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Conserved domains on  [gi|928166055|ref|XP_013978270|]
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probable asparagine--tRNA ligase, mitochondrial isoform X6 [Canis lupus familiaris]

Protein Classification

asparagine--tRNA ligase( domain architecture ID 1000489)

asparagine--tRNA ligase catalyzes the attachment of asparagine to tRNA(Asn)

EC:  6.1.1.22
Gene Ontology:  GO:0004816|GO:0003676|GO:0005524|GO:0006421

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
asnC super family cl35230
asparaginyl-tRNA synthetase; Validated
 14-257 2.70e-124

asparaginyl-tRNA synthetase; Validated


The actual alignment was detected with superfamily member PRK03932:

Pssm-ID: 235176 [Multi-domain]  Cd Length: 450  Bit Score: 360.96  E-value: 2.70e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  14 AFTQVFTFGPTFRAENSQSRRHLAEFYMVEAEISFVEsLQDLMQVMEGLFKTATMMVLSNCPEDVELCHKFIAPGQKERL 93
Cdd:PRK03932 206 ALGKVYTFGPTFRAENSNTRRHLAEFWMIEPEMAFAD-LEDNMDLAEEMLKYVVKYVLENCPDDLEFLNRRVDKGDIERL 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  94 EHMLKNNFLIISYTEAVEILKQSSQNFTFTPEWGVDLHTEHEKYLVKHCGNIPVFVINYPLALKPFYMRDNEDGpqHTVA 173
Cdd:PRK03932 285 ENFIESPFPRITYTEAIEILQKSGKKFEFPVEWGDDLGSEHERYLAEEHFKKPVFVTNYPKDIKAFYMRLNPDG--KTVA 362

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055 174 AVDLLVPGVGELFGGSLREERYHFLEQRLARSGL-TETYQWYLDLRRFGSVPHGGFGMGFERYLQCILGIDNIKDVIPFP 252
Cdd:PRK03932 363 AMDLLAPGIGEIIGGSQREERLDVLEARIKELGLnKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFP 442


                 ....*
gi 928166055 253 RFTHS 257
Cdd:PRK03932 443 RTPGR 447
 
Name Accession Description Interval E-value
asnC PRK03932
asparaginyl-tRNA synthetase; Validated
 14-257 2.70e-124

asparaginyl-tRNA synthetase; Validated


Pssm-ID: 235176 [Multi-domain]  Cd Length: 450  Bit Score: 360.96  E-value: 2.70e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  14 AFTQVFTFGPTFRAENSQSRRHLAEFYMVEAEISFVEsLQDLMQVMEGLFKTATMMVLSNCPEDVELCHKFIAPGQKERL 93
Cdd:PRK03932 206 ALGKVYTFGPTFRAENSNTRRHLAEFWMIEPEMAFAD-LEDNMDLAEEMLKYVVKYVLENCPDDLEFLNRRVDKGDIERL 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  94 EHMLKNNFLIISYTEAVEILKQSSQNFTFTPEWGVDLHTEHEKYLVKHCGNIPVFVINYPLALKPFYMRDNEDGpqHTVA 173
Cdd:PRK03932 285 ENFIESPFPRITYTEAIEILQKSGKKFEFPVEWGDDLGSEHERYLAEEHFKKPVFVTNYPKDIKAFYMRLNPDG--KTVA 362

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055 174 AVDLLVPGVGELFGGSLREERYHFLEQRLARSGL-TETYQWYLDLRRFGSVPHGGFGMGFERYLQCILGIDNIKDVIPFP 252
Cdd:PRK03932 363 AMDLLAPGIGEIIGGSQREERLDVLEARIKELGLnKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFP 442


                 ....*
gi 928166055 253 RFTHS 257
Cdd:PRK03932 443 RTPGR 447
AsnS COG0017
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 14-258 8.08e-117

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: 341.26  E-value: 8.08e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  14 AFTQVFTFGPTFRAENSQSRRHLAEFYMVEAEISFVEsLQDLMQVMEGLFKTATMMVLSNCPEDVELCHKFIapgqkERL 93
Cdd:COG0017  194 ALEKVYTFGPTFRAEKSNTRRHLAEFWMIEPEMAFAD-LEDVMDLAEEMLKYIIKYVLENCPEELEFLGRDV-----ERL 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  94 EHMLKNNFLIISYTEAVEILKQSSQNFtftpEWGVDLHTEHEKYLVKHCGNIPVFVINYPLALKPFYMRDNEDGPQhTVA 173
Cdd:COG0017  268 EKVPESPFPRITYTEAIEILKKSGEKV----EWGDDLGTEHERYLGEEFFKKPVFVTDYPKEIKAFYMKPNPDDPK-TVA 342

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055 174 AVDLLVPGVGELFGGSLREERYHFLEQRLARSGL-TETYQWYLDLRRFGSVPHGGFGMGFERYLQCILGIDNIKDVIPFP 252
Cdd:COG0017  343 AFDLLAPGIGEIIGGSQREHRYDVLVERIKEKGLdPEDYEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFP 422


                 ....*.
gi 928166055 253 RFTHSC 258
Cdd:COG0017  423 RDPGRL 428
AsxRS_core cd00776
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ...
 14-256 1.86e-111

