|
Name |
Accession |
Description |
Interval |
E-value |
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
65-555 |
4.10e-150 |
|
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: 438.74 E-value: 4.10e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 65 HKELRVQGHVRFLRKQKRFAFAHISDGSSLQPIQAVLTPE-------QATNLTQGAAVEVTG-IWQPspPGKQQSHELQA 136
Cdd:TIGR00457 16 GDEVTVSGWVRTKRSSKKIIFLELNDGSSLGPIQAVINGEdnpylfqLLKSLTTGSSVSVTGkVVES--PGKGQPVELQV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 137 TKVDIVGEADPAassstqTYPIQKKFHTPDFLRQLPHLRLRTPFNALLSRLRSEFIYQVTEEFRSHrdlNFVQVQPPLIT 216
Cdd:TIGR00457 94 KKIEVVGEAEPD------DYPLQKKEHSLEFLRDIAHLRLRTNTLGAVMRVRNALSQAIHRYFQEN---GFTWVSPPILT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 217 SSDCEGAGEVFSIRPRDVVIEEgkavEFFKSPKYLTVSSQLHLEAYAAELGNVWTLSPTFRAEKSDTPRHLSEFYMLEVE 296
Cdd:TIGR00457 165 SNDCEGAGELFRVSTGNIDFSQ----DFFGKEAYLTVSGQLYLETYALALSKVYTFGPTFRAEKSNTSRHLSEFWMIEPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 297 MSYMDsLEPLTAFVETLLRNMTQRVYKSpVAQEIfsfkatDDLTKDTTNAHLEKRWMALIEgpRWPRITFAHAIKHLHEA 376
Cdd:TIGR00457 241 MAFAN-LNDLLQLAETLIKYIIKAVLEN-CSQEL------KFLEKNFDKDLIKRLENIINN--KFARITYTDAIEILKES 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 377 VNTglvtFDFSPSWSGGLQLEHEKFLVDTIGKGlPIFVTDYPKAVKPFYMLPSSGSSnesgeTVACFDLLLPEICEVVGG 456
Cdd:TIGR00457 311 DKN----FEYEDFWGDDLQTEHERFLAEEYFKP-PVFVTNYPKDIKAFYMKLNDDGK-----TVAAMDLLAPGIGEIIGG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 457 SLREHRLSPLIRNMREHGLlklkdstpepssavdakapyphllaNEElgSIQWYADLRRWGTVPHGGFGLGFDRFVGYLA 536
Cdd:TIGR00457 381 SEREDDLDKLENRMKEMGL-------------------------DTD--ALNWYLDLRKYGSVPHSGFGLGFERLLAYIT 433
|
490
....*....|....*....
gi 302501169 537 GVSSLRDLVPFPRHFGRAD 555
Cdd:TIGR00457 434 GLENIRDAIPFPRTPGNIN 452
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
66-555 |
4.38e-149 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 435.69 E-value: 4.38e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 66 KELRVQGHVRFLRKQKRFAFAHISDGSSLQPIQAVLTP-----EQATNLTQGAAVEVTGIWQPSPpGKQQSHELQATKVD 140
Cdd:PRK03932 17 QEVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDNgeeyfEEIKKLTTGSSVIVTGTVVESP-RAGQGYELQATKIE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 141 IVGEADpaassstQTYPIQKKFHTPDFLRQLPHLRLRTP-FNALLsRLRSEFIYQVTEEFRSHrdlNFVQVQPPLITSSD 219
Cdd:PRK03932 96 VIGEDP-------EDYPIQKKRHSIEFLREIAHLRPRTNkFGAVM-RIRNTLAQAIHEFFNEN---GFVWVDTPIITASD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 220 CEGAGEVFSIRPRDVVIEEgkavEFFKSPKYLTVSSQLHLEAYAAELGNVWTLSPTFRAEKSDTPRHLSEFYMLEVEMSY 299
Cdd:PRK03932 165 CEGAGELFRVTTLDLDFSK----DFFGKEAYLTVSGQLYAEAYAMALGKVYTFGPTFRAENSNTRRHLAEFWMIEPEMAF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 300 MDsLEPLTAFVETLLRNMTQRVY-KSPVAQEIF-SFKATDDLTKdttnahLEKrwmaLIEGPrWPRITFAHAIKHLHEAV 377
Cdd:PRK03932 241 AD-LEDNMDLAEEMLKYVVKYVLeNCPDDLEFLnRRVDKGDIER------LEN----FIESP-FPRITYTEAIEILQKSG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 378 ntglVTFDFSPSWSGGLQLEHEKFLVDTIGKGlPIFVTDYPKAVKPFYMLPssgssNESGETVACFDLLLPEICEVVGGS 457
Cdd:PRK03932 309 ----KKFEFPVEWGDDLGSEHERYLAEEHFKK-PVFVTNYPKDIKAFYMRL-----NPDGKTVAAMDLLAPGIGEIIGGS 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 458 LREHRLSPLIRNMREHGLlklkdstpepssavdakapyphllaNEElgSIQWYADLRRWGTVPHGGFGLGFDRFVGYLAG 537
Cdd:PRK03932 379 QREERLDVLEARIKELGL-------------------------NKE--DYWWYLDLRRYGSVPHSGFGLGFERLVAYITG 431
|
490
....*....|....*...
gi 302501169 538 VSSLRDLVPFPRHFGRAD 555
Cdd:PRK03932 432 LDNIRDVIPFPRTPGRAE 449
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
61-554 |
2.08e-146 |
|
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: 428.32 E-value: 2.08e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 61 SSLDHKELRVQGHVRFLRKQKRFAFAHISDGSSLqpIQAVLTP------EQATNLTQGAAVEVTGIWQPSPpGKQQSHEL 134
Cdd:COG0017 10 PEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGF--IQVVVKKdklenfEEAKKLTTESSVEVTGTVVESP-RAPQGVEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 135 QATKVDIVGEADpaassstQTYPIQKKFHTPDFLRQLPHLRLRTP-FNALLsRLRSEFIYQVTEEFRSHrdlNFVQVQPP 213
Cdd:COG0017 87 QAEEIEVLGEAD-------EPYPLQPKRHSLEFLLDNRHLRLRTNrFGAIF-RIRSELARAIREFFQER---GFVEVHTP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 214 LITSSDCEGAGEVFSirprdvvieegkaVEFFKSPKYLTVSSQLHLEAYAAELGNVWTLSPTFRAEKSDTPRHLSEFYML 293
Cdd:COG0017 156 IITASATEGGGELFP-------------VDYFGKEAYLTQSGQLYKEALAMALEKVYTFGPTFRAEKSNTRRHLAEFWMI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 294 EVEMSYMDsLEPLTAFVETLLRNMTQRVYKspvaqeifsfKATDDLtkDTTNAHLEkRWMALIEGPrWPRITFAHAIKHL 373
Cdd:COG0017 223 EPEMAFAD-LEDVMDLAEEMLKYIIKYVLE----------NCPEEL--EFLGRDVE-RLEKVPESP-FPRITYTEAIEIL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 374 HEAvntglvtfDFSPSWSGGLQLEHEKFLVDTIGKGlPIFVTDYPKAVKPFYMLPssgsSNESGETVACFDLLLPEICEV 453
Cdd:COG0017 288 KKS--------GEKVEWGDDLGTEHERYLGEEFFKK-PVFVTDYPKEIKAFYMKP----NPDDPKTVAAFDLLAPGIGEI 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 454 VGGSLREHRLSPLIRNMREHGLlklkdstpepssavdakapyphllaNEElgSIQWYADLRRWGTVPHGGFGLGFDRFVG 533
Cdd:COG0017 355 IGGSQREHRYDVLVERIKEKGL-------------------------DPE--DYEWYLDLRRYGSVPHAGFGLGLERLVM 407
|
490 500
....*....|....*....|.
