|
Name |
Accession |
Description |
Interval |
E-value |
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
27-428 |
0e+00 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 514.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 27 KMRVRDALRvQDARGECVTVQGWIRSVRSQKEVLFLHVNDGSSLESLQIVADSSFDS----RELTFGSSVQVQGQLVKSQ 102
Cdd:PRK03932 3 RVSIKDILK-GKYVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDNGEEYfeeiKKLTTGSSVIVTGTVVESP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 103 SKRQNVELKAEKIEVIGDcEAKAFPIKyKERHPLEYLRQYPHLRCRTNALGSILRVRSEATAAIHSYFKDNGFVHIHTPV 182
Cdd:PRK03932 82 RAGQGYELQATKIEVIGE-DPEDYPIQ-KKRHSIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVDTPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 183 LTSNDCEGAGELFQVepSSKIKGPKESFFDVPAFLTVSGQLHLEVMSGAFTQVFTFGPTFRAENSQSRRHLAEFYMVEAE 262
Cdd:PRK03932 160 ITASDCEGAGELFRV--TTLDLDFSKDFFGKEAYLTVSGQLYAEAYAMALGKVYTFGPTFRAENSNTRRHLAEFWMIEPE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 263 ISFVEsLQDLMQVMEELFKATTEMVLSHCPEDVELCHQFIAAGQKGRLEHMLKNNFLIISYTEAIEILKQASQNFAFT-- 340
Cdd:PRK03932 238 MAFAD-LEDNMDLAEEMLKYVVKYVLENCPDDLEFLNRRVDKGDIERLENFIESPFPRITYTEAIEILQKSGKKFEFPve 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 341 ---------------------------PK---------------VAAVDLLVPGVGELFGGSLREERYHVLEQRLARSGL 378
Cdd:PRK03932 317 wgddlgseherylaeehfkkpvfvtnyPKdikafymrlnpdgktVAAMDLLAPGIGEIIGGSQREERLDVLEARIKELGL 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 568950598 379 -TKAYQWYLDLRKFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFPRFTHS 428
Cdd:PRK03932 397 nKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGR 447
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
27-429 |
6.72e-170 |
|
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: 483.01 E-value: 6.72e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 27 KMRVRDALrvQDARGECVTVQGWIRSVRSQKEVLFLHVNDGSSLesLQIVADSS----FDS-RELTFGSSVQVQGQLVKS 101
Cdd:COG0017 2 RTYIKDLL--PEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGF--IQVVVKKDklenFEEaKKLTTESSVEVTGTVVES 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 102 QSKRQNVELKAEKIEVIGDCEaKAFPIKYKeRHPLEYLRQYPHLRCRTNALGSILRVRSEATAAIHSYFKDNGFVHIHTP 181
Cdd:COG0017 78 PRAPQGVELQAEEIEVLGEAD-EPYPLQPK-RHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVEVHTP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 182 VLTSNDCEGAGELFQVEpsskikgpkesFFDVPAFLTVSGQLHLEVMSGAFTQVFTFGPTFRAENSQSRRHLAEFYMVEA 261
Cdd:COG0017 156 IITASATEGGGELFPVD-----------YFGKEAYLTQSGQLYKEALAMALEKVYTFGPTFRAEKSNTRRHLAEFWMIEP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 262 EISFVEsLQDLMQVMEELFKATTEMVLSHCPEDVELCHQFIAagqkgRLEHMLKNNFLIISYTEAIEILKQASQNFAF-- 339
Cdd:COG0017 225 EMAFAD-LEDVMDLAEEMLKYIIKYVLENCPEELEFLGRDVE-----RLEKVPESPFPRITYTEAIEILKKSGEKVEWgd 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 340 ---------------------T--PK----------------VAAVDLLVPGVGELFGGSLREERYHVLEQRLARSGL-T 379
Cdd:COG0017 299 dlgteherylgeeffkkpvfvTdyPKeikafymkpnpddpktVAAFDLLAPGIGEIIGGSQREHRYDVLVERIKEKGLdP 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 568950598 380 KAYQWYLDLRKFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFPRFTHSC 429
Cdd:COG0017 379 EDYEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRL 428
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
27-429 |
4.61e-160 |
|
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: 459.15 E-value: 4.61e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 27 KMRVRDALR-VQDARGECVTVQGWIRSVRSQKEVLFLHVNDGSSLESLQIVADSSFDSRE------LTFGSSVQVQGQLV 99
Cdd:TIGR00457 1 SAAIKDLLQqVYKFVGDEVTVSGWVRTKRSSKKIIFLELNDGSSLGPIQAVINGEDNPYLfqllksLTTGSSVSVTGKVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 100 KSQSKRQNVELKAEKIEVIGDCEAKAFPIKyKERHPLEYLRQYPHLRCRTNALGSILRVRSEATAAIHSYFKDNGFVHIH 179
Cdd:TIGR00457 81 ESPGKGQPVELQVKKIEVVGEAEPDDYPLQ-KKEHSLEFLRDIAHLRLRTNTLGAVMRVRNALSQAIHRYFQENGFTWVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 180 TPVLTSNDCEGAGELFQVepSSKIKGPKESFFDVPAFLTVSGQLHLEVMSGAFTQVFTFGPTFRAENSQSRRHLAEFYMV 259
Cdd:TIGR00457 160 PPILTSNDCEGAGELFRV--STGNIDFSQDFFGKEAYLTVSGQLYLETYALALSKVYTFGPTFRAEKSNTSRHLSEFWMI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 260 EAEISFVEsLQDLMQVMEELFKATTEMVLSHCPEDVELCHQFIAAGQKGRLEHMLKNNFLIISYTEAIEILKQASQNFAF 339
Cdd:TIGR00457 238 EPEMAFAN-LNDLLQLAETLIKYIIKAVLENCSQELKFLEKNFDKDLIKRLENIINNKFARITYTDAIEILKESDKNFEY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 340 TPK--------------------------------------------VAAVDLLVPGVGELFGGSLREERYHVLEQRLAR 375
Cdd:TIGR00457 317 EDFwgddlqteherflaeeyfkppvfvtnypkdikafymklnddgktVAAMDLLAPGIGEIIGGSEREDDLDKLENRMKE 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 568950598 376 SGL-TKAYQWYLDLRKFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFPRFTHSC 429
Cdd:TIGR00457 397 MGLdTDALNWYLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGNI 451
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
133-427 |
8.77e-134 |
|
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: 387.31 E-value: 8.77e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 133 RHPLEYLRQYPHLRCRTNALGSILRVRSEATAAIHSYFKDNGFVHIHTPVLTSNDCEGAGELFQVepsskikgpkeSFFD 212
Cdd:cd00776 1 DANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKV-----------SYFG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 213 VPAFLTVSGQLHLEVMSGAFTQVFTFGPTFRAENSQSRRHLAEFYMVEAEISFVESLQDLMQVMEELFKATTEMVLSHCP 292
Cdd:cd00776 70 KPAYLAQSPQLYKEMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEDYNEVMDLIEELIKYIFKRVLERCA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 293 EDVELChqfiaaGQKGRLEHMLKNNFLIISYTEAIEILKQASQNFAFTPK------------------------------ 342
Cdd:cd00776 150 KELELV------NQLNRELLKPLEPFPRITYDEAIELLREKGVEEEVKWGedlsteherllgeivkgdpvfvtdypkeik 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 343 -------------VAAVDLLVPGVGELFGGSLREERYHVLEQRLARSGL-TKAYQWYLDLRKFGSVPHGGFGMGFERYLQ 408
Cdd:cd00776 224 pfymkpdddnpetVESFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGLdPESFEWYLDLRKYGMPPHGGFGLGLERLVM 303
|
330
....*....|....*....
