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Conserved domains on  [gi|2734471020|ref|WP_346659893|]
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amino acid--tRNA ligase-related protein, partial [Bacillus subtilis]

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
 1-156 6.31e-99

asparaginyl-tRNA synthetase; Validated


The actual alignment was detected with superfamily member PRK03932:

Pssm-ID: 235176 [Multi-domain]  Cd Length: 450  Bit Score: 291.63  E-value: 6.31e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020   1 RISYDEAIELLQQSG-KFPD-VKWGEDFGSPEETYLAE-HFSKPVFVMNYPKAIKPFYMKPHPTrDDVVICADMLAPeGY 77
Cdd:PRK03932  294 RITYTEAIEILQKSGkKFEFpVEWGDDLGSEHERYLAEeHFKKPVFVTNYPKDIKAFYMRLNPD-GKTVAAMDLLAP-GI 371

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2734471020  78 GEIIGGSERATDPKYLEEQIIKAGLDIKDYEWYLDLRRYGSVPHSGFGLGLERAVTWITGEDHIREAIPFPRLLNRIYP 156
Cdd:PRK03932  372 GEIIGGSQREERLDVLEARIKELGLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
 
Name Accession Description Interval E-value
asnC PRK03932
asparaginyl-tRNA synthetase; Validated
 1-156 6.31e-99

asparaginyl-tRNA synthetase; Validated


Pssm-ID: 235176 [Multi-domain]  Cd Length: 450  Bit Score: 291.63  E-value: 6.31e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020   1 RISYDEAIELLQQSG-KFPD-VKWGEDFGSPEETYLAE-HFSKPVFVMNYPKAIKPFYMKPHPTrDDVVICADMLAPeGY 77
Cdd:PRK03932  294 RITYTEAIEILQKSGkKFEFpVEWGDDLGSEHERYLAEeHFKKPVFVTNYPKDIKAFYMRLNPD-GKTVAAMDLLAP-GI 371

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2734471020  78 GEIIGGSERATDPKYLEEQIIKAGLDIKDYEWYLDLRRYGSVPHSGFGLGLERAVTWITGEDHIREAIPFPRLLNRIYP 156
Cdd:PRK03932  372 GEIIGGSQREERLDVLEARIKELGLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
AsnS COG0017
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 1-156 4.14e-95

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: 281.17  E-value: 4.14e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020   1 RISYDEAIELLQQSGKfpDVKWGEDFGSPEETYLAE-HFSKPVFVMNYPKAIKPFYMKPHPTRDDVVICADMLAPeGYGE 79
Cdd:COG0017   277 RITYTEAIEILKKSGE--KVEWGDDLGTEHERYLGEeFFKKPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAP-GIGE 353

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2734471020  80 IIGGSERATDPKYLEEQIIKAGLDIKDYEWYLDLRRYGSVPHSGFGLGLERAVTWITGEDHIREAIPFPRLLNRIYP 156
Cdd:COG0017   354 IIGGSQREHRYDVLVERIKEKGLDPEDYEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
AsxRS_core cd00776
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ...
 1-149 6.37e-72

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: 218.59  E-value: 6.37e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020   1 RISYDEAIELLQQSGKFPDVKWGEDFGSPEETYLAEH-FSKPVFVMNYPKAIKPFYMKPHPTRDDVVICADMLAPeGYGE 79
Cdd:cd00776   171 RITYDEAIELLREKGVEEEVKWGEDLSTEHERLLGEIvKGDPVFVTDYPKEIKPFYMKPDDDNPETVESFDLLMP-GVGE 249

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020  80 IIGGSERATDPKYLEEQIIKAGLDIKDYEWYLDLRRYGSVPHSGFGLGLERAVTWITGEDHIREAIPFPR 149
Cdd:cd00776   250 IVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFPR 319
asnS TIGR00457
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ...
 1-156 8.79e-72

