|
Name |
Accession |
Description |
Interval |
E-value |
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
4-247 |
2.56e-124 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 360.58 E-value: 2.56e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 4 AFTQVFTFGPTFRAENSQSRRHLAEFYMIEAEISFVDsLQDLMQVIEELFKATTMMVLSKCPEDVELCHKFIAPGQKDRL 83
Cdd:PRK03932 206 ALGKVYTFGPTFRAENSNTRRHLAEFWMIEPEMAFAD-LEDNMDLAEEMLKYVVKYVLENCPDDLEFLNRRVDKGDIERL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 84 EHMLKNNFLIISYTEAVEILKQASQNFTFTPEWGADLRTEHEKYLVKHCGNIPVFVINYPLTLKPFYMRDNEDGpqHTVA 163
Cdd:PRK03932 285 ENFIESPFPRITYTEAIEILQKSGKKFEFPVEWGDDLGSEHERYLAEEHFKKPVFVTNYPKDIKAFYMRLNPDG--KTVA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 164 AVDLLVPGVGELFGGGLREERYHFLEERLARSGL-TEVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFP 242
Cdd:PRK03932 363 AMDLLAPGIGEIIGGSQREERLDVLEARIKELGLnKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFP 442
|
....*
gi 343098477 243 RFPHS 247
Cdd:PRK03932 443 RTPGR 447
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
1-248 |
1.87e-118 |
|
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: 344.73 E-value: 1.87e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 1 MSGAFTQVFTFGPTFRAENSQSRRHLAEFYMIEAEISFVDsLQDLMQVIEELFKATTMMVLSKCPEDVELCHKFIapgqk 80
Cdd:COG0017 191 LAMALEKVYTFGPTFRAEKSNTRRHLAEFWMIEPEMAFAD-LEDVMDLAEEMLKYIIKYVLENCPEELEFLGRDV----- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 81 DRLEHMLKNNFLIISYTEAVEILKQASQNFtftpEWGADLRTEHEKYLVKHCGNIPVFVINYPLTLKPFYMRDNEDGPQh 160
Cdd:COG0017 265 ERLEKVPESPFPRITYTEAIEILKKSGEKV----EWGDDLGTEHERYLGEEFFKKPVFVTDYPKEIKAFYMKPNPDDPK- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 161 TVAAVDLLVPGVGELFGGGLREERYHFLEERLARSGL-TEVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVI 239
Cdd:COG0017 340 TVAAFDLLAPGIGEIIGGSQREHRYDVLVERIKEKGLdPEDYEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVI 419
|
....*....
gi 343098477 240 PFPRFPHSC 248
Cdd:COG0017 420 PFPRDPGRL 428
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
1-246 |
9.61e-113 |
|
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: 326.45 E-value: 9.61e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 1 MSGAFTQVFTFGPTFRAENSQSRRHLAEFYMIEAEISFVDSLQDLMQVIEELFKATTMMVLSKCPEDVELChkfiapGQK 80
Cdd:cd00776 85 LIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEDYNEVMDLIEELIKYIFKRVLERCAKELELV------NQL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 81 DRLEHMLKNNFLIISYTEAVEILKQASQNftFTPEWGADLRTEHEKYLVKHCGNIPVFVINYPLTLKPFYMRDNEDGPQh 160
Cdd:cd00776 159 NRELLKPLEPFPRITYDEAIELLREKGVE--EEVKWGEDLSTEHERLLGEIVKGDPVFVTDYPKEIKPFYMKPDDDNPE- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 161 TVAAVDLLVPGVGELFGGGLREERYHFLEERLARSGL-TEVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVI 239
Cdd:cd00776 236 TVESFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGLdPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAI 315
|
....*..
