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Conserved domains on  [gi|2449770317|gb|WDU58470|]
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lysine--tRNA ligase [Pseudemcibacter aquimaris]

Protein Classification

lysine--tRNA ligase( domain architecture ID 11443364)

lysine--tRNA ligase catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA(Lys)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LysS COG1384
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ...
11-522 0e+00

Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA synthetase, class I is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


:

Pssm-ID: 440994 [Multi-domain]  Cd Length: 525  Bit Score: 823.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317  11 AVESKAWPFQEAEKLIKRLERSGKDKdmVIFETGYGPSGLPHIGTFGEVARTTMVKNAFELLtGKKSKIVCFSDDMDGLR 90
Cdd:COG1384     5 APDSKAWPFEEADKLLKRLEKKGKEP--VVFETGYGPSGLPHIGTFGEVARTTMVRRALREL-GIPTRLICFSDDMDGLR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317  91 KVPDNLPNQDMLAQHIGKPLTQVPDPFGTHESFAHHNNARLNAFLDSFGFEYEFISATDAYKSGDMDETLLKMLGAYEKI 170
Cdd:COG1384    82 KVPDNVPNQEMLEKYLGKPLTRIPDPFGCHESFGEHFNARLRAFLDSFGFEYEFISATELYKSGRFDEALLRALENYDKI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 171 MNVILPTLGEERRKTYSPFLPICPRTGIVLQVPMVDRNVEKGTVSYIDEETGETVEVPVTGGNCKMQWKADWAMRWVGLG 250
Cdd:COG1384   162 REILLPYLGEERRATYSPFLPICPKCGRVLQTPVIEVDAEAGTVTYRCEGCGHEGETPVTGGNGKLQWKVDWAMRWAALG 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 251 VDYEMAGKDLSE-SVKLSSAIS-RILGATPPEGLSYELFLDEKGQKISKSKGNGISMEEWLQYGTQESLSLYMYQSPRKA 328
Cdd:COG1384   242 VDFEPFGKDHAAgSVDSGSKIArEVLGGEPPEGFVYELFLDENGEKISKSKGNGLTVEEWLEYAEPESLRYFMFRKPKKA 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 329 KKLYFDVIPKTVDEYLTHLAKFPSL---EGKQKYASPIWHMHGENPPAED-VPVTFALLLNLVSASNAENKETLWGFISN 404
Cdd:COG1384   322 KDLDFDVIPKLVDEYDRFERKYFGEedqEEEERLANRVYHIHVGNPPKEMpLPVPYRFLLNLAQVANAEDKEVLWGFLRR 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 405 YAKGATPEEYPILDNLVGYALEYYENFVKPNKNYRAP--------TADEVKALEMLKSEIENIaDDVEASDIQTAVFSVG 476
Cdd:COG1384   402 YAPDATPETHPRLDERVERARRWARDFVPPTKKFRLPeelpdvelDDKERAALEDLAERLEAL-EDWDAEEIQNEVYEVG 480
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 2449770317 477 KENNYEnLREWFGALYEILLGQKEGPRMGSFIALYGKDKFIDLINE 522
Cdd:COG1384   481 KEHGFE-LRDWFKALYEVLLGQEQGPRLGSFLALLGKEFVIALIRR 525
 
Name Accession Description Interval E-value
LysS COG1384
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ...
11-522 0e+00

Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA synthetase, class I is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 440994 [Multi-domain]  Cd Length: 525  Bit Score: 823.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317  11 AVESKAWPFQEAEKLIKRLERSGKDKdmVIFETGYGPSGLPHIGTFGEVARTTMVKNAFELLtGKKSKIVCFSDDMDGLR 90
Cdd:COG1384     5 APDSKAWPFEEADKLLKRLEKKGKEP--VVFETGYGPSGLPHIGTFGEVARTTMVRRALREL-GIPTRLICFSDDMDGLR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317  91 KVPDNLPNQDMLAQHIGKPLTQVPDPFGTHESFAHHNNARLNAFLDSFGFEYEFISATDAYKSGDMDETLLKMLGAYEKI 170
Cdd:COG1384    82 KVPDNVPNQEMLEKYLGKPLTRIPDPFGCHESFGEHFNARLRAFLDSFGFEYEFISATELYKSGRFDEALLRALENYDKI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 171 MNVILPTLGEERRKTYSPFLPICPRTGIVLQVPMVDRNVEKGTVSYIDEETGETVEVPVTGGNCKMQWKADWAMRWVGLG 250
Cdd:COG1384   162 REILLPYLGEERRATYSPFLPICPKCGRVLQTPVIEVDAEAGTVTYRCEGCGHEGETPVTGGNGKLQWKVDWAMRWAALG 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 251 VDYEMAGKDLSE-SVKLSSAIS-RILGATPPEGLSYELFLDEKGQKISKSKGNGISMEEWLQYGTQESLSLYMYQSPRKA 328
Cdd:COG1384   242 VDFEPFGKDHAAgSVDSGSKIArEVLGGEPPEGFVYELFLDENGEKISKSKGNGLTVEEWLEYAEPESLRYFMFRKPKKA 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 329 KKLYFDVIPKTVDEYLTHLAKFPSL---EGKQKYASPIWHMHGENPPAED-VPVTFALLLNLVSASNAENKETLWGFISN 404
Cdd:COG1384   322 KDLDFDVIPKLVDEYDRFERKYFGEedqEEEERLANRVYHIHVGNPPKEMpLPVPYRFLLNLAQVANAEDKEVLWGFLRR 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 405 YAKGATPEEYPILDNLVGYALEYYENFVKPNKNYRAP--------TADEVKALEMLKSEIENIaDDVEASDIQTAVFSVG 476
Cdd:COG1384   402 YAPDATPETHPRLDERVERARRWARDFVPPTKKFRLPeelpdvelDDKERAALEDLAERLEAL-EDWDAEEIQNEVYEVG 480
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 2449770317 477 KENNYEnLREWFGALYEILLGQKEGPRMGSFIALYGKDKFIDLINE 522
Cdd:COG1384   481 KEHGFE-LRDWFKALYEVLLGQEQGPRLGSFLALLGKEFVIALIRR 525
lysK PRK00750
lysyl-tRNA synthetase; Reviewed
11-524 0e+00

lysyl-tRNA synthetase; Reviewed


Pssm-ID: 234829 [Multi-domain]  Cd Length: 510  Bit Score: 801.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317  11 AVESKAWPFQEAEKLIKRLersgKDKDMVIFETGYGPSGLPHIGTFGEVARTTMVKNAFELLtGKKSKIVCFSDDMDGLR 90
Cdd:PRK00750    1 AEKSKHWADEEAEKIIKRL----GKKPPVVVETGIGPSGLPHIGNFREVARTDMVRRALRDL-GIKTRLIFFSDDMDGLR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317  91 KVPDNLPNQDMLAQHIGKPLTQVPDPFGTHESFAHHNNARLNAFLDSFGFEYEFISATDAYKSGDMDETLLKMLGAYEKI 170
Cdd:PRK00750   76 KVPDNVPNQEMLEEYLGKPLTEIPDPFGCHESYAEHFNAPLREFLDRFGIEYEFISATECYKSGRYDEAILTALENRDEI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 171 MNVILPTLGEERRKTYSPFLPICPRTGIVLQVPMVDRNVEKGTVSYIDeETGETVEVPVTGGNCKMQWKADWAMRWVGLG 250
Cdd:PRK00750  156 MEILLPYLGEERQATYSPFLPICPKCGKVLTTPVISYDAEAGTVTYDC-ECGHEGEVPVTGGHGKLQWKVDWPMRWAALG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 251 VDYEMAGKDLSE-SVKLSSAISR-ILGATPPEGLSYELFLDEKGQKISKSKGNGISMEEWLQYGTQESLSLYMYQSPRKA 328
Cdd:PRK00750  235 VDFEPFGKDHASaSYDTSKKIAReILGGEPPEPFVYELFLDKKGEKISKSKGNVITIEDWLEYAPPESLRLFMFARPKPA 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 329 KKLYFDVIPKTVDEYLTHLAKFPSLEGKQKY---ASPIWHMHGENPPaedvPVTFALLLNLVSASNAENKETLWGFISNY 405
Cdd:PRK00750  315 KRLDFDVIPKLVDEYDRFERKYFGQEEKKEEeelANPVYHIHNGNPL----PVPFRLLLNLAQIANAEDKEVLWGFLKRY 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 406 AKGATPEEYPILDNLVGYALEYYENFVKPNKNYRAPTADEVKALEMLKSEIENIADDVEASDIQTAVFSVGKENNYENLR 485
Cdd:PRK00750  391 APGATPETHPRLDRLVEYAINWYRDFVAPEKKYRAPTEKERAALEDLDDALRELADGADAEEIQNEIYEVAKKELGVNPR 470
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 2449770317 486 EWFGALYEILLGQKEGPRMGSFIALYGKDKFIDLINEAL 524
Cdd:PRK00750  471 DWFKALYEVLLGQSQGPRLGSFIALLGIDFVIALIREAL 509
tRNA-synt_1f pfam01921
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from ...
15-370 0e+00

tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from prokaryotes.


Pssm-ID: 396483  Cd Length: 357  Bit Score: 520.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317  15 KAWPFQEAEKLIKRlerSGKDKDMVIFETGYGPSGLPHIGTFGEVARTTMVKNAFELLtGKKSKIVCFSDDMDGLRKVPD 94
Cdd:pfam01921   1 KHWPDKEAEKLLKE---RKKRGGEYLVASGISPSGLPHIGNFREVLRTDAVRRALRKR-GFEVRLIAFSDDMDGLRKVPD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317  95 NLPNQDMLAQHIGKPLTQVPDPFGTHESFAHHNNARLNAFLDSFGFEYEFISATDAYKSGDMDETLLKMLGAYEKIMNVI 174
Cdd:pfam01921  77 NVPNSEMLEKYLGKPLTRIPDPFGCHESYAEHFNAPFREFLDRFGIEYEFISATELYKSGLYDEAIKIALENRDEIMEIL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 175 LPTLGEERRKTYSPFLPICPRTGIVLQVPMVDRNvEKGTVSYIDEETGETVEVPVTGGNCKMQWKADWAMRWVGLGVDYE 254
Cdd:pfam01921 157 NPYRGEERQETYSPYLPICPKCGRVLTTPVVEYD-EGGTIRYRCDECGHEGEVDIRGGNGKLQWKVDWAMRWAALGVDFE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 255 MAGKDLSE---SVKLSSAIS-RILGATPPEGLSYELFLDEKGQKISKSKGNGISMEEWLQYGTQESLSLYMYQS-PRKAK 329
Cdd:pfam01921 236 PFGKDHAApggSYDTSSRIAdEIFGGEPPEGFPYELILLKGGGKMSSSKGNVITPEDWLEYAPPESLRFLMFRTkPKKAK 315
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2449770317 330 KLYFDVIPKTVDEYLTHLAKFP-SLEGKQKYASPIWHMHGEN 370
Cdd:pfam01921 316 DLDFDVIPRLVDEYDRLERIYFaKQEEEKELLNRVYELSNGN 357
LysRS_core_class_I cd00674
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) ...
15-367 1.22e-131

catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. The class I LysRS is found only in archaea and some bacteria and has evolved separately from class II LysRS, as the two do not share structural or sequence similarity.


Pssm-ID: 173900 [Multi-domain]  Cd Length: 353  Bit Score: 386.68  E-value: 1.22e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317  15 KAWPFQEAEKLIKRLersgKDKDMVIFETGYGPSGLPHIGTFGEVARTTMVKNAFELLtGKKSKIVCFSDDMDGLRKVPD 94
Cdd:cd00674     1 MHWADVIAEKIIEER----KGKEKYVVASGISPSGHIHIGNFREVITADLVARALRDL-GFEVRLIYSWDDYDRLRKVPP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317  95 NLPnqDMLAQHIGKPLTQVPDPFGTHESFAHHNNARLNAFLDSFGFEYEFISATDAYKSGDMDETLLKMLGAYEKIMNVI 174
Cdd:cd00674    76 NVP--ESYEQYIGMPLSSVPDPFGCCESYAEHFERPFEESLEKLGIEVEFISQSQMYKSGLYDENILIALEKRDEIMAIL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 175 LPTLGEERRKTYSPFLPICPRTGiVLQVPMVDRNVEKGTVSYIDEEtGETVEVPVTGGNCKMQWKADWAMRWVGLGVDYE 254
Cdd:cd00674   154 NEYRGRELQETWYPFMPYCEKCG-KDTTTVEAYDAKAGTVTYKCEC-GHEETVDIRTGRGKLTWRVDWPMRWAILGVDFE 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 255 MAGKD-LSE--SVKLSSAISR-ILGATPPEGLSYELFLDEKGQKISKSKGNGISMEEWLQYGTQESLSLYMYQSPRKAKK 330
Cdd:cd00674   232 PFGKDhASAggSYDTGKEIAReIFGGEPPVPVMYEFIGLKGGGKMSSSKGNVITPSDWLEVAPPEVLRYLYARRKNPEKH 311
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2449770317 331 LYFDV-IPKTVDEYLTHLAKFPSLEGKQKYAS----PIWHMH 367
Cdd:cd00674   312 IGFDLdILRLYDEYDRLERKYYGVEDAAEKEErelkRIYELS 353
lysS_arch TIGR00467
lysyl-tRNA synthetase, archaeal and spirochete; This model represents the lysyl-tRNA ...
22-524 2.54e-54

