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Conserved domains on  [gi|71984122|ref|NP_001021405|]
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Asparagine--tRNA ligase, cytoplasmic [Caenorhabditis elegans]

Protein Classification

asparagine--tRNA ligase( domain architecture ID 10137780)

asparagine--tRNA ligase catalyzes the attachment of asparagine to tRNA(Asn)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AsxRS_core cd00776
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ...
 220-541 1.77e-159

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: 457.03  E-value: 1.77e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 220 AGVDVMLDNRHLVIRGENASRILRIRAAATRAMRDHFFAAGYTEVAPPTLVQTQVEGGSTLFGLDYYGEPAYLTQSSQLY 299
Cdd:cd00776   2 ANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQLY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 300 LETCNAALGDVYCISQSYRAEKSRTRRHLSEYQHVEAECAFI-TFDQLMDRIEALVCDTVDRLLADPVTK-SLIEFVNPG 377
Cdd:cd00776  82 KEMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAKElELVNQLNRE 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 378 YKAPARPFKRMPYKEAIEWLQKNDVRNEMgekfVYGEDIAEAAERRMTDTI-GVPILLNRFPHGIKAFYMPRCADDNELT 456
Cdd:cd00776 162 LLKPLEPFPRITYDEAIELLREKGVEEEV----KWGEDLSTEHERLLGEIVkGDPVFVTDYPKEIKPFYMKPDDDNPETV 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 457 ESVDLLMPGVGEIVGGSMRIWKEDQLLAAFEKGGLDSKNYYWYMDQRKYGSVPHGGYGLGLERFICWLTDTNHIRDVCLY 536
Cdd:cd00776 238 ESFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILF 317


                ....*
gi 71984122 537 PRFVG 541
Cdd:cd00776 318 PRDPK 322
AsnRS_cyto_like_N cd04323
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ...
 123-206 2.13e-39

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: 138.14  E-value: 2.13e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 123 RVSIKAWVHRLRRQGKsLMFLVLRDGYGFLQCVLNDKLCQ-SYDAVTLSTETSVQVYGIIKALPDGKSAPDGHELTVDYW 201
Cdd:cd04323   1 RVKVFGWVHRLRSQKK-LMFLVLRDGTGFLQCVLSKKLVTeFYDAKSLTQESSVEVTGEVKEDPRAKQAPGGYELQVDYL 79


                ....*
gi 71984122 202 EVIGK 206
Cdd:cd04323  80 EIIGE 84
 
Name Accession Description Interval E-value
AsxRS_core cd00776
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ...
 220-541 1.77e-159

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: 457.03  E-value: 1.77e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 220 AGVDVMLDNRHLVIRGENASRILRIRAAATRAMRDHFFAAGYTEVAPPTLVQTQVEGGSTLFGLDYYGEPAYLTQSSQLY 299
Cdd:cd00776   2 ANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQLY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 300 LETCNAALGDVYCISQSYRAEKSRTRRHLSEYQHVEAECAFI-TFDQLMDRIEALVCDTVDRLLADPVTK-SLIEFVNPG 377
Cdd:cd00776  82 KEMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAKElELVNQLNRE 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 378 YKAPARPFKRMPYKEAIEWLQKNDVRNEMgekfVYGEDIAEAAERRMTDTI-GVPILLNRFPHGIKAFYMPRCADDNELT 456
Cdd:cd00776 162 LLKPLEPFPRITYDEAIELLREKGVEEEV----KWGEDLSTEHERLLGEIVkGDPVFVTDYPKEIKPFYMKPDDDNPETV 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 457 ESVDLLMPGVGEIVGGSMRIWKEDQLLAAFEKGGLDSKNYYWYMDQRKYGSVPHGGYGLGLERFICWLTDTNHIRDVCLY 536
Cdd:cd00776 238 ESFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILF 317


                ....*
gi 71984122 537 PRFVG 541
Cdd:cd00776 318 PRDPK 322
AsnS COG0017
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 118-545 4.18e-151

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: 439.87  E-value: 4.18e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 118 QHRDQRVSIKAWVHRLRRQGKsLMFLVLRDGYGFLQCVLNDKLCQSYDAVT-LSTETSVQVYGIIKALPDgksAPDGHEL 196
Cdd:COG0017  11 EHVGQEVTVAGWVRTKRDSGG-ISFLILRDGSGFIQVVVKKDKLENFEEAKkLTTESSVEVTGTVVESPR---APQGVEL 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 197 TVDYWEVIGKA----PaggIDNVlneSAGVDVMLDNRHLVIRGENASRILRIRAAATRAMRDHFFAAGYTEVAPPTLVQT 272
Cdd:COG0017  87 QAEEIEVLGEAdepyP---LQPK---RHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVEVHTPIITAS 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 273 QVEGGSTLFGLDYYGEPAYLTQSSQLYLETCNAALGDVYCISQSYRAEKSRTRRHLSEYQHVEAECAFITFDQLMDRIEA 352
Cdd:COG0017 161 ATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMALEKVYTFGPTFRAEKSNTRRHLAEFWMIEPEMAFADLEDVMDLAEE 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 353 LVCDTVDRLL--ADPVTKSLIEFVNPGYKAPARPFKRMPYKEAIEWLQKNdvrnemGEKFVYGEDIAEAAERRMTDTIG- 429
Cdd:COG0017 241 MLKYIIKYVLenCPEELEFLGRDVERLEKVPESPFPRITYTEAIEILKKS------GEKVEWGDDLGTEHERYLGEEFFk 314

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 430 VPILLNRFPHGIKAFYMPRCADDNELTESVDLLMPGVGEIVGGSMRIWKEDQLLAAFEKGGLDSKNYYWYMDQRKYGSVP 509
Cdd:COG0017 315 KPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAPGIGEIIGGSQREHRYDVLVERIKEKGLDPEDYEWYLDLRRYGSVP 394

                       410       420       430
                ....*....|....*....|....*....|....*.
gi 71984122 510 HGGYGLGLERFICWLTDTNHIRDVCLYPRFVGRCAP 545
Cdd:COG0017 395 HAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
asnS TIGR00457
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ...
 118-545 3.09e-139

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: 410.62  E-value: 3.09e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122   118 QHRDQRVSIKAWVHRLRRQGKsLMFLVLRDG--YGFLQCVLNDKLCQSY--DAVTLSTETSVQVYGIIKALPdgkSAPDG 193
Cdd:TIGR00457  13 KFVGDEVTVSGWVRTKRSSKK-IIFLELNDGssLGPIQAVINGEDNPYLfqLLKSLTTGSSVSVTGKVVESP---GKGQP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122   194 HELTVDYWEVIGKAPAGGIDNVLNESaGVDVMLDNRHLVIRGENASRILRIRAAATRAMRDHFFAAGYTEVAPPTLVQTQ 273
Cdd:TIGR00457  89 VELQVKKIEVVGEAEPDDYPLQKKEH-SLEFLRDIAHLRLRTNTLGAVMRVRNALSQAIHRYFQENGFTWVSPPILTSND 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122   274 VEGGSTLFGL---------DYYGEPAYLTQSSQLYLETCNAALGDVYCISQSYRAEKSRTRRHLSEYQHVEAECAFITFD 344
Cdd:TIGR00457 168 CEGAGELFRVstgnidfsqDFFGKEAYLTVSGQLYLETYALALSKVYTFGPTFRAEKSNTSRHLSEFWMIEPEMAFANLN 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122   345 QLMDRIEALVCDTVDRLLADpvTKSLIEFVNPGYKAPARP---------FKRMPYKEAIEWLQKNDVRNEMGEKFvyGED 415
Cdd:TIGR00457 248 DLLQLAETLIKYIIKAVLEN--CSQELKFLEKNFDKDLIKrleniinnkFARITYTDAIEILKESDKNFEYEDFW--GDD 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122   416 IAEAAERRMTDTIGV-PILLNRFPHGIKAFYMPRCaDDNELTESVDLLMPGVGEIVGGSMRIWKEDQLLAAFEKGGLDSK 494
Cdd:TIGR00457 324 LQTEHERFLAEEYFKpPVFVTNYPKDIKAFYMKLN-DDGKTVAAMDLLAPGIGEIIGGSEREDDLDKLENRMKEMGLDTD 402