gi 343098477 240 PFPRFPH 246
Cdd:cd00776 316 LFPRDPK 322
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
4-248 |
5.94e-109 |
|
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative asparaginyl-tRNA synthetases (asnS), archaeal/eukaryotic type aspartyl-tRNA synthetases (aspS_arch), and bacterial type aspartyl-tRNA synthetases (aspS_bact), there is a striking similarity between asnS and aspS_arch in gap pattern and in sequence, and a striking divergence of aspS_bact. Consequently, a separate model was built for each of the three groups. This model, asnS, represents asparaginyl-tRNA synthetases from the three domains of life. Some species lack this enzyme and charge tRNA(asn) by misacylation with Asp, followed by transamidation of Asp to Asn. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273086 [Multi-domain] Cd Length: 453 Bit Score: 321.64 E-value: 5.94e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 4 AFTQVFTFGPTFRAENSQSRRHLAEFYMIEAEISFVDsLQDLMQVIEELFKATTMMVLSKCPEDVELCHKFIAPGQKDRL 83
Cdd:TIGR00457 209 ALSKVYTFGPTFRAEKSNTSRHLSEFWMIEPEMAFAN-LNDLLQLAETLIKYIIKAVLENCSQELKFLEKNFDKDLIKRL 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 84 EHMLKNNFLIISYTEAVEILKQASQNFTFTPEWGADLRTEHEKYLVKHCGNIPVFVINYPLTLKPFYMRDNEDGpqHTVA 163
Cdd:TIGR00457 288 ENIINNKFARITYTDAIEILKESDKNFEYEDFWGDDLQTEHERFLAEEYFKPPVFVTNYPKDIKAFYMKLNDDG--KTVA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 164 AVDLLVPGVGELFGGGLREERYHFLEERLARSGL-TEVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFP 242
Cdd:TIGR00457 366 AMDLLAPGIGEIIGGSEREDDLDKLENRMKEMGLdTDALNWYLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFP 445
|
....*.
gi 343098477 243 RFPHSC 248
Cdd:TIGR00457 446 RTPGNI 451
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
1-243 |
4.70e-69 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 215.12 E-value: 4.70e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 1 MSGAFTQVFTFGPTFRAENSQSRRHLaEFYMIEAEISFVDsLQDLMQVIEELFKATTMMVLsKCPEDVELchkfiapgqk 80
Cdd:pfam00152 86 MVAGFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVD-YEDVMDLTEELIKEIFKEVE-GIAKELEG---------- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 81 dRLEHMLKNNFLIISYTEAVEILKQASqnftfTPEWGADLRTEHEKYLV----KHCGNIPVFVINYPLTLKPFYMRDNED 156
Cdd:pfam00152 153 -GTLLDLKKPFPRITYAEAIEKLNGKD-----VEELGYGSDKPDLRFLLelviDKNKFNPLWVTDFPAEHHPFTMPKDED 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 157 GPQHTvAAVDLLVPGVgELFGGGLREERYHFLEERLARSGLT-----EVYQWYLDLRRFGSVPHGGFGMGFERYLQCILG 231
Cdd:pfam00152 227 DPALA-EAFDLVLNGV-EIGGGSIRIHDPELQEERFEEQGLDpeeaeEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTG 304
|
250
....*....|..
gi 343098477 232 VDNIKDVIPFPR 243
Cdd:pfam00152 305 LESIREVIAFPK 316
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
4-247 |
2.56e-124 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 360.58 E-value: 2.56e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 4 AFTQVFTFGPTFRAENSQSRRHLAEFYMIEAEISFVDsLQDLMQVIEELFKATTMMVLSKCPEDVELCHKFIAPGQKDRL 83
Cdd:PRK03932 206 ALGKVYTFGPTFRAENSNTRRHLAEFWMIEPEMAFAD-LEDNMDLAEEMLKYVVKYVLENCPDDLEFLNRRVDKGDIERL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 84 EHMLKNNFLIISYTEAVEILKQASQNFTFTPEWGADLRTEHEKYLVKHCGNIPVFVINYPLTLKPFYMRDNEDGpqHTVA 163
Cdd:PRK03932 285 ENFIESPFPRITYTEAIEILQKSGKKFEFPVEWGDDLGSEHERYLAEEHFKKPVFVTNYPKDIKAFYMRLNPDG--KTVA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 164 AVDLLVPGVGELFGGGLREERYHFLEERLARSGL-TEVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFP 242
Cdd:PRK03932 363 AMDLLAPGIGEIIGGSQREERLDVLEARIKELGLnKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFP 442
|
....*
gi 343098477 243 RFPHS 247
Cdd:PRK03932 443 RTPGR 447
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
1-248 |
1.87e-118 |
|
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: 344.73 E-value: 1.87e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 1 MSGAFTQVFTFGPTFRAENSQSRRHLAEFYMIEAEISFVDsLQDLMQVIEELFKATTMMVLSKCPEDVELCHKFIapgqk 80
Cdd:COG0017 191 LAMALEKVYTFGPTFRAEKSNTRRHLAEFWMIEPEMAFAD-LEDVMDLAEEMLKYIIKYVLENCPEELEFLGRDV----- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 81 DRLEHMLKNNFLIISYTEAVEILKQASQNFtftpEWGADLRTEHEKYLVKHCGNIPVFVINYPLTLKPFYMRDNEDGPQh 160
Cdd:COG0017 265 ERLEKVPESPFPRITYTEAIEILKKSGEKV----EWGDDLGTEHERYLGEEFFKKPVFVTDYPKEIKAFYMKPNPDDPK- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 161 TVAAVDLLVPGVGELFGGGLREERYHFLEERLARSGL-TEVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVI 239
Cdd:COG0017 340 TVAAFDLLAPGIGEIIGGSQREHRYDVLVERIKEKGLdPEDYEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVI 419
|
....*....