gi 568950598 409 CILGVDNIKDVIPFPRFTH 427
Cdd:cd00776 304 WLLGLDNIREAILFPRDPK 322
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
31-424 |
3.46e-131 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 389.72 E-value: 3.46e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 31 RDALRVQDARG----------ECVTVQGWIRSVRSQKEVLFLHVNDGSSLESLQIVADS------SFDSRELTFGSSVQV 94
Cdd:PLN02603 87 RKKLRIADVKGgedeglarvgKTLNVMGWVRTLRAQSSVTFIEVNDGSCLSNMQCVMTPdaegydQVESGLITTGASVLV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 95 QGQLVKSQSKRQNVELKAEKIEVIGDCEAkAFPIKyKERHPLEYLRQYPHLRCRTNALGSILRVRSEATAAIHSYFKDNG 174
Cdd:PLN02603 167 QGTVVSSQGGKQKVELKVSKIVVVGKSDP-SYPIQ-KKRVSREFLRTKAHLRPRTNTFGAVARVRNALAYATHKFFQENG 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 175 FVHIHTPVLTSNDCEGAGELFQVE---PSSKIKG-------PK---------ESFFDVPAFLTVSGQLHLEVMSGAFTQV 235
Cdd:PLN02603 245 FVWVSSPIITASDCEGAGEQFCVTtliPNSAENGgslvddiPKtkdglidwsQDFFGKPAFLTVSGQLNGETYATALSDV 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 236 FTFGPTFRAENSQSRRHLAEFYMVEAEISFVEsLQDLMQVMEELFKATTEMVLSHCPEDVELCHQFIAAGQKGRLEHMLK 315
Cdd:PLN02603 325 YTFGPTFRAENSNTSRHLAEFWMIEPELAFAD-LNDDMACATAYLQYVVKYILENCKEDMEFFNTWIEKGIIDRLSDVVE 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 316 NNFLIISYTEAIEILKQASQNFAFT------------------------------PK---------------VAAVDLLV 350
Cdd:PLN02603 404 KNFVQLSYTDAIELLLKAKKKFEFPvkwgldlqseheryiteeafggrpviirdyPKeikafymrenddgktVAAMDMLV 483
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568950598 351 PGVGELFGGSLREERYHVLEQRLARSGLTK-AYQWYLDLRKFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFPR 424
Cdd:PLN02603 484 PRVGELIGGSQREERLEYLEARLDELKLNKeSYWWYLDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFPR 558
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
41-425 |
3.04e-106 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 325.80 E-value: 3.04e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 41 GECVTVQGWIRSVRSQKE--VLFLHVNDGSSLESLQIVADSSFD--SRELTFGSSVQVQGQLV---KSQSKRQNVELKAE 113
Cdd:PLN02221 50 GQKVRIGGWVKTGREQGKgtFAFLEVNDGSCPANLQVMVDSSLYdlSTLVATGTCVTVDGVLKvppEGKGTKQKIELSVE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 114 KIEVIGDCEAKAFPIKyKERHPLEYLRQYPHLRCRTNALGSILRVRSEATAAIHSYFKDNGFVHIHTPVLTSNDCEGAGE 193
Cdd:PLN02221 130 KVIDVGTVDPTKYPLP-KTKLTLEFLRDVLHLRSRTNSISAVARIRNALAFATHSFFQEHSFLYIHTPIITTSDCEGAGE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 194 LFQV------------------------------------EPSSKIKGPKES---------------------------- 209
Cdd:PLN02221 209 MFQVttlinyterleqdlidnpppteadveaarlivkergEVVAQLKAAKASkeeitaavaelkiakeslahieersklk 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 210 ---------------FFDVPAFLTVSGQLHLEVMSGAFTQVFTFGPTFRAENSQSRRHLAEFYMVEAEISFVEsLQDLMQ 274
Cdd:PLN02221 289 pglpkkdgkidyskdFFGRQAFLTVSGQLQVETYACALSSVYTFGPTFRAENSHTSRHLAEFWMVEPEIAFAD-LEDDMN 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 275 VMEELFKATTEMVLSHCPEDVELCHQFIAAGQKGRLEHMLKNNFLIISYTEAIEILKQA-SQNFAFT------------- 340
Cdd:PLN02221 368 CAEAYVKYMCKWLLDKCFDDMELMAKNFDSGCIDRLRMVASTPFGRITYTEAIELLEEAvAKGKEFDnnvewgidlaseh 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 341 ------------------PK---------------VAAVDLLVPGVGELFGGSLREERYHVLEQRLARSGL-TKAYQWYL 386
Cdd:PLN02221 448 eryltevlfqkplivynyPKgikafymrlnddektVAAMDVLVPKVGELIGGSQREERYDVIKQRIEEMGLpIEPYEWYL 527
|
490 500 510
....*....|....*....|....*....|....*....