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 71984122   495 NYYWYMDQRKYGSVPHGGYGLGLERFICWLTDTNHIRDVCLYPRFVGRCAP 545
Cdd:TIGR00457 403 ALNWYLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGNINF 453
asnC PRK03932
asparaginyl-tRNA synthetase; Validated
 118-545 4.77e-122

asparaginyl-tRNA synthetase; Validated


Pssm-ID: 235176 [Multi-domain]  Cd Length: 450  Bit Score: 366.36  E-value: 4.77e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  118 QHRDQRVSIKAWVHRLRRQGKsLMFLVLRDGYGF--LQCVLNDKLCQSYDAVTLSTETSVQVYGIIKALPDgksAPDGHE 195
Cdd:PRK03932  13 KYVGQEVTVRGWVRTKRDSGK-IAFLQLRDGSCFkqLQVVKDNGEEYFEEIKKLTTGSSVIVTGTVVESPR---AGQGYE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  196 LTVDYWEVIGKAPaggidnvlnES-------AGVDVMLDNRHLVIRGENASRILRIRAAATRAMRDHFFAAGYTEVAPPT 268
Cdd:PRK03932  89 LQATKIEVIGEDP---------EDypiqkkrHSIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVDTPI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  269 LVQTQVEGGSTLF---------GLDYYGEPAYLTQSSQLYLETCNAALGDVYCISQSYRAEKSRTRRHLSEYQHVEAECA 339
Cdd:PRK03932 160 ITASDCEGAGELFrvttldldfSKDFFGKEAYLTVSGQLYAEAYAMALGKVYTFGPTFRAENSNTRRHLAEFWMIEPEMA 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  340 FITFDQLMDRIEALVCDTVDR----------LLADPVTKSLIE----FVNPgykaparPFKRMPYKEAIEWLQKNDVRNE 405
Cdd:PRK03932 240 FADLEDNMDLAEEMLKYVVKYvlencpddleFLNRRVDKGDIErlenFIES-------PFPRITYTEAIEILQKSGKKFE 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  406 mgEKFVYGEDIAEAAERRMTDTI-GVPILLNRFPHGIKAFYMpRCADDNELTESVDLLMPGVGEIVGGSMRIWKEDQLLA 484
Cdd:PRK03932 313 --FPVEWGDDLGSEHERYLAEEHfKKPVFVTNYPKDIKAFYM-RLNPDGKTVAAMDLLAPGIGEIIGGSQREERLDVLEA 389

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71984122  485 AFEKGGLDSKNYYWYMDQRKYGSVPHGGYGLGLERFICWLTDTNHIRDVCLYPRFVGRCAP 545
Cdd:PRK03932 390 RIKELGLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
tRNA-synt_2 pfam00152
tRNA synthetases class II (D, K and N);
221-538 1.10e-91

tRNA synthetases class II (D, K and N);


Pssm-ID: 425487 [Multi-domain]  Cd Length: 318  Bit Score: 283.69  E-value: 1.10e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122   221 GVDVMLDNRHLVIRGENASRILRIRAAATRAMRDHFFAAGYTEVAPPTLVQTQVEGGSTLFGL------DYYgepaYLTQ 294
Cdd:pfam00152   1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVpsralgKFY----ALPQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122   295 SSQLYLETCNAA-LGDVYCISQSYRAEKSRTRRHLsEYQHVEAECAFITFDQLMDRIEALVCDTVDRlladpVTKSLIEF 373
Cdd:pfam00152  77 SPQLYKQLLMVAgFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVDYEDVMDLTEELIKEIFKE-----VEGIAKEL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122   374 VNPGYKAPARPFKRMPYKEAIEWLQKNDVrnemgekFVYGEDIAEAAERRMTD-----TIGVPILLNRFPHGIKAFYMPR 448
Cdd:pfam00152 151 EGGTLLDLKKPFPRITYAEAIEKLNGKDV-------EELGYGSDKPDLRFLLElvidkNKFNPLWVTDFPAEHHPFTMPK 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122   449 CADDNELTESVDLLMPGVgEIVGGSMRIWKEDQLLAAFEKGGLD----SKNYYWYMDQRKYGSVPHGGYGLGLERFICWL 524
Cdd:pfam00152 224 DEDDPALAEAFDLVLNGV-EIGGGSIRIHDPELQEERFEEQGLDpeeaEEKFGFYLDALKYGAPPHGGLGIGLDRLVMLL 302

                         330
                  ....*....|....
gi 71984122   525 TDTNHIRDVCLYPR 538
Cdd:pfam00152 303 TGLESIREVIAFPK 316
AsnRS_cyto_like_N cd04323
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ...
 123-206 2.13e-39

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: 138.14  E-value: 2.13e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 123 RVSIKAWVHRLRRQGKsLMFLVLRDGYGFLQCVLNDKLCQ-SYDAVTLSTETSVQVYGIIKALPDGKSAPDGHELTVDYW 201
Cdd:cd04323   1 RVKVFGWVHRLRSQKK-LMFLVLRDGTGFLQCVLSKKLVTeFYDAKSLTQESSVEVTGEVKEDPRAKQAPGGYELQVDYL 79


                ....*
gi 71984122 202 EVIGK 206
Cdd:cd04323  80 EIIGE 84
tRNA_anti-codon pfam01336
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ...
 124-204 9.89e-15

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: 69.19  E-value: 9.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122   124 VSIKAWVHRLRRQGKSLMFLVLRDGYGFLQCVLNDKlCQSYDAVTLSTETSVQVYGIIKalpdgKSAPDGHELTVDYWEV 203
Cdd:pfam01336   1 VTVAGRVTSIRRSGGKLLFLTLRDGTGSIQVVVFKE-EAEKLAKKLKEGDVVRVTGKVK-----KRKGGELELVVEEIEL 74


                  .
gi 71984122   204 I 204
Cdd:pfam01336  75 L 75
 
Name Accession Description Interval E-value
AsxRS_core cd00776
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ...
 220-541 1.77e-159

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: 457.03  E-value: 1.77e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 220 AGVDVMLDNRHLVIRGENASRILRIRAAATRAMRDHFFAAGYTEVAPPTLVQTQVEGGSTLFGLDYYGEPAYLTQSSQLY 299
Cdd:cd00776   2 ANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQLY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 300 LETCNAALGDVYCISQSYRAEKSRTRRHLSEYQHVEAECAFI-TFDQLMDRIEALVCDTVDRLLADPVTK-SLIEFVNPG 377
Cdd:cd00776  82 KEMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAKElELVNQLNRE 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 378 YKAPARPFKRMPYKEAIEWLQKNDVRNEMgekfVYGEDIAEAAERRMTDTI-GVPILLNRFPHGIKAFYMPRCADDNELT 456
Cdd:cd00776 162 LLKPLEPFPRITYDEAIELLREKGVEEEV----KWGEDLSTEHERLLGEIVkGDPVFVTDYPKEIKPFYMKPDDDNPETV 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 457 ESVDLLMPGVGEIVGGSMRIWKEDQLLAAFEKGGLDSKNYYWYMDQRKYGSVPHGGYGLGLERFICWLTDTNHIRDVCLY 536
Cdd:cd00776 238 ESFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILF 317


                ....*
gi 71984122 537 PRFVG 541
Cdd:cd00776 318 PRDPK 322
AsnS COG0017
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 118-545 4.18e-151

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: 439.87  E-value: 4.18e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 118 QHRDQRVSIKAWVHRLRRQGKsLMFLVLRDGYGFLQCVLNDKLCQSYDAVT-LSTETSVQVYGIIKALPDgksAPDGHEL 196
Cdd:COG0017  11 EHVGQEVTVAGWVRTKRDSGG-ISFLILRDGSGFIQVVVKKDKLENFEEAKkLTTESSVEVTGTVVESPR---APQGVEL 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 197 TVDYWEVIGKA----PaggIDNVlneSAGVDVMLDNRHLVIRGENASRILRIRAAATRAMRDHFFAAGYTEVAPPTLVQT 272
Cdd:COG0017  87 QAEEIEVLGEAdepyP---LQPK---RHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVEVHTPIITAS 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 273 QVEGGSTLFGLDYYGEPAYLTQSSQLYLETCNAALGDVYCISQSYRAEKSRTRRHLSEYQHVEAECAFITFDQLMDRIEA 352
Cdd:COG0017 161 ATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMALEKVYTFGPTFRAEKSNTRRHLAEFWMIEPEMAFADLEDVMDLAEE 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 353 LVCDTVDRLL--ADPVTKSLIEFVNPGYKAPARPFKRMPYKEAIEWLQKNdvrnemGEKFVYGEDIAEAAERRMTDTIG- 429
Cdd:COG0017 241 MLKYIIKYVLenCPEELEFLGRDVERLEKVPESPFPRITYTEAIEILKKS------GEKVEWGDDLGTEHERYLGEEFFk 314

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 430 VPILLNRFPHGIKAFYMPRCADDNELTESVDLLMPGVGEIVGGSMRIWKEDQLLAAFEKGGLDSKNYYWYMDQRKYGSVP 509
Cdd:COG0017 315 KPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAPGIGEIIGGSQREHRYDVLVERIKEKGLDPEDYEWYLDLRRYGSVP 394