gi 343098477 240 PFPRFPHSC 248
Cdd:COG0017 420 PFPRDPGRL 428
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
1-246 |
9.61e-113 |
|
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: 326.45 E-value: 9.61e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 1 MSGAFTQVFTFGPTFRAENSQSRRHLAEFYMIEAEISFVDSLQDLMQVIEELFKATTMMVLSKCPEDVELChkfiapGQK 80
Cdd:cd00776 85 LIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEDYNEVMDLIEELIKYIFKRVLERCAKELELV------NQL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 81 DRLEHMLKNNFLIISYTEAVEILKQASQNftFTPEWGADLRTEHEKYLVKHCGNIPVFVINYPLTLKPFYMRDNEDGPQh 160
Cdd:cd00776 159 NRELLKPLEPFPRITYDEAIELLREKGVE--EEVKWGEDLSTEHERLLGEIVKGDPVFVTDYPKEIKPFYMKPDDDNPE- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 161 TVAAVDLLVPGVGELFGGGLREERYHFLEERLARSGL-TEVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVI 239
Cdd:cd00776 236 TVESFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGLdPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAI 315
|
....*..
gi 343098477 240 PFPRFPH 246
Cdd:cd00776 316 LFPRDPK 322
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
4-248 |
5.94e-109 |
|
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative asparaginyl-tRNA synthetases (asnS), archaeal/eukaryotic type aspartyl-tRNA synthetases (aspS_arch), and bacterial type aspartyl-tRNA synthetases (aspS_bact), there is a striking similarity between asnS and aspS_arch in gap pattern and in sequence, and a striking divergence of aspS_bact. Consequently, a separate model was built for each of the three groups. This model, asnS, represents asparaginyl-tRNA synthetases from the three domains of life. Some species lack this enzyme and charge tRNA(asn) by misacylation with Asp, followed by transamidation of Asp to Asn. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273086 [Multi-domain] Cd Length: 453 Bit Score: 321.64 E-value: 5.94e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 4 AFTQVFTFGPTFRAENSQSRRHLAEFYMIEAEISFVDsLQDLMQVIEELFKATTMMVLSKCPEDVELCHKFIAPGQKDRL 83
Cdd:TIGR00457 209 ALSKVYTFGPTFRAEKSNTSRHLSEFWMIEPEMAFAN-LNDLLQLAETLIKYIIKAVLENCSQELKFLEKNFDKDLIKRL 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 84 EHMLKNNFLIISYTEAVEILKQASQNFTFTPEWGADLRTEHEKYLVKHCGNIPVFVINYPLTLKPFYMRDNEDGpqHTVA 163
Cdd:TIGR00457 288 ENIINNKFARITYTDAIEILKESDKNFEYEDFWGDDLQTEHERFLAEEYFKPPVFVTNYPKDIKAFYMKLNDDG--KTVA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 164 AVDLLVPGVGELFGGGLREERYHFLEERLARSGL-TEVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFP 242
Cdd:TIGR00457 366 AMDLLAPGIGEIIGGSEREDDLDKLENRMKEMGLdTDALNWYLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFP 445
|
....*.
gi 343098477 243 RFPHSC 248
Cdd:TIGR00457 446 RTPGNI 451
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
4-247 |
2.03e-93 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 285.33 E-value: 2.03e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 4 AFTQVFTFGPTFRAENSQSRRHLAEFYMIEAEISFVDsLQDLMQVIEELFKATTMMVLSKCPEDVELCHKFIAPGQKDRL 83
Cdd:PLN02603 320 ALSDVYTFGPTFRAENSNTSRHLAEFWMIEPELAFAD-LNDDMACATAYLQYVVKYILENCKEDMEFFNTWIEKGIIDRL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 84 EHMLKNNFLIISYTEAVEILKQASQNFTFTPEWGADLRTEHEKYLVKHC-GNIPVFVINYPLTLKPFYMRDNEDGpqHTV 162
Cdd:PLN02603 399 SDVVEKNFVQLSYTDAIELLLKAKKKFEFPVKWGLDLQSEHERYITEEAfGGRPVIIRDYPKEIKAFYMRENDDG--KTV 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 163 AAVDLLVPGVGELFGGGLREERYHFLEERLARSGLT-EVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVIPF 241
Cdd:PLN02603 477 AAMDMLVPRVGELIGGSQREERLEYLEARLDELKLNkESYWWYLDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPF 556
|
....*.