gi 568950598 387 DLRKFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFPRF 425
Cdd:PLN02221 528 DLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPRY 566
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
9-425 |
1.03e-93 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 293.85 E-value: 1.03e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 9 GALRLCSSVSCPRPRAsakmRVRDALRVQDARGECVTVQGWIRSVRSQK--EVLFLHVNDGSSLESLQIVADSSFDSREL 86
Cdd:PTZ00425 53 SRIRICNVLNVPKSEK----EFNDNSRKNKYIDQIITVCGWSKAVRKQGggRFCFVNLNDGSCHLNLQIIVDQSIENYEK 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 87 TF----GSSVQVQGQLVKSQSK--------RQNVELKAE-----KIEVIGD-CEAKAFPIKyKERHPLEYLRQYPHLRCR 148
Cdd:PTZ00425 129 LLkcgvGCCFRFTGKLIISPVQnenkkgllKENVELALKdnsihNFEIYGEnLDPQKYPLS-KKNHGKEFLREVAHLRPR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 149 TNALGSILRVRSEATAAIHSYFKDNGFVHIHTPVLTSNDCEGAGELFQV------------------------------- 197
Cdd:PTZ00425 208 SYFISSVIRIRNALAIATHLFFQSRGFLYIHTPLITTSDCEGGGEMFTVttllgedadyraiprvnkknkkgekrediln 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 198 ---------------------EPSSKIKGPKESFFDVPAFLTVSGQLHLEVMSGAFTQVFTFGPTFRAENSQSRRHLAEF 256
Cdd:PTZ00425 288 tcnannnngnssssnavsspaYPDQYLIDYKKDFFSKQAFLTVSGQLSLENLCSSMGDVYTFGPTFRAENSHTSRHLAEF 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 257 YMVEAEISFVEsLQDLMQVMEELFKATTEMVLSHCPEDVELCHQFIAAGQKGRLEHMLKNNFLIISYTEAIEILKQASQN 336
Cdd:PTZ00425 368 WMIEPEIAFAD-LYDNMELAESYIKYCIGYVLNNNFDDIYYFEENVETGLISRLKNILDEDFAKITYTNVIDLLQPYSDS 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 337 F-------------------------------------AFTPK-------VAAVDLLVPGVGELFGGSLREERYHVLEQR 372
Cdd:PTZ00425 447 FevpvkwgmdlqseherfvaeqifkkpvivynypkdlkAFYMKlnedqktVAAMDVLVPKIGEVIGGSQREDNLERLDKM 526
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 568950598 373 LARSGLT-KAYQWYLDLRKFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFPRF 425
Cdd:PTZ00425 527 IKEKKLNmESYWWYRQLRKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFPRY 580
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
51-424 |
1.37e-91 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 289.46 E-value: 1.37e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 51 RSVRSQKEVLFLHVNDGSSLESLQIVADSSFD--SRELTFGSSVQVQG--QLVKSQSKRQNVELKAEKIEVIGDCEAKAF 126
Cdd:PLN02532 127 KSAPPPPSVAYLLISDGSCVASLQVVVDSALAplTQLMATGTCILAEGvlKLPLPAQGKHVIELEVEKILHIGTVDPEKY 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 127 PIKyKERHPLEYLRQYPHLRCRTNALGSILRVRSEATAAIHSYFKDNGFVHIHTPVLTSNDCEGAGELFQV--------- 197
Cdd:PLN02532 207 PLS-KKRLPLDMLRDFSHFRPRTTTVASVTRVRSALTHATHTFFQDHGFLYVQVPIITTTDATGFGEMFRVttllgksdd 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 198 -----------------------------------------------------------------EPSSKIKGPKES--- 209
Cdd:PLN02532 286 keekkpvhetegisleavkaaikektnlveelkrsesnrealvaaeqdlrktnqlasqleakeklKTGTSVKADKLSfsk 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 210 -FFDVPAFLTVSGQLHLEVMSGAFTQVFTFGPTFRAENSQSRRHLAEFYMVEAEISFVEsLQDLMQVMEELFKATTEMVL 288
Cdd:PLN02532 366 dFFSRPTYLTVSGRLHLESYACALGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAFSE-LEDAMNCAEDYFKFLCKWVL 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 289 SHCPEDVELCHQFIAAGQKGRLEHMLKNNFLIISYTEAIEILKQASQN---------FAFT------------------- 340
Cdd:PLN02532 445 ENCSEDMKFVSKRIDKTISTRLEAIISSSLQRISYTEAVDLLKQATDKkfetkpewgIALTtehlsyladeiykkpviiy 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 341 --PK---------------VAAVDLLVPGVGELFGGSLREERYHVLEQRLARSGLTK-AYQWYLDLRKFGSVPHGGFGMG 402
Cdd:PLN02532 525 nyPKelkpfyvrlnddgktVAAFDLVVPKVGTVITGSQNEERMDILNARIEELGLPReQYEWYLDLRRHGTVKHSGFSLG 604
|
490 500
....*....|....*....|..
gi 568950598 403 FERYLQCILGVDNIKDVIPFPR 424
Cdd:PLN02532 605 FELMVLFATGLPDVRDAIPFPR 626
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
136-426 |
3.29e-81 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 252.87 E-value: 3.29e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 136 LEYLRQYPHLRCRTNALGSILRVRSEATAAIHSYFKDNGFVHIHTPVLTSNDCEGAGELFQVEpsSKIKGPkesFFdvpa 215
Cdd:pfam00152 2 EETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVP--SRALGK---FY---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 216 FLTVSGQLHLEV-MSGAFTQVFTFGPTFRAENSQSRRHLaEFYMVEAEISFVEsLQDLMQVMEELFKATTEMVLsHCPED 294
Cdd:pfam00152 73 ALPQSPQLYKQLlMVAGFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVD-YEDVMDLTEELIKEIFKEVE-GIAKE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 295 VELchqfiaagqkGRLEHmLKNNFLIISYTEAIEILKQASQ-------------------------NFAF--------TP 341
Cdd:pfam00152 150 LEG----------GTLLD-LKKPFPRITYAEAIEKLNGKDVeelgygsdkpdlrfllelvidknkfNPLWvtdfpaehHP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 342 -----------KVAAVDLLVPGVgELFGGSLREERYHVLEQRLARSGLTKA-----YQWYLDLRKFGSVPHGGFGMGFER 405
Cdd:pfam00152 219 ftmpkdeddpaLAEAFDLVLNGV-EIGGGSIRIHDPELQEERFEEQGLDPEeaeekFGFYLDALKYGAPPHGGLGIGLDR 297
|
330 340
....*....|....*....|.
