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Conserved domains on  [gi|3323370|gb|AAC26594|]
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lysyl-tRNA synthetase (lysS-2) [Treponema pallidum subsp. pallidum str. Nichols]

Protein Classification

EF-P lysine aminoacylase GenX( domain architecture ID 11455190)

EF-P lysine aminoacylase GenX catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EpmA COG2269
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ...
 1-345 1.84e-108

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: 319.36  E-value: 1.84e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370    1 MDTESVLFRAQCLRAVRDFFLEHHYIELDTPALARALVPERCLEVFQTEYFTsvHAKDTQKLYLVPSPEVFLKPLIAQLQ 80
Cdd:COG2269   1 ASREALRARARLLAAIRAFFAERGVLEVETPALSVAPGTDPHLDSFATEFIG--PDGGGRPLYLHTSPEFAMKRLLAAGS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370   81 RSAFQISKCYRNGESmGALHRPEFTMVEYYTVYADYKTSLDVSSKLFRFVVEQVQshpladpyscacfCAPFEYVTVEEA 160
Cdd:COG2269  79 GPIYQIAKVFRNGER-GRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAAG-------------FAPAERLSYQEA 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370  161 FLRYAGFSLsHASSVQTLAQEVLRSGIDLGAragvdytQWSWDDLYELLLVHIVEPKLRsiKDRCVVLYDYPIQISCLAQ 240
Cdd:COG2269 145 FLRYLGIDP-LTADLDELAAAAAAAGLRVAD-------DDDRDDLLDLLLSERVEPQLG--RDRPTFLYDYPASQAALAR 214

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370  241 ehtgrsgiqstsPNKGDAPhwvVKERWELYVRGVELINCYTEQRDAKHVTRYCREEQTAKQGSARVVHPVPEGFAHACAR 320
Cdd:COG2269 215 ------------ISPDDPR---VAERFELYACGVELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAA 279

                       330       340
                ....*....|....*....|....*.
gi 3323370  321 -MPPCSGAALGFDRLVALLAGRHSLD 345
Cdd:COG2269 280 gLPDCSGVALGFDRLLMLALGAERID 305
 
Name Accession Description Interval E-value
EpmA COG2269
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ...
 1-345 1.84e-108

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: 319.36  E-value: 1.84e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370    1 MDTESVLFRAQCLRAVRDFFLEHHYIELDTPALARALVPERCLEVFQTEYFTsvHAKDTQKLYLVPSPEVFLKPLIAQLQ 80
Cdd:COG2269   1 ASREALRARARLLAAIRAFFAERGVLEVETPALSVAPGTDPHLDSFATEFIG--PDGGGRPLYLHTSPEFAMKRLLAAGS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370   81 RSAFQISKCYRNGESmGALHRPEFTMVEYYTVYADYKTSLDVSSKLFRFVVEQVQshpladpyscacfCAPFEYVTVEEA 160
Cdd:COG2269  79 GPIYQIAKVFRNGER-GRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAAG-------------FAPAERLSYQEA 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370  161 FLRYAGFSLsHASSVQTLAQEVLRSGIDLGAragvdytQWSWDDLYELLLVHIVEPKLRsiKDRCVVLYDYPIQISCLAQ 240
Cdd:COG2269 145 FLRYLGIDP-LTADLDELAAAAAAAGLRVAD-------DDDRDDLLDLLLSERVEPQLG--RDRPTFLYDYPASQAALAR 214

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370  241 ehtgrsgiqstsPNKGDAPhwvVKERWELYVRGVELINCYTEQRDAKHVTRYCREEQTAKQGSARVVHPVPEGFAHACAR 320
Cdd:COG2269 215 ------------ISPDDPR---VAERFELYACGVELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAA 279

                       330       340
                ....*....|....*....|....*.
gi 3323370  321 -MPPCSGAALGFDRLVALLAGRHSLD 345
Cdd:COG2269 280 gLPDCSGVALGFDRLLMLALGAERID 305
genX TIGR00462
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ...
 19-345 1.57e-70

EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous to the C-terminal region of lysyl-tRNA synthetase (LysS). Multiple sequence alignment of these proteins with the homologous regions of collected LysS proteins shows that these proteins form a distinct set rather than just similar truncations of LysS. The protein is termed GenX after its designation in E. coli. Interestingly, genX often is located near a homolog of lysine-2,3-aminomutase. Its function is unknown. [Unknown function, General]


Pssm-ID: 273090 [Multi-domain]  Cd Length: 290  Bit Score: 221.66  E-value: 1.57e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370     19 FFLEHHYIELDTPALARALVPERCLEVFQTEYFTSvhAKDTQKLYLVPSPEVFLKPLIAQLQRSAFQISKCYRNGESmGA 98
Cdd:TIGR00462   1 FFAERGVLEVETPLLSPAPVTDPHLDAFATEFVGP--DGQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGER-GR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370     99 LHRPEFTMVEYYTVYADYKTSLDVSSKLFRFVveqvqshpLADPyscacfCAPFEYVTVEEAFLRYAGFSLsHASSVQTL 178
Cdd:TIGR00462  78 RHNPEFTMLEWYRPGFDYHDLMDEVEALLQEL--------LGDP------FAPAERLSYQEAFLRYAGIDP-LTASLAEL 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370    179 AQEVLRSGIDLGARAgvdytqwSWDDLYELLLVHIVEPKLRsiKDRCVVLYDYPIQISCLAQehtgrsgiqstsPNKGDA 258
Cdd:TIGR00462 143 QAAAAAHGIRASEED-------DRDDLLDLLFSEKVEPHLG--FGRPTFLYDYPASQAALAR------------ISPDDP 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370    259 PhwvVKERWELYVRGVELINCYTEQRDAKHVTRYCREEQTAKQGSARVVHPVPEGFAHACAR-MPPCSGAALGFDRLVAL 337
Cdd:TIGR00462 202 R---VAERFELYIKGLELANGFHELTDAAEQRRRFEADNALRKALGLPRYPLDERFLAALEAgLPECSGVALGVDRLLML 278