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: 222.26  E-value: 8.79e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020   1 RISYDEAIELLQQSGK---FPDvKWGEDFGSPEETYLAE-HFSKPVFVMNYPKAIKPFYMKPHpTRDDVVICADMLAPeG 76
Cdd:TIGR00457 297 RITYTDAIEILKESDKnfeYED-FWGDDLQTEHERFLAEeYFKPPVFVTNYPKDIKAFYMKLN-DDGKTVAAMDLLAP-G 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020  77 YGEIIGGSERATDPKYLEEQIIKAGLDIKDYEWYLDLRRYGSVPHSGFGLGLERAVTWITGEDHIREAIPFPRLLNRIYP 156
Cdd:TIGR00457 374 IGEIIGGSEREDDLDKLENRMKEMGLDTDALNWYLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGNINF 453
tRNA-synt_2 pfam00152
tRNA synthetases class II (D, K and N);
1-150 3.95e-42

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


Pssm-ID: 425487 [Multi-domain]  Cd Length: 318  Bit Score: 142.32  E-value: 3.95e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020   1 RISYDEAIELLQQSGkfpDVKWGEDFGSPEETYLAE-----HFSKPVFVMNYPKAIKPFYMKPHPTRDDVVICADMLAPe 75
Cdd:pfam00152 164 RITYAEAIEKLNGKD---VEELGYGSDKPDLRFLLElvidkNKFNPLWVTDFPAEHHPFTMPKDEDDPALAEAFDLVLN- 239

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2734471020  76 GYgEIIGGSERATDPKYLEEQIIKAGLD----IKDYEWYLDLRRYGSVPHSGFGLGLERAVTWITGEDHIREAIPFPRL 150
Cdd:pfam00152 240 GV-EIGGGSIRIHDPELQEERFEEQGLDpeeaEEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAFPKT 317
 
Name Accession Description Interval E-value
asnC PRK03932
asparaginyl-tRNA synthetase; Validated
 1-156 6.31e-99

asparaginyl-tRNA synthetase; Validated


Pssm-ID: 235176 [Multi-domain]  Cd Length: 450  Bit Score: 291.63  E-value: 6.31e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020   1 RISYDEAIELLQQSG-KFPD-VKWGEDFGSPEETYLAE-HFSKPVFVMNYPKAIKPFYMKPHPTrDDVVICADMLAPeGY 77
Cdd:PRK03932  294 RITYTEAIEILQKSGkKFEFpVEWGDDLGSEHERYLAEeHFKKPVFVTNYPKDIKAFYMRLNPD-GKTVAAMDLLAP-GI 371

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2734471020  78 GEIIGGSERATDPKYLEEQIIKAGLDIKDYEWYLDLRRYGSVPHSGFGLGLERAVTWITGEDHIREAIPFPRLLNRIYP 156
Cdd:PRK03932  372 GEIIGGSQREERLDVLEARIKELGLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
AsnS COG0017
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 1-156 4.14e-95

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: 281.17  E-value: 4.14e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020   1 RISYDEAIELLQQSGKfpDVKWGEDFGSPEETYLAE-HFSKPVFVMNYPKAIKPFYMKPHPTRDDVVICADMLAPeGYGE 79
Cdd:COG0017   277 RITYTEAIEILKKSGE--KVEWGDDLGTEHERYLGEeFFKKPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAP-GIGE 353

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2734471020  80 IIGGSERATDPKYLEEQIIKAGLDIKDYEWYLDLRRYGSVPHSGFGLGLERAVTWITGEDHIREAIPFPRLLNRIYP 156
Cdd:COG0017   354 IIGGSQREHRYDVLVERIKEKGLDPEDYEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
AsxRS_core cd00776
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ...
 1-149 6.37e-72

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: 218.59  E-value: 6.37e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020   1 RISYDEAIELLQQSGKFPDVKWGEDFGSPEETYLAEH-FSKPVFVMNYPKAIKPFYMKPHPTRDDVVICADMLAPeGYGE 79
Cdd:cd00776   171 RITYDEAIELLREKGVEEEVKWGEDLSTEHERLLGEIvKGDPVFVTDYPKEIKPFYMKPDDDNPETVESFDLLMP-GVGE 249

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020  80 IIGGSERATDPKYLEEQIIKAGLDIKDYEWYLDLRRYGSVPHSGFGLGLERAVTWITGEDHIREAIPFPR 149
Cdd:cd00776   250 IVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFPR 319
asnS TIGR00457
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ...
 1-156 8.79e-72

