|
Name |
Accession |
Description |
Interval |
E-value |
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
6-467 |
0e+00 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 822.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 6 RTKIVDLLKRTDIGAMVNVKGWVRTRRGSKQVNFIALNDGSTINNLQIVVDLANFDEEMLKLITTGACISVNGEMVESVG 85
Cdd:PRK03932 3 RVSIKDILKGKYVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDNGEEYFEEIKKLTTGSSVIVTGTVVESPR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 86 SGQKVEVQAREIEVLGTCDNTYPLQKKGHSMEFLREIAHLRPRTNTFGAVFRIRHNMAIAIHKFFHEKGFFYFHTPIITA 165
Cdd:PRK03932 83 AGQGYELQATKIEVIGEDPEDYPIQKKRHSIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVDTPIITA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 166 SDCEGAGQMFQVTTMNLydlkkdergsiSYEDDFFGKQASLTVSGQLEGELAATALGAIYTFGPTFRAENSNTPRHLAEF 245
Cdd:PRK03932 163 SDCEGAGELFRVTTLDL-----------DFSKDFFGKEAYLTVSGQLYAEAYAMALGKVYTFGPTFRAENSNTRRHLAEF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 246 WMIEPEVAFNDITDNMDLAEEFIKYCVKWALDNCADDVKFLNDMFDKGLIERLQGVLKDDFVRLPYTDGIKILEEavaKG 325
Cdd:PRK03932 232 WMIEPEMAFADLEDNMDLAEEMLKYVVKYVLENCPDDLEFLNRRVDKGDIERLENFIESPFPRITYTEAIEILQK---SG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 326 HKFEFPVYWGVDLASEHERFLVEEHFKRPVILTDYPKEIKAFYMKQNEDGKTVRAMDVLFPKIGEIIGGSEREADYNKLM 405
Cdd:PRK03932 309 KKFEFPVEWGDDLGSEHERYLAEEHFKKPVFVTNYPKDIKAFYMRLNPDGKTVAAMDLLAPGIGEIIGGSQREERLDVLE 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490425014 406 TRIEEMHIPMKDMWWYLDTRKFGTCPHSGFGLGFERLLLFVTGMANIRDVIPFPRTPRNADF 467
Cdd:PRK03932 389 ARIKELGLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
6-465 |
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: 708.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 6 RTKIVDLLKrTDIGAMVNVKGWVRTRRGSKQVNFIALNDGSTInnLQIVVD---LANFDEemLKLITTGACISVNGEMVE 82
Cdd:COG0017 2 RTYIKDLLP-EHVGQEVTVAGWVRTKRDSGGISFLILRDGSGF--IQVVVKkdkLENFEE--AKKLTTESSVEVTGTVVE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 83 SVGSGQKVEVQAREIEVLGTCDNTYPLQKKGHSMEFLREIAHLRPRTNTFGAVFRIRHNMAIAIHKFFHEKGFFYFHTPI 162
Cdd:COG0017 77 SPRAPQGVELQAEEIEVLGEADEPYPLQPKRHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVEVHTPI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 163 ITASDCEGAGQMFQVttmnlydlkkdergsisyedDFFGKQASLTVSGQLEGELAATALGAIYTFGPTFRAENSNTPRHL 242
Cdd:COG0017 157 ITASATEGGGELFPV--------------------DYFGKEAYLTQSGQLYKEALAMALEKVYTFGPTFRAEKSNTRRHL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 243 AEFWMIEPEVAFNDITDNMDLAEEFIKYCVKWALDNCADDVKFLNDMfdkglIERLQGVLKDDFVRLPYTDGIKILEEav 322
Cdd:COG0017 217 AEFWMIEPEMAFADLEDVMDLAEEMLKYIIKYVLENCPEELEFLGRD-----VERLEKVPESPFPRITYTEAIEILKK-- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 323 aKGHKFEfpvyWGVDLASEHERFLVEEHFKRPVILTDYPKEIKAFYMKQN-EDGKTVRAMDVLFPKIGEIIGGSEREADY 401
Cdd:COG0017 290 -SGEKVE----WGDDLGTEHERYLGEEFFKKPVFVTDYPKEIKAFYMKPNpDDPKTVAAFDLLAPGIGEIIGGSQREHRY 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490425014 402 NKLMTRIEEMHIPMKDMWWYLDTRKFGTCPHSGFGLGFERLLLFVTGMANIRDVIPFPRTPRNA 465
Cdd:COG0017 365 DVLVERIKEKGLDPEDYEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRL 428
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
7-467 |
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: 666.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 7 TKIVDLLK--RTDIGAMVNVKGWVRTRRGSKQVNFIALNDGSTINNLQIVVD--LANFDEEMLKLITTGACISVNGEMVE 82
Cdd:TIGR00457 2 AAIKDLLQqvYKFVGDEVTVSGWVRTKRSSKKIIFLELNDGSSLGPIQAVINgeDNPYLFQLLKSLTTGSSVSVTGKVVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 83 SVGSGQKVEVQAREIEVLGTCD-NTYPLQKKGHSMEFLREIAHLRPRTNTFGAVFRIRHNMAIAIHKFFHEKGFFYFHTP 161
Cdd:TIGR00457 82 SPGKGQPVELQVKKIEVVGEAEpDDYPLQKKEHSLEFLRDIAHLRLRTNTLGAVMRVRNALSQAIHRYFQENGFTWVSPP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 162 IITASDCEGAGQMFQVTTmnlydlkkderGSISYEDDFFGKQASLTVSGQLEGELAATALGAIYTFGPTFRAENSNTPRH 241
Cdd:TIGR00457 162 ILTSNDCEGAGELFRVST-----------GNIDFSQDFFGKEAYLTVSGQLYLETYALALSKVYTFGPTFRAEKSNTSRH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 242 LAEFWMIEPEVAFNDITDNMDLAEEFIKYCVKWALDNCADDVKFLNDMFDKGLIERLQGVLKDDFVRLPYTDGIKILEEA 321
Cdd:TIGR00457 231 LSEFWMIEPEMAFANLNDLLQLAETLIKYIIKAVLENCSQELKFLEKNFDKDLIKRLENIINNKFARITYTDAIEILKES 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 322 VAKghkFEFPVYWGVDLASEHERFLVEEHFKRPVILTDYPKEIKAFYMKQNEDGKTVRAMDVLFPKIGEIIGGSEREADY 401
Cdd:TIGR00457 311 DKN---FEYEDFWGDDLQTEHERFLAEEYFKPPVFVTNYPKDIKAFYMKLNDDGKTVAAMDLLAPGIGEIIGGSEREDDL 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490425014 402 NKLMTRIEEMHIPMKDMWWYLDTRKFGTCPHSGFGLGFERLLLFVTGMANIRDVIPFPRTPRNADF 467
Cdd:TIGR00457 388 DKLENRMKEMGLDTDALNWYLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGNINF 453
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
2-467 |
0e+00 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 598.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 2 EKIG----RTKIVDLLKRTD-----IGAMVNVKGWVRTRRGSKQVNFIALNDGSTINNLQIVVDL--ANFDEEMLKLITT 70
Cdd:PLN02603 81 EAVGefrkKLRIADVKGGEDeglarVGKTLNVMGWVRTLRAQSSVTFIEVNDGSCLSNMQCVMTPdaEGYDQVESGLITT 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 71 GACISVNGEMVESVGSGQKVEVQAREIEVLGTCDNTYPLQKKGHSMEFLREIAHLRPRTNTFGAVFRIRHNMAIAIHKFF 150
Cdd:PLN02603 161 GASVLVQGTVVSSQGGKQKVELKVSKIVVVGKSDPSYPIQKKRVSREFLRTKAHLRPRTNTFGAVARVRNALAYATHKFF 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 151 HEKGFFYFHTPIITASDCEGAGQMFQVTTM----------NLYDLKKDERGSISYEDDFFGKQASLTVSGQLEGELAATA 220
Cdd:PLN02603 241 QENGFVWVSSPIITASDCEGAGEQFCVTTLipnsaenggsLVDDIPKTKDGLIDWSQDFFGKPAFLTVSGQLNGETYATA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 221 LGAIYTFGPTFRAENSNTPRHLAEFWMIEPEVAFNDITDNMDLAEEFIKYCVKWALDNCADDVKFLNDMFDKGLIERLQG 300
Cdd:PLN02603 321 LSDVYTFGPTFRAENSNTSRHLAEFWMIEPELAFADLNDDMACATAYLQYVVKYILENCKEDMEFFNTWIEKGIIDRLSD 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 301 VLKDDFVRLPYTDGIKILeeaVAKGHKFEFPVYWGVDLASEHERFLVEEHFK-RPVILTDYPKEIKAFYMKQNEDGKTVR 379
Cdd:PLN02603 401 VVEKNFVQLSYTDAIELL---LKAKKKFEFPVKWGLDLQSEHERYITEEAFGgRPVIIRDYPKEIKAFYMRENDDGKTVA 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 380 AMDVLFPKIGEIIGGSEREADYNKLMTRIEEMHIPMKDMWWYLDTRKFGTCPHSGFGLGFERLLLFVTGMANIRDVIPFP 459
Cdd:PLN02603 478 AMDMLVPRVGELIGGSQREERLEYLEARLDELKLNKESYWWYLDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFP 557
|
....*...