lysyl-tRNA synthetase, archaeal and spirochete; This model represents the lysyl-tRNA synthetases that are class I amino-acyl tRNA synthetases. It includes archaeal and spirochete examples of the enzyme. All other known examples are class IIc amino-acyl tRNA synthetases and seem to form a separate orthologous set. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273094 [Multi-domain]  Cd Length: 515  Bit Score: 191.27  E-value: 2.54e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317  22 AEKLIKRlersgKDKDMVIFETGYGPSGLPHIGTFGEVARTTMVKNAFeLLTGKKSKIVCFSDDMDGLRKVPDNLPnqDM 101
Cdd:TIGR00467   8 AEKLKKE-----KPKNLYTVASGITPSGHIHIGNFREVITADAIARAL-RDSGSEARFIYIADNYDPLRKVYPFLP--EE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 102 LAQHIGKPLTQVPDPFGTHESFAHHNNARLNAFLDSFGFEYEFISATDAYKSGDMDETLLKMLGAYEKIMNVILPTLGEE 181
Cdd:TIGR00467  80 LETYLGMPLTRIPDPEGCKTSYAEHFLIPFLESLPVLGINPEFIRASKQYTSGLYASQIKIALDHRKEISEILNEYRTSK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 182 RRKTYSPFLPICPRTGivlqvpmvdrNVEKGTVSYIDE-------ETGETVEVPVTGGNCKMQWKADWAMRWVGLGVDYE 254
Cdd:TIGR00467 160 LEENWYPISVFCENCG----------RDTTTVNNYDNEysieyscECGNQESVDIYTGAIKLPWRVDWPARWKIEKVTFE 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 255 MAGKDLSE---SVKLSSAISR-ILGATPPEGLSYE-LFLDEKGQKISKSKGNGISMEEWLQYGTQESLSlYMYQSPRKAK 329
Cdd:TIGR00467 230 PAGKDHAAaggSYDTGVNIAKeIFQYSPPVTVQYEwISLKGKGGKMSSSKGDVISVKDVLEVYTPEITR-FLFARTKPEF 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 330 KLYFDVIPKTVDEYLTHLAKF-----PSLEGKQKYASPIWHMHGENPPaEDVP--VTFALLLNLVSASNAENKETLWGFI 402
Cdd:TIGR00467 309 HISFDLDVIKLYEDYDKFERFyygvkDKDEEKKRAFKRIYELSQPMPS-ERIPyqVPFRHLSVISQIFENNDIEKILEIL 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 403 SNYAKGATPEEYPILDNLVGYALEYYENFVKPNKNYRAPTADEVKAL------EMLKSEIENIADDVE-ASDIQTAVFSV 475
Cdd:TIGR00467 388 KRVQYTVDDQKDKLINKRLNCARNWIRKYAPEDFKFSLRSKFDNMEIleenskKAINELAEFLKKNFEvATEIHNLIYKI 467
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 2449770317 476 GKENNYENlREWFGALYEILLGQKEGPRMGSFIALYGKDKFIDLINEAL 524
Cdd:TIGR00467 468 SKENGIEP-ALAFQAIYKILLGKEYGPKLGGFIKILGIDRVEKRTSKYV 515
 
