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Conserved domains on  [gi|12851415|dbj|BAB29032|]
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unnamed protein product, partial [Mus musculus]

Protein Classification

class-II aminoacyl-tRNA synthetase family protein( domain architecture ID 1270)

class-II aminoacyl-tRNA synthetase family protein contains a class II tRNA amino-acyl synthetase-like catalytic core domain

PubMed:  8274143|10447505
SCOP:  4001782

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
class_II_aaRS-like_core super family cl00268
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
 2-247 2.22e-111

Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.


The actual alignment was detected with superfamily member cd00776:

Pssm-ID: 444800 [Multi-domain]  Cd Length: 322  Bit Score: 322.98  E-value: 2.22e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415   2 SSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFL-TFEDLLNRLEDLVCDVVDRVLKSPVASI--VY 78
Cdd:cd00776  77 SPQLYKEMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAKELelVN 156

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415  79 ELNPNFKPPKRPFRRMNYSDAIEWLKEHDVKKEDgtfyEFGDDIPEAPERLMTDTI-NEPILLCRFPVEIKSFYMQRCPE 157
Cdd:cd00776 157 QLNRELLKPLEPFPRITYDEAIELLREKGVEEEV----KWGEDLSTEHERLLGEIVkGDPVFVTDYPKEIKPFYMKPDDD 232

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415 158 DPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIR 237
Cdd:cd00776 233 NPETVESFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIR 312

                       250
                ....*....|
gi 12851415 238 DVCLYPRFLQ 247
Cdd:cd00776 313 EAILFPRDPK 322
 
Name Accession Description Interval E-value
AsxRS_core cd00776
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ...
 2-247 2.22e-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: 322.98  E-value: 2.22e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415   2 SSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFL-TFEDLLNRLEDLVCDVVDRVLKSPVASI--VY 78
Cdd:cd00776  77 SPQLYKEMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAKELelVN 156

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415  79 ELNPNFKPPKRPFRRMNYSDAIEWLKEHDVKKEDgtfyEFGDDIPEAPERLMTDTI-NEPILLCRFPVEIKSFYMQRCPE 157
Cdd:cd00776 157 QLNRELLKPLEPFPRITYDEAIELLREKGVEEEV----KWGEDLSTEHERLLGEIVkGDPVFVTDYPKEIKPFYMKPDDD 232

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415 158 DPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIR 237
Cdd:cd00776 233 NPETVESFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIR 312

                       250
                ....*....|
gi 12851415 238 DVCLYPRFLQ 247
Cdd:cd00776 313 EAILFPRDPK 322
asnS TIGR00457
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ...
 2-251 2.51e-96

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: 289.28  E-value: 2.51e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415     2 SSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSpVASIVYELN 81
Cdd:TIGR00457 198 SGQLYLETYALALSKVYTFGPTFRAEKSNTSRHLSEFWMIEPEMAFANLNDLLQLAETLIKYIIKAVLEN-CSQELKFLE 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415    82 PNFKPPKRP---------FRRMNYSDAIEWLKEHDVKKEDGTFyeFGDDIPEAPERLMTDTI-NEPILLCRFPVEIKSFY 151
Cdd:TIGR00457 277 KNFDKDLIKrleniinnkFARITYTDAIEILKESDKNFEYEDF--WGDDLQTEHERFLAEEYfKPPVFVTNYPKDIKAFY 354

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415   152 MQRCpEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWIL 231
Cdd:TIGR00457 355 MKLN-DDGKTVAAMDLLAPGIGEIIGGSEREDDLDKLENRMKEMGLDTDALNWYLDLRKYGSVPHSGFGLGFERLLAYIT 433

                         250       260
                  ....*....|....*....|
gi 12851415   232 NRYHIRDVCLYPRFLQRCRP 251
Cdd:TIGR00457 434 GLENIRDAIPFPRTPGNINF 453
AsnS COG0017
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 2-251 4.33e-87

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: 264.99  E-value: 4.33e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415   2 SSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPVASI-VYEL 80
Cdd:COG0017 183 SGQLYKEALAMALEKVYTFGPTFRAEKSNTRRHLAEFWMIEPEMAFADLEDVMDLAEEMLKYIIKYVLENCPEELeFLGR 262

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415  81 NPNF--KPPKRPFRRMNYSDAIEWLKEHDVKkedgtfYEFGDDI-PEApERLMTDTI-NEPILLCRFPVEIKSFYMQRCP 156
Cdd:COG0017 263 DVERleKVPESPFPRITYTEAIEILKKSGEK------VEWGDDLgTEH-ERYLGEEFfKKPVFVTDYPKEIKAFYMKPNP 335

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415 157 EDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHI 236
Cdd:COG0017 336 DDPKTVAAFDLLAPGIGEIIGGSQREHRYDVLVERIKEKGLDPEDYEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENI 415