gi 490425014 460 RTPRNADF 467
Cdd:PLN02603 558 RVPGSAEF 565
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
6-467 |
0e+00 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 543.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 6 RTKIVDLLKRTDIGA-----MVNVKGWVRTRR--GSKQVNFIALNDGSTINNLQIVVDLANFDeeMLKLITTGACISVNG 78
Cdd:PLN02221 32 RVLIRSILDRPDGGAglagqKVRIGGWVKTGReqGKGTFAFLEVNDGSCPANLQVMVDSSLYD--LSTLVATGTCVTVDG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 79 EMV---ESVGSGQKVEVQAREIEVLGTCD-NTYPLQKKGHSMEFLREIAHLRPRTNTFGAVFRIRHNMAIAIHKFFHEKG 154
Cdd:PLN02221 110 VLKvppEGKGTKQKIELSVEKVIDVGTVDpTKYPLPKTKLTLEFLRDVLHLRSRTNSISAVARIRNALAFATHSFFQEHS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 155 FFYFHTPIITASDCEGAGQMFQVTTM---------NLYD-------------------------LKK------------- 187
Cdd:PLN02221 190 FLYIHTPIITTSDCEGAGEMFQVTTLinyterleqDLIDnpppteadveaarlivkergevvaqLKAakaskeeitaava 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 188 ------------DER-----------GSISYEDDFFGKQASLTVSGQLEGELAATALGAIYTFGPTFRAENSNTPRHLAE 244
Cdd:PLN02221 270 elkiakeslahiEERsklkpglpkkdGKIDYSKDFFGRQAFLTVSGQLQVETYACALSSVYTFGPTFRAENSHTSRHLAE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 245 FWMIEPEVAFNDITDNMDLAEEFIKYCVKWALDNCADDVKFLNDMFDKGLIERLQGVLKDDFVRLPYTDGIKILEEAVAK 324
Cdd:PLN02221 350 FWMVEPEIAFADLEDDMNCAEAYVKYMCKWLLDKCFDDMELMAKNFDSGCIDRLRMVASTPFGRITYTEAIELLEEAVAK 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 325 GHKFEFPVYWGVDLASEHERFLVEEHFKRPVILTDYPKEIKAFYMKQNEDGKTVRAMDVLFPKIGEIIGGSEREADYNKL 404
Cdd:PLN02221 430 GKEFDNNVEWGIDLASEHERYLTEVLFQKPLIVYNYPKGIKAFYMRLNDDEKTVAAMDVLVPKVGELIGGSQREERYDVI 509
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490425014 405 MTRIEEMHIPMKDMWWYLDTRKFGTCPHSGFGLGFERLLLFVTGMANIRDVIPFPRTPRNADF 467
Cdd:PLN02221 510 KQRIEEMGLPIEPYEWYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPRYPGKADL 572
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
18-467 |
1.27e-172 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 497.62 E-value: 1.27e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 18 IGAMVNVKGWVRTRR--GSKQVNFIALNDGSTINNLQIVVDLANFDEEMLKLITTGACISVNGEMVESVGSGQKVEVQAR 95
Cdd:PTZ00425 80 IDQIITVCGWSKAVRkqGGGRFCFVNLNDGSCHLNLQIIVDQSIENYEKLLKCGVGCCFRFTGKLIISPVQNENKKGLLK 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 96 EIEVLGTCDNT---------------YPLQKKGHSMEFLREIAHLRPRTNTFGAVFRIRHNMAIAIHKFFHEKGFFYFHT 160
Cdd:PTZ00425 160 ENVELALKDNSihnfeiygenldpqkYPLSKKNHGKEFLREVAHLRPRSYFISSVIRIRNALAIATHLFFQSRGFLYIHT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 161 PIITASDCEGAGQMFQVTTM-------------NLYDLKKDERGS------------------------------ISYED 197
Cdd:PTZ00425 240 PLITTSDCEGGGEMFTVTTLlgedadyraiprvNKKNKKGEKREDilntcnannnngnssssnavsspaypdqylIDYKK 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 198 DFFGKQASLTVSGQLEGELAATALGAIYTFGPTFRAENSNTPRHLAEFWMIEPEVAFNDITDNMDLAEEFIKYCVKWALD 277
Cdd:PTZ00425 320 DFFSKQAFLTVSGQLSLENLCSSMGDVYTFGPTFRAENSHTSRHLAEFWMIEPEIAFADLYDNMELAESYIKYCIGYVLN 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 278 NCADDVKFLNDMFDKGLIERLQGVLKDDFVRLPYTDGIKILEEAvakGHKFEFPVYWGVDLASEHERFLVEEHFKRPVIL 357
Cdd:PTZ00425 400 NNFDDIYYFEENVETGLISRLKNILDEDFAKITYTNVIDLLQPY---SDSFEVPVKWGMDLQSEHERFVAEQIFKKPVIV 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 358 TDYPKEIKAFYMKQNEDGKTVRAMDVLFPKIGEIIGGSEREADYNKLMTRIEEMHIPMKDMWWYLDTRKFGTCPHSGFGL 437
Cdd:PTZ00425 477 YNYPKDLKAFYMKLNEDQKTVAAMDVLVPKIGEVIGGSQREDNLERLDKMIKEKKLNMESYWWYRQLRKFGSHPHAGFGL 556
|
490 500 510
....*....|....*....|....*....|
gi 490425014 438 GFERLLLFVTGMANIRDVIPFPRTPRNADF 467
Cdd:PTZ00425 557 GFERLIMLVTGVDNIKDTIPFPRYPGHAEF 586
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
114-463 |
2.83e-147 |
|
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: 423.13 E-value: 2.83e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 114 HSMEFLREIAHLRPRTNTFGAVFRIRHNMAIAIHKFFHEKGFFYFHTPIITASDCEGagqmfqvttmnlydlkkderGSI 193
Cdd:cd00776 2 ANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEG--------------------GAE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 194 SYEDDFFGKQASLTVSGQLEGELAATALGAIYTFGPTFRAENSNTPRHLAEFWMIEPEVAF-NDITDNMDLAEEFIKYCV 272
Cdd:cd00776 62 LFKVSYFGKPAYLAQSPQLYKEMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFiEDYNEVMDLIEELIKYIF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 273 KWALDNCADDVKFLNDmfdkglIERLQGVLKDDFVRLPYTDGIKILEEavakgHKFEFPVYWGVDLASEHERFLVEEHFK 352
Cdd:cd00776 142 KRVLERCAKELELVNQ------LNRELLKPLEPFPRITYDEAIELLRE-----KGVEEEVKWGEDLSTEHERLLGEIVKG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 353 RPVILTDYPKEIKAFYMKQNED-GKTVRAMDVLFPKIGEIIGGSEREADYNKLMTRIEEMHIPMKDMWWYLDTRKFGTCP 431
Cdd:cd00776 211 DPVFVTDYPKEIKPFYMKPDDDnPETVESFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPP 290
|
330 340 350
....*....|....*....|....*....|..
