|
Name |
Accession |
Description |
Interval |
E-value |
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
27-474 |
0e+00 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 591.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 27 KLSVRDALgAQNASGERIKIQGWIRSVRSQKEVLFLHVNDGSSLESLQVVADSGLDS----RELNFGSSVEVQGQLIKSP 102
Cdd:PRK03932 3 RVSIKDIL-KGKYVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDNGEEYfeeiKKLTTGSSVIVTGTVVESP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 103 SKRQNVELKAEKIKVIGNcDAKDFPIKyKERHPLEYLRQYPHFRCRTNVLGSILRIRSEATAAIHSFFKDSGFVHIHTPI 182
Cdd:PRK03932 82 RAGQGYELQATKIEVIGE-DPEDYPIQ-KKRHSIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVDTPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 183 ITSNDSEGAGELFQLepSGKLKVPEENFFNVPAFLTVSGQLHLEVMSGAFTQVFTFGPTFRAENSQSRRHLAEFYMIEAE 262
Cdd:PRK03932 160 ITASDCEGAGELFRV--TTLDLDFSKDFFGKEAYLTVSGQLYAEAYAMALGKVYTFGPTFRAENSNTRRHLAEFWMIEPE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 263 ISFVDsLQDLMQVIEELFKATTMMVLSKCPEDVELCHKFIAPGQKDRLEHMLKNNFLIISYTEAVEILKQASQNFTFTPE 342
Cdd:PRK03932 238 MAFAD-LEDNMDLAEEMLKYVVKYVLENCPDDLEFLNRRVDKGDIERLENFIESPFPRITYTEAIEILQKSGKKFEFPVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 343 WGADLRTEHEKYLV-KHCGNiPVFVINYPLTLKPFYMRDNEDGpqHTVAAVDLLVPGVGELFGGGLREERYHFLEERLAR 421
Cdd:PRK03932 317 WGDDLGSEHERYLAeEHFKK-PVFVTNYPKDIKAFYMRLNPDG--KTVAAMDLLAPGIGEIIGGSQREERLDVLEARIKE 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 226491502 422 SGL-TEVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFPRFPHS 474
Cdd:PRK03932 394 LGLnKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGR 447
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
29-475 |
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: 556.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 29 SVRDALGAQnaSGERIKIQGWIRSVRSQKEVLFLHVNDGSSLesLQVVADSGL-----DSRELNFGSSVEVQGQLIKSPS 103
Cdd:COG0017 4 YIKDLLPEH--VGQEVTVAGWVRTKRDSGGISFLILRDGSGF--IQVVVKKDKlenfeEAKKLTTESSVEVTGTVVESPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 104 KRQNVELKAEKIKVIGNCDaKDFPIKYKeRHPLEYLRQYPHFRCRTNVLGSILRIRSEATAAIHSFFKDSGFVHIHTPII 183
Cdd:COG0017 80 APQGVELQAEEIEVLGEAD-EPYPLQPK-RHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVEVHTPII 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 184 TSNDSEGAGELFQLEpsgklkvpeenFFNVPAFLTVSGQLHLEVMSGAFTQVFTFGPTFRAENSQSRRHLAEFYMIEAEI 263
Cdd:COG0017 158 TASATEGGGELFPVD-----------YFGKEAYLTQSGQLYKEALAMALEKVYTFGPTFRAEKSNTRRHLAEFWMIEPEM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 264 SFVDsLQDLMQVIEELFKATTMMVLSKCPEDVELCHKFIapgqkDRLEHMLKNNFLIISYTEAVEILKQASQNFtftpEW 343
Cdd:COG0017 227 AFAD-LEDVMDLAEEMLKYIIKYVLENCPEELEFLGRDV-----ERLEKVPESPFPRITYTEAIEILKKSGEKV----EW 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 344 GADLRTEHEKYLVKHCGNIPVFVINYPLTLKPFYMRDNEDGPQhTVAAVDLLVPGVGELFGGGLREERYHFLEERLARSG 423
Cdd:COG0017 297 GDDLGTEHERYLGEEFFKKPVFVTDYPKEIKAFYMKPNPDDPK-TVAAFDLLAPGIGEIIGGSQREHRYDVLVERIKEKG 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 226491502 424 L-TEVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFPRFPHSC 475
Cdd:COG0017 376 LdPEDYEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRL 428
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
27-475 |
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: 531.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 27 KLSVRDAL-GAQNASGERIKIQGWIRSVRSQKEVLFLHVNDGSSLESLQVVADSGLDSRE------LNFGSSVEVQGQLI 99
Cdd:TIGR00457 1 SAAIKDLLqQVYKFVGDEVTVSGWVRTKRSSKKIIFLELNDGSSLGPIQAVINGEDNPYLfqllksLTTGSSVSVTGKVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 100 KSPSKRQNVELKAEKIKVIGNCDAKDFPIKyKERHPLEYLRQYPHFRCRTNVLGSILRIRSEATAAIHSFFKDSGFVHIH 179
Cdd:TIGR00457 81 ESPGKGQPVELQVKKIEVVGEAEPDDYPLQ-KKEHSLEFLRDIAHLRLRTNTLGAVMRVRNALSQAIHRYFQENGFTWVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 180 TPIITSNDSEGAGELFQLEPSGKlkVPEENFFNVPAFLTVSGQLHLEVMSGAFTQVFTFGPTFRAENSQSRRHLAEFYMI 259
Cdd:TIGR00457 160 PPILTSNDCEGAGELFRVSTGNI--DFSQDFFGKEAYLTVSGQLYLETYALALSKVYTFGPTFRAEKSNTSRHLSEFWMI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 260 EAEISFVDsLQDLMQVIEELFKATTMMVLSKCPEDVELCHKFIAPGQKDRLEHMLKNNFLIISYTEAVEILKQASQNFTF 339
Cdd:TIGR00457 238 EPEMAFAN-LNDLLQLAETLIKYIIKAVLENCSQELKFLEKNFDKDLIKRLENIINNKFARITYTDAIEILKESDKNFEY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 340 TPEWGADLRTEHEKYLVKHCGNIPVFVINYPLTLKPFYMRDNEDGpqHTVAAVDLLVPGVGELFGGGLREERYHFLEERL 419
Cdd:TIGR00457 317 EDFWGDDLQTEHERFLAEEYFKPPVFVTNYPKDIKAFYMKLNDDG--KTVAAMDLLAPGIGEIIGGSEREDDLDKLENRM 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 226491502 420 ARSGL-TEVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFPRFPHSC 475
Cdd:TIGR00457 395 KEMGLdTDALNWYLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGNI 451
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
133-473 |
6.82e-157 |
|
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: 447.78 E-value: 6.82e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 133 RHPLEYLRQYPHFRCRTNVLGSILRIRSEATAAIHSFFKDSGFVHIHTPIITSNDSEGAGELFQLepsgklkvpeeNFFN 212
Cdd:cd00776 1 DANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKV-----------SYFG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 213 VPAFLTVSGQLHLEVMSGAFTQVFTFGPTFRAENSQSRRHLAEFYMIEAEISFVDSLQDLMQVIEELFKATTMMVLSKCP 292
Cdd:cd00776 70 KPAYLAQSPQLYKEMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEDYNEVMDLIEELIKYIFKRVLERCA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 293 EDVELChkfiapGQKDRLEHMLKNNFLIISYTEAVEILKQASQNftFTPEWGADLRTEHEKYLVKHCGNIPVFVINYPLT 372
Cdd:cd00776 150 KELELV------NQLNRELLKPLEPFPRITYDEAIELLREKGVE--EEVKWGEDLSTEHERLLGEIVKGDPVFVTDYPKE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 373 LKPFYMRDNEDGPQhTVAAVDLLVPGVGELFGGGLREERYHFLEERLARSGL-TEVYQWYLDLRRFGSVPHGGFGMGFER 451
Cdd:cd00776 222 IKPFYMKPDDDNPE-TVESFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGLdPESFEWYLDLRKYGMPPHGGFGLGLER 300
|
330 340
....*....|....*....|..