                  ....*...
gi 3323370    338 LAGRHSLD 345
Cdd:TIGR00462 279 ALGADSID 286
PRK09350 PRK09350
elongation factor P--(R)-beta-lysine ligase;
9-345 1.64e-59

elongation factor P--(R)-beta-lysine ligase;


Pssm-ID: 236474 [Multi-domain]  Cd Length: 306  Bit Score: 193.99  E-value: 1.64e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370     9 RAQCLRAVRDFFLEHHYIELDTPALARALVPERCLEVFQTEyFTSVHAKDTQKLYLVPSPEVFLKPLIAQLQRSAFQISK 88
Cdd:PRK09350   8 RAKIIAEIRRFFADRGVLEVETPILSQATVTDIHLVPFETR-FVGPGASQGKTLWLMTSPEYHMKRLLAAGSGPIFQICK 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370    89 CYRNGEsMGALHRPEFTMVEYYTVYADYKTSLDVSSKLFRFVVEqvqshpladpyscacfCAPFEYVTVEEAFLRYAG-- 166
Cdd:PRK09350  87 SFRNEE-AGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLD----------------CEPAESLSYQQAFLRYLGid 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370   167 -FSLSHASSVQTLAQEVLRSGIDlgaragvdyTQWSWDDLYELLLVHIVEPKLRsiKDRCVVLYDYPIQISCLAQEHTGR 245
Cdd:PRK09350 150 pLSADKTQLREVAAKLGLSNIAD---------EEEDRDTLLQLLFTFGVEPNIG--KEKPTFVYHFPASQAALAKISTED 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370   246 SGiqstspnkgdaphwvVKERWELYVRGVELINCYTEQRDAKHVTRycREEQTAKQGSAR--VVHPVPEGFAHACAR-MP 322
Cdd:PRK09350 219 HR---------------VAERFEVYFKGIELANGFHELTDAREQRQ--RFEQDNRKRAARglPQQPIDENLIAALEAgLP 281

                        330       340
                 ....*....|....*....|...
gi 3323370   323 PCSGAALGFDRLVALLAGRHSLD 345
Cdd:PRK09350 282 DCSGVALGVDRLIMLALGAESIS 304
LysRS_core cd00775
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ...
 9-344 5.16e-41

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: 146.19  E-value: 5.16e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370    9 RAQCLRAVRDFFLEHHYIELDTP--------ALARALVperclevfqteyfTSVHAKDTQkLYLVPSPEVFLKPLI-AQL 79
Cdd:cd00775  11 RSKIISYIRKFLDDRGFLEVETPmlqpiaggAAARPFI-------------THHNALDMD-LYLRIAPELYLKRLIvGGF 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370   80 QRsAFQISKCYRNgESMGALHRPEFTMVEYYTVYADYKTSLDVSSKLFRFVVEQVQShPLADPYS--CACFCAPFEYVTV 157
Cdd:cd00775  77 ER-VYEIGRNFRN-EGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKING-KTKIEYGgkELDFTPPFKRVTM 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370  158 EEAFLRYAGFSLSHASSVQTlaQEVLRSGIDLGARAGVDytQWSWDDLYELLLVHIVEPKLrsIKDrcVVLYDYPIQISC 237
Cdd:cd00775 154 VDALKEKTGIDFPELDLEQP--EELAKLLAKLIKEKIEK--PRTLGKLLDKLFEEFVEPTL--IQP--TFIIDHPVEISP 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370  238 LAQEHTGRSGIqstspnkgdaphwvvKERWELYVRGVELINCYTEQRDAkhVTRYCREEQTAKQGSAR--VVHPVPEGFA 315
Cdd:cd00775 226 LAKRHRSNPGL---------------TERFELFICGKEIANAYTELNDP--FDQRERFEEQAKQKEAGddEAMMMDEDFV 288

                       330       340       350
                ....*....|....*....|....*....|
gi 3323370  316 HACAR-MPPCSGAALGFDRLVALLAGRHSL 344
Cdd:cd00775 289 TALEYgMPPTGGLGIGIDRLVMLLTDSNSI 318
tRNA-synt_2 pfam00152
tRNA synthetases class II (D, K and N);
9-343 1.47e-30

tRNA synthetases class II (D, K and N);


Pssm-ID: 425487 [Multi-domain]  Cd Length: 318  Bit Score: 118.05  E-value: 1.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370      9 RAQCLRAVRDFFLEHHYIELDTPALARALVPERClEVFQteyftsVHAKDTQKLYLVP-SPEVFLKPL-IAQLQRsAFQI 86
Cdd:pfam00152  25 RSKIIKAIRNFLDENGFLEVETPILTKSATPEGA-RDFL------VPSRALGKFYALPqSPQLYKQLLmVAGFDR-VFQI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370     87 SKCYRNgESMGALHRPEFTMVEYYTVYADYKTSLDVSSKLFRFVVEQVQshpladpySCACFCAPFEYVTVEEAFLRYag 166
Cdd:pfam00152  97 ARCFRD-EDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVE--------GIAKELEGGTLLDLKKPFPRI-- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370    167 fslshassvqTLAQevlrsGIDLGARAGVDYTQWSWDDLYELLLVHIVEPKLrsiKDRCVVLYDYPIQISCLaqehtgrs 246
Cdd:pfam00152 166 ----------TYAE-----AIEKLNGKDVEELGYGSDKPDLRFLLELVIDKN---KFNPLWVTDFPAEHHPF-------- 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370    247 giqsTSPNKGDAPHWVvkERWELYVRGVELINCYTEQRDakhvtrycREEQTAK---QG-SARVVHPVPEGFAHA-CARM 321
Cdd:pfam00152 220 ----TMPKDEDDPALA--EAFDLVLNGVEIGGGSIRIHD--------PELQEERfeeQGlDPEEAEEKFGFYLDAlKYGA 285