gi 490425014 432 HSGFGLGFERLLLFVTGMANIRDVIPFPRTPR 463
Cdd:cd00776 291 HGGFGLGLERLVMWLLGLDNIREAILFPRDPK 322
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
29-461 |
2.92e-142 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 421.59 E-value: 2.92e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 29 RTRRGSKQVNFIALNDGSTINNLQIVVD--LANFDEemlkLITTGACISVNG--EMVESVGSGQKVEVQAREIEVLGTCD 104
Cdd:PLN02532 127 KSAPPPPSVAYLLISDGSCVASLQVVVDsaLAPLTQ----LMATGTCILAEGvlKLPLPAQGKHVIELEVEKILHIGTVD 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 105 -NTYPLQKKGHSMEFLREIAHLRPRTNTFGAVFRIRHNMAIAIHKFFHEKGFFYFHTPIITASDCEGAGQMFQVTTM--- 180
Cdd:PLN02532 203 pEKYPLSKKRLPLDMLRDFSHFRPRTTTVASVTRVRSALTHATHTFFQDHGFLYVQVPIITTTDATGFGEMFRVTTLlgk 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 181 -----------------------------NLYD-LKKDERG------------------------------------SIS 194
Cdd:PLN02532 283 sddkeekkpvhetegisleavkaaikektNLVEeLKRSESNrealvaaeqdlrktnqlasqleakeklktgtsvkadKLS 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 195 YEDDFFGKQASLTVSGQLEGELAATALGAIYTFGPTFRAENSNTPRHLAEFWMIEPEVAFNDITDNMDLAEEFIKYCVKW 274
Cdd:PLN02532 363 FSKDFFSRPTYLTVSGRLHLESYACALGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAFSELEDAMNCAEDYFKFLCKW 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 275 ALDNCADDVKFLNDMFDKGLIERLQGVLKDDFVRLPYTDGIKILEEAVAKghKFEFPVYWGVDLASEHERFLVEEHFKRP 354
Cdd:PLN02532 443 VLENCSEDMKFVSKRIDKTISTRLEAIISSSLQRISYTEAVDLLKQATDK--KFETKPEWGIALTTEHLSYLADEIYKKP 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 355 VILTDYPKEIKAFYMKQNEDGKTVRAMDVLFPKIGEIIGGSEREADYNKLMTRIEEMHIPMKDMWWYLDTRKFGTCPHSG 434
Cdd:PLN02532 521 VIIYNYPKELKPFYVRLNDDGKTVAAFDLVVPKVGTVITGSQNEERMDILNARIEELGLPREQYEWYLDLRRHGTVKHSG 600
|
490 500
....*....|....*....|....*..
gi 490425014 435 FGLGFERLLLFVTGMANIRDVIPFPRT 461
Cdd:PLN02532 601 FSLGFELMVLFATGLPDVRDAIPFPRS 627
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
6-460 |
2.12e-82 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 260.89 E-value: 2.12e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 6 RTKIVDLLKRTDiGAMVNVKGWVRTRRGSKQVNFIALNDGSTInnLQIVVDLANFDE--EMLKLITTGACISVNGEMVES 83
Cdd:PRK05159 4 RHLTSELTPELD-GEEVTLAGWVHEIRDLGGIAFLILRDRSGI--IQVVVKKKVDEElfETIKKLKRESVVSVTGTVKAN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 84 VGSGQKVEVQAREIEVLGTCDNTYPLQ---KKGHSMEFLREIAHL---RPRTNtfgAVFRIRHNMAIAIHKFFHEKGFFY 157
Cdd:PRK05159 81 PKAPGGVEVIPEEIEVLNKAEEPLPLDisgKVLAELDTRLDNRFLdlrRPRVR---AIFKIRSEVLRAFREFLYENGFTE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 158 FHTPIITASDCEGAGQMFQVttmnlydlkkdergsisyedDFFGKQASLTVSGQLEGE-LAATALGAIYTFGPTFRAENS 236
Cdd:PRK05159 158 IFTPKIVASGTEGGAELFPI--------------------DYFEKEAYLAQSPQLYKQmMVGAGFERVFEIGPVFRAEEH 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 237 NTPRHLAEFWMIEPEVAF-NDITDNMDLAEEFIKYCVKWALDNCADDVKFLNDMFDkglierlqgVLKDDFVRLPYTDGI 315
Cdd:PRK05159 218 NTSRHLNEYTSIDVEMGFiDDHEDVMDLLENLLRYMYEDVAENCEKELELLGIELP---------VPETPIPRITYDEAI 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 316 KILEEavaKGHKFEfpvyWGVDLASEHERFL----VEEHFKRPVILTDYPKEIKAFYMKQNEDGKTV-RAMDVLFPKIgE 390
Cdd:PRK05159 289 EILKS---KGNEIS----WGDDLDTEGERLLgeyvKEEYGSDFYFITDYPSEKRPFYTMPDEDDPEIsKSFDLLFRGL-E 360
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 391 IIGGSEREADYNKLMTRIEEMHIPMKDMWWYLDTRKFGTCPHSGFGLGFERLLLFVTGMANIRDVIPFPR 460
Cdd:PRK05159 361 ITSGGQRIHRYDMLVESIKEKGLNPESFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFPR 430
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
115-462 |
6.11e-75 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 237.85 E-value: 6.11e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 115 SMEFLREIAHLRPRTNTFGAVFRIRHNMAIAIHKFFHEKGFFYFHTPIITASDCEGAGQMFQVTTMNLydlkkdergsis 194
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRAL------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 195 yeDDFFgkqaSLTVSGQLEGE-LAATALGAIYTFGPTFRAENSNTPRHLaEFWMIEPEVAFNDITDNMDLAEEFIKYCVK 273
Cdd:pfam00152 69 --GKFY----ALPQSPQLYKQlLMVAGFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVDYEDVMDLTEELIKEIFK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 274 wALDNCADDVkflndmFDKGLIErlqgvLKDDFVRLPYTDGIKILEEavakghkfEFPVYWGVDLASEHERFLVE----E 349
Cdd:pfam00152 142 -EVEGIAKEL------EGGTLLD-----LKKPFPRITYAEAIEKLNG--------KDVEELGYGSDKPDLRFLLElvidK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 350 HFKRPVILTDYPKEIKAFYMKQNEDGK-TVRAMDVLFPKIgEIIGGSEREADYNKLMTRIEEMHI----PMKDMWWYLDT 424
Cdd:pfam00152 202 NKFNPLWVTDFPAEHHPFTMPKDEDDPaLAEAFDLVLNGV-EIGGGSIRIHDPELQEERFEEQGLdpeeAEEKFGFYLDA 280
|
330 340 350
....*....|....*....|....*....|....*...