gi 226491502 452 YLQCILGVDNIKDVIPFPRFPH 473
Cdd:cd00776 301 LVMWLLGLDNIREAILFPRDPK 322
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
27-474 |
6.49e-156 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 454.43 E-value: 6.49e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 27 KLSVRDALGAQNAS----GERIKIQGWIRSVRSQKEVLFLHVNDGSSLESLQVVADSG------LDSRELNFGSSVEVQG 96
Cdd:PLN02603 89 KLRIADVKGGEDEGlarvGKTLNVMGWVRTLRAQSSVTFIEVNDGSCLSNMQCVMTPDaegydqVESGLITTGASVLVQG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 97 QLIKSPSKRQNVELKAEKIKVIGNCDAKdFPIKyKERHPLEYLRQYPHFRCRTNVLGSILRIRSEATAAIHSFFKDSGFV 176
Cdd:PLN02603 169 TVVSSQGGKQKVELKVSKIVVVGKSDPS-YPIQ-KKRVSREFLRTKAHLRPRTNTFGAVARVRNALAYATHKFFQENGFV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 177 HIHTPIITSNDSEGAGELFQL--------EPSGKL--KVPE---------ENFFNVPAFLTVSGQLHLEVMSGAFTQVFT 237
Cdd:PLN02603 247 WVSSPIITASDCEGAGEQFCVttlipnsaENGGSLvdDIPKtkdglidwsQDFFGKPAFLTVSGQLNGETYATALSDVYT 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 238 FGPTFRAENSQSRRHLAEFYMIEAEISFVDsLQDLMQVIEELFKATTMMVLSKCPEDVELCHKFIAPGQKDRLEHMLKNN 317
Cdd:PLN02603 327 FGPTFRAENSNTSRHLAEFWMIEPELAFAD-LNDDMACATAYLQYVVKYILENCKEDMEFFNTWIEKGIIDRLSDVVEKN 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 318 FLIISYTEAVEILKQASQNFTFTPEWGADLRTEHEKYLVKHC-GNIPVFVINYPLTLKPFYMRDNEDGpqHTVAAVDLLV 396
Cdd:PLN02603 406 FVQLSYTDAIELLLKAKKKFEFPVKWGLDLQSEHERYITEEAfGGRPVIIRDYPKEIKAFYMRENDDG--KTVAAMDMLV 483
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226491502 397 PGVGELFGGGLREERYHFLEERLARSGLT-EVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFPRFPHS 474
Cdd:PLN02603 484 PRVGELIGGSQREERLEYLEARLDELKLNkESYWWYLDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFPRVPGS 562
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
21-472 |
1.19e-138 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 410.54 E-value: 1.19e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 21 KHKPSAKLSVRDAL----GAQNASGERIKIQGWIRSVRSQKE--VLFLHVNDGSSLESLQVVADSGLD--SRELNFGSSV 92
Cdd:PLN02221 26 KAQFSDRVLIRSILdrpdGGAGLAGQKVRIGGWVKTGREQGKgtFAFLEVNDGSCPANLQVMVDSSLYdlSTLVATGTCV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 93 EVQGqLIKSPSK----RQNVELKAEKIKVIGNCDAKDFPIKyKERHPLEYLRQYPHFRCRTNVLGSILRIRSEATAAIHS 168
Cdd:PLN02221 106 TVDG-VLKVPPEgkgtKQKIELSVEKVIDVGTVDPTKYPLP-KTKLTLEFLRDVLHLRSRTNSISAVARIRNALAFATHS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 169 FFKDSGFVHIHTPIITSNDSEGAGELFQ---------------------------------------------------- 196
Cdd:PLN02221 184 FFQEHSFLYIHTPIITTSDCEGAGEMFQvttlinyterleqdlidnpppteadveaarlivkergevvaqlkaakaskee 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 197 -----------------LEPSGKLK--VPE--------ENFFNVPAFLTVSGQLHLEVMSGAFTQVFTFGPTFRAENSQS 249
Cdd:PLN02221 264 itaavaelkiakeslahIEERSKLKpgLPKkdgkidysKDFFGRQAFLTVSGQLQVETYACALSSVYTFGPTFRAENSHT 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 250 RRHLAEFYMIEAEISFVDsLQDLMQVIEELFKATTMMVLSKCPEDVELCHKFIAPGQKDRLEHMLKNNFLIISYTEAVEI 329
Cdd:PLN02221 344 SRHLAEFWMVEPEIAFAD-LEDDMNCAEAYVKYMCKWLLDKCFDDMELMAKNFDSGCIDRLRMVASTPFGRITYTEAIEL 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 330 LKQA---SQNFTFTPEWGADLRTEHEKYLVKHCGNIPVFVINYPLTLKPFYMRDNEDgpQHTVAAVDLLVPGVGELFGGG 406
Cdd:PLN02221 423 LEEAvakGKEFDNNVEWGIDLASEHERYLTEVLFQKPLIVYNYPKGIKAFYMRLNDD--EKTVAAMDVLVPKVGELIGGS 500
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226491502 407 LREERYHFLEERLARSGL-TEVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFPRFP 472
Cdd:PLN02221 501 QREERYDVIKQRIEEMGLpIEPYEWYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPRYP 567
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
51-470 |
5.52e-121 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 367.27 E-value: 5.52e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 51 RSVRSQKEVLFLHVNDGSSLESLQVVADSGLD--SRELNFGSSVEVQG--QLIKSPSKRQNVELKAEKIKVIGNCDAKDF 126
Cdd:PLN02532 127 KSAPPPPSVAYLLISDGSCVASLQVVVDSALAplTQLMATGTCILAEGvlKLPLPAQGKHVIELEVEKILHIGTVDPEKY 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 127 PIKyKERHPLEYLRQYPHFRCRTNVLGSILRIRSEATAAIHSFFKDSGFVHIHTPIITSNDSEGAGELF----------- 195
Cdd:PLN02532 207 PLS-KKRLPLDMLRDFSHFRPRTTTVASVTRVRSALTHATHTFFQDHGFLYVQVPIITTTDATGFGEMFrvttllgksdd 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 196 ---------------------------------------------------------QLEPSGKLKVP----------EE 208
Cdd:PLN02532 286 keekkpvhetegisleavkaaikektnlveelkrsesnrealvaaeqdlrktnqlasQLEAKEKLKTGtsvkadklsfSK 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 209 NFFNVPAFLTVSGQLHLEVMSGAFTQVFTFGPTFRAENSQSRRHLAEFYMIEAEISFVDsLQDLMQVIEELFKATTMMVL 288
Cdd:PLN02532 366 DFFSRPTYLTVSGRLHLESYACALGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAFSE-LEDAMNCAEDYFKFLCKWVL 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 289 SKCPEDVELCHKFIAPGQKDRLEHMLKNNFLIISYTEAVEILKQASQN-FTFTPEWGADLRTEHEKYLVKHCGNIPVFVI 367
Cdd:PLN02532 445 ENCSEDMKFVSKRIDKTISTRLEAIISSSLQRISYTEAVDLLKQATDKkFETKPEWGIALTTEHLSYLADEIYKKPVIIY 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 368 NYPLTLKPFYMRDNEDGpqHTVAAVDLLVPGVGELFGGGLREERYHFLEERLARSGLT-EVYQWYLDLRRFGSVPHGGFG 446
Cdd:PLN02532 525 NYPKELKPFYVRLNDDG--KTVAAFDLVVPKVGTVITGSQNEERMDILNARIEELGLPrEQYEWYLDLRRHGTVKHSGFS 602
|
490 500
....*....|....*....|....