gi 302501169 534 YLAGVSSLRDLVPFPRHFGRA 554
Cdd:COG0017 408 WLTGLENIREVIPFPRDPGRL 428
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
163-549 |
3.95e-115 |
|
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: 344.16 E-value: 3.95e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 163 HTPDFLRQLPHLRLRTPFNALLSRLRSEFIYQVTEEFRSHrdlNFVQVQPPLITSSDCEGAGEVFSirprdvvieegkaV 242
Cdd:cd00776 2 ANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLREN---GFTEVHTPKITSTDTEGGAELFK-------------V 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 243 EFFKSPKYLTVSSQLHLEAYAAELGNVWTLSPTFRAEKSDTPRHLSEFYMLEVEMSYMDSLEPLTAFVETLLRNMTQRVY 322
Cdd:cd00776 66 SYFGKPAYLAQSPQLYKEMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEDYNEVMDLIEELIKYIFKRVL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 323 KSPVAQ-EIFSFKATDDltkdttnahlekrwmaLIEGPRWPRITFAHAIKHLHEAVNTglvtfdFSPSWSGGLQLEHEKF 401
Cdd:cd00776 146 ERCAKElELVNQLNREL----------------LKPLEPFPRITYDEAIELLREKGVE------EEVKWGEDLSTEHERL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 402 LVDTIGKGlPIFVTDYPKAVKPFYMLPssgsSNESGETVACFDLLLPEICEVVGGSLREHRLSPLIRNMREHGLlklkds 481
Cdd:cd00776 204 LGEIVKGD-PVFVTDYPKEIKPFYMKP----DDDNPETVESFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGL------ 272
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 302501169 482 TPEpssavdakapyphllaneelgSIQWYADLRRWGTVPHGGFGLGFDRFVGYLAGVSSLRDLVPFPR 549
Cdd:cd00776 273 DPE---------------------SFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFPR 319
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
165-549 |
6.55e-64 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 211.66 E-value: 6.55e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 165 PDFLRQLPHLRLRTPFNALLSRLRSEFIYQVTEEFRSHrdlNFVQVQPPLITSSDCEGAGEVFSIRPRdvvieegKAVEF 244
Cdd:pfam00152 2 EETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDEN---GFLEVETPILTKSATPEGARDFLVPSR-------ALGKF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 245 FkspkYLTVSSQLHLEAY-AAELGNVWTLSPTFRAEKSDTPRHLsEFYMLEVEMSYMDSLEpLTAFVETLLRNMTQRVYK 323
Cdd:pfam00152 72 Y----ALPQSPQLYKQLLmVAGFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVDYED-VMDLTEELIKEIFKEVEG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 324 SPVAQEIFSFKatdDLTKDttnahlekrwmaliegprWPRITFAHAIKHLHEAVNtglvtfdfsPSWSGGLQLEHEKFLV 403
Cdd:pfam00152 146 IAKELEGGTLL---DLKKP------------------FPRITYAEAIEKLNGKDV---------EELGYGSDKPDLRFLL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 404 DTIGKGL---PIFVTDYPKAVKPFYMlpssGSSNESGETVACFDLLLPEIcEVVGGSLREHRLSPLIRNMREHGLLKLKd 480
Cdd:pfam00152 196 ELVIDKNkfnPLWVTDFPAEHHPFTM----PKDEDDPALAEAFDLVLNGV-EIGGGSIRIHDPELQEERFEEQGLDPEE- 269
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 302501169 481 stpepssavdAKAPYphllaneelgsiQWYADLRRWGTVPHGGFGLGFDRFVGYLAGVSSLRDLVPFPR 549
Cdd:pfam00152 270 ----------AEEKF------------GFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAFPK 316
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
65-555 |
4.10e-150 |
|
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: 438.74 E-value: 4.10e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 65 HKELRVQGHVRFLRKQKRFAFAHISDGSSLQPIQAVLTPE-------QATNLTQGAAVEVTG-IWQPspPGKQQSHELQA 136
Cdd:TIGR00457 16 GDEVTVSGWVRTKRSSKKIIFLELNDGSSLGPIQAVINGEdnpylfqLLKSLTTGSSVSVTGkVVES--PGKGQPVELQV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 137 TKVDIVGEADPAassstqTYPIQKKFHTPDFLRQLPHLRLRTPFNALLSRLRSEFIYQVTEEFRSHrdlNFVQVQPPLIT 216
Cdd:TIGR00457 94 KKIEVVGEAEPD------DYPLQKKEHSLEFLRDIAHLRLRTNTLGAVMRVRNALSQAIHRYFQEN---GFTWVSPPILT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 217 SSDCEGAGEVFSIRPRDVVIEEgkavEFFKSPKYLTVSSQLHLEAYAAELGNVWTLSPTFRAEKSDTPRHLSEFYMLEVE 296
Cdd:TIGR00457 165 SNDCEGAGELFRVSTGNIDFSQ----DFFGKEAYLTVSGQLYLETYALALSKVYTFGPTFRAEKSNTSRHLSEFWMIEPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 297 MSYMDsLEPLTAFVETLLRNMTQRVYKSpVAQEIfsfkatDDLTKDTTNAHLEKRWMALIEgpRWPRITFAHAIKHLHEA 376
Cdd:TIGR00457 241 MAFAN-LNDLLQLAETLIKYIIKAVLEN-CSQEL------KFLEKNFDKDLIKRLENIINN--KFARITYTDAIEILKES 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 377 VNTglvtFDFSPSWSGGLQLEHEKFLVDTIGKGlPIFVTDYPKAVKPFYMLPSSGSSnesgeTVACFDLLLPEICEVVGG 456
Cdd:TIGR00457 311 DKN----FEYEDFWGDDLQTEHERFLAEEYFKP-PVFVTNYPKDIKAFYMKLNDDGK-----TVAAMDLLAPGIGEIIGG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 457 SLREHRLSPLIRNMREHGLlklkdstpepssavdakapyphllaNEElgSIQWYADLRRWGTVPHGGFGLGFDRFVGYLA 536
Cdd:TIGR00457 381 SEREDDLDKLENRMKEMGL-------------------------DTD--ALNWYLDLRKYGSVPHSGFGLGFERLLAYIT 433
|
490
....*....|....*....