gi 568950598 406 YLQCILGVDNIKDVIPFPRFT 426
Cdd:pfam00152 298 LVMLLTGLESIREVIAFPKTR 318
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
38-424 |
7.15e-70 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 227.38 E-value: 7.15e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 38 DARGECVTVQGWIRSVRSQKEVLFLHVNDGSSLesLQIVADSS------FDSRELTFGSSVQVQGQLVKSQSKRQNVELK 111
Cdd:PRK05159 13 ELDGEEVTLAGWVHEIRDLGGIAFLILRDRSGI--IQVVVKKKvdeelfETIKKLKRESVVSVTGTVKANPKAPGGVEVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 112 AEKIEVIGdcEAKA---FPIKYKERHPLEYLRQYPHLRCRTNALGSILRVRSEATAAIHSYFKDNGFVHIHTPVLTSNDC 188
Cdd:PRK05159 91 PEEIEVLN--KAEEplpLDISGKVLAELDTRLDNRFLDLRRPRVRAIFKIRSEVLRAFREFLYENGFTEIFTPKIVASGT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 189 EGAGELFQVepsskikgpkeSFFDVPAFLTVSGQLHLEVMSGA-FTQVFTFGPTFRAENSQSRRHLAEFYMVEAEISFVE 267
Cdd:PRK05159 169 EGGAELFPI-----------DYFEKEAYLAQSPQLYKQMMVGAgFERVFEIGPVFRAEEHNTSRHLNEYTSIDVEMGFID 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 268 SLQDLMQVMEELFKATTEMVLSHCPEDVELchqfiaagqkgrLEHML---KNNFLIISYTEAIEILKQASQNFAFT---- 340
Cdd:PRK05159 238 DHEDVMDLLENLLRYMYEDVAENCEKELEL------------LGIELpvpETPIPRITYDEAIEILKSKGNEISWGddld 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 341 -------------------------PKVA----------------AVDLLVPGVgELFGGSLREERYHVLEQRLARSGL- 378
Cdd:PRK05159 306 tegerllgeyvkeeygsdfyfitdyPSEKrpfytmpdeddpeiskSFDLLFRGL-EITSGGQRIHRYDMLVESIKEKGLn 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 568950598 379 TKAYQWYLDLRKFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFPR 424
Cdd:PRK05159 385 PESFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFPR 430
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
41-424 |
7.44e-46 |
|
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: 163.84 E-value: 7.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 41 GECVTVQGWIRSVRSQKEVLFLHVNDGSSLesLQIVADSSFDSRE-------LTFGSSVQVQGQLVKSQSKRQNVELKAE 113
Cdd:TIGR00458 12 GQEVTFMGWVHEIRDLGGLIFVLLRDREGL--IQITAPAKKVSKNlfkwakkLNLESVVAVRGIVKIKEKAPGGFEIIPT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 114 KIEVIGDCEAkAFPIKYKERHP--LEYLRQYPHLRCRTNALGSILRVRSEATAAIHSYFKDNGFVHIHTPVLTSNDCEGA 191
Cdd:TIGR00458 90 KIEVINEAKE-PLPLDPTEKVPaeLDTRLDYRFLDLRRPTVQAIFRIRSGVLESVREFLAEEGFIEVHTPKLVASATEGG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 192 GELFQVepsskikgpkeSFFDVPAFLTVSGQLHLEV-MSGAFTQVFTFGPTFRAENSQSRRHLAEFYMVEAEISFVESlQ 270
Cdd:TIGR00458 169 TELFPI-----------TYFEREAFLGQSPQLYKQQlMAAGFERVYEIGPIFRAEEHNTHRHLNEATSIDIEMAFEDH-H 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 271 DLMQVMEELFKATTEMVLSHCPEDVELchqfiaagqKGRLEHMLKNNFLIISYTEAIEILKQA----------------- 333
Cdd:TIGR00458 237 DVMDILEELVVRVFEDVPERCAHQLET---------LEFKLEKPEGKFVRLTYDEAIEMANAKgveigwgedlsteaeka 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 334 -----------------SQNFAFTPKVA------AVDLLVPGVgELFGGSLREERYHVLEQRLARSGLT-KAYQWYLDLR 389
Cdd:TIGR00458 308 lgeemdglyfitdwpteIRPFYTMPDEDnpeiskSFDLMYRDL-EISSGAQRIHLHDLLVERIKAKGLNpEGFKDYLEAF 386
|
410 420 430
....*....|....*....|....*....|....*
gi 568950598 390 KFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFPR 424
Cdd:TIGR00458 387 SYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFPR 421
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
154-424 |
8.12e-39 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 142.85 E-value: 8.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 154 SILRVRSEATAAIHSYFKDNGFVHIHTPVLTSNDCEGAGElfqvEPSSKIKGPKESFFDVPAFLTVSGQLHLEVMSGAFT 233
Cdd:PRK06462 28 KVLKVQSSILRYTREFLDGRGFVEVLPPIISPSTDPLMGL----GSDLPVKQISIDFYGVEYYLADSMILHKQLALRMLG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 234 QVFTFGPTFRAEN--SQSRRHLAEFYMVEAEISFVeSLQDLMQVMEELFKATTEMVLSHCPEDVElchqfiaagQKGRLE 311
Cdd:PRK06462 104 KIFYLSPNFRLEPvdKDTGRHLYEFTQLDIEIEGA-DLDEVMDLIEDLIKYLVKELLEEHEDELE---------FFGRDL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 312 HMLKNNFLIISYTEAIEIL------------------KQASQNFA------------------FTPKVAAV----DLLVP 351
Cdd:PRK06462 174 PHLKRPFKRITHKEAVEILneegcrgidleelgsegeKSLSEHFEepfwiidipkgsrefydrEDPERPGVlrnyDLLLP 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568950598 352 -GVGELFGGSLREERYHVLEQRLARSGLT-KAYQWYLDLRKFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFPR 424