                       250
                ....*....|....*
gi 12851415 237 RDVCLYPRFLQRCRP 251
Cdd:COG0017 416 REVIPFPRDPGRLTP 430
tRNA-synt_2 pfam00152
tRNA synthetases class II (D, K and N);
2-244 7.67e-76

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


Pssm-ID: 425487 [Multi-domain]  Cd Length: 318  Bit Score: 232.46  E-value: 7.67e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415     2 SSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHLaEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPVasivYEL 80
Cdd:pfam00152  77 SPQLYKQLLMVAgFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAK----ELE 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415    81 NPNFKPPKRPFRRMNYSDAIEWLKEHDVkkedgtfYEFGDDIPEAPERLMTD-----TINEPILLCRFPVEIKSFYMQRC 155
Cdd:pfam00152 152 GGTLLDLKKPFPRITYAEAIEKLNGKDV-------EELGYGSDKPDLRFLLElvidkNKFNPLWVTDFPAEHHPFTMPKD 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415   156 PEDPRLTESVDVLMPNVgEIVGGSMRSWDSEEILEGYKREGIDP----APYYWYTDQRKYGTCPHGGYGLGLERFLSWIL 231
Cdd:pfam00152 225 EDDPALAEAFDLVLNGV-EIGGGSIRIHDPELQEERFEEQGLDPeeaeEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLT 303

                         250
                  ....*....|...
gi 12851415   232 NRYHIRDVCLYPR 244
Cdd:pfam00152 304 GLESIREVIAFPK 316
asnC PRK03932
asparaginyl-tRNA synthetase; Validated
 2-251 7.48e-73

asparaginyl-tRNA synthetase; Validated


Pssm-ID: 235176 [Multi-domain]  Cd Length: 450  Bit Score: 228.84  E-value: 7.48e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415    2 SSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVL-----------K 70
Cdd:PRK03932 195 SGQLYAEAYAMALGKVYTFGPTFRAENSNTRRHLAEFWMIEPEMAFADLEDNMDLAEEMLKYVVKYVLencpddleflnR 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415   71 SPVASIVYELNpNFKPPkrPFRRMNYSDAIEWLKEHDVKKEDGTfyEFGDDI--PEapERLMTDTINE-PILLCRFPVEI 147
Cdd:PRK03932 275 RVDKGDIERLE-NFIES--PFPRITYTEAIEILQKSGKKFEFPV--EWGDDLgsEH--ERYLAEEHFKkPVFVTNYPKDI 347

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415  148 KSFYMQRCPEDpRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFL 227
Cdd:PRK03932 348 KAFYMRLNPDG-KTVAAMDLLAPGIGEIIGGSQREERLDVLEARIKELGLNKEDYWWYLDLRRYGSVPHSGFGLGFERLV 426

                        250       260
                 ....*....|....*....|....
gi 12851415  228 SWILNRYHIRDVCLYPRFLQRCRP 251
Cdd:PRK03932 427 AYITGLDNIRDVIPFPRTPGRAEF 450
 
Name Accession Description Interval E-value
AsxRS_core cd00776
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ...
 2-247 2.22e-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: 322.98  E-value: 2.22e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415   2 SSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFL-TFEDLLNRLEDLVCDVVDRVLKSPVASI--VY 78
Cdd:cd00776  77 SPQLYKEMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAKELelVN 156

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415  79 ELNPNFKPPKRPFRRMNYSDAIEWLKEHDVKKEDgtfyEFGDDIPEAPERLMTDTI-NEPILLCRFPVEIKSFYMQRCPE 157
Cdd:cd00776 157 QLNRELLKPLEPFPRITYDEAIELLREKGVEEEV----KWGEDLSTEHERLLGEIVkGDPVFVTDYPKEIKPFYMKPDDD 232

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415 158 DPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIR 237
Cdd:cd00776 233 NPETVESFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIR 312

                       250
                ....*....|
gi 12851415 238 DVCLYPRFLQ 247
Cdd:cd00776 313 EAILFPRDPK 322
asnS TIGR00457
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ...
 2-251 2.51e-96

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: 289.28  E-value: 2.51e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415     2 SSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSpVASIVYELN 81
Cdd:TIGR00457 198 SGQLYLETYALALSKVYTFGPTFRAEKSNTSRHLSEFWMIEPEMAFANLNDLLQLAETLIKYIIKAVLEN-CSQELKFLE 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415    82 PNFKPPKRP---------FRRMNYSDAIEWLKEHDVKKEDGTFyeFGDDIPEAPERLMTDTI-NEPILLCRFPVEIKSFY 151
Cdd:TIGR00457 277 KNFDKDLIKrleniinnkFARITYTDAIEILKESDKNFEYEDF--WGDDLQTEHERFLAEEYfKPPVFVTNYPKDIKAFY 354

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415   152 MQRCpEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWIL 231
Cdd:TIGR00457 355 MKLN-DDGKTVAAMDLLAPGIGEIIGGSEREDDLDKLENRMKEMGLDTDALNWYLDLRKYGSVPHSGFGLGFERLLAYIT 433