gi 302501169 537 GVSSLRDLVPFPRHFGRAD 555
Cdd:TIGR00457 434 GLENIRDAIPFPRTPGNIN 452
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
66-555 |
4.38e-149 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 435.69 E-value: 4.38e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 66 KELRVQGHVRFLRKQKRFAFAHISDGSSLQPIQAVLTP-----EQATNLTQGAAVEVTGIWQPSPpGKQQSHELQATKVD 140
Cdd:PRK03932 17 QEVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDNgeeyfEEIKKLTTGSSVIVTGTVVESP-RAGQGYELQATKIE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 141 IVGEADpaassstQTYPIQKKFHTPDFLRQLPHLRLRTP-FNALLsRLRSEFIYQVTEEFRSHrdlNFVQVQPPLITSSD 219
Cdd:PRK03932 96 VIGEDP-------EDYPIQKKRHSIEFLREIAHLRPRTNkFGAVM-RIRNTLAQAIHEFFNEN---GFVWVDTPIITASD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 220 CEGAGEVFSIRPRDVVIEEgkavEFFKSPKYLTVSSQLHLEAYAAELGNVWTLSPTFRAEKSDTPRHLSEFYMLEVEMSY 299
Cdd:PRK03932 165 CEGAGELFRVTTLDLDFSK----DFFGKEAYLTVSGQLYAEAYAMALGKVYTFGPTFRAENSNTRRHLAEFWMIEPEMAF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 300 MDsLEPLTAFVETLLRNMTQRVY-KSPVAQEIF-SFKATDDLTKdttnahLEKrwmaLIEGPrWPRITFAHAIKHLHEAV 377
Cdd:PRK03932 241 AD-LEDNMDLAEEMLKYVVKYVLeNCPDDLEFLnRRVDKGDIER------LEN----FIESP-FPRITYTEAIEILQKSG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 378 ntglVTFDFSPSWSGGLQLEHEKFLVDTIGKGlPIFVTDYPKAVKPFYMLPssgssNESGETVACFDLLLPEICEVVGGS 457
Cdd:PRK03932 309 ----KKFEFPVEWGDDLGSEHERYLAEEHFKK-PVFVTNYPKDIKAFYMRL-----NPDGKTVAAMDLLAPGIGEIIGGS 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 458 LREHRLSPLIRNMREHGLlklkdstpepssavdakapyphllaNEElgSIQWYADLRRWGTVPHGGFGLGFDRFVGYLAG 537
Cdd:PRK03932 379 QREERLDVLEARIKELGL-------------------------NKE--DYWWYLDLRRYGSVPHSGFGLGFERLVAYITG 431
|
490
....*....|....*...
gi 302501169 538 VSSLRDLVPFPRHFGRAD 555
Cdd:PRK03932 432 LDNIRDVIPFPRTPGRAE 449
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
61-554 |
2.08e-146 |
|
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: 428.32 E-value: 2.08e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 61 SSLDHKELRVQGHVRFLRKQKRFAFAHISDGSSLqpIQAVLTP------EQATNLTQGAAVEVTGIWQPSPpGKQQSHEL 134
Cdd:COG0017 10 PEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGF--IQVVVKKdklenfEEAKKLTTESSVEVTGTVVESP-RAPQGVEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 135 QATKVDIVGEADpaassstQTYPIQKKFHTPDFLRQLPHLRLRTP-FNALLsRLRSEFIYQVTEEFRSHrdlNFVQVQPP 213
Cdd:COG0017 87 QAEEIEVLGEAD-------EPYPLQPKRHSLEFLLDNRHLRLRTNrFGAIF-RIRSELARAIREFFQER---GFVEVHTP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 214 LITSSDCEGAGEVFSirprdvvieegkaVEFFKSPKYLTVSSQLHLEAYAAELGNVWTLSPTFRAEKSDTPRHLSEFYML 293
Cdd:COG0017 156 IITASATEGGGELFP-------------VDYFGKEAYLTQSGQLYKEALAMALEKVYTFGPTFRAEKSNTRRHLAEFWMI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 294 EVEMSYMDsLEPLTAFVETLLRNMTQRVYKspvaqeifsfKATDDLtkDTTNAHLEkRWMALIEGPrWPRITFAHAIKHL 373
Cdd:COG0017 223 EPEMAFAD-LEDVMDLAEEMLKYIIKYVLE----------NCPEEL--EFLGRDVE-RLEKVPESP-FPRITYTEAIEIL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 374 HEAvntglvtfDFSPSWSGGLQLEHEKFLVDTIGKGlPIFVTDYPKAVKPFYMLPssgsSNESGETVACFDLLLPEICEV 453
Cdd:COG0017 288 KKS--------GEKVEWGDDLGTEHERYLGEEFFKK-PVFVTDYPKEIKAFYMKP----NPDDPKTVAAFDLLAPGIGEI 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 454 VGGSLREHRLSPLIRNMREHGLlklkdstpepssavdakapyphllaNEElgSIQWYADLRRWGTVPHGGFGLGFDRFVG 533
Cdd:COG0017 355 IGGSQREHRYDVLVERIKEKGL-------------------------DPE--DYEWYLDLRRYGSVPHAGFGLGLERLVM 407
|
490 500
....*....|....*....|.
