|
Name |
Accession |
Description |
Interval |
E-value |
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
225-544 |
1.44e-148 |
|
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: 429.29 E-value: 1.44e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 225 DVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYL 304
Cdd:cd00776 3 NLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQLYK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 305 ETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFL-TFEDLLNRLEDLVCDVVDRVLKSPVASI--VYELNPNF 381
Cdd:cd00776 83 EMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAKELelVNQLNREL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 382 KPPKRPFRRMNYSDAIEWLKEHDVKKEDgtfyEFGDDIPEAPERLMTDTI-NEPILLCRFPVEIKSFYMQRCPEDPRLTE 460
Cdd:cd00776 163 LKPLEPFPRITYDEAIELLREKGVEEEV----KWGEDLSTEHERLLGEIVkGDPVFVTDYPKEIKPFYMKPDDDNPETVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 461 SVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYP 540
Cdd:cd00776 239 SFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
....
gi 1781914484 541 RFLQ 544
Cdd:cd00776 319 RDPK 322
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
115-548 |
9.24e-147 |
|
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl/asparaginyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439788 [Multi-domain] Cd Length: 430 Bit Score: 428.70 E-value: 9.24e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 115 VKIS-ALEGYRGQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQCYNGVV-LSTESSVAVYGTLNLTPKgk 192
Cdd:COG0017 3 TYIKdLLPEHVGQEVTVAGWVRTKRDSGG-ISFLILRDGSGFIQVVVKKDKLENFEEAKkLTTESSVEVTGTVVESPR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 193 qAPGGHELSCDFWELVGLA----PaggadnLINEESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEV 268
Cdd:COG0017 80 -APQGVELQAEEIEVLGEAdepyP------LQPKRHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVEV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 269 TTPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFE 348
Cdd:COG0017 153 HTPIITASATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMALEKVYTFGPTFRAEKSNTRRHLAEFWMIEPEMAFADLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 349 DLLNRLEDLVCDVVDRVLKSPVASI-VYELNPNF--KPPKRPFRRMNYSDAIEWLKEHDVKkedgtfYEFGDDI-PEApE 424
Cdd:COG0017 233 DVMDLAEEMLKYIIKYVLENCPEELeFLGRDVERleKVPESPFPRITYTEAIEILKKSGEK------VEWGDDLgTEH-E 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 425 RLMTDTI-NEPILLCRFPVEIKSFYMQRCPEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYT 503
Cdd:COG0017 306 RYLGEEFfKKPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAPGIGEIIGGSQREHRYDVLVERIKEKGLDPEDYEWYL 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1781914484 504 DQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 548
Cdd:COG0017 386 DLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
125-548 |
1.51e-143 |
|
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: 421.40 E-value: 1.51e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 125 GQRVKVFGWVHRlRRQGKNLMFLVLRDGT--GYLQCVLSDDLCQCYNGVV--LSTESSVAVYGTLNLTPKGKQapgGHEL 200
Cdd:TIGR00457 16 GDEVTVSGWVRT-KRSSKKIIFLELNDGSslGPIQAVINGEDNPYLFQLLksLTTGSSVSVTGKVVESPGKGQ---PVEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 201 SCDFWELVGLAPAGGADNLInEESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEG 280
Cdd:TIGR00457 92 QVKKIEVVGEAEPDDYPLQK-KEHSLEFLRDIAHLRLRTNTLGAVMRVRNALSQAIHRYFQENGFTWVSPPILTSNDCEG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 281 GATLFKL---------DYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFEDLL 351
Cdd:TIGR00457 171 AGELFRVstgnidfsqDFFGKEAYLTVSGQLYLETYALALSKVYTFGPTFRAEKSNTSRHLSEFWMIEPEMAFANLNDLL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 352 NRLEDLVCDVVDRVLKSpVASIVYELNPNFKPPKRP---------FRRMNYSDAIEWLKEHDVKKEDGTFyeFGDDIPEA 422