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: 323.75  E-value: 1.86e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  14 AFTQVFTFGPTFRAENSQSRRHLAEFYMVEAEISFVESLQDLMQVMEGLFKTATMMVLSNCPEDVELChkfiapGQKERL 93
Cdd:cd00776   88 ALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEDYNEVMDLIEELIKYIFKRVLERCAKELELV------NQLNRE 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  94 EHMLKNNFLIISYTEAVEILKQSSQNftFTPEWGVDLHTEHEKYLVKHCGNIPVFVINYPLALKPFYMRDNEDGPQhTVA 173
Cdd:cd00776  162 LLKPLEPFPRITYDEAIELLREKGVE--EEVKWGEDLSTEHERLLGEIVKGDPVFVTDYPKEIKPFYMKPDDDNPE-TVE 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055 174 AVDLLVPGVGELFGGSLREERYHFLEQRLARSGL-TETYQWYLDLRRFGSVPHGGFGMGFERYLQCILGIDNIKDVIPFP 252
Cdd:cd00776  239 SFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGLdPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318


                 ....
gi 928166055 253 RFTH 256
Cdd:cd00776  319 RDPK 322
asnS TIGR00457
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ...
 14-258 3.28e-109

asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative asparaginyl-tRNA synthetases (asnS), archaeal/eukaryotic type aspartyl-tRNA synthetases (aspS_arch), and bacterial type aspartyl-tRNA synthetases (aspS_bact), there is a striking similarity between asnS and aspS_arch in gap pattern and in sequence, and a striking divergence of aspS_bact. Consequently, a separate model was built for each of the three groups. This model, asnS, represents asparaginyl-tRNA synthetases from the three domains of life. Some species lack this enzyme and charge tRNA(asn) by misacylation with Asp, followed by transamidation of Asp to Asn. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273086 [Multi-domain]  Cd Length: 453  Bit Score: 322.41  E-value: 3.28e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055   14 AFTQVFTFGPTFRAENSQSRRHLAEFYMVEAEISFVEsLQDLMQVMEGLFKTATMMVLSNCPEDVELCHKFIAPGQKERL 93
Cdd:TIGR00457 209 ALSKVYTFGPTFRAEKSNTSRHLSEFWMIEPEMAFAN-LNDLLQLAETLIKYIIKAVLENCSQELKFLEKNFDKDLIKRL 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055   94 EHMLKNNFLIISYTEAVEILKQSSQNFTFTPEWGVDLHTEHEKYLVKHCGNIPVFVINYPLALKPFYMRDNEDGpqHTVA 173
Cdd:TIGR00457 288 ENIINNKFARITYTDAIEILKESDKNFEYEDFWGDDLQTEHERFLAEEYFKPPVFVTNYPKDIKAFYMKLNDDG--KTVA 365

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  174 AVDLLVPGVGELFGGSLREERYHFLEQRLARSGL-TETYQWYLDLRRFGSVPHGGFGMGFERYLQCILGIDNIKDVIPFP 252
Cdd:TIGR00457 366 AMDLLAPGIGEIIGGSEREDDLDKLENRMKEMGLdTDALNWYLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFP 445


                  ....*.
gi 928166055  253 RFTHSC 258
Cdd:TIGR00457 446 RTPGNI 451
tRNA-synt_2 pfam00152
tRNA synthetases class II (D, K and N);
15-255 2.53e-68

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


Pssm-ID: 425487 [Multi-domain]  Cd Length: 318  Bit Score: 213.58  E-value: 2.53e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055   15 FTQVFTFGPTFRAENSQSRRHLaEFYMVEAEISFVEsLQDLMQVMEGLFKTATMMVLsNCPEDVELchkfiapgqkeRLE 94
Cdd:pfam00152  90 FDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVD-YEDVMDLTEELIKEIFKEVE-GIAKELEG-----------GTL 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055   95 HMLKNNFLIISYTEAVEILKQSSqnftfTPEWGVDLHTEHEKYLV----KHCGNIPVFVINYPLALKPFYMRDNEDGPQH 170
Cdd:pfam00152 156 LDLKKPFPRITYAEAIEKLNGKD-----VEELGYGSDKPDLRFLLelviDKNKFNPLWVTDFPAEHHPFTMPKDEDDPAL 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  171 TvAAVDLLVPGVgELFGGSLREERYHFLEQRLARSGLT-----ETYQWYLDLRRFGSVPHGGFGMGFERYLQCILGIDNI 245
Cdd:pfam00152 231 A-EAFDLVLNGV-EIGGGSIRIHDPELQEERFEEQGLDpeeaeEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESI 308

                         250
                  ....*....|
gi 928166055  246 KDVIPFPRFT 255
Cdd:pfam00152 309 REVIAFPKTR 318
 