gi 302501169 534 YLAGVSSLRDLVPFPRHFGRA 554
Cdd:COG0017 408 WLTGLENIREVIPFPRDPGRL 428
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
163-549 |
3.95e-115 |
|
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: 344.16 E-value: 3.95e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 163 HTPDFLRQLPHLRLRTPFNALLSRLRSEFIYQVTEEFRSHrdlNFVQVQPPLITSSDCEGAGEVFSirprdvvieegkaV 242
Cdd:cd00776 2 ANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLREN---GFTEVHTPKITSTDTEGGAELFK-------------V 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 243 EFFKSPKYLTVSSQLHLEAYAAELGNVWTLSPTFRAEKSDTPRHLSEFYMLEVEMSYMDSLEPLTAFVETLLRNMTQRVY 322
Cdd:cd00776 66 SYFGKPAYLAQSPQLYKEMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEDYNEVMDLIEELIKYIFKRVL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 323 KSPVAQ-EIFSFKATDDltkdttnahlekrwmaLIEGPRWPRITFAHAIKHLHEAVNTglvtfdFSPSWSGGLQLEHEKF 401
Cdd:cd00776 146 ERCAKElELVNQLNREL----------------LKPLEPFPRITYDEAIELLREKGVE------EEVKWGEDLSTEHERL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 402 LVDTIGKGlPIFVTDYPKAVKPFYMLPssgsSNESGETVACFDLLLPEICEVVGGSLREHRLSPLIRNMREHGLlklkds 481
Cdd:cd00776 204 LGEIVKGD-PVFVTDYPKEIKPFYMKP----DDDNPETVESFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGL------ 272
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 302501169 482 TPEpssavdakapyphllaneelgSIQWYADLRRWGTVPHGGFGLGFDRFVGYLAGVSSLRDLVPFPR 549
Cdd:cd00776 273 DPE---------------------SFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFPR 319
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
66-555 |
5.90e-95 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 300.74 E-value: 5.90e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 66 KELRVQGHVRFLRKQKRFAFAHISDGSSLQPIQAVLTPE-------QATNLTQGAAVEVTGIWQPSPPGKQQShELQATK 138
Cdd:PLN02603 108 KTLNVMGWVRTLRAQSSVTFIEVNDGSCLSNMQCVMTPDaegydqvESGLITTGASVLVQGTVVSSQGGKQKV-ELKVSK 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 139 VDIVGEADPaassstqTYPIQKKFHTPDFLRQLPHLRLRTPFNALLSRLRSEFIYQVTEEFRshrDLNFVQVQPPLITSS 218
Cdd:PLN02603 187 IVVVGKSDP-------SYPIQKKRVSREFLRTKAHLRPRTNTFGAVARVRNALAYATHKFFQ---ENGFVWVSSPIITAS 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 219 DCEGAGEVFSI-------------------RPRDVVIEEGKavEFFKSPKYLTVSSQLHLEAYAAELGNVWTLSPTFRAE 279
Cdd:PLN02603 257 DCEGAGEQFCVttlipnsaenggslvddipKTKDGLIDWSQ--DFFGKPAFLTVSGQLNGETYATALSDVYTFGPTFRAE 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 280 KSDTPRHLSEFYMLEVEMSYMDSLEPL---TAFVETLLRNMTQRvykspvAQEIFSFKAT--DDLTKDTTNAHLEKRWMA 354
Cdd:PLN02603 335 NSNTSRHLAEFWMIEPELAFADLNDDMacaTAYLQYVVKYILEN------CKEDMEFFNTwiEKGIIDRLSDVVEKNFVQ 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 355 LiegprwpriTFAHAIKHLHEAVNTglvtFDFSPSWSGGLQLEHEKFLVDTIGKGLPIFVTDYPKAVKPFYMlpssgSSN 434
Cdd:PLN02603 409 L---------SYTDAIELLLKAKKK----FEFPVKWGLDLQSEHERYITEEAFGGRPVIIRDYPKEIKAFYM-----REN 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 435 ESGETVACFDLLLPEICEVVGGSLREHRLSPLIRNMREhglLKLkdstpepssavdakapyphllaNEElgSIQWYADLR 514
Cdd:PLN02603 471 DDGKTVAAMDMLVPRVGELIGGSQREERLEYLEARLDE---LKL----------------------NKE--SYWWYLDLR 523
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 302501169 515 RWGTVPHGGFGLGFDRFVGYLAGVSSLRDLVPFPRHFGRAD 555
Cdd:PLN02603 524 RYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFPRVPGSAE 564
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
61-555 |
2.55e-83 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 270.33 E-value: 2.55e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 61 SSLDHKELRVQGHVRFLRKQKR--FAFAHISDGSSLQPIQAVLTP--EQATNLTQ-GAAVEVTGIWQPSPPGK--QQSHE 133
Cdd:PLN02221 46 AGLAGQKVRIGGWVKTGREQGKgtFAFLEVNDGSCPANLQVMVDSslYDLSTLVAtGTCVTVDGVLKVPPEGKgtKQKIE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 134 LQATKVDIVGEADPAassstqTYPIQKKFHTPDFLRQLPHLRLRTPFNALLSRLRSEFIYQVTEEFRSHrdlNFVQVQPP 213
Cdd:PLN02221 126 LSVEKVIDVGTVDPT------KYPLPKTKLTLEFLRDVLHLRSRTNSISAVARIRNALAFATHSFFQEH---SFLYIHTP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 214 LITSSDCEGAGEVFSIR--------------------------PRDVVIEEGKAV------------------------- 242
Cdd:PLN02221 197 IITTSDCEGAGEMFQVTtlinyterleqdlidnpppteadveaARLIVKERGEVVaqlkaakaskeeitaavaelkiake 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 243 --------------------------EFFKSPKYLTVSSQLHLEAYAAELGNVWTLSPTFRAEKSDTPRHLSEFYMLEVE 296
Cdd:PLN02221 277 slahieersklkpglpkkdgkidyskDFFGRQAFLTVSGQLQVETYACALSSVYTFGPTFRAENSHTSRHLAEFWMVEPE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 297 MSYMDsLEPLTAFVETLLRNMTQRVYKspvaqeifsfKATDDL---TKDTTNAHLEKrwMALIEGPRWPRITFAHAIKHL 373
Cdd:PLN02221 357 IAFAD-LEDDMNCAEAYVKYMCKWLLD----------KCFDDMelmAKNFDSGCIDR--LRMVASTPFGRITYTEAIELL 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 374 HEAVNTGLVtFDFSPSWSGGLQLEHEKFLVDTIGKGlPIFVTDYPKAVKPFYMlpssgSSNESGETVACFDLLLPEICEV 453
Cdd:PLN02221 424 EEAVAKGKE-FDNNVEWGIDLASEHERYLTEVLFQK-PLIVYNYPKGIKAFYM-----RLNDDEKTVAAMDVLVPKVGEL 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 454 VGGSLREHRLSPLIRNMREHGLlklkdstpepssavdAKAPYphllaneelgsiQWYADLRRWGTVPHGGFGLGFDRFVG 533
Cdd:PLN02221 497 IGGSQREERYDVIKQRIEEMGL---------------PIEPY------------EWYLDLRRYGTVKHCGFGLGFERMIL 549
|
570 580
....*....|....*....|..