Cdd:PRK06462 254 eGYGEAVSGGEREYEYEEIVERIREHGVDpEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQPFPR 328
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
156-424 |
2.95e-33 |
|
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: 126.05 E-value: 2.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 156 LRVRSEATAAIHSYFKDNGFVHIHTPVLTSNDCEGAGELFQVepsskikgpKESFFDVPAFLTVSGQLHLE-VMSGAFTQ 234
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLV---------KYNALGLDYYLRISPQLFKKrLMVGGLDR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 235 VFTFGPTFRAENSqSRRHLAEFYMVEAEISFVEsLQDLMQVMEELFKATTEMVLSHcpedvelchqfiAAGQKGRLEHML 314
Cdd:cd00669 72 VFEINRNFRNEDL-RARHQPEFTMMDLEMAFAD-YEDVIELTERLVRHLAREVLGV------------TAVTYGFELEDF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 315 KNNFLIISYTEAIEILKQ---------------ASQNfAFTPKVA-AVDLLVPGVgELFGGSLREERYHVLEQRLARSGL 378
Cdd:cd00669 138 GLPFPRLTYREALERYGQplfltdypaemhsplASPH-DVNPEIAdAFDLFINGV-EVGNGSSRLHDPDIQAEVFQEQGI 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 568950598 379 TKAYQ-----WYLDLRKFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFPR 424
Cdd:cd00669 216 NKEAGmeyfeFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPK 266
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
44-119 |
6.52e-32 |
|
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: 116.13 E-value: 6.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 44 VTVQGWIRSVRSQKEVLFLHVNDGSSLESLQIVADSSFDSRE----LTFGSSVQVQGQLVKSQSKRQNVELKAEKIEVIG 119
Cdd:cd04318 2 VTVNGWVRSVRDSKKISFIELNDGSCLKNLQVVVDKELTNFKeilkLSTGSSIRVEGVLVKSPGAKQPFELQAEKIEVLG 81
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
36-424 |
4.91e-31 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 124.82 E-value: 4.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 36 VQDARGECVTVQGWIRSVRSQKEVLFLHVNdgSSLESLQIVADSSFD---------SRELTFGSSVQVQGQL------VK 100
Cdd:PLN02850 76 GEELAGSEVLIRGRVHTIRGKGKSAFLVLR--QSGFTVQCVVFVSEVtvskgmvkyAKQLSRESVVDVEGVVsvpkkpVK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 101 SQSkrQNVELKAEKIEVIG--------DCEAKAFPIKYKERhPLEYLRQYPH-----------LRCRTNALGSILRVRSE 161
Cdd:PLN02850 154 GTT--QQVEIQVRKIYCVSkalatlpfNVEDAARSESEIEK-ALQTGEQLVRvgqdtrlnnrvLDLRTPANQAIFRIQSQ 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 162 ATAAIHSYFKDNGFVHIHTPVLTSNDCEGAGELFQVEpsskikgpkesFFDVPAFLTVSGQLHLEV-MSGAFTQVFTFGP 240
Cdd:PLN02850 231 VCNLFREFLLSKGFVEIHTPKLIAGASEGGSAVFRLD-----------YKGQPACLAQSPQLHKQMaICGDFRRVFEIGP 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 241 TFRAENSQSRRHLAEFYMVEAEISFVESLQDLMQVMEELFKATTEMVLSHCPEDVElchqfiAAGQKGRLEhMLK--NNF 318
Cdd:PLN02850 300 VFRAEDSFTHRHLCEFTGLDLEMEIKEHYSEVLDVVDELFVAIFDGLNERCKKELE------AIREQYPFE-PLKylPKT 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 319 LIISYTEAIEILKQASQ--------NFAFTPKVAAV-------------------------------------DLLVPGv 353
Cdd:PLN02850 373 LRLTFAEGIQMLKEAGVevdplgdlNTESERKLGQLvkekygtdfyilhryplavrpfytmpcpddpkysnsfDVFIRG- 451
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568950598 354 GELFGGSLREERYHVLEQRLARSGL-TKAYQWYLDLRKFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFPR 424
Cdd:PLN02850 452 EEIISGAQRVHDPELLEKRAEECGIdVKTISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPR 523
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
33-424 |
8.04e-28 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 115.48 E-value: 8.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 33 ALRVQDARGECVTVQGWIRSVRSQKEVLFLHVNDGSslESLQIVADSSFDSR--------ELTFGSSVQVQGQLVK---- 100
Cdd:PTZ00401 70 VLSKPELVDKTVLIRARVSTTRKKGKMAFMVLRDGS--DSVQAMAAVEGDVPkemidfigQIPTESIVDVEATVCKveqp 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 101 -SQSKRQNVELKAEKIEVIGDcEAKAFPIKYKERHPLE-----YLRQYPHLRCR-----TNALGSILRVRSEATAAIHSY 169
Cdd:PTZ00401 148 iTSTSHSDIELKVKKIHTVTE-SLRTLPFTLEDASRKEsdegaKVNFDTRLNSRwmdlrTPASGAIFRLQSRVCQYFRQF 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 170 FKDNGFVHIHTPVLTSNDCEGAGELFQVEpsskikgpkesFFDVPAFLTVSGQLHLE-VMSGAFTQVFTFGPTFRAENSQ 248
Cdd:PTZ00401 227 LIDSDFCEIHSPKIINAPSEGGANVFKLE-----------YFNRFAYLAQSPQLYKQmVLQGDVPRVFEVGPVFRSENSN 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 249 SRRHLAEFYMVEAEISFVESLQDLMQVMEELFKATTEMVLSHCPEDVELCHQF----------------IAAG------- 305