                       410       420       430
                ....*....|....*....|....*....|....*.
gi 71984122 510 HGGYGLGLERFICWLTDTNHIRDVCLYPRFVGRCAP 545
Cdd:COG0017 395 HAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
asnS TIGR00457
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ...
 118-545 3.09e-139

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: 410.62  E-value: 3.09e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122   118 QHRDQRVSIKAWVHRLRRQGKsLMFLVLRDG--YGFLQCVLNDKLCQSY--DAVTLSTETSVQVYGIIKALPdgkSAPDG 193
Cdd:TIGR00457  13 KFVGDEVTVSGWVRTKRSSKK-IIFLELNDGssLGPIQAVINGEDNPYLfqLLKSLTTGSSVSVTGKVVESP---GKGQP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122   194 HELTVDYWEVIGKAPAGGIDNVLNESaGVDVMLDNRHLVIRGENASRILRIRAAATRAMRDHFFAAGYTEVAPPTLVQTQ 273
Cdd:TIGR00457  89 VELQVKKIEVVGEAEPDDYPLQKKEH-SLEFLRDIAHLRLRTNTLGAVMRVRNALSQAIHRYFQENGFTWVSPPILTSND 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122   274 VEGGSTLFGL---------DYYGEPAYLTQSSQLYLETCNAALGDVYCISQSYRAEKSRTRRHLSEYQHVEAECAFITFD 344
Cdd:TIGR00457 168 CEGAGELFRVstgnidfsqDFFGKEAYLTVSGQLYLETYALALSKVYTFGPTFRAEKSNTSRHLSEFWMIEPEMAFANLN 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122   345 QLMDRIEALVCDTVDRLLADpvTKSLIEFVNPGYKAPARP---------FKRMPYKEAIEWLQKNDVRNEMGEKFvyGED 415
Cdd:TIGR00457 248 DLLQLAETLIKYIIKAVLEN--CSQELKFLEKNFDKDLIKrleniinnkFARITYTDAIEILKESDKNFEYEDFW--GDD 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122   416 IAEAAERRMTDTIGV-PILLNRFPHGIKAFYMPRCaDDNELTESVDLLMPGVGEIVGGSMRIWKEDQLLAAFEKGGLDSK 494
Cdd:TIGR00457 324 LQTEHERFLAEEYFKpPVFVTNYPKDIKAFYMKLN-DDGKTVAAMDLLAPGIGEIIGGSEREDDLDKLENRMKEMGLDTD 402

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 71984122   495 NYYWYMDQRKYGSVPHGGYGLGLERFICWLTDTNHIRDVCLYPRFVGRCAP 545
Cdd:TIGR00457 403 ALNWYLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGNINF 453
asnC PRK03932
asparaginyl-tRNA synthetase; Validated
 118-545 4.77e-122

asparaginyl-tRNA synthetase; Validated


Pssm-ID: 235176 [Multi-domain]  Cd Length: 450  Bit Score: 366.36  E-value: 4.77e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  118 QHRDQRVSIKAWVHRLRRQGKsLMFLVLRDGYGF--LQCVLNDKLCQSYDAVTLSTETSVQVYGIIKALPDgksAPDGHE 195
Cdd:PRK03932  13 KYVGQEVTVRGWVRTKRDSGK-IAFLQLRDGSCFkqLQVVKDNGEEYFEEIKKLTTGSSVIVTGTVVESPR---AGQGYE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  196 LTVDYWEVIGKAPaggidnvlnES-------AGVDVMLDNRHLVIRGENASRILRIRAAATRAMRDHFFAAGYTEVAPPT 268
Cdd:PRK03932  89 LQATKIEVIGEDP---------EDypiqkkrHSIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVDTPI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  269 LVQTQVEGGSTLF---------GLDYYGEPAYLTQSSQLYLETCNAALGDVYCISQSYRAEKSRTRRHLSEYQHVEAECA 339
Cdd:PRK03932 160 ITASDCEGAGELFrvttldldfSKDFFGKEAYLTVSGQLYAEAYAMALGKVYTFGPTFRAENSNTRRHLAEFWMIEPEMA 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  340 FITFDQLMDRIEALVCDTVDR----------LLADPVTKSLIE----FVNPgykaparPFKRMPYKEAIEWLQKNDVRNE 405
Cdd:PRK03932 240 FADLEDNMDLAEEMLKYVVKYvlencpddleFLNRRVDKGDIErlenFIES-------PFPRITYTEAIEILQKSGKKFE 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  406 mgEKFVYGEDIAEAAERRMTDTI-GVPILLNRFPHGIKAFYMpRCADDNELTESVDLLMPGVGEIVGGSMRIWKEDQLLA 484
Cdd:PRK03932 313 --FPVEWGDDLGSEHERYLAEEHfKKPVFVTNYPKDIKAFYM-RLNPDGKTVAAMDLLAPGIGEIIGGSQREERLDVLEA 389

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71984122  485 AFEKGGLDSKNYYWYMDQRKYGSVPHGGYGLGLERFICWLTDTNHIRDVCLYPRFVGRCAP 545
Cdd:PRK03932 390 RIKELGLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
aspC PRK05159
aspartyl-tRNA synthetase; Provisional
 122-538 1.81e-99

aspartyl-tRNA synthetase; Provisional


Pssm-ID: 235354 [Multi-domain]  Cd Length: 437  Bit Score: 307.89  E-value: 1.81e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  122 QRVSIKAWVHRLRRQGKsLMFLVLRDGYGFLQCVL-NDKLCQSYDAV-TLSTETSVQVYGIIKALPdgkSAPDGHELTVD 199
Cdd:PRK05159  17 EEVTLAGWVHEIRDLGG-IAFLILRDRSGIIQVVVkKKVDEELFETIkKLKRESVVSVTGTVKANP---KAPGGVEVIPE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  200 YWEVIGKA-------PAGGIDNVLnesagvDVMLDNRHLVIRGENASRILRIRAAATRAMRDHFFAAGYTEVAPPTLVQT 272
Cdd:PRK05159  93 EIEVLNKAeeplpldISGKVLAEL------DTRLDNRFLDLRRPRVRAIFKIRSEVLRAFREFLYENGFTEIFTPKIVAS 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  273 QVEGGSTLFGLDYYGEPAYLTQSSQLYLETCNAALGD-VYCISQSYRAEKSRTRRHLSEYQHVEAECAFITFDQ-LMDRI 350
Cdd:PRK05159 167 GTEGGAELFPIDYFEKEAYLAQSPQLYKQMMVGAGFErVFEIGPVFRAEEHNTSRHLNEYTSIDVEMGFIDDHEdVMDLL 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  351 EALVCDTVDRLLADpVTKSLiEFVNPGYKAPARPFKRMPYKEAIEWLqkndvrNEMGEKFVYGEDIAEAAER----RMTD 426
Cdd:PRK05159 247 ENLLRYMYEDVAEN-CEKEL-ELLGIELPVPETPIPRITYDEAIEIL------KSKGNEISWGDDLDTEGERllgeYVKE 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  427 TIGVPIL-LNRFPHGIKAFYMPRCADDNELTESVDLLMPGVgEIVGGSMRIWKEDQLLAAFEKGGLDSKNYYWYMDQRKY 505
Cdd:PRK05159 319 EYGSDFYfITDYPSEKRPFYTMPDEDDPEISKSFDLLFRGL-EITSGGQRIHRYDMLVESIKEKGLNPESFEFYLEAFKY 397

                        410       420       430
                 ....*....|....*....|....*....|...
gi 71984122  506 GSVPHGGYGLGLERFICWLTDTNHIRDVCLYPR 538
Cdd:PRK05159 398 GMPPHGGFGLGLERLTMKLLGLENIREAVLFPR 430
tRNA-synt_2 pfam00152
tRNA synthetases class II (D, K and N);
221-538 1.10e-91

tRNA synthetases class II (D, K and N);


Pssm-ID: 425487 [Multi-domain]  Cd Length: 318  Bit Score: 283.69  E-value: 1.10e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122   221 GVDVMLDNRHLVIRGENASRILRIRAAATRAMRDHFFAAGYTEVAPPTLVQTQVEGGSTLFGL------DYYgepaYLTQ 294
Cdd:pfam00152   1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVpsralgKFY----ALPQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122   295 SSQLYLETCNAA-LGDVYCISQSYRAEKSRTRRHLsEYQHVEAECAFITFDQLMDRIEALVCDTVDRlladpVTKSLIEF 373
Cdd:pfam00152  77 SPQLYKQLLMVAgFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVDYEDVMDLTEELIKEIFKE-----VEGIAKEL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122   374 VNPGYKAPARPFKRMPYKEAIEWLQKNDVrnemgekFVYGEDIAEAAERRMTD-----TIGVPILLNRFPHGIKAFYMPR 448
Cdd:pfam00152 151 EGGTLLDLKKPFPRITYAEAIEKLNGKDV-------EELGYGSDKPDLRFLLElvidkNKFNPLWVTDFPAEHHPFTMPK 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122   449 CADDNELTESVDLLMPGVgEIVGGSMRIWKEDQLLAAFEKGGLD----SKNYYWYMDQRKYGSVPHGGYGLGLERFICWL 524
Cdd:pfam00152 224 DEDDPALAEAFDLVLNGV-EIGGGSIRIHDPELQEERFEEQGLDpeeaEEKFGFYLDALKYGAPPHGGLGIGLDRLVMLL 302