Name Accession Description Interval E-value
asnC PRK03932
asparaginyl-tRNA synthetase; Validated
 14-257 2.70e-124

asparaginyl-tRNA synthetase; Validated


Pssm-ID: 235176 [Multi-domain]  Cd Length: 450  Bit Score: 360.96  E-value: 2.70e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  14 AFTQVFTFGPTFRAENSQSRRHLAEFYMVEAEISFVEsLQDLMQVMEGLFKTATMMVLSNCPEDVELCHKFIAPGQKERL 93
Cdd:PRK03932 206 ALGKVYTFGPTFRAENSNTRRHLAEFWMIEPEMAFAD-LEDNMDLAEEMLKYVVKYVLENCPDDLEFLNRRVDKGDIERL 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  94 EHMLKNNFLIISYTEAVEILKQSSQNFTFTPEWGVDLHTEHEKYLVKHCGNIPVFVINYPLALKPFYMRDNEDGpqHTVA 173
Cdd:PRK03932 285 ENFIESPFPRITYTEAIEILQKSGKKFEFPVEWGDDLGSEHERYLAEEHFKKPVFVTNYPKDIKAFYMRLNPDG--KTVA 362

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055 174 AVDLLVPGVGELFGGSLREERYHFLEQRLARSGL-TETYQWYLDLRRFGSVPHGGFGMGFERYLQCILGIDNIKDVIPFP 252
Cdd:PRK03932 363 AMDLLAPGIGEIIGGSQREERLDVLEARIKELGLnKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFP 442


                 ....*
gi 928166055 253 RFTHS 257
Cdd:PRK03932 443 RTPGR 447
AsnS COG0017
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 14-258 8.08e-117

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: 341.26  E-value: 8.08e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  14 AFTQVFTFGPTFRAENSQSRRHLAEFYMVEAEISFVEsLQDLMQVMEGLFKTATMMVLSNCPEDVELCHKFIapgqkERL 93
Cdd:COG0017  194 ALEKVYTFGPTFRAEKSNTRRHLAEFWMIEPEMAFAD-LEDVMDLAEEMLKYIIKYVLENCPEELEFLGRDV-----ERL 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  94 EHMLKNNFLIISYTEAVEILKQSSQNFtftpEWGVDLHTEHEKYLVKHCGNIPVFVINYPLALKPFYMRDNEDGPQhTVA 173
Cdd:COG0017  268 EKVPESPFPRITYTEAIEILKKSGEKV----EWGDDLGTEHERYLGEEFFKKPVFVTDYPKEIKAFYMKPNPDDPK-TVA 342

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055 174 AVDLLVPGVGELFGGSLREERYHFLEQRLARSGL-TETYQWYLDLRRFGSVPHGGFGMGFERYLQCILGIDNIKDVIPFP 252
Cdd:COG0017  343 AFDLLAPGIGEIIGGSQREHRYDVLVERIKEKGLdPEDYEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFP 422


                 ....*.
gi 928166055 253 RFTHSC 258
Cdd:COG0017  423 RDPGRL 428
AsxRS_core cd00776
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ...
 14-256 1.86e-111

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: 323.75  E-value: 1.86e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  14 AFTQVFTFGPTFRAENSQSRRHLAEFYMVEAEISFVESLQDLMQVMEGLFKTATMMVLSNCPEDVELChkfiapGQKERL 93
Cdd:cd00776   88 ALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEDYNEVMDLIEELIKYIFKRVLERCAKELELV------NQLNRE 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  94 EHMLKNNFLIISYTEAVEILKQSSQNftFTPEWGVDLHTEHEKYLVKHCGNIPVFVINYPLALKPFYMRDNEDGPQhTVA 173
Cdd:cd00776  162 LLKPLEPFPRITYDEAIELLREKGVE--EEVKWGEDLSTEHERLLGEIVKGDPVFVTDYPKEIKPFYMKPDDDNPE-TVE 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055 174 AVDLLVPGVGELFGGSLREERYHFLEQRLARSGL-TETYQWYLDLRRFGSVPHGGFGMGFERYLQCILGIDNIKDVIPFP 252
Cdd:cd00776  239 SFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGLdPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318


                 ....
gi 928166055 253 RFTH 256
Cdd:cd00776  319 RDPK 322
asnS TIGR00457
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ...
 14-258 3.28e-109

asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative asparaginyl-tRNA synthetases (asnS), archaeal/eukaryotic type aspartyl-tRNA synthetases (aspS_arch), and bacterial type aspartyl-tRNA synthetases (aspS_bact), there is a striking similarity between asnS and aspS_arch in gap pattern and in sequence, and a striking divergence of aspS_bact. Consequently, a separate model was built for each of the three groups. This model, asnS, represents asparaginyl-tRNA synthetases from the three domains of life. Some species lack this enzyme and charge tRNA(asn) by misacylation with Asp, followed by transamidation of Asp to Asn. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273086 [Multi-domain]  Cd Length: 453  Bit Score: 322.41  E-value: 3.28e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055   14 AFTQVFTFGPTFRAENSQSRRHLAEFYMVEAEISFVEsLQDLMQVMEGLFKTATMMVLSNCPEDVELCHKFIAPGQKERL 93
Cdd:TIGR00457 209 ALSKVYTFGPTFRAEKSNTSRHLSEFWMIEPEMAFAN-LNDLLQLAETLIKYIIKAVLENCSQELKFLEKNFDKDLIKRL 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055   94 EHMLKNNFLIISYTEAVEILKQSSQNFTFTPEWGVDLHTEHEKYLVKHCGNIPVFVINYPLALKPFYMRDNEDGpqHTVA 173
Cdd:TIGR00457 288 ENIINNKFARITYTDAIEILKESDKNFEYEDFWGDDLQTEHERFLAEEYFKPPVFVTNYPKDIKAFYMKLNDDG--KTVA 365

