|
Name |
Accession |
Description |
Interval |
E-value |
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
4-465 |
0e+00 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 844.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 4 MKRTKVVDAFDASLYGTKVNVKGWVRTRRGNKNVNFIAVNDGSTIKNIQVVVDLSKFSEAEMKPITTGACISVIGTLVES 83
Cdd:PRK03932 1 MMRVSIKDILKGKYVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDNGEEYFEEIKKLTTGSSVIVTGTVVES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 84 QGKGQQAEIQADSIELYGgADPDVYPLQKKGHTLEFLREIAHLRPRTNTFGAVLRIRHNMAYAIHKYFNDRGFFYLNTPL 163
Cdd:PRK03932 81 PRAGQGYELQATKIEVIG-EDPEDYPIQKKRHSIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVDTPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 164 ITGSDCEGAGAMFQVTTLDLnqvpktedgavDYSEDFFGKPTSLTVSGQLEGELGAMSLGAIYTFGPTFRAENSNTPRHL 243
Cdd:PRK03932 160 ITASDCEGAGELFRVTTLDL-----------DFSKDFFGKEAYLTVSGQLYAEAYAMALGKVYTFGPTFRAENSNTRRHL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 244 AEFWMVEPEVAFNEIGENMDLAEDFLKYLIRYALDHCQDDLEFLCQMYDKELIDRLKFVVDNDFVRLPYTEGVKILEESG 323
Cdd:PRK03932 229 AEFWMIEPEMAFADLEDNMDLAEEMLKYVVKYVLENCPDDLEFLNRRVDKGDIERLENFIESPFPRITYTEAIEILQKSG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 324 HKFEYPVYWGADLQSEHERFLVEEHFKKPVILTDYPKEIKAFYMKMNDDGKTVRAMDVLFPRIGEIIGGSQREENYDKLL 403
Cdd:PRK03932 309 KKFEFPVEWGDDLGSEHERYLAEEHFKKPVFVTNYPKDIKAFYMRLNPDGKTVAAMDLLAPGIGEIIGGSQREERLDVLE 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 749817351 404 ARIEELHIPMKDMWWYLDTRRFGTAPHSGFGLGFERLLLFVTGMTNIRDVIPFPRTPKNAEF 465
Cdd:PRK03932 389 ARIKELGLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
5-464 |
0e+00 |
|
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: 714.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 5 KRTKVVDAFdASLYGTKVNVKGWVRTRRGNKNVNFIAVNDGSTIknIQVVVDLSKFSE-AEMKPITTGACISVIGTLVES 83
Cdd:COG0017 1 KRTYIKDLL-PEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGF--IQVVVKKDKLENfEEAKKLTTESSVEVTGTVVES 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 84 QGKGQQAEIQADSIELYGGADpDVYPLQKKGHTLEFLREIAHLRPRTNTFGAVLRIRHNMAYAIHKYFNDRGFFYLNTPL 163
Cdd:COG0017 78 PRAPQGVELQAEEIEVLGEAD-EPYPLQPKRHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVEVHTPI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 164 ITGSDCEGAGAMFQVttldlnqvpktedgavdyseDFFGKPTSLTVSGQLEGELGAMSLGAIYTFGPTFRAENSNTPRHL 243
Cdd:COG0017 157 ITASATEGGGELFPV--------------------DYFGKEAYLTQSGQLYKEALAMALEKVYTFGPTFRAEKSNTRRHL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 244 AEFWMVEPEVAFNEIGENMDLAEDFLKYLIRYALDHCQDDLEFLCQMydkelIDRLKFVVDNDFVRLPYTEGVKILEESG 323
Cdd:COG0017 217 AEFWMIEPEMAFADLEDVMDLAEEMLKYIIKYVLENCPEELEFLGRD-----VERLEKVPESPFPRITYTEAIEILKKSG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 324 HKFEypvyWGADLQSEHERFLVEEHFKKPVILTDYPKEIKAFYMKMN-DDGKTVRAMDVLFPRIGEIIGGSQREENYDKL 402
Cdd:COG0017 292 EKVE----WGDDLGTEHERYLGEEFFKKPVFVTDYPKEIKAFYMKPNpDDPKTVAAFDLLAPGIGEIIGGSQREHRYDVL 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 749817351 403 LARIEELHIPMKDMWWYLDTRRFGTAPHSGFGLGFERLLLFVTGMTNIRDVIPFPRTPKNAE 464
Cdd:COG0017 368 VERIKEKGLDPEDYEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLT 429
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
19-465 |
0e+00 |
|
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: 671.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 19 GTKVNVKGWVRTRRGNKNVNFIAVNDGSTIKNIQVVVDLSK--FSEAEMKPITTGACISVIGTLVESQGKGQQAEIQADS 96
Cdd:TIGR00457 16 GDEVTVSGWVRTKRSSKKIIFLELNDGSSLGPIQAVINGEDnpYLFQLLKSLTTGSSVSVTGKVVESPGKGQPVELQVKK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 97 IELYGGADPDVYPLQKKGHTLEFLREIAHLRPRTNTFGAVLRIRHNMAYAIHKYFNDRGFFYLNTPLITGSDCEGAGAMF 176
Cdd:TIGR00457 96 IEVVGEAEPDDYPLQKKEHSLEFLRDIAHLRLRTNTLGAVMRVRNALSQAIHRYFQENGFTWVSPPILTSNDCEGAGELF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 177 QVTTldlnqvpktedGAVDYSEDFFGKPTSLTVSGQLEGELGAMSLGAIYTFGPTFRAENSNTPRHLAEFWMVEPEVAFN 256
Cdd:TIGR00457 176 RVST-----------GNIDFSQDFFGKEAYLTVSGQLYLETYALALSKVYTFGPTFRAEKSNTSRHLSEFWMIEPEMAFA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 257 EIGENMDLAEDFLKYLIRYALDHCQDDLEFLCQMYDKELIDRLKFVVDNDFVRLPYTEGVKILEESGHKFEYPVYWGADL 336
Cdd:TIGR00457 245 NLNDLLQLAETLIKYIIKAVLENCSQELKFLEKNFDKDLIKRLENIINNKFARITYTDAIEILKESDKNFEYEDFWGDDL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 337 QSEHERFLVEEHFKKPVILTDYPKEIKAFYMKMNDDGKTVRAMDVLFPRIGEIIGGSQREENYDKLLARIEELHIPMKDM 416
Cdd:TIGR00457 325 QTEHERFLAEEYFKPPVFVTNYPKDIKAFYMKLNDDGKTVAAMDLLAPGIGEIIGGSEREDDLDKLENRMKEMGLDTDAL 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 749817351 417 WWYLDTRRFGTAPHSGFGLGFERLLLFVTGMTNIRDVIPFPRTPKNAEF 465
Cdd:TIGR00457 405 NWYLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGNINF 453
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
2-465 |
0e+00 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 612.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 2 ETMKRTKVVDAFD-----ASLYGTKVNVKGWVRTRRGNKNVNFIAVNDGSTIKNIQVVVDLSK--FSEAEMKPITTGACI 74
Cdd:PLN02603 85 EFRKKLRIADVKGgedegLARVGKTLNVMGWVRTLRAQSSVTFIEVNDGSCLSNMQCVMTPDAegYDQVESGLITTGASV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 75 SVIGTLVESQGKGQQAEIQADSIELYGGADPDvYPLQKKGHTLEFLREIAHLRPRTNTFGAVLRIRHNMAYAIHKYFNDR 154
Cdd:PLN02603 165 LVQGTVVSSQGGKQKVELKVSKIVVVGKSDPS-YPIQKKRVSREFLRTKAHLRPRTNTFGAVARVRNALAYATHKFFQEN 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 155 GFFYLNTPLITGSDCEGAGAMFQVTTL----------DLNQVPKTEDGAVDYSEDFFGKPTSLTVSGQLEGELGAMSLGA 224
Cdd:PLN02603 244 GFVWVSSPIITASDCEGAGEQFCVTTLipnsaenggsLVDDIPKTKDGLIDWSQDFFGKPAFLTVSGQLNGETYATALSD 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 225 IYTFGPTFRAENSNTPRHLAEFWMVEPEVAFNEIGENMDLAEDFLKYLIRYALDHCQDDLEFLCQMYDKELIDRLKFVVD 304
Cdd:PLN02603 324 VYTFGPTFRAENSNTSRHLAEFWMIEPELAFADLNDDMACATAYLQYVVKYILENCKEDMEFFNTWIEKGIIDRLSDVVE 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 305 NDFVRLPYTEGVKILEESGHKFEYPVYWGADLQSEHERFLVEEHF-KKPVILTDYPKEIKAFYMKMNDDGKTVRAMDVLF 383
Cdd:PLN02603 404 KNFVQLSYTDAIELLLKAKKKFEFPVKWGLDLQSEHERYITEEAFgGRPVIIRDYPKEIKAFYMRENDDGKTVAAMDMLV 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 384 PRIGEIIGGSQREENYDKLLARIEELHIPMKDMWWYLDTRRFGTAPHSGFGLGFERLLLFVTGMTNIRDVIPFPRTPKNA 463
Cdd:PLN02603 484 PRVGELIGGSQREERLEYLEARLDELKLNKESYWWYLDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFPRVPGSA 563
|
..
