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Conserved domains on  [gi|1309078214|gb|PKP60323|]
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MAG: aspartate--tRNA(Asn) ligase, partial [Candidatus Altiarchaeales archaeon HGW-Altiarchaeales-2]

Protein Classification

aspartate--tRNA ligase( domain architecture ID 1002249)

aspartate--tRNA ligase attaches aspartate to the 3' OH group of ribose of tRNA(Asp)

CATH:  3.30.1360.30
EC:  6.1.1.12
Gene Ontology:  GO:0003676|GO:0005524|GO:0006422|GO:0004815
SCOP:  4001480

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
aspC super family cl35289
aspartyl-tRNA synthetase; Provisional
 2-187 1.20e-81

aspartyl-tRNA synthetase; Provisional


The actual alignment was detected with superfamily member PRK05159:

Pssm-ID: 235354 [Multi-domain]  Cd Length: 437  Bit Score: 248.57  E-value: 1.20e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214   2 ATYFRAESHDTTRHLNEITAFDCEMSFVDTENDVMDVIEGLMKTILSEARD--SEEVKILNKEISIPEK-FPRLCYDECL 78
Cdd:PRK05159  209 GPVFRAEEHNTSRHLNEYTSIDVEMGFIDDHEDVMDLLENLLRYMYEDVAEncEKELELLGIELPVPETpIPRITYDEAI 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214  79 LYLNEKNITIEWGGDIDTKCERVLGEVVKDKFGSELFFITKYPLKIKPFYTAPEnfDADDKYSRAFDLEYKGVEISSGGQ 158
Cdd:PRK05159  289 EILKSKGNEISWGDDLDTEGERLLGEYVKEEYGSDFYFITDYPSEKRPFYTMPD--EDDPEISKSFDLLFRGLEITSGGQ 366

                         170       180
                  ....*....|....*....|....*....
gi 1309078214 159 RVHIHNLLAERIKRCNLNPENFKFYLDAF 187
Cdd:PRK05159  367 RIHRYDMLVESIKEKGLNPESFEFYLEAF 395
 
Name Accession Description Interval E-value
aspC PRK05159
aspartyl-tRNA synthetase; Provisional
 2-187 1.20e-81

aspartyl-tRNA synthetase; Provisional


Pssm-ID: 235354 [Multi-domain]  Cd Length: 437  Bit Score: 248.57  E-value: 1.20e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214   2 ATYFRAESHDTTRHLNEITAFDCEMSFVDTENDVMDVIEGLMKTILSEARD--SEEVKILNKEISIPEK-FPRLCYDECL 78
Cdd:PRK05159  209 GPVFRAEEHNTSRHLNEYTSIDVEMGFIDDHEDVMDLLENLLRYMYEDVAEncEKELELLGIELPVPETpIPRITYDEAI 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214  79 LYLNEKNITIEWGGDIDTKCERVLGEVVKDKFGSELFFITKYPLKIKPFYTAPEnfDADDKYSRAFDLEYKGVEISSGGQ 158
Cdd:PRK05159  289 EILKSKGNEISWGDDLDTEGERLLGEYVKEEYGSDFYFITDYPSEKRPFYTMPD--EDDPEISKSFDLLFRGLEITSGGQ 366

                         170       180
                  ....*....|....*....|....*....
gi 1309078214 159 RVHIHNLLAERIKRCNLNPENFKFYLDAF 187
Cdd:PRK05159  367 RIHRYDMLVESIKEKGLNPESFEFYLEAF 395
AsnS COG0017
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 5-187 1.85e-66

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: 209.14  E-value: 1.85e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214   5 FRAESHDTTRHLNEITAFDCEMSFVDtENDVMDVIEGLMKTILSEARD--SEEVKILNKEISIPEK-----FPRLCYDEC 77
Cdd:COG0017   205 FRAEKSNTRRHLAEFWMIEPEMAFAD-LEDVMDLAEEMLKYIIKYVLEncPEELEFLGRDVERLEKvpespFPRITYTEA 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214  78 LLYLNEKNITIEWGGDIDTKCERVLGEvvkdKFGSELFFITKYPLKIKPFYTAPEnfDADDKYSRAFDLEYKGV-EISSG 156
Cdd:COG0017   284 IEILKKSGEKVEWGDDLGTEHERYLGE----EFFKKPVFVTDYPKEIKAFYMKPN--PDDPKTVAAFDLLAPGIgEIIGG 357