Cdd:TIGR00457 251 QLAETLIKYIIKAVLEN-CSQELKFLEKNFDKDLIKrleniinnkFARITYTDAIEILKESDKNFEYEDF--WGDDLQTE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 423 PERLMTDTI-NEPILLCRFPVEIKSFYMQRCpEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYW 501
Cdd:TIGR00457 328 HERFLAEEYfKPPVFVTNYPKDIKAFYMKLN-DDGKTVAAMDLLAPGIGEIIGGSEREDDLDKLENRMKEMGLDTDALNW 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1781914484 502 YTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 548
Cdd:TIGR00457 407 YLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGNINF 453
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
121-548 |
9.07e-111 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 337.47 E-value: 9.07e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 121 EGYRGQRVKVFGWVHRlRRQGKNLMFLVLRDGTGY--LQCVLSDDLCqcYNGVV--LSTESSVAVYGTLNLTPKgkqAPG 196
Cdd:PRK03932 12 GKYVGQEVTVRGWVRT-KRDSGKIAFLQLRDGSCFkqLQVVKDNGEE--YFEEIkkLTTGSSVIVTGTVVESPR---AGQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 197 GHELSCDFWELVGLAPAggaDNLINE-ESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQ 275
Cdd:PRK03932 86 GYELQATKIEVIGEDPE---DYPIQKkRHSIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVDTPIITA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 276 TQVEGGATLFKL---------DYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLT 346
Cdd:PRK03932 163 SDCEGAGELFRVttldldfskDFFGKEAYLTVSGQLYAEAYAMALGKVYTFGPTFRAENSNTRRHLAEFWMIEPEMAFAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 347 FEDLLNRLEDLVCDVVDRVL-----------KSPVASIVYELNpNFKPPkrPFRRMNYSDAIEWLKEHDVKKEDGTfyEF 415
Cdd:PRK03932 243 LEDNMDLAEEMLKYVVKYVLencpddleflnRRVDKGDIERLE-NFIES--PFPRITYTEAIEILQKSGKKFEFPV--EW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 416 GDDI--PEapERLMTDTINE-PILLCRFPVEIKSFYMQRCPEDpRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKRE 492
Cdd:PRK03932 318 GDDLgsEH--ERYLAEEHFKkPVFVTNYPKDIKAFYMRLNPDG-KTVAAMDLLAPGIGEIIGGSQREERLDVLEARIKEL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1781914484 493 GIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 548
Cdd:PRK03932 395 GLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
225-541 |
1.00e-105 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 319.90 E-value: 1.00e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 225 DVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGATLFKL------DYFgeeaFLTQ 298
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVpsralgKFY----ALPQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 299 SSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHLaEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPvasiVYEL 377
Cdd:pfam00152 77 SPQLYKQLLMVAgFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIA----KELE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 378 NPNFKPPKRPFRRMNYSDAIEWLKEHDVkkedgtfYEFGDDIPEAPERLMTD-----TINEPILLCRFPVEIKSFYMQRC 452
Cdd:pfam00152 152 GGTLLDLKKPFPRITYAEAIEKLNGKDV-------EELGYGSDKPDLRFLLElvidkNKFNPLWVTDFPAEHHPFTMPKD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 453 PEDPRLTESVDVLMPNVgEIVGGSMRSWDSEEILEGYKREGIDP----APYYWYTDQRKYGTCPHGGYGLGLERFLSWIL 528
Cdd:pfam00152 225 EDDPALAEAFDLVLNGV-EIGGGSIRIHDPELQEERFEEQGLDPeeaeEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLT 303
|
330
....*....|...
gi 1781914484 529 NRYHIRDVCLYPR 541
Cdd:pfam00152 304 GLESIREVIAFPK 316
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
127-209 |
5.08e-40 |
|
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: 140.06 E-value: 5.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 127 RVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQ-CYNGVVLSTESSVAVYGTLNLTPKGKQAPGGHELSCDFW 205
Cdd:cd04323 1 RVKVFGWVHRLRSQKK-LMFLVLRDGTGFLQCVLSKKLVTeFYDAKSLTQESSVEVTGEVKEDPRAKQAPGGYELQVDYL 79
|
....