gi 749817351 464 EF 465
Cdd:PLN02603 564 EF 565
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
15-465 |
0e+00 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 532.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 15 ASLYGTKVNVKGWVRTRR--GNKNVNFIAVNDGSTIKNIQVVVDLSKFSEAEMkpITTGACISVIGTL-VESQGKG--QQ 89
Cdd:PLN02221 46 AGLAGQKVRIGGWVKTGReqGKGTFAFLEVNDGSCPANLQVMVDSSLYDLSTL--VATGTCVTVDGVLkVPPEGKGtkQK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 90 AEIQADSIELYGGADPDVYPLQKKGHTLEFLREIAHLRPRTNTFGAVLRIRHNMAYAIHKYFNDRGFFYLNTPLITGSDC 169
Cdd:PLN02221 124 IELSVEKVIDVGTVDPTKYPLPKTKLTLEFLRDVLHLRSRTNSISAVARIRNALAFATHSFFQEHSFLYIHTPIITTSDC 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 170 EGAGAMFQVTTL---------DL-NQVPKTE------------------------------------------------- 190
Cdd:PLN02221 204 EGAGEMFQVTTLinyterleqDLiDNPPPTEadveaarlivkergevvaqlkaakaskeeitaavaelkiakeslahiee 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 191 -----------DGAVDYSEDFFGKPTSLTVSGQLEGELGAMSLGAIYTFGPTFRAENSNTPRHLAEFWMVEPEVAFNEIG 259
Cdd:PLN02221 284 rsklkpglpkkDGKIDYSKDFFGRQAFLTVSGQLQVETYACALSSVYTFGPTFRAENSHTSRHLAEFWMVEPEIAFADLE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 260 ENMDLAEDFLKYLIRYALDHCQDDLEFLCQMYDKELIDRLKFVVDNDFVRLPYTEGVKILEES---GHKFEYPVYWGADL 336
Cdd:PLN02221 364 DDMNCAEAYVKYMCKWLLDKCFDDMELMAKNFDSGCIDRLRMVASTPFGRITYTEAIELLEEAvakGKEFDNNVEWGIDL 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 337 QSEHERFLVEEHFKKPVILTDYPKEIKAFYMKMNDDGKTVRAMDVLFPRIGEIIGGSQREENYDKLLARIEELHIPMKDM 416
Cdd:PLN02221 444 ASEHERYLTEVLFQKPLIVYNYPKGIKAFYMRLNDDEKTVAAMDVLVPKVGELIGGSQREERYDVIKQRIEEMGLPIEPY 523
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 749817351 417 WWYLDTRRFGTAPHSGFGLGFERLLLFVTGMTNIRDVIPFPRTPKNAEF 465
Cdd:PLN02221 524 EWYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPRYPGKADL 572
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
22-465 |
1.59e-170 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 492.23 E-value: 1.59e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 22 VNVKGWVRTRR--GNKNVNFIAVNDGSTIKNIQVVVDLSKFSEAEMKPITTGACISVIGTLVES--QGKGQQAEIQAD-- 95
Cdd:PTZ00425 84 ITVCGWSKAVRkqGGGRFCFVNLNDGSCHLNLQIIVDQSIENYEKLLKCGVGCCFRFTGKLIISpvQNENKKGLLKENve 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 96 ---------SIELYG-GADPDVYPLQKKGHTLEFLREIAHLRPRTNTFGAVLRIRHNMAYAIHKYFNDRGFFYLNTPLIT 165
Cdd:PTZ00425 164 lalkdnsihNFEIYGeNLDPQKYPLSKKNHGKEFLREVAHLRPRSYFISSVIRIRNALAIATHLFFQSRGFLYIHTPLIT 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 166 GSDCEGAGAMFQVTTL-----DLNQVP----------KTEDGA----------------------------VDYSEDFFG 202
Cdd:PTZ00425 244 TSDCEGGGEMFTVTTLlgedaDYRAIPrvnkknkkgeKREDILntcnannnngnssssnavsspaypdqylIDYKKDFFS 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 203 KPTSLTVSGQLEGELGAMSLGAIYTFGPTFRAENSNTPRHLAEFWMVEPEVAFNEIGENMDLAEDFLKYLIRYALDHCQD 282
Cdd:PTZ00425 324 KQAFLTVSGQLSLENLCSSMGDVYTFGPTFRAENSHTSRHLAEFWMIEPEIAFADLYDNMELAESYIKYCIGYVLNNNFD 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 283 DLEFLCQMYDKELIDRLKFVVDNDFVRLPYTEGVKILEESGHKFEYPVYWGADLQSEHERFLVEEHFKKPVILTDYPKEI 362
Cdd:PTZ00425 404 DIYYFEENVETGLISRLKNILDEDFAKITYTNVIDLLQPYSDSFEVPVKWGMDLQSEHERFVAEQIFKKPVIVYNYPKDL 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 363 KAFYMKMNDDGKTVRAMDVLFPRIGEIIGGSQREENYDKLLARIEELHIPMKDMWWYLDTRRFGTAPHSGFGLGFERLLL 442
Cdd:PTZ00425 484 KAFYMKLNEDQKTVAAMDVLVPKIGEVIGGSQREDNLERLDKMIKEKKLNMESYWWYRQLRKFGSHPHAGFGLGFERLIM 563
|
490 500
....*....|....*....|...