                         250       260
                  ....*....|....*....|
gi 12851415   232 NRYHIRDVCLYPRFLQRCRP 251
Cdd:TIGR00457 434 GLENIRDAIPFPRTPGNINF 453
AsnS COG0017
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 2-251 4.33e-87

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: 264.99  E-value: 4.33e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415   2 SSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPVASI-VYEL 80
Cdd:COG0017 183 SGQLYKEALAMALEKVYTFGPTFRAEKSNTRRHLAEFWMIEPEMAFADLEDVMDLAEEMLKYIIKYVLENCPEELeFLGR 262

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415  81 NPNF--KPPKRPFRRMNYSDAIEWLKEHDVKkedgtfYEFGDDI-PEApERLMTDTI-NEPILLCRFPVEIKSFYMQRCP 156
Cdd:COG0017 263 DVERleKVPESPFPRITYTEAIEILKKSGEK------VEWGDDLgTEH-ERYLGEEFfKKPVFVTDYPKEIKAFYMKPNP 335

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415 157 EDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHI 236
Cdd:COG0017 336 DDPKTVAAFDLLAPGIGEIIGGSQREHRYDVLVERIKEKGLDPEDYEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENI 415

                       250
                ....*....|....*
gi 12851415 237 RDVCLYPRFLQRCRP 251
Cdd:COG0017 416 REVIPFPRDPGRLTP 430
tRNA-synt_2 pfam00152
tRNA synthetases class II (D, K and N);
2-244 7.67e-76

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


Pssm-ID: 425487 [Multi-domain]  Cd Length: 318  Bit Score: 232.46  E-value: 7.67e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415     2 SSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHLaEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPVasivYEL 80
Cdd:pfam00152  77 SPQLYKQLLMVAgFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAK----ELE 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415    81 NPNFKPPKRPFRRMNYSDAIEWLKEHDVkkedgtfYEFGDDIPEAPERLMTD-----TINEPILLCRFPVEIKSFYMQRC 155
Cdd:pfam00152 152 GGTLLDLKKPFPRITYAEAIEKLNGKDV-------EELGYGSDKPDLRFLLElvidkNKFNPLWVTDFPAEHHPFTMPKD 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415   156 PEDPRLTESVDVLMPNVgEIVGGSMRSWDSEEILEGYKREGIDP----APYYWYTDQRKYGTCPHGGYGLGLERFLSWIL 231
Cdd:pfam00152 225 EDDPALAEAFDLVLNGV-EIGGGSIRIHDPELQEERFEEQGLDPeeaeEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLT 303

                         250
                  ....*....|...
gi 12851415   232 NRYHIRDVCLYPR 244
Cdd:pfam00152 304 GLESIREVIAFPK 316
asnC PRK03932
asparaginyl-tRNA synthetase; Validated
 2-251 7.48e-73

asparaginyl-tRNA synthetase; Validated


Pssm-ID: 235176 [Multi-domain]  Cd Length: 450  Bit Score: 228.84  E-value: 7.48e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415    2 SSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVL-----------K 70
Cdd:PRK03932 195 SGQLYAEAYAMALGKVYTFGPTFRAENSNTRRHLAEFWMIEPEMAFADLEDNMDLAEEMLKYVVKYVLencpddleflnR 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415   71 SPVASIVYELNpNFKPPkrPFRRMNYSDAIEWLKEHDVKKEDGTfyEFGDDI--PEapERLMTDTINE-PILLCRFPVEI 147
Cdd:PRK03932 275 RVDKGDIERLE-NFIES--PFPRITYTEAIEILQKSGKKFEFPV--EWGDDLgsEH--ERYLAEEHFKkPVFVTNYPKDI 347

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415  148 KSFYMQRCPEDpRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFL 227
Cdd:PRK03932 348 KAFYMRLNPDG-KTVAAMDLLAPGIGEIIGGSQREERLDVLEARIKELGLNKEDYWWYLDLRRYGSVPHSGFGLGFERLV 426

                        250       260
                 ....*....|....*....|....
gi 12851415  228 SWILNRYHIRDVCLYPRFLQRCRP 251
Cdd:PRK03932 427 AYITGLDNIRDVIPFPRTPGRAEF 450
aspC PRK05159
aspartyl-tRNA synthetase; Provisional
 2-251 9.80e-50

aspartyl-tRNA synthetase; Provisional


Pssm-ID: 235354 [Multi-domain]  Cd Length: 437  Bit Score: 168.44  E-value: 9.80e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415    2 SSQLYLETCLPALGD-VFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLT-FEDLLNRLEDLVCDVVDRVLKSPVASIVyE 79
Cdd:PRK05159 189 SPQLYKQMMVGAGFErVFEIGPVFRAEEHNTSRHLNEYTSIDVEMGFIDdHEDVMDLLENLLRYMYEDVAENCEKELE-L 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415   80 LNPNFKPPKRPFRRMNYSDAIEWLKEHDVKKEdgtfyeFGDDIPEAPERLMTDTINE-----PILLCRFPVEIKSFYMQR 154
Cdd:PRK05159 268 LGIELPVPETPIPRITYDEAIEILKSKGNEIS------WGDDLDTEGERLLGEYVKEeygsdFYFITDYPSEKRPFYTMP 341