Name Accession Description Interval E-value
LysS COG1384
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ...
11-522 0e+00

Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA synthetase, class I is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 440994 [Multi-domain]  Cd Length: 525  Bit Score: 823.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317  11 AVESKAWPFQEAEKLIKRLERSGKDKdmVIFETGYGPSGLPHIGTFGEVARTTMVKNAFELLtGKKSKIVCFSDDMDGLR 90
Cdd:COG1384     5 APDSKAWPFEEADKLLKRLEKKGKEP--VVFETGYGPSGLPHIGTFGEVARTTMVRRALREL-GIPTRLICFSDDMDGLR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317  91 KVPDNLPNQDMLAQHIGKPLTQVPDPFGTHESFAHHNNARLNAFLDSFGFEYEFISATDAYKSGDMDETLLKMLGAYEKI 170
Cdd:COG1384    82 KVPDNVPNQEMLEKYLGKPLTRIPDPFGCHESFGEHFNARLRAFLDSFGFEYEFISATELYKSGRFDEALLRALENYDKI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 171 MNVILPTLGEERRKTYSPFLPICPRTGIVLQVPMVDRNVEKGTVSYIDEETGETVEVPVTGGNCKMQWKADWAMRWVGLG 250
Cdd:COG1384   162 REILLPYLGEERRATYSPFLPICPKCGRVLQTPVIEVDAEAGTVTYRCEGCGHEGETPVTGGNGKLQWKVDWAMRWAALG 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 251 VDYEMAGKDLSE-SVKLSSAIS-RILGATPPEGLSYELFLDEKGQKISKSKGNGISMEEWLQYGTQESLSLYMYQSPRKA 328
Cdd:COG1384   242 VDFEPFGKDHAAgSVDSGSKIArEVLGGEPPEGFVYELFLDENGEKISKSKGNGLTVEEWLEYAEPESLRYFMFRKPKKA 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 329 KKLYFDVIPKTVDEYLTHLAKFPSL---EGKQKYASPIWHMHGENPPAED-VPVTFALLLNLVSASNAENKETLWGFISN 404
Cdd:COG1384   322 KDLDFDVIPKLVDEYDRFERKYFGEedqEEEERLANRVYHIHVGNPPKEMpLPVPYRFLLNLAQVANAEDKEVLWGFLRR 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 405 YAKGATPEEYPILDNLVGYALEYYENFVKPNKNYRAP--------TADEVKALEMLKSEIENIaDDVEASDIQTAVFSVG 476
Cdd:COG1384   402 YAPDATPETHPRLDERVERARRWARDFVPPTKKFRLPeelpdvelDDKERAALEDLAERLEAL-EDWDAEEIQNEVYEVG 480
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 2449770317 477 KENNYEnLREWFGALYEILLGQKEGPRMGSFIALYGKDKFIDLINE 522
Cdd:COG1384   481 KEHGFE-LRDWFKALYEVLLGQEQGPRLGSFLALLGKEFVIALIRR 525
lysK PRK00750
lysyl-tRNA synthetase; Reviewed
11-524 0e+00