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1309078214 157 GQRVHIHNLLAERIKRCNLNPENFKFYLDAF 187
Cdd:COG0017   358 SQREHRYDVLVERIKEKGLDPEDYEWYLDLR 388
AsxRS_core cd00776
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ...
 5-187 1.05e-61

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: 193.94  E-value: 1.05e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214   5 FRAESHDTTRHLNEITAFDCEMSFVDTENDVMDVIEGLMKTILSE-----ARDSEEVKILNKEISIP-EKFPRLCYDECL 78
Cdd:cd00776    99 FRAEKSNTRRHLSEFWMLEAEMAFIEDYNEVMDLIEELIKYIFKRvlercAKELELVNQLNRELLKPlEPFPRITYDEAI 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214  79 LYLNEKNIT--IEWGGDIDTKCERVLGEVVKDKFgselFFITKYPLKIKPFYTAPEnfDADDKYSRAFDLEYKGV-EISS 155
Cdd:cd00776   179 ELLREKGVEeeVKWGEDLSTEHERLLGEIVKGDP----VFVTDYPKEIKPFYMKPD--DDNPETVESFDLLMPGVgEIVG 252

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1309078214 156 GGQRVHIHNLLAERIKRCNLNPENFKFYLDAF 187
Cdd:cd00776   253 GSQRIHDYDELEERIKEHGLDPESFEWYLDLR 284
aspS_nondisc TIGR00458
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ...
 5-187 6.27e-56

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: 181.95  E-value: 6.27e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214   5 FRAESHDTTRHLNEITAFDCEMSFVDtENDVMDVIEGLMKTILSEA--RDSEEVKILNKEISIPE-KFPRLCYDECLLYL 81
Cdd:TIGR00458 209 FRAEEHNTHRHLNEATSIDIEMAFED-HHDVMDILEELVVRVFEDVpeRCAHQLETLEFKLEKPEgKFVRLTYDEAIEMA 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214  82 NEKNITIEWGGDIDTKCERVLGEVVKDkfgseLFFITKYPLKIKPFYTAPEnfDADDKYSRAFDLEYKGVEISSGGQRVH 161
Cdd:TIGR00458 288 NAKGVEIGWGEDLSTEAEKALGEEMDG-----LYFITDWPTEIRPFYTMPD--EDNPEISKSFDLMYRDLEISSGAQRIH 360

                         170       180
                  ....*....|....*....|....*.
gi 1309078214 162 IHNLLAERIKRCNLNPENFKFYLDAF 187
Cdd:TIGR00458 361 LHDLLVERIKAKGLNPEGFKDYLEAF 386
tRNA-synt_2 pfam00152
tRNA synthetases class II (D, K and N);
5-187 2.40e-48

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


Pssm-ID: 425487 [Multi-domain]  Cd Length: 318  Bit Score: 159.65  E-value: 2.40e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214   5 FRAESHDTTRHLnEITAFDCEMSFVDtENDVMDVIEGLMKTILSEARDSEEVKILNKEISIPEKFPRLCYDECLLYLNEK 84
Cdd:pfam00152 100 FRDEDLRTDRQP-EFTQLDLEMSFVD-YEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDLKKPFPRITYAEAIEKLNGK 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214  85 NItIEWGGDIDTKCERVLGEVVKDKFGSELFFITKYPLKIKPFYTAPEnfDADDKYSRAFDLEYKGVEISSGGQRVHIHN 164
Cdd:pfam00152 178 DV-EELGYGSDKPDLRFLLELVIDKNKFNPLWVTDFPAEHHPFTMPKD--EDDPALAEAFDLVLNGVEIGGGSIRIHDPE 254

                         170       180
                  ....*....|....*....|....*..
gi 1309078214 165 LLAERIKRCNLNP----ENFKFYLDAF 187
Cdd:pfam00152 255 LQEERFEEQGLDPeeaeEKFGFYLDAL 281
 