gi 302501169 534 YLAGVSSLRDLVPFPRHFGRAD 555
Cdd:PLN02221 550 FATGIDNIRDVIPFPRYPGKAD 571
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
13-556 |
1.25e-74 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 249.02 E-value: 1.25e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 13 ASSVGKHSAVPYrrcLSTTPTRFNNHQANPITLRCAQIFEQ------------SKSGTTPSSLDHKELRVQghvRFLRKQ 80
Cdd:PLN02532 59 AKEVKKEPAPPP---PPQSPSSAGDQSPGHKDVRCTEILQSrvpifrsiakvlSGGGSTYPVREKTEIAIQ---KSAPPP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 81 KRFAFAHISDGSSLQPIQ-----AVLTPEQATNLtqGAAVEVTGIW-QPSPPGKQQSHELQATKVDIVGEADPaassstQ 154
Cdd:PLN02532 133 PSVAYLLISDGSCVASLQvvvdsALAPLTQLMAT--GTCILAEGVLkLPLPAQGKHVIELEVEKILHIGTVDP------E 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 155 TYPIQKKFHTPDFLRQLPHLRLRTPFNALLSRLRSEFIYQVTEEFRSHrdlNFVQVQPPLITSSDCEGAGEVFSIRP--- 231
Cdd:PLN02532 205 KYPLSKKRLPLDMLRDFSHFRPRTTTVASVTRVRSALTHATHTFFQDH---GFLYVQVPIITTTDATGFGEMFRVTTllg 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 232 ----------------------RDVVIEEGKAVE---------------------------------------------- 243
Cdd:PLN02532 282 ksddkeekkpvhetegisleavKAAIKEKTNLVEelkrsesnrealvaaeqdlrktnqlasqleakeklktgtsvkadkl 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 244 -----FFKSPKYLTVSSQLHLEAYAAELGNVWTLSPTFRAEKSDTPRHLSEFYMLEVEMSYMDsLEPLTAFVETLLRNMT 318
Cdd:PLN02532 362 sfskdFFSRPTYLTVSGRLHLESYACALGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAFSE-LEDAMNCAEDYFKFLC 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 319 QRVYKSPVAQEIFSFKATDDltkdTTNAHLEkrwmALIEGPrWPRITFAHAIKHLHEAVNTglvTFDFSPSWSGGLQLEH 398
Cdd:PLN02532 441 KWVLENCSEDMKFVSKRIDK----TISTRLE----AIISSS-LQRISYTEAVDLLKQATDK---KFETKPEWGIALTTEH 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 399 EKFLVDTIGKGlPIFVTDYPKAVKPFYMlpssgSSNESGETVACFDLLLPEICEVVGGSLREHRLSPLIRNMREHGLLKl 478
Cdd:PLN02532 509 LSYLADEIYKK-PVIIYNYPKELKPFYV-----RLNDDGKTVAAFDLVVPKVGTVITGSQNEERMDILNARIEELGLPR- 581
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 302501169 479 kdstpepssavdakapyphllanEELgsiQWYADLRRWGTVPHGGFGLGFDRFVGYLAGVSSLRDLVPFPRHFGRADC 556
Cdd:PLN02532 582 -----------------------EQY---EWYLDLRRHGTVKHSGFSLGFELMVLFATGLPDVRDAIPFPRSWGKANN 633
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
68-555 |
6.08e-67 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 227.60 E-value: 6.08e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 68 LRVQGHVRFLRKQK--RFAFAHISDGS---SLQPI--QAVLTPEQATNLTQGAAVEVTGIWQPSPPGKQQSHELQATKVD 140
Cdd:PTZ00425 84 ITVCGWSKAVRKQGggRFCFVNLNDGSchlNLQIIvdQSIENYEKLLKCGVGCCFRFTGKLIISPVQNENKKGLLKENVE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 141 ------------IVGE-ADPaassstQTYPIQKKFHTPDFLRQLPHLRLRTPFNALLSRLRSEFIYQVTEEFRSHrdlNF 207
Cdd:PTZ00425 164 lalkdnsihnfeIYGEnLDP------QKYPLSKKNHGKEFLREVAHLRPRSYFISSVIRIRNALAIATHLFFQSR---GF 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 208 VQVQPPLITSSDCEGAGEVFSIR------------PR-DVVIEEGKAVE------------------------------- 243
Cdd:PTZ00425 235 LYIHTPLITTSDCEGGGEMFTVTtllgedadyraiPRvNKKNKKGEKREdilntcnannnngnssssnavsspaypdqyl 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 244 ------FFKSPKYLTVSSQLHLEAYAAELGNVWTLSPTFRAEKSDTPRHLSEFYMLEVEMSYMDSLEPLTaFVETLLRNM 317
Cdd:PTZ00425 315 idykkdFFSKQAFLTVSGQLSLENLCSSMGDVYTFGPTFRAENSHTSRHLAEFWMIEPEIAFADLYDNME-LAESYIKYC 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 318 TQRVYKSPVaQEIFSFKatddltkDTTNAHLEKRWMALIEgPRWPRITFAHAIKHLHEAVNTglvtFDFSPSWSGGLQLE 397
Cdd:PTZ00425 394 IGYVLNNNF-DDIYYFE-------ENVETGLISRLKNILD-EDFAKITYTNVIDLLQPYSDS----FEVPVKWGMDLQSE 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 398 HEKFLVDTIGKGlPIFVTDYPKAVKPFYMlpssgSSNESGETVACFDLLLPEICEVVGGSLREHRLSPLIRNMREHGLlk 477
Cdd:PTZ00425 461 HERFVAEQIFKK-PVIVYNYPKDLKAFYM-----KLNEDQKTVAAMDVLVPKIGEVIGGSQREDNLERLDKMIKEKKL-- 532
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 302501169 478 lkdstpepssavdakapyphllaneELGSIQWYADLRRWGTVPHGGFGLGFDRFVGYLAGVSSLRDLVPFPRHFGRAD 555
Cdd:PTZ00425 533 -------------------------NMESYWWYRQLRKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFPRYPGHAE 585
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
165-549 |
6.55e-64 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 211.66 E-value: 6.55e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 165 PDFLRQLPHLRLRTPFNALLSRLRSEFIYQVTEEFRSHrdlNFVQVQPPLITSSDCEGAGEVFSIRPRdvvieegKAVEF 244
Cdd:pfam00152 2 EETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDEN---GFLEVETPILTKSATPEGARDFLVPSR-------ALGKF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 245 FkspkYLTVSSQLHLEAY-AAELGNVWTLSPTFRAEKSDTPRHLsEFYMLEVEMSYMDSLEpLTAFVETLLRNMTQRVYK 323
Cdd:pfam00152 72 Y----ALPQSPQLYKQLLmVAGFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVDYED-VMDLTEELIKEIFKEVEG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 324 SPVAQEIFSFKatdDLTKDttnahlekrwmaliegprWPRITFAHAIKHLHEAVNtglvtfdfsPSWSGGLQLEHEKFLV 403
Cdd:pfam00152 146 IAKELEGGTLL---DLKKP------------------FPRITYAEAIEKLNGKDV---------EELGYGSDKPDLRFLL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 404 DTIGKGL---PIFVTDYPKAVKPFYMlpssGSSNESGETVACFDLLLPEIcEVVGGSLREHRLSPLIRNMREHGLLKLKd 480
Cdd:pfam00152 196 ELVIDKNkfnPLWVTDFPAEHHPFTM----PKDEDDPALAEAFDLVLNGV-EIGGGSIRIHDPELQEERFEEQGLDPEE- 269
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 302501169 481 stpepssavdAKAPYphllaneelgsiQWYADLRRWGTVPHGGFGLGFDRFVGYLAGVSSLRDLVPFPR 549
Cdd:pfam00152 270 ----------AEEKF------------GFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAFPK 316
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
63-549 |
5.67e-54 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 188.86 E-value: 5.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 63 LDHKELRVQGHVRFLRKQKRFAFAHISDGSSLqpIQAVL-------TPEQATNLTQGAAVEVTGIWQPSP--PGkqqSHE 133
Cdd:PRK05159 14 LDGEEVTLAGWVHEIRDLGGIAFLILRDRSGI--IQVVVkkkvdeeLFETIKKLKRESVVSVTGTVKANPkaPG---GVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 134 LQATKVDIVGEADPaassstqTYPIQ---KKFHTPDFLRQLPHLRLRTPFNALLSRLRSEfiyqVTEEFRSH-RDLNFVQ 209
Cdd:PRK05159 89 VIPEEIEVLNKAEE-------PLPLDisgKVLAELDTRLDNRFLDLRRPRVRAIFKIRSE----VLRAFREFlYENGFTE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 210 VQPPLITSSDCEGAGEVFSIrprdvvieegkavEFFKSPKYLTVSSQLhleaY-----AAELGNVWTLSPTFRAEKSDTP 284
Cdd:PRK05159 158 IFTPKIVASGTEGGAELFPI-------------DYFEKEAYLAQSPQL----YkqmmvGAGFERVFEIGPVFRAEEHNTS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 285 RHLSEFYMLEVEMSYMDSLEPLTAFVETLLRNMTQRVYKspvaqeifsfKATDDLtkDTTNAHLEKrwmalIEGPrWPRI 364
Cdd:PRK05159 221 RHLNEYTSIDVEMGFIDDHEDVMDLLENLLRYMYEDVAE----------NCEKEL--ELLGIELPV-----PETP-IPRI 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 365 TFAHAIKHLHEAVNtglvtfdfSPSWSGGLQLEHEKFLVDTIGK---GLPIFVTDYPKAVKPFYMLPSSGSSNESGEtva 441
Cdd:PRK05159 283 TYDEAIEILKSKGN--------EISWGDDLDTEGERLLGEYVKEeygSDFYFITDYPSEKRPFYTMPDEDDPEISKS--- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 442 cFDLLLPEIcEVVGGSLREHRLSPLIRNMREHGLlklkdsTPEpssavdakapyphllaneelgSIQWYADLRRWGTVPH 521
Cdd:PRK05159 352 -FDLLFRGL-EITSGGQRIHRYDMLVESIKEKGL------NPE---------------------SFEFYLEAFKYGMPPH 402
|
490 500
....*....|....*....|....*...