gi 1781914484 206 ELVG 209
Cdd:cd04323 80 EIIG 83
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
128-208 |
1.09e-13 |
|
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: 66.10 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 128 VKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVL-SDDLCQCYNgvVLSTESSVAVYGTLNLTPKgkqapGGHELSCDFWE 206
Cdd:pfam01336 1 VTVAGRVTSIRRSGGKLLFLTLRDGTGSIQVVVfKEEAEKLAK--KLKEGDVVRVTGKVKKRKG-----GELELVVEEIE 73
|
..
gi 1781914484 207 LV 208
Cdd:pfam01336 74 LL 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 ... |
225-544 |
1.44e-148 |
|
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: 429.29 E-value: 1.44e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 225 DVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYL 304
Cdd:cd00776 3 NLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQLYK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 305 ETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFL-TFEDLLNRLEDLVCDVVDRVLKSPVASI--VYELNPNF 381
Cdd:cd00776 83 EMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAKELelVNQLNREL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 382 KPPKRPFRRMNYSDAIEWLKEHDVKKEDgtfyEFGDDIPEAPERLMTDTI-NEPILLCRFPVEIKSFYMQRCPEDPRLTE 460
Cdd:cd00776 163 LKPLEPFPRITYDEAIELLREKGVEEEV----KWGEDLSTEHERLLGEIVkGDPVFVTDYPKEIKPFYMKPDDDNPETVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 461 SVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYP 540
Cdd:cd00776 239 SFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
....
gi 1781914484 541 RFLQ 544
Cdd:cd00776 319 RDPK 322
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
115-548 |
9.24e-147 |
|
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl/asparaginyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439788 [Multi-domain] Cd Length: 430 Bit Score: 428.70 E-value: 9.24e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 115 VKIS-ALEGYRGQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQCYNGVV-LSTESSVAVYGTLNLTPKgk 192
Cdd:COG0017 3 TYIKdLLPEHVGQEVTVAGWVRTKRDSGG-ISFLILRDGSGFIQVVVKKDKLENFEEAKkLTTESSVEVTGTVVESPR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 193 qAPGGHELSCDFWELVGLA----PaggadnLINEESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEV 268
Cdd:COG0017 80 -APQGVELQAEEIEVLGEAdepyP------LQPKRHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVEV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 269 TTPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFE 348
Cdd:COG0017 153 HTPIITASATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMALEKVYTFGPTFRAEKSNTRRHLAEFWMIEPEMAFADLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 349 DLLNRLEDLVCDVVDRVLKSPVASI-VYELNPNF--KPPKRPFRRMNYSDAIEWLKEHDVKkedgtfYEFGDDI-PEApE 424
Cdd:COG0017 233 DVMDLAEEMLKYIIKYVLENCPEELeFLGRDVERleKVPESPFPRITYTEAIEILKKSGEK------VEWGDDLgTEH-E 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 425 RLMTDTI-NEPILLCRFPVEIKSFYMQRCPEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYT 503
Cdd:COG0017 306 RYLGEEFfKKPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAPGIGEIIGGSQREHRYDVLVERIKEKGLDPEDYEWYL 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1781914484 504 DQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 548
Cdd:COG0017 386 DLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
125-548 |
1.51e-143 |
|
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: 421.40 E-value: 1.51e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 125 GQRVKVFGWVHRlRRQGKNLMFLVLRDGT--GYLQCVLSDDLCQCYNGVV--LSTESSVAVYGTLNLTPKGKQapgGHEL 200
Cdd:TIGR00457 16 GDEVTVSGWVRT-KRSSKKIIFLELNDGSslGPIQAVINGEDNPYLFQLLksLTTGSSVSVTGKVVESPGKGQ---PVEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 201 SCDFWELVGLAPAGGADNLInEESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEG 280