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415  155 CPEDPRLTESVDVLMPNVgEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRY 234
Cdd:PRK05159 342 DEDDPEISKSFDLLFRGL-EITSGGQRIHRYDMLVESIKEKGLNPESFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLE 420

                        250
                 ....*....|....*..
gi 12851415  235 HIRDVCLYPRFLQRCRP 251
Cdd:PRK05159 421 NIREAVLFPRDRHRLTP 437
PLN02221 PLN02221
asparaginyl-tRNA synthetase
 2-245 4.30e-44

asparaginyl-tRNA synthetase


Pssm-ID: 177867 [Multi-domain]  Cd Length: 572  Bit Score: 156.31  E-value: 4.30e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415    2 SSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPVASIvyEL- 80
Cdd:PLN02221 314 SGQLQVETYACALSSVYTFGPTFRAENSHTSRHLAEFWMVEPEIAFADLEDDMNCAEAYVKYMCKWLLDKCFDDM--ELm 391

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415   81 NPNFKP---------PKRPFRRMNYSDAIEWLKEHDVK-KEDGTFYEFGDDIPEAPERLMTDTI-NEPILLCRFPVEIKS 149
Cdd:PLN02221 392 AKNFDSgcidrlrmvASTPFGRITYTEAIELLEEAVAKgKEFDNNVEWGIDLASEHERYLTEVLfQKPLIVYNYPKGIKA 471

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415  150 FYMqRCPEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSW 229
Cdd:PLN02221 472 FYM-RLNDDEKTVAAMDVLVPKVGELIGGSQREERYDVIKQRIEEMGLPIEPYEWYLDLRRYGTVKHCGFGLGFERMILF 550

                        250
                 ....*....|....*.
gi 12851415  230 ILNRYHIRDVCLYPRF 245
Cdd:PLN02221 551 ATGIDNIRDVIPFPRY 566
PRK06462 PRK06462
asparagine synthetase A; Reviewed
 2-244 5.17e-43

asparagine synthetase A; Reviewed


Pssm-ID: 235808 [Multi-domain]  Cd Length: 335  Bit Score: 148.63  E-value: 5.17e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415    2 SSQLYLETCLPALGDVFCIAQSYRAEQ--SRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPVASIvYE 79
Cdd:PRK06462  90 SMILHKQLALRMLGKIFYLSPNFRLEPvdKDTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHEDEL-EF 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415   80 LNPNFKPPKRPFRRMNYSDAIEWLKEHDVKKEDgtFYEFGDDIpeapERLMTDTINEPILLCRFPVEIKSFYMQRCPEDP 159
Cdd:PRK06462 169 FGRDLPHLKRPFKRITHKEAVEILNEEGCRGID--LEELGSEG----EKSLSEHFEEPFWIIDIPKGSREFYDREDPERP 242

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415  160 RLTESVDVLMPN-VGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRD 238
Cdd:PRK06462 243 GVLRNYDLLLPEgYGEAVSGGEREYEYEEIVERIREHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIRE 322


                 ....*.
gi 12851415  239 VCLYPR 244
Cdd:PRK06462 323 VQPFPR 328
PTZ00425 PTZ00425
asparagine-tRNA ligase; Provisional
 2-245 1.61e-40

asparagine-tRNA ligase; Provisional


Pssm-ID: 240414 [Multi-domain]  Cd Length: 586  Bit Score: 146.71  E-value: 1.61e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415    2 SSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPVASIVY-EL 80
Cdd:PTZ00425 331 SGQLSLENLCSSMGDVYTFGPTFRAENSHTSRHLAEFWMIEPEIAFADLYDNMELAESYIKYCIGYVLNNNFDDIYYfEE 410

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415   81 NPNFKPPKR-------PFRRMNYSDAIEWLKEHDVKKEdgTFYEFGDDIPEAPERLMTDTI-NEPILLCRFPVEIKSFYM 152
Cdd:PTZ00425 411 NVETGLISRlknildeDFAKITYTNVIDLLQPYSDSFE--VPVKWGMDLQSEHERFVAEQIfKKPVIVYNYPKDLKAFYM 488

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415  153 qRCPEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILN 232
Cdd:PTZ00425 489 -KLNEDQKTVAAMDVLVPKIGEVIGGSQREDNLERLDKMIKEKKLNMESYWWYRQLRKFGSHPHAGFGLGFERLIMLVTG 567