gi 749817351 443 FVTGMTNIRDVIPFPRTPKNAEF 465
Cdd:PTZ00425 564 LVTGVDNIKDTIPFPRYPGHAEF 586
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
115-461 |
1.39e-149 |
|
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: 428.91 E-value: 1.39e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 115 HTLEFLREIAHLRPRTNTFGAVLRIRHNMAYAIHKYFNDRGFFYLNTPLITGSDCEGagamfqvttldlnqvpktedGAV 194
Cdd:cd00776 2 ANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEG--------------------GAE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 195 DYSEDFFGKPTSLTVSGQLEGELGAMSLGAIYTFGPTFRAENSNTPRHLAEFWMVEPEVAFNE-IGENMDLAEDFLKYLI 273
Cdd:cd00776 62 LFKVSYFGKPAYLAQSPQLYKEMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEdYNEVMDLIEELIKYIF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 274 RYALDHCQDDLEFLCQMYDKELIdrlkfvVDNDFVRLPYTEGVKILEEsgHKFEYPVYWGADLQSEHERFLVEEHFKKPV 353
Cdd:cd00776 142 KRVLERCAKELELVNQLNRELLK------PLEPFPRITYDEAIELLRE--KGVEEEVKWGEDLSTEHERLLGEIVKGDPV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 354 ILTDYPKEIKAFYMKMNDD-GKTVRAMDVLFPRIGEIIGGSQREENYDKLLARIEELHIPMKDMWWYLDTRRFGTAPHSG 432
Cdd:cd00776 214 FVTDYPKEIKPFYMKPDDDnPETVESFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGG 293
|
330 340
....*....|....*....|....*....
gi 749817351 433 FGLGFERLLLFVTGMTNIRDVIPFPRTPK 461
Cdd:cd00776 294 FGLGLERLVMWLLGLDNIREAILFPRDPK 322
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
29-459 |
1.67e-141 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 419.66 E-value: 1.67e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 29 RTRRGNKNVNFIAVNDGSTIKNIQVVVDLSKFSEAEMKPitTGACISVIGTLVE---SQGKgQQAEIQADSIELYGGADP 105
Cdd:PLN02532 127 KSAPPPPSVAYLLISDGSCVASLQVVVDSALAPLTQLMA--TGTCILAEGVLKLplpAQGK-HVIELEVEKILHIGTVDP 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 106 DVYPLQKKGHTLEFLREIAHLRPRTNTFGAVLRIRHNMAYAIHKYFNDRGFFYLNTPLITGSDCEGAGAMFQVTTL---- 181
Cdd:PLN02532 204 EKYPLSKKRLPLDMLRDFSHFRPRTTTVASVTRVRSALTHATHTFFQDHGFLYVQVPIITTTDATGFGEMFRVTTLlgks 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 182 -------------------------------------------------DL---NQV-------------PKTEDGAVDY 196
Cdd:PLN02532 284 ddkeekkpvhetegisleavkaaikektnlveelkrsesnrealvaaeqDLrktNQLasqleakeklktgTSVKADKLSF 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 197 SEDFFGKPTSLTVSGQLEGELGAMSLGAIYTFGPTFRAENSNTPRHLAEFWMVEPEVAFNEIGENMDLAEDFLKYLIRYA 276
Cdd:PLN02532 364 SKDFFSRPTYLTVSGRLHLESYACALGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAFSELEDAMNCAEDYFKFLCKWV 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 277 LDHCQDDLEFLCQMYDKELIDRLKFVVDNDFVRLPYTEGVKILEE-SGHKFEYPVYWGADLQSEHERFLVEEHFKKPVIL 355
Cdd:PLN02532 444 LENCSEDMKFVSKRIDKTISTRLEAIISSSLQRISYTEAVDLLKQaTDKKFETKPEWGIALTTEHLSYLADEIYKKPVII 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 356 TDYPKEIKAFYMKMNDDGKTVRAMDVLFPRIGEIIGGSQREENYDKLLARIEELHIPMKDMWWYLDTRRFGTAPHSGFGL 435
Cdd:PLN02532 524 YNYPKELKPFYVRLNDDGKTVAAFDLVVPKVGTVITGSQNEERMDILNARIEELGLPREQYEWYLDLRRHGTVKHSGFSL 603
|
490 500
....*....|....*....|....
gi 749817351 436 GFERLLLFVTGMTNIRDVIPFPRT 459
Cdd:PLN02532 604 GFELMVLFATGLPDVRDAIPFPRS 627
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
4-458 |
1.03e-81 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 259.35 E-value: 1.03e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 4 MKRTKVVDAFDASLYGTKVNVKGWVRTRRGNKNVNFIAVNDGSTIknIQVVVDLSKFSEAE--MKPITTGACISVIGTLV 81
Cdd:PRK05159 1 MMKRHLTSELTPELDGEEVTLAGWVHEIRDLGGIAFLILRDRSGI--IQVVVKKKVDEELFetIKKLKRESVVSVTGTVK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 82 ESQgkgqQA----EIQADSIELYGGADP----DVYplQKKGHTLEFLREIAHL---RPRTNtfgAVLRIRHNMAYAIHKY 150
Cdd:PRK05159 79 ANP----KApggvEVIPEEIEVLNKAEEplplDIS--GKVLAELDTRLDNRFLdlrRPRVR---AIFKIRSEVLRAFREF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 151 FNDRGFFYLNTPLITGSDCEGAGAMFqvttldlnqvpktedgAVDYsedfFGKPTSLTVSGQLEGE-LGAMSLGAIYTFG 229
Cdd:PRK05159 150 LYENGFTEIFTPKIVASGTEGGAELF----------------PIDY----FEKEAYLAQSPQLYKQmMVGAGFERVFEIG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 230 PTFRAENSNTPRHLAEFWMVEPEVAFNEiGEN--MDLAEDFLKYLIRYALDHCQDDLEFLcqmyDKELIdrlkfVVDNDF 307
Cdd:PRK05159 210 PVFRAEEHNTSRHLNEYTSIDVEMGFID-DHEdvMDLLENLLRYMYEDVAENCEKELELL----GIELP-----VPETPI 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 308 VRLPYTEGVKILEESGHKFEypvyWGADLQSEHERFL----VEEHFKKPVILTDYPKEIKAFY-MKMNDDGKTVRAMDVL 382
Cdd:PRK05159 280 PRITYDEAIEILKSKGNEIS----WGDDLDTEGERLLgeyvKEEYGSDFYFITDYPSEKRPFYtMPDEDDPEISKSFDLL 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 749817351 383 FPRIgEIIGGSQREENYDKLLARIEELHIPMKDMWWYLDTRRFGTAPHSGFGLGFERLLLFVTGMTNIRDVIPFPR 458
Cdd:PRK05159 356 FRGL-EITSGGQRIHRYDMLVESIKEKGLNPESFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFPR 430
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
125-460 |
1.61e-70 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 226.29 E-value: 1.61e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 125 HLRPRTNTFGAVLRIRHNMAYAIHKYFNDRGFFYLNTPLITGSDCEGAGAMFQVTTLDLNqvpktedgavdyseDFFgkp 204
Cdd:pfam00152 10 YLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALG--------------KFY--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 205 tSLTVSGQLEGELGAMS-LGAIYTFGPTFRAENSNTPRHLaEFWMVEPEVAFNEIGENMDLAEDFLKYLIRYALDHCQDd 283
Cdd:pfam00152 73 -ALPQSPQLYKQLLMVAgFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKE- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 284 leflcqMYDKELIDrlkfvVDNDFVRLPYTEGVKILEEsghkfEYPVYWGADLQSEHERFLVE----EHFKKPVILTDYP 359
Cdd:pfam00152 150 ------LEGGTLLD-----LKKPFPRITYAEAIEKLNG-----KDVEELGYGSDKPDLRFLLElvidKNKFNPLWVTDFP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 360 KEIKAFYMKMNDDGK-TVRAMDVLFPRIgEIIGGSQREENYDKLLARIEELHI----PMKDMWWYLDTRRFGTAPHSGFG 434
Cdd:pfam00152 214 AEHHPFTMPKDEDDPaLAEAFDLVLNGV-EIGGGSIRIHDPELQEERFEEQGLdpeeAEEKFGFYLDALKYGAPPHGGLG 292
|
330 340
....*....|....*....|....*.