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  174 AVDLLVPGVGELFGGSLREERYHFLEQRLARSGL-TETYQWYLDLRRFGSVPHGGFGMGFERYLQCILGIDNIKDVIPFP 252
Cdd:TIGR00457 366 AMDLLAPGIGEIIGGSEREDDLDKLENRMKEMGLdTDALNWYLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFP 445


                  ....*.
gi 928166055  253 RFTHSC 258
Cdd:TIGR00457 446 RTPGNI 451
PLN02603 PLN02603
asparaginyl-tRNA synthetase
 14-253 8.76e-93

asparaginyl-tRNA synthetase


Pssm-ID: 178213 [Multi-domain]  Cd Length: 565  Bit Score: 284.17  E-value: 8.76e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  14 AFTQVFTFGPTFRAENSQSRRHLAEFYMVEAEISFVEsLQDLMQVMEGLFKTATMMVLSNCPEDVELCHKFIAPGQKERL 93
Cdd:PLN02603 320 ALSDVYTFGPTFRAENSNTSRHLAEFWMIEPELAFAD-LNDDMACATAYLQYVVKYILENCKEDMEFFNTWIEKGIIDRL 398

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  94 EHMLKNNFLIISYTEAVEILKQSSQNFTFTPEWGVDLHTEHEKYLVKHC-GNIPVFVINYPLALKPFYMRDNEDGpqHTV 172
Cdd:PLN02603 399 SDVVEKNFVQLSYTDAIELLLKAKKKFEFPVKWGLDLQSEHERYITEEAfGGRPVIIRDYPKEIKAFYMRENDDG--KTV 476

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055 173 AAVDLLVPGVGELFGGSLREERYHFLEQRLARSGLT-ETYQWYLDLRRFGSVPHGGFGMGFERYLQCILGIDNIKDVIPF 251
Cdd:PLN02603 477 AAMDMLVPRVGELIGGSQREERLEYLEARLDELKLNkESYWWYLDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPF 556


                 ..
gi 928166055 252 PR 253
Cdd:PLN02603 557 PR 558
PLN02221 PLN02221
asparaginyl-tRNA synthetase
 14-254 5.72e-89

asparaginyl-tRNA synthetase


Pssm-ID: 177867 [Multi-domain]  Cd Length: 572  Bit Score: 274.56  E-value: 5.72e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  14 AFTQVFTFGPTFRAENSQSRRHLAEFYMVEAEISFVEsLQDLMQVMEGLFKTATMMVLSNCPEDVELCHKFIAPGQKERL 93
Cdd:PLN02221 325 ALSSVYTFGPTFRAENSHTSRHLAEFWMVEPEIAFAD-LEDDMNCAEAYVKYMCKWLLDKCFDDMELMAKNFDSGCIDRL 403

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  94 EHMLKNNFLIISYTEAVEILKQS---SQNFTFTPEWGVDLHTEHEKYLVKHCGNIPVFVINYPLALKPFYMRDNEDgpQH 170
Cdd:PLN02221 404 RMVASTPFGRITYTEAIELLEEAvakGKEFDNNVEWGIDLASEHERYLTEVLFQKPLIVYNYPKGIKAFYMRLNDD--EK 481

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055 171 TVAAVDLLVPGVGELFGGSLREERYHFLEQRLARSGL-TETYQWYLDLRRFGSVPHGGFGMGFERYLQCILGIDNIKDVI 249
Cdd:PLN02221 482 TVAAMDVLVPKVGELIGGSQREERYDVIKQRIEEMGLpIEPYEWYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVI 561


                 ....*
gi 928166055 250 PFPRF 254
Cdd:PLN02221 562 PFPRY 566
PTZ00425 PTZ00425
asparagine-tRNA ligase; Provisional
 18-254 5.00e-79

asparagine-tRNA ligase; Provisional


Pssm-ID: 240414 [Multi-domain]  Cd Length: 586  Bit Score: 249.17  E-value: 5.00e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  18 VFTFGPTFRAENSQSRRHLAEFYMVEAEISFVEsLQDLMQVMEGLFKTATMMVLSNCPEDVELCHKFIAPGQKERLEHML 97
Cdd:PTZ00425 346 VYTFGPTFRAENSHTSRHLAEFWMIEPEIAFAD-LYDNMELAESYIKYCIGYVLNNNFDDIYYFEENVETGLISRLKNIL 424

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  98 KNNFLIISYTEAVEILKQSSQNFTFTPEWGVDLHTEHEKYLVKHCGNIPVFVINYPLALKPFYMRDNEDgpQHTVAAVDL 177
Cdd:PTZ00425 425 DEDFAKITYTNVIDLLQPYSDSFEVPVKWGMDLQSEHERFVAEQIFKKPVIVYNYPKDLKAFYMKLNED--QKTVAAMDV 502