gi 226491502 447 MGFERYLQCILGVDNIKDVIPFPR 470
Cdd:PLN02532 603 LGFELMVLFATGLPDVRDAIPFPR 626
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
11-472 |
2.81e-118 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 358.95 E-value: 2.81e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 11 VRFCSSAPFPKHKPSAKLSVRDalgaQNASGERIKIQGWIRSVRSQK--EVLFLHVNDGSSLESLQVVADSGLDSRE--- 85
Cdd:PTZ00425 55 IRICNVLNVPKSEKEFNDNSRK----NKYIDQIITVCGWSKAVRKQGggRFCFVNLNDGSCHLNLQIIVDQSIENYEkll 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 86 -LNFGSSVEVQGQLIKSPSK--------RQNVELKAE-----KIKVIG-NCDAKDFPIKyKERHPLEYLRQYPHFRCRTN 150
Cdd:PTZ00425 131 kCGVGCCFRFTGKLIISPVQnenkkgllKENVELALKdnsihNFEIYGeNLDPQKYPLS-KKNHGKEFLREVAHLRPRSY 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 151 VLGSILRIRSEATAAIHSFFKDSGFVHIHTPIITSNDSEGAGELFQLE------------PSGKLKVPE----------- 207
Cdd:PTZ00425 210 FISSVIRIRNALAIATHLFFQSRGFLYIHTPLITTSDCEGGGEMFTVTtllgedadyraiPRVNKKNKKgekredilntc 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 208 -----------------------------ENFFNVPAFLTVSGQLHLEVMSGAFTQVFTFGPTFRAENSQSRRHLAEFYM 258
Cdd:PTZ00425 290 nannnngnssssnavsspaypdqylidykKDFFSKQAFLTVSGQLSLENLCSSMGDVYTFGPTFRAENSHTSRHLAEFWM 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 259 IEAEISFVDsLQDLMQVIEELFKATTMMVLSKCPEDVELCHKFIAPGQKDRLEHMLKNNFLIISYTEAVEILKQASQNFT 338
Cdd:PTZ00425 370 IEPEIAFAD-LYDNMELAESYIKYCIGYVLNNNFDDIYYFEENVETGLISRLKNILDEDFAKITYTNVIDLLQPYSDSFE 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 339 FTPEWGADLRTEHEKYLVKHCGNIPVFVINYPLTLKPFYMRDNEDgpQHTVAAVDLLVPGVGELFGGGLREERYHFLEER 418
Cdd:PTZ00425 449 VPVKWGMDLQSEHERFVAEQIFKKPVIVYNYPKDLKAFYMKLNED--QKTVAAMDVLVPKIGEVIGGSQREDNLERLDKM 526
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 226491502 419 LARSGLT-EVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFPRFP 472
Cdd:PTZ00425 527 IKEKKLNmESYWWYRQLRKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFPRYP 581
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
136-470 |
1.69e-94 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 288.70 E-value: 1.69e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 136 LEYLRQYPHFRCRTNVLGSILRIRSEATAAIHSFFKDSGFVHIHTPIITSNDSEGAGELFQLePSGKLKvpeeNFFnvpa 215
Cdd:pfam00152 2 EETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLV-PSRALG----KFY---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 216 FLTVSGQLHLEV-MSGAFTQVFTFGPTFRAENSQSRRHLaEFYMIEAEISFVDsLQDLMQVIEELFKATTMMVLsKCPED 294
Cdd:pfam00152 73 ALPQSPQLYKQLlMVAGFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVD-YEDVMDLTEELIKEIFKEVE-GIAKE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 295 VELchkfiapgqkdRLEHMLKNNFLIISYTEAVEILKQASqnftfTPEWGADLRTEHEKYLV----KHCGNIPVFVINYP 370
Cdd:pfam00152 150 LEG-----------GTLLDLKKPFPRITYAEAIEKLNGKD-----VEELGYGSDKPDLRFLLelviDKNKFNPLWVTDFP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 371 LTLKPFYMRDNEDGPQHTvAAVDLLVPGVgELFGGGLREERYHFLEERLARSGLT-----EVYQWYLDLRRFGSVPHGGF 445
Cdd:pfam00152 214 AEHHPFTMPKDEDDPALA-EAFDLVLNGV-EIGGGSIRIHDPELQEERFEEQGLDpeeaeEKFGFYLDALKYGAPPHGGL 291
|
330 340
....*....|....*....|....*
gi 226491502 446 GMGFERYLQCILGVDNIKDVIPFPR 470
Cdd:pfam00152 292 GIGLDRLVMLLTGLESIREVIAFPK 316
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
41-473 |
6.51e-88 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 275.53 E-value: 6.51e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 41 GERIKIQGWIRSVRSQKEVLFLHVNDGSSLesLQVVADSG------LDSRELNFGSSVEVQGQLIKSPSKRQNVELKAEK 114
Cdd:PRK05159 16 GEEVTLAGWVHEIRDLGGIAFLILRDRSGI--IQVVVKKKvdeelfETIKKLKRESVVSVTGTVKANPKAPGGVEVIPEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 115 IKVIGNCDAKdFPI---KYKERHP---LEY----LRqyphfRCRTNvlgSILRIRSEATAAIHSFFKDSGFVHIHTPIIT 184
Cdd:PRK05159 94 IEVLNKAEEP-LPLdisGKVLAELdtrLDNrfldLR-----RPRVR---AIFKIRSEVLRAFREFLYENGFTEIFTPKIV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 185 SNDSEGAGELFQLepsgklkvpeeNFFNVPAFLTVSGQLHLEVMSGA-FTQVFTFGPTFRAENSQSRRHLAEFYMIEAEI 263
Cdd:PRK05159 165 ASGTEGGAELFPI-----------DYFEKEAYLAQSPQLYKQMMVGAgFERVFEIGPVFRAEEHNTSRHLNEYTSIDVEM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 264 SFVDSLQDLMQVIEELFKATTMMVLSKCPEDVELchkfiapgqkdrLEHML---KNNFLIISYTEAVEILKQASQNftft 340
Cdd:PRK05159 234 GFIDDHEDVMDLLENLLRYMYEDVAENCEKELEL------------LGIELpvpETPIPRITYDEAIEILKSKGNE---- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 341 PEWGADLRTEHEKYLVKH----CGNIPVFVINYPLTLKPFYMRDNEDGPQHTvAAVDLLVPGVgELFGGGLREERYHFLE 416
Cdd:PRK05159 298 ISWGDDLDTEGERLLGEYvkeeYGSDFYFITDYPSEKRPFYTMPDEDDPEIS-KSFDLLFRGL-EITSGGQRIHRYDMLV 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 226491502 417 ERLARSGL-TEVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFPRFPH 473