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: 222.26  E-value: 8.79e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020   1 RISYDEAIELLQQSGK---FPDvKWGEDFGSPEETYLAE-HFSKPVFVMNYPKAIKPFYMKPHpTRDDVVICADMLAPeG 76
Cdd:TIGR00457 297 RITYTDAIEILKESDKnfeYED-FWGDDLQTEHERFLAEeYFKPPVFVTNYPKDIKAFYMKLN-DDGKTVAAMDLLAP-G 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020  77 YGEIIGGSERATDPKYLEEQIIKAGLDIKDYEWYLDLRRYGSVPHSGFGLGLERAVTWITGEDHIREAIPFPRLLNRIYP 156
Cdd:TIGR00457 374 IGEIIGGSEREDDLDKLENRMKEMGLDTDALNWYLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGNINF 453
PLN02221 PLN02221
asparaginyl-tRNA synthetase
 1-156 3.90e-47

asparaginyl-tRNA synthetase


Pssm-ID: 177867 [Multi-domain]  Cd Length: 572  Bit Score: 160.54  E-value: 3.90e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020   1 RISYDEAIELLQQS---GKFPD--VKWGEDFGSPEETYLAEH-FSKPVFVMNYPKAIKPFYMKphpTRDD--VVICADML 72
Cdd:PLN02221  413 RITYTEAIELLEEAvakGKEFDnnVEWGIDLASEHERYLTEVlFQKPLIVYNYPKGIKAFYMR---LNDDekTVAAMDVL 489

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020  73 APEgYGEIIGGSERATDPKYLEEQIIKAGLDIKDYEWYLDLRRYGSVPHSGFGLGLERAVTWITGEDHIREAIPFPRlln 152
Cdd:PLN02221  490 VPK-VGELIGGSQREERYDVIKQRIEEMGLPIEPYEWYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPR--- 565


                  ....
gi 2734471020 153 riYP 156
Cdd:PLN02221  566 --YP 567
PLN02603 PLN02603
asparaginyl-tRNA synthetase
 1-150 1.42e-46

asparaginyl-tRNA synthetase


Pssm-ID: 178213 [Multi-domain]  Cd Length: 565  Bit Score: 158.98  E-value: 1.42e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020   1 RISYDEAIELLQQSGK---FPdVKWGEDFGSPEETYLAEHF--SKPVFVMNYPKAIKPFYMKPHptrDD--VVICADMLA 73
Cdd:PLN02603  408 QLSYTDAIELLLKAKKkfeFP-VKWGLDLQSEHERYITEEAfgGRPVIIRDYPKEIKAFYMREN---DDgkTVAAMDMLV 483

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2734471020  74 PEgYGEIIGGSERATDPKYLEEQIIKAGLDIKDYEWYLDLRRYGSVPHSGFGLGLERAVTWITGEDHIREAIPFPRL 150
Cdd:PLN02603  484 PR-VGELIGGSQREERLEYLEARLDELKLNKESYWWYLDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFPRV 559
PRK06462 PRK06462
asparagine synthetase A; Reviewed
 1-149 1.15e-44

asparagine synthetase A; Reviewed


Pssm-ID: 235808 [Multi-domain]  Cd Length: 335  Bit Score: 149.40  E-value: 1.15e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020   1 RISYDEAIELLQQSGKFPDVKwgEDFGSPEETYLAEHFSKPVFVMNYPKAIKPFYMKPHPTRDDVVICADMLAPEGYGEI 80
Cdd:PRK06462  182 RITHKEAVEILNEEGCRGIDL--EELGSEGEKSLSEHFEEPFWIIDIPKGSREFYDREDPERPGVLRNYDLLLPEGYGEA 259

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2734471020  81 IGGSERATDPKYLEEQIIKAGLDIKDYEWYLDLRRYGSVPHSGFGLGLERAVTWITGEDHIREAIPFPR 149
Cdd:PRK06462  260 VSGGEREYEYEEIVERIREHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQPFPR 328
PTZ00425 PTZ00425
asparagine-tRNA ligase; Provisional
 1-156 2.66e-42

asparagine-tRNA ligase; Provisional


Pssm-ID: 240414 [Multi-domain]  Cd Length: 586  Bit Score: 147.86  E-value: 2.66e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020   1 RISYDEAIELLQQ-SGKFP-DVKWGEDFGSPEETYLAEH-FSKPVFVMNYPKAIKPFYMKPHPTRDDVViCADMLAPEgY 77
Cdd:PTZ00425  430 KITYTNVIDLLQPySDSFEvPVKWGMDLQSEHERFVAEQiFKKPVIVYNYPKDLKAFYMKLNEDQKTVA-AMDVLVPK-I 507