Cdd:PTZ00401 296 THRHLTEFVGLDVEMRINEHYYEVLDLAESLFNYIFERLATHTKELKAVCQQYpfeplvwkltpermkeLGVGvisegve 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 306 ----QKGRLEHMlKNNFLIISYTEAIEILkqasqNFAFTPKVAAVDlLVPGVGELFGGSLREERYHV---LEQRLARSG- 377
Cdd:PTZ00401 376 ptdkYQARVHNM-DSRMLRINYMHCIELL-----NTVLEEKMAPTD-DINTTNEKLLGKLVKERYGTdffISDRFPSSAr 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 378 ------------LTKAYQW------------------------------------YLDLRKFGSVPHGGFGMGFERYLQC 409
Cdd:PTZ00401 449 pfytmeckdderFTNSYDMfirgeeissgaqrihdpdlllarakmlnvdltpikeYVDSFRLGAWPHGGFGVGLERVVML 528
|
490
....*....|....*
gi 568950598 410 ILGVDNIKDVIPFPR 424
Cdd:PTZ00401 529 YLGLSNVRLASLFPR 543
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
156-423 |
4.26e-25 |
|
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: 103.81 E-value: 4.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 156 LRVRSEATAAIHSYFKDNGFVHIHTPVLTSNDCEGAGElFQVePSSKIKGpkeSFFDVPAfltvSGQLHLEV-MSGAFTQ 234
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTPEGARD-FLV-PSRLHPG---KFYALPQ----SPQLFKQLlMVSGFDR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 235 VFTFGPTFRAENSQSRRHlAEFYMVEAEISFVESlQDLMQVMEELFKATTEMVLShcpedvelchqfiaagqkgrleHML 314
Cdd:cd00777 72 YFQIARCFRDEDLRADRQ-PEFTQIDIEMSFVDQ-EDIMSLIEGLLKYVFKEVLG----------------------VEL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 315 KNNFLIISYTEAI--------------------EILKQASQNFAFT-PK---------------VAAVDLLVPGVgELFG 358
Cdd:cd00777 128 TTPFPRMTYAEAMerygfkflwivdfplfewdeEEGRLVSAHHPFTaPKeedldllekdpedarAQAYDLVLNGV-ELGG 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 359 GSLREERYHVLEQRLARSGLTKAYQW-----YLDLRKFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFP 423
Cdd:cd00777 207 GSIRIHDPDIQEKVFEILGLSEEEAEekfgfLLEAFKYGAPPHGGIALGLDRLVMLLTGSESIRDVIAFP 276
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
44-119 |
1.28e-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: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 44 VTVQGWIRSVRSQKEVLFLHVNDGSSleSLQIVADSSFDS------RELTFGSSVQVQGQLVKSQ---SKRQNVELKAEK 114
Cdd:cd04100 2 VTLAGWVHSRRDHGGLIFIDLRDGSG--IVQVVVNKEELGeffeeaEKLRTESVVGVTGTVVKRPegnLATGEIELQAEE 79
|
....*
gi 568950598 115 IEVIG 119
Cdd:cd04100 80 LEVLS 84
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
33-328 |
1.04e-17 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 85.12 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 33 ALRVQDArGECVTVQGWIRSVRSQKEVLFLHVNDGSSLesLQIVADSSFDS----RELTFGSSVQVQGQLVKSQSKRQN- 107
Cdd:PRK00476 10 ELRESHV-GQTVTLCGWVHRRRDHGGLIFIDLRDREGI--VQVVFDPDAEAfevaESLRSEYVIQVTGTVRARPEGTVNp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 108 ------VELKAEKIEVIGDCEAKAFPIKYKErHPLEYLR-QYPHLRCRTNALGSILRVRSEATAAIHSYFKDNGFVHIHT 180
Cdd:PRK00476 87 nlptgeIEVLASELEVLNKSKTLPFPIDDEE-DVSEELRlKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDDNGFLEIET 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 181 PVLTSNDCEGAGElFQVePSSKIKGpkeSFFDVPAfltvSGQL--HLEVMSGaFTQVFTFGPTFRAENSQSRRhLAEFYM 258
Cdd:PRK00476 166 PILTKSTPEGARD-YLV-PSRVHPG---KFYALPQ----SPQLfkQLLMVAG-FDRYYQIARCFRDEDLRADR-QPEFTQ 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 259 VEAEISFVESlQDLMQVMEELFKATTEMVLshcpeDVElchqfiaagqkgrlehmLKNNFLIISYTEAIE 328
Cdd:PRK00476 235 IDIEMSFVTQ-EDVMALMEGLIRHVFKEVL-----GVD-----------------LPTPFPRMTYAEAMR 281
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
38-279 |
3.59e-15 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 77.72 E-value: 3.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 38 DARGECVTVQGWIRSVRSQKEVLFLHVNDGSSLesLQIVADSSFDSRELTFGSS-------VQVQGQLVKSQSKRQNVEL 110
Cdd:PRK12820 15 DDTGREVCLAGWVDAFRDHGELLFIHLRDRNGF--IQAVFSPEAAPADVYELAAslraefcVALQGEVQKRLEETENPHI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 111 KAEKIEV-------IGDCEAKAFPIKYKER----------HPLEYLR-QYPHLRCRTNALGSILRVRSEATAAIHSYFKD 172
Cdd:PRK12820 93 ETGDIEVfvrelsiLAASEALPFAISDKAMtagagsagadAVNEDLRlQYRYLDIRRPAMQDHLAKRHRIIKCARDFLDS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 173 NGFVHIHTPVLTSNDCEGAGELFQvepSSKIKgPKEsFFDVPAFLTVSGQLhleVMSGAFTQVFTFGPTFRAENSQSRRH 252
Cdd:PRK12820 173 RGFLEIETPILTKSTPEGARDYLV---PSRIH-PKE-FYALPQSPQLFKQL---LMIAGFERYFQLARCFRDEDLRPNRQ 244
|
250 260
....*....|....*....|....*..