Name Accession Description Interval E-value
aspC PRK05159
aspartyl-tRNA synthetase; Provisional
 2-187 1.20e-81

aspartyl-tRNA synthetase; Provisional


Pssm-ID: 235354 [Multi-domain]  Cd Length: 437  Bit Score: 248.57  E-value: 1.20e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214   2 ATYFRAESHDTTRHLNEITAFDCEMSFVDTENDVMDVIEGLMKTILSEARD--SEEVKILNKEISIPEK-FPRLCYDECL 78
Cdd:PRK05159  209 GPVFRAEEHNTSRHLNEYTSIDVEMGFIDDHEDVMDLLENLLRYMYEDVAEncEKELELLGIELPVPETpIPRITYDEAI 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214  79 LYLNEKNITIEWGGDIDTKCERVLGEVVKDKFGSELFFITKYPLKIKPFYTAPEnfDADDKYSRAFDLEYKGVEISSGGQ 158
Cdd:PRK05159  289 EILKSKGNEISWGDDLDTEGERLLGEYVKEEYGSDFYFITDYPSEKRPFYTMPD--EDDPEISKSFDLLFRGLEITSGGQ 366

                         170       180
                  ....*....|....*....|....*....
gi 1309078214 159 RVHIHNLLAERIKRCNLNPENFKFYLDAF 187
Cdd:PRK05159  367 RIHRYDMLVESIKEKGLNPESFEFYLEAF 395
AsnS COG0017
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 5-187 1.85e-66

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: 209.14  E-value: 1.85e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214   5 FRAESHDTTRHLNEITAFDCEMSFVDtENDVMDVIEGLMKTILSEARD--SEEVKILNKEISIPEK-----FPRLCYDEC 77
Cdd:COG0017   205 FRAEKSNTRRHLAEFWMIEPEMAFAD-LEDVMDLAEEMLKYIIKYVLEncPEELEFLGRDVERLEKvpespFPRITYTEA 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214  78 LLYLNEKNITIEWGGDIDTKCERVLGEvvkdKFGSELFFITKYPLKIKPFYTAPEnfDADDKYSRAFDLEYKGV-EISSG 156
Cdd:COG0017   284 IEILKKSGEKVEWGDDLGTEHERYLGE----EFFKKPVFVTDYPKEIKAFYMKPN--PDDPKTVAAFDLLAPGIgEIIGG 357

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1309078214 157 GQRVHIHNLLAERIKRCNLNPENFKFYLDAF 187
Cdd:COG0017   358 SQREHRYDVLVERIKEKGLDPEDYEWYLDLR 388
AsxRS_core cd00776
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ...
 5-187 1.05e-61

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: 193.94  E-value: 1.05e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214   5 FRAESHDTTRHLNEITAFDCEMSFVDTENDVMDVIEGLMKTILSE-----ARDSEEVKILNKEISIP-EKFPRLCYDECL 78
Cdd:cd00776    99 FRAEKSNTRRHLSEFWMLEAEMAFIEDYNEVMDLIEELIKYIFKRvlercAKELELVNQLNRELLKPlEPFPRITYDEAI 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214  79 LYLNEKNIT--IEWGGDIDTKCERVLGEVVKDKFgselFFITKYPLKIKPFYTAPEnfDADDKYSRAFDLEYKGV-EISS 155
Cdd:cd00776   179 ELLREKGVEeeVKWGEDLSTEHERLLGEIVKGDP----VFVTDYPKEIKPFYMKPD--DDNPETVESFDLLMPGVgEIVG 252

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1309078214 156 GGQRVHIHNLLAERIKRCNLNPENFKFYLDAF 187
Cdd:cd00776   253 GSQRIHDYDELEERIKEHGLDPESFEWYLDLR 284
aspS_nondisc TIGR00458
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ...
 5-187 6.27e-56

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: 181.95  E-value: 6.27e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214   5 FRAESHDTTRHLNEITAFDCEMSFVDtENDVMDVIEGLMKTILSEA--RDSEEVKILNKEISIPE-KFPRLCYDECLLYL 81
Cdd:TIGR00458 209 FRAEEHNTHRHLNEATSIDIEMAFED-HHDVMDILEELVVRVFEDVpeRCAHQLETLEFKLEKPEgKFVRLTYDEAIEMA 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214  82 NEKNITIEWGGDIDTKCERVLGEVVKDkfgseLFFITKYPLKIKPFYTAPEnfDADDKYSRAFDLEYKGVEISSGGQRVH 161
Cdd:TIGR00458 288 NAKGVEIGWGEDLSTEAEKALGEEMDG-----LYFITDWPTEIRPFYTMPD--EDNPEISKSFDLMYRDLEISSGAQRIH 360

