvlddGELegikaLVESLSPEQAEQLLAAC 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 466 FVldYPIEISPLAKPHRGNAGLT-ERFELFIcGREM------ANAFSELTD-PV----DQRTRLEEQVRQHNAKRAEAVR 533
Cdd:PLN02903 452 GA--GPGDLILFAAGPTSSVNKTlDRLRQFI-AKTLdlidpsRHSILWVTDfPMfewnEDEQRLEALHHPFTAPNPEDMG 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 534 ESPEPNAKKDDDDDESYEV-------------------------TLDEDF---LTALEYGMPPASGMGLGIDRLVMLLTN 585
Cdd:PLN02903 529 DLSSARALAYDMVYNGVEIgggslriyrrdvqqkvleaiglspeEAESKFgylLEALDMGAPPHGGIAYGLDRLVMLLAG 608
|
570
....*....|.
gi 15231261 586 SASIRDVIAFP 596
Cdd:PLN02903 609 AKSIRDVIAFP 619
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
136-596 |
3.98e-19 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 90.82 E-value: 3.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 136 VSIAGRVVARRAFGKLAFLTLRDDSGTIQ-LYCEKERLSDDQFEQLKQF-----IDI-GDILGASGSMKRTEKGELSICV 208
Cdd:PTZ00401 81 VLIRARVSTTRKKGKMAFMVLRDGSDSVQaMAAVEGDVPKEMIDFIGQIptesiVDVeATVCKVEQPITSTSHSDIELKV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 209 NSFSILTKSLLPLP----DKYHGLTD------IDKRYRQRYVDMiANPEVADVFRRRAKIVSEIRKTVESFGYLEVETPV 278
Cdd:PTZ00401 161 KKIHTVTESLRTLPftleDASRKESDegakvnFDTRLNSRWMDL-RTPASGAIFRLQSRVCQYFRQFLIDSDFCEIHSPK 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 279 LQGAA--GGAEARPFVTFHnslgRDLYLRIATELHLKRMLVGGFEKVYEIGRIFRNEGIST-RHNPEFT--TIEMyEAYS 353
Cdd:PTZ00401 240 IINAPseGGANVFKLEYFN----RFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNThRHLTEFVglDVEM-RINE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 354 DYHSMMDMAELIVtqCSM-----AVNGKLtidyqgTEICLERPWRretmhNLVKEITGINFSELGedlgnakdtvLLALQ 428
Cdd:PTZ00401 315 HYYEVLDLAESLF--NYIferlaTHTKEL------KAVCQQYPFE-----PLVWKLTPERMKELG----------VGVIS 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 429 DVLEPKDKSGIRACSSLGH-----------LLNEIFEVVVEP-------------KLVQPTFVLD------YPIEISPL- 477
Cdd:PTZ00401 372 EGVEPTDKYQARVHNMDSRmlrinymhcieLLNTVLEEKMAPtddinttnekllgKLVKERYGTDffisdrFPSSARPFy 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 478 AKPHRGNAGLTERFELFICGREMANAFSELTDPvdqrtrleeqvrQHNAKRAEAVrespepnakkdddddeSYEVTLDED 557
Cdd:PTZ00401 452 TMECKDDERFTNSYDMFIRGEEISSGAQRIHDP------------DLLLARAKML----------------NVDLTPIKE 503
|
490 500 510
....*....|....*....|....*....|....*....
gi 15231261 558 FLTALEYGMPPASGMGLGIDRLVMLLTNSASIRDVIAFP 596
Cdd:PTZ00401 504 YVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFP 542
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
255-365 |
1.44e-17 |
|
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.