gi 568950598 253 lAEFYMVEAEISFVESlQDLMQVMEEL 279
Cdd:PRK12820 245 -PEFTQLDIEASFIDE-EFIFELIEEL 269
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
33-328 |
2.06e-14 |
|
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: 75.03 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 33 ALRVQDArGECVTVQGWIRSVRSQKEVLFLHVNDGSSLesLQIVADSSFDS------RELTFGSSVQVQGQLVKSQSKRQ 106
Cdd:COG0173 9 ELRESDV-GQEVTLSGWVHRRRDHGGLIFIDLRDRYGI--TQVVFDPDDSAeafekaEKLRSEYVIAVTGKVRARPEGTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 107 N-------VELKAEKIEVIGDCEAKAFPIKyKERHPLEYLR-QYPHLRCRTNALGSILRVRSEATAAIHSYFKDNGFVHI 178
Cdd:COG0173 86 NpklptgeIEVLASELEILNKAKTPPFQID-DDTDVSEELRlKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDENGFLEI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 179 HTPVLTSNDCEGAGElFQVePSSKIKGpkeSFFDVPAfltvSGQL--HLEVMSGaFTQVFTFGPTFRAENSQSRRHlAEF 256
Cdd:COG0173 165 ETPILTKSTPEGARD-YLV-PSRVHPG---KFYALPQ----SPQLfkQLLMVSG-FDRYFQIARCFRDEDLRADRQ-PEF 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568950598 257 YMVEAEISFVESlQDLMQVMEELFKATTEMVLshcpeDVElchqfiaagqkgrlehmLKNNFLIISYTEAIE 328
Cdd:COG0173 234 TQLDIEMSFVDQ-EDVFELMEGLIRHLFKEVL-----GVE-----------------LPTPFPRMTYAEAME 282
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
4-282 |
5.36e-13 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 70.97 E-value: 5.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 4 ARRLLGALRLCSSVSCPRPRASAKMRVRDAL------------RVQDArGECVTVQGWIRSVRSQKEVLFLHVNDGSSLE 71
Cdd:PLN02903 24 RTTLLSTSSAASSAATVIPVVSAVDSMSSQLtwpsrshlcgalSVNDV-GSRVTLCGWVDLHRDMGGLTFLDVRDHTGIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 72 SLQIVADSSFDSRE----LTFGSSVQVQGQLVKSQSKRQN-------VELKAEKIEVIGDCEAK-AFPIKY---KERHPL 136
Cdd:PLN02903 103 QVVTLPDEFPEAHRtanrLRNEYVVAVEGTVRSRPQESPNkkmktgsVEVVAESVDILNVVTKSlPFLVTTadeQKDSIK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 137 EYLR-QYPHLRCRTNALGSILRVRSEATAAIHSYFKD-NGFVHIHTPVLTSNDCEGAGELFqvePSSKIKgPKEsFFDVP 214
Cdd:PLN02903 183 EEVRlRYRVLDLRRPQMNANLRLRHRVVKLIRRYLEDvHGFVEIETPILSRSTPEGARDYL---VPSRVQ-PGT-FYALP 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568950598 215 AfltvSGQLHLE-VMSGAFTQVFTFGPTFRAENSQSRRHlAEFYMVEAEISFVEsLQDLMQVMEELFKA 282
Cdd:PLN02903 258 Q----SPQLFKQmLMVSGFDRYYQIARCFRDEDLRADRQ-PEFTQLDMELAFTP-LEDMLKLNEDLIRQ 320
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
44-118 |
8.12e-11 |
|
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: 57.63 E-value: 8.12e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568950598 44 VTVQGWIRSV-RSQKEVLFLHVNDGSSleSLQIVADSSFDSRE---LTFGSSVQVQGQLVKSQSKRqnVELKAEKIEVI 118
Cdd:pfam01336 1 VTVAGRVTSIrRSGGKLLFLTLRDGTG--SIQVVVFKEEAEKLakkLKEGDVVRVTGKVKKRKGGE--LELVVEEIELL 75
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
158-283 |
2.96e-08 |
|
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: 53.66 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 158 VRSEATAAIHSYFKDNGFVHIHTPVLTSN-DCEGAGELFQVEPSSKiKGPKESFFDVPAFLTVSGQLHLEVMSGAFTQVF 236
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREpLLEKAGHEPKDLLPVG-AENEEDLYLRPTLEPGLVRLFVSHIRKLPLRLA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 568950598 237 TFGPTFRAENSQ-SRRHLAEFYMVEAEISFVES-----LQDLMQVMEELFKAT 283
Cdd:cd00768 80 EIGPAFRNEGGRrGLRRVREFTQLEGEVFGEDGeeaseFEELIELTEELLRAL 132
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
34-148 |
5.84e-08 |
|
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: 51.37 E-value: 5.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 34 LRVQDArGECVTVQGWIRSVRSQKEVLFLHVNDGSSLesLQIVADSSFDS-----RELTFGSSVQVQGQLVKSQSKRQN- 107
Cdd:cd04317 8 LRESHV-GQEVTLCGWVQRRRDHGGLIFIDLRDRYGI--VQVVFDPEEAPefelaEKLRNESVIQVTGKVRARPEGTVNp 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 568950598 108 ------VELKAEKIEVIGDCEAKAFPIKYKErHPLEYLR-QYPHLRCR 148
Cdd:cd04317 85 klptgeIEVVASELEVLNKAKTLPFEIDDDV-NVSEELRlKYRYLDLR 131
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
20-261 |
6.33e-08 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 54.97 E-value: 6.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 20 PRPRASAKMRVR----DALR----------------VQDAR----GECVTVQGWIRSVRSQKEVLFLHVNDGSSleSLQI 75
Cdd:PRK02983 606 PEPRLPEQVRVRlaklEALRaagvdpypvgvppthtVAEALdaptGEEVSVSGRVLRIRDYGGVLFADLRDWSG--ELQV 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 76 VADSS---------FDsRELTFGSSVQVQGQLVksQSKRQNVELKAEKIEVIGDCeakafpikykeRHPLEYLRQY---P 143
Cdd:PRK02983 684 LLDASrleqgsladFR-AAVDLGDLVEVTGTMG--TSRNGTLSLLVTSWRLAGKC-----------LRPLPDKWKGltdP 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 144 HLRCRTNALG--------SILRVRSEATAAIHSYFKDNGFVHIHTPVLTSndcegagelfqvepsskIKG-----PkesF 210
Cdd:PRK02983 750 EARVRQRYLDlavnpearDLLRARSAVVRAVRETLVARGFLEVETPILQQ-----------------VHGganarP---F 809
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 568950598 211 ------FDVPAFLTVSGQLHLE-VMSGAFTQVFTFGPTFRAENSQSrRHLAEFYMVEA 261
Cdd:PRK02983 810 vthinaYDMDLYLRIAPELYLKrLCVGGVERVFELGRNFRNEGVDA-THNPEFTLLEA 866
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
44-119 |
7.79e-08 |
|
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: 49.54 E-value: 7.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 44 VTVQGWIRSVRSQKEVLFLHVNDGSSLesLQIV-----ADSSFDSRELTFGSSVQVQGQLVK---SQSKRQNVELKAEKI 115
Cdd:cd04323 2 VKVFGWVHRLRSQKKLMFLVLRDGTGF--LQCVlskklVTEFYDAKSLTQESSVEVTGEVKEdprAKQAPGGYELQVDYL 79
|
....