                        250
                 ....*....|...
gi 12851415  233 RYHIRDVCLYPRF 245
Cdd:PTZ00425 568 VDNIKDTIPFPRY 580
PLN02603 PLN02603
asparaginyl-tRNA synthetase
 2-244 2.21e-38

asparaginyl-tRNA synthetase


Pssm-ID: 178213 [Multi-domain]  Cd Length: 565  Bit Score: 140.49  E-value: 2.21e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415    2 SSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPV-------- 73
Cdd:PLN02603 309 SGQLNGETYATALSDVYTFGPTFRAENSNTSRHLAEFWMIEPELAFADLNDDMACATAYLQYVVKYILENCKedmeffnt 388

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415   74 ---ASIVYELNpnfKPPKRPFRRMNYSDAIEWLKEhdVKKEDGTFYEFGDDIPEAPERLMTDTI--NEPILLCRFPVEIK 148
Cdd:PLN02603 389 wieKGIIDRLS---DVVEKNFVQLSYTDAIELLLK--AKKKFEFPVKWGLDLQSEHERYITEEAfgGRPVIIRDYPKEIK 463

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415  149 SFYMqRCPEDPRLTESVDVLMPNVGEIVGGSMRSwDSEEILEGYKRE-GIDPAPYYWYTDQRKYGTCPHGGYGLGLERFL 227
Cdd:PLN02603 464 AFYM-RENDDGKTVAAMDMLVPRVGELIGGSQRE-ERLEYLEARLDElKLNKESYWWYLDLRRYGSVPHAGFGLGFERLV 541

                        250
                 ....*....|....*..
gi 12851415  228 SWILNRYHIRDVCLYPR 244
Cdd:PLN02603 542 QFATGIDNIRDAIPFPR 558
PLN02850 PLN02850
aspartate-tRNA ligase
 1-251 1.97e-29

aspartate-tRNA ligase


Pssm-ID: 215456 [Multi-domain]  Cd Length: 530  Bit Score: 115.57  E-value: 1.97e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415    1 ESSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHLAEFTHveaecpfLTFEDLLNRLEDLVCDVVDRVLKSpvasIVYE 79
Cdd:PLN02850 277 QSPQLHKQMAICGdFRRVFEIGPVFRAEDSFTHRHLCEFTG-------LDLEMEIKEHYSEVLDVVDELFVA----IFDG 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415   80 LNPN-------------FKPPK--RPFRRMNYSDAIEWLKEHDVKKEDgtfyeFGDDIPEApERLMTDTINEP-----IL 139
Cdd:PLN02850 346 LNERckkeleaireqypFEPLKylPKTLRLTFAEGIQMLKEAGVEVDP-----LGDLNTES-ERKLGQLVKEKygtdfYI 419

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415  140 LCRFPVEIKSFYMQRCPEDPRLTESVDVLMPNvGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGY 219
Cdd:PLN02850 420 LHRYPLAVRPFYTMPCPDDPKYSNSFDVFIRG-EEIISGAQRVHDPELLEKRAEECGIDVKTISTYIDSFRYGAPPHGGF 498

                        250       260       270
                 ....*....|....*....|....*....|..
gi 12851415  220 GLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 251
Cdd:PLN02850 499 GVGLERVVMLFCGLNNIRKTSLFPRDPQRLAP 530
Asp_Lys_Asn_RS_core cd00669
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ...
 1-244 3.19e-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: 108.33  E-value: 3.19e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415   1 ESSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRrHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLkspvASIVYE 79
Cdd:cd00669  55 ISPQLFKKRLMVGgLDRVFEINRNFRNEDLRAR-HQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVL----GVTAVT 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415  80 LNPNFKPPKRPFRRMNYSDAIEWLKEhdvkkedgtfyefgddipeaperlmtdtinePILLCRFPVEIKSFYMQRCPEDP 159
Cdd:cd00669 130 YGFELEDFGLPFPRLTYREALERYGQ-------------------------------PLFLTDYPAEMHSPLASPHDVNP 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415 160 RLTESVDVLMPNVgEIVGGSMRSWDSEEILEGYKREGIDPAP----YYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYH 235
Cdd:cd00669 179 EIADAFDLFINGV-EVGNGSSRLHDPDIQAEVFQEQGINKEAgmeyFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPT 257


                ....*....
gi 12851415 236 IRDVCLYPR 244
Cdd:cd00669 258 IREVIAFPK 266
PTZ00401 PTZ00401
aspartyl-tRNA synthetase; Provisional
 1-251 1.12e-26

aspartyl-tRNA synthetase; Provisional


Pssm-ID: 173592 [Multi-domain]  Cd Length: 550  Bit Score: 107.77  E-value: 1.12e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415    1 ESSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLT-FEDLLNRLEDLVCDVVDRVLKS------- 71
Cdd:PTZ00401 265 QSPQLYKQMVLQGdVPRVFEVGPVFRSENSNTHRHLTEFVGLDVEMRINEhYYEVLDLAESLFNYIFERLATHtkelkav 344