gi 749817351 435 LGFERLLLFVTGMTNIRDVIPFPRTP 460
Cdd:pfam00152 293 IGLDRLVMLLTGLESIREVIAFPKTR 318
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
136-460 |
6.37e-57 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 191.39 E-value: 6.37e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 136 VLRIRHNMAYAIHKYFNDRGFFYLNTPLITGSDCEGAGamfqvttldlnqvPKTEDGAVDYSEDFFGKPTSLTVSGQLEG 215
Cdd:PRK06462 29 VLKVQSSILRYTREFLDGRGFVEVLPPIISPSTDPLMG-------------LGSDLPVKQISIDFYGVEYYLADSMILHK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 216 ELGAMSLGAIYTFGPTFRAEN--SNTPRHLAEFWMVEPEVAFNEIGENMDLAEDFLKYLIRYALDHCQDDLEFLcqmyDK 293
Cdd:PRK06462 96 QLALRMLGKIFYLSPNFRLEPvdKDTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHEDELEFF----GR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 294 ELiDRLKFvvdnDFVRLPYTEGVKILEESGHKFEyPVYwgaDLQSEHERFLvEEHFKKPVILTDYPKEIKAFYMKmNDDG 373
Cdd:PRK06462 172 DL-PHLKR----PFKRITHKEAVEILNEEGCRGI-DLE---ELGSEGEKSL-SEHFEEPFWIIDIPKGSREFYDR-EDPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 374 KT--VRAMDVLFP-RIGEIIGGSQREENYDKLLARIEELHIPMKDMWWYLDTRRFGTAPHSGFGLGFERLLLFVTGMTNI 450
Cdd:PRK06462 241 RPgvLRNYDLLLPeGYGEAVSGGEREYEYEEIVERIREHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHI 320
|
330
....*....|
gi 749817351 451 RDVIPFPRTP 460
Cdd:PRK06462 321 REVQPFPRVP 330
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
19-461 |
2.68e-52 |
|
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative asparaginyl-tRNA synthetases (asnS), archaeal/eukaryotic type aspartyl-tRNA synthetases (aspS_arch), and bacterial type aspartyl-tRNA synthetases (aspS_bact), there is a striking similarity between asnS and aspS_arch in gap pattern and in sequence, and a striking divergence of aspS_bact. Consequently, a separate model was built for each of the three groups. This model, aspS_arch, represents aspartyl-tRNA synthetases from the eukaryotic cytosol and from the Archaea. In some species, this enzyme aminoacylates tRNA for both Asp and Asn; Asp-tRNA(asn) is subsequently transamidated to Asn-tRNA(asn). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273087 [Multi-domain] Cd Length: 428 Bit Score: 181.95 E-value: 2.68e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 19 GTKVNVKGWVRTRRGNKNVNFIAVNDGSTIknIQVVVDlSKFSEAEM----KPITTGACISVIGTLVESQGKGQQAEIQA 94
Cdd:TIGR00458 12 GQEVTFMGWVHEIRDLGGLIFVLLRDREGL--IQITAP-AKKVSKNLfkwaKKLNLESVVAVRGIVKIKEKAPGGFEIIP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 95 DSIELYGGADP--DVYPLQKKGHTLEFLREIAHLRPRTNTFGAVLRIRHNMAYAIHKYFNDRGFFYLNTPLITGSDCEGA 172
Cdd:TIGR00458 89 TKIEVINEAKEplPLDPTEKVPAELDTRLDYRFLDLRRPTVQAIFRIRSGVLESVREFLAEEGFIEVHTPKLVASATEGG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 173 GAMFQVTtldlnqvpktedgavdysedFFGKPTSLTVSGQLEGE-LGAMSLGAIYTFGPTFRAENSNTPRHLAEFWMVEP 251
Cdd:TIGR00458 169 TELFPIT--------------------YFEREAFLGQSPQLYKQqLMAAGFERVYEIGPIFRAEEHNTHRHLNEATSIDI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 252 EVAFNEIGENMDLAEDFLKYLIRYALDHCQDDLEFLCQMYDKElidrlkfvvDNDFVRLPYTEGVKILEESGHkfeyPVY 331
Cdd:TIGR00458 229 EMAFEDHHDVMDILEELVVRVFEDVPERCAHQLETLEFKLEKP---------EGKFVRLTYDEAIEMANAKGV----EIG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 332 WGADLQSEHERFLVEEhFKKPVILTDYPKEIKAFY-MKMNDDGKTVRAMDvLFPRIGEIIGGSQREENYDKLLARIEELH 410
Cdd:TIGR00458 296 WGEDLSTEAEKALGEE-MDGLYFITDWPTEIRPFYtMPDEDNPEISKSFD-LMYRDLEISSGAQRIHLHDLLVERIKAKG 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 749817351 411 IPMKDMWWYLDTRRFGTAPHSGFGLGFERLLLFVTGMTNIRDVIPFPRTPK 461
Cdd:TIGR00458 374 LNPEGFKDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFPRDRK 424
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
10-461 |
3.49e-50 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 178.75 E-value: 3.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 10 VDAFDASLYGTKVNVKGWVRTRRGNKNVNFIAVND-GSTI------KNIQVVVDLSKFseaeMKPITTGACISVIGTLV- 81
Cdd:PLN02850 72 VSDLGEELAGSEVLIRGRVHTIRGKGKSAFLVLRQsGFTVqcvvfvSEVTVSKGMVKY----AKQLSRESVVDVEGVVSv 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 82 ---ESQGKGQQAEIQADSIELYGGADP--------------DVYPLQKKGHtlEFLREIAHLRP-------RTNTFGAVL 137
Cdd:PLN02850 148 pkkPVKGTTQQVEIQVRKIYCVSKALAtlpfnvedaarsesEIEKALQTGE--QLVRVGQDTRLnnrvldlRTPANQAIF 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 138 RIRHNMAYAIHKYFNDRGFFYLNTP-LITGSDcEGAGAMFQVttldlnqvpktedgavdyseDFFGKPTSLTVSGQLEGE 216
Cdd:PLN02850 226 RIQSQVCNLFREFLLSKGFVEIHTPkLIAGAS-EGGSAVFRL--------------------DYKGQPACLAQSPQLHKQ 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 217 LGAMS-LGAIYTFGPTFRAENSNTPRHLAEFWMVEPEVAFNE-IGENMDLAEDFLKYLIRYALDHCQDDLEFLCQMYDKE 294
Cdd:PLN02850 285 MAICGdFRRVFEIGPVFRAEDSFTHRHLCEFTGLDLEMEIKEhYSEVLDVVDELFVAIFDGLNERCKKELEAIREQYPFE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 295 lidRLKFVvdNDFVRLPYTEGVKILEESGHKFEyPVywgADLQSEHERFL---VEEHFKKPV-ILTDYPKEIKAFY-MKM 369
Cdd:PLN02850 365 ---PLKYL--PKTLRLTFAEGIQMLKEAGVEVD-PL---GDLNTESERKLgqlVKEKYGTDFyILHRYPLAVRPFYtMPC 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 370 NDDGKTVRAMDVlFPRIGEIIGGSQREENYDKLLARIEELHIPMKDMWWYLDTRRFGTAPHSGFGLGFERLLLFVTGMTN 449
Cdd:PLN02850 436 PDDPKYSNSFDV-FIRGEEIISGAQRVHDPELLEKRAEECGIDVKTISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNN 514
|
490
....*....|..