                         330       340
                  ....*....|....*....|..
gi 3323370    322 PPCSGAALGFDRLVALLAGRHS 343
Cdd:pfam00152 286 PPHGGLGIGLDRLVMLLTGLES 307
 
Name Accession Description Interval E-value
EpmA COG2269
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ...
 1-345 1.84e-108

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: 319.36  E-value: 1.84e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370    1 MDTESVLFRAQCLRAVRDFFLEHHYIELDTPALARALVPERCLEVFQTEYFTsvHAKDTQKLYLVPSPEVFLKPLIAQLQ 80
Cdd:COG2269   1 ASREALRARARLLAAIRAFFAERGVLEVETPALSVAPGTDPHLDSFATEFIG--PDGGGRPLYLHTSPEFAMKRLLAAGS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370   81 RSAFQISKCYRNGESmGALHRPEFTMVEYYTVYADYKTSLDVSSKLFRFVVEQVQshpladpyscacfCAPFEYVTVEEA 160
Cdd:COG2269  79 GPIYQIAKVFRNGER-GRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAAG-------------FAPAERLSYQEA 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370  161 FLRYAGFSLsHASSVQTLAQEVLRSGIDLGAragvdytQWSWDDLYELLLVHIVEPKLRsiKDRCVVLYDYPIQISCLAQ 240
Cdd:COG2269 145 FLRYLGIDP-LTADLDELAAAAAAAGLRVAD-------DDDRDDLLDLLLSERVEPQLG--RDRPTFLYDYPASQAALAR 214

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370  241 ehtgrsgiqstsPNKGDAPhwvVKERWELYVRGVELINCYTEQRDAKHVTRYCREEQTAKQGSARVVHPVPEGFAHACAR 320
Cdd:COG2269 215 ------------ISPDDPR---VAERFELYACGVELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAA 279

                       330       340
                ....*....|....*....|....*.
gi 3323370  321 -MPPCSGAALGFDRLVALLAGRHSLD 345
Cdd:COG2269 280 gLPDCSGVALGFDRLLMLALGAERID 305
genX TIGR00462
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ...
 19-345 1.57e-70

EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous to the C-terminal region of lysyl-tRNA synthetase (LysS). Multiple sequence alignment of these proteins with the homologous regions of collected LysS proteins shows that these proteins form a distinct set rather than just similar truncations of LysS. The protein is termed GenX after its designation in E. coli. Interestingly, genX often is located near a homolog of lysine-2,3-aminomutase. Its function is unknown. [Unknown function, General]


Pssm-ID: 273090 [Multi-domain]  Cd Length: 290  Bit Score: 221.66  E-value: 1.57e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370     19 FFLEHHYIELDTPALARALVPERCLEVFQTEYFTSvhAKDTQKLYLVPSPEVFLKPLIAQLQRSAFQISKCYRNGESmGA 98
Cdd:TIGR00462   1 FFAERGVLEVETPLLSPAPVTDPHLDAFATEFVGP--DGQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGER-GR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370     99 LHRPEFTMVEYYTVYADYKTSLDVSSKLFRFVveqvqshpLADPyscacfCAPFEYVTVEEAFLRYAGFSLsHASSVQTL 178
Cdd:TIGR00462  78 RHNPEFTMLEWYRPGFDYHDLMDEVEALLQEL--------LGDP------FAPAERLSYQEAFLRYAGIDP-LTASLAEL 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370    179 AQEVLRSGIDLGARAgvdytqwSWDDLYELLLVHIVEPKLRsiKDRCVVLYDYPIQISCLAQehtgrsgiqstsPNKGDA 258
Cdd:TIGR00462 143 QAAAAAHGIRASEED-------DRDDLLDLLFSEKVEPHLG--FGRPTFLYDYPASQAALAR------------ISPDDP 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370    259 PhwvVKERWELYVRGVELINCYTEQRDAKHVTRYCREEQTAKQGSARVVHPVPEGFAHACAR-MPPCSGAALGFDRLVAL 337
Cdd:TIGR00462 202 R---VAERFELYIKGLELANGFHELTDAAEQRRRFEADNALRKALGLPRYPLDERFLAALEAgLPECSGVALGVDRLLML 278


                  ....*...
gi 3323370    338 LAGRHSLD 345
Cdd:TIGR00462 279 ALGADSID 286
PRK09350 PRK09350
elongation factor P--(R)-beta-lysine ligase;
9-345 1.64e-59

elongation factor P--(R)-beta-lysine ligase;


Pssm-ID: 236474 [Multi-domain]  Cd Length: 306  Bit Score: 193.99  E-value: 1.64e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370     9 RAQCLRAVRDFFLEHHYIELDTPALARALVPERCLEVFQTEyFTSVHAKDTQKLYLVPSPEVFLKPLIAQLQRSAFQISK 88
Cdd:PRK09350   8 RAKIIAEIRRFFADRGVLEVETPILSQATVTDIHLVPFETR-FVGPGASQGKTLWLMTSPEYHMKRLLAAGSGPIFQICK 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370    89 CYRNGEsMGALHRPEFTMVEYYTVYADYKTSLDVSSKLFRFVVEqvqshpladpyscacfCAPFEYVTVEEAFLRYAG-- 166
Cdd:PRK09350  87 SFRNEE-AGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLD----------------CEPAESLSYQQAFLRYLGid 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370   167 -FSLSHASSVQTLAQEVLRSGIDlgaragvdyTQWSWDDLYELLLVHIVEPKLRsiKDRCVVLYDYPIQISCLAQEHTGR 245
Cdd:PRK09350 150 pLSADKTQLREVAAKLGLSNIAD---------EEEDRDTLLQLLFTFGVEPNIG--KEKPTFVYHFPASQAALAKISTED 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370   246 SGiqstspnkgdaphwvVKERWELYVRGVELINCYTEQRDAKHVTRycREEQTAKQGSAR--VVHPVPEGFAHACAR-MP 322
Cdd:PRK09350 219 HR---------------VAERFEVYFKGIELANGFHELTDAREQRQ--RFEQDNRKRAARglPQQPIDENLIAALEAgLP 281