gi 343098477 242 PRFPHS 247
Cdd:PLN02603 557 PRVPGS 562
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
4-245 |
5.77e-90 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 276.49 E-value: 5.77e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 4 AFTQVFTFGPTFRAENSQSRRHLAEFYMIEAEISFVDsLQDLMQVIEELFKATTMMVLSKCPEDVELCHKFIAPGQKDRL 83
Cdd:PLN02221 325 ALSSVYTFGPTFRAENSHTSRHLAEFWMVEPEIAFAD-LEDDMNCAEAYVKYMCKWLLDKCFDDMELMAKNFDSGCIDRL 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 84 EHMLKNNFLIISYTEAVEILKQA---SQNFTFTPEWGADLRTEHEKYLVKHCGNIPVFVINYPLTLKPFYMRDNEDgpQH 160
Cdd:PLN02221 404 RMVASTPFGRITYTEAIELLEEAvakGKEFDNNVEWGIDLASEHERYLTEVLFQKPLIVYNYPKGIKAFYMRLNDD--EK 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 161 TVAAVDLLVPGVGELFGGGLREERYHFLEERLARSGL-TEVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVI 239
Cdd:PLN02221 482 TVAAMDVLVPKVGELIGGSQREERYDVIKQRIEEMGLpIEPYEWYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVI 561
|
....*.
gi 343098477 240 PFPRFP 245
Cdd:PLN02221 562 PFPRYP 567
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
8-245 |
4.44e-79 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 248.78 E-value: 4.44e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 8 VFTFGPTFRAENSQSRRHLAEFYMIEAEISFVDsLQDLMQVIEELFKATTMMVLSKCPEDVELCHKFIAPGQKDRLEHML 87
Cdd:PTZ00425 346 VYTFGPTFRAENSHTSRHLAEFWMIEPEIAFAD-LYDNMELAESYIKYCIGYVLNNNFDDIYYFEENVETGLISRLKNIL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 88 KNNFLIISYTEAVEILKQASQNFTFTPEWGADLRTEHEKYLVKHCGNIPVFVINYPLTLKPFYMRDNEDgpQHTVAAVDL 167
Cdd:PTZ00425 425 DEDFAKITYTNVIDLLQPYSDSFEVPVKWGMDLQSEHERFVAEQIFKKPVIVYNYPKDLKAFYMKLNED--QKTVAAMDV 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 343098477 168 LVPGVGELFGGGLREERYHFLEERLARSGLT-EVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFPRFP 245
Cdd:PTZ00425 503 LVPKIGEVIGGSQREDNLERLDKMIKEKKLNmESYWWYRQLRKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFPRYP 581
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
4-243 |
1.17e-73 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 235.92 E-value: 1.17e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 4 AFTQVFTFGPTFRAENSQSRRHLAEFYMIEAEISFVDsLQDLMQVIEELFKATTMMVLSKCPEDVELCHKFIAPGQKDRL 83
Cdd:PLN02532 388 ALGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAFSE-LEDAMNCAEDYFKFLCKWVLENCSEDMKFVSKRIDKTISTRL 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 84 EHMLKNNFLIISYTEAVEILKQASQN-FTFTPEWGADLRTEHEKYLVKHCGNIPVFVINYPLTLKPFYMRDNEDGpqHTV 162
Cdd:PLN02532 467 EAIISSSLQRISYTEAVDLLKQATDKkFETKPEWGIALTTEHLSYLADEIYKKPVIIYNYPKELKPFYVRLNDDG--KTV 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 163 AAVDLLVPGVGELFGGGLREERYHFLEERLARSGLT-EVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVIPF 241
Cdd:PLN02532 545 AAFDLVVPKVGTVITGSQNEERMDILNARIEELGLPrEQYEWYLDLRRHGTVKHSGFSLGFELMVLFATGLPDVRDAIPF 624
|
..