gi 749817351 450 IRDVIPFPRTPK 461
Cdd:PLN02850 515 IRKTSLFPRDPQ 526
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
21-101 |
4.32e-36 |
|
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli asparaginyl-tRNA synthetase (AsnRS) and, in Arabidopsis thaliana and Saccharomyces cerevisiae mitochondrial (mt) AsnRS. This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. S. cerevisiae mtAsnRS can charge E.coli tRNA with asparagines. Mutations in the gene for S. cerevisiae mtAsnRS has been found to induce a "petite" phenotype typical for a mutation in a nuclear gene that results in a non-functioning mitochondrial protein synthesis system.
Pssm-ID: 239813 [Multi-domain] Cd Length: 82 Bit Score: 128.07 E-value: 4.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 21 KVNVKGWVRTRRGNKNVNFIAVNDGSTIKNIQVVVDLSKFSEAEMKPITTGACISVIGTLVESQGKGQQAEIQADSIELY 100
Cdd:cd04318 1 EVTVNGWVRSVRDSKKISFIELNDGSCLKNLQVVVDKELTNFKEILKLSTGSSIRVEGVLVKSPGAKQPFELQAEKIEVL 80
|
.
gi 749817351 101 G 101
Cdd:cd04318 81 G 81
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
129-461 |
1.81e-33 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 132.81 E-value: 1.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 129 RTNTFGAVLRIRHNMAYAIHKYFNDRGFFYLNTPLITGSDCEGAGAMFQVttldlnqvpktedgavdyseDFFGKPTSLT 208
Cdd:PTZ00401 205 RTPASGAIFRLQSRVCQYFRQFLIDSDFCEIHSPKIINAPSEGGANVFKL--------------------EYFNRFAYLA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 209 VSGQLEGELGAM-SLGAIYTFGPTFRAENSNTPRHLAEFWMVEPEVAFNE-IGENMDLAEDFLKYLIRYALDHCQDdLEF 286
Cdd:PTZ00401 265 QSPQLYKQMVLQgDVPRVFEVGPVFRSENSNTHRHLTEFVGLDVEMRINEhYYEVLDLAESLFNYIFERLATHTKE-LKA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 287 LCQMYD-------------KEL-----------IDRLKFVVDN---DFVRLPYTEGVKILEESghkFEYPVYWGADLQSE 339
Cdd:PTZ00401 344 VCQQYPfeplvwkltpermKELgvgvisegvepTDKYQARVHNmdsRMLRINYMHCIELLNTV---LEEKMAPTDDINTT 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 340 HERFL---VEEHFKKPVILTD-YPKEIKAFY-MKMNDDGKTVRAMDvLFPRIGEIIGGSQREENYDKLLARIEELHI--- 411
Cdd:PTZ00401 421 NEKLLgklVKERYGTDFFISDrFPSSARPFYtMECKDDERFTNSYD-MFIRGEEISSGAQRIHDPDLLLARAKMLNVdlt 499
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 749817351 412 PMKDmwwYLDTRRFGTAPHSGFGLGFERLLLFVTGMTNIRDVIPFPRTPK 461
Cdd:PTZ00401 500 PIKE---YVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFPRDPQ 546
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
137-459 |
4.48e-32 |
|
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: 123.36 E-value: 4.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 137 LRIRHNMAYAIHKYFNDRGFFYLNTPLITGSDCEGAGAMFQVTTLDLNqvpktEDGAVDYSEDFFGKptSLTVSGqlege 216
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALG-----LDYYLRISPQLFKK--RLMVGG----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 217 lgamsLGAIYTFGPTFRAEnSNTPRHLAEFWMVEPEVAFNEIGENMDLAEDFLKYLIRYALDHCQDDLEFlcqmydkELI 296
Cdd:cd00669 69 -----LDRVFEINRNFRNE-DLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYGF-------ELE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 297 DRLKfvvdnDFVRLPYTEGVKILeesghkfeypvywgadlqseherflveehfKKPVILTDYPKEIKAFYMKMNDDGKTV 376
Cdd:cd00669 136 DFGL-----PFPRLTYREALERY------------------------------GQPLFLTDYPAEMHSPLASPHDVNPEI 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 377 -RAMDvLFPRIGEIIGGSQREENYDKLLARIEELHI----PMKDMWWYLDTRRFGTAPHSGFGLGFERLLLFVTGMTNIR 451
Cdd:cd00669 181 aDAFD-LFINGVEVGNGSSRLHDPDIQAEVFQEQGInkeaGMEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIR 259
|
....*...
gi 749817351 452 DVIPFPRT 459
Cdd:cd00669 260 EVIAFPKM 267
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
21-101 |
1.50e-18 |
|
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. Class 2b aaRSs include the homodimeric aspartyl-, asparaginyl-, and lysyl-tRNA synthetases (AspRS, AsnRS, and LysRS). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Included in this group are archeal and archeal-like AspRSs which are non-discriminating and can charge both tRNAAsp and tRNAAsn. E. coli cells have two isoforms of LysRSs (LysS and LysU) encoded by two distinct genes, which are differentially regulated. The cytoplasmic and the mitochondrial isoforms of human LysRS are encoded by a single gene. Yeast cytoplasmic and mitochondrial LysRSs participate in mitochondrial import of cytoplasmic tRNAlysCUU. In addition to their housekeeping role, human LysRS may function as a signaling molecule that activates immune cells. Tomato LysRS may participate in a process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging. AsnRS is immunodominant antigen of the filarial nematode Brugia malayai and is of interest as a target for anti-parasitic drug design. Human AsnRS has been shown to be a pro-inflammatory chemokine which interacts with CCR3 chemokine receptors on T cells, immature dendritic cells and macrophages.