                        330       340
                 ....*....|....*....|...
gi 3323370   323 PCSGAALGFDRLVALLAGRHSLD 345
Cdd:PRK09350 282 DCSGVALGVDRLIMLALGAESIS 304
LysRS_core cd00775
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ...
 9-344 5.16e-41

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: 146.19  E-value: 5.16e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370    9 RAQCLRAVRDFFLEHHYIELDTP--------ALARALVperclevfqteyfTSVHAKDTQkLYLVPSPEVFLKPLI-AQL 79
Cdd:cd00775  11 RSKIISYIRKFLDDRGFLEVETPmlqpiaggAAARPFI-------------THHNALDMD-LYLRIAPELYLKRLIvGGF 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370   80 QRsAFQISKCYRNgESMGALHRPEFTMVEYYTVYADYKTSLDVSSKLFRFVVEQVQShPLADPYS--CACFCAPFEYVTV 157
Cdd:cd00775  77 ER-VYEIGRNFRN-EGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKING-KTKIEYGgkELDFTPPFKRVTM 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370  158 EEAFLRYAGFSLSHASSVQTlaQEVLRSGIDLGARAGVDytQWSWDDLYELLLVHIVEPKLrsIKDrcVVLYDYPIQISC 237
Cdd:cd00775 154 VDALKEKTGIDFPELDLEQP--EELAKLLAKLIKEKIEK--PRTLGKLLDKLFEEFVEPTL--IQP--TFIIDHPVEISP 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370  238 LAQEHTGRSGIqstspnkgdaphwvvKERWELYVRGVELINCYTEQRDAkhVTRYCREEQTAKQGSAR--VVHPVPEGFA 315
Cdd:cd00775 226 LAKRHRSNPGL---------------TERFELFICGKEIANAYTELNDP--FDQRERFEEQAKQKEAGddEAMMMDEDFV 288

                       330       340       350
                ....*....|....*....|....*....|
gi 3323370  316 HACAR-MPPCSGAALGFDRLVALLAGRHSL 344
Cdd:cd00775 289 TALEYgMPPTGGLGIGIDRLVMLLTDSNSI 318
LysU COG1190
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ...
 9-343 1.76e-39

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: 145.56  E-value: 1.76e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370    9 RAQCLRAVRDFFLEHHYIELDTP--------ALARalvPerclevFQTeyftsvH--AKDtQKLYLVPSPEVFLKPLI-A 77
Cdd:COG1190 177 RSKIIRAIRRFLDERGFLEVETPmlqpiaggAAAR---P------FIT------HhnALD-MDLYLRIAPELYLKRLIvG 240

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370   78 QLQRsAFQISKCYRNgESMGALHRPEFTMVEYYTVYADYKTSLDVSSKLFRFVVEQV--------QSHPLaDpyscacFC 149
Cdd:COG1190 241 GFER-VFEIGRNFRN-EGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVlgttkvtyQGQEI-D------LS 311

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370  150 APFEYVTVEEAFLRYAGFSLSHASSVQTLAQEVLRSGIDLGAragvdytQWSWDDLYELLLVHIVEPKLrsikdrcvV-- 227
Cdd:COG1190 312 PPWRRITMVEAIKEATGIDVTPLTDDEELRALAKELGIEVDP-------GWGRGKLIDELFEELVEPKL--------Iqp 376

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370  228 --LYDYPIQISCLAQEHTGRSGIqsTspnkgdaphwvvkERWELYVRGVELINCYTE------QRDakhvtRYCREEQTA 299
Cdd:COG1190 377 tfVTDYPVEVSPLAKRHRDDPGL--T-------------ERFELFIAGREIANAFSElndpidQRE-----RFEEQLELK 436

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 3323370  300 KQG--SArvvHPVPEGF--A--HAcarMPPCSGAALGFDRLVALLAGRHS 343
Cdd:COG1190 437 AAGddEA---MPMDEDFlrAleYG---MPPTGGLGIGIDRLVMLLTDSPS 480
lysS PRK00484
lysyl-tRNA synthetase; Reviewed
 9-343 3.01e-36

lysyl-tRNA synthetase; Reviewed


Pssm-ID: 234778 [Multi-domain]  Cd Length: 491  Bit Score: 136.76  E-value: 3.01e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370     9 RAQCLRAVRDFFLEHHYIELDTP--------ALARalvPerclevfqteyFTSVH-AKDtQKLYLVPSPEVFLKPLI-AQ 78
Cdd:PRK00484 175 RSKIISAIRRFLDNRGFLEVETPmlqpiaggAAAR---P-----------FITHHnALD-IDLYLRIAPELYLKRLIvGG 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370    79 LQRsAFQISKCYRNgESMGALHRPEFTMVEYYTVYADYKTSLDVSSKLFRFVVEQV--------QSHPLaDpyscacFCA 150
Cdd:PRK00484 240 FER-VYEIGRNFRN-EGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVlgttkvtyQGTEI-D------FGP 310