gi 302501169 522 GGFGLGFDRFVGYLAGVSSLRDLVPFPR 549
Cdd:PRK05159 403 GGFGLGLERLTMKLLGLENIREAVLFPR 430
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
176-549 |
2.45e-37 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 140.93 E-value: 2.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 176 LRTPFNALLSRLRSEFIYQVTEEFRSHrdlNFVQVQPPLITSSDCEGAGEVFSIRPRDVVIEegkaveFFKSPKYLTVSS 255
Cdd:PRK06462 21 ISSEKYRKVLKVQSSILRYTREFLDGR---GFVEVLPPIISPSTDPLMGLGSDLPVKQISID------FYGVEYYLADSM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 256 QLHLEAYAAELGNVWTLSPTFRAE--KSDTPRHLSEFYMLEVEMSYMDsLEPLTAFVETLLRNMTQRVyKSPVAQEIFSF 333
Cdd:PRK06462 92 ILHKQLALRMLGKIFYLSPNFRLEpvDKDTGRHLYEFTQLDIEIEGAD-LDEVMDLIEDLIKYLVKEL-LEEHEDELEFF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 334 kaTDDLTKDTTNahlekrwmaliegprWPRITFAHAIKHLHEAVNTGLVTFDFSPSWsgglqlehEKFLVDTIGKglPIF 413
Cdd:PRK06462 170 --GRDLPHLKRP---------------FKRITHKEAVEILNEEGCRGIDLEELGSEG--------EKSLSEHFEE--PFW 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 414 VTDYPKAVKPFYMLPSSGSSNESGEtvacFDLLLPE-ICEVVGGSLREHRLSPLIRNMREHGLlklkdsTPEPssavdak 492
Cdd:PRK06462 223 IIDIPKGSREFYDREDPERPGVLRN----YDLLLPEgYGEAVSGGEREYEYEEIVERIREHGV------DPEK------- 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 302501169 493 apYphllaneelgsiQWYADLRRWGTVPHGGFGLGFDRFVGYLAGVSSLRDLVPFPR 549
Cdd:PRK06462 286 --Y------------KWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQPFPR 328
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
63-549 |
7.83e-33 |
|
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: 130.33 E-value: 7.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 63 LDHKELRVQGHVRFLRKQKRFAFAHISDGSSLqpIQAVLTPE--------QATNLTQGAAVEVTGIWQPSPPGKQqSHEL 134
Cdd:TIGR00458 10 MDGQEVTFMGWVHEIRDLGGLIFVLLRDREGL--IQITAPAKkvsknlfkWAKKLNLESVVAVRGIVKIKEKAPG-GFEI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 135 QATKVDIVGEADpaassstQTYPIQKKFHTPDFLR-QLPH--LRLRTPFNALLSRLRSEFIYQVTEEFRSHRdlnFVQVQ 211
Cdd:TIGR00458 87 IPTKIEVINEAK-------EPLPLDPTEKVPAELDtRLDYrfLDLRRPTVQAIFRIRSGVLESVREFLAEEG---FIEVH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 212 PPLITSSDCEGAGEVFSIrprdvvieegkavEFFKSPKYLTVSSQLHLEAY-AAELGNVWTLSPTFRAEKSDTPRHLSEF 290
Cdd:TIGR00458 157 TPKLVASATEGGTELFPI-------------TYFEREAFLGQSPQLYKQQLmAAGFERVYEIGPIFRAEEHNTHRHLNEA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 291 YMLEVEMSYMDSLEpltafVETLLRNMTQRVYkspvaqeifsfkatDDLTKDTTNAH-LEKRWMALIEGPrWPRITFAHA 369
Cdd:TIGR00458 224 TSIDIEMAFEDHHD-----VMDILEELVVRVF--------------EDVPERCAHQLeTLEFKLEKPEGK-FVRLTYDEA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 370 IkhlhEAVNTGLVTFdfspSWSGGLQLEHEKFLVDTIGkGLpIFVTDYPKAVKPFYMLPSSGSSNESGEtvacFDLLLPE 449
Cdd:TIGR00458 284 I----EMANAKGVEI----GWGEDLSTEAEKALGEEMD-GL-YFITDWPTEIRPFYTMPDEDNPEISKS----FDLMYRD 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 450 IcEVVGGSLREHRLSPLIRNMREHGLlklkdsTPEpssavdakapyphllaneelgSIQWYADLRRWGTVPHGGFGLGFD 529
Cdd:TIGR00458 350 L-EISSGAQRIHLHDLLVERIKAKGL------NPE---------------------GFKDYLEAFSYGMPPHAGWGLGAE 401
|
490 500
....*....|....*....|
gi 302501169 530 RFVGYLAGVSSLRDLVPFPR 549
Cdd:TIGR00458 402 RFVMFLLGLKNIREAVLFPR 421
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
62-549 |
2.22e-28 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 119.04 E-value: 2.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 62 SLDHKELRVQGHVRFLRKQKRFAFAHISdgSSLQPIQAVLTPEQ----------ATNLTQGAAVEVTGIWQ-PSPP--GK 128
Cdd:PLN02850 78 ELAGSEVLIRGRVHTIRGKGKSAFLVLR--QSGFTVQCVVFVSEvtvskgmvkyAKQLSRESVVDVEGVVSvPKKPvkGT 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 129 QQSHELQATKVDIVGEADPA-------ASSSTQTypIQKKFHTPD-FLRQLPHLRL-------RTPFNALLSRLRSefiy 193
Cdd:PLN02850 156 TQQVEIQVRKIYCVSKALATlpfnvedAARSESE--IEKALQTGEqLVRVGQDTRLnnrvldlRTPANQAIFRIQS---- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 194 QVTEEFR-SHRDLNFVQVQPPLITSSDCEGAGEVFSIrprdvvieegkavEFFKSPKYLTVSSQLHLE-AYAAELGNVWT 271
Cdd:PLN02850 230 QVCNLFReFLLSKGFVEIHTPKLIAGASEGGSAVFRL-------------DYKGQPACLAQSPQLHKQmAICGDFRRVFE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 272 LSPTFRAEKSDTPRHLSEFYMLEVEMSYMDSlepltaFVETLlrnmtqrvyksPVAQEIFSFKATddltkdttnaHLEKR 351
Cdd:PLN02850 297 IGPVFRAEDSFTHRHLCEFTGLDLEMEIKEH------YSEVL-----------DVVDELFVAIFD----------GLNER 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 352 WMALIE--GPRWP-----------RITFAHAIKHLHEAvntglvTFDFSPswSGGLQLEHEKFLVDTIGK--GLPIFVTD 416
Cdd:PLN02850 350 CKKELEaiREQYPfeplkylpktlRLTFAEGIQMLKEA------GVEVDP--LGDLNTESERKLGQLVKEkyGTDFYILH 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 417 -YPKAVKPFYMLPSSGSSNESGEtvacFDLLL--PEICEvvgGSLREHRLSPLIRNMREHGLlklkdstpepssavdaka 493
Cdd:PLN02850 422 rYPLAVRPFYTMPCPDDPKYSNS----FDVFIrgEEIIS---GAQRVHDPELLEKRAEECGI------------------ 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 302501169 494 pyphllaneELGSIQWYADLRRWGTVPHGGFGLGFDRFVGYLAGVSSLRDLVPFPR 549
Cdd:PLN02850 477 ---------DVKTISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPR 523