gi 490425014 425 RKFGTCPHSGFGLGFERLLLFVTGMANIRDVIPFPRTP 462
Cdd:pfam00152 281 LKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAFPKTR 318
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
135-462 |
7.90e-58 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 194.08 E-value: 7.90e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 135 VFRIRHNMAIAIHKFFHEKGFFYFHTPIITasdcegagqmfQVTT--MNLYDLKKDERGSIsyedDFFGKQASLTVSGQL 212
Cdd:PRK06462 29 VLKVQSSILRYTREFLDGRGFVEVLPPIIS-----------PSTDplMGLGSDLPVKQISI----DFYGVEYYLADSMIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 213 EGELAATALGAIYTFGPTFRAEN--SNTPRHLAEFWMIEPEVAFNDITDNMDLAEEFIKYCVKWALDNCADDVKFLndmf 290
Cdd:PRK06462 94 HKQLALRMLGKIFYLSPNFRLEPvdKDTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHEDELEFF---- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 291 dkgliERLQGVLKDDFVRLPYTDGIKILEEAVAKGHKFEfpvywgvDLASEHERFLvEEHFKRPVILTDYPKEIKAFYMK 370
Cdd:PRK06462 170 -----GRDLPHLKRPFKRITHKEAVEILNEEGCRGIDLE-------ELGSEGEKSL-SEHFEEPFWIIDIPKGSREFYDR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 371 Q--NEDGkTVRAMDVLFPK-IGEIIGGSEREADYNKLMTRIEEMHIPMKDMWWYLDTRKFGTCPHSGFGLGFERLLLFVT 447
Cdd:PRK06462 237 EdpERPG-VLRNYDLLLPEgYGEAVSGGEREYEYEEIVERIREHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYIC 315
|
330
....*....|....*
gi 490425014 448 GMANIRDVIPFPRTP 462
Cdd:PRK06462 316 GLRHIREVQPFPRVP 330
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
8-463 |
6.39e-57 |
|
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: 194.27 E-value: 6.39e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 8 KIVDLLKRTDiGAMVNVKGWVRTRRGSKQVNFIALNDGSTInnLQIVVDLANFDEEMLKLITT---GACISVNGEMVESV 84
Cdd:TIGR00458 2 YSADIKPEMD-GQEVTFMGWVHEIRDLGGLIFVLLRDREGL--IQITAPAKKVSKNLFKWAKKlnlESVVAVRGIVKIKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 85 GSGQKVEVQAREIEVLGTCDNTYPL---QKKGHSMEFLREIAHLRPRTNTFGAVFRIRHNMAIAIHKFFHEKGFFYFHTP 161
Cdd:TIGR00458 79 KAPGGFEIIPTKIEVINEAKEPLPLdptEKVPAELDTRLDYRFLDLRRPTVQAIFRIRSGVLESVREFLAEEGFIEVHTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 162 IITASDCEGAGQMFQVTtmnlydlkkdergsisyeddFFGKQASLTVSGQLEGE-LAATALGAIYTFGPTFRAENSNTPR 240
Cdd:TIGR00458 159 KLVASATEGGTELFPIT--------------------YFEREAFLGQSPQLYKQqLMAAGFERVYEIGPIFRAEEHNTHR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 241 HLAEFWMIEPEVAFNDITDNMDLAEEFIKYCVKWALDNCADDVKFLNDMFDKGlierlqgvlKDDFVRLPYTDGIKILEe 320
Cdd:TIGR00458 219 HLNEATSIDIEMAFEDHHDVMDILEELVVRVFEDVPERCAHQLETLEFKLEKP---------EGKFVRLTYDEAIEMAN- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 321 avAKGHkfefPVYWGVDLASEHERFLVEEhFKRPVILTDYPKEIKAFY-MKQNEDGKTVRAMDvLFPKIGEIIGGSEREA 399
Cdd:TIGR00458 289 --AKGV----EIGWGEDLSTEAEKALGEE-MDGLYFITDWPTEIRPFYtMPDEDNPEISKSFD-LMYRDLEISSGAQRIH 360
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490425014 400 DYNKLMTRIEEMHIPMKDMWWYLDTRKFGTCPHSGFGLGFERLLLFVTGMANIRDVIPFPRTPR 463
Cdd:TIGR00458 361 LHDLLVERIKAKGLNPEGFKDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFPRDRK 424
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
7-463 |
5.76e-42 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 156.41 E-value: 5.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 7 TKIVDLLKRTDiGAMVNVKGWVRTRRGSKQVNFIALND-GSTInnlQIVV--DLANFDEEMLKLITTGACIS-VNGEMVE 82
Cdd:PLN02850 70 TDVSDLGEELA-GSEVLIRGRVHTIRGKGKSAFLVLRQsGFTV---QCVVfvSEVTVSKGMVKYAKQLSRESvVDVEGVV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 83 SV------GSGQKVEVQAREIEVLGTCDNTYPLQ---------KKGHSMEFLREIAH-----------LRPRTNTFGAVF 136
Cdd:PLN02850 146 SVpkkpvkGTTQQVEIQVRKIYCVSKALATLPFNvedaarsesEIEKALQTGEQLVRvgqdtrlnnrvLDLRTPANQAIF 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 137 RIRHNMAIAIHKFFHEKGFFYFHTPIITASDCEGAGQMFQVttmnlydlkkdergsisyedDFFGKQASLTVSGQLEGEL 216
Cdd:PLN02850 226 RIQSQVCNLFREFLLSKGFVEIHTPKLIAGASEGGSAVFRL--------------------DYKGQPACLAQSPQLHKQM 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 217 AATA-LGAIYTFGPTFRAENSNTPRHLAEFWMIEPEVAFND-ITDNMDLAEEFIKYCVKWALDNCADDVKFLNDMFDkgl 294
Cdd:PLN02850 286 AICGdFRRVFEIGPVFRAEDSFTHRHLCEFTGLDLEMEIKEhYSEVLDVVDELFVAIFDGLNERCKKELEAIREQYP--- 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 295 IERLQgvLKDDFVRLPYTDGIKILEEAvakghkfefpvywGV------DLASEHERFL---VEEHFKRPV-ILTDYPKEI 364
Cdd:PLN02850 363 FEPLK--YLPKTLRLTFAEGIQMLKEA-------------GVevdplgDLNTESERKLgqlVKEKYGTDFyILHRYPLAV 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 365 KAFY-MKQNEDGKTVRAMDVlFPKIGEIIGGSEREADYNKLMTRIEEMHIPMKDMWWYLDTRKFGTCPHSGFGLGFERLL 443
Cdd:PLN02850 428 RPFYtMPCPDDPKYSNSFDV-FIRGEEIISGAQRVHDPELLEKRAEECGIDVKTISTYIDSFRYGAPPHGGFGVGLERVV 506
|
490 500
....*....|....*....|
gi 490425014 444 LFVTGMANIRDVIPFPRTPR 463
Cdd:PLN02850 507 MLFCGLNNIRKTSLFPRDPQ 526
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
22-102 |
2.38e-35 |
|
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: 126.14 E-value: 2.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 22 VNVKGWVRTRRGSKQVNFIALNDGSTINNLQIVVDLANFDEEMLKLITTGACISVNGEMVESVGSGQKVEVQAREIEVLG 101
Cdd:cd04318 2 VTVNGWVRSVRDSKKISFIELNDGSCLKNLQVVVDKELTNFKEILKLSTGSSIRVEGVLVKSPGAKQPFELQAEKIEVLG 81
|
.