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415   72 ----PVASIVYELNP-------------NFKPPKR----------PFRRMNYSDAIEWLKEHDVKKEDGTfyefgDDIPE 124
Cdd:PTZ00401 345 cqqyPFEPLVWKLTPermkelgvgviseGVEPTDKyqarvhnmdsRMLRINYMHCIELLNTVLEEKMAPT-----DDINT 419

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415  125 APERLMTDTINEP-----ILLCRFPVEIKSFYMQRCPEDPRLTESVDVLMPNvGEIVGGSMRSWDSEEILEGYKREGIDP 199
Cdd:PTZ00401 420 TNEKLLGKLVKERygtdfFISDRFPSSARPFYTMECKDDERFTNSYDMFIRG-EEISSGAQRIHDPDLLLARAKMLNVDL 498

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 12851415  200 APYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 251
Cdd:PTZ00401 499 TPIKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFPRDPQRTTP 550
PLN02532 PLN02532
asparagine-tRNA synthetase
 2-244 1.53e-24

asparagine-tRNA synthetase


Pssm-ID: 215291 [Multi-domain]  Cd Length: 633  Bit Score: 101.87  E-value: 1.53e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415    2 SSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPVA------- 74
Cdd:PLN02532 377 SGRLHLESYACALGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAFSELEDAMNCAEDYFKFLCKWVLENCSEdmkfvsk 456

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415   75 ----SIVYELNPNFkppKRPFRRMNYSDAIEWLKEH-DVKKEdgTFYEFGddIPEAPERL--MTDTI-NEPILLCRFPVE 146
Cdd:PLN02532 457 ridkTISTRLEAII---SSSLQRISYTEAVDLLKQAtDKKFE--TKPEWG--IALTTEHLsyLADEIyKKPVIIYNYPKE 529

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415  147 IKSFYMqRCPEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERF 226
Cdd:PLN02532 530 LKPFYV-RLNDDGKTVAAFDLVVPKVGTVITGSQNEERMDILNARIEELGLPREQYEWYLDLRRHGTVKHSGFSLGFELM 608

                        250
                 ....*....|....*...
gi 12851415  227 LSWILNRYHIRDVCLYPR 244
Cdd:PLN02532 609 VLFATGLPDVRDAIPFPR 626
AspRS_core cd00777
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ...
 18-243 1.46e-12

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: 65.67  E-value: 1.46e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415  18 FCIAQSYRAEQSRTRRHlAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKspvasivyelnpnfKPPKRPFRRMNYS 97
Cdd:cd00777  73 FQIARCFRDEDLRADRQ-PEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG--------------VELTTPFPRMTYA 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415  98 DAIE-------W-----LKEHDvkKEDGTfYEFGDDIPEAPERLMTDTINEpillcrFPVEIKSfymqrcpedprltESV 165
Cdd:cd00777 138 EAMErygfkflWivdfpLFEWD--EEEGR-LVSAHHPFTAPKEEDLDLLEK------DPEDARA-------------QAY 195

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415 166 DVLMpNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYY----WYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCL 241
Cdd:cd00777 196 DLVL-NGVELGGGSIRIHDPDIQEKVFEILGLSEEEAEekfgFLLEAFKYGAPPHGGIALGLDRLVMLLTGSESIRDVIA 274


                ..
gi 12851415 242 YP 243
Cdd:cd00777 275 FP 276
lysS PRK00484
lysyl-tRNA synthetase; Reviewed
 32-243 1.04e-09

lysyl-tRNA synthetase; Reviewed


Pssm-ID: 234778 [Multi-domain]  Cd Length: 491  Bit Score: 58.18  E-value: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415   32 RRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPVasIVY---ELNpnFKPPkrpFRRMNYSDAI-------- 100
Cdd:PRK00484 257 TRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTK--VTYqgtEID--FGPP---FKRLTMVDAIkeytgvdf 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415  101 ---------EWLKEHDVKKEDgtFYEFGDDIPEAPERLMTDTINEPILLCRFPVEI----KsfymqRCPEDPRLTESVDV 167
Cdd:PRK00484 330 ddmtdeearALAKELGIEVEK--SWGLGKLINELFEEFVEPKLIQPTFITDYPVEIsplaK-----RHREDPGLTERFEL 402

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415  168 lmpnvgeIVGGSmrswdseEILEGYKrEGIDPApyywytDQRK----------------------------YGTCPHGGY 219
Cdd:PRK00484 403 -------FIGGR-------EIANAFS-ELNDPI------DQRErfeaqveakeagddeamfmdedflraleYGMPPTGGL 461