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
44-549 |
2.98e-27 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 115.86 E-value: 2.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 44 TLRCAQIFEQSKSGTTPSSLDhKELRVQGHVRFLRKQKRFAFAHISDGS-SLQPIQAVL--TPEQATNLTQGAAVE---- 116
Cdd:PTZ00401 58 TTYKSRTFIPVAVLSKPELVD-KTVLIRARVSTTRKKGKMAFMVLRDGSdSVQAMAAVEgdVPKEMIDFIGQIPTEsivd 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 117 ----VTGIWQPSPPGKQQSHELQATKVDIVGEADPA-------ASSSTQTYPIQKKFHTPDFLRQLPhlrLRTPFNALLS 185
Cdd:PTZ00401 137 veatVCKVEQPITSTSHSDIELKVKKIHTVTESLRTlpftledASRKESDEGAKVNFDTRLNSRWMD---LRTPASGAIF 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 186 RLRSefiyQVTEEFRSHR-DLNFVQVQPPLITSSDCEGAGEVFSirprdvvieegkaVEFFKSPKYLTVSSQLHLE-AYA 263
Cdd:PTZ00401 214 RLQS----RVCQYFRQFLiDSDFCEIHSPKIINAPSEGGANVFK-------------LEYFNRFAYLAQSPQLYKQmVLQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 264 AELGNVWTLSPTFRAEKSDTPRHLSEFYMLEVEMSYMDSLEPLTAFVETLLRNMTQRVYK-----SPVAQ----EIFSFK 334
Cdd:PTZ00401 277 GDVPRVFEVGPVFRSENSNTHRHLTEFVGLDVEMRINEHYYEVLDLAESLFNYIFERLAThtkelKAVCQqypfEPLVWK 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 335 ATDDLTKDTTNAHLEK------RWMALIE--GPRWPRITFAHAIKHLHEAVNTGLVTFDfspswsgGLQLEHEKFLVDTI 406
Cdd:PTZ00401 357 LTPERMKELGVGVISEgveptdKYQARVHnmDSRMLRINYMHCIELLNTVLEEKMAPTD-------DINTTNEKLLGKLV 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 407 GK--GLPIFVTD-YPKAVKPFYMLPSSGSSNESGEtvacFDLLLPEIcEVVGGSLREHRLSPLIRNMRehgllklkdstp 483
Cdd:PTZ00401 430 KEryGTDFFISDrFPSSARPFYTMECKDDERFTNS----YDMFIRGE-EISSGAQRIHDPDLLLARAK------------ 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 302501169 484 epssavdakapyphlLANEELGSIQWYADLRRWGTVPHGGFGLGFDRFVGYLAGVSSLRDLVPFPR 549
Cdd:PTZ00401 493 ---------------MLNVDLTPIKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFPR 543
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
67-144 |
1.39e-24 |
|
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: 97.25 E-value: 1.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 67 ELRVQGHVRFLRKQKRFAFAHISDGSSLQPIQAVLTPEQAT-----NLTQGAAVEVTGIWQPSpPGKQQSHELQATKVDI 141
Cdd:cd04318 1 EVTVNGWVRSVRDSKKISFIELNDGSCLKNLQVVVDKELTNfkeilKLSTGSSIRVEGVLVKS-PGAKQPFELQAEKIEV 79
|
...
gi 302501169 142 VGE 144
Cdd:cd04318 80 LGE 82
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
186-549 |
4.30e-22 |
|
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: 96.01 E-value: 4.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 186 RLRSEFIYQVTEEFRSHrdlNFVQVQPPLITSSDCEGAGEVFSIRPRDVvieeGKAVeffkspkYLTVSSQLHLEAY-AA 264
Cdd:cd00669 2 KVRSKIIKAIRDFMDDR---GFLEVETPMLQKITGGAGARPFLVKYNAL----GLDY-------YLRISPQLFKKRLmVG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 265 ELGNVWTLSPTFRAEKSDTpRHLSEFYMLEVEMSYMDsLEPLTAFVETLLRNMTQRVykspvaqeifsfkatddltKDTT 344
Cdd:cd00669 68 GLDRVFEINRNFRNEDLRA-RHQPEFTMMDLEMAFAD-YEDVIELTERLVRHLAREV-------------------LGVT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 345 NAHLEKRwmaLIEGPR-WPRITFAHAIKHLheavntglvtfdfspswsgglqlehekflvdtigkGLPIFVTDYPKAVKP 423
Cdd:cd00669 127 AVTYGFE---LEDFGLpFPRLTYREALERY-----------------------------------GQPLFLTDYPAEMHS 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 424 FYMLPSSGSSNESGEtvacFDLLLPEIcEVVGGSLREHRLSPLIRNMREHGLlklkdstpepssavdakapyphllaNEE 503
Cdd:cd00669 169 PLASPHDVNPEIADA----FDLFINGV-EVGNGSSRLHDPDIQAEVFQEQGI-------------------------NKE 218
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 302501169 504 LG--SIQWYADLRRWGTVPHGGFGLGFDRFVGYLAGVSSLRDLVPFPR 549
Cdd:cd00669 219 AGmeYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPK 266
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
62-322 |
1.03e-08 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 58.07 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 62 SLDH--KELRVQGHVRFLRKQKRFAFAHISDGSSLqpIQAVLTPE--------QATNLTQGAAVEVTGIWQPSPPGKQQS 131
Cdd:PRK12820 13 SLDDtgREVCLAGWVDAFRDHGELLFIHLRDRNGF--IQAVFSPEaapadvyeLAASLRAEFCVALQGEVQKRLEETENP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 132 HeLQATKVDI-VGEADPAASSSTQTYPIQKKFHTP------------DFLRQLPHLRLRTPF--NALLSRLRsefIYQVT 196
Cdd:PRK12820 91 H-IETGDIEVfVRELSILAASEALPFAISDKAMTAgagsagadavneDLRLQYRYLDIRRPAmqDHLAKRHR---IIKCA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 197 EEFRSHRdlNFVQVQPPLITSSDCEGAGEVF---SIRPRdvvieegkavEFFKSPKYLTVSSQLHLeayAAELGNVWTLS 273
Cdd:PRK12820 167 RDFLDSR--GFLEIETPILTKSTPEGARDYLvpsRIHPK----------EFYALPQSPQLFKQLLM---IAGFERYFQLA 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 302501169 274 PTFRAEKSdTPRHLSEFYMLEVEMSYMDSlepltAFVETLLRNMTQRVY 322
Cdd:PRK12820 232 RCFRDEDL-RPNRQPEFTQLDIEASFIDE-----EFIFELIEELTARMF 274
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
67-144 |
1.61e-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: 51.85 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 67 ELRVQGHVRFLRKQKRFAFAHISDGSSLqpIQAVLT------PEQATNLTQGAAVEVTGIWQPSPPGKQQ--SHELQATK 138
Cdd:cd04323 1 RVKVFGWVHRLRSQKKLMFLVLRDGTGF--LQCVLSkklvteFYDAKSLTQESSVEVTGEVKEDPRAKQApgGYELQVDY 78
|
....*.