gi 343098477 242 PR 243
Cdd:PLN02532 625 PR 626
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
1-243 |
4.70e-69 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 215.12 E-value: 4.70e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 1 MSGAFTQVFTFGPTFRAENSQSRRHLaEFYMIEAEISFVDsLQDLMQVIEELFKATTMMVLsKCPEDVELchkfiapgqk 80
Cdd:pfam00152 86 MVAGFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVD-YEDVMDLTEELIKEIFKEVE-GIAKELEG---------- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 81 dRLEHMLKNNFLIISYTEAVEILKQASqnftfTPEWGADLRTEHEKYLV----KHCGNIPVFVINYPLTLKPFYMRDNED 156
Cdd:pfam00152 153 -GTLLDLKKPFPRITYAEAIEKLNGKD-----VEELGYGSDKPDLRFLLelviDKNKFNPLWVTDFPAEHHPFTMPKDED 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 157 GPQHTvAAVDLLVPGVgELFGGGLREERYHFLEERLARSGLT-----EVYQWYLDLRRFGSVPHGGFGMGFERYLQCILG 231
Cdd:pfam00152 227 DPALA-EAFDLVLNGV-EIGGGSIRIHDPELQEERFEEQGLDpeeaeEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTG 304
|
250
....*....|..
gi 343098477 232 VDNIKDVIPFPR 243
Cdd:pfam00152 305 LESIREVIAFPK 316
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
1-246 |
4.23e-60 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 195.41 E-value: 4.23e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 1 MSGAFTQVFTFGPTFRAENSQSRRHLAEFYMIEAEISFVDSLQDLMQVIEELFKATTMMVLSKCPEDVELchkfiapgqk 80
Cdd:PRK05159 198 VGAGFERVFEIGPVFRAEEHNTSRHLNEYTSIDVEMGFIDDHEDVMDLLENLLRYMYEDVAENCEKELEL---------- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 81 drLEHML---KNNFLIISYTEAVEILKQASQNftftPEWGADLRTEHEKYLVKH----CGNIPVFVINYPLTLKPFYMRD 153
Cdd:PRK05159 268 --LGIELpvpETPIPRITYDEAIEILKSKGNE----ISWGDDLDTEGERLLGEYvkeeYGSDFYFITDYPSEKRPFYTMP 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 154 NEDGPQHTvAAVDLLVPGVgELFGGGLREERYHFLEERLARSGL-TEVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGV 232
Cdd:PRK05159 342 DEDDPEIS-KSFDLLFRGL-EITSGGQRIHRYDMLVESIKEKGLnPESFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGL 419
|
250
....*....|....
gi 343098477 233 DNIKDVIPFPRFPH 246
Cdd:PRK05159 420 ENIREAVLFPRDRH 433
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
4-245 |
1.17e-42 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 147.47 E-value: 1.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 4 AFTQVFTFGPTFRAEN--SQSRRHLAEFYMIEAEISFVDsLQDLMQVIEELFKATTMMVLSKCPEDVELCHKfiapgqkd 81
Cdd:PRK06462 101 MLGKIFYLSPNFRLEPvdKDTGRHLYEFTQLDIEIEGAD-LDEVMDLIEDLIKYLVKELLEEHEDELEFFGR-------- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 82 RLEHmLKNNFLIISYTEAVEILKqasqNFTFTPEWGADLRTEHEKYLVKHCGNiPVFVINYPLTLKPFYMRDNEDGPQHT 161
Cdd:PRK06462 172 DLPH-LKRPFKRITHKEAVEILN----EEGCRGIDLEELGSEGEKSLSEHFEE-PFWIIDIPKGSREFYDREDPERPGVL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 162 VAAvDLLVP-GVGELFGGGLREERYHFLEERLARSGLT-EVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVI 239
Cdd:PRK06462 246 RNY-DLLLPeGYGEAVSGGEREYEYEEIVERIREHGVDpEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQ 324
|
....*.
gi 343098477 240 PFPRFP 245
Cdd:PRK06462 325 PFPRVP 330
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
1-246 |
9.28e-37 |
|
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: 134.18 E-value: 9.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 1 MSGAFTQVFTFGPTFRAENSQSRRHLAEFYMIEAEISFVDSlQDLMQVIEELFKATTMMVLSKCPEDVE-LCHKF-IAPG 78
Cdd:TIGR00458 195 MAAGFERVYEIGPIFRAEEHNTHRHLNEATSIDIEMAFEDH-HDVMDILEELVVRVFEDVPERCAHQLEtLEFKLeKPEG 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 79 QKDRLEhmlknnfliisYTEAVEILKQASQNFTftpeWGADLRTEHEKYLVKHCGNIpVFVINYPLTLKPFYMRDNEDGP 158
Cdd:TIGR00458 274 KFVRLT-----------YDEAIEMANAKGVEIG----WGEDLSTEAEKALGEEMDGL-YFITDWPTEIRPFYTMPDEDNP 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 159 QHTvAAVDLLVPGVgELFGGGLREERYHFLEERLARSGLT-EVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKD 237
Cdd:TIGR00458 338 EIS-KSFDLMYRDL-EISSGAQRIHLHDLLVERIKAKGLNpEGFKDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIRE 415
|
....*....