gi 490425014 102 T 102
Cdd:cd04318 82 E 82
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
7-463 |
1.85e-33 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 132.81 E-value: 1.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 7 TKIVDLLKRTDIGAMVNVKGWVRTRRGSKQVNFIALNDGStiNNLQIVVDLA-NFDEEMLKLITTGACISV--------N 77
Cdd:PTZ00401 66 IPVAVLSKPELVDKTVLIRARVSTTRKKGKMAFMVLRDGS--DSVQAMAAVEgDVPKEMIDFIGQIPTESIvdveatvcK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 78 GEMVESVGSGQKVEVQAREIEVLGTCDNTYPL---------QKKGHSMEFLREIAH--LRPRTNTFGAVFRIRHNMAIAI 146
Cdd:PTZ00401 144 VEQPITSTSHSDIELKVKKIHTVTESLRTLPFtledasrkeSDEGAKVNFDTRLNSrwMDLRTPASGAIFRLQSRVCQYF 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 147 HKFFHEKGFFYFHTPIITASDCEGAGQMFQVttmnlydlkkdergsisyedDFFGKQASLTVSGQLEGELAATA-LGAIY 225
Cdd:PTZ00401 224 RQFLIDSDFCEIHSPKIINAPSEGGANVFKL--------------------EYFNRFAYLAQSPQLYKQMVLQGdVPRVF 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 226 TFGPTFRAENSNTPRHLAEFWMIEPEVAFND-ITDNMDLAEEFIKYcvkwALDNCADDVKFLNDM-----FD----KGLI 295
Cdd:PTZ00401 284 EVGPVFRSENSNTHRHLTEFVGLDVEMRINEhYYEVLDLAESLFNY----IFERLATHTKELKAVcqqypFEplvwKLTP 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 296 ERLQ----GVLKDD-----------------FVRLPYTDGIK----ILEEAVAKGHkfefpvywgvDLASEHERF---LV 347
Cdd:PTZ00401 360 ERMKelgvGVISEGveptdkyqarvhnmdsrMLRINYMHCIEllntVLEEKMAPTD----------DINTTNEKLlgkLV 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 348 EEHFKRPVILTD-YPKEIKAFY-MKQNEDGKTVRAMDvLFPKIGEIIGGSEREADYNKLMTRIEEMHI---PMKDmwwYL 422
Cdd:PTZ00401 430 KERYGTDFFISDrFPSSARPFYtMECKDDERFTNSYD-MFIRGEEISSGAQRIHDPDLLLARAKMLNVdltPIKE---YV 505
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 490425014 423 DTRKFGTCPHSGFGLGFERLLLFVTGMANIRDVIPFPRTPR 463
Cdd:PTZ00401 506 DSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFPRDPQ 546
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
136-463 |
5.47e-32 |
|
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of class II aminoacyl-tRNA synthetases of the subgroup containing aspartyl, lysyl, and asparaginyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. Nearly all class II tRNA synthetases are dimers and enzymes in this subgroup are homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.
Pssm-ID: 238358 [Multi-domain] Cd Length: 269 Bit Score: 122.97 E-value: 5.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 136 FRIRHNMAIAIHKFFHEKGFFYFHTPIITASDCEGAGQMFQVTTMNLydlkkdergsisyeddffGKQASLTVSGQLEGE 215
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNAL------------------GLDYYLRISPQLFKK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 216 -LAATALGAIYTFGPTFRAEnSNTPRHLAEFWMIEPEVAFNDITDNMDLAEEFIKYCVKWALDNCADDVKFLNDMFDKgl 294
Cdd:cd00669 63 rLMVGGLDRVFEINRNFRNE-DLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYGFELEDFGL-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 295 ierlqgvlkdDFVRLPYTDGIKILeeavakghkfefpvywgvdlaseherflveehfKRPVILTDYPKEIKAFY-MKQNE 373
Cdd:cd00669 140 ----------PFPRLTYREALERY---------------------------------GQPLFLTDYPAEMHSPLaSPHDV 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 374 DGKTVRAMDvLFPKIGEIIGGSEREADYNKLMTRIEEMHI----PMKDMWWYLDTRKFGTCPHSGFGLGFERLLLFVTGM 449
Cdd:cd00669 177 NPEIADAFD-LFINGVEVGNGSSRLHDPDIQAEVFQEQGInkeaGMEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNS 255
|
330
....*....|....
gi 490425014 450 ANIRDVIPFPRTPR 463
Cdd:cd00669 256 PTIREVIAFPKMRR 269
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
22-102 |
3.18e-18 |
|
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. Class 2b aaRSs include the homodimeric aspartyl-, asparaginyl-, and lysyl-tRNA synthetases (AspRS, AsnRS, and LysRS). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Included in this group are archeal and archeal-like AspRSs which are non-discriminating and can charge both tRNAAsp and tRNAAsn. E. coli cells have two isoforms of LysRSs (LysS and LysU) encoded by two distinct genes, which are differentially regulated. The cytoplasmic and the mitochondrial isoforms of human LysRS are encoded by a single gene. Yeast cytoplasmic and mitochondrial LysRSs participate in mitochondrial import of cytoplasmic tRNAlysCUU. In addition to their housekeeping role, human LysRS may function as a signaling molecule that activates immune cells. Tomato LysRS may participate in a process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging. AsnRS is immunodominant antigen of the filarial nematode Brugia malayai and is of interest as a target for anti-parasitic drug design. Human AsnRS has been shown to be a pro-inflammatory chemokine which interacts with CCR3 chemokine receptors on T cells, immature dendritic cells and macrophages.