gi 302501169 139 VDIVGE 144
Cdd:cd04323 79 LEIIGE 84
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
517-548 |
3.99e-06 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 49.68 E-value: 3.99e-06
10 20 30
....*....|....*....|....*....|..
gi 302501169 517 GTVPHGGFGLGFDRFVGYLAGVSSLRDLVPFP 548
Cdd:PRK00476 525 GAPPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
452-549 |
4.16e-06 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 49.79 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 452 EVVGGSLREHRlspliRNMREHgLLKLKDSTPEpssavDAKAPYPHLLANEELGSiqwyadlrrwgtVPHGGFGLGFDRF 531
Cdd:PLN02903 546 EIGGGSLRIYR-----RDVQQK-VLEAIGLSPE-----EAESKFGYLLEALDMGA------------PPHGGIAYGLDRL 602
|
90
....*....|....*...
gi 302501169 532 VGYLAGVSSLRDLVPFPR 549
Cdd:PLN02903 603 VMLLAGAKSIRDVIAFPK 620
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
250-548 |
4.73e-06 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 49.29 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 250 YLTVSSQLHLEAYA-AELGNVWTLSPTFRAEKSDTpRHLSEFYMLEVEMSYMDsLEPLTAFVETLLRNMTQRVY---KSP 325
Cdd:PRK12445 235 YLRIAPELYLKRLVvGGFERVFEINRNFRNEGISV-RHNPEFTMMELYMAYAD-YHDLIELTESLFRTLAQEVLgttKVT 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 326 VAQEIFSFkatddltkdttnahlekrwmalieGPRWPRITFAHAI-KHLHEAVNTGLVTFDFSPSWSGGLQLEHEKF--- 401
Cdd:PRK12445 313 YGEHVFDF------------------------GKPFEKLTMREAIkKYRPETDMADLDNFDAAKALAESIGITVEKSwgl 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 402 ------LVDTIGKG---LPIFVTDYPKAVKPfymlpssgssnesgetVACFDLLLPEICE----VVGGslREhrlsplIR 468
Cdd:PRK12445 369 grivteIFDEVAEAhliQPTFITEYPAEVSP----------------LARRNDVNPEITDrfefFIGG--RE------IG 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 469 NmrehGLLKLKDSTPEP---SSAVDAKAPYPhllaNEELGSIQWYADLRRWGTVPHGGFGLGFDRFVGYLAGVSSLRDLV 545
Cdd:PRK12445 425 N----GFSELNDAEDQAerfQEQVNAKAAGD----DEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVI 496
|
...
gi 302501169 546 PFP 548
Cdd:PRK12445 497 LFP 499
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
517-548 |
6.35e-06 |
|
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439943 [Multi-domain] Cd Length: 589 Bit Score: 48.84 E-value: 6.35e-06
10 20 30
....*....|....*....|....*....|..
gi 302501169 517 GTVPHGGFGLGFDRFVGYLAGVSSLRDLVPFP 548
Cdd:COG0173 524 GAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
69-142 |
1.28e-05 |
|
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: 43.38 E-value: 1.28e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 302501169 69 RVQGHVRFLRKQ-KRFAFAHISDGSSlqPIQAVLTPE----QATNLTQGAAVEVTGIWQPSPPGKqqsHELQATKVDIV 142
Cdd:pfam01336 2 TVAGRVTSIRRSgGKLLFLTLRDGTG--SIQVVVFKEeaekLAKKLKEGDVVRVTGKVKKRKGGE---LELVVEEIELL 75
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
276-423 |
1.53e-05 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 47.78 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 276 FRAEKSDTpRHLSEFYMLEVEMSYMDsLEPLTAFVETLLRNMTQRVYKSPV----AQEIfsfkatdDLTKDttnahlekr 351
Cdd:PRK00484 250 FRNEGIDT-RHNPEFTMLEFYQAYAD-YNDMMDLTEELIRHLAQAVLGTTKvtyqGTEI-------DFGPP--------- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 352 wmaliegprWPRITFAHAIKHlHEAVNTGLVTFD------------FSPSWSGGLQLEH--EKF----LVDtigkglPIF 413
Cdd:PRK00484 312 ---------FKRLTMVDAIKE-YTGVDFDDMTDEearalakelgieVEKSWGLGKLINElfEEFvepkLIQ------PTF 375
|
170
....*....|
gi 302501169 414 VTDYPKAVKP 423
Cdd:PRK00484 376 ITDYPVEISP 385
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
190-305 |
2.82e-03 |
|
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.
Pssm-ID: 238391 [Multi-domain] Cd Length: 211 Bit Score: 39.41 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302501169 190 EFIYQVTEEFrsHRDLNFVQVQPPLITS-SDCEGAGEVFSIRPRDVVIEEGKAveffkspkYLTVSSQLHLEAYAAELGN 268
Cdd:cd00768 3 SKIEQKLRRF--MAELGFQEVETPIVERePLLEKAGHEPKDLLPVGAENEEDL--------YLRPTLEPGLVRLFVSHIR 72
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 302501169 269 -----VWTLSPTFRAEKSDT-PRHLSEFYMLEVEMSYMDSLEP 305
Cdd:cd00768 73 klplrLAEIGPAFRNEGGRRgLRRVREFTQLEGEVFGEDGEEA 115
|
|
| |