                         330
                  ....*....|....
gi 71984122   525 TDTNHIRDVCLYPR 538
Cdd:pfam00152 303 TGLESIREVIAFPK 316
PLN02603 PLN02603
asparaginyl-tRNA synthetase
 80-541 6.00e-61

asparaginyl-tRNA synthetase


Pssm-ID: 178213 [Multi-domain]  Cd Length: 565  Bit Score: 210.60  E-value: 6.00e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122   80 EKEAEEAQHAALEEAKKITFSLDKSLPEAKVIKIGESVqhrdqrvSIKAWVHRLRRQgKSLMFLVLRDGYGF--LQCVLN 157
Cdd:PLN02603  73 EAAKGAFGEAVGEFRKKLRIADVKGGEDEGLARVGKTL-------NVMGWVRTLRAQ-SSVTFIEVNDGSCLsnMQCVMT 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  158 DKlCQSYDAV---TLSTETSVQVYGIIKALPDGKSAPdghELTVDYWEVIGKA-PAGGIDNvlnESAGVDVMLDNRHLVI 233
Cdd:PLN02603 145 PD-AEGYDQVesgLITTGASVLVQGTVVSSQGGKQKV---ELKVSKIVVVGKSdPSYPIQK---KRVSREFLRTKAHLRP 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  234 RGENASRILRIRAAATRAMRDHFFAAGYTEVAPPTLVQTQVEGGSTLF-------------------------GL----- 283
Cdd:PLN02603 218 RTNTFGAVARVRNALAYATHKFFQENGFVWVSSPIITASDCEGAGEQFcvttlipnsaenggslvddipktkdGLidwsq 297

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  284 DYYGEPAYLTQSSQLYLETCNAALGDVYCISQSYRAEKSRTRRHLSEYQHVEAECAFITFDQLMDRIEALVCDTVDRLLA 363
Cdd:PLN02603 298 DFFGKPAFLTVSGQLNGETYATALSDVYTFGPTFRAENSNTSRHLAEFWMIEPELAFADLNDDMACATAYLQYVVKYILE 377

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  364 DpvTKSLIEFVNPGYK---------APARPFKRMPYKEAIEWLQKNDVRNEMGEKfvYGEDIAEAAERRMTDTI--GVPI 432
Cdd:PLN02603 378 N--CKEDMEFFNTWIEkgiidrlsdVVEKNFVQLSYTDAIELLLKAKKKFEFPVK--WGLDLQSEHERYITEEAfgGRPV 453

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  433 LLNRFPHGIKAFYMpRCADDNELTESVDLLMPGVGEIVGGSMRIWKEDQLLAAFEKGGLDSKNYYWYMDQRKYGSVPHGG 512
Cdd:PLN02603 454 IIRDYPKEIKAFYM-RENDDGKTVAAMDMLVPRVGELIGGSQREERLEYLEARLDELKLNKESYWWYLDLRRYGSVPHAG 532

                        490       500
                 ....*....|....*....|....*....
gi 71984122  513 YGLGLERFICWLTDTNHIRDVCLYPRFVG 541
Cdd:PLN02603 533 FGLGFERLVQFATGIDNIRDAIPFPRVPG 561
PLN02221 PLN02221
asparaginyl-tRNA synthetase
 122-542 2.21e-58

asparaginyl-tRNA synthetase


Pssm-ID: 177867 [Multi-domain]  Cd Length: 572  Bit Score: 203.69  E-value: 2.21e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  122 QRVSIKAWVHRLRRQGK-SLMFLVLRDGY--GFLQCVLNDKLcqsYDAVTL-STETSVQVYGIIKALPDGKSAPDGHELT 197
Cdd:PLN02221  51 QKVRIGGWVKTGREQGKgTFAFLEVNDGScpANLQVMVDSSL---YDLSTLvATGTCVTVDGVLKVPPEGKGTKQKIELS 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  198 VDywEVIGKAPAGGIDNVLNESA-GVDVMLDNRHLVIRGENASRILRIRAAATRAMRDHFFAAGYTEVAPPTLVQTQVEG 276
Cdd:PLN02221 128 VE--KVIDVGTVDPTKYPLPKTKlTLEFLRDVLHLRSRTNSISAVARIRNALAFATHSFFQEHSFLYIHTPIITTSDCEG 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  277 GSTLF--------------------------------------------------------------------------- 281
Cdd:PLN02221 206 AGEMFqvttlinyterleqdlidnpppteadveaarlivkergevvaqlkaakaskeeitaavaelkiakeslahieers 285

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  282 ----GL-----------DYYGEPAYLTQSSQLYLETCNAALGDVYCISQSYRAEKSRTRRHLSEYQHVEAECAFITFDQL 346
Cdd:PLN02221 286 klkpGLpkkdgkidyskDFFGRQAFLTVSGQLQVETYACALSSVYTFGPTFRAENSHTSRHLAEFWMVEPEIAFADLEDD 365

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  347 MDRIEALV----------CDTVDRLLADPVTKSLIEFVNPGYKAParpFKRMPYKEAIEWLQKNDVRNEMGEKFV-YGED 415
Cdd:PLN02221 366 MNCAEAYVkymckwlldkCFDDMELMAKNFDSGCIDRLRMVASTP---FGRITYTEAIELLEEAVAKGKEFDNNVeWGID 442

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  416 IAEAAERRMTDTI-GVPILLNRFPHGIKAFYMpRCADDNELTESVDLLMPGVGEIVGGSMRIWKEDQLLAAFEKGGLDSK 494
Cdd:PLN02221 443 LASEHERYLTEVLfQKPLIVYNYPKGIKAFYM-RLNDDEKTVAAMDVLVPKVGELIGGSQREERYDVIKQRIEEMGLPIE 521

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*...
gi 71984122  495 NYYWYMDQRKYGSVPHGGYGLGLERFICWLTDTNHIRDVCLYPRFVGR 542
Cdd:PLN02221 522 PYEWYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPRYPGK 569
PLN02850 PLN02850
aspartate-tRNA ligase
 69-545 3.25e-49

aspartate-tRNA ligase


Pssm-ID: 215456 [Multi-domain]  Cd Length: 530  Bit Score: 177.98  E-value: 3.25e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122   69 EVKKLEKAgcREKEAEEAQHAALEEAKK--------ITFSLDKSLPEAKV-IKIGESV-QHRDQRVSIKAWVHRLRRQGK 138
Cdd:PLN02850  21 AAAKAEKL--RREATAKAAAASLEDEDDplasnygdVPLEELQSKVTGREwTDVSDLGeELAGSEVLIRGRVHTIRGKGK 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  139 SLmFLVLRDGYGFLQCVLN-DKLCQSYDAV----TLSTETSVQVYGIIKaLPDG--KSAPDGHELTVDYWEVIGKA---- 207
Cdd:PLN02850  99 SA-FLVLRQSGFTVQCVVFvSEVTVSKGMVkyakQLSRESVVDVEGVVS-VPKKpvKGTTQQVEIQVRKIYCVSKAlatl 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  208 ---------PAGGIDNVLNESA-----GVDVMLDNRHLVIRGENASRILRIRAAATRAMRDHFFAAGYTEVAPPTLVQTQ 273
Cdd:PLN02850 177 pfnvedaarSESEIEKALQTGEqlvrvGQDTRLNNRVLDLRTPANQAIFRIQSQVCNLFREFLLSKGFVEIHTPKLIAGA 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  274 VEGGSTLFGLDYYGEPAYLTQSSQLYLETcnAALGD---VYCISQSYRAEKSRTRRHLseyqhveaeCAFITFDQLMDRI 350
Cdd:PLN02850 257 SEGGSAVFRLDYKGQPACLAQSPQLHKQM--AICGDfrrVFEIGPVFRAEDSFTHRHL---------CEFTGLDLEMEIK 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  351 EAL--VCDTVDRL-------LADPVTKSLiEFVNPGYkaPARPFK------RMPYKEAIEWLQkndvrnEMGEKFVYGED 415
Cdd:PLN02850 326 EHYseVLDVVDELfvaifdgLNERCKKEL-EAIREQY--PFEPLKylpktlRLTFAEGIQMLK------EAGVEVDPLGD 396