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370   151 PFEYVTVEEAFLRYAGFSLSHASSVQTLAqevlrsgidLGARAGVDY-TQWSWDDLYELLLVHIVEPKLrsikdrcvV-- 227
Cdd:PRK00484 311 PFKRLTMVDAIKEYTGVDFDDMTDEEARA---------LAKELGIEVeKSWGLGKLINELFEEFVEPKL--------Iqp 373

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370   228 --LYDYPIQISCLAQEHTGRSGIqsTspnkgdaphwvvkERWELYVRGVELINCYTE------QRDakhvtRYcrEEQTA 299
Cdd:PRK00484 374 tfITDYPVEISPLAKRHREDPGL--T-------------ERFELFIGGREIANAFSElndpidQRE-----RF--EAQVE 431

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 3323370   300 K--QGS--ArvvHPVPEGFAHA-CARMPPCSGAALGFDRLVALLAGRHS 343
Cdd:PRK00484 432 AkeAGDdeA---MFMDEDFLRAlEYGMPPTGGLGIGIDRLVMLLTDSPS 477
tRNA-synt_2 pfam00152
tRNA synthetases class II (D, K and N);
9-343 1.47e-30

tRNA synthetases class II (D, K and N);


Pssm-ID: 425487 [Multi-domain]  Cd Length: 318  Bit Score: 118.05  E-value: 1.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370      9 RAQCLRAVRDFFLEHHYIELDTPALARALVPERClEVFQteyftsVHAKDTQKLYLVP-SPEVFLKPL-IAQLQRsAFQI 86
Cdd:pfam00152  25 RSKIIKAIRNFLDENGFLEVETPILTKSATPEGA-RDFL------VPSRALGKFYALPqSPQLYKQLLmVAGFDR-VFQI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370     87 SKCYRNgESMGALHRPEFTMVEYYTVYADYKTSLDVSSKLFRFVVEQVQshpladpySCACFCAPFEYVTVEEAFLRYag 166
Cdd:pfam00152  97 ARCFRD-EDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVE--------GIAKELEGGTLLDLKKPFPRI-- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370    167 fslshassvqTLAQevlrsGIDLGARAGVDYTQWSWDDLYELLLVHIVEPKLrsiKDRCVVLYDYPIQISCLaqehtgrs 246
Cdd:pfam00152 166 ----------TYAE-----AIEKLNGKDVEELGYGSDKPDLRFLLELVIDKN---KFNPLWVTDFPAEHHPF-------- 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370    247 giqsTSPNKGDAPHWVvkERWELYVRGVELINCYTEQRDakhvtrycREEQTAK---QG-SARVVHPVPEGFAHA-CARM 321
Cdd:pfam00152 220 ----TMPKDEDDPALA--EAFDLVLNGVEIGGGSIRIHD--------PELQEERfeeQGlDPEEAEEKFGFYLDAlKYGA 285

                         330       340
                  ....*....|....*....|..
gi 3323370    322 PPCSGAALGFDRLVALLAGRHS 343
Cdd:pfam00152 286 PPHGGLGIGLDRLVMLLTGLES 307
PTZ00385 PTZ00385
lysyl-tRNA synthetase; Provisional
 4-349 6.32e-30

lysyl-tRNA synthetase; Provisional


Pssm-ID: 185588 [Multi-domain]  Cd Length: 659  Bit Score: 120.52  E-value: 6.32e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370     4 ESVLFRAQCLRAVRDFFLEHHYIELDTPALaralvpERCLEVFQTEYFTSVHAKDTQKLYLVPSPEVFLKPLIAQLQRSA 83
Cdd:PTZ00385 231 ETIKKRHVMLQALRDYFNERNFVEVETPVL------HTVASGANAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERI 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370    84 FQISKCYRNgESMGALHRPEFTMVEYYTVYADYKTSLDVSSKLFRFV------VEQVQSHP---LADPYSCAcFCAPFEY 154
Cdd:PTZ00385 305 YEIGKVFRN-EDADRSHNPEFTSCEFYAAYHTYEDLMPMTEDIFRQLamrvngTTVVQIYPenaHGNPVTVD-LGKPFRR 382

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370   155 VTVEEAFLRYAGFSLSHASSVQT------LAQEVLRSGIDLGAragVDYTQWSWDDLYELLLV-HIVEPKLrsikdrcvv 227
Cdd:PTZ00385 383 VSVYDEIQRMSGVEFPPPNELNTpkgiayMSVVMLRYNIPLPP---VRTAAKMFEKLIDFFITdRVVEPTF--------- 450

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370   228 LYDYPIQISCLAQEHTGRSGIqstspnkgdaphwvvKERWELYVRGVELINCYTEQRDAKHVTRYCREEQTAKQGSARVV 307
Cdd:PTZ00385 451 VMDHPLFMSPLAKEQVSRPGL---------------AERFELFVNGIEYCNAYSELNDPHEQYHRFQQQLVDRQGGDEEA 515

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 3323370   308 HPVPEGFAHAC-ARMPPCSGAALGFDRLVALLAGRHSL-DAFVY 349
Cdd:PTZ00385 516 MPLDETFLKSLqVGLPPTAGWGMGIDRALMLLTNSSNIrDGIIF 559
PLN02502 PLN02502
lysyl-tRNA synthetase
 9-338 1.02e-24

lysyl-tRNA synthetase


Pssm-ID: 215278 [Multi-domain]  Cd Length: 553  Bit Score: 105.07  E-value: 1.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370     9 RAQCLRAVRDFFLEHHYIELDTP--------ALARalvPerclevfqteyFTSVHAKDTQKLYLVPSPEVFLKPLI-AQL 79
Cdd:PLN02502 232 RAKIISYIRRFLDDRGFLEVETPmlnmiaggAAAR---P-----------FVTHHNDLNMDLYLRIATELHLKRLVvGGF 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370    80 QRsAFQISKCYRNgESMGALHRPEFTMVEYYTVYADYKTSLDVSSKLFRFVVEQVQ-SHPLadPYSCA--CFCAPFEYVT 156
Cdd:PLN02502 298 ER-VYEIGRQFRN-EGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKELTgSYKI--KYHGIeiDFTPPFRRIS 373