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 928166055 178 LVPGVGELFGGSLREERYHFLEQRLARSGLT-ETYQWYLDLRRFGSVPHGGFGMGFERYLQCILGIDNIKDVIPFPRF 254
Cdd:PTZ00425 503 LVPKIGEVIGGSQREDNLERLDKMIKEKKLNmESYWWYRQLRKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFPRY 580
PLN02532 PLN02532
asparagine-tRNA synthetase
 14-253 1.96e-75

asparagine-tRNA synthetase


Pssm-ID: 215291 [Multi-domain]  Cd Length: 633  Bit Score: 240.93  E-value: 1.96e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  14 AFTQVFTFGPTFRAENSQSRRHLAEFYMVEAEISFVEsLQDLMQVMEGLFKTATMMVLSNCPEDVELCHKFIAPGQKERL 93
Cdd:PLN02532 388 ALGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAFSE-LEDAMNCAEDYFKFLCKWVLENCSEDMKFVSKRIDKTISTRL 466

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  94 EHMLKNNFLIISYTEAVEILKQSSQN-FTFTPEWGVDLHTEHEKYLVKHCGNIPVFVINYPLALKPFYMRDNEDGpqHTV 172
Cdd:PLN02532 467 EAIISSSLQRISYTEAVDLLKQATDKkFETKPEWGIALTTEHLSYLADEIYKKPVIIYNYPKELKPFYVRLNDDG--KTV 544

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055 173 AAVDLLVPGVGELFGGSLREERYHFLEQRLARSGLT-ETYQWYLDLRRFGSVPHGGFGMGFERYLQCILGIDNIKDVIPF 251
Cdd:PLN02532 545 AAFDLVVPKVGTVITGSQNEERMDILNARIEELGLPrEQYEWYLDLRRHGTVKHSGFSLGFELMVLFATGLPDVRDAIPF 624


                 ..
gi 928166055 252 PR 253
Cdd:PLN02532 625 PR 626
tRNA-synt_2 pfam00152
tRNA synthetases class II (D, K and N);
15-255 2.53e-68

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


Pssm-ID: 425487 [Multi-domain]  Cd Length: 318  Bit Score: 213.58  E-value: 2.53e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055   15 FTQVFTFGPTFRAENSQSRRHLaEFYMVEAEISFVEsLQDLMQVMEGLFKTATMMVLsNCPEDVELchkfiapgqkeRLE 94
Cdd:pfam00152  90 FDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVD-YEDVMDLTEELIKEIFKEVE-GIAKELEG-----------GTL 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055   95 HMLKNNFLIISYTEAVEILKQSSqnftfTPEWGVDLHTEHEKYLV----KHCGNIPVFVINYPLALKPFYMRDNEDGPQH 170
Cdd:pfam00152 156 LDLKKPFPRITYAEAIEKLNGKD-----VEELGYGSDKPDLRFLLelviDKNKFNPLWVTDFPAEHHPFTMPKDEDDPAL 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  171 TvAAVDLLVPGVgELFGGSLREERYHFLEQRLARSGLT-----ETYQWYLDLRRFGSVPHGGFGMGFERYLQCILGIDNI 245
Cdd:pfam00152 231 A-EAFDLVLNGV-EIGGGSIRIHDPELQEERFEEQGLDpeeaeEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESI 308

                         250
                  ....*....|
gi 928166055  246 KDVIPFPRFT 255
Cdd:pfam00152 309 REVIAFPKTR 318
aspC PRK05159
aspartyl-tRNA synthetase; Provisional
 15-253 1.12e-57

aspartyl-tRNA synthetase; Provisional


Pssm-ID: 235354 [Multi-domain]  Cd Length: 437  Bit Score: 189.63  E-value: 1.12e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  15 FTQVFTFGPTFRAENSQSRRHLAEFYMVEAEISFVESLQDLMQVMEGLFKTATMMVLSNCPEDVELchkfiapgqkerLE 94
Cdd:PRK05159 202 FERVFEIGPVFRAEEHNTSRHLNEYTSIDVEMGFIDDHEDVMDLLENLLRYMYEDVAENCEKELEL------------LG 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  95 HML---KNNFLIISYTEAVEILKQSSQNftftPEWGVDLHTEHEKYLVKH----CGNIPVFVINYPLALKPFYMRDNEDG 167
Cdd:PRK05159 270 IELpvpETPIPRITYDEAIEILKSKGNE----ISWGDDLDTEGERLLGEYvkeeYGSDFYFITDYPSEKRPFYTMPDEDD 345

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055 168 PQHTvAAVDLLVPGVgELFGGSLREERYHFLEQRLARSGL-TETYQWYLDLRRFGSVPHGGFGMGFERYLQCILGIDNIK 246
Cdd:PRK05159 346 PEIS-KSFDLLFRGL-EITSGGQRIHRYDMLVESIKEKGLnPESFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIR 423