gi 343098477 238 VIPFPRFPH 246
Cdd:TIGR00458 416 AVLFPRDRK 424
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
2-248 |
2.56e-30 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 117.89 E-value: 2.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 2 SGAFTQVFTFGPTFRAENSQSRRHLAEFYMIEAEISFVDSLQDLMQVIEELFKATTMMVLSKCPEDVELC---HKFiapg 78
Cdd:PLN02850 288 CGDFRRVFEIGPVFRAEDSFTHRHLCEFTGLDLEMEIKEHYSEVLDVVDELFVAIFDGLNERCKKELEAIreqYPF---- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 79 qkDRLEHMLKNnfLIISYTEAVEILKQASqnftFTPEWGADLRTEHEKYL---VKHCGNIPVFVIN-YPLTLKPFYMRDN 154
Cdd:PLN02850 364 --EPLKYLPKT--LRLTFAEGIQMLKEAG----VEVDPLGDLNTESERKLgqlVKEKYGTDFYILHrYPLAVRPFYTMPC 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 155 EDGPQHTvAAVDLLVPGvGELFGGGLREERYHFLEERLARSGL-TEVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVD 233
Cdd:PLN02850 436 PDDPKYS-NSFDVFIRG-EEIISGAQRVHDPELLEKRAEECGIdVKTISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLN 513
|
250
....*....|....*
gi 343098477 234 NIKDVIPFPRFPHSC 248
Cdd:PLN02850 514 NIRKTSLFPRDPQRL 528
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
1-243 |
1.54e-23 |
|
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: 95.62 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 1 MSGAFTQVFTFGPTFRAENSqSRRHLAEFYMIEAEISFVDsLQDLMQVIEELFKATTMMVLSKcpEDVELCHKFIAPGQK 80
Cdd:cd00669 65 MVGGLDRVFEINRNFRNEDL-RARHQPEFTMMDLEMAFAD-YEDVIELTERLVRHLAREVLGV--TAVTYGFELEDFGLP 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 81 drlehmlknnFLIISYTEAVEILKQasqnftftpewgadlrtehekylvkhcgniPVFVINYPLTLKPFYMRDNEDGPQH 160
Cdd:cd00669 141 ----------FPRLTYREALERYGQ------------------------------PLFLTDYPAEMHSPLASPHDVNPEI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 161 TvAAVDLLVPGVgELFGGGLREERYHFLEERLARSGLTEVYQ-----WYLDLRRFGSVPHGGFGMGFERYLQCILGVDNI 235
Cdd:cd00669 181 A-DAFDLFINGV-EVGNGSSRLHDPDIQAEVFQEQGINKEAGmeyfeFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTI 258
|
....*...
gi 343098477 236 KDVIPFPR 243
Cdd:cd00669 259 REVIAFPK 266
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
1-246 |
6.87e-20 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 88.13 E-value: 6.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 1 MSGAFTQVFTFGPTFRAENSQSRRHLAEFYMIEAEISFVDSLQDLMQVIEELFKATTMMVLSKCPEDVELCHKF------ 74
Cdd:PTZ00401 275 LQGDVPRVFEVGPVFRSENSNTHRHLTEFVGLDVEMRINEHYYEVLDLAESLFNYIFERLATHTKELKAVCQQYpfeplv 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 75 --IAPGQKDRLE------------------HMLKNNFLIISYTEAVEILKQASQNfTFTPEwgADLRTEHEKYL---VKH 131
Cdd:PTZ00401 355 wkLTPERMKELGvgvisegveptdkyqarvHNMDSRMLRINYMHCIELLNTVLEE-KMAPT--DDINTTNEKLLgklVKE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 132 CGNIPVFVIN-YPLTLKPFYMRDNEDGPQHTvAAVDLLVPGvGELFGGGlreERYHFLEERLARSGLTEV----YQWYLD 206
Cdd:PTZ00401 432 RYGTDFFISDrFPSSARPFYTMECKDDERFT-NSYDMFIRG-EEISSGA---QRIHDPDLLLARAKMLNVdltpIKEYVD 506
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 343098477 207 LRRFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFPRFPH 246
Cdd:PTZ00401 507 SFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFPRDPQ 546
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
1-242 |
3.83e-15 |
|
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. AspRS is a homodimer, which attaches a specific amino acid to the 3' OH group of ribose of the appropriate tRNA. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. AspRS in this family differ from those found in the AsxRS family by a GAD insert in the core domain.