Pssm-ID: 239766 [Multi-domain] Cd Length: 85 Bit Score: 79.15 E-value: 3.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 22 VNVKGWVRTRRGSKQVNFIALNDGSTInnLQIVVDLANFDE--EMLKLITTGACISVNGEMVES---VGSGQKVEVQARE 96
Cdd:cd04100 2 VTLAGWVHSRRDHGGLIFIDLRDGSGI--VQVVVNKEELGEffEEAEKLRTESVVGVTGTVVKRpegNLATGEIELQAEE 79
|
....*.
gi 490425014 97 IEVLGT 102
Cdd:cd04100 80 LEVLSK 85
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
136-461 |
3.17e-17 |
|
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. AspRS is a homodimer, which attaches a specific amino acid to the 3' OH group of ribose of the appropriate tRNA. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. AspRS in this family differ from those found in the AsxRS family by a GAD insert in the core domain.
Pssm-ID: 238400 [Multi-domain] Cd Length: 280 Bit Score: 81.47 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 136 FRIRHNMAIAIHKFFHEKGFFYFHTPIITASDCEGAgQMFQVTtmnlydlkkdergSISYEDDFFgkqaSLTVSGQLEGE 215
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTPEGA-RDFLVP-------------SRLHPGKFY----ALPQSPQLFKQ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 216 -LAATALGAIYTFGPTFRAENSNTPRHlAEFWMIEPEVAFNDITDNMDLAEEFIKYCVKwaldncaddvkflndmfdkgl 294
Cdd:cd00777 63 lLMVSGFDRYFQIARCFRDEDLRADRQ-PEFTQIDIEMSFVDQEDIMSLIEGLLKYVFK--------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 295 iERLQGVLKDDFVRLPYtdgikilEEAVAK-GHKF----EFPVYwgvDLASEHERFLVEEH-FKRPV-----ILTDYPKE 363
Cdd:cd00777 121 -EVLGVELTTPFPRMTY-------AEAMERyGFKFlwivDFPLF---EWDEEEGRLVSAHHpFTAPKeedldLLEKDPED 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 364 IKAfymkqnedgktvRAMDVLFPKIgEIIGGSEREADYnKLMTRI--------EEMHipmKDMWWYLDTRKFGTCPHSGF 435
Cdd:cd00777 190 ARA------------QAYDLVLNGV-ELGGGSIRIHDP-DIQEKVfeilglseEEAE---EKFGFLLEAFKYGAPPHGGI 252
|
330 340
....*....|....*....|....*.
gi 490425014 436 GLGFERLLLFVTGMANIRDVIPFPRT 461
Cdd:cd00777 253 ALGLDRLVMLLTGSESIRDVIAFPKT 278
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
224-459 |
6.67e-14 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 73.58 E-value: 6.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 224 IYTFGPTFRAENSNTpRHLAEFWMIEPEVAFNDITDNMDLAEEFIKYCVKWALDNcaDDVKFLNDMFDkglierlqgvLK 303
Cdd:PRK00484 243 VYEIGRNFRNEGIDT-RHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGT--TKVTYQGTEID----------FG 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 304 DDFVRLPYTDGIK----------ILEEA--VAKGHKFEFPVYWG----VDLASEHerfLVEEHFKRPVILTDYPKEIK-- 365
Cdd:PRK00484 310 PPFKRLTMVDAIKeytgvdfddmTDEEAraLAKELGIEVEKSWGlgklINELFEE---FVEPKLIQPTFITDYPVEISpl 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 366 AfymKQNED--GKTVRAmdvlfpkigE-IIGGSEREADYNKL------MTRIEE------------MHIpmkDmWWYLDT 424
Cdd:PRK00484 387 A---KRHREdpGLTERF---------ElFIGGREIANAFSELndpidqRERFEAqveakeagddeaMFM---D-EDFLRA 450
|
250 260 270
....*....|....*....|....*....|....*
gi 490425014 425 RKFGTCPHSGFGLGFERLLLFVTGMANIRDVIPFP 459
Cdd:PRK00484 451 LEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
13-171 |
3.77e-13 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 71.64 E-value: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 13 LKRTDIGAMVNVKGWVRTRRGSKQVNFIALNDGSTInnLQIVVDLanfDEEMLKLITT-GA--CISVNGEmVESVGSGQ- 88
Cdd:PRK00476 11 LRESHVGQTVTLCGWVHRRRDHGGLIFIDLRDREGI--VQVVFDP---DAEAFEVAESlRSeyVIQVTGT-VRARPEGTv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 89 -------KVEVQAREIEVLGTCDnTYPLQKKGHS-------MEF----LReiahlRPR-TNTfgavFRIRHNMAIAIHKF 149
Cdd:PRK00476 85 npnlptgEIEVLASELEVLNKSK-TLPFPIDDEEdvseelrLKYryldLR-----RPEmQKN----LKLRSKVTSAIRNF 154
|
170 180
....*....|....*....|..
gi 490425014 150 FHEKGFFYFHTPIITASDCEGA 171
Cdd:PRK00476 155 LDDNGFLEIETPILTKSTPEGA 176
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
224-459 |
1.15e-12 |
|
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: 68.77 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 224 IYTFGPTFRAENSNTpRHLAEFWMIEPEVAFNDITDNMDLAEEFIKYCVKWALDNcaDDVKFLNDMFD-------KGLIE 296
Cdd:cd00775 79 VYEIGRNFRNEGIDL-THNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGK--TKIEYGGKELDftppfkrVTMVD 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 297 RLQGVLKDDFvrlPYTDGIKILEEA----VAKGHKFEFPVYWGVDLASEHERFlVEEHFKRPVILTDYPKEIKAFYMKQN 372
Cdd:cd00775 156 ALKEKTGIDF---PELDLEQPEELAkllaKLIKEKIEKPRTLGKLLDKLFEEF-VEPTLIQPTFIIDHPVEISPLAKRHR 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 373 ED-GKTVRAMdvLFPKIGEIIGGSEREADYNKLMTRIEEmHIPMKDM---------WWYLDTRKFGTCPHSGFGLGFERL 442
Cdd:cd00775 232 SNpGLTERFE--LFICGKEIANAYTELNDPFDQRERFEE-QAKQKEAgddeammmdEDFVTALEYGMPPTGGLGIGIDRL 308
|
250
....*....|....*..
gi 490425014 443 LLFVTGMANIRDVIPFP 459
Cdd:cd00775 309 VMLLTDSNSIRDVILFP 325
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
13-171 |
4.59e-12 |
|
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: 68.10 E-value: 4.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 13 LKRTDIGAMVNVKGWVRTRR--GSkqVNFIALNDGSTInnLQIVVDlANFDEEMLKLITT-GA--CISVNGEmVESVGSG 87
Cdd:COG0173 10 LRESDVGQEVTLSGWVHRRRdhGG--LIFIDLRDRYGI--TQVVFD-PDDSAEAFEKAEKlRSeyVIAVTGK-VRARPEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 88 QK--------VEVQAREIEVLGTCDnTYPLQKKGHSM--EFLReiahLR-----PRTNTFGAVFRIRHNMAIAIHKFFHE 152
Cdd:COG0173 84 TVnpklptgeIEVLASELEILNKAK-TPPFQIDDDTDvsEELR----LKyryldLRRPEMQKNLILRHKVTKAIRNYLDE 158
|
170
....*....|....*....