                        250       260
                 ....*....|....*....|....
gi 12851415  220 GLGLERFLSWILNRYHIRDVCLYP 243
Cdd:PRK00484 462 GIGIDRLVMLLTDSPSIRDVILFP 485
PTZ00385 PTZ00385
lysyl-tRNA synthetase; Provisional
 4-250 8.05e-08

lysyl-tRNA synthetase; Provisional


Pssm-ID: 185588 [Multi-domain]  Cd Length: 659  Bit Score: 52.73  E-value: 8.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415    4 QLYLETCL-PALGDVFCIAQSYRAEQSrTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPVASIVYEL-- 80
Cdd:PTZ00385 290 ELHLKQCIvGGMERIYEIGKVFRNEDA-DRSHNPEFTSCEFYAAYHTYEDLMPMTEDIFRQLAMRVNGTTVVQIYPENah 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415   81 -NPNFKPPKRPFRRMNYSDAI------EWLKEHDVKKEDGTFY----EFGDDIPEAPER------------LMTDTINEP 137
Cdd:PTZ00385 369 gNPVTVDLGKPFRRVSVYDEIqrmsgvEFPPPNELNTPKGIAYmsvvMLRYNIPLPPVRtaakmfeklidfFITDRVVEP 448

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415  138 ILLCRFPVEIKSFYMQRCPEdPRLTESVDVLMPNVgEIVGGSMRSWDSEEILEGYKREGID-------PAPY-YWYTDQR 209
Cdd:PTZ00385 449 TFVMDHPLFMSPLAKEQVSR-PGLAERFELFVNGI-EYCNAYSELNDPHEQYHRFQQQLVDrqggdeeAMPLdETFLKSL 526

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 12851415  210 KYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCR 250
Cdd:PTZ00385 527 QVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFPLLRQDIR 567
PRK12445 PRK12445
lysyl-tRNA synthetase; Reviewed
 17-243 1.08e-07

lysyl-tRNA synthetase; Reviewed


Pssm-ID: 171504 [Multi-domain]  Cd Length: 505  Bit Score: 51.99  E-value: 1.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415   17 VFCIAQSYRAEqSRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVL---KSPVASIVYELNPNFKP------- 86
Cdd:PRK12445 255 VFEINRNFRNE-GISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLgttKVTYGEHVFDFGKPFEKltmreai 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415   87 ----PKRPFRRMNYSDAIEWLKEH---DVKKEDGtfyeFGDDIPEAPERLMTDTINEPILLCRFPVEIkSFYMQRCPEDP 159
Cdd:PRK12445 334 kkyrPETDMADLDNFDAAKALAESigiTVEKSWG----LGRIVTEIFDEVAEAHLIQPTFITEYPAEV-SPLARRNDVNP 408

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415  160 RLTESVDVLMPNvGEIVGGSMRSWDSEEILEGY------KREGIDPAPYYW--YTDQRKYGTCPHGGYGLGLERFLSWIL 231
Cdd:PRK12445 409 EITDRFEFFIGG-REIGNGFSELNDAEDQAERFqeqvnaKAAGDDEAMFYDedYVTALEYGLPPTAGLGIGIDRMIMLFT 487

                        250
                 ....*....|..
gi 12851415  232 NRYHIRDVCLYP 243
Cdd:PRK12445 488 NSHTIRDVILFP 499
PLN02903 PLN02903
aminoacyl-tRNA ligase
 1-101 1.31e-05

aminoacyl-tRNA ligase


Pssm-ID: 215490 [Multi-domain]  Cd Length: 652  Bit Score: 45.93  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415    1 ESSQLYLETCLPALGD-VFCIAQSYRAEQSRTRRHlAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPVAsivye 79
Cdd:PLN02903 258 QSPQLFKQMLMVSGFDrYYQIARCFRDEDLRADRQ-PEFTQLDMELAFTPLEDMLKLNEDLIRQVFKEIKGVQLP----- 331

                         90       100
                 ....*....|....*....|..
gi 12851415   80 lnpnfkppkRPFRRMNYSDAIE 101
Cdd:PLN02903 332 ---------NPFPRLTYAEAMS 344
PRK12820 PRK12820
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ...
 168-244 1.16e-04

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


Pssm-ID: 105955 [Multi-domain]  Cd Length: 706  Bit Score: 43.05  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415  168 LMPNVGEIVGGSMRSWDSEEILEGYKREGIDPA----PYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYP 243
Cdd:PRK12820 493 LVVNGEELGGGSIRINDKDIQLRIFAALGLSEEdiedKFGFFLRAFDFAAPPHGGIALGLDRVVSMILQTPSIREVIAFP 572


                 .
gi 12851415  244 R 244
Cdd:PRK12820 573 K 573
genX TIGR00462
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ...
 15-163 5.82e-04

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


Pssm-ID: 273090 [Multi-domain]  Cd Length: 290  Bit Score: 40.23  E-value: 5.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415    15 GDVFCIAQSYRAEQsRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVvdrvlkspvasivyelnpnFKPPKRPFRRM 94
Cdd:TIGR00462  61 GPIFQICKVFRNGE-RGRRHNPEFTMLEWYRPGFDYHDLMDEVEALLQEL-------------------LGDPFAPAERL 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415    95 NYSDA-IEWLKEHDVKKEDGTFYE----FGDDIPEAP------ERLMTDTI------NEPILLCRFPVEIKSFyMQRCPE 157
Cdd:TIGR00462 121 SYQEAfLRYAGIDPLTASLAELQAaaaaHGIRASEEDdrddllDLLFSEKVephlgfGRPTFLYDYPASQAAL-ARISPD 199