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370   157 ----VEEAflryAGFSLSHASSvqtlAQEVLRSGIDLGARAGVD-----YTQWSWDDLYElllvHIVEPKLRSikdRCVV 227
Cdd:PLN02502 374 mislVEEA----TGIDFPADLK----SDEANAYLIAACEKFDVKcpppqTTGRLLNELFE----EFLEETLVQ---PTFV 438

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370   228 LyDYPIQISCLAQEHTGRSGiqstspnkgdaphwvVKERWELYVRGVELINCYTEQRDAkhVTRYCREEQTAKQGSArvv 307
Cdd:PLN02502 439 L-DHPVEMSPLAKPHRSKPG---------------LTERFELFINGRELANAFSELTDP--VDQRERFEEQVKQHNA--- 497

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 3323370   308 hpvpeGFAHACAR-----------MPPCSGAALGFDRLVALL 338
Cdd:PLN02502 498 -----GDDEAMALdedfctaleygLPPTGGWGLGIDRLVMLL 534
PRK12445 PRK12445
lysyl-tRNA synthetase; Reviewed
 4-344 2.15e-24

lysyl-tRNA synthetase; Reviewed


Pssm-ID: 171504 [Multi-domain]  Cd Length: 505  Bit Score: 103.60  E-value: 2.15e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370     4 ESVLFRAQCLRAVRDFFLEHHYIELDTPALAraLVPERClevfQTEYFTSVHAKDTQKLYLVPSPEVFLKPLIAQLQRSA 83
Cdd:PRK12445 182 QTFVVRSKILAAIRQFMVARGFMEVETPMMQ--VIPGGA----SARPFITHHNALDLDMYLRIAPELYLKRLVVGGFERV 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370    84 FQISKCYRNgESMGALHRPEFTMVEYYTVYADYKTSLDVSSKLFRFVVEQVQSHPLAdPYSCAC--FCAPFEYVTVEEAF 161
Cdd:PRK12445 256 FEINRNFRN-EGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKV-TYGEHVfdFGKPFEKLTMREAI 333

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370   162 LRYAGFS----LSHASSVQTLAQEVlrsGIDLGARAGVDYTQWSWDDlyELLLVHIVEPKLrsikdrcvvLYDYPIQISC 237
Cdd:PRK12445 334 KKYRPETdmadLDNFDAAKALAESI---GITVEKSWGLGRIVTEIFD--EVAEAHLIQPTF---------ITEYPAEVSP 399

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370   238 LAQEHtgrsgiqSTSPNkgdaphwvVKERWELYVRGVELINCYTEQRDAKHVTRYCREEQTAKQGSARVVHPVPEGFAHA 317
Cdd:PRK12445 400 LARRN-------DVNPE--------ITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTA 464

                        330       340
                 ....*....|....*....|....*...
gi 3323370   318 CAR-MPPCSGAALGFDRLVALLAGRHSL 344
Cdd:PRK12445 465 LEYgLPPTAGLGIGIDRMIMLFTNSHTI 492
Asp_Lys_Asn_RS_core cd00669
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ...
 9-344 8.00e-24

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: 98.70  E-value: 8.00e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370    9 RAQCLRAVRDFFLEHHYIELDTPALaRALVPERCLEVFQTEYFTSVHakdtqKLYLVPSPEVFLKPLIAQLQRSAFQISK 88
Cdd:cd00669   4 RSKIIKAIRDFMDDRGFLEVETPML-QKITGGAGARPFLVKYNALGL-----DYYLRISPQLFKKRLMVGGLDRVFEINR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370   89 CYRNgESMGALHRPEFTMVEYYTVYADYKTSLDVSSKLFRFVVEQVQSH-PLADPYSCACFCAPFEYVTVEEAFLRYAGF 167
Cdd:cd00669  78 NFRN-EDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVtAVTYGFELEDFGLPFPRLTYREALERYGQP 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370  168 slshassvqtlaqevlrsgidlgaragvdytqwswddlyelllvhivepklrsikdrcVVLYDYPiqisclAQEHTgrsg 247
Cdd:cd00669 157 ----------------------------------------------------------LFLTDYP------AEMHS---- 168

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370  248 iQSTSPNKGDAphwVVKERWELYVRGVELINCYTEQRDAKhvtryCREEQTAKQGSARVVHPVPEGFAHACAR--MPPCS 325
Cdd:cd00669 169 -PLASPHDVNP---EIADAFDLFINGVEVGNGSSRLHDPD-----IQAEVFQEQGINKEAGMEYFEFYLKALEygLPPHG 239

                       330
                ....*....|....*....
gi 3323370  326 GAALGFDRLVALLAGRHSL 344
Cdd:cd00669 240 GLGIGIDRLIMLMTNSPTI 258
lysS PRK02983
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
9-341 8.38e-24

bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;


Pssm-ID: 235095 [Multi-domain]  Cd Length: 1094  Bit Score: 102.73  E-value: 8.38e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370      9 RAQCLRAVRDFFLEHHYIELDTPAL--------ARALVperclevfqteyfTSVHAKDtQKLYLVPSPEVFLKPLIAQLQ 80
Cdd:PRK02983  773 RSAVVRAVRETLVARGFLEVETPILqqvhgganARPFV-------------THINAYD-MDLYLRIAPELYLKRLCVGGV 838