                         170       180
                  ....*....|....*....|....*.
gi 1309078214 162 IHNLLAERIKRCNLNPENFKFYLDAF 187
Cdd:TIGR00458 361 LHDLLVERIKAKGLNPEGFKDYLEAF 386
tRNA-synt_2 pfam00152
tRNA synthetases class II (D, K and N);
5-187 2.40e-48

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


Pssm-ID: 425487 [Multi-domain]  Cd Length: 318  Bit Score: 159.65  E-value: 2.40e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214   5 FRAESHDTTRHLnEITAFDCEMSFVDtENDVMDVIEGLMKTILSEARDSEEVKILNKEISIPEKFPRLCYDECLLYLNEK 84
Cdd:pfam00152 100 FRDEDLRTDRQP-EFTQLDLEMSFVD-YEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDLKKPFPRITYAEAIEKLNGK 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214  85 NItIEWGGDIDTKCERVLGEVVKDKFGSELFFITKYPLKIKPFYTAPEnfDADDKYSRAFDLEYKGVEISSGGQRVHIHN 164
Cdd:pfam00152 178 DV-EELGYGSDKPDLRFLLELVIDKNKFNPLWVTDFPAEHHPFTMPKD--EDDPALAEAFDLVLNGVEIGGGSIRIHDPE 254

                         170       180
                  ....*....|....*....|....*..
gi 1309078214 165 LLAERIKRCNLNP----ENFKFYLDAF 187
Cdd:pfam00152 255 LQEERFEEQGLDPeeaeEKFGFYLDAL 281
PLN02850 PLN02850
aspartate-tRNA ligase
 5-187 1.43e-42

aspartate-tRNA ligase


Pssm-ID: 215456 [Multi-domain]  Cd Length: 530  Bit Score: 149.09  E-value: 1.43e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214   5 FRAESHDTTRHLNEITAFDCEMSFVDTENDVMDVIEGLMKTILS--EARDSEEVKILNKEISI-PEKFP----RLCYDEC 77
Cdd:PLN02850  301 FRAEDSFTHRHLCEFTGLDLEMEIKEHYSEVLDVVDELFVAIFDglNERCKKELEAIREQYPFePLKYLpktlRLTFAEG 380

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214  78 LLYLNEKNITIEWGGDIDTKCERVLGEVVKDKFGSELFFITKYPLKIKPFYTAPenfDADD-KYSRAFDLEYKGVEISSG 156
Cdd:PLN02850  381 IQMLKEAGVEVDPLGDLNTESERKLGQLVKEKYGTDFYILHRYPLAVRPFYTMP---CPDDpKYSNSFDVFIRGEEIISG 457

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1309078214 157 GQRVHIHNLLAERIKRCNLNPENFKFYLDAF 187
Cdd:PLN02850  458 AQRVHDPELLEKRAEECGIDVKTISTYIDSF 488
asnC PRK03932
asparaginyl-tRNA synthetase; Validated
 5-185 4.07e-30

asparaginyl-tRNA synthetase; Validated


Pssm-ID: 235176 [Multi-domain]  Cd Length: 450  Bit Score: 114.05  E-value: 4.07e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214   5 FRAESHDTTRHLNEITAFDCEMSFVDTEnDVMDVIEGLMKTILSEARD--SEEVKILNKEIS----------IPEKFPRL 72
Cdd:PRK03932  217 FRAENSNTRRHLAEFWMIEPEMAFADLE-DNMDLAEEMLKYVVKYVLEncPDDLEFLNRRVDkgdierlenfIESPFPRI 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214  73 CYDECLLYLNEKNIT----IEWGGDIDTKCERVLGEVVKDKfgseLFFITKYPLKIKPFYTAPenfDADDKYSRAFDLEY 148
Cdd:PRK03932  296 TYTEAIEILQKSGKKfefpVEWGDDLGSEHERYLAEEHFKK----PVFVTNYPKDIKAFYMRL---NPDGKTVAAMDLLA 368