Pssm-ID: 238400 [Multi-domain] Cd Length: 280 Bit Score: 72.99 E-value: 3.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 1 MSGAFTQVFTFGPTFRAENSQSRRHlAEFYMIEAEISFVDSlQDLMQVIEELFkattmmvlskcpedvelCHKFiapgqK 80
Cdd:cd00777 65 MVSGFDRYFQIARCFRDEDLRADRQ-PEFTQIDIEMSFVDQ-EDIMSLIEGLL-----------------KYVF-----K 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 81 DRLEHMLKNNFLIISYTEAVEilkqasqNFTFTPEWGADL-----RTEHEKYLVKHcgnipvfvinYPLTL-KPFYMRDN 154
Cdd:cd00777 121 EVLGVELTTPFPRMTYAEAME-------RYGFKFLWIVDFplfewDEEEGRLVSAH----------HPFTApKEEDLDLL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 155 EDGPQHTVA-AVDLLVPGVgELFGGGLREERYHFLEERLARSGLTEVYQW-----YLDLRRFGSVPHGGFGMGFERYLQC 228
Cdd:cd00777 184 EKDPEDARAqAYDLVLNGV-ELGGGSIRIHDPDIQEKVFEILGLSEEEAEekfgfLLEAFKYGAPPHGGIALGLDRLVML 262
|
250
....*....|....
gi 343098477 229 ILGVDNIKDVIPFP 242
Cdd:cd00777 263 LTGSESIRDVIAFP 276
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
3-242 |
1.45e-10 |
|
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: 60.29 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 3 GAFTQVFTFGPTFRAEnSQSRRHLAEFYMIEAEISFVDsLQDLMQVIEELFKATTMMVLSKCP---EDVELChkFIAPGQ 79
Cdd:cd00775 74 GGFERVYEIGRNFRNE-GIDLTHNPEFTMIEFYEAYAD-YNDMMDLTEDLFSGLVKKINGKTKieyGGKELD--FTPPFK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 80 K----DRLEHMLKNNFLIISYTEAVEILKQASQNFTFTPEWG---ADLRTE-HEKYLVKHCGNiPVFVINYPLTLKPFYM 151
Cdd:cd00775 150 RvtmvDALKEKTGIDFPELDLEQPEELAKLLAKLIKEKIEKPrtlGKLLDKlFEEFVEPTLIQ-PTFIIDHPVEISPLAK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 152 RDNEDgpqhtvaavdllvPGVG---ELFGGGlRE-------------ERYHFLEE-RLARSGLTE--VYQW-YLDLRRFG 211
Cdd:cd00775 229 RHRSN-------------PGLTerfELFICG-KEianaytelndpfdQRERFEEQaKQKEAGDDEamMMDEdFVTALEYG 294
|
250 260 270
....*....|....*....|....*....|.
gi 343098477 212 SVPHGGFGMGFERYLQCILGVDNIKDVIPFP 242
Cdd:cd00775 295 MPPTGGLGIGIDRLVMLLTDSNSIRDVILFP 325
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
153-243 |
1.73e-07 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 51.71 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 153 DNEDGPQHTVAAVDLLVPGVgELFGGGLREERYHFLEERLARSGLT-----EVYQWYLDLRRFGSVPHGGFGMGFERYLQ 227
Cdd:PLN02903 526 DMGDLSSARALAYDMVYNGV-EIGGGSLRIYRRDVQQKVLEAIGLSpeeaeSKFGYLLEALDMGAPPHGGIAYGLDRLVM 604
|
90
....*....|....*.
gi 343098477 228 CILGVDNIKDVIPFPR 243
Cdd:PLN02903 605 LLAGAKSIRDVIAFPK 620
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
3-242 |
2.86e-07 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 50.83 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 3 GAFTQVFTFGPTFRAENSqSRRHLAEFYMIEAEISFVDsLQDLMQVIEELFKATTMMVLSKCPEDV-ELCHKFIAPGQKD 81
Cdd:PRK12445 250 GGFERVFEINRNFRNEGI-SVRHNPEFTMMELYMAYAD-YHDLIELTESLFRTLAQEVLGTTKVTYgEHVFDFGKPFEKL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 82 RLEHMLK-----NNFLIISYTEAVEILKQaSQNFTFTPEWG-ADLRTE-----HEKYLVKhcgniPVFVINYPLTLKPFy 150
Cdd:PRK12445 328 TMREAIKkyrpeTDMADLDNFDAAKALAE-SIGITVEKSWGlGRIVTEifdevAEAHLIQ-----PTFITEYPAEVSPL- 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 151 MRDNEDGPQHTvAAVDLLVPGvgELFGGGLRE------ERYHFLEERLARS-GLTEVYQW---YLDLRRFGSVPHGGFGM 220
Cdd:PRK12445 401 ARRNDVNPEIT-DRFEFFIGG--REIGNGFSElndaedQAERFQEQVNAKAaGDDEAMFYdedYVTALEYGLPPTAGLGI 477
|
250 260
....*....|....*....|..