Cdd:PRK05159 376 ESIKEKGLnPESFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFPRDRH 433
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
41-473 |
1.21e-58 |
|
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: 199.28 E-value: 1.21e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 41 GERIKIQGWIRSVRSQKEVLFLHVNDGSSLesLQVVADSGLDSRE-------LNFGSSVEVQGQLIKSPSKRQNVELKAE 113
Cdd:TIGR00458 12 GQEVTFMGWVHEIRDLGGLIFVLLRDREGL--IQITAPAKKVSKNlfkwakkLNLESVVAVRGIVKIKEKAPGGFEIIPT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 114 KIKVIGNCDAKdFPIKYKERHP--LEYLRQYPHFRCRTNVLGSILRIRSEATAAIHSFFKDSGFVHIHTPIITSNDSEGA 191
Cdd:TIGR00458 90 KIEVINEAKEP-LPLDPTEKVPaeLDTRLDYRFLDLRRPTVQAIFRIRSGVLESVREFLAEEGFIEVHTPKLVASATEGG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 192 GELFQLepsgklkvpeeNFFNVPAFLTVSGQLHLEV-MSGAFTQVFTFGPTFRAENSQSRRHLAEFYMIEAEISFVDSlQ 270
Cdd:TIGR00458 169 TELFPI-----------TYFEREAFLGQSPQLYKQQlMAAGFERVYEIGPIFRAEEHNTHRHLNEATSIDIEMAFEDH-H 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 271 DLMQVIEELFKATTMMVLSKCPEDVE-LCHKF-IAPGQKDRLEhmlknnfliisYTEAVEILKQASQNFTftpeWGADLR 348
Cdd:TIGR00458 237 DVMDILEELVVRVFEDVPERCAHQLEtLEFKLeKPEGKFVRLT-----------YDEAIEMANAKGVEIG----WGEDLS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 349 TEHEKYLVKHCGNIpVFVINYPLTLKPFYMRDNEDGPQHTvAAVDLLVPGVgELFGGGLREERYHFLEERLARSGLT-EV 427
Cdd:TIGR00458 302 TEAEKALGEEMDGL-YFITDWPTEIRPFYTMPDEDNPEIS-KSFDLMYRDL-EISSGAQRIHLHDLLVERIKAKGLNpEG 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 226491502 428 YQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFPRFPH 473
Cdd:TIGR00458 379 FKDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFPRDRK 424
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
154-472 |
4.59e-57 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 192.16 E-value: 4.59e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 154 SILRIRSEATAAIHSFFKDSGFVHIHTPIITSNDSEGAGelfqLEPSGKLKVPEENFFNVPAFLTVSGQLHLEVMSGAFT 233
Cdd:PRK06462 28 KVLKVQSSILRYTREFLDGRGFVEVLPPIISPSTDPLMG----LGSDLPVKQISIDFYGVEYYLADSMILHKQLALRMLG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 234 QVFTFGPTFRAEN--SQSRRHLAEFYMIEAEISFVDsLQDLMQVIEELFKATTMMVLSKCPEDVELCHKfiapgqkdRLE 311
Cdd:PRK06462 104 KIFYLSPNFRLEPvdKDTGRHLYEFTQLDIEIEGAD-LDEVMDLIEDLIKYLVKELLEEHEDELEFFGR--------DLP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 312 HmLKNNFLIISYTEAVEILKqasqNFTFTPEWGADLRTEHEKYLVKHCGNiPVFVINYPLTLKPFYMRDNEDGPQHTVAA 391
Cdd:PRK06462 175 H-LKRPFKRITHKEAVEILN----EEGCRGIDLEELGSEGEKSLSEHFEE-PFWIIDIPKGSREFYDREDPERPGVLRNY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 392 vDLLVP-GVGELFGGGLREERYHFLEERLARSGLT-EVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFP 469
Cdd:PRK06462 249 -DLLLPeGYGEAVSGGEREYEYEEIVERIREHGVDpEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQPFP 327
|
...
gi 226491502 470 RFP 472
Cdd:PRK06462 328 RVP 330
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
40-475 |
2.87e-44 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 162.95 E-value: 2.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 40 SGERIKIQGWIRSVRSQKEVLFLHVNdgSSLESLQVVAD--------------SGLdSRElnfgSSVEVQGqLIKSPSK- 104
Cdd:PLN02850 80 AGSEVLIRGRVHTIRGKGKSAFLVLR--QSGFTVQCVVFvsevtvskgmvkyaKQL-SRE----SVVDVEG-VVSVPKKp 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 105 ----RQNVELKAEKIKVIGNCDAK-DFPIKYKERHPLEYL------RQYPH--------FRC---RTNVLGSILRIRSEA 162
Cdd:PLN02850 152 vkgtTQQVEIQVRKIYCVSKALATlPFNVEDAARSESEIEkalqtgEQLVRvgqdtrlnNRVldlRTPANQAIFRIQSQV 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 163 TAAIHSFFKDSGFVHIHTPIITSNDSEGAGELFQLEpsgklkvpeenFFNVPAFLTVSGQLHLEV-MSGAFTQVFTFGPT 241
Cdd:PLN02850 232 CNLFREFLLSKGFVEIHTPKLIAGASEGGSAVFRLD-----------YKGQPACLAQSPQLHKQMaICGDFRRVFEIGPV 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 242 FRAENSQSRRHLAEFYMIEAEISFVDSLQDLMQVIEELFKATTMMVLSKCPEDVELC---HKFiapgqkDRLEHMLKNnf 318
Cdd:PLN02850 301 FRAEDSFTHRHLCEFTGLDLEMEIKEHYSEVLDVVDELFVAIFDGLNERCKKELEAIreqYPF------EPLKYLPKT-- 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 319 LIISYTEAVEILKQASqnftFTPEWGADLRTEHEKYL---VKHCGNIPVFVIN-YPLTLKPFYMRDNEDGPQHTvAAVDL 394
Cdd:PLN02850 373 LRLTFAEGIQMLKEAG----VEVDPLGDLNTESERKLgqlVKEKYGTDFYILHrYPLAVRPFYTMPCPDDPKYS-NSFDV 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 395 LVPGvGELFGGGLREERYHFLEERLARSGL-TEVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFPRFPH 473
Cdd:PLN02850 448 FIRG-EEIISGAQRVHDPELLEKRAEECGIdVKTISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPRDPQ 526
|
..