Pssm-ID: 239766 [Multi-domain] Cd Length: 85 Bit Score: 79.92 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 21 KVNVKGWVRTRRGNKNVNFIAVNDGSTIknIQVVVDLSKFSE--AEMKPITTGACISVIGTLVESQG---KGQQAEIQAD 95
Cdd:cd04100 1 EVTLAGWVHSRRDHGGLIFIDLRDGSGI--VQVVVNKEELGEffEEAEKLRTESVVGVTGTVVKRPEgnlATGEIELQAE 78
|
....*.
gi 749817351 96 SIELYG 101
Cdd:cd04100 79 ELEVLS 84
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
137-459 |
3.87e-17 |
|
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: 81.47 E-value: 3.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 137 LRIRHNMAYAIHKYFNDRGFFYLNTPLITGSdcegagamfqvttldlnqvpkTEDGAVDY---SEDFFGKPTSLTVSGQL 213
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKS---------------------TPEGARDFlvpSRLHPGKFYALPQSPQL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 214 EGELGAMS-LGAIYTFGPTFRAENSNTPRHlAEFWMVEPEVAFNEIGENMDLAEDFLKYLIRYALDHcqDDLEFLCQMYD 292
Cdd:cd00777 60 FKQLLMVSgFDRYFQIARCFRDEDLRADRQ-PEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLGV--ELTTPFPRMTY 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 293 KELIDR--LKFVVDNDFVRLPYTEGVKILEESGHKFEYPvywgadlQSEHERFLVEEhfkkpviltdyPKEIKAfymkmn 370
Cdd:cd00777 137 AEAMERygFKFLWIVDFPLFEWDEEEGRLVSAHHPFTAP-------KEEDLDLLEKD-----------PEDARA------ 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 371 ddgktvRAMDVLFPRIgEIIGGSQREENYDkLLARI-EELHIPMKDMW----WYLDTRRFGTAPHSGFGLGFERLLLFVT 445
Cdd:cd00777 193 ------QAYDLVLNGV-ELGGGSIRIHDPD-IQEKVfEILGLSEEEAEekfgFLLEAFKYGAPPHGGIALGLDRLVMLLT 264
|
330
....*....|....
gi 749817351 446 GMTNIRDVIPFPRT 459
Cdd:cd00777 265 GSESIRDVIAFPKT 278
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
3-172 |
5.07e-11 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 64.70 E-value: 5.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 3 TMKRTKVVDAFDASLYGTKVNVKGWVRTRRGNKNVNFIAVNDGSTIknIQVVVDLSK--FSEAEmkPITTGACISVIGTl 80
Cdd:PRK00476 1 HMMRTHYCGELRESHVGQTVTLCGWVHRRRDHGGLIFIDLRDREGI--VQVVFDPDAeaFEVAE--SLRSEYVIQVTGT- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 81 VESQGKGQ--------QAEIQADSIELYGGADPDVYPLQKKGHTLE-------FL---REIAHLRprtntfgavLRIRHN 142
Cdd:PRK00476 76 VRARPEGTvnpnlptgEIEVLASELEVLNKSKTLPFPIDDEEDVSEelrlkyrYLdlrRPEMQKN---------LKLRSK 146
|
170 180 190
....*....|....*....|....*....|
gi 749817351 143 MAYAIHKYFNDRGFFYLNTPLITGSDCEGA 172
Cdd:PRK00476 147 VTSAIRNFLDDNGFLEIETPILTKSTPEGA 176
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
225-457 |
1.21e-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: 62.60 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 225 IYTFGPTFRAENSNTpRHLAEFWMVEPEVAFNEIGENMDLAEDFLKYLIryalDHCQDDLEFlcqMYDKELID------R 298
Cdd:cd00775 79 VYEIGRNFRNEGIDL-THNPEFTMIEFYEAYADYNDMMDLTEDLFSGLV----KKINGKTKI---EYGGKELDftppfkR 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 299 LKFV--------VDNDFVRLPYT-EGVKILEES-GHKFEYPVYWGADLQSEHERFlVEEHFKKPVILTDYPKEIKAFyMK 368
Cdd:cd00775 151 VTMVdalkektgIDFPELDLEQPeELAKLLAKLiKEKIEKPRTLGKLLDKLFEEF-VEPTLIQPTFIIDHPVEISPL-AK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 369 MNDD--GKTVRAMdvLFPRIGEIIGG--------SQREENYDKLLARI---EELHIPMKDmwwYLDTRRFGTAPHSGFGL 435
Cdd:cd00775 229 RHRSnpGLTERFE--LFICGKEIANAytelndpfDQRERFEEQAKQKEagdDEAMMMDED---FVTALEYGMPPTGGLGI 303
|
250 260
....*....|....*....|..
gi 749817351 436 GFERLLLFVTGMTNIRDVIPFP 457
Cdd:cd00775 304 GIDRLVMLLTDSNSIRDVILFP 325
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
22-99 |
2.46e-10 |
|
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic acids. The family includes the anti-codon binding domain of lysyl, aspartyl, and asparaginyl -tRNA synthetases (See pfam00152). Aminoacyl-tRNA synthetases catalyze the addition of an amino acid to the appropriate tRNA molecule EC:6.1.1.-. This family also includes part of RecG helicase involved in DNA repair. Replication factor A is a hetero-trimeric complex, that contains a subunit in this family. This domain is also found at the C-terminus of bacterial DNA polymerase III alpha chain.
Pssm-ID: 460164 [Multi-domain] Cd Length: 75 Bit Score: 56.47 E-value: 2.46e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 749817351 22 VNVKGWV-RTRRGNKNVNFIAVNDGSTIknIQVVVDlSKFSEAEMKPITTGACISVIGTLVESQGKGqqAEIQADSIEL 99
Cdd:pfam01336 1 VTVAGRVtSIRRSGGKLLFLTLRDGTGS--IQVVVF-KEEAEKLAKKLKEGDVVRVTGKVKKRKGGE--LELVVEEIEL 74
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
225-457 |
3.87e-09 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 58.56 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 225 IYTFGPTFRAENSNTpRHLAEFWMVEPEVAFNEIGENMDLAEDflkyLIRYALDHCQDDLEFlcqMYDKELID------R 298
Cdd:PRK00484 243 VYEIGRNFRNEGIDT-RHNPEFTMLEFYQAYADYNDMMDLTEE----LIRHLAQAVLGTTKV---TYQGTEIDfgppfkR 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 299 LKFV------VDNDFVRLPYTEGVKILEEsgHKFEYPVYWG-ADLQSEHERFLVEEHFKKPVILTDYPKEIK--AfymKM 369
Cdd:PRK00484 315 LTMVdaikeyTGVDFDDMTDEEARALAKE--LGIEVEKSWGlGKLINELFEEFVEPKLIQPTFITDYPVEISplA---KR 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 370 NDDGktvramdvlfPRIGE----IIGGS--------------QREenydKLLARIEElhipmKDM---------WWYLDT 422
Cdd:PRK00484 390 HRED----------PGLTErfelFIGGReianafselndpidQRE----RFEAQVEA-----KEAgddeamfmdEDFLRA 450
|
250 260 270
....*....|....*....|....*....|....*
gi 749817351 423 RRFGTAPHSGFGLGFERLLLFVTGMTNIRDVIPFP 457
Cdd:PRK00484 451 LEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
4-172 |
1.91e-08 |
|
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: 56.55 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 4 MKRTKVVDAFDASLYGTKVNVKGWVRTRRGNKNVNFIAVNDGSTIknIQVVVDLSKFSEA--EMKPITTGACISVIGTlV 81
Cdd:COG0173 1 MYRTHYCGELRESDVGQEVTLSGWVHRRRDHGGLIFIDLRDRYGI--TQVVFDPDDSAEAfeKAEKLRSEYVIAVTGK-V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 82 ESQGKGQ--------QAEIQADSIELYGGADPDVYPLQKKGHTLEFLReiahLRP-----RTNTFGAVLRIRHNMAYAIH 148
Cdd:COG0173 78 RARPEGTvnpklptgEIEVLASELEILNKAKTPPFQIDDDTDVSEELR----LKYryldlRRPEMQKNLILRHKVTKAIR 153
|
170 180
....*....|....*....|....