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  416 IAEAAERRM---------TDTigvpILLNRFPHGIKAFY-MPrCADDNELTESVDLLMPGvGEIVGGSMRIWKEDQLLAA 485
Cdd:PLN02850 397 LNTESERKLgqlvkekygTDF----YILHRYPLAVRPFYtMP-CPDDPKYSNSFDVFIRG-EEIISGAQRVHDPELLEKR 470

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  486 FEKGGLDSKNYYWYMDQRKYGSVPHGGYGLGLERFICWLTDTNHIRDVCLYPRFVGRCAP 545
Cdd:PLN02850 471 AEECGIDVKTISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPRDPQRLAP 530
PRK06462 PRK06462
asparagine synthetase A; Reviewed
 233-545 1.84e-48

asparagine synthetase A; Reviewed


Pssm-ID: 235808 [Multi-domain]  Cd Length: 335  Bit Score: 170.97  E-value: 1.84e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  233 IRGENASRILRIRAAATRAMRDHFFAAGYTEVAPPTLvqTQV-----EGGSTL----FGLDYYGEPAYLTQSSQLYLETC 303
Cdd:PRK06462  21 ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPII--SPStdplmGLGSDLpvkqISIDFYGVEYYLADSMILHKQLA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  304 NAALGDVYCISQSYRAE--KSRTRRHLSEYQHVEAECAFITFDQLMDRIEALVCDTVDRLLAdpVTKSLIEFVNPGYKAP 381
Cdd:PRK06462  99 LRMLGKIFYLSPNFRLEpvDKDTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLE--EHEDELEFFGRDLPHL 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  382 ARPFKRMPYKEAIEWLQKNDVRNEmgEKFVYGEDiaeaAERRMTDTIGVPILLNRFPHGIKAFYmprcadDNELTES--- 458
Cdd:PRK06462 177 KRPFKRITHKEAVEILNEEGCRGI--DLEELGSE----GEKSLSEHFEEPFWIIDIPKGSREFY------DREDPERpgv 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  459 ---VDLLMP-GVGEIVGGSMRIWKEDQLLAAFEKGGLDSKNYYWYMDQRKYGSVPHGGYGLGLERFICWLTDTNHIRDVC 534
Cdd:PRK06462 245 lrnYDLLLPeGYGEAVSGGEREYEYEEIVERIREHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQ 324

                        330
                 ....*....|.
gi 71984122  535 LYPRFVGRCAP 545
Cdd:PRK06462 325 PFPRVPGIVAL 335
PTZ00425 PTZ00425
asparagine-tRNA ligase; Provisional
 284-541 6.04e-41

asparagine-tRNA ligase; Provisional


Pssm-ID: 240414 [Multi-domain]  Cd Length: 586  Bit Score: 155.95  E-value: 6.04e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  284 DYYGEPAYLTQSSQLYLETCNAALGDVYCISQSYRAEKSRTRRHLSEYQHVEAECAFITFDQLMDRIEALVCDTVDRLLA 363
Cdd:PTZ00425 320 DFFSKQAFLTVSGQLSLENLCSSMGDVYTFGPTFRAENSHTSRHLAEFWMIEPEIAFADLYDNMELAESYIKYCIGYVLN 399

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  364 D----------PVTKSLIEFVNpgyKAPARPFKRMPYKEAIEWLQKNDVRNEMGEKfvYGEDIAEAAERRMTDTI-GVPI 432
Cdd:PTZ00425 400 NnfddiyyfeeNVETGLISRLK---NILDEDFAKITYTNVIDLLQPYSDSFEVPVK--WGMDLQSEHERFVAEQIfKKPV 474

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  433 LLNRFPHGIKAFYMpRCADDNELTESVDLLMPGVGEIVGGSMRIWKEDQLLAAFEKGGLDSKNYYWYMDQRKYGSVPHGG 512
Cdd:PTZ00425 475 IVYNYPKDLKAFYM-KLNEDQKTVAAMDVLVPKIGEVIGGSQREDNLERLDKMIKEKKLNMESYWWYRQLRKFGSHPHAG 553

                        250       260
                 ....*....|....*....|....*....
gi 71984122  513 YGLGLERFICWLTDTNHIRDVCLYPRFVG 541
Cdd:PTZ00425 554 FGLGFERLIMLVTGVDNIKDTIPFPRYPG 582
AsnRS_cyto_like_N cd04323
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ...
 123-206 2.13e-39

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: 138.14  E-value: 2.13e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 123 RVSIKAWVHRLRRQGKsLMFLVLRDGYGFLQCVLNDKLCQ-SYDAVTLSTETSVQVYGIIKALPDGKSAPDGHELTVDYW 201
Cdd:cd04323   1 RVKVFGWVHRLRSQKK-LMFLVLRDGTGFLQCVLSKKLVTeFYDAKSLTQESSVEVTGEVKEDPRAKQAPGGYELQVDYL 79


                ....*
gi 71984122 202 EVIGK 206
Cdd:cd04323  80 EIIGE 84
PTZ00401 PTZ00401
aspartyl-tRNA synthetase; Provisional
 67-545 5.49e-37

aspartyl-tRNA synthetase; Provisional


Pssm-ID: 173592 [Multi-domain]  Cd Length: 550  Bit Score: 143.98  E-value: 5.49e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122   67 EAEVKKLEKAGCREKEAEEAQHAALEEAKkiTFSLDKSLPEAKVIKigesVQHRDQRVSIKAWVHRLRRQGKsLMFLVLR 146
Cdd:PTZ00401  30 EEKARAAEKAALVEKYKDVFGAAPMVQST--TYKSRTFIPVAVLSK----PELVDKTVLIRARVSTTRKKGK-MAFMVLR 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  147 DGYGFLQC---VLNDKLCQSYDAV-TLSTETSVQVYGII--KALPDGKSAPDGHELTVDYWEVIGKA----PAGGIDNVL 216
Cdd:PTZ00401 103 DGSDSVQAmaaVEGDVPKEMIDFIgQIPTESIVDVEATVckVEQPITSTSHSDIELKVKKIHTVTESlrtlPFTLEDASR 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  217 NES-----AGVDVMLDNRHLVIRGENASRILRIRAAATRAMRDHFFAAGYTEVAPPTLVQTQVEGGSTLFGLDYYGEPAY 291
Cdd:PTZ00401 183 KESdegakVNFDTRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLIDSDFCEIHSPKIINAPSEGGANVFKLEYFNRFAY 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  292 LTQSSQLYLETcnAALGD---VYCISQSYRAEKSRTRRHLSEYQHVEAECAFIT-FDQLMDRIEALVCDTVDRLLA---- 363
Cdd:PTZ00401 263 LAQSPQLYKQM--VLQGDvprVFEVGPVFRSENSNTHRHLTEFVGLDVEMRINEhYYEVLDLAESLFNYIFERLAThtke 340

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  364 ----------DPVTKSLI-------------EFVNPG--YKAPARPFK----RMPYKEAIEWLqkNDVrneMGEKFVYGE 414
Cdd:PTZ00401 341 lkavcqqypfEPLVWKLTpermkelgvgvisEGVEPTdkYQARVHNMDsrmlRINYMHCIELL--NTV---LEEKMAPTD 415

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  415 DIAEAAERRMTDTI----GVPILL-NRFPHGIKAFYMPRCADDNELTESVDLLMPGvGEIVGGSMRIWKEDQLLAAFEKG 489
Cdd:PTZ00401 416 DINTTNEKLLGKLVkeryGTDFFIsDRFPSSARPFYTMECKDDERFTNSYDMFIRG-EEISSGAQRIHDPDLLLARAKML 494

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 71984122  490 GLDSKNYYWYMDQRKYGSVPHGGYGLGLERFICWLTDTNHIRDVCLYPRFVGRCAP 545
Cdd:PTZ00401 495 NVDLTPIKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFPRDPQRTTP 550
Asp_Lys_Asn_RS_core cd00669
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ...
 242-538 1.72e-35

Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of class II aminoacyl-tRNA synthetases of the subgroup containing aspartyl, lysyl, and asparaginyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. Nearly all class II tRNA synthetases are dimers and enzymes in this subgroup are homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.