gi 226491502 474 SC 475
Cdd:PLN02850 527 RL 528
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
1-473 |
4.47e-36 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 140.51 E-value: 4.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 1 MLGVRCLLRSVRFCSSapfpKHKPSAKLSVRDALGaqnasgERIKIQGWIRSVRSQKEVLFLHVNDGS-SLESLQVVADS 79
Cdd:PTZ00401 48 VFGAAPMVQSTTYKSR----TFIPVAVLSKPELVD------KTVLIRARVSTTRKKGKMAFMVLRDGSdSVQAMAAVEGD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 80 gLDSRELNF------GSSVEVQG------QLIKSPSKrQNVELKAEKIKVIGNC---------------DAKDFPIKYKE 132
Cdd:PTZ00401 118 -VPKEMIDFigqiptESIVDVEAtvckveQPITSTSH-SDIELKVKKIHTVTESlrtlpftledasrkeSDEGAKVNFDT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 133 RHPLEYLRqyphfrCRTNVLGSILRIRSEATAAIHSFFKDSGFVHIHTPIITSNDSEGAGELFQLEpsgklkvpeenFFN 212
Cdd:PTZ00401 196 RLNSRWMD------LRTPASGAIFRLQSRVCQYFRQFLIDSDFCEIHSPKIINAPSEGGANVFKLE-----------YFN 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 213 VPAFLTVSGQLHLE-VMSGAFTQVFTFGPTFRAENSQSRRHLAEFYMIEAEISFVDSLQDLMQVIEELFKATTMMVLSKC 291
Cdd:PTZ00401 259 RFAYLAQSPQLYKQmVLQGDVPRVFEVGPVFRSENSNTHRHLTEFVGLDVEMRINEHYYEVLDLAESLFNYIFERLATHT 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 292 PEDVELCHKF--------IAPGQKDRLE------------------HMLKNNFLIISYTEAVEILKQASQNfTFTPEwgA 345
Cdd:PTZ00401 339 KELKAVCQQYpfeplvwkLTPERMKELGvgvisegveptdkyqarvHNMDSRMLRINYMHCIELLNTVLEE-KMAPT--D 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 346 DLRTEHEKY---LVKHCGNIPVFVIN-YPLTLKPFYMRDNEDGPQHTvAAVDLLVPGvGELFGGGlreERYHFLEERLAR 421
Cdd:PTZ00401 416 DINTTNEKLlgkLVKERYGTDFFISDrFPSSARPFYTMECKDDERFT-NSYDMFIRG-EEISSGA---QRIHDPDLLLAR 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 226491502 422 SGLTEV----YQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFPRFPH 473
Cdd:PTZ00401 491 AKMLNVdltpIKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFPRDPQ 546
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
156-470 |
1.86e-35 |
|
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: 132.60 E-value: 1.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 156 LRIRSEATAAIHSFFKDSGFVHIHTPIITSNDSEGAGELFQLepsgKLKVPEENffnvpAFLTVSGQLHLE-VMSGAFTQ 234
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLV----KYNALGLD-----YYLRISPQLFKKrLMVGGLDR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 235 VFTFGPTFRAENSqSRRHLAEFYMIEAEISFVDsLQDLMQVIEELFKATTMMVLSKcpEDVELCHKFIAPGQKdrlehml 314
Cdd:cd00669 72 VFEINRNFRNEDL-RARHQPEFTMMDLEMAFAD-YEDVIELTERLVRHLAREVLGV--TAVTYGFELEDFGLP------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 315 knnFLIISYTEAVEILKQasqnftftpewgadlrtehekylvkhcgniPVFVINYPLTLKPFYMRDNEDGPQHTvAAVDL 394
Cdd:cd00669 141 ---FPRLTYREALERYGQ------------------------------PLFLTDYPAEMHSPLASPHDVNPEIA-DAFDL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 395 LVPGVgELFGGGLREERYHFLEERLARSGLTEVYQ-----WYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFP 469
Cdd:cd00669 187 FINGV-EVGNGSSRLHDPDIQAEVFQEQGINKEAGmeyfeFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFP 265
|
.
gi 226491502 470 R 470
Cdd:cd00669 266 K 266
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
44-120 |
2.27e-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: 118.05 E-value: 2.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 44 IKIQGWIRSVRSQKEVLFLHVNDGSSLESLQVVADSGLDSRE----LNFGSSVEVQGQLIKSPSKRQNVELKAEKIKVIG 119
Cdd:cd04318 2 VTVNGWVRSVRDSKKISFIELNDGSCLKNLQVVVDKELTNFKeilkLSTGSSIRVEGVLVKSPGAKQPFELQAEKIEVLG 81
|
.
gi 226491502 120 N 120
Cdd:cd04318 82 E 82
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
156-469 |
3.53e-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: 104.58 E-value: 3.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 156 LRIRSEATAAIHSFFKDSGFVHIHTPIITSNDSEGAGELfqLEPSgklKVPEENFFNVPAfltvSGQLHLEV-MSGAFTQ 234
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTPEGARDF--LVPS---RLHPGKFYALPQ----SPQLFKQLlMVSGFDR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 235 VFTFGPTFRAENSQSRRHlAEFYMIEAEISFVDSlQDLMQVIEELFkattmmvlskcpedvelCHKFiapgqKDRLEHML 314
Cdd:cd00777 72 YFQIARCFRDEDLRADRQ-PEFTQIDIEMSFVDQ-EDIMSLIEGLL-----------------KYVF-----KEVLGVEL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 315 KNNFLIISYTEAVEilkqasqNFTFTPEWGADL-----RTEHEKYLVKHcgnipvfvinYPLTL-KPFYMRDNEDGPQHT 388
Cdd:cd00777 128 TTPFPRMTYAEAME-------RYGFKFLWIVDFplfewDEEEGRLVSAH----------HPFTApKEEDLDLLEKDPEDA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 389 VA-AVDLLVPGVgELFGGGLREERYHFLEERLARSGLTEVYQW-----YLDLRRFGSVPHGGFGMGFERYLQCILGVDNI 462
Cdd:cd00777 191 RAqAYDLVLNGV-ELGGGSIRIHDPDIQEKVFEILGLSEEEAEekfgfLLEAFKYGAPPHGGIALGLDRLVMLLTGSESI 269
|
....*..
gi 226491502 463 KDVIPFP 469
Cdd:cd00777 270 RDVIAFP 276
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
43-119 |
5.12e-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: 78.76 E-value: 5.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 43 RIKIQGWIRSVRSQKEVLFLHVNDGSSleSLQVVADSGLDS------RELNFGSSVEVQGQLIKSP---SKRQNVELKAE 113
Cdd:cd04100 1 EVTLAGWVHSRRDHGGLIFIDLRDGSG--IVQVVVNKEELGeffeeaEKLRTESVVGVTGTVVKRPegnLATGEIELQAE 78
|
....*.