gi 490425014 153 KGFFYFHTPIITASDCEGA 171
Cdd:COG0173 159 NGFLEIETPILTKSTPEGA 177
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
22-459 |
1.41e-10 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 63.16 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 22 VNVKGWVRTRRGSKQVNFIALNDGStiNNLQIVVDLANFDE----EMLKLITTGACISVNGEMVESvgSGQKVEVQAREI 97
Cdd:PRK12445 68 VSVAGRMMTRRIMGKASFVTLQDVG--GRIQLYVARDSLPEgvynDQFKKWDLGDIIGARGTLFKT--QTGELSIHCTEL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 98 EVLGTCdnTYPLQKKGHSME---------FLREIAHLRPRTNtfgavFRIRHNMAIAIHKFFHEKGFFYFHTPIITASDC 168
Cdd:PRK12445 144 RLLTKA--LRPLPDKFHGLQdqevryrqrYLDLIANDKSRQT-----FVVRSKILAAIRQFMVARGFMEVETPMMQVIPG 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 169 EGAGQMFqVTTMNLYDLkkdergsisyedDFFgkqasLTVSGQLE-GELAATALGAIYTFGPTFRAENSNTpRHLAEFWM 247
Cdd:PRK12445 217 GASARPF-ITHHNALDL------------DMY-----LRIAPELYlKRLVVGGFERVFEINRNFRNEGISV-RHNPEFTM 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 248 IEPEVAFNDITDNMDLAEEFIKYCVKWALDNCadDVKFLNDMFDKGL-IERL---QGVLK----DDFVRLPYTDGIKILE 319
Cdd:PRK12445 278 MELYMAYADYHDLIELTESLFRTLAQEVLGTT--KVTYGEHVFDFGKpFEKLtmrEAIKKyrpeTDMADLDNFDAAKALA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 320 EAVAkghkFEFPVYWGVD-LASEHERFLVEEHFKRPVILTDYPKEIKAFyMKQNEDGKTVRAMDVLFPKIGEIIGGSERE 398
Cdd:PRK12445 356 ESIG----ITVEKSWGLGrIVTEIFDEVAEAHLIQPTFITEYPAEVSPL-ARRNDVNPEITDRFEFFIGGREIGNGFSEL 430
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 399 ADYNKLMTRIEEmHIPMK------DMWW---YLDTRKFGTCPHSGFGLGFERLLLFVTGMANIRDVIPFP 459
Cdd:PRK12445 431 NDAEDQAERFQE-QVNAKaagddeAMFYdedYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
19-459 |
1.31e-09 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 60.39 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 19 GAMVNVKGWVRTRRGSKQVNFIAL-NDGSTInnlQIVVDLANFDE-----EMLK-LITTGACISVNGemveSVGSGQKVE 91
Cdd:PLN02502 108 DVSVSVAGRIMAKRAFGKLAFYDLrDDGGKI---QLYADKKRLDLdeeefEKLHsLVDRGDIVGVTG----TPGKTKKGE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 92 --VQAREIEVLGTCDNTYPLQKKG-------HSMEFLREIAHLRPRTntfgaVFRIRHNMAIAIHKFFHEKGFFYFHTPI 162
Cdd:PLN02502 181 lsIFPTSFEVLTKCLLMLPDKYHGltdqetrYRQRYLDLIANPEVRD-----IFRTRAKIISYIRRFLDDRGFLEVETPM 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 163 ITASDCEGAGQMFqVTTMNlyDLKKDERGSISYEddFFGKQasLTVSGqlegelaataLGAIYTFGPTFRAENSNTpRHL 242
Cdd:PLN02502 256 LNMIAGGAAARPF-VTHHN--DLNMDLYLRIATE--LHLKR--LVVGG----------FERVYEIGRQFRNEGIST-RHN 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 243 AEFWMIEPEVAFNDITDNMDLAEEFIKYCVK-----WALDNCADDVKF--------LNDMFDKGLIERLQGVLKDDFVRL 309
Cdd:PLN02502 318 PEFTTCEFYQAYADYNDMMELTEEMVSGMVKeltgsYKIKYHGIEIDFtppfrrisMISLVEEATGIDFPADLKSDEANA 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 310 PYTDGIKILEEAVAK----GHKfefpvywgVDLASEHerfLVEEHFKRPVILTDYPKEI----KAFYMKQnedGKTVRAM 381
Cdd:PLN02502 398 YLIAACEKFDVKCPPpqttGRL--------LNELFEE---FLEETLVQPTFVLDHPVEMsplaKPHRSKP---GLTERFE 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 382 dvLFpkigeiIGGSEREADYNKL------MTRIEEM---HIPMKDMWWYLDTR-----KFGTCPHSGFGLGFERLLLFVT 447
Cdd:PLN02502 464 --LF------INGRELANAFSELtdpvdqRERFEEQvkqHNAGDDEAMALDEDfctalEYGLPPTGGWGLGIDRLVMLLT 535
|
490
....*....|..
gi 490425014 448 GMANIRDVIPFP 459
Cdd:PLN02502 536 DSASIRDVIAFP 547
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
22-100 |
3.49e-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: 53.01 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 22 VNVKGWV-RTRRGSKQVNFIALNDGSTInnLQIVVDLANFdEEMLKLITTGACISVNGEMVESvgSGQKVEVQAREIEVL 100
Cdd:pfam01336 1 VTVAGRVtSIRRSGGKLLFLTLRDGTGS--IQVVVFKEEA-EKLAKKLKEGDVVRVTGKVKKR--KGGELELVVEEIELL 75
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
6-105 |
4.17e-07 |
|
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: 49.06 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 6 RTKIVDLLKRTDIGAMVNVKGWVRTRRGSKQVNFIALNDGSTInnLQIVVDLANFDE-EMLKLITTGACISVNGEmVESV 84
Cdd:cd04317 1 RTHYCGELRESHVGQEVTLCGWVQRRRDHGGLIFIDLRDRYGI--VQVVFDPEEAPEfELAEKLRNESVIQVTGK-VRAR 77
|
90 100
....*....|....*....|....*....