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370     81 RSAFQISKCYRNgESMGALHRPEFTMVEYYTVYADYKTSLDVSSKLFRFVV-----EQVQSHPLADPYSCAC-FCAPFEY 154
Cdd:PRK02983  839 ERVFELGRNFRN-EGVDATHNPEFTLLEAYQAHADYDTMRDLTRELIQNAAqaahgAPVVMRPDGDGVLEPVdISGPWPV 917

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370    155 VTVEEAFLRYAGFSLSHASSVQTLAQevlrsgidLGARAGVDY-TQWSWDDLYELLLVHIVEPklrsikdRCV--VLY-D 230
Cdd:PRK02983  918 VTVHDAVSEALGEEIDPDTPLAELRK--------LCDAAGIPYrTDWDAGAVVLELYEHLVED-------RTTfpTFYtD 982

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370    231 YPIQISCLAQEHTGRSGiqstspnkgdaphwvVKERWELYVRGVELINCYTEQRDAkhVTRYCR-EEQT--AKQGSARVV 307
Cdd:PRK02983  983 FPTSVSPLTRPHRSDPG---------------LAERWDLVAWGVELGTAYSELTDP--VEQRRRlTEQSllAAGGDPEAM 1045

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 3323370    308 HpVPEGF----AHAcarMPPCSGAALGFDRLVALLAGR 341
Cdd:PRK02983 1046 E-LDEDFlqalEYA---MPPTGGLGMGVDRLVMLLTGR 1079
AsxRS_core cd00776
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ...
 9-343 1.49e-15

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: 76.45  E-value: 1.49e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370    9 RAQCLRAVRDFFLEHHYIELDTPALARALVpERCLEVFQTEYFtsvhakdTQKLYLVPSPEVFLKPLIAQLQRsAFQISK 88
Cdd:cd00776  27 RSEVLRAFREFLRENGFTEVHTPKITSTDT-EGGAELFKVSYF-------GKPAYLAQSPQLYKEMLIAALER-VYEIGP 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370   89 CYRNGESMGALHRPEFTMVEYYTVYA-DYKTSLDVSSKLFRFVVEQVQSHPLADPYSCACFcaPFEYVTVEEAFLRyagf 167
Cdd:cd00776  98 VFRAEKSNTRRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAKELELVNQL--NRELLKPLEPFPR---- 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370  168 sLSHASSVQTLAQEVLRS----GIDLGARAgvdytqwswddlyELLLVHIVepklrsiKDRCVVLYDYPIQIsclaqeht 243
Cdd:cd00776 172 -ITYDEAIELLREKGVEEevkwGEDLSTEH-------------ERLLGEIV-------KGDPVFVTDYPKEI-------- 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370  244 gRSGIqsTSPNkGDAPHWVvkERWELYVRGVELInCYTEQR--DAKHVTRYCREEQTakqgsarvvhpVPEGFAHAC-AR 320
Cdd:cd00776 223 -KPFY--MKPD-DDNPETV--ESFDLLMPGVGEI-VGGSQRihDYDELEERIKEHGL-----------DPESFEWYLdLR 284

                       330       340
                ....*....|....*....|....*.
gi 3323370  321 ---MPPCSGAALGFDRLVALLAGRHS 343
Cdd:cd00776 285 kygMPPHGGFGLGLERLVMWLLGLDN 310
PTZ00417 PTZ00417
lysine-tRNA ligase; Provisional
 9-344 1.88e-15

lysine-tRNA ligase; Provisional


Pssm-ID: 173607 [Multi-domain]  Cd Length: 585  Bit Score: 77.36  E-value: 1.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370     9 RAQCLRAVRDFFLEHHYIELDTPALAraLVPERClevfQTEYFTSVHAKDTQKLYLVPSPEVFLKPLIAQLQRSAFQISK 88
Cdd:PTZ00417 256 RTKIINYLRNFLNDRGFIEVETPTMN--LVAGGA----NARPFITHHNDLDLDLYLRIATELPLKMLIVGGIDKVYEIGK 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370    89 CYRNgESMGALHRPEFTMVEYYTVYADYKTSLDVSSKLFRFVVEQV---------QSHPLADPYSCAcFCAPFEYVTVEE 159
Cdd:PTZ00417 330 VFRN-EGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHLfgtykilynKDGPEKDPIEID-FTPPYPKVSIVE 407

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370   160 AFLRYAGFSLSHASSvqtlAQEVLRSGIDLGARAGVDYTQ-WSWDDLYELLLVHIVEPKLrsiKDRCVVLYDYPIQISCL 238
Cdd:PTZ00417 408 ELEKLTNTKLEQPFD----SPETINKMINLIKENKIEMPNpPTAAKLLDQLASHFIENKY---PNKPFFIIEHPQIMSPL 480

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370   239 AQEHTGRSGIqstspnkgdaphwvvKERWELYVRGVELINCYTEQRDA-KHVTRYCREEQTAKQGSArvvhpvpEGF--- 314
Cdd:PTZ00417 481 AKYHRSKPGL---------------TERLEMFICGKEVLNAYTELNDPfKQKECFSAQQKDREKGDA-------EAFqfd 538

                        330       340       350
                 ....*....|....*....|....*....|....
gi 3323370   315 AHACAR----MPPCSGAALGFDRLVALLAGRHSL 344
Cdd:PTZ00417 539 AAFCTSleygLPPTGGLGLGIDRITMFLTNKNCI 572
class_II_aaRS-like_core cd00768
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
 13-148 2.90e-11

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: 62.14  E-value: 2.90e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370   13 LRAVRDFFLEHHYIELDTPALARALVPERCLEVFQTEYFTSVHAKDtqKLYLVPSPEVFLKPLIAQLQRSA----FQISK 88
Cdd:cd00768   6 EQKLRRFMAELGFQEVETPIVEREPLLEKAGHEPKDLLPVGAENEE--DLYLRPTLEPGLVRLFVSHIRKLplrlAEIGP 83