Pssm-ID: 238358 [Multi-domain]  Cd Length: 269  Bit Score: 133.76  E-value: 1.72e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 242 LRIRAAATRAMRDHFFAAGYTEVAPPTLVQTQVEGGSTLFGLDYY--GEPAYLTQSSQLYLETCNAA-LGDVYCISQSYR 318
Cdd:cd00669   1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNalGLDYYLRISPQLFKKRLMVGgLDRVFEINRNFR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 319 AEKSRTRrHLSEYQHVEAECAFITFDQLMDRIEALVcdtvdRLLADPVTKSLIEFVNPGYKAPARPFKRMPYKEAIEWLq 398
Cdd:cd00669  81 NEDLRAR-HQPEFTMMDLEMAFADYEDVIELTERLV-----RHLAREVLGVTAVTYGFELEDFGLPFPRLTYREALERY- 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 399 kndvrnemgekfvygediaeaaerrmtdtiGVPILLNRFPHGIKAFYMPRCADDNELTESVDLLMPGVgEIVGGSMRIWK 478
Cdd:cd00669 154 ------------------------------GQPLFLTDYPAEMHSPLASPHDVNPEIADAFDLFINGV-EVGNGSSRLHD 202

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71984122 479 EDQLLAAFEKGGLDSKN----YYWYMDQRKYGSVPHGGYGLGLERFICWLTDTNHIRDVCLYPR 538
Cdd:cd00669 203 PDIQAEVFQEQGINKEAgmeyFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPK 266
PLN02532 PLN02532
asparagine-tRNA synthetase
 284-542 2.15e-34

asparagine-tRNA synthetase


Pssm-ID: 215291 [Multi-domain]  Cd Length: 633  Bit Score: 137.69  E-value: 2.15e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  284 DYYGEPAYLTQSSQLYLETCNAALGDVYCISQSYRAEKSRTRRHLSEYQHVEAECAFITFDQLMDRIEALV---CDTV-- 358
Cdd:PLN02532 366 DFFSRPTYLTVSGRLHLESYACALGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAFSELEDAMNCAEDYFkflCKWVle 445

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  359 ---DRL-----LADPVTKSLIEfvnpgyKAPARPFKRMPYKEAIEWLQKNdVRNEMGEKFVYGEDIAEAAERRMTDTI-G 429
Cdd:PLN02532 446 ncsEDMkfvskRIDKTISTRLE------AIISSSLQRISYTEAVDLLKQA-TDKKFETKPEWGIALTTEHLSYLADEIyK 518

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  430 VPILLNRFPHGIKAFYMpRCADDNELTESVDLLMPGVGEIVGGSMRIWKEDQLLAAFEKGGLDSKNYYWYMDQRKYGSVP 509
Cdd:PLN02532 519 KPVIIYNYPKELKPFYV-RLNDDGKTVAAFDLVVPKVGTVITGSQNEERMDILNARIEELGLPREQYEWYLDLRRHGTVK 597

                        250       260       270
                 ....*....|....*....|....*....|...
gi 71984122  510 HGGYGLGLERFICWLTDTNHIRDVCLYPRFVGR 542
Cdd:PLN02532 598 HSGFSLGFELMVLFATGLPDVRDAIPFPRSWGK 630
Asp_Lys_Asn_RS_N cd04100
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ...
 123-206 2.03e-24

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: 96.87  E-value: 2.03e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 123 RVSIKAWVHRLRRQGKsLMFLVLRDGYGFLQCVLNDKLCQS--YDAVTLSTETSVQVYGIIKALPDGKSAPDGHELTVDY 200
Cdd:cd04100   1 EVTLAGWVHSRRDHGG-LIFIDLRDGSGIVQVVVNKEELGEffEEAEKLRTESVVGVTGTVVKRPEGNLATGEIELQAEE 79


                ....*.
gi 71984122 201 WEVIGK 206
Cdd:cd04100  80 LEVLSK 85
AspRS_core cd00777
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ...
 242-537 8.05e-22

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: 95.33  E-value: 8.05e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 242 LRIRAAATRAMRDHFFAAGYTEVAPPTLVQTQVEGGStlfglDYY-------GEPAYLTQSSQLYLETCNAALGDVYC-I 313
Cdd:cd00777   1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTPEGAR-----DFLvpsrlhpGKFYALPQSPQLFKQLLMVSGFDRYFqI 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 314 SQSYRAEKSRTRRHlSEYQHVEAECAFITFDQLMDRIEALVCDTVDRLLADPVTKsliefvnpgykaparPFKRMPYKEA 393
Cdd:cd00777  76 ARCFRDEDLRADRQ-PEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLGVELTT---------------PFPRMTYAEA 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 394 IE-------WLqkNDV----RNEMGEKFVY---------GEDIAeaaerrmtdtigvpiLLNRFPHGIKAfymprcaddn 453
Cdd:cd00777 140 MErygfkflWI--VDFplfeWDEEEGRLVSahhpftapkEEDLD---------------LLEKDPEDARA---------- 192

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 454 eltESVDLLMPGVgEIVGGSMRIWKEDQLLAAFEKGGLDSKNYY----WYMDQRKYGSVPHGGYGLGLERFICWLTDTNH 529
Cdd:cd00777 193 ---QAYDLVLNGV-ELGGGSIRIHDPDIQEKVFEILGLSEEEAEekfgFLLEAFKYGAPPHGGIALGLDRLVMLLTGSES 268


                ....*...
gi 71984122 530 IRDVCLYP 537
Cdd:cd00777 269 IRDVIAFP 276
aspS PRK00476
aspartyl-tRNA synthetase; Validated
 118-406 1.05e-18

aspartyl-tRNA synthetase; Validated


Pssm-ID: 234775 [Multi-domain]  Cd Length: 588  Bit Score: 89.36  E-value: 1.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  118 QHRDQRVSIKAWVHRLRRQGKsLMFLVLRDGYGFLQCVLNDKLCQSYDAVTLSTETSVQVYGIIKALPDGKSAPD---GH 194
Cdd:PRK00476  14 SHVGQTVTLCGWVHRRRDHGG-LIFIDLRDREGIVQVVFDPDAEAFEVAESLRSEYVIQVTGTVRARPEGTVNPNlptGE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  195 -ELTVDYWEVIGKA-----PAGGIDNVlNEsagvDVMLDNRHLVIRGENASRILRIRAAATRAMRDHFFAAGYTEVAPPT 268
Cdd:PRK00476  93 iEVLASELEVLNKSktlpfPIDDEEDV-SE----ELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDDNGFLEIETPI 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  269 LVQTQVEG------------GStlFgldyygepaY-LTQSSQL------------YletcnaalgdvYCISQSYRAEKSR 323
Cdd:PRK00476 168 LTKSTPEGardylvpsrvhpGK--F---------YaLPQSPQLfkqllmvagfdrY-----------YQIARCFRDEDLR 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  324 TRRHLSEYQhVEAECAFITFDQLMDRIEALVCDTVDRLLADPVTKsliefvnpgykaparPFKRMPYKEAIEW--LQKND 401
Cdd:PRK00476 226 ADRQPEFTQ-IDIEMSFVTQEDVMALMEGLIRHVFKEVLGVDLPT---------------PFPRMTYAEAMRRygSDKPD 289


                 ....*
gi 71984122  402 VRNEM 406
Cdd:PRK00476 290 LRFGL 294
PRK12820 PRK12820
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ...
 116-538 2.02e-16

bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional


Pssm-ID: 105955 [Multi-domain]  Cd Length: 706  Bit Score: 82.73  E-value: 2.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  116 SVQHRDQRVSIKAWVHRLRRQGKsLMFLVLRDGYGFLQCVLNDKLCQS--YD-AVTLSTETSVQVYGIIKALPDGKSAPD 192
Cdd:PRK12820  13 SLDDTGREVCLAGWVDAFRDHGE-LLFIHLRDRNGFIQAVFSPEAAPAdvYElAASLRAEFCVALQGEVQKRLEETENPH 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  193 ---------GHELTVDYWEVI------GKAPAGGIDNVLNESAGVDVMLDNRHLVIRGENASRILRIRAAATRAMRDHFF 257
Cdd:PRK12820  92 ietgdievfVRELSILAASEAlpfaisDKAMTAGAGSAGADAVNEDLRLQYRYLDIRRPAMQDHLAKRHRIIKCARDFLD 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  258 AAGYTEVAPPTLVQTQVEGG------STLFGLDYYGEPayltQSSQLYLETCN-AALGDVYCISQSYRAEKSRTRRHlSE 330
Cdd:PRK12820 172 SRGFLEIETPILTKSTPEGArdylvpSRIHPKEFYALP----QSPQLFKQLLMiAGFERYFQLARCFRDEDLRPNRQ-PE 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  331 YQHVEAECAFITFDQLMDRIEALVCdtvdRLLAdpvtksliefvnPGYKAPARPFKRMPYKEAI---------------- 394
Cdd:PRK12820 247 FTQLDIEASFIDEEFIFELIEELTA----RMFA------------IGGIALPRPFPRMPYAEAMdttgsdrpdlrfdlkf 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  395 ----------------------------------EWLQKNDVRNEMGEKFV-------------------------YGED 415
Cdd:PRK12820 311 adatdifentrygifkqilqrggrikginikgqsEKLSKNVLQNEYAKEIApsfgakgmtwmraeaggldsnivqfFSAD 390