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2734471020  78 GEIIGGSERATDPKYLEEQIIKAGLDIKDYEWYLDLRRYGSVPHSGFGLGLERAVTWITGEDHIREAIPFPRllnriYP 156
Cdd:PTZ00425  508 GEVIGGSQREDNLERLDKMIKEKKLNMESYWWYRQLRKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFPR-----YP 581
tRNA-synt_2 pfam00152
tRNA synthetases class II (D, K and N);
1-150 3.95e-42

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


Pssm-ID: 425487 [Multi-domain]  Cd Length: 318  Bit Score: 142.32  E-value: 3.95e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020   1 RISYDEAIELLQQSGkfpDVKWGEDFGSPEETYLAE-----HFSKPVFVMNYPKAIKPFYMKPHPTRDDVVICADMLAPe 75
Cdd:pfam00152 164 RITYAEAIEKLNGKD---VEELGYGSDKPDLRFLLElvidkNKFNPLWVTDFPAEHHPFTMPKDEDDPALAEAFDLVLN- 239

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2734471020  76 GYgEIIGGSERATDPKYLEEQIIKAGLD----IKDYEWYLDLRRYGSVPHSGFGLGLERAVTWITGEDHIREAIPFPRL 150
Cdd:pfam00152 240 GV-EIGGGSIRIHDPELQEERFEEQGLDpeeaEEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAFPKT 317
aspC PRK05159
aspartyl-tRNA synthetase; Provisional
 1-156 1.13e-41

aspartyl-tRNA synthetase; Provisional


Pssm-ID: 235354 [Multi-domain]  Cd Length: 437  Bit Score: 143.79  E-value: 1.13e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020   1 RISYDEAIELLQQSGKfpDVKWGEDFGSPEETYLAEHF-----SKPVFVMNYPKAIKPFYMKPHPtrDDVVICA--DMLA 73
Cdd:PRK05159  281 RITYDEAIEILKSKGN--EISWGDDLDTEGERLLGEYVkeeygSDFYFITDYPSEKRPFYTMPDE--DDPEISKsfDLLF 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020  74 PEGygEIIGGSERATDPKYLEEQIIKAGLDIKDYEWYLDLRRYGSVPHSGFGLGLERAVTWITGEDHIREAIPFPRLLNR 153
Cdd:PRK05159  357 RGL--EITSGGQRIHRYDMLVESIKEKGLNPESFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFPRDRHR 434


                  ...
gi 2734471020 154 IYP 156
Cdd:PRK05159  435 LTP 437
PLN02532 PLN02532
asparagine-tRNA synthetase
 1-149 6.51e-38

asparagine-tRNA synthetase


Pssm-ID: 215291 [Multi-domain]  Cd Length: 633  Bit Score: 136.15  E-value: 6.51e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020   1 RISYDEAIELLQQ--SGKFP-DVKWGEDFGSPEETYLAEHFSK-PVFVMNYPKAIKPFYMKphpTRDD--VVICADMLAP 74
Cdd:PLN02532  476 RISYTEAVDLLKQatDKKFEtKPEWGIALTTEHLSYLADEIYKkPVIIYNYPKELKPFYVR---LNDDgkTVAAFDLVVP 552

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2734471020  75 EGyGEIIGGSERATDPKYLEEQIIKAGLDIKDYEWYLDLRRYGSVPHSGFGLGLERAVTWITGEDHIREAIPFPR 149
Cdd:PLN02532  553 KV-GTVITGSQNEERMDILNARIEELGLPREQYEWYLDLRRHGTVKHSGFSLGFELMVLFATGLPDVRDAIPFPR 626
aspS_nondisc TIGR00458
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ...
 1-156 3.11e-28

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: 107.60  E-value: 3.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020   1 RISYDEAIELLQQSGKfpDVKWGEDFGSPEETYLAEHFSKPVFVMNYPKAIKPFYMKPHPTRDDVVICADMLapEGYGEI 80
Cdd:TIGR00458 277 RLTYDEAIEMANAKGV--EIGWGEDLSTEAEKALGEEMDGLYFITDWPTEIRPFYTMPDEDNPEISKSFDLM--YRDLEI 352