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1309078214 149 KGV-EISSGGQRVHIHNLLAERIKRCNLNPENFKFYLD 185
Cdd:PRK03932  369 PGIgEIIGGSQREERLDVLEARIKELGLNKEDYWWYLD 406
asnS TIGR00457
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ...
 5-185 1.33e-29

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: 112.86  E-value: 1.33e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214   5 FRAESHDTTRHLNEITAFDCEMSFVDTeNDVMDVIEGLMKTILSEARD--SEEVKILNKEISIPE----------KFPRL 72
Cdd:TIGR00457 220 FRAEKSNTSRHLSEFWMIEPEMAFANL-NDLLQLAETLIKYIIKAVLEncSQELKFLEKNFDKDLikrleniinnKFARI 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214  73 CYDECLLYLNEKNITIE----WGGDIDTKCERVLGEvvkdKFGSELFFITKYPLKIKPFYTAPenfDADDKYSRAFDLEY 148
Cdd:TIGR00457 299 TYTDAIEILKESDKNFEyedfWGDDLQTEHERFLAE----EYFKPPVFVTNYPKDIKAFYMKL---NDDGKTVAAMDLLA 371

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1309078214 149 KGV-EISSGGQRVHIHNLLAERIKRCNLNPENFKFYLD 185
Cdd:TIGR00457 372 PGIgEIIGGSEREDDLDKLENRMKEMGLDTDALNWYLD 409
Asp_Lys_Asn_RS_core cd00669
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ...
 5-187 9.81e-28

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: 104.87  E-value: 9.81e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214   5 FRAEsHDTTRHLNEITAFDCEMSFVDTEnDVMDVIEGLMKTILSEARDSEEVKILNKEISIPEKFPRLCYDECLlylnek 84
Cdd:cd00669    79 FRNE-DLRARHQPEFTMMDLEMAFADYE-DVIELTERLVRHLAREVLGVTAVTYGFELEDFGLPFPRLTYREAL------ 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214  85 nitiewggdidtkcervlgevvkDKFGsELFFITKYPLKIKPFYTAPenFDADDKYSRAFDLEYKGVEISSGGQRVHIHN 164
Cdd:cd00669   151 -----------------------ERYG-QPLFLTDYPAEMHSPLASP--HDVNPEIADAFDLFINGVEVGNGSSRLHDPD 204

                         170       180
                  ....*....|....*....|....*..
gi 1309078214 165 LLAERIKRCNLNPEN----FKFYLDAF 187
Cdd:cd00669   205 IQAEVFQEQGINKEAgmeyFEFYLKAL 231
PRK06462 PRK06462
asparagine synthetase A; Reviewed
 5-185 2.72e-25

asparagine synthetase A; Reviewed


Pssm-ID: 235808 [Multi-domain]  Cd Length: 335  Bit Score: 99.71  E-value: 2.72e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214   5 FRAES--HDTTRHLNEITAFDCEMSFVDTeNDVMDVIEGLMKTILSEARDSEEVKILNKEISIPE---KFPRLCYDECLL 79
Cdd:PRK06462  112 FRLEPvdKDTGRHLYEFTQLDIEIEGADL-DEVMDLIEDLIKYLVKELLEEHEDELEFFGRDLPHlkrPFKRITHKEAVE 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214  80 YLNEKNITIEWGGDIDTKCERVLGEVVKdkfgsELFFITKYPLKIKPFYTAPEnfDADDKYSRAFDLEY-KGV-EISSGG 157
Cdd:PRK06462  191 ILNEEGCRGIDLEELGSEGEKSLSEHFE-----EPFWIIDIPKGSREFYDRED--PERPGVLRNYDLLLpEGYgEAVSGG 263