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  416 IAEAAERR------------------------------MTDTIGV-------PILLNRFP-------HGIKAFYMPRCAD 451
Cdd:PRK12820 391 EKEALKRRfhaedgdviimiadascaivlsalgqlrlhLADRLGLipegvfhPLWITDFPlfeatddGGVTSSHHPFTAP 470

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  452 DNE-------------LTESVDLLMPGvGEIVGGSMRIWKEDQLLAAFEKGGL---DSKNYY-WYMDQRKYGSVPHGGYG 514
Cdd:PRK12820 471 DREdfdpgdieelldlRSRAYDLVVNG-EELGGGSIRINDKDIQLRIFAALGLseeDIEDKFgFFLRAFDFAAPPHGGIA 549

                        570       580
                 ....*....|....*....|....
gi 71984122  515 LGLERFICWLTDTNHIRDVCLYPR 538
Cdd:PRK12820 550 LGLDRVVSMILQTPSIREVIAFPK 573
PLN02903 PLN02903
aminoacyl-tRNA ligase
 123-544 6.94e-15

aminoacyl-tRNA ligase


Pssm-ID: 215490 [Multi-domain]  Cd Length: 652  Bit Score: 77.52  E-value: 6.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  123 RVSIKAWVHRLRRQGkSLMFLVLRDGYGFLQCV-LNDKLCQSYDAVT-LSTETSVQVYGIIKALPDG---KSAPDGH-EL 196
Cdd:PLN02903  74 RVTLCGWVDLHRDMG-GLTFLDVRDHTGIVQVVtLPDEFPEAHRTANrLRNEYVVAVEGTVRSRPQEspnKKMKTGSvEV 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  197 TVDYWEVIGK---------APAGGIDNVLNEsagvDVMLDNRHLVIRGENASRILRIRAAATRAMRDHFF-AAGYTEVAP 266
Cdd:PLN02903 153 VAESVDILNVvtkslpflvTTADEQKDSIKE----EVRLRYRVLDLRRPQMNANLRLRHRVVKLIRRYLEdVHGFVEIET 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  267 PTLVQTQVEGGstlfgLDYY-------GEPAYLTQSSQLYLETCNAALGD-VYCISQSYRAEKSRTRRHlSEYQHVEAEC 338
Cdd:PLN02903 229 PILSRSTPEGA-----RDYLvpsrvqpGTFYALPQSPQLFKQMLMVSGFDrYYQIARCFRDEDLRADRQ-PEFTQLDMEL 302

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  339 AFITFDQLMDRIEALVCDTVDRLLadpvtksliefvnpGYKAPaRPFKRMPYKEAIE----------------------- 395
Cdd:PLN02903 303 AFTPLEDMLKLNEDLIRQVFKEIK--------------GVQLP-NPFPRLTYAEAMSkygsdkpdlryglelvdvsdvfa 367

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  396 --------------------------------WLQKNDVRNEM--------------------GEKFVYGEDIAEAAERR 423
Cdd:PLN02903 368 essfkvfagalesggvvkaicvpdgkkisnntALKKGDIYNEAiksgakglaflkvlddgeleGIKALVESLSPEQAEQL 447

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  424 MTDTIGVP---ILLNRFPHG-----------------------------IKAFYM-------------------PRCADD 452
Cdd:PLN02903 448 LAACGAGPgdlILFAAGPTSsvnktldrlrqfiaktldlidpsrhsilwVTDFPMfewnedeqrlealhhpftaPNPEDM 527

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  453 NELTE----SVDLLMPGVgEIVGGSMRIWKEDQLLAAFEKGGL---DSKNYYWY-MDQRKYGSVPHGGYGLGLERFICWL 524
Cdd:PLN02903 528 GDLSSaralAYDMVYNGV-EIGGGSLRIYRRDVQQKVLEAIGLspeEAESKFGYlLEALDMGAPPHGGIAYGLDRLVMLL 606

                        570       580
                 ....*....|....*....|.
gi 71984122  525 TDTNHIRDVCLYPRFV-GRCA 544
Cdd:PLN02903 607 AGAKSIRDVIAFPKTTtAQCA 627
tRNA_anti-codon pfam01336
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ...
 124-204 9.89e-15

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: 69.19  E-value: 9.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122   124 VSIKAWVHRLRRQGKSLMFLVLRDGYGFLQCVLNDKlCQSYDAVTLSTETSVQVYGIIKalpdgKSAPDGHELTVDYWEV 203
Cdd:pfam01336   1 VTVAGRVTSIRRSGGKLLFLTLRDGTGSIQVVVFKE-EAEKLAKKLKEGDVVRVTGKVK-----KRKGGELELVVEEIEL 74


                  .
gi 71984122   204 I 204
Cdd:pfam01336  75 L 75
EcAspRS_like_N cd04317
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ...
 113-207 3.74e-14

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: 69.47  E-value: 3.74e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 113 IGE-SVQHRDQRVSIKAWVHRLRRQGKsLMFLVLRDGYGFLQCVLNDKLCQSYD-AVTLSTETSVQVYGIIKALPDGKSA 190
Cdd:cd04317   5 CGElRESHVGQEVTLCGWVQRRRDHGG-LIFIDLRDRYGIVQVVFDPEEAPEFElAEKLRNESVIQVTGKVRARPEGTVN 83

                        90       100
                ....*....|....*....|.
gi 71984122 191 PD---GH-ELTVDYWEVIGKA 207
Cdd:cd04317  84 PKlptGEiEVVASELEVLNKA 104
AspS COG0173
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ...
 118-406 6.98e-14

Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439943 [Multi-domain]  Cd Length: 589  Bit Score: 74.26  E-value: 6.98e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 118 QHRDQRVSIKAWVHRLRRQGkSLMFLVLRDGYGFLQCVLN-DKLCQSYD-AVTLSTETSVQVYGIIKALPDG---KSAPD 192
Cdd:COG0173  13 SDVGQEVTLSGWVHRRRDHG-GLIFIDLRDRYGITQVVFDpDDSAEAFEkAEKLRSEYVIAVTGKVRARPEGtvnPKLPT 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 193 GH-ELTVDYWEVIGKA------PAGGIDNvlNEsagvDVMLDNRHLVIRGENASRILRIRAAATRAMRDHFFAAGYTEVA 265
Cdd:COG0173  92 GEiEVLASELEILNKAktppfqIDDDTDV--SE----ELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDENGFLEIE 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 266 PPTLVQTQVEG------------GStlFgldyygepaY-LTQSSQLY--LetcnaaL---G-DVY-----CisqsYRAEK 321
Cdd:COG0173 166 TPILTKSTPEGardylvpsrvhpGK--F---------YaLPQSPQLFkqL------LmvsGfDRYfqiarC----FRDED 224

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 322 SRTRRHLSEYQhVEAECAFITFDQLMDRIEALVCDTVDRLLadpvtksliefvnpGYKAPaRPFKRMPYKEAIEW--LQK 399
Cdd:COG0173 225 LRADRQPEFTQ-LDIEMSFVDQEDVFELMEGLIRHLFKEVL--------------GVELP-TPFPRMTYAEAMERygSDK 288


                ....*..
gi 71984122 400 NDVRNEM 406
Cdd:COG0173 289 PDLRFGL 295
PhAsnRS_like_N cd04319
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ...
 123-231 4.14e-11

PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus horikoshii AsnRS asparaginyl-tRNA synthetase (AsnRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The archeal enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose.


Pssm-ID: 239814 [Multi-domain]  Cd Length: 103  Bit Score: 59.85  E-value: 4.14e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 123 RVSIKAWVHRLRRQGKSLmFLVLRDGYGFLQCVLNDKLCQSY--DAVTLSTETSVQVYGIIKALPdgkSAPDGHELTVDY 200
Cdd:cd04319   1 KVTLAGWVYRKREVGKKA-FIVLRDSTGIVQAVFSKDLNEEAyrEAKKVGIESSVIVEGAVKADP---RAPGGAEVHGEK 76

                        90       100       110
                ....*....|....*....|....*....|.
gi 71984122 201 WEVIGKAPAGGIdnvlNESAGVDVMLDNRHL 231
Cdd:cd04319  77 LEIIQNVEFFPI----TEDASDEFLLDVRHL 103
AspRS_cyto_N cd04320
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ...
 124-182 4.18e-09

AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces cerevisiae and human cytoplasmic aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis.