Pssm-ID: 238391 [Multi-domain] Cd Length: 211 Bit Score: 81.78 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 255 RAKIVSEIRKTVESFGYLEVETPVLQ----GAAGGAEARPFVTFHNSLGRDLYLRIATELHLKRMLVG----GFEKVYEI 326
Cdd:cd00768 2 RSKIEQKLRRFMAELGFQEVETPIVEreplLEKAGHEPKDLLPVGAENEEDLYLRPTLEPGLVRLFVShirkLPLRLAEI 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15231261 327 GRIFRNEGIS--TRHNPEFTTIEMYEAYSDYHSMMDMAELI 365
Cdd:cd00768 82 GPAFRNEGGRrgLRRVREFTQLEGEVFGEDGEEASEFEELI 122
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
110-596 |
1.79e-17 |
|
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: 85.82 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 110 SHSANQLQEiyKHLanGEEsdneidcVSIAGRVVARRAFGKLAFLTLRDDSGTIQLYCEKERLSD--DQFEQLK-QFIdi 186
Cdd:COG0173 4 THYCGELRE--SDV--GQE-------VTLSGWVHRRRDHGGLIFIDLRDRYGITQVVFDPDDSAEafEKAEKLRsEYV-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 187 gdiLGASGS-MKRTEK--------GELSICVNSFSILTKS-LLPLPDKYHGLTDIDKRYRQRYVDMiANPEVADVFRRRA 256
Cdd:COG0173 71 ---IAVTGKvRARPEGtvnpklptGEIEVLASELEILNKAkTPPFQIDDDTDVSEELRLKYRYLDL-RRPEMQKNLILRH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 257 KIVSEIRKTVESFGYLEVETPVL-----QGAaggaearpfvtfhnslgRDlYL---RiateLH-------------LKRM 315
Cdd:COG0173 147 KVTKAIRNYLDENGFLEIETPILtkstpEGA-----------------RD-YLvpsR----VHpgkfyalpqspqlFKQL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 316 L-VGGFEKVYEIGRIFRNEgiSTRHN--PEFTTI--EMyeaysdyhSMMDMAELivtqcsMAVNGKLTI----DYQGTEI 386
Cdd:COG0173 205 LmVSGFDRYFQIARCFRDE--DLRADrqPEFTQLdiEM--------SFVDQEDV------FELMEGLIRhlfkEVLGVEL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 387 clERPWRR----ETMH-------------------NLVKE---------------ITGIN-----------FSELGE--- 414
Cdd:COG0173 269 --PTPFPRmtyaEAMErygsdkpdlrfglelvdvtDIFKDsgfkvfagaaenggrVKAINvpggaslsrkqIDELTEfak 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 415 DLGnAK---------------------DTVLLALQDVLEPK---------DKSGIrACSSLGHLLNEI---FEVVVEPKL 461
Cdd:COG0173 347 QYG-AKglayikvnedglkspiakflsEEELAAILERLGAKpgdliffvaDKPKV-VNKALGALRLKLgkeLGLIDEDEF 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 462 vQPTFVLDYPI-EISPLAKphrgnaglteRFElficgrEMANAFS---------ELTDPVDQRTRleeQ----------- 520
Cdd:COG0173 425 -AFLWVVDFPLfEYDEEEG----------RWV------AMHHPFTmpkdedldlLETDPGKVRAK---Aydlvlngyelg 484
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 521 ---VRQHNA---KRA-EAVRESPEpnakkdddddesyEVtlDEDF---LTALEYGMPPASGMGLGIDRLVMLLTNSASIR 590
Cdd:COG0173 485 ggsIRIHDPelqEKVfELLGISEE-------------EA--EEKFgflLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIR 549
|
....*.
gi 15231261 591 DVIAFP 596
Cdd:COG0173 550 DVIAFP 555
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
252-596 |
4.75e-17 |
|
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: 81.85 E-value: 4.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 252 FRRRAKIVSEIRKTVESFGYLEVETPVLQGAA-GGAearpfvtfhnslgRDlYLrIATELH-------------LKRML- 316
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTpEGA-------------RD-FL-VPSRLHpgkfyalpqspqlFKQLLm 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 317 VGGFEKVYEIGRIFRNEGISTRHNPEFTTIEMYEAYSDYHSMMDMAELIVTQCSMAVNGkltidyqgteICLERPWRRet 396
Cdd:cd00777 66 VSGFDRYFQIARCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG----------VELTTPFPR-- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 397 mhnlvkeitgINFSELgedlgnakdtvllalqdvlepKDKSGIRACsslghllneifevvvepklvqptFVLDYPI---- 472
Cdd:cd00777 134 ----------MTYAEA---------------------MERYGFKFL-----------------------WIVDFPLfewd 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 473 EIS--------PLAKPHRGNAGLTER---------FELFICGREMANAfseltdpvdqrtrleeQVRQHNAKRAEAVRES 535
Cdd:cd00777 160 EEEgrlvsahhPFTAPKEEDLDLLEKdpedaraqaYDLVLNGVELGGG----------------SIRIHDPDIQEKVFEI 223
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231261 536 pepnAKKDDDDDEsyevtldEDF---LTALEYGMPPASGMGLGIDRLVMLLTNSASIRDVIAFP 596
Cdd:cd00777 224 ----LGLSEEEAE-------EKFgflLEAFKYGAPPHGGIALGLDRLVMLLTGSESIRDVIAFP 276
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
136-214 |
6.20e-17 |
|
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: 75.35 E-value: 6.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 136 VSIAGRVVA-RRAFGKLAFLTLRDDSGTIQLYCEKErlsddQFEQLKQFIDIGDILGASGSMKRTEKGELSICVNSFSIL 214
Cdd:pfam01336 1 VTVAGRVTSiRRSGGKLLFLTLRDGTGSIQVVVFKE-----EAEKLAKKLKEGDVVRVTGKVKKRKGGELELVVEEIELL 75
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
136-216 |
5.61e-16 |
|
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: 72.98 E-value: 5.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 136 VSIAGRVVARRAFGKLAFLTLRDDSGTIQLYCEKErLSDDQFEQLKQfIDIGDILGASGSMKRTEK-----GELSICVNS 210
Cdd:cd04100 2 VTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKE-ELGEFFEEAEK-LRTESVVGVTGTVVKRPEgnlatGEIELQAEE 79
|
....*.