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2734471020  81 IGGSERATDPKYLEEQIIKAGLDIKDYEWYLDLRRYGSVPHSGFGLGLERAVTWITGEDHIREAIPFPRLLNRIYP 156
Cdd:TIGR00458 353 SSGAQRIHLHDLLVERIKAKGLNPEGFKDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFPRDRKRLTP 428
PLN02850 PLN02850
aspartate-tRNA ligase
 1-156 1.19e-26

aspartate-tRNA ligase


Pssm-ID: 215456 [Multi-domain]  Cd Length: 530  Bit Score: 104.02  E-value: 1.19e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020   1 RISYDEAIELLQQSGkfPDVKWGEDFGSPEETYLA----EHFSKPVFVMN-YPKAIKPFYMKPHPTRD------DVVICA 69
Cdd:PLN02850  374 RLTFAEGIQMLKEAG--VEVDPLGDLNTESERKLGqlvkEKYGTDFYILHrYPLAVRPFYTMPCPDDPkysnsfDVFIRG 451

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020  70 DmlapegygEIIGGSERATDPKYLEEQIIKAGLDIKDYEWYLDLRRYGSVPHSGFGLGLERAVTWITGEDHIREAIPFPR 149
Cdd:PLN02850  452 E--------EIISGAQRVHDPELLEKRAEECGIDVKTISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPR 523


                  ....*..
gi 2734471020 150 LLNRIYP 156
Cdd:PLN02850  524 DPQRLAP 530
Asp_Lys_Asn_RS_core cd00669
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ...
 36-149 1.36e-16

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: 74.05  E-value: 1.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020  36 EHFSKPVFVMNYPKAIKPFYMKPHPTRDDVVICADMLApEGYgEIIGGSERATDPKYLEEQIIKAGLD----IKDYEWYL 111
Cdd:cd00669   151 ERYGQPLFLTDYPAEMHSPLASPHDVNPEIADAFDLFI-NGV-EVGNGSSRLHDPDIQAEVFQEQGINkeagMEYFEFYL 228

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2734471020 112 DLRRYGSVPHSGFGLGLERAVTWITGEDHIREAIPFPR 149
Cdd:cd00669   229 KALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPK 266
PTZ00401 PTZ00401
aspartyl-tRNA synthetase; Provisional
 1-156 3.50e-14

aspartyl-tRNA synthetase; Provisional


Pssm-ID: 173592 [Multi-domain]  Cd Length: 550  Bit Score: 68.48  E-value: 3.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020   1 RISYDEAIELLQQSGKfPDVKWGEDFGSPEETYLA----EHFSKPVFVMN-YPKAIKPFYMKPHPTRDDVVICADMLApE 75
Cdd:PTZ00401  393 RINYMHCIELLNTVLE-EKMAPTDDINTTNEKLLGklvkERYGTDFFISDrFPSSARPFYTMECKDDERFTNSYDMFI-R 470

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020  76 GYgEIIGGSERATDPKYLEEQIIKAGLDIKDYEWYLDLRRYGSVPHSGFGLGLERAVTWITGEDHIREAIPFPRLLNRIY 155
Cdd:PTZ00401  471 GE-EISSGAQRIHDPDLLLARAKMLNVDLTPIKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFPRDPQRTT 549


                  .
gi 2734471020 156 P 156
Cdd:PTZ00401  550 P 550
PLN02502 PLN02502
lysyl-tRNA synthetase
 31-150 3.88e-08

lysyl-tRNA synthetase


Pssm-ID: 215278 [Multi-domain]  Cd Length: 553  Bit Score: 51.14  E-value: 3.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020  31 ETYLAEHFSKPVFVMNYPKAIKPFyMKPHPTRDDVV------ICADMLApEGYGEIiggseraTDP----KYLEEQIiKA 100
Cdd:PLN02502  425 EEFLEETLVQPTFVLDHPVEMSPL-AKPHRSKPGLTerfelfINGRELA-NAFSEL-------TDPvdqrERFEEQV-KQ 494