gi 226491502 114 KIKVIG 119
Cdd:cd04100 79 ELEVLS 84
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
40-470 |
2.06e-16 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 81.96 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 40 SGERIKIQGWIRSVRSQKEVLFLHVNDGSSLesLQVVADSGLDSREL-NFGSS------VEVQGQLIKSPSKRQN----- 107
Cdd:PRK12820 17 TGREVCLAGWVDAFRDHGELLFIHLRDRNGF--IQAVFSPEAAPADVyELAASlraefcVALQGEVQKRLEETENphiet 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 108 --VELKAEKIKVIGNCDAKDFPIKYKER----------HPLEYLR-QYPHFRCRTNVLGSILRIRSEATAAIHSFFKDSG 174
Cdd:PRK12820 95 gdIEVFVRELSILAASEALPFAISDKAMtagagsagadAVNEDLRlQYRYLDIRRPAMQDHLAKRHRIIKCARDFLDSRG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 175 FVHIHTPIITSNDSEGAGELfqLEPSgklKVPEENFFNVPAFLTVSGQLhleVMSGAFTQVFTFGPTFRAENSQSRRHlA 254
Cdd:PRK12820 175 FLEIETPILTKSTPEGARDY--LVPS---RIHPKEFYALPQSPQLFKQL---LMIAGFERYFQLARCFRDEDLRPNRQ-P 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 255 EFYMIEAEISFVDSlQDLMQVIEELFK-------------------ATTMMVLSKCPEDVELCHKFI------------- 302
Cdd:PRK12820 246 EFTQLDIEASFIDE-EFIFELIEELTArmfaiggialprpfprmpyAEAMDTTGSDRPDLRFDLKFAdatdifentrygi 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 303 ---------------APGQKDRL-EHMLKNNF---LIISYTEAVEILKQASQ--------NFTFTPEWGADLRTEHEK-- 353
Cdd:PRK12820 325 fkqilqrggrikginIKGQSEKLsKNVLQNEYakeIAPSFGAKGMTWMRAEAggldsnivQFFSADEKEALKRRFHAEdg 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 354 -------------------YLVKHCGN----------IPVFVINYPL-----------TLKPFYMRDNEDGPQHTVA--- 390
Cdd:PRK12820 405 dviimiadascaivlsalgQLRLHLADrlglipegvfHPLWITDFPLfeatddggvtsSHHPFTAPDREDFDPGDIEell 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 391 -----AVDLLVPGvGELFGGGLREERYHFLEERLARSGLTE-----VYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVD 460
Cdd:PRK12820 485 dlrsrAYDLVVNG-EELGGGSIRINDKDIQLRIFAALGLSEediedKFGFFLRAFDFAAPPHGGIALGLDRVVSMILQTP 563
|
570
....*....|
gi 226491502 461 NIKDVIPFPR 470
Cdd:PRK12820 564 SIREVIAFPK 573
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
156-469 |
8.33e-16 |
|
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: 78.40 E-value: 8.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 156 LRIRSEATAAIHSFFKDSGFVHIHTPIItsndsegagelfQLEPSGKLKVP---EENFFNVPAFLTVSGQLHLE-VMSGA 231
Cdd:cd00775 8 FIVRSKIISYIRKFLDDRGFLEVETPML------------QPIAGGAAARPfitHHNALDMDLYLRIAPELYLKrLIVGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 232 FTQVFTFGPTFRAEnSQSRRHLAEFYMIEAEISFVDsLQDLMQVIEELFKATTMMVLSKCP---EDVELChkFIAPGQK- 307
Cdd:cd00775 76 FERVYEIGRNFRNE-GIDLTHNPEFTMIEFYEAYAD-YNDMMDLTEDLFSGLVKKINGKTKieyGGKELD--FTPPFKRv 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 308 ---DRLEHMLKNNFLIISYTEAVEILKQASQNFTFTPEWG---ADLRTE-HEKYLVKHCGNiPVFVINYPLTLKPFYMRD 380
Cdd:cd00775 152 tmvDALKEKTGIDFPELDLEQPEELAKLLAKLIKEKIEKPrtlGKLLDKlFEEFVEPTLIQ-PTFIIDHPVEISPLAKRH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 381 NEDgpqhtvaavdllvPGVG---ELFGGGlRE-------------ERYHFLEE-RLARSGLTE--VYQW-YLDLRRFGSV 440
Cdd:cd00775 231 RSN-------------PGLTerfELFICG-KEianaytelndpfdQRERFEEQaKQKEAGDDEamMMDEdFVTALEYGMP 296
|
330 340
....*....|....*....|....*....
gi 226491502 441 PHGGFGMGFERYLQCILGVDNIKDVIPFP 469
Cdd:cd00775 297 PTGGLGIGIDRLVMLLTDSNSIRDVILFP 325
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
39-469 |
1.53e-13 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 72.76 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 39 ASGER-----IKIQGWIRSVRSQKEVLFLHVNdgSSLESLQVVADSGLD-SRE--------LNFGSSVEVQGqlIKSPSK 104
Cdd:PTZ00385 100 ASGDRaaqatVRVAGRVTSVRDIGKIIFVTIR--SNGNELQVVGQVGEHfTREdlkklkvsLRVGDIIGADG--VPCRMQ 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 105 RQNVELKAEKIKVI---------------GNCDAKDFPIKYKERhpleylrqYPHFRCRTNVLGSIlRIRSEATAAIHSF 169
Cdd:PTZ00385 176 RGELSVAASRMLILspyvctdqvvcpnlrGFTVLQDNDVKYRYR--------FTDMMTNPCVIETI-KKRHVMLQALRDY 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 170 FKDSGFVHIHTPIITSNDSEGAGELFqlepsgklkVPEENFFNVPAFLTVSGQLHL-EVMSGAFTQVFTFGPTFRAENSq 248
Cdd:PTZ00385 247 FNERNFVEVETPVLHTVASGANAKSF---------VTHHNANAMDLFLRVAPELHLkQCIVGGMERIYEIGKVFRNEDA- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 249 SRRHLAEFYMIEAEISFvDSLQDLMQVIEELFKATTMMV------------LSKCPEDVELCHKFIAPGQKDRLEHMLK- 315
Cdd:PTZ00385 317 DRSHNPEFTSCEFYAAY-HTYEDLMPMTEDIFRQLAMRVngttvvqiypenAHGNPVTVDLGKPFRRVSVYDEIQRMSGv 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 316 --------NNFLIISYTEAVEIlkqaSQNFTFTPEWGADLRTEH--EKYLVKHCGNiPVFVINYPLTLKPfymrdnedgp 385
Cdd:PTZ00385 396 efpppnelNTPKGIAYMSVVML----RYNIPLPPVRTAAKMFEKliDFFITDRVVE-PTFVMDHPLFMSP---------- 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 386 qhtVAAVDLLVPGVGE---LFGGGLR-----------EERYHFLEERLA-RSGLTE----VYQWYLDLRRFGSVPHGGFG 446
Cdd:PTZ00385 461 ---LAKEQVSRPGLAErfeLFVNGIEycnayselndpHEQYHRFQQQLVdRQGGDEeampLDETFLKSLQVGLPPTAGWG 537
|
490 500
....*....|....*....|...
gi 226491502 447 MGFERYLQCILGVDNIKDVIPFP 469
Cdd:PTZ00385 538 MGIDRALMLLTNSSNIRDGIIFP 560
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
29-469 |
1.95e-13 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 73.07 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 29 SVRDALGAQnaSGERIKIQGWIRSVRSQKEVLFLHVNDGSSleSLQVVAD-SGLDSRELNF-------GSSVEVQGQLIK 100
Cdd:PRK02983 641 TVAEALDAP--TGEEVSVSGRVLRIRDYGGVLFADLRDWSG--ELQVLLDaSRLEQGSLADfraavdlGDLVEVTGTMGT 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 101 SpsKRQNVELKAEKIKVIGNCdakdfpikykeRHPLEYLRQY---PHFRCRTNVLG--------SILRIRSEATAAIHSF 169
Cdd:PRK02983 717 S--RNGTLSLLVTSWRLAGKC-----------LRPLPDKWKGltdPEARVRQRYLDlavnpearDLLRARSAVVRAVRET 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 170 FKDSGFVHIHTPIITSNDSEGAGELFqlepsgklkVPEENFFNVPAFLTVSGQLHLE-VMSGAFTQVFTFGPTFRAENSQ 248