gi 15231261 211 FSILTK 216
Cdd:cd04100 80 LEVLSK 85
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
136-596 |
1.74e-13 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 73.20 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 136 VSIAGRVVARRAFGKLAFLTLRDDSGTIQ--LYCEKERLSDDQFEQLKQFI--DIGDILGASGSMKRTEKG---ELSICV 208
Cdd:PLN02850 84 VLIRGRVHTIRGKGKSAFLVLRQSGFTVQcvVFVSEVTVSKGMVKYAKQLSreSVVDVEGVVSVPKKPVKGttqQVEIQV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 209 NSFSILTKSLLPLP----DKYHGLTDIDK---------------RYRQRYVDMIAnPEVADVFRRRAKIVSEIRKTVESF 269
Cdd:PLN02850 164 RKIYCVSKALATLPfnveDAARSESEIEKalqtgeqlvrvgqdtRLNNRVLDLRT-PANQAIFRIQSQVCNLFREFLLSK 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 270 GYLEVETPVLqgAAGGAEARPFVTFHNSLGRDLYLRIATELHlKRMLV-GGFEKVYEIGRIFRNEGIST-RHNPEFT--T 345
Cdd:PLN02850 243 GFVEIHTPKL--IAGASEGGSAVFRLDYKGQPACLAQSPQLH-KQMAIcGDFRRVFEIGPVFRAEDSFThRHLCEFTglD 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 346 IEMyEAYSDYHSMMD-MAELIVTqcsmAVNGkltidyqgteicLERPWRretmhnlvKEITGINFSELGEDLGNAKDTVL 424
Cdd:PLN02850 320 LEM-EIKEHYSEVLDvVDELFVA----IFDG------------LNERCK--------KELEAIREQYPFEPLKYLPKTLR 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 425 LALQDVLEPKDKSGIRAcSSLGHLLNEIFEV---VVEPKLVQPTFVLD-YPIEISPL-AKPHRGNAGLTERFELFICGRE 499
Cdd:PLN02850 375 LTFAEGIQMLKEAGVEV-DPLGDLNTESERKlgqLVKEKYGTDFYILHrYPLAVRPFyTMPCPDDPKYSNSFDVFIRGEE 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 500 -MANAfseltdpvdQRTRLEEQVrqhnAKRAEAVrespepnakkdddddeSYEVTLDEDFLTALEYGMPPASGMGLGIDR 578
Cdd:PLN02850 454 iISGA---------QRVHDPELL----EKRAEEC----------------GIDVKTISTYIDSFRYGAPPHGGFGVGLER 504
|
490
....*....|....*...