gi 490425014 85 GSGQK--------VEVQAREIEVLGTCDN 105
Cdd:cd04317 78 PEGTVnpklptgeIEVVASELEVLNKAKT 106
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
6-269 |
4.55e-07 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 52.48 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 6 RTKIVDLLKRTDIGAMVNVKGWVRTRRGSKQVNFIALNDGSTInnLQIVVDLANFDE--EMLKLITTGACISVNGEM--- 80
Cdd:PLN02903 59 RSHLCGALSVNDVGSRVTLCGWVDLHRDMGGLTFLDVRDHTGI--VQVVTLPDEFPEahRTANRLRNEYVVAVEGTVrsr 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 81 -VESVG----SGQkVEVQAREIEVLGTCDNTYPL-------QKKGHSMEFLREIAHLRPRTNTFGAVFRIRHNMAIAIHK 148
Cdd:PLN02903 137 pQESPNkkmkTGS-VEVVAESVDILNVVTKSLPFlvttadeQKDSIKEEVRLRYRVLDLRRPQMNANLRLRHRVVKLIRR 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 149 FFHEK-GFFYFHTPIITASDCEGAGQMF---QVTTMNLYDLKKDERgsisyeddFFgKQAsLTVSGqlegelaataLGAI 224
Cdd:PLN02903 216 YLEDVhGFVEIETPILSRSTPEGARDYLvpsRVQPGTFYALPQSPQ--------LF-KQM-LMVSG----------FDRY 275
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 490425014 225 YTFGPTFRAENSNTPRHlAEFWMIEPEVAFNDITDNMDLAEEFIK 269
Cdd:PLN02903 276 YQIARCFRDEDLRADRQ-PEFTQLDMELAFTPLEDMLKLNEDLIR 319
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
137-459 |
4.61e-06 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 49.26 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 137 RIRHNMAIAIHKFFHEKGFFYFHTPIITASdCEGAGQMFQVTTMNLYDLkkdergsisyedDFFgkqasLTVSGQLE-GE 215
Cdd:PTZ00385 234 KKRHVMLQALRDYFNERNFVEVETPVLHTV-ASGANAKSFVTHHNANAM------------DLF-----LRVAPELHlKQ 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 216 LAATALGAIYTFGPTFRAENSNTpRHLAEFWMIEPEVAFNDITDNMDLAEEFIKYC---------VKWALDNCADDVKFL 286
Cdd:PTZ00385 296 CIVGGMERIYEIGKVFRNEDADR-SHNPEFTSCEFYAAYHTYEDLMPMTEDIFRQLamrvngttvVQIYPENAHGNPVTV 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 287 N--------DMFDKglIERLQGVLKDDFVRLPYTDGIKILEeAVAKGHKFEFP-VYWGVDLASEHERFLVEEHFKRPVIL 357
Cdd:PTZ00385 375 DlgkpfrrvSVYDE--IQRMSGVEFPPPNELNTPKGIAYMS-VVMLRYNIPLPpVRTAAKMFEKLIDFFITDRVVEPTFV 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 358 TDYPkeikaFYMKQNEDGKTVRamdvlfPKIGE----IIGGSEREADYNKLMTRIEEMH----------------IPMKD 417
Cdd:PTZ00385 452 MDHP-----LFMSPLAKEQVSR------PGLAErfelFVNGIEYCNAYSELNDPHEQYHrfqqqlvdrqggdeeaMPLDE 520
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 490425014 418 MwwYLDTRKFGTCPHSGFGLGFERLLLFVTGMANIRDVIPFP 459
Cdd:PTZ00385 521 T--FLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFP 560
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
138-265 |
6.67e-06 |
|
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: 47.11 E-value: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 138 IRHNMAIAIHKFFHEKGFFYFHTPIIT-ASDCEGAGQMFQVTtmnlyDLKKDERgsisyEDDFFGKQASLTVSGQLEGEL 216
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVErEPLLEKAGHEPKDL-----LPVGAEN-----EEDLYLRPTLEPGLVRLFVSH 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 490425014 217 AATALGAIYTFGPTFRAENSNT-PRHLAEFWMIEPEVAFNDITDNMDLAE 265
Cdd:cd00768 71 IRKLPLRLAEIGPAFRNEGGRRgLRRVREFTQLEGEVFGEDGEEASEFEE 120
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
19-459 |
1.28e-05 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 48.04 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 19 GAMVNVKGWVRTRRGSKQVNFIALNDGSTinNLQIVVDLANFDEEML----KLITTGACISVNGEMVESvGSGqKVEVQA 94
Cdd:PRK02983 651 GEEVSVSGRVLRIRDYGGVLFADLRDWSG--ELQVLLDASRLEQGSLadfrAAVDLGDLVEVTGTMGTS-RNG-TLSLLV 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 95 REIEVLGTCDNTYPLQKKGhsmeFLREIAHLRPR-----TNTFG-AVFRIRHNMAIAIHKFFHEKGFFYFHTPIITASDC 168
Cdd:PRK02983 727 TSWRLAGKCLRPLPDKWKG----LTDPEARVRQRyldlaVNPEArDLLRARSAVVRAVRETLVARGFLEVETPILQQVHG 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 169 EGAGQMFqVTTMNLYDLKKDERgsISYEddFFGKQasLTVSGqlegelaataLGAIYTFGPTFRAENSNtPRHLAEFWMI 248
Cdd:PRK02983 803 GANARPF-VTHINAYDMDLYLR--IAPE--LYLKR--LCVGG----------VERVFELGRNFRNEGVD-ATHNPEFTLL 864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 249 EPEVAFNDITDNMDLAEEFIKycvkwaldNCADDVkflndmFDKGLIERLQGVLKDDFVRL------------------- 309
Cdd:PRK02983 865 EAYQAHADYDTMRDLTRELIQ--------NAAQAA------HGAPVVMRPDGDGVLEPVDIsgpwpvvtvhdavsealge 930
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 310 ---PYTDgikiLEE--AVAKGHKFEFPVYWGV-DLASE-HERfLVEEHFKRPVILTDYPKEIKAFYMKQNEDgktvramd 382
Cdd:PRK02983 931 eidPDTP----LAElrKLCDAAGIPYRTDWDAgAVVLElYEH-LVEDRTTFPTFYTDFPTSVSPLTRPHRSD-------- 997
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 383 vlfPKIGE----IIGGSEREADYNKLMTRIEE------------------MHIPmKDmwwYLDTRKFGTCPHSGFGLGFE 440
Cdd:PRK02983 998 ---PGLAErwdlVAWGVELGTAYSELTDPVEQrrrlteqsllaaggdpeaMELD-ED---FLQALEYAMPPTGGLGMGVD 1070
|
490
....*....|....*....
gi 490425014 441 RLLLFVTGmANIRDVIPFP 459
Cdd:PRK02983 1071 RLVMLLTG-RSIRETLPFP 1088
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
22-101 |
2.01e-05 |
|
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: 42.99 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 22 VNVKGWVRTRRGSKQVNFIALNDGSTInnLQIVV--DLANFDEEMLKLiTTGACISVNGEMVESVGSGQK---VEVQARE 96
Cdd:cd04323 2 VKVFGWVHRLRSQKKLMFLVLRDGTGF--LQCVLskKLVTEFYDAKSL-TQESSVEVTGEVKEDPRAKQApggYELQVDY 78
|
....*
gi 490425014 97 IEVLG 101
Cdd:cd04323 79 LEIIG 83
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
13-171 |
3.76e-05 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 46.13 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 13 LKRTDIGAMVNVKGWVRTRRGSKQVNFIALNDGSTInnLQIVVDLANFDEEMLKL---ITTGACISVNGEMVESVGSGQ- 88
Cdd:PRK12820 12 LSLDDTGREVCLAGWVDAFRDHGELLFIHLRDRNGF--IQAVFSPEAAPADVYELaasLRAEFCVALQGEVQKRLEETEn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490425014 89 ------KVEVQAREIEVLGTCDN-TYPLQKKG-----------HSMEFLR-EIAHLRPRTNTFGAVFRIRHNMAIAIHKF 149
Cdd:PRK12820 90 phietgDIEVFVRELSILAASEAlPFAISDKAmtagagsagadAVNEDLRlQYRYLDIRRPAMQDHLAKRHRIIKCARDF 169
|
170 180
....*....|....*....|..
gi 490425014 150 FHEKGFFYFHTPIITASDCEGA 171
Cdd:PRK12820 170 LDSRGFLEIETPILTKSTPEGA 191
|
|
| |