gi 343098477 221 GFERYLQCILGVDNIKDVIPFP 242
Cdd:PRK12445 478 GIDRMIMLFTNSHTIRDVILFP 499
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
136-243 |
4.15e-06 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 47.29 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 136 PVFVINYPL-----------TLKPFYMRDNEDGPQHTVA--------AVDLLVPGvGELFGGGLREERYHFLEERLARSG 196
Cdd:PRK12820 443 PLWITDFPLfeatddggvtsSHHPFTAPDREDFDPGDIEelldlrsrAYDLVVNG-EELGGGSIRINDKDIQLRIFAALG 521
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 343098477 197 LTE-----VYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFPR 243
Cdd:PRK12820 522 LSEediedKFGFFLRAFDFAAPPHGGIALGLDRVVSMILQTPSIREVIAFPK 573
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
3-242 |
9.45e-06 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 46.24 E-value: 9.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 3 GAFTQVFTFGPTFRAENSqSRRHLAEFYMIEAEISFVDsLQDLMQVIEELFKATTMMVL--SKCP-EDVELchKFIAPGQ 79
Cdd:PRK00484 238 GGFERVYEIGRNFRNEGI-DTRHNPEFTMLEFYQAYAD-YNDMMDLTEELIRHLAQAVLgtTKVTyQGTEI--DFGPPFK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 80 K----DRLEHMLKNNFLIISYTEAVEILKQAsqNFTFTPEWGA----DLRTEH--EKYLVKhcgniPVFVINYPLTLKPF 149
Cdd:PRK00484 314 RltmvDAIKEYTGVDFDDMTDEEARALAKEL--GIEVEKSWGLgkliNELFEEfvEPKLIQ-----PTFITDYPVEISPL 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 150 YMRDNEDgpqhtvaavdllvPGVG---ELFGGGlRE---------------ERyhFLEE-RLARSGLTEVYQwyLD---L 207
Cdd:PRK00484 387 AKRHRED-------------PGLTerfELFIGG-REianafselndpidqrER--FEAQvEAKEAGDDEAMF--MDedfL 448
|
250 260 270
....*....|....*....|....*....|....*..
gi 343098477 208 R--RFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFP 242
Cdd:PRK00484 449 RalEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
3-242 |
1.10e-05 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 46.18 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 3 GAFTQVFTFGPTFRAENSqSRRHLAEFYMIEAEISFvDSLQDLMQVIEELFKATTMMV------------LSKCPEDVEL 70
Cdd:PTZ00385 299 GGMERIYEIGKVFRNEDA-DRSHNPEFTSCEFYAAY-HTYEDLMPMTEDIFRQLAMRVngttvvqiypenAHGNPVTVDL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 71 CHKFIAPGQKDRLEHMLK---------NNFLIISYTEAVEIlkqaSQNFTFTPEWGADLRTEH--EKYLVKHCGNiPVFV 139
Cdd:PTZ00385 377 GKPFRRVSVYDEIQRMSGvefpppnelNTPKGIAYMSVVML----RYNIPLPPVRTAAKMFEKliDFFITDRVVE-PTFV 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343098477 140 INYPLTLKPfymrdnedgpqhtVAAVDLLVPGVGE---LFGGGLR-----------EERYHFLEERLA-RSGLTE----V 200
Cdd:PTZ00385 452 MDHPLFMSP-------------LAKEQVSRPGLAErfeLFVNGIEycnayselndpHEQYHRFQQQLVdRQGGDEeampL 518
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 343098477 201 YQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFP 242
Cdd:PTZ00385 519 DETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFP 560
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
209-242 |
1.66e-04 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 42.36 E-value: 1.66e-04
10 20 30
....*....|....*....|....*....|....
gi 343098477 209 RFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFP 242
Cdd:PRK00476 523 KYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
209-242 |
3.07e-04 |
|
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439943 [Multi-domain] Cd Length: 589 Bit Score: 41.52 E-value: 3.07e-04
10 20 30
....*....|....*....|....*....|....
gi 343098477 209 RFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFP 242
Cdd:COG0173 522 KYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
|
|
| |