lysyl-tRNA synthetase; Reviewed


Pssm-ID: 234829 [Multi-domain]  Cd Length: 510  Bit Score: 801.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317  11 AVESKAWPFQEAEKLIKRLersgKDKDMVIFETGYGPSGLPHIGTFGEVARTTMVKNAFELLtGKKSKIVCFSDDMDGLR 90
Cdd:PRK00750    1 AEKSKHWADEEAEKIIKRL----GKKPPVVVETGIGPSGLPHIGNFREVARTDMVRRALRDL-GIKTRLIFFSDDMDGLR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317  91 KVPDNLPNQDMLAQHIGKPLTQVPDPFGTHESFAHHNNARLNAFLDSFGFEYEFISATDAYKSGDMDETLLKMLGAYEKI 170
Cdd:PRK00750   76 KVPDNVPNQEMLEEYLGKPLTEIPDPFGCHESYAEHFNAPLREFLDRFGIEYEFISATECYKSGRYDEAILTALENRDEI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 171 MNVILPTLGEERRKTYSPFLPICPRTGIVLQVPMVDRNVEKGTVSYIDeETGETVEVPVTGGNCKMQWKADWAMRWVGLG 250
Cdd:PRK00750  156 MEILLPYLGEERQATYSPFLPICPKCGKVLTTPVISYDAEAGTVTYDC-ECGHEGEVPVTGGHGKLQWKVDWPMRWAALG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 251 VDYEMAGKDLSE-SVKLSSAISR-ILGATPPEGLSYELFLDEKGQKISKSKGNGISMEEWLQYGTQESLSLYMYQSPRKA 328
Cdd:PRK00750  235 VDFEPFGKDHASaSYDTSKKIAReILGGEPPEPFVYELFLDKKGEKISKSKGNVITIEDWLEYAPPESLRLFMFARPKPA 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 329 KKLYFDVIPKTVDEYLTHLAKFPSLEGKQKY---ASPIWHMHGENPPaedvPVTFALLLNLVSASNAENKETLWGFISNY 405
Cdd:PRK00750  315 KRLDFDVIPKLVDEYDRFERKYFGQEEKKEEeelANPVYHIHNGNPL----PVPFRLLLNLAQIANAEDKEVLWGFLKRY 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 406 AKGATPEEYPILDNLVGYALEYYENFVKPNKNYRAPTADEVKALEMLKSEIENIADDVEASDIQTAVFSVGKENNYENLR 485
Cdd:PRK00750  391 APGATPETHPRLDRLVEYAINWYRDFVAPEKKYRAPTEKERAALEDLDDALRELADGADAEEIQNEIYEVAKKELGVNPR 470
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 2449770317 486 EWFGALYEILLGQKEGPRMGSFIALYGKDKFIDLINEAL 524
Cdd:PRK00750  471 DWFKALYEVLLGQSQGPRLGSFIALLGIDFVIALIREAL 509
tRNA-synt_1f pfam01921
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from ...
15-370 0e+00

tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from prokaryotes.


Pssm-ID: 396483  Cd Length: 357  Bit Score: 520.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317  15 KAWPFQEAEKLIKRlerSGKDKDMVIFETGYGPSGLPHIGTFGEVARTTMVKNAFELLtGKKSKIVCFSDDMDGLRKVPD 94
Cdd:pfam01921   1 KHWPDKEAEKLLKE---RKKRGGEYLVASGISPSGLPHIGNFREVLRTDAVRRALRKR-GFEVRLIAFSDDMDGLRKVPD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317  95 NLPNQDMLAQHIGKPLTQVPDPFGTHESFAHHNNARLNAFLDSFGFEYEFISATDAYKSGDMDETLLKMLGAYEKIMNVI 174
Cdd:pfam01921  77 NVPNSEMLEKYLGKPLTRIPDPFGCHESYAEHFNAPFREFLDRFGIEYEFISATELYKSGLYDEAIKIALENRDEIMEIL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 175 LPTLGEERRKTYSPFLPICPRTGIVLQVPMVDRNvEKGTVSYIDEETGETVEVPVTGGNCKMQWKADWAMRWVGLGVDYE 254
Cdd:pfam01921 157 NPYRGEERQETYSPYLPICPKCGRVLTTPVVEYD-EGGTIRYRCDECGHEGEVDIRGGNGKLQWKVDWAMRWAALGVDFE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 255 MAGKDLSE---SVKLSSAIS-RILGATPPEGLSYELFLDEKGQKISKSKGNGISMEEWLQYGTQESLSLYMYQS-PRKAK 329
Cdd:pfam01921 236 PFGKDHAApggSYDTSSRIAdEIFGGEPPEGFPYELILLKGGGKMSSSKGNVITPEDWLEYAPPESLRFLMFRTkPKKAK 315
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2449770317 330 KLYFDVIPKTVDEYLTHLAKFP-SLEGKQKYASPIWHMHGEN 370
Cdd:pfam01921 316 DLDFDVIPRLVDEYDRLERIYFaKQEEEKELLNRVYELSNGN 357
LysRS_core_class_I cd00674
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) ...
15-367 1.22e-131

catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. The class I LysRS is found only in archaea and some bacteria and has evolved separately from class II LysRS, as the two do not share structural or sequence similarity.