gi 15231261 579 LVMLLTNSASIRDVIAFP 596
Cdd:PLN02850 505 VVMLFCGLNNIRKTSLFP 522
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
121-596 |
1.08e-12 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 70.14 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 121 KHLANGEESDNEidcVSIAGRVVARRAFGKLAFLTLRDDSGTIQLYCEKERlSDDQFEQLKQfIDIGDILGASGSMKRTE 200
Cdd:PRK03932 7 KDILKGKYVGQE---VTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDN-GEEYFEEIKK-LTTGSSVIVTGTVVESP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 201 --KGELSICVNSFSILTKSL--LPLPDKYHG---LTDIdkRY-RQRyvdmiaNPEVADVFRRRAKIVSEIRKTVESFGYL 272
Cdd:PRK03932 82 raGQGYELQATKIEVIGEDPedYPIQKKRHSiefLREI--AHlRPR------TNKFGAVMRIRNTLAQAIHEFFNENGFV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 273 EVETPVLQGAA--GGAEArpFVTFHNSL-------GRDLYLRIATELHLKRMLVGgFEKVYEIGRIFRNEGIST-RHNPE 342
Cdd:PRK03932 154 WVDTPIITASDceGAGEL--FRVTTLDLdfskdffGKEAYLTVSGQLYAEAYAMA-LGKVYTFGPTFRAENSNTrRHLAE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 343 FTTIEMYEAYSDYHSMMDMAELIVtqcsmavngKLTIDYqgteiCLERpwRRETMhnlvkeitginfselgEDLGNAKDT 422
Cdd:PRK03932 231 FWMIEPEMAFADLEDNMDLAEEML---------KYVVKY-----VLEN--CPDDL----------------EFLNRRVDK 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 423 VLLA-LQDVLEPK-------------DKSGIRacsslghllneiFEVVV---------------EPKLVQPTFVLDYPIE 473
Cdd:PRK03932 279 GDIErLENFIESPfprityteaieilQKSGKK------------FEFPVewgddlgseherylaEEHFKKPVFVTNYPKD 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 474 IsplaKP--HRGNA-------------GLTErfelfICG---REmanafseltdpvDQRTRLEEQVRQHNAkraeavres 535
Cdd:PRK03932 347 I----KAfyMRLNPdgktvaamdllapGIGE-----IIGgsqRE------------ERLDVLEARIKELGL--------- 396
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231261 536 pepnakkdddDDESYEVTLDedfltaL-EYGMPPASGMGLGIDRLVMLLTNSASIRDVIAFP 596
Cdd:PRK03932 397 ----------NKEDYWWYLD------LrRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFP 442
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
243-596 |
3.55e-08 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 55.41 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 243 IANPEVADVFRRRAKIVSEIRKTVESFGYLEVETPVLQ-----GAAGGAEARPFVTFHNSLGRDLYLRIATELHlKRMLV 317
Cdd:PRK06462 21 ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIISpstdpLMGLGSDLPVKQISIDFYGVEYYLADSMILH-KQLAL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 318 GGFEKVYEIGRIFRNEG---ISTRHNPEFTTIEMYEAYSDYHSMMDMAElivtqcsmavngkltidyqgteiclerpwrr 394
Cdd:PRK06462 100 RMLGKIFYLSPNFRLEPvdkDTGRHLYEFTQLDIEIEGADLDEVMDLIE------------------------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 395 ETMHNLVKEI---TGINFSELGEDLGN-AKDTVLLALQDVLEPKDKSGIRACSSLghLLNEIFEVVVEPKLVQPTFVLDY 470
Cdd:PRK06462 149 DLIKYLVKELleeHEDELEFFGRDLPHlKRPFKRITHKEAVEILNEEGCRGIDLE--ELGSEGEKSLSEHFEEPFWIIDI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 471 PIEISPL-AKPHRGNAGLTERFELFicgreMANAFSELTDPVDQRTRLEEQVRqhnakraeavrespepNAKKDDDDDES 549
Cdd:PRK06462 227 PKGSREFyDREDPERPGVLRNYDLL-----LPEGYGEAVSGGEREYEYEEIVE----------------RIREHGVDPEK 285
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15231261 550 YevtldEDFLTALEYGMPPASGMGLGIDRLVMLLTNSASIRDVIAFP 596
Cdd:PRK06462 286 Y-----KWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQPFP 327
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
109-241 |
3.66e-08 |
|
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli aspartyl-tRNA synthetase (AspRS), the human mitochondrial (mt) AspRS-2, the discriminating (D) Thermus thermophilus AspRS-1, and the nondiscriminating (ND) Helicobacter pylori AspRS. These homodimeric enzymes are class2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. Human mtAspRS participates in mitochondrial biosynthesis; this enzyme been shown to charge E.coli native tRNAsp in addition to in vitro transcribed human mitochondrial tRNAsp. T. thermophilus is rare among bacteria in having both a D_AspRS and a ND_AspRS. H.pylori ND-AspRS can charge both tRNAASp and tRNAAsn, it is fractionally more efficient at aminoacylating tRNAAsp over tRNAAsn. The H.pylori genome does not contain AsnRS.