                  ....*.
gi 12851415   158 DPRLTE 163
Cdd:TIGR00462 200 DPRVAE 205
aspS PRK00476
aspartyl-tRNA synthetase; Validated
 18-102 1.15e-03

aspartyl-tRNA synthetase; Validated


Pssm-ID: 234775 [Multi-domain]  Cd Length: 588  Bit Score: 39.67  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415   18 FCIAQSYRAEQSRTRRhLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPVasivyelnpnfkppKRPFRRMNYS 97
Cdd:PRK00476 213 YQIARCFRDEDLRADR-QPEFTQIDIEMSFVTQEDVMALMEGLIRHVFKEVLGVDL--------------PTPFPRMTYA 277


                 ....*
gi 12851415   98 DAIEW 102
Cdd:PRK00476 278 EAMRR 282
PTZ00417 PTZ00417
lysine-tRNA ligase; Provisional
 17-243 2.29e-03

lysine-tRNA ligase; Provisional


Pssm-ID: 173607 [Multi-domain]  Cd Length: 585  Bit Score: 38.84  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415   17 VFCIAQSYRAEqSRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSpvASIVY-----ELNP---NFKPPk 88
Cdd:PTZ00417 324 VYEIGKVFRNE-GIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHLFGT--YKILYnkdgpEKDPieiDFTPP- 399

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415   89 rpFRRMNYSDAIEWLKE----------HDVKKEDGTFYEFGDDIPEAP------ERLMTDTI-----NEPILLCRFPvEI 147
Cdd:PTZ00417 400 --YPKVSIVEELEKLTNtkleqpfdspETINKMINLIKENKIEMPNPPtaakllDQLASHFIenkypNKPFFIIEHP-QI 476

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415  148 KSFYMQRCPEDPRLTESVDVLMPNvGEIVGGSMRSWDSEEILEGYK-----REGIDPAPYYW---YTDQRKYGTCPHGGY 219
Cdd:PTZ00417 477 MSPLAKYHRSKPGLTERLEMFICG-KEVLNAYTELNDPFKQKECFSaqqkdREKGDAEAFQFdaaFCTSLEYGLPPTGGL 555

                        250       260
                 ....*....|....*....|....
gi 12851415  220 GLGLERFLSWILNRYHIRDVCLYP 243
Cdd:PTZ00417 556 GLGIDRITMFLTNKNCIKDVILFP 579
aspS PRK00476
aspartyl-tRNA synthetase; Validated
 174-243 3.37e-03

aspartyl-tRNA synthetase; Validated


Pssm-ID: 234775 [Multi-domain]  Cd Length: 588  Bit Score: 38.51  E-value: 3.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415  174 EIVGGSMRSWDSE------EILegykreGIDPApyywytDQR----------KYGTCPHGGYGLGLERFLSWILNRYHIR 237
Cdd:PRK00476 483 ELGGGSIRIHRPEiqekvfEIL------GISEE------EAEekfgflldalKYGAPPHGGIAFGLDRLVMLLAGADSIR 550


                 ....*.
gi 12851415  238 DVCLYP 243
Cdd:PRK00476 551 DVIAFP 556
AspS COG0173
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ...
 174-243 4.51e-03

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


Pssm-ID: 439943 [Multi-domain]  Cd Length: 589  Bit Score: 38.06  E-value: 4.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415 174 EIVGGSMRSWDSE------EILegykreGIDPApyywytDQR----------KYGTCPHGGYGLGLERFLSWILNRYHIR 237
Cdd:COG0173 482 ELGGGSIRIHDPElqekvfELL------GISEE------EAEekfgflleafKYGAPPHGGIAFGLDRLVMLLAGEDSIR 549


                ....*.
gi 12851415 238 DVCLYP 243
Cdd:COG0173 550 DVIAFP 555
EpmA COG2269
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ...
 15-78 6.82e-03

Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441870 [Multi-domain]  Cd Length: 309  Bit Score: 37.01  E-value: 6.82e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12851415  15 GDVFCIAQSYRAEQsRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPVASIVY 78
Cdd:COG2269  79 GPIYQIAKVFRNGE-RGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAAGFAPAERLSY 141
AspS COG0173
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ...
 20-102 8.36e-03

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


Pssm-ID: 439943 [Multi-domain]  Cd Length: 589  Bit Score: 37.29  E-value: 8.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851415  20 IAQSYRAEQSRTRRHlAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKspvasivYELnpnfkppKRPFRRMNYSDA 99
Cdd:COG0173 216 IARCFRDEDLRADRQ-PEFTQLDIEMSFVDQEDVFELMEGLIRHLFKEVLG-------VEL-------PTPFPRMTYAEA 280


                ...
gi 12851415 100 IEW 102
Cdd:COG0173 281 MER 283
 
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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