Cdd:PRK02983 784 LVARGFLEVETPILQQVHGGANARPF---------VTHINAYDMDLYLRIAPELYLKrLCVGGVERVFELGRNFRNEGVD 854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 249 SrRHLAEFYMIEAEISFVDSLQdLMQVIEELFKATTMMVLSKcpedvelcHKFIAPGQKDRLEHM-LKNNFLIISYTEAV 327
Cdd:PRK02983 855 A-THNPEFTLLEAYQAHADYDT-MRDLTRELIQNAAQAAHGA--------PVVMRPDGDGVLEPVdISGPWPVVTVHDAV 924
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 328 ---------------EILKQASQN-FTFTPEWGA-DLRTEHEKYLVKHCGNIPVFVINYPLTLKPFYMRDNEDgPQhtVA 390
Cdd:PRK02983 925 sealgeeidpdtplaELRKLCDAAgIPYRTDWDAgAVVLELYEHLVEDRTTFPTFYTDFPTSVSPLTRPHRSD-PG--LA 1001
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 391 AV-DLLVPGVgELfGGGLRE-----ERYHFLEER--LARSG---LTEVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGV 459
Cdd:PRK02983 1002 ERwDLVAWGV-EL-GTAYSEltdpvEQRRRLTEQslLAAGGdpeAMELDEDFLQALEYAMPPTGGLGMGVDRLVMLLTGR 1079
|
490
....*....|
gi 226491502 460 dNIKDVIPFP 469
Cdd:PRK02983 1080 -SIRETLPFP 1088
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
124-469 |
4.47e-13 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 71.25 E-value: 4.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 124 KDFPIKYKERhpleYLRQYPHFRCRTNvlgsiLRIRSEATAAIHSFFKDSGFVHIHTPIItsndsegagelfQLEPSGKL 203
Cdd:PRK12445 161 QDQEVRYRQR----YLDLIANDKSRQT-----FVVRSKILAAIRQFMVARGFMEVETPMM------------QVIPGGAS 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 204 KVP---EENFFNVPAFLTVSGQLHLE-VMSGAFTQVFTFGPTFRAENSqSRRHLAEFYMIEAEISFVDsLQDLMQVIEEL 279
Cdd:PRK12445 220 ARPfitHHNALDLDMYLRIAPELYLKrLVVGGFERVFEINRNFRNEGI-SVRHNPEFTMMELYMAYAD-YHDLIELTESL 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 280 FKATTMMVLSKCPEDV-ELCHKFIAPGQKDRLEHMLK-----NNFLIISYTEAVEILKQaSQNFTFTPEWG-ADLRTE-- 350
Cdd:PRK12445 298 FRTLAQEVLGTTKVTYgEHVFDFGKPFEKLTMREAIKkyrpeTDMADLDNFDAAKALAE-SIGITVEKSWGlGRIVTEif 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 351 ---HEKYLVKhcgniPVFVINYPLTLKPFyMRDNEDGPQHTvAAVDLLVPGvgELFGGGLRE------ERYHFLEERLAR 421
Cdd:PRK12445 377 devAEAHLIQ-----PTFITEYPAEVSPL-ARRNDVNPEIT-DRFEFFIGG--REIGNGFSElndaedQAERFQEQVNAK 447
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 226491502 422 S-GLTEVYQW---YLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFP 469
Cdd:PRK12445 448 AaGDDEAMFYdedYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
33-282 |
4.87e-13 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 71.25 E-value: 4.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 33 ALGAQNAsGERIKIQGWIRSVRSQKEVLFLHVNDGSSLesLQVVADSGLDS----RELNFGSSVEVQGQLIKSPSKRQN- 107
Cdd:PRK00476 10 ELRESHV-GQTVTLCGWVHRRRDHGGLIFIDLRDREGI--VQVVFDPDAEAfevaESLRSEYVIQVTGTVRARPEGTVNp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 108 ------VELKAEKIKVIGNCDAKDFPIKYKErHPLEYLR-QYphfRC---RTNVLGSILRIRSEATAAIHSFFKDSGFVH 177
Cdd:PRK00476 87 nlptgeIEVLASELEVLNKSKTLPFPIDDEE-DVSEELRlKY---RYldlRRPEMQKNLKLRSKVTSAIRNFLDDNGFLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 178 IHTPIITSNDSEGAGElFqLEPS----GKlkvpeenFFNVPAfltvSGQL--HLEVMSGaFTQVFTFGPTFRAENSQSRR 251
Cdd:PRK00476 163 IETPILTKSTPEGARD-Y-LVPSrvhpGK-------FYALPQ----SPQLfkQLLMVAG-FDRYYQIARCFRDEDLRADR 228
|
250 260 270
....*....|....*....|....*....|.
gi 226491502 252 hLAEFYMIEAEISFVDSlQDLMQVIEELFKA 282
Cdd:PRK00476 229 -QPEFTQIDIEMSFVTQ-EDVMALMEGLIRH 257
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
1-282 |
6.58e-13 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 70.97 E-value: 6.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 1 MLGVRCLLRSVRfCSSAPFPKHKPSAKLSVRDAL---------GA--QNASGERIKIQGWIRSVRSQKEVLFLHVNDGSS 69
Cdd:PLN02903 22 RKRTTLLSTSSA-ASSAATVIPVVSAVDSMSSQLtwpsrshlcGAlsVNDVGSRVTLCGWVDLHRDMGGLTFLDVRDHTG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 70 LESLQVVADSGLDSRE----LNFGSSVEVQGQLIKSPSKRQN-------VELKAEKIKVIGNCDAK-DFPIKY---KERH 134
Cdd:PLN02903 101 IVQVVTLPDEFPEAHRtanrLRNEYVVAVEGTVRSRPQESPNkkmktgsVEVVAESVDILNVVTKSlPFLVTTadeQKDS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 135 PLEYLR-QYPHFRCRTNVLGSILRIRSEATAAIHSFFKDS-GFVHIHTPIITSNDSEGAGELfqLEPSgklKVPEENFFN 212
Cdd:PLN02903 181 IKEEVRlRYRVLDLRRPQMNANLRLRHRVVKLIRRYLEDVhGFVEIETPILSRSTPEGARDY--LVPS---RVQPGTFYA 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226491502 213 VPAfltvSGQLHLE-VMSGAFTQVFTFGPTFRAENSQSRRHlAEFYMIEAEISFVDsLQDLMQVIEELFKA 282
Cdd:PLN02903 256 LPQ----SPQLFKQmLMVSGFDRYYQIARCFRDEDLRADRQ-PEFTQLDMELAFTP-LEDMLKLNEDLIRQ 320
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
41-469 |
9.53e-12 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 66.94 E-value: 9.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 41 GERIKIQGWIRSVRSQKEVLFLHVNDGSSleSLQVVAD-SGLDSRELNF---------GSSVEVQGQLIKSpsKRQNVEL 110
Cdd:PLN02502 108 DVSVSVAGRIMAKRAFGKLAFYDLRDDGG--KIQLYADkKRLDLDEEEFeklhslvdrGDIVGVTGTPGKT--KKGELSI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 111 KAEKIKVIGNC-----DA----KDFPIKYKERHpLEyLRQYPHFRcrtnvlgSILRIRSEATAAIHSFFKDSGFVHIHTP 181
Cdd:PLN02502 184 FPTSFEVLTKCllmlpDKyhglTDQETRYRQRY-LD-LIANPEVR-------DIFRTRAKIISYIRRFLDDRGFLEVETP 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 182 IItsndsegagelfQLEPSGKLKVPEENFFN---VPAFLTVSGQLHL-EVMSGAFTQVFTFGPTFRAENSqSRRHLAEFY 257
Cdd:PLN02502 255 ML------------NMIAGGAAARPFVTHHNdlnMDLYLRIATELHLkRLVVGGFERVYEIGRQFRNEGI-STRHNPEFT 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 258 MIEAEISFVDsLQDLMQVIEELFkatTMMVLSKCP------EDVELChkFIAPGQK----DRLEHMLKNNFL-IISYTEA 326
Cdd:PLN02502 322 TCEFYQAYAD-YNDMMELTEEMV---SGMVKELTGsykikyHGIEID--FTPPFRRismiSLVEEATGIDFPaDLKSDEA 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 327 VEILKQASQNFTFT----PEWGADLRTEHEKYLVKHCGNiPVFVINYPLTLKPF--YMRDNedgpqhtvaavdllvPGVG 400