                         170       180
                  ....*....|....*....|....*...
gi 1309078214 158 QRVHIHNLLAERIKRCNLNPENFKFYLD 185
Cdd:PRK06462  264 EREYEYEEIVERIREHGVDPEKYKWYLE 291
PTZ00401 PTZ00401
aspartyl-tRNA synthetase; Provisional
 5-187 1.31e-24

aspartyl-tRNA synthetase; Provisional


Pssm-ID: 173592 [Multi-domain]  Cd Length: 550  Bit Score: 99.68  E-value: 1.31e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214   5 FRAESHDTTRHLNEITAFDCEMSFVDTENDVMDVIEGLMKTILSE-ARDSEEVKILNKEISI--------PEKFP----- 70
Cdd:PTZ00401  289 FRSENSNTHRHLTEFVGLDVEMRINEHYYEVLDLAESLFNYIFERlATHTKELKAVCQQYPFeplvwkltPERMKelgvg 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214  71 ------------------------RLCYDECLLYLN----EKnitIEWGGDIDTKCERVLGEVVKDKFGSELFFITKYPL 122
Cdd:PTZ00401  369 visegveptdkyqarvhnmdsrmlRINYMHCIELLNtvleEK---MAPTDDINTTNEKLLGKLVKERYGTDFFISDRFPS 445

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1309078214 123 KIKPFYTAPenFDADDKYSRAFDLEYKGVEISSGGQRVHIHNLLAERIKRCNLNPENFKFYLDAF 187
Cdd:PTZ00401  446 SARPFYTME--CKDDERFTNSYDMFIRGEEISSGAQRIHDPDLLLARAKMLNVDLTPIKEYVDSF 508
PLN02603 PLN02603
asparaginyl-tRNA synthetase
 5-185 7.46e-17

asparaginyl-tRNA synthetase


Pssm-ID: 178213 [Multi-domain]  Cd Length: 565  Bit Score: 77.32  E-value: 7.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214   5 FRAESHDTTRHLNEITAFDCEMSFVDTENDV---MDVIEGLMKTILSEAR-DSE------EVKILNKEISIPEK-FPRLC 73
Cdd:PLN02603  331 FRAENSNTSRHLAEFWMIEPELAFADLNDDMacaTAYLQYVVKYILENCKeDMEffntwiEKGIIDRLSDVVEKnFVQLS 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214  74 YD---ECLLYLNEK-NITIEWGGDIDTKCERVLGEVVkdkFGSELFFITKYPLKIKPFYTAPENfdaDDKYSRAFDLEYK 149
Cdd:PLN02603  411 YTdaiELLLKAKKKfEFPVKWGLDLQSEHERYITEEA---FGGRPVIIRDYPKEIKAFYMREND---DGKTVAAMDMLVP 484

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1309078214 150 GV-EISSGGQRVHIHNLLAERIKRCNLNPENFKFYLD 185
Cdd:PLN02603  485 RVgELIGGSQREERLEYLEARLDELKLNKESYWWYLD 521
PLN02532 PLN02532
asparagine-tRNA synthetase
 5-185 2.70e-15

asparagine-tRNA synthetase


Pssm-ID: 215291 [Multi-domain]  Cd Length: 633  Bit Score: 72.98  E-value: 2.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214   5 FRAESHDTTRHLNEITAFDCEMSFVDTEnDVMDVIEG----LMKTILSEArdSEEVKILNKEI----------SIPEKFP 70
Cdd:PLN02532  399 FRADRIDSARHLAEMWMVEVEMAFSELE-DAMNCAEDyfkfLCKWVLENC--SEDMKFVSKRIdktistrleaIISSSLQ 475

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214  71 RLCYDECLLYLNEKNIT-----IEWGGDIDTKCERVLGevvkDKFGSELFFITKYPLKIKPFYTapeNFDADDKYSRAFD 145
Cdd:PLN02532  476 RISYTEAVDLLKQATDKkfetkPEWGIALTTEHLSYLA----DEIYKKPVIIYNYPKELKPFYV---RLNDDGKTVAAFD 548

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1309078214 146 LEY-KGVEISSGGQRVHIHNLLAERIKRCNLNPENFKFYLD 185
Cdd:PLN02532  549 LVVpKVGTVITGSQNEERMDILNARIEELGLPREQYEWYLD 589
PLN02221 PLN02221
asparaginyl-tRNA synthetase
 5-185 3.19e-15

asparaginyl-tRNA synthetase


Pssm-ID: 177867 [Multi-domain]  Cd Length: 572  Bit Score: 72.72  E-value: 3.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214   5 FRAESHDTTRHLNEITAFDCEMSFVDTENDvMDVIEGLMKT----ILSEARDSEE----------VKILNKEISIPekFP 70
Cdd:PLN02221  336 FRAENSHTSRHLAEFWMVEPEIAFADLEDD-MNCAEAYVKYmckwLLDKCFDDMElmaknfdsgcIDRLRMVASTP--FG 412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214  71 RLCYDECLLYLNEK-------NITIEWGGDIDTKCERVLGEVVKDKfgseLFFITKYPLKIKPFYTapeNFDADDKYSRA 143
Cdd:PLN02221  413 RITYTEAIELLEEAvakgkefDNNVEWGIDLASEHERYLTEVLFQK----PLIVYNYPKGIKAFYM---RLNDDEKTVAA 485