Pssm-ID: 239815 [Multi-domain]  Cd Length: 102  Bit Score: 54.11  E-value: 4.18e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71984122 124 VSIKAWVHRLRRQGKSLMFLVLRDGYGFLQCVLN-DKLCQSYDAVT----LSTETSVQVYGIIK 182
Cdd:cd04320   2 VLIRARVHTSRAQGAKLAFLVLRQQGYTIQGVLAaSAEGVSKQMVKwagsLSKESIVDVEGTVK 65
ND_PkAspRS_like_N cd04316
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ...
 122-207 5.30e-09

ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the homodimeric non-discriminating (ND) Pyrococcus kodakaraensis aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. P. kodakaraensis AspRS is a class 2b aaRS. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. P. kodakaraensis ND-AspRS can charge both tRNAAsp and tRNAAsn. Some of the enzymes in this group may be discriminating, based on the presence of homologs of asparaginyl-tRNA synthetase (AsnRS) in their completed genomes.


Pssm-ID: 239811 [Multi-domain]  Cd Length: 108  Bit Score: 53.86  E-value: 5.30e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 122 QRVSIKAWVHRLRRQGKsLMFLVLRDGYGFLQCVLNDKLCQSY---DAVTLSTETSVQVYGIIKALPdgkSAPDGHELTV 198
Cdd:cd04316  13 EEVTVAGWVHEIRDLGG-IKFVILRDREGIVQVTAPKKKVDKElfkTVRKLSRESVISVTGTVKAEP---KAPNGVEIIP 88


                ....*....
gi 71984122 199 DYWEVIGKA 207
Cdd:cd04316  89 EEIEVLSEA 97
PRK12445 PRK12445
lysyl-tRNA synthetase; Reviewed
 223-537 1.60e-07

lysyl-tRNA synthetase; Reviewed


Pssm-ID: 171504 [Multi-domain]  Cd Length: 505  Bit Score: 53.91  E-value: 1.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  223 DVMLDNRHL-VIRGENASRILRIRAAATRAMRDHFFAAGYTEVAPPtLVQTQVEGGSTLFGLDYYGE---PAYLTQSSQL 298
Cdd:PRK12445 164 EVRYRQRYLdLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETP-MMQVIPGGASARPFITHHNAldlDMYLRIAPEL 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  299 YLET-CNAALGDVYCISQSYRAEkSRTRRHLSEYQHVEAECAFITFDQLMDRIEALVCDTVDRLLAD---PVTKSLIEFv 374
Cdd:PRK12445 243 YLKRlVVGGFERVFEINRNFRNE-GISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTtkvTYGEHVFDF- 320

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  375 npgykapARPFKRMPYKEAIewlQKNDVRNEMG--EKFVYGEDIAEAAERRMTDTIGV------------------PILL 434
Cdd:PRK12445 321 -------GKPFEKLTMREAI---KKYRPETDMAdlDNFDAAKALAESIGITVEKSWGLgrivteifdevaeahliqPTFI 390

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122  435 NRFPHGIKAfyMPRCADDN-ELTESVDLLMPGvGEIVGGSMRIWKEDQLLAAFEK------GGLDSKNYY--WYMDQRKY 505
Cdd:PRK12445 391 TEYPAEVSP--LARRNDVNpEITDRFEFFIGG-REIGNGFSELNDAEDQAERFQEqvnakaAGDDEAMFYdeDYVTALEY 467

                        330       340       350
                 ....*....|....*....|....*....|..
gi 71984122  506 GSVPHGGYGLGLERFICWLTDTNHIRDVCLYP 537
Cdd:PRK12445 468 GLPPTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
LysRS_core cd00775
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ...
 236-537 4.94e-07

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: 51.82  E-value: 4.94e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 236 ENASRILRIRAAATRAMRDHFFAAGYTEVAPPTLvqTQVEGGSTL--F-----GLDYygePAYLTQSSQLYLET-CNAAL 307
Cdd:cd00775   2 EEVRQTFIVRSKIISYIRKFLDDRGFLEVETPML--QPIAGGAAArpFithhnALDM---DLYLRIAPELYLKRlIVGGF 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 308 GDVYCISQSYRAEkSRTRRHLSEYQHVEAECAFITFDQLMDRIEALVCDTVDRLLA-DPVT--KSLIEFvnpgykapARP 384
Cdd:cd00775  77 ERVYEIGRNFRNE-GIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGkTKIEygGKELDF--------TPP 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 385 FKRMPYKEAIEWLQKNDVRNEMGEK-FVYGEDIAEAAERRMTDTIGVPILLNR-FPHGIKAFYM-------------P-- 447
Cdd:cd00775 148 FKRVTMVDALKEKTGIDFPELDLEQpEELAKLLAKLIKEKIEKPRTLGKLLDKlFEEFVEPTLIqptfiidhpveisPla 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 448 -RCADDNELTESVDLlmpgvgeIVGGsmriwKE------------DQL------LAAFEKGGLDSKNYYW-YMDQRKYGS 507
Cdd:cd00775 228 kRHRSNPGLTERFEL-------FICG-----KEianaytelndpfDQRerfeeqAKQKEAGDDEAMMMDEdFVTALEYGM 295

                       330       340       350
                ....*....|....*....|....*....|
gi 71984122 508 VPHGGYGLGLERFICWLTDTNHIRDVCLYP 537
Cdd:cd00775 296 PPTGGLGIGIDRLVMLLTDSNSIRDVILFP 325
lysS PRK02983
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
113-354 4.12e-06

bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;


Pssm-ID: 235095 [Multi-domain]  Cd Length: 1094  Bit Score: 49.96  E-value: 4.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122   113 IGESVQHRD-QRVSIKAWVHRLRRQGKsLMFLVLRDGYGFLQCVLNDKLCQSYDAVTLSTETS----VQVYGIIkalpdG 187
Cdd:PRK02983  642 VAEALDAPTgEEVSVSGRVLRIRDYGG-VLFADLRDWSGELQVLLDASRLEQGSLADFRAAVDlgdlVEVTGTM-----G 715

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122   188 KSAPDGHELTVDYWEVIGKA--PaggIDNVLNESAGVDVMLDNRH--LVIRGEnASRILRIRAAATRAMRDHFFAAGYTE 263
Cdd:PRK02983  716 TSRNGTLSLLVTSWRLAGKClrP---LPDKWKGLTDPEARVRQRYldLAVNPE-ARDLLRARSAVVRAVRETLVARGFLE 791

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122   264 VAPPTLvQtQVEGGST----LFGLDYYGEPAYLTQSSQLYLET-CNAALGDVYCISQSYRAEK-SRTrrHLSEYQHVEAE 337
Cdd:PRK02983  792 VETPIL-Q-QVHGGANarpfVTHINAYDMDLYLRIAPELYLKRlCVGGVERVFELGRNFRNEGvDAT--HNPEFTLLEAY 867

                         250
                  ....*....|....*..
gi 71984122   338 CAFITFDQLMDRIEALV 354
Cdd:PRK02983  868 QAHADYDTMRDLTRELI 884
PLN02502 PLN02502
lysyl-tRNA synthetase
 505-537 1.31e-04

lysyl-tRNA synthetase


Pssm-ID: 215278 [Multi-domain]  Cd Length: 553  Bit Score: 44.60  E-value: 1.31e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 71984122  505 YGSVPHGGYGLGLERFICWLTDTNHIRDVCLYP 537
Cdd:PLN02502 515 YGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFP 547
PTZ00417 PTZ00417
lysine-tRNA ligase; Provisional
 504-537 5.68e-04

lysine-tRNA ligase; Provisional


Pssm-ID: 173607 [Multi-domain]  Cd Length: 585  Bit Score: 42.69  E-value: 5.68e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 71984122  504 KYGSVPHGGYGLGLERFICWLTDTNHIRDVCLYP 537
Cdd:PTZ00417 546 EYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFP 579
ScAspRS_mt_like_N cd04321
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ...
 123-199 5.81e-04

ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces cerevisiae mitochondrial (mt) aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this fungal group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Mutations in the gene for S. cerevisiae mtAspRS result in a "petite" phenotype typical for a mutation in a nuclear gene that results in a non-functioning mitochondrial protein synthesis system.


Pssm-ID: 239816 [Multi-domain]  Cd Length: 86  Bit Score: 38.84  E-value: 5.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984122 123 RVSIKAWVHRLRRQGKSLMFLVLRDGYG-FLQCVLNDKlcqsYDAVTL----STETSVQVYGIIKALPDGKSAP-DGHEL 196
Cdd:cd04321   1 KVTLNGWIDRKPRIVKKLSFADLRDPNGdIIQLVSTAK----KDAFSLlksiTAESPVQVRGKLQLKEAKSSEKnDEWEL 76


                ...
gi 71984122 197 TVD 199
Cdd:cd04321  77 VVD 79
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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