Cdd:PLN02502 396 NAYLIAACEKFDVKcpppQTTGRLLNELFEEFLEETLVQ-PTFVLDHPVEMSPLakPHRSK---------------PGLT 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 401 ---ELFGGGlRE------------ERYHFLEERLARSGLTEVYQWYLD------LrRFGSVPHGGFGMGFERYLQCILGV 459
Cdd:PLN02502 460 erfELFING-RElanafseltdpvDQRERFEEQVKQHNAGDDEAMALDedfctaL-EYGLPPTGGWGLGIDRLVMLLTDS 537
|
490
....*....|
gi 226491502 460 DNIKDVIPFP 469
Cdd:PLN02502 538 ASIRDVIAFP 547
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
158-283 |
8.59e-10 |
|
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: 58.67 E-value: 8.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 158 IRSEATAAIHSFFKDSGFVHIHTPIITSN-DSEGAGELFQLEPSGKlKVPEENFFNVPAFLTVSGQLHLEVMSGAFTQVF 236
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREpLLEKAGHEPKDLLPVG-AENEEDLYLRPTLEPGLVRLFVSHIRKLPLRLA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 226491502 237 TFGPTFRAENSQ-SRRHLAEFYMIEAEISFVDS-----LQDLMQVIEELFKAT 283
Cdd:cd00768 80 EIGPAFRNEGGRrGLRRVREFTQLEGEVFGEDGeeaseFEELIELTEELLRAL 132
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
41-282 |
1.28e-09 |
|
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: 60.40 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 41 GERIKIQGWIRSVRSQKEVLFLHVNDGSSLesLQVVADSGLDS------RELNFGSSVEVQGQLIKSPSKRQN------- 107
Cdd:COG0173 16 GQEVTLSGWVHRRRDHGGLIFIDLRDRYGI--TQVVFDPDDSAeafekaEKLRSEYVIAVTGKVRARPEGTVNpklptge 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 108 VELKAEKIKVIGNCDAKDFPIKyKERHPLEYLR-QYphfR---CRTNVLGSILRIRSEATAAIHSFFKDSGFVHIHTPII 183
Cdd:COG0173 94 IEVLASELEILNKAKTPPFQID-DDTDVSEELRlKY---RyldLRRPEMQKNLILRHKVTKAIRNYLDENGFLEIETPIL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 184 TSNDSEGAGElFqLEPS----GKlkvpeenFFNVPAfltvSGQL--HLEVMSGaFTQVFTFGPTFRAENSQSRRHlAEFY 257
Cdd:COG0173 170 TKSTPEGARD-Y-LVPSrvhpGK-------FYALPQ----SPQLfkQLLMVSG-FDRYFQIARCFRDEDLRADRQ-PEFT 234
|
250 260
....*....|....*....|....*
gi 226491502 258 MIEAEISFVDSlQDLMQVIEELFKA 282
Cdd:COG0173 235 QLDIEMSFVDQ-EDVFELMEGLIRH 258
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
43-120 |
1.46e-09 |
|
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: 54.55 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 43 RIKIQGWIRSVRSQKEVLFLHVNDGSSLesLQVVADSGL-----DSRELNFGSSVEVQGQLIKSPSKRQ---NVELKAEK 114
Cdd:cd04323 1 RVKVFGWVHRLRSQKKLMFLVLRDGTGF--LQCVLSKKLvtefyDAKSLTQESSVEVTGEVKEDPRAKQapgGYELQVDY 78
|
....*.
gi 226491502 115 IKVIGN 120
Cdd:cd04323 79 LEIIGE 84
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
157-469 |
2.03e-09 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 59.72 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 157 RIRSEATAAIHSFFKDSGFVHIHTPIItsndsegagelfQLEPSGKLKVPEE---NFFNVPAFLTVSGQLHLE---VmsG 230
Cdd:PRK00484 173 RKRSKIISAIRRFLDNRGFLEVETPML------------QPIAGGAAARPFIthhNALDIDLYLRIAPELYLKrliV--G 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 231 AFTQVFTFGPTFRAENSqSRRHLAEFYMIEAEISFVDsLQDLMQVIEELFKATTMMVL--SKCP-EDVELchKFIAPGQK 307
Cdd:PRK00484 239 GFERVYEIGRNFRNEGI-DTRHNPEFTMLEFYQAYAD-YNDMMDLTEELIRHLAQAVLgtTKVTyQGTEI--DFGPPFKR 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 308 ----DRLEHMLKNNFLIISYTEAVEILKQAsqNFTFTPEWGA----DLRTEH--EKYLVKhcgniPVFVINYPLTLKPFY 377
Cdd:PRK00484 315 ltmvDAIKEYTGVDFDDMTDEEARALAKEL--GIEVEKSWGLgkliNELFEEfvEPKLIQ-----PTFITDYPVEISPLA 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 378 MRDNEDgpqhtvaavdllvPGVG---ELFGGGlRE---------------ERyhFLEE-RLARSGLTEVYQwyLD---LR 435
Cdd:PRK00484 388 KRHRED-------------PGLTerfELFIGG-REianafselndpidqrER--FEAQvEAKEAGDDEAMF--MDedfLR 449
|
330 340 350
....*....|....*....|....*....|....*.
gi 226491502 436 --RFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFP 469
Cdd:PRK00484 450 alEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
44-118 |
9.40e-09 |
|
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: 51.85 E-value: 9.40e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226491502 44 IKIQGWIRSV-RSQKEVLFLHVNDGSSleSLQVVADSGLDSRE---LNFGSSVEVQGQLIKSPSKRqnVELKAEKIKVI 118
Cdd:pfam01336 1 VTVAGRVTSIrRSGGKLLFLTLRDGTG--SIQVVVFKEEAEKLakkLKEGDVVRVTGKVKKRKGGE--LELVVEEIELL 75
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
43-144 |
2.52e-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: 45.98 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 43 RIKIQGWIRSVRSQKEVLFLHVNDGSSLesLQVVADSGL------DSRELNFGSSVEVQGQLIKSPSKRQNVELKAEKIK 116
Cdd:cd04319 1 KVTLAGWVYRKREVGKKAFIVLRDSTGI--VQAVFSKDLneeayrEAKKVGIESSVIVEGAVKADPRAPGGAEVHGEKLE 78
|
90 100
....*....|....*....|....*...
gi 226491502 117 VIGNcdAKDFPIkyKERHPLEYLRQYPH 144
Cdd:cd04319 79 IIQN--VEFFPI--TEDASDEFLLDVRH 102
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
41-142 |
2.64e-06 |
|
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: 46.75 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 41 GERIKIQGWIRSVRSQKEVLFLHVNDGSSLesLQVVADSGLDS-----RELNFGSSVEVQGQLIKSPSKRQN-------V 108
Cdd:cd04317 14 GQEVTLCGWVQRRRDHGGLIFIDLRDRYGI--VQVVFDPEEAPefelaEKLRNESVIQVTGKVRARPEGTVNpklptgeI 91
|
90 100 110
....*....|....*....|....*....|....*
gi 226491502 109 ELKAEKIKVIGNCDAKDFPIKYKErHPLEYLR-QY 142
Cdd:cd04317 92 EVVASELEVLNKAKTLPFEIDDDV-NVSEELRlKY 125
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
41-118 |
2.02e-03 |
|
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: 37.68 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491502 41 GERIKIQGWIRSVRSQKEVLFLHVNDGSSLesLQVVA-----DSGL--DSRELNFGSSVEVQGQLIKSPSKRQNVELKAE 113
Cdd:cd04316 12 GEEVTVAGWVHEIRDLGGIKFVILRDREGI--VQVTApkkkvDKELfkTVRKLSRESVISVTGTVKAEPKAPNGVEIIPE 89
|
....*
gi 226491502 114 KIKVI 118
Cdd:cd04316 90 EIEVL 94
|
|
| |