gi 749817351 149 KYFNDRGFFYLNTPLITGSDCEGA 172
Cdd:COG0173 154 NYLDENGFLEIETPILTKSTPEGA 177
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
21-457 |
4.62e-08 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 55.45 E-value: 4.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 21 KVNVKGWVRTRRGNKNVNFIAVNDGStiKNIQVVVDLSKFSEA----EMKPITTGACISVIGTLVESQGKgqQAEIQADS 96
Cdd:PRK12445 67 EVSVAGRMMTRRIMGKASFVTLQDVG--GRIQLYVARDSLPEGvyndQFKKWDLGDIIGARGTLFKTQTG--ELSIHCTE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 97 IELYGGAdpdVYPLQKKGHTLE---------FLREIAHLRPRtNTFgavlRIRHNMAYAIHKYFNDRGFFYLNTPL---I 164
Cdd:PRK12445 143 LRLLTKA---LRPLPDKFHGLQdqevryrqrYLDLIANDKSR-QTF----VVRSKILAAIRQFMVARGFMEVETPMmqvI 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 165 TGsdceGAGAMFQVT---TLDLnqvpkteDGAVDYSEDFFGKptSLTVSGqlegelgamsLGAIYTFGPTFRAENSNTpR 241
Cdd:PRK12445 215 PG----GASARPFIThhnALDL-------DMYLRIAPELYLK--RLVVGG----------FERVFEINRNFRNEGISV-R 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 242 HLAEFWMVEPEVAFNEIGENMDLAEDFLKYLIRYAL--------DHCQDDLEFLCQMYDKELIDrlKFVVDNDFVRLPYT 313
Cdd:PRK12445 271 HNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLgttkvtygEHVFDFGKPFEKLTMREAIK--KYRPETDMADLDNF 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 314 EGVKILEES-GHKFEYPvyWG-ADLQSEHERFLVEEHFKKPVILTDYPKEIKAFyMKMNDDGKTV----------RAMDV 381
Cdd:PRK12445 349 DAAKALAESiGITVEKS--WGlGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPL-ARRNDVNPEItdrfeffiggREIGN 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 749817351 382 LFPRIGEIIGGSQR-EENYDKLLARIEELHIPMKDmwwYLDTRRFGTAPHSGFGLGFERLLLFVTGMTNIRDVIPFP 457
Cdd:PRK12445 426 GFSELNDAEDQAERfQEQVNAKAAGDDEAMFYDED---YVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
137-457 |
1.23e-07 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 54.27 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 137 LRIRHNMAYAIHKYFNDRGFFYLNTPLITgSDCEGAGAMFQVTTLDLNQVpktedgavdyseDFFgkptsLTVSGQL--- 213
Cdd:PTZ00385 233 IKKRHVMLQALRDYFNERNFVEVETPVLH-TVASGANAKSFVTHHNANAM------------DLF-----LRVAPELhlk 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 214 EGELGAMSlgAIYTFGPTFRAENSNTpRHLAEFWMVEPEVAFNEIGENMDLAEDFLKYLIRYALDHCQddLEFLCQ---- 289
Cdd:PTZ00385 295 QCIVGGME--RIYEIGKVFRNEDADR-SHNPEFTSCEFYAAYHTYEDLMPMTEDIFRQLAMRVNGTTV--VQIYPEnahg 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 290 ---------------MYDK-ELIDRLKFVVDNDFVR---LPYTEGVKILeesgHKFEYP-VYWGADLQSEHERFLVEEHF 349
Cdd:PTZ00385 370 npvtvdlgkpfrrvsVYDEiQRMSGVEFPPPNELNTpkgIAYMSVVMLR----YNIPLPpVRTAAKMFEKLIDFFITDRV 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 350 KKPVILTDYPkeikafyMKMNDDGKTVRAMDVLFPRIGEIIGGSQREENYDKLLARIEELH----------------IPM 413
Cdd:PTZ00385 446 VEPTFVMDHP-------LFMSPLAKEQVSRPGLAERFELFVNGIEYCNAYSELNDPHEQYHrfqqqlvdrqggdeeaMPL 518
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 749817351 414 KDMwwYLDTRRFGTAPHSGFGLGFERLLLFVTGMTNIRDVIPFP 457
Cdd:PTZ00385 519 DET--FLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFP 560
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
21-126 |
1.97e-07 |
|
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus horikoshii AsnRS asparaginyl-tRNA synthetase (AsnRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The archeal enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose.
Pssm-ID: 239814 [Multi-domain] Cd Length: 103 Bit Score: 49.06 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 21 KVNVKGWVRTRRGNKNVNFIAVNDGSTIknIQVVVDLSKFSEA--EMKPITTGACISVIGTLVESQGKGQQAEIQADSIE 98
Cdd:cd04319 1 KVTLAGWVYRKREVGKKAFIVLRDSTGI--VQAVFSKDLNEEAyrEAKKVGIESSVIVEGAVKADPRAPGGAEVHGEKLE 78
|
90 100
....*....|....*....|....*...
gi 749817351 99 LYGGADPdvYPLQKKGHTlEFLREIAHL 126
Cdd:cd04319 79 IIQNVEF--FPITEDASD-EFLLDVRHL 103
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
420-459 |
2.43e-07 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 53.15 E-value: 2.43e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 749817351 420 LDTRRFGTAPHSGFGLGFERLLLFVTGMTNIRDVIPFPRT 459
Cdd:PRK00476 519 LDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFPKT 558
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
21-101 |
4.12e-07 |
|
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and Saccharomyces cerevisiae cytoplasmic asparaginyl-tRNA synthetase (AsnRS), in Brugia malayai AsnRs and, in various putative bacterial AsnRSs. This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. AsnRS is immunodominant antigen of the filarial nematode B. malayai and of interest as a target for anti-parasitic drug design. Human AsnRS has been shown to be a pro-inflammatory chemokine which interacts with CCR3 chemokine receptors on T cells, immature dendritic cells and macrophages.
Pssm-ID: 239818 [Multi-domain] Cd Length: 84 Bit Score: 47.61 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 21 KVNVKGWVRTRRGNKNVNFIAVNDGSTIknIQVVV---DLSKFSEAemKPITTGACISVIGTLVESQgKGQQA----EIQ 93
Cdd:cd04323 1 RVKVFGWVHRLRSQKKLMFLVLRDGTGF--LQCVLskkLVTEFYDA--KSLTQESSVEVTGEVKEDP-RAKQApggyELQ 75
|
....*...