                 ....*..
gi 928166055 247 DVIPFPR 253
Cdd:PRK05159 424 EAVLFPR 430
PRK06462 PRK06462
asparagine synthetase A; Reviewed
 12-253 3.45e-40

asparagine synthetase A; Reviewed


Pssm-ID: 235808 [Multi-domain]  Cd Length: 335  Bit Score: 141.70  E-value: 3.45e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  12 LKAFTQVFTFGPTFRAEN--SQSRRHLAEFYMVEAEISFVeSLQDLMQVMEGLFKTATMMVLSNCPEDVELCHKfiapgq 89
Cdd:PRK06462  99 LRMLGKIFYLSPNFRLEPvdKDTGRHLYEFTQLDIEIEGA-DLDEVMDLIEDLIKYLVKELLEEHEDELEFFGR------ 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  90 keRLEHmLKNNFLIISYTEAVEILKQSSQNFTFTPEWGvdlhTEHEKYLVKHCGNiPVFVINYPLALKPFYMRDNEDGPQ 169
Cdd:PRK06462 172 --DLPH-LKRPFKRITHKEAVEILNEEGCRGIDLEELG----SEGEKSLSEHFEE-PFWIIDIPKGSREFYDREDPERPG 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055 170 HTVAAvDLLVP-GVGELFGGSLREERYHFLEQRLARSGLT-ETYQWYLDLRRFGSVPHGGFGMGFERYLQCILGIDNIKD 247
Cdd:PRK06462 244 VLRNY-DLLLPeGYGEAVSGGEREYEYEEIVERIREHGVDpEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIRE 322


                 ....*.
gi 928166055 248 VIPFPR 253
Cdd:PRK06462 323 VQPFPR 328
aspS_nondisc TIGR00458
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ...
 15-253 7.93e-34

nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative asparaginyl-tRNA synthetases (asnS), archaeal/eukaryotic type aspartyl-tRNA synthetases (aspS_arch), and bacterial type aspartyl-tRNA synthetases (aspS_bact), there is a striking similarity between asnS and aspS_arch in gap pattern and in sequence, and a striking divergence of aspS_bact. Consequently, a separate model was built for each of the three groups. This model, aspS_arch, represents aspartyl-tRNA synthetases from the eukaryotic cytosol and from the Archaea. In some species, this enzyme aminoacylates tRNA for both Asp and Asn; Asp-tRNA(asn) is subsequently transamidated to Asn-tRNA(asn). [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273087 [Multi-domain]  Cd Length: 428  Bit Score: 126.48  E-value: 7.93e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055   15 FTQVFTFGPTFRAENSQSRRHLAEFYMVEAEISFVESlQDLMQVMEGLFKTATMMVLSNCPEDVE-LCHKFIAPGQKerl 93
Cdd:TIGR00458 199 FERVYEIGPIFRAEEHNTHRHLNEATSIDIEMAFEDH-HDVMDILEELVVRVFEDVPERCAHQLEtLEFKLEKPEGK--- 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055   94 ehmlknnFLIISYTEAVEILKQSSQNFTftpeWGVDLHTEHEKYLVKHCGNIpVFVINYPLALKPFYMRDNEDGPQHTvA 173
Cdd:TIGR00458 275 -------FVRLTYDEAIEMANAKGVEIG----WGEDLSTEAEKALGEEMDGL-YFITDWPTEIRPFYTMPDEDNPEIS-K 341

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  174 AVDLLVPGVgELFGGSLREERYHFLEQRLARSGLT-ETYQWYLDLRRFGSVPHGGFGMGFERYLQCILGIDNIKDVIPFP 252
Cdd:TIGR00458 342 SFDLMYRDL-EISSGAQRIHLHDLLVERIKAKGLNpEGFKDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFP 420


                  .
gi 928166055  253 R 253
Cdd:TIGR00458 421 R 421
PLN02850 PLN02850
aspartate-tRNA ligase
 15-253 9.75e-31

aspartate-tRNA ligase


Pssm-ID: 215456 [Multi-domain]  Cd Length: 530  Bit Score: 119.43  E-value: 9.75e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  15 FTQVFTFGPTFRAENSQSRRHLAEFYMVEAEISFVESLQDLMQVMEGLFKTATMMVLSNCPEDVELC---HKFiapgqkE 91
Cdd:PLN02850 291 FRRVFEIGPVFRAEDSFTHRHLCEFTGLDLEMEIKEHYSEVLDVVDELFVAIFDGLNERCKKELEAIreqYPF------E 364

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  92 RLEHMLKNnfLIISYTEAVEILKqssqnftftpEWGV------DLHTEHEKYL---VKHCGNIPVFVIN-YPLALKPFYM 161
Cdd:PLN02850 365 PLKYLPKT--LRLTFAEGIQMLK----------EAGVevdplgDLNTESERKLgqlVKEKYGTDFYILHrYPLAVRPFYT 432

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055 162 RDNEDGPQHTvAAVDLLVPGvGELFGGSLREERYHFLEQRLARSGL-TETYQWYLDLRRFGSVPHGGFGMGFERYLQCIL 240
Cdd:PLN02850 433 MPCPDDPKYS-NSFDVFIRG-EEIISGAQRVHDPELLEKRAEECGIdVKTISTYIDSFRYGAPPHGGFGVGLERVVMLFC 510