Pssm-ID: 239812 [Multi-domain] Cd Length: 135 Bit Score: 52.52 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 109 KSHSANQLQEiyKHLanGEEsdneidcVSIAGRVVARRAFGKLAFLTLRDDSGTIQLYCEKERLSD-DQFEQLK-QFidi 186
Cdd:cd04317 1 RTHYCGELRE--SHV--GQE-------VTLCGWVQRRRDHGGLIFIDLRDRYGIVQVVFDPEEAPEfELAEKLRnES--- 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231261 187 gdILGASGS-MKRTEK--------GELSICVNSFSILTKS-LLPLPDKYHGLTDIDKRYRQRYVD 241
Cdd:cd04317 67 --VIQVTGKvRARPEGtvnpklptGEIEVVASELEVLNKAkTLPFEIDDDVNVSEELRLKYRYLD 129
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
303-596 |
1.31e-06 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 51.18 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 303 YLRIATELHLKRmLVGGFEKVYEIGRIFRNEGIST-RHNPEFTTIEMYEAYSDYHSMMDMAELIVTQCSMAV--NGKLTI 379
Cdd:PTZ00425 327 FLTVSGQLSLEN-LCSSMGDVYTFGPTFRAENSHTsRHLAEFWMIEPEIAFADLYDNMELAESYIKYCIGYVlnNNFDDI 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 380 DYqgteiclerpWRRETMHNLVKEITGInfseLGEDLGNAKDT----VLLALQDVLEPKDKSGIracsslgHLLNEIFEV 455
Cdd:PTZ00425 406 YY----------FEENVETGLISRLKNI----LDEDFAKITYTnvidLLQPYSDSFEVPVKWGM-------DLQSEHERF 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 456 VVEPKLVQPTFVLDYPieisplakphrgnaglterfelficgREMANAFSELTDpvDQRTRLEEQVRQhnAKRAEAVRES 535
Cdd:PTZ00425 465 VAEQIFKKPVIVYNYP--------------------------KDLKAFYMKLNE--DQKTVAAMDVLV--PKIGEVIGGS 514
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231261 536 P-EPNAKKDDDDDESYEVTLDED--FLTALEYGMPPASGMGLGIDRLVMLLTNSASIRDVIAFP 596
Cdd:PTZ00425 515 QrEDNLERLDKMIKEKKLNMESYwwYRQLRKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFP 578
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
125-223 |
4.11e-06 |
|
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: 45.77 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 125 NGEEsdneidcVSIAGRVVARRAFGKLAFLTLRDDSGTIQLYCEKERLSDDQFEQLKQfIDIGDILGASGSMKRTEK--G 202
Cdd:cd04316 11 DGEE-------VTVAGWVHEIRDLGGIKFVILRDREGIVQVTAPKKKVDKELFKTVRK-LSRESVISVTGTVKAEPKapN 82
|
90 100
....*....|....*....|.
gi 15231261 203 ELSICVNSFSILTKSLLPLPD 223
Cdd:cd04316 83 GVEIIPEEIEVLSEAKTPLPL 103
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
259-596 |
8.06e-06 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 48.71 E-value: 8.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 259 VSEIRKTVESFGYLEVETPVLQGAAGGAEARPFvtFHNSLGRDLYLRIATELHLKRMlVGGFEKVYEIGRIFRNEGI-ST 337
Cdd:PLN02532 331 EQDLRKTNQLASQLEAKEKLKTGTSVKADKLSF--SKDFFSRPTYLTVSGRLHLESY-ACALGNVYTFGPRFRADRIdSA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 338 RHNPEFTTIEMYEAYSDYHSMMDMAE--------LIVTQCSMAVN------GKLTIDYqgTEICLERPWRRetmhnlvke 403
Cdd:PLN02532 408 RHLAEMWMVEVEMAFSELEDAMNCAEdyfkflckWVLENCSEDMKfvskriDKTISTR--LEAIISSSLQR--------- 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 404 itgINFSElgedlgnAKDTVLLALQDVLEPKDKSGIRACSS-LGHLLNEIFEvvvepklvQPTFVLDYPIEISPLAKPHR 482
Cdd:PLN02532 477 ---ISYTE-------AVDLLKQATDKKFETKPEWGIALTTEhLSYLADEIYK--------KPVIIYNYPKELKPFYVRLN 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 483 GNAGLTERFEL-------FICGREMANAFSELTdpvdqrTRLEEQVRQHnakraeavrespepnakkdddddESYEVTLD 555
Cdd:PLN02532 539 DDGKTVAAFDLvvpkvgtVITGSQNEERMDILN------ARIEELGLPR-----------------------EQYEWYLD 589
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 15231261 556 edfltALEYGMPPASGMGLGIDRLVMLLTNSASIRDVIAFP 596
Cdd:PLN02532 590 -----LRRHGTVKHSGFSLGFELMVLFATGLPDVRDAIPFP 625
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
253-333 |
2.29e-04 |
|
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. It is responsible for the attachment of histidine to the 3' OH group of ribose of the appropriate tRNA. This domain 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. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ. HisZ along with HisG catalyze the first reaction in histidine biosynthesis. HisZ is found only in a subset of bacteria and differs from HisRS in lacking a C-terminal anti-codon binding domain.