Pssm-ID: 173900 [Multi-domain]  Cd Length: 353  Bit Score: 386.68  E-value: 1.22e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317  15 KAWPFQEAEKLIKRLersgKDKDMVIFETGYGPSGLPHIGTFGEVARTTMVKNAFELLtGKKSKIVCFSDDMDGLRKVPD 94
Cdd:cd00674     1 MHWADVIAEKIIEER----KGKEKYVVASGISPSGHIHIGNFREVITADLVARALRDL-GFEVRLIYSWDDYDRLRKVPP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317  95 NLPnqDMLAQHIGKPLTQVPDPFGTHESFAHHNNARLNAFLDSFGFEYEFISATDAYKSGDMDETLLKMLGAYEKIMNVI 174
Cdd:cd00674    76 NVP--ESYEQYIGMPLSSVPDPFGCCESYAEHFERPFEESLEKLGIEVEFISQSQMYKSGLYDENILIALEKRDEIMAIL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 175 LPTLGEERRKTYSPFLPICPRTGiVLQVPMVDRNVEKGTVSYIDEEtGETVEVPVTGGNCKMQWKADWAMRWVGLGVDYE 254
Cdd:cd00674   154 NEYRGRELQETWYPFMPYCEKCG-KDTTTVEAYDAKAGTVTYKCEC-GHEETVDIRTGRGKLTWRVDWPMRWAILGVDFE 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 255 MAGKD-LSE--SVKLSSAISR-ILGATPPEGLSYELFLDEKGQKISKSKGNGISMEEWLQYGTQESLSLYMYQSPRKAKK 330
Cdd:cd00674   232 PFGKDhASAggSYDTGKEIAReIFGGEPPVPVMYEFIGLKGGGKMSSSKGNVITPSDWLEVAPPEVLRYLYARRKNPEKH 311
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2449770317 331 LYFDV-IPKTVDEYLTHLAKFPSLEGKQKYAS----PIWHMH 367
Cdd:cd00674   312 IGFDLdILRLYDEYDRLERKYYGVEDAAEKEErelkRIYELS 353
lysS_arch TIGR00467
lysyl-tRNA synthetase, archaeal and spirochete; This model represents the lysyl-tRNA ...
22-524 2.54e-54

lysyl-tRNA synthetase, archaeal and spirochete; This model represents the lysyl-tRNA synthetases that are class I amino-acyl tRNA synthetases. It includes archaeal and spirochete examples of the enzyme. All other known examples are class IIc amino-acyl tRNA synthetases and seem to form a separate orthologous set. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273094 [Multi-domain]  Cd Length: 515  Bit Score: 191.27  E-value: 2.54e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317  22 AEKLIKRlersgKDKDMVIFETGYGPSGLPHIGTFGEVARTTMVKNAFeLLTGKKSKIVCFSDDMDGLRKVPDNLPnqDM 101
Cdd:TIGR00467   8 AEKLKKE-----KPKNLYTVASGITPSGHIHIGNFREVITADAIARAL-RDSGSEARFIYIADNYDPLRKVYPFLP--EE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 102 LAQHIGKPLTQVPDPFGTHESFAHHNNARLNAFLDSFGFEYEFISATDAYKSGDMDETLLKMLGAYEKIMNVILPTLGEE 181
Cdd:TIGR00467  80 LETYLGMPLTRIPDPEGCKTSYAEHFLIPFLESLPVLGINPEFIRASKQYTSGLYASQIKIALDHRKEISEILNEYRTSK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 182 RRKTYSPFLPICPRTGivlqvpmvdrNVEKGTVSYIDE-------ETGETVEVPVTGGNCKMQWKADWAMRWVGLGVDYE 254
Cdd:TIGR00467 160 LEENWYPISVFCENCG----------RDTTTVNNYDNEysieyscECGNQESVDIYTGAIKLPWRVDWPARWKIEKVTFE 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 255 MAGKDLSE---SVKLSSAISR-ILGATPPEGLSYE-LFLDEKGQKISKSKGNGISMEEWLQYGTQESLSlYMYQSPRKAK 329
Cdd:TIGR00467 230 PAGKDHAAaggSYDTGVNIAKeIFQYSPPVTVQYEwISLKGKGGKMSSSKGDVISVKDVLEVYTPEITR-FLFARTKPEF 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 330 KLYFDVIPKTVDEYLTHLAKF-----PSLEGKQKYASPIWHMHGENPPaEDVP--VTFALLLNLVSASNAENKETLWGFI 402
Cdd:TIGR00467 309 HISFDLDVIKLYEDYDKFERFyygvkDKDEEKKRAFKRIYELSQPMPS-ERIPyqVPFRHLSVISQIFENNDIEKILEIL 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449770317 403 SNYAKGATPEEYPILDNLVGYALEYYENFVKPNKNYRAPTADEVKAL------EMLKSEIENIADDVE-ASDIQTAVFSV 475
Cdd:TIGR00467 388 KRVQYTVDDQKDKLINKRLNCARNWIRKYAPEDFKFSLRSKFDNMEIleenskKAINELAEFLKKNFEvATEIHNLIYKI 467
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 2449770317 476 GKENNYENlREWFGALYEILLGQKEGPRMGSFIALYGKDKFIDLINEAL 524
Cdd:TIGR00467 468 SKENGIEP-ALAFQAIYKILLGKEYGPKLGGFIKILGIDRVEKRTSKYV 515
IleRS_core cd00818
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ...
288-333 1.51e-03

catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases (IleRS) catalytic core domain . This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. IleRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.


Pssm-ID: 173909 [Multi-domain]  Cd Length: 338  Bit Score: 40.68  E-value: 1.51e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2449770317 288 LDEKGQKISKSKGNGIS-MEEWLQYGTqESLSLYMYQSPRKAKKLYF 333
Cdd:cd00818   293 LDEDGRKMSKSLGNYVDpQEVVDKYGA-DALRLWVASSDVYAEDLRF 338
Ile_Leu_Val_MetRS_core cd00668
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ...
273-322 2.48e-03

catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases. These class I enzymes are all monomers. However, in some species, MetRS functions as a homodimer, as a result of an additional C-terminal domain. These enzymes aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. Enzymes in this subfamily share an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids. MetRS has a significantly shorter insertion, which lacks the editing function.


Pssm-ID: 185674 [Multi-domain]  Cd Length: 312  Bit Score: 40.09  E-value: 2.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2449770317 273 ILGATPPEGL-SYELFLDEKGQKISKSKGNGISMEEWL-QYGTqESLSLYMY 322
Cdd:cd00668   251 LFGEIPPKNLlVHGFVLDEGGQKMSKSKGNVIDPSDVVeKYGA-DALRYYLT 301
IleS COG0060
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ...
288-326 2.77e-03

Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439830 [Multi-domain]  Cd Length: 931  Bit Score: 40.45  E-value: 2.77e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2449770317 288 LDEKGQKISKSKGNGISMEEWL-QYGTqESLSLYMYQSPR 326
Cdd:COG0060   597 LDEDGRKMSKSLGNVVDPQEVIdKYGA-DILRLWVASSDY 635
ValS COG0525
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ...
286-303 6.98e-03

Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 440291 [Multi-domain]  Cd Length: 877  Bit Score: 39.26  E-value: 6.98e-03
                          10
                  ....*....|....*...
gi 2449770317 286 LFLDEKGQKISKSKGNGI 303
Cdd:COG0525   514 LVRDEQGRKMSKSKGNVI 531
tRNA-synt_1 pfam00133
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ...
282-325 9.46e-03

tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too dissimilar to be included.


Pssm-ID: 459685 [Multi-domain]  Cd Length: 602  Bit Score: 38.55  E-value: 9.46e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2449770317 282 LSYELFLDEKGQKISKSKGNGISMEEWL-QYGTqESLSLYMYQSP 325
Cdd:pfam00133 551 LVHGLVRDEQGRKMSKSLGNVIDPLDVIdKYGA-DALRLWLANSD 594
valS PRK05729
valyl-tRNA synthetase; Reviewed
286-303 9.48e-03

valyl-tRNA synthetase; Reviewed


Pssm-ID: 235582 [Multi-domain]  Cd Length: 874  Bit Score: 38.93  E-value: 9.48e-03
                          10
                  ....*....|....*...
gi 2449770317 286 LFLDEKGQKISKSKGNGI 303
Cdd:PRK05729  512 LVRDEQGRKMSKSKGNVI 529
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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