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1309078214 144 FDLEYKGV-EISSGGQRVHIHNLLAERIKRCNLNPENFKFYLD 185
Cdd:PLN02221  486 MDVLVPKVgELIGGSQREERYDVIKQRIEEMGLPIEPYEWYLD 528
AspS COG0173
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ...
 18-76 1.00e-10

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: 59.63  E-value: 1.00e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1309078214  18 EITAFDCEMSFVDtENDVMDVIEGLMKTILSEardseevkILNKEISIPekFPRLCYDE 76
Cdd:COG0173   232 EFTQLDIEMSFVD-QEDVFELMEGLIRHLFKE--------VLGVELPTP--FPRMTYAE 279
aspS PRK00476
aspartyl-tRNA synthetase; Validated
 18-76 1.99e-10

aspartyl-tRNA synthetase; Validated


Pssm-ID: 234775 [Multi-domain]  Cd Length: 588  Bit Score: 58.93  E-value: 1.99e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1309078214  18 EITAFDCEMSFVdTENDVMDVIEGLMKTILSEardseevkILNKEISIPekFPRLCYDE 76
Cdd:PRK00476  231 EFTQIDIEMSFV-TQEDVMALMEGLIRHVFKE--------VLGVDLPTP--FPRMTYAE 278
PTZ00425 PTZ00425
asparagine-tRNA ligase; Provisional
 5-183 3.20e-10

asparagine-tRNA ligase; Provisional


Pssm-ID: 240414 [Multi-domain]  Cd Length: 586  Bit Score: 58.11  E-value: 3.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214   5 FRAESHDTTRHLNEITAFDCEMSFVDTEnDVMDVIEGLMK----TILSEARDS---EEVKILNKEIS-----IPEKFPRL 72
Cdd:PTZ00425  353 FRAENSHTSRHLAEFWMIEPEIAFADLY-DNMELAESYIKycigYVLNNNFDDiyyFEENVETGLISrlkniLDEDFAKI 431

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214  73 CY----DECLLYLNEKNITIEWGGDIDTKCERVLGEVVKDKfgseLFFITKYPLKIKPFYTapeNFDADDKYSRAFD-LE 147
Cdd:PTZ00425  432 TYtnviDLLQPYSDSFEVPVKWGMDLQSEHERFVAEQIFKK----PVIVYNYPKDLKAFYM---KLNEDQKTVAAMDvLV 504

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1309078214 148 YKGVEISSGGQRVHIHNLLAERIKRCNLNPENFKFY 183
Cdd:PTZ00425  505 PKIGEVIGGSQREDNLERLDKMIKEKKLNMESYWWY 540
lysS PRK00484
lysyl-tRNA synthetase; Reviewed
 5-126 2.71e-03

lysyl-tRNA synthetase; Reviewed


Pssm-ID: 234778 [Multi-domain]  Cd Length: 491  Bit Score: 37.76  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078214   5 FRAESHDTtRHLNEITAFDCEMSFVDTeNDVMDVIEGLMKTILSEARDSEEVKILNKEISIPEKFPRLCYDECLLYLNEK 84
Cdd:PRK00484  250 FRNEGIDT-RHNPEFTMLEFYQAYADY-NDMMDLTEELIRHLAQAVLGTTKVTYQGTEIDFGPPFKRLTMVDAIKEYTGV 327

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1309078214  85 NITIEWGGDIDTKCERvLGEVVKDKFG-----SELF------------FITKYPLKIKP 126
Cdd:PRK00484  328 DFDDMTDEEARALAKE-LGIEVEKSWGlgkliNELFeefvepkliqptFITDYPVEISP 385
 
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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