Cdd:TIGR00457 92 QVKKIEVVGEAEPDDYPLQK-KEHSLEFLRDIAHLRLRTNTLGAVMRVRNALSQAIHRYFQENGFTWVSPPILTSNDCEG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 281 GATLFKL---------DYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFEDLL 351
Cdd:TIGR00457 171 AGELFRVstgnidfsqDFFGKEAYLTVSGQLYLETYALALSKVYTFGPTFRAEKSNTSRHLSEFWMIEPEMAFANLNDLL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 352 NRLEDLVCDVVDRVLKSpVASIVYELNPNFKPPKRP---------FRRMNYSDAIEWLKEHDVKKEDGTFyeFGDDIPEA 422
Cdd:TIGR00457 251 QLAETLIKYIIKAVLEN-CSQELKFLEKNFDKDLIKrleniinnkFARITYTDAIEILKESDKNFEYEDF--WGDDLQTE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 423 PERLMTDTI-NEPILLCRFPVEIKSFYMQRCpEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYW 501
Cdd:TIGR00457 328 HERFLAEEYfKPPVFVTNYPKDIKAFYMKLN-DDGKTVAAMDLLAPGIGEIIGGSEREDDLDKLENRMKEMGLDTDALNW 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1781914484 502 YTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 548
Cdd:TIGR00457 407 YLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGNINF 453
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
121-548 |
9.07e-111 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 337.47 E-value: 9.07e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 121 EGYRGQRVKVFGWVHRlRRQGKNLMFLVLRDGTGY--LQCVLSDDLCqcYNGVV--LSTESSVAVYGTLNLTPKgkqAPG 196
Cdd:PRK03932 12 GKYVGQEVTVRGWVRT-KRDSGKIAFLQLRDGSCFkqLQVVKDNGEE--YFEEIkkLTTGSSVIVTGTVVESPR---AGQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 197 GHELSCDFWELVGLAPAggaDNLINE-ESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQ 275
Cdd:PRK03932 86 GYELQATKIEVIGEDPE---DYPIQKkRHSIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVDTPIITA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 276 TQVEGGATLFKL---------DYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLT 346
Cdd:PRK03932 163 SDCEGAGELFRVttldldfskDFFGKEAYLTVSGQLYAEAYAMALGKVYTFGPTFRAENSNTRRHLAEFWMIEPEMAFAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 347 FEDLLNRLEDLVCDVVDRVL-----------KSPVASIVYELNpNFKPPkrPFRRMNYSDAIEWLKEHDVKKEDGTfyEF 415
Cdd:PRK03932 243 LEDNMDLAEEMLKYVVKYVLencpddleflnRRVDKGDIERLE-NFIES--PFPRITYTEAIEILQKSGKKFEFPV--EW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 416 GDDI--PEapERLMTDTINE-PILLCRFPVEIKSFYMQRCPEDpRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKRE 492
Cdd:PRK03932 318 GDDLgsEH--ERYLAEEHFKkPVFVTNYPKDIKAFYMRLNPDG-KTVAAMDLLAPGIGEIIGGSQREERLDVLEARIKEL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1781914484 493 GIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 548
Cdd:PRK03932 395 GLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
225-541 |
1.00e-105 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 319.90 E-value: 1.00e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 225 DVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGATLFKL------DYFgeeaFLTQ 298
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVpsralgKFY----ALPQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 299 SSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHLaEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPvasiVYEL 377
Cdd:pfam00152 77 SPQLYKQLLMVAgFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIA----KELE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 378 NPNFKPPKRPFRRMNYSDAIEWLKEHDVkkedgtfYEFGDDIPEAPERLMTD-----TINEPILLCRFPVEIKSFYMQRC 452
Cdd:pfam00152 152 GGTLLDLKKPFPRITYAEAIEKLNGKDV-------EELGYGSDKPDLRFLLElvidkNKFNPLWVTDFPAEHHPFTMPKD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 453 PEDPRLTESVDVLMPNVgEIVGGSMRSWDSEEILEGYKREGIDP----APYYWYTDQRKYGTCPHGGYGLGLERFLSWIL 528
Cdd:pfam00152 225 EDDPALAEAFDLVLNGV-EIGGGSIRIHDPELQEERFEEQGLDPeeaeEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLT 303
|
330
....*....|...
gi 1781914484 529 NRYHIRDVCLYPR 541
Cdd:pfam00152 304 GLESIREVIAFPK 316