                        250
                 ....*....|...
gi 928166055 241 GIDNIKDVIPFPR 253
Cdd:PLN02850 511 GLNNIRKTSLFPR 523
Asp_Lys_Asn_RS_core cd00669
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ...
 15-253 8.12e-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: 96.78  E-value: 8.12e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  15 FTQVFTFGPTFRAENSqSRRHLAEFYMVEAEISFVEsLQDLMQVMEGLFKTATMMVLSNcpedvelchkfiapGQKERLE 94
Cdd:cd00669   69 LDRVFEINRNFRNEDL-RARHQPEFTMMDLEMAFAD-YEDVIELTERLVRHLAREVLGV--------------TAVTYGF 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  95 HML--KNNFLIISYTEAVEILKQssqnftftpewgvdlhtehekylvkhcgniPVFVINYPLALKPFYMRDNEDGPQHTv 172
Cdd:cd00669  133 ELEdfGLPFPRLTYREALERYGQ------------------------------PLFLTDYPAEMHSPLASPHDVNPEIA- 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055 173 AAVDLLVPGVgELFGGSLRE-----ERYHFLEQRLARSGLTETYQWYLDLRRFGSVPHGGFGMGFERYLQCILGIDNIKD 247
Cdd:cd00669  182 DAFDLFINGV-EVGNGSSRLhdpdiQAEVFQEQGINKEAGMEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIRE 260


                 ....*.
gi 928166055 248 VIPFPR 253
Cdd:cd00669  261 VIAFPK 266
PTZ00401 PTZ00401
aspartyl-tRNA synthetase; Provisional
 17-253 7.61e-19

aspartyl-tRNA synthetase; Provisional


Pssm-ID: 173592 [Multi-domain]  Cd Length: 550  Bit Score: 85.43  E-value: 7.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  17 QVFTFGPTFRAENSQSRRHLAEFYMVEAEISFVESLQDLMQVMEGLFKTATMMVLSNCPEDVELCHKF--------IAPG 88
Cdd:PTZ00401 281 RVFEVGPVFRSENSNTHRHLTEFVGLDVEMRINEHYYEVLDLAESLFNYIFERLATHTKELKAVCQQYpfeplvwkLTPE 360

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  89 QKERLE------------------HMLKNNFLIISYTEAVEILKQS-SQNFTFTPewgvDLHTEHEKYL---VKHCGNIP 146
Cdd:PTZ00401 361 RMKELGvgvisegveptdkyqarvHNMDSRMLRINYMHCIELLNTVlEEKMAPTD----DINTTNEKLLgklVKERYGTD 436

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055 147 VFVIN-YPLALKPFYMRDNEDGPQHTvAAVDLLVPGvGELFGGSLREERYHFLEQRLARSGLTET-YQWYLDLRRFGSVP 224
Cdd:PTZ00401 437 FFISDrFPSSARPFYTMECKDDERFT-NSYDMFIRG-EEISSGAQRIHDPDLLLARAKMLNVDLTpIKEYVDSFRLGAWP 514

                        250       260
                 ....*....|....*....|....*....
gi 928166055 225 HGGFGMGFERYLQCILGIDNIKDVIPFPR 253
Cdd:PTZ00401 515 HGGFGVGLERVVMLYLGLSNVRLASLFPR 543
AspRS_core cd00777
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ...
 25-252 2.67e-15

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: 73.76  E-value: 2.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  25 FRAENSQSRRHlAEFYMVEAEISFVESlQDLMQVMEGLFktatmmvlsncpedvelCHKFiapgqKERLEHMLKNNFLII 104
Cdd:cd00777   79 FRDEDLRADRQ-PEFTQIDIEMSFVDQ-EDIMSLIEGLL-----------------KYVF-----KEVLGVELTTPFPRM 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055 105 SYTEAVEilkqssqNFTFTPEWGVD-----LHTEHEKYLVKHcgnipvfvinYPL-ALKPFYMRDNEDGPQHTVA-AVDL 177
Cdd:cd00777  135 TYAEAME-------RYGFKFLWIVDfplfeWDEEEGRLVSAH----------HPFtAPKEEDLDLLEKDPEDARAqAYDL 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055 178 LVPGVgELFGGSLREERYHFLEQRLARSGLTETYQW-----YLDLRRFGSVPHGGFGMGFERYLQCILGIDNIKDVIPFP 252
Cdd:cd00777  198 VLNGV-ELGGGSIRIHDPDIQEKVFEILGLSEEEAEekfgfLLEAFKYGAPPHGGIALGLDRLVMLLTGSESIRDVIAFP 276
PLN02903 PLN02903
aminoacyl-tRNA ligase
 163-260 6.37e-09

aminoacyl-tRNA ligase


Pssm-ID: 215490 [Multi-domain]  Cd Length: 652  Bit Score: 55.95  E-value: 6.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055 163 DNEDGPQHTVAAVDLLVPGVgELFGGSLREERYHFLEQRLARSGLT-----ETYQWYLDLRRFGSVPHGGFGMGFERYLQ 237
Cdd:PLN02903 526 DMGDLSSARALAYDMVYNGV-EIGGGSLRIYRRDVQQKVLEAIGLSpeeaeSKFGYLLEALDMGAPPHGGIAYGLDRLVM 604

                         90       100
                 ....*....|....*....|....
gi 928166055 238 CILGIDNIKDVIPFPRFTHS-CIL 260
Cdd:PLN02903 605 LLAGAKSIRDVIAFPKTTTAqCAL 628
LysRS_core cd00775
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ...
 15-252 1.26e-08