gi 568950598 116 EVIG 119
Cdd:cd04323 80 EIIG 83
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
156-288 |
2.74e-07 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 52.76 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 156 LRVRSEATAAIHSYFKDNGFVHIHTPVLtsndcegagelfQVEPSSKIKGP---KESFFDVPAFLTVSGQLHLE-VMSGA 231
Cdd:PRK12445 184 FVVRSKILAAIRQFMVARGFMEVETPMM------------QVIPGGASARPfitHHNALDLDMYLRIAPELYLKrLVVGG 251
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 568950598 232 FTQVFTFGPTFRAENSqSRRHLAEFYMVEAEISFVEsLQDLMQVMEELFKATTEMVL 288
Cdd:PRK12445 252 FERVFEINRNFRNEGI-SVRHNPEFTMMELYMAYAD-YHDLIELTESLFRTLAQEVL 306
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
44-423 |
1.74e-06 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 50.42 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 44 VTVQGWIRSVRSQKEVLFLHVNdgSSLESLQIVADSSFD-SRE--------LTFGSSVQVQGqlVKSQSKRQNVELKAEK 114
Cdd:PTZ00385 110 VRVAGRVTSVRDIGKIIFVTIR--SNGNELQVVGQVGEHfTREdlkklkvsLRVGDIIGADG--VPCRMQRGELSVAASR 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 115 IEVIGD--CEAKAFPIKYK-----ERHPLEYLRQYPHLRCRTNALGSIlRVRSEATAAIHSYFKDNGFVHIHTPVLTSND 187
Cdd:PTZ00385 186 MLILSPyvCTDQVVCPNLRgftvlQDNDVKYRYRFTDMMTNPCVIETI-KKRHVMLQALRDYFNERNFVEVETPVLHTVA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 188 CEGAGELFQVEPSSKikgpkesffDVPAFLTVSGQLHL-EVMSGAFTQVFTFGPTFRAENSqSRRHLAEFYMVEAEISFv 266
Cdd:PTZ00385 265 SGANAKSFVTHHNAN---------AMDLFLRVAPELHLkQCIVGGMERIYEIGKVFRNEDA-DRSHNPEFTSCEFYAAY- 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 267 ESLQDLMQVMEELFKAT------TEMVLSHC------PEDVELCHQFIAAGQKGRLEHMLK---------NNFLIISYTE 325
Cdd:PTZ00385 334 HTYEDLMPMTEDIFRQLamrvngTTVVQIYPenahgnPVTVDLGKPFRRVSVYDEIQRMSGvefpppnelNTPKGIAYMS 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 326 AIEI--------LKQASQNFA----------------------FTPKVAAVDLLVPGVG---ELFGGSLR---------- 362
Cdd:PTZ00385 414 VVMLryniplppVRTAAKMFEklidffitdrvveptfvmdhplFMSPLAKEQVSRPGLAerfELFVNGIEycnayselnd 493
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568950598 363 -EERYHVLEQRLA--RSGLTKAY---QWYLDLRKFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFP 423
Cdd:PTZ00385 494 pHEQYHRFQQQLVdrQGGDEEAMpldETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFP 560
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
44-145 |
7.17e-06 |
|
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: 44.44 E-value: 7.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 44 VTVQGWIRSVRSQKEVLFLHVNDGSSLesLQIV------ADSSFDSRELTFGSSVQVQGQLVKSQSKRQNVELKAEKIEV 117
Cdd:cd04319 2 VTLAGWVYRKREVGKKAFIVLRDSTGI--VQAVfskdlnEEAYREAKKVGIESSVIVEGAVKADPRAPGGAEVHGEKLEI 79
|
90 100
....*....|....*....|....*...
gi 568950598 118 IGDCEakAFPIkyKERHPLEYLRQYPHL 145
Cdd:cd04319 80 IQNVE--FFPI--TEDASDEFLLDVRHL 103
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
41-125 |
1.52e-04 |
|
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the homodimeric non-discriminating (ND) Pyrococcus kodakaraensis aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. P. kodakaraensis AspRS is a class 2b aaRS. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation 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. P. kodakaraensis ND-AspRS can charge both tRNAAsp and tRNAAsn. Some of the enzymes in this group may be discriminating, based on the presence of homologs of asparaginyl-tRNA synthetase (AsnRS) in their completed genomes.
Pssm-ID: 239811 [Multi-domain] Cd Length: 108 Bit Score: 40.76 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 41 GECVTVQGWIRSVRSQKEVLFLHVNDGSSLesLQIVA------DSSFD-SRELTFGSSVQVQGQlVKSQSKRQN-VELKA 112
Cdd:cd04316 12 GEEVTVAGWVHEIRDLGGIKFVILRDREGI--VQVTApkkkvdKELFKtVRKLSRESVISVTGT-VKAEPKAPNgVEIIP 88
|
90
....*....|...
gi 568950598 113 EKIEVIGdcEAKA 125
Cdd:cd04316 89 EEIEVLS--EAKT 99
|
|
| ScAspRS_mt_like_N |
cd04321 |
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
44-117 |
3.50e-04 |
|
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces cerevisiae mitochondrial (mt) aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this fungal 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. Mutations in the gene for S. cerevisiae mtAspRS result in a "petite" phenotype typical for a mutation in a nuclear gene that results in a non-functioning mitochondrial protein synthesis system.
Pssm-ID: 239816 [Multi-domain] Cd Length: 86 Bit Score: 39.22 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 44 VTVQGWI--RSVRSQKEVlFLHVNDgSSLESLQIVADSSFDS----RELTFGSSVQVQGQLvksQSKRQNVELKAEKIEV 117
Cdd:cd04321 2 VTLNGWIdrKPRIVKKLS-FADLRD-PNGDIIQLVSTAKKDAfsllKSITAESPVQVRGKL---QLKEAKSSEKNDEWEL 76
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
44-118 |
4.35e-03 |
|
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces cerevisiae and human cytoplasmic aspartyl-tRNA synthetase (AspRS). 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.
Pssm-ID: 239815 [Multi-domain] Cd Length: 102 Bit Score: 36.39 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950598 44 VTVQGWIRSVRSQKEVL-FLHVNDGSSleSLQIVADSSFDS---------RELTFGSSVQVQGQLVKSQSK-----RQNV 108
Cdd:cd04320 2 VLIRARVHTSRAQGAKLaFLVLRQQGY--TIQGVLAASAEGvskqmvkwaGSLSKESIVDVEGTVKKPEEPiksctQQDV 79
|
90
....*....|
gi 568950598 109 ELKAEKIEVI 118
Cdd:cd04320 80 ELHIEKIYVV 89
|
|
| |