Pssm-ID: 238396 [Multi-domain] Cd Length: 261 Bit Score: 43.36 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 253 RRRAKIVSEIRKTVESFGYLEVETP------VLQGAAGGAEARPFVTFHNSLGRDLYLR------IAtELHLKRMLVGGF 320
Cdd:cd00773 3 ALRRYIEDTLREVFERYGYEEIDTPvfeyteLFLRKSGDEVSKEMYRFKDKGGRDLALRpdltapVA-RAVAENLLSLPL 81
|
90
....*....|....
gi 15231261 321 E-KVYEIGRIFRNE 333
Cdd:cd00773 82 PlKLYYIGPVFRYE 95
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
551-596 |
7.19e-04 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 42.65 E-value: 7.19e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 15231261 551 EVTLDED----FLTALEYGMPPASGMGLGIDRLVMLLTNSASIRDVIAFP 596
Cdd:PLN02603 508 ELKLNKEsywwYLDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFP 557
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
255-373 |
1.98e-03 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 40.87 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 255 RAKIVSEIRKTVESFGYLEVETPVLQGA-------AGGAE-ARPFVTFHNSLGRDLYLRIATELHLKRMLVGGFE----- 321
Cdd:PRK12420 21 RNKIKRALEDVFERYGCKPLETPTLNMYelmsskyGGGDEiLKEIYTLTDQGKRDLALRYDLTIPFAKVVAMNPNirlpf 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15231261 322 KVYEIGRIFRNEGISTRHNPEFTTIEMYEAYSDyhSMMDMAELIvtqcSMAV 373
Cdd:PRK12420 101 KRYEIGKVFRDGPIKQGRFREFIQCDVDIVGVE--SVMAEAELM----SMAF 146
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
253-333 |
3.74e-03 |
|
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439894 [Multi-domain] Cd Length: 422 Bit Score: 40.11 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 253 RRRAKIVSEIRKTVESFGYLEVETPVLQ-----GAAGGAEarpFV-----TFHNSLGRDLYLR------IAtelhlkRML 316
Cdd:COG0124 19 AKWQYVEDTIREVFERYGFQEIRTPIFEytelfARKIGED---IVekemyTFEDRGGRSLTLRpegtapVA------RAV 89
|
90 100
....*....|....*....|...
gi 15231261 317 V-GGFE-----KVYEIGRIFRNE 333
Cdd:COG0124 90 AeHGNElpfpfKLYYIGPVFRYE 112
|
|
| YhcR |
COG4085 |
DNA/RNA endonuclease YhcR, contains UshA esterase domain [RNA processing and modification]; |
104-210 |
4.06e-03 |
|
DNA/RNA endonuclease YhcR, contains UshA esterase domain [RNA processing and modification];
Pssm-ID: 443261 [Multi-domain] Cd Length: 131 Bit Score: 37.73 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231261 104 AYKWEKSHSANQLQEIYKHLANGEESDNEIdcVSIAGRVVARRA--FGKLAFLTLRDDSGTIQLYCEKERLSDDQFEQLK 181
Cdd:COG4085 15 ALLGISSLIIFPLQPGEITIAEIREGLGEY--VTVEGVVTAVKVarDGGILFLKLQDGTGGINVYAFGDVAEELLNYGPF 92
|
90 100
....*....|....*....|....*....
gi 15231261 182 QFIDIGDILGASGSMKrTEKGELSICVNS 210
Cdd:COG4085 93 PEIKEGDKVRVTGRVT-EYKGRYEIILND 120
|
|
| |