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: 54.51  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  15 FTQVFTFGPTFRAEnSQSRRHLAEFYMVEAEISFVeSLQDLMQVMEGLFKTATMMVLSNCP---EDVELCHKF------I 85
Cdd:cd00775   76 FERVYEIGRNFRNE-GIDLTHNPEFTMIEFYEAYA-DYNDMMDLTEDLFSGLVKKINGKTKieyGGKELDFTPpfkrvtM 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  86 APGQKERLEHMLKNNFLIISYTEAVEILKQSSQNFTFTPEWGVDLHTEHEKYLVKHCGNiPVFVINYPLALKPFYMRDNE 165
Cdd:cd00775  154 VDALKEKTGIDFPELDLEQPEELAKLLAKLIKEKIEKPRTLGKLLDKLFEEFVEPTLIQ-PTFIIDHPVEISPLAKRHRS 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055 166 DgpqhtvaavdllvPGVGELF----GGslRE-------------ERYHFLEQ-RLARSGLTETYQW---YLDLRRFGSVP 224
Cdd:cd00775  233 N-------------PGLTERFelfiCG--KEianaytelndpfdQRERFEEQaKQKEAGDDEAMMMdedFVTALEYGMPP 297

                        250       260
                 ....*....|....*....|....*...
gi 928166055 225 HGGFGMGFERYLQCILGIDNIKDVIPFP 252
Cdd:cd00775  298 TGGLGIGIDRLVMLLTDSNSIRDVILFP 325
PRK12820 PRK12820
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ...
 146-253 3.66e-07

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


Pssm-ID: 105955 [Multi-domain]  Cd Length: 706  Bit Score: 50.76  E-value: 3.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055 146 PVFVINYPL-----------ALKPFYMRDNEDGPQHTVA--------AVDLLVPGvGELFGGSLREERYHFLEQRLARSG 206
Cdd:PRK12820 443 PLWITDFPLfeatddggvtsSHHPFTAPDREDFDPGDIEelldlrsrAYDLVVNG-EELGGGSIRINDKDIQLRIFAALG 521

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 928166055 207 LTE-----TYQWYLDLRRFGSVPHGGFGMGFERYLQCILGIDNIKDVIPFPR 253
Cdd:PRK12820 522 LSEediedKFGFFLRAFDFAAPPHGGIALGLDRVVSMILQTPSIREVIAFPK 573
PRK12445 PRK12445
lysyl-tRNA synthetase; Reviewed
 14-252 4.52e-07

lysyl-tRNA synthetase; Reviewed


Pssm-ID: 171504 [Multi-domain]  Cd Length: 505  Bit Score: 50.45  E-value: 4.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  14 AFTQVFTFGPTFRAENSqSRRHLAEFYMVEAEISFVEsLQDLMQVMEGLFKTATMMVLSNCPEDV-ELCHKFIAPGQKER 92
Cdd:PRK12445 251 GFERVFEINRNFRNEGI-SVRHNPEFTMMELYMAYAD-YHDLIELTESLFRTLAQEVLGTTKVTYgEHVFDFGKPFEKLT 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055  93 LEHMLK-----NNFLIISYTEAVEILKQSSqNFTFTPEWGVD-LHTE-----HEKYLVKhcgniPVFVINYPLALKPFyM 161
Cdd:PRK12445 329 MREAIKkyrpeTDMADLDNFDAAKALAESI-GITVEKSWGLGrIVTEifdevAEAHLIQ-----PTFITEYPAEVSPL-A 401

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055 162 RDNEDGPQHTvAAVDLLVPG--VGELFG--GSLREERYHFLEQRLARSGLTETYQWY----LDLRRFGSVPHGGFGMGFE 233
Cdd:PRK12445 402 RRNDVNPEIT-DRFEFFIGGreIGNGFSelNDAEDQAERFQEQVNAKAAGDDEAMFYdedyVTALEYGLPPTAGLGIGID 480

                        250
                 ....*....|....*....
gi 928166055 234 RYLQCILGIDNIKDVIPFP 252
Cdd:PRK12445 481 RMIMLFTNSHTIRDVILFP 499
PTZ00385 PTZ00385
lysyl-tRNA synthetase; Provisional
 146-252 2.20e-04

lysyl-tRNA synthetase; Provisional


Pssm-ID: 185588 [Multi-domain]  Cd Length: 659  Bit Score: 42.33  E-value: 2.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928166055 146 PVFVINYPLALKPFyMRDNEDGPQhTVAAVDLLVPGV------GELfggSLREERYHFLEQRLA-RSG-------LTETY 211
Cdd:PTZ00385 448 PTFVMDHPLFMSPL-AKEQVSRPG-LAERFELFVNGIeycnaySEL---NDPHEQYHRFQQQLVdRQGgdeeampLDETF 522

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 928166055 212 qwyLDLRRFGSVPHGGFGMGFERYLQCILGIDNIKDVIPFP 252
Cdd:PTZ00385 523 ---LKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFP 560
aspS PRK00476
aspartyl-tRNA synthetase; Validated
 219-252 7.34e-04

aspartyl-tRNA synthetase; Validated


Pssm-ID: 234775 [Multi-domain]  Cd Length: 588  Bit Score: 40.44  E-value: 7.34e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 928166055 219 RFGSVPHGGFGMGFERYLQCILGIDNIKDVIPFP 252
Cdd:PRK00476 523 KYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
AspS COG0173
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ...
 219-252 8.13e-04

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: 40.37  E-value: 8.13e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 928166055 219 RFGSVPHGGFGMGFERYLQCILGIDNIKDVIPFP 252
Cdd:COG0173  522 KYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
 
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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