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2734471020 101 GLDIKDYEWYLD------LRrYGSVPHSGFGLGLERAVTWITGEDHIREAIPFPRL 150
Cdd:PLN02502  495 HNAGDDEAMALDedfctaLE-YGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFPAM 549
PTZ00385 PTZ00385
lysyl-tRNA synthetase; Provisional
 2-150 5.64e-07

lysyl-tRNA synthetase; Provisional


Pssm-ID: 185588 [Multi-domain]  Cd Length: 659  Bit Score: 47.72  E-value: 5.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020   2 ISYDEAIeLLQQSGKFPDVKWGED-FGSPEETYLAEHFSKPVFVMNYPKAIKPFyMKPHPTRDDVVicadmlapEGYGEI 80
Cdd:PTZ00385  409 IAYMSVV-MLRYNIPLPPVRTAAKmFEKLIDFFITDRVVEPTFVMDHPLFMSPL-AKEQVSRPGLA--------ERFELF 478

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020  81 IGGSE------RATDP-----KYLEEQIIKAGLDIKDY---EWYLDLRRYGSVPHSGFGLGLERAVTWITGEDHIREAIP 146
Cdd:PTZ00385  479 VNGIEycnaysELNDPheqyhRFQQQLVDRQGGDEEAMpldETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGII 558


                  ....
gi 2734471020 147 FPRL 150
Cdd:PTZ00385  559 FPLL 562
LysRS_core cd00775
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ...
 31-150 6.04e-07

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: 47.58  E-value: 6.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020  31 ETYLAEHFSKPVFVMNYPKAIKPFyMKPHPTRDDVVicadmlapEGYGEIIGGSERA------TDP-----KYLEEQIIK 99
Cdd:cd00775   203 EEFVEPTLIQPTFIIDHPVEISPL-AKRHRSNPGLT--------ERFELFICGKEIAnaytelNDPfdqreRFEEQAKQK 273

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2734471020 100 AGLD----IKDYEwYLDLRRYGSVPHSGFGLGLERAVTWITGEDHIREAIPFPRL 150
Cdd:cd00775   274 EAGDdeamMMDED-FVTALEYGMPPTGGLGIGIDRLVMLLTDSNSIRDVILFPAM 327
lysS PRK00484
lysyl-tRNA synthetase; Reviewed
 1-148 6.40e-07

lysyl-tRNA synthetase; Reviewed


Pssm-ID: 234778 [Multi-domain]  Cd Length: 491  Bit Score: 47.39  E-value: 6.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020   1 RISYDEAIELLQQSGKFPDVKWG------EDFgspeETYLAEHFSKPVFVMNYPKAIKPFyMKPHPTRDDVVicadmlap 74
Cdd:PRK00484  331 DMTDEEARALAKELGIEVEKSWGlgklinELF----EEFVEPKLIQPTFITDYPVEISPL-AKRHREDPGLT-------- 397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020  75 egygE----IIGGSERAT------DP----KYLEEQIIK--AGLD---IKDYEwYLDLRRYGSVPHSGFGLGLERAVTWI 135
Cdd:PRK00484  398 ----ErfelFIGGREIANafselnDPidqrERFEAQVEAkeAGDDeamFMDED-FLRALEYGMPPTGGLGIGIDRLVMLL 472

                         170
                  ....*....|...
gi 2734471020 136 TGEDHIREAIPFP 148
Cdd:PRK00484  473 TDSPSIRDVILFP 485
aspS PRK00476
aspartyl-tRNA synthetase; Validated
 76-148 7.27e-07

aspartyl-tRNA synthetase; Validated


Pssm-ID: 234775 [Multi-domain]  Cd Length: 588  Bit Score: 47.37  E-value: 7.27e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2734471020  76 GYgEIIGGSERATDPKyLEEQIIKA-GLDIKDYE----WYLDLRRYGSVPHSGFGLGLERAVTWITGEDHIREAIPFP 148
Cdd:PRK00476  481 GY-ELGGGSIRIHRPE-IQEKVFEIlGISEEEAEekfgFLLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
PRK12820 PRK12820
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ...
 78-149 1.90e-06