gi 749817351 94 ADSIELYG 101
Cdd:cd04323 76 VDYLEIIG 83
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
19-278 |
1.70e-06 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 50.56 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 19 GTKVNVKGWVRTRRGNKNVNFIAVNDGSTIknIQVVVDLSKFSEA---------EMKPITTGACISVIGTLVESQGKGQQ 89
Cdd:PLN02903 72 GSRVTLCGWVDLHRDMGGLTFLDVRDHTGI--VQVVTLPDEFPEAhrtanrlrnEYVVAVEGTVRSRPQESPNKKMKTGS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 90 AEIQADSIE-----------LYGGADpDVYPLQKKGHTLEFlreiAHLRPRTNTFGAVLRIRHNMAYAIHKYFNDR-GFF 157
Cdd:PLN02903 150 VEVVAESVDilnvvtkslpfLVTTAD-EQKDSIKEEVRLRY----RVLDLRRPQMNANLRLRHRVVKLIRRYLEDVhGFV 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 158 YLNTPLITGSdcegagamfqvttldlnqvpkTEDGAVDY-------SEDFFGKPTS-------LTVSGqlegelgamsLG 223
Cdd:PLN02903 225 EIETPILSRS---------------------TPEGARDYlvpsrvqPGTFYALPQSpqlfkqmLMVSG----------FD 273
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 749817351 224 AIYTFGPTFRAENSNTPRHlAEFWMVEPEVAFNEIGENMDLAEDflkyLIRYALD 278
Cdd:PLN02903 274 RYYQIARCFRDEDLRADRQ-PEFTQLDMELAFTPLEDMLKLNED----LIRQVFK 323
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
17-457 |
1.83e-06 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 50.39 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 17 LYGTKVNVKGWVR--TRRGNKNVNFIAVNDGStikNIQVVVDL-------SKFSEAEMKpITTGACISVIGTLVESQgKG 87
Cdd:PTZ00417 130 LEDTILNVTGRIMrvSASGQKLRFFDLVGDGA---KIQVLANFafhdhtkSNFAECYDK-IRRGDIVGIVGFPGKSK-KG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 88 QQAEIQADSIEL----------YGGADPDVYPLQKkghtleFLREIAHLRPRTnTFgavlRIRHNMAYAIHKYFNDRGFF 157
Cdd:PTZ00417 205 ELSIFPKETIILspclhmlpmkYGLKDTEIRYRQR------YLDLMINESTRS-TF----ITRTKIINYLRNFLNDRGFI 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 158 YLNTP---LITGsdceGAGAMFQVT-----TLDLNQVPKTEdgavdysedffgKPTSLTVSGQLEgelgamslgAIYTFG 229
Cdd:PTZ00417 274 EVETPtmnLVAG----GANARPFIThhndlDLDLYLRIATE------------LPLKMLIVGGID---------KVYEIG 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 230 PTFRAEN-SNTprHLAEFWMVEPEVAFNEIGENMDLAEDFLK---------YLIRYALDHCQDD---LEFLCQMYDKELI 296
Cdd:PTZ00417 329 KVFRNEGiDNT--HNPEFTSCEFYWAYADFYDLIKWSEDFFSqlvmhlfgtYKILYNKDGPEKDpieIDFTPPYPKVSIV 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 297 DRLKFVVdNDFVRLPY------TEGVKILEEsgHKFEYPVYWGA----DLQSEHerFLVEEHFKKPVILTDYPKeikafy 366
Cdd:PTZ00417 407 EELEKLT-NTKLEQPFdspetiNKMINLIKE--NKIEMPNPPTAakllDQLASH--FIENKYPNKPFFIIEHPQ------ 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 367 mKMNDDGKTVRAMDVLFPRIGEIIGGSQREENYDKL---LARIEELHIPMKDM-----------WWYLDTRRFGTAPHSG 432
Cdd:PTZ00417 476 -IMSPLAKYHRSKPGLTERLEMFICGKEVLNAYTELndpFKQKECFSAQQKDRekgdaeafqfdAAFCTSLEYGLPPTGG 554
|
490 500
....*....|....*....|....*
gi 749817351 433 FGLGFERLLLFVTGMTNIRDVIPFP 457
Cdd:PTZ00417 555 LGLGIDRITMFLTNKNCIKDVILFP 579
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
424-459 |
2.22e-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: 50.00 E-value: 2.22e-06
10 20 30
....*....|....*....|....*....|....*.
gi 749817351 424 RFGTAPHSGFGLGFERLLLFVTGMTNIRDVIPFPRT 459
Cdd:COG0173 522 KYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFPKT 557
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
420-459 |
1.25e-05 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 47.86 E-value: 1.25e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 749817351 420 LDTRRFGTAPHSGFGLGFERLLLFVTGMTNIRDVIPFPRT 459
Cdd:PLN02903 582 LEALDMGAPPHGGIAYGLDRLVMLLAGAKSIRDVIAFPKT 621
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
19-121 |
7.00e-05 |
|
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli aspartyl-tRNA synthetase (AspRS), the human mitochondrial (mt) AspRS-2, the discriminating (D) Thermus thermophilus AspRS-1, and the nondiscriminating (ND) Helicobacter pylori AspRS. These homodimeric enzymes are class2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. Human mtAspRS participates in mitochondrial biosynthesis; this enzyme been shown to charge E.coli native tRNAsp in addition to in vitro transcribed human mitochondrial tRNAsp. T. thermophilus is rare among bacteria in having both a D_AspRS and a ND_AspRS. H.pylori ND-AspRS can charge both tRNAASp and tRNAAsn, it is fractionally more efficient at aminoacylating tRNAAsp over tRNAAsn. The H.pylori genome does not contain AsnRS.
Pssm-ID: 239812 [Multi-domain] Cd Length: 135 Bit Score: 42.51 E-value: 7.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 19 GTKVNVKGWVRTRRGNKNVNFIAVNDGSTIknIQVVVDLSKFSE-AEMKPITTGACISVIGTlVESQGKGQ--------Q 89
Cdd:cd04317 14 GQEVTLCGWVQRRRDHGGLIFIDLRDRYGI--VQVVFDPEEAPEfELAEKLRNESVIQVTGK-VRARPEGTvnpklptgE 90
|
90 100 110
....*....|....*....|....*....|..
gi 749817351 90 AEIQADSIELYGGADPDVYPLQKKGHTLEFLR 121
Cdd:cd04317 91 IEVVASELEVLNKAKTLPFEIDDDVNVSEELR 122
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
425-457 |
5.01e-04 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 42.67 E-value: 5.01e-04
10 20 30
....*....|....*....|....*....|...
gi 749817351 425 FGTAPHSGFGLGFERLLLFVTGMTNIRDVIPFP 457
Cdd:PLN02502 515 YGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFP 547
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
419-457 |
8.06e-04 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 41.87 E-value: 8.06e-04
10 20 30
....*....|....*....|....*....|....*....
gi 749817351 419 YLDTRRFGTAPHSGFGLGFERLLLFVTGmTNIRDVIPFP 457
Cdd:PRK02983 1051 FLQALEYAMPPTGGLGMGVDRLVMLLTG-RSIRETLPFP 1088
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
139-278 |
3.49e-03 |
|
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.
Pssm-ID: 238391 [Multi-domain] Cd Length: 211 Bit Score: 38.64 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749817351 139 IRHNMAYAIHKYFNDRGFFYLNTPLITG-SDCEGAGAMFQVTTldlnqvpKTEDGAvdySEDFFGKPTSLTVSGQLEGEL 217
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVERePLLEKAGHEPKDLL-------PVGAEN---EEDLYLRPTLEPGLVRLFVSH 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 749817351 218 GAMSLGAIYTFGPTFRAENSNT-PRHLAEFWMVEPEVAFNEIGEnmdlaEDFLKYLIRYALD 278
Cdd:cd00768 71 IRKLPLRLAEIGPAFRNEGGRRgLRRVREFTQLEGEVFGEDGEE-----ASEFEELIELTEE 127
|
|
| |