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3323370   89 CYRNGE-SMGALHRPEFTMVEYYTVYADYKTSLDVSS------KLFR-------FVVEQVQSHPLADPYSCACF 148
Cdd:cd00768  84 AFRNEGgRRGLRRVREFTQLEGEVFGEDGEEASEFEElielteELLRalgikldIVFVEKTPGEFSPGGAGPGF 157
AspRS_core cd00777
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ...
 7-168 1.33e-10

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: 61.44  E-value: 1.33e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370    7 LFRAQCLRAVRDFFLEHHYIELDTPALARA--------LVPERclevfqteyftsVHAKdtqKLYLVP-SPEVFlKPL-- 75
Cdd:cd00777   2 RLRSRVIKAIRNFLDEQGFVEIETPILTKStpegardfLVPSR------------LHPG---KFYALPqSPQLF-KQLlm 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370   76 IAQLQRSaFQISKCYRNgESMGALHRPEFTMVEYYTVYADYKTSLDVSSKLFRFVVEQVQSHPLAdpyscacfcAPFEYV 155
Cdd:cd00777  66 VSGFDRY-FQIARCFRD-EDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLGVELT---------TPFPRM 134

                       170
                ....*....|...
gi 3323370  156 TVEEAFLRYaGFS 168
Cdd:cd00777 135 TYAEAMERY-GFK 146
aspS PRK00476
aspartyl-tRNA synthetase; Validated
 8-164 8.16e-06

aspartyl-tRNA synthetase; Validated


Pssm-ID: 234775 [Multi-domain]  Cd Length: 588  Bit Score: 47.37  E-value: 8.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370     8 FRAQCLRAVRDFFLEHHYIELDTPALARA--------LVPERclevfqteyftsVHAKdtqKLYLVP-SPEVFlKPL--I 76
Cdd:PRK00476 143 LRSKVTSAIRNFLDDNGFLEIETPILTKStpegardyLVPSR------------VHPG---KFYALPqSPQLF-KQLlmV 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370    77 AQLQRSaFQISKCYRNgESMGALHRPEFTMVeyytvyaDYKTS-------LDVSSKLFRFVVEQVQSHPLADpyscacfc 149
Cdd:PRK00476 207 AGFDRY-YQIARCFRD-EDLRADRQPEFTQI-------DIEMSfvtqedvMALMEGLIRHVFKEVLGVDLPT-------- 269

                        170
                 ....*....|....*
gi 3323370   150 aPFEYVTVEEAFLRY 164
Cdd:PRK00476 270 -PFPRMTYAEAMRRY 283
AsnS COG0017
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 9-137 4.23e-05

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: 45.04  E-value: 4.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370    9 RAQCLRAVRDFFLEHHYIELDTPalarALVPERC---LEVFQTEYFtsvhAKDTqklYLVPSPevflkpliaQLqrsafq 85
Cdd:COG0017 133 RSELARAIREFFQERGFVEVHTP----IITASATeggGELFPVDYF----GKEA---YLTQSG---------QL------ 186

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3323370   86 iskcyrNGESM-GALHR-----P--------------EFTMVEYYTVYADYKTSLDVSSKLFRFVVEQVQSH 137
Cdd:COG0017 187 ------YKEALaMALEKvytfgPtfraeksntrrhlaEFWMIEPEMAFADLEDVMDLAEEMLKYIIKYVLEN 252
PRK12820 PRK12820
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ...
 4-115 6.51e-05

bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional


Pssm-ID: 105955 [Multi-domain]  Cd Length: 706  Bit Score: 44.59  E-value: 6.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370     4 ESVLFRAQCLRAVRDFFLEHHYIELDTPALARA--------LVPERclevfqteyftsVHAKDtqkLYLVP-SPEVFLKP 74
Cdd:PRK12820 154 DHLAKRHRIIKCARDFLDSRGFLEIETPILTKStpegardyLVPSR------------IHPKE---FYALPqSPQLFKQL 218

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 3323370    75 L-IAQLQRSaFQISKCYRNgESMGALHRPEFTMVEYYTVYAD 115
Cdd:PRK12820 219 LmIAGFERY-FQLARCFRD-EDLRPNRQPEFTQLDIEASFID 258
AspS COG0173
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ...
 8-164 3.59e-03

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: 39.21  E-value: 3.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370    8 FRAQCLRAVRDFFLEHHYIELDTPALARA--------LVPERclevfqteyftsVHAKdtqKLYLVP-SPEVFlKPL--I 76
Cdd:COG0173 144 LRHKVTKAIRNYLDENGFLEIETPILTKStpegardyLVPSR------------VHPG---KFYALPqSPQLF-KQLlmV 207

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323370   77 AQLQRSaFQISKCYRNgESMGALHRPEFTMVeyytvyaDYKTS-------LDVSSKLFRFVVEQVQSHPLADpyscacfc 149
Cdd:COG0173 208 SGFDRY-FQIARCFRD-EDLRADRQPEFTQL-------DIEMSfvdqedvFELMEGLIRHLFKEVLGVELPT-------- 270

                       170
                ....*....|....*
gi 3323370  150 aPFEYVTVEEAFLRY 164
Cdd:COG0173 271 -PFPRMTYAEAMERY 284
AspS COG0173
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ...
 322-344 6.67e-03

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: 38.44  E-value: 6.67e-03
                        10        20
                ....*....|....*....|...
gi 3323370  322 PPCSGAALGFDRLVALLAGRHSL 344
Cdd:COG0173 526 PPHGGIAFGLDRLVMLLAGEDSI 548
 
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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