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


Pssm-ID: 105955 [Multi-domain]  Cd Length: 706  Bit Score: 46.52  E-value: 1.90e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2734471020  78 GEIIGGSERATDPKYLEEQIIKA-GL---DIKD-YEWYLDLRRYGSVPHSGFGLGLERAVTWITGEDHIREAIPFPR 149
Cdd:PRK12820  497 GEELGGGSIRINDKDIQLRIFAAlGLseeDIEDkFGFFLRAFDFAAPPHGGIALGLDRVVSMILQTPSIREVIAFPK 573
AspS COG0173
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ...
 76-148 3.71e-06

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: 45.37  E-value: 3.71e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2734471020  76 GYgEIIGGSERATDPKyLEEQIIKA-GLDIKDYE----WYLDLRRYGSVPHSGFGLGLERAVTWITGEDHIREAIPFP 148
Cdd:COG0173   480 GY-ELGGGSIRIHDPE-LQEKVFELlGISEEEAEekfgFLLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
lysS PRK02983
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
41-148 1.35e-05

bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;


Pssm-ID: 235095 [Multi-domain]  Cd Length: 1094  Bit Score: 43.80  E-value: 1.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020   41 PVFVMNYPKAIKPFYMkPHPT------RDDVVICADMLApEGYGEIiggseraTDP----KYLEEQIIKAG--------L 102
Cdd:PRK02983   977 PTFYTDFPTSVSPLTR-PHRSdpglaeRWDLVAWGVELG-TAYSEL-------TDPveqrRRLTEQSLLAAggdpeameL 1047

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2734471020  103 DikdyEWYLDLRRYGSVPHSGFGLGLERAVTWITGEDhIREAIPFP 148
Cdd:PRK02983  1048 D----EDFLQALEYAMPPTGGLGMGVDRLVMLLTGRS-IRETLPFP 1088
PTZ00417 PTZ00417
lysine-tRNA ligase; Provisional
 34-150 6.35e-05

lysine-tRNA ligase; Provisional


Pssm-ID: 173607 [Multi-domain]  Cd Length: 585  Bit Score: 41.92  E-value: 6.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020  34 LAEHF------SKPVFVMNYPKAIKPF--YMKPHP---TRDDVVICADmlapegygEIIGGSERATDPkYLEEQIIKAgl 102
Cdd:PTZ00417  454 LASHFienkypNKPFFIIEHPQIMSPLakYHRSKPgltERLEMFICGK--------EVLNAYTELNDP-FKQKECFSA-- 522

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2734471020 103 DIKDYE-----------WYLDLRRYGSVPHSGFGLGLERAVTWITGEDHIREAIPFPRL 150
Cdd:PTZ00417  523 QQKDREkgdaeafqfdaAFCTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFPTM 581
PLN02903 PLN02903
aminoacyl-tRNA ligase
 78-149 2.24e-04

aminoacyl-tRNA ligase


Pssm-ID: 215490 [Multi-domain]  Cd Length: 652  Bit Score: 40.16  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020  78 GEIIGGS----ERATDPKYLEeqIIkaGLDIKDYE----WYLDLRRYGSVPHSGFGLGLERAVTWITGEDHIREAIPFPR 149
Cdd:PLN02903  545 VEIGGGSlriyRRDVQQKVLE--AI--GLSPEEAEskfgYLLEALDMGAPPHGGIAYGLDRLVMLLAGAKSIRDVIAFPK 620
PRK12445 PRK12445
lysyl-tRNA synthetase; Reviewed
 3-150 7.05e-04

lysyl-tRNA synthetase; Reviewed


Pssm-ID: 171504 [Multi-domain]  Cd Length: 505  Bit Score: 38.89  E-value: 7.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020   3 SYDEAIELLQQSGKFPDVKWG------EDFGSPEETylaeHFSKPVFVMNYPKAIKPFYMK----PHPTRDDVVICADML 72
Cdd:PRK12445  347 NFDAAKALAESIGITVEKSWGlgrivtEIFDEVAEA----HLIQPTFITEYPAEVSPLARRndvnPEITDRFEFFIGGRE 422

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734471020  73 APEGYGEIIGGSERATdpKYLEEQIIKAGLDIKDY---EWYLDLRRYGSVPHSGFGLGLERAVTWITGEDHIREAIPFPR 149
Cdd:PRK12445  423 IGNGFSELNDAEDQAE--RFQEQVNAKAAGDDEAMfydEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFPA 500


                  .
gi 2734471020 150 L 150
Cdd:PRK12445  501 M 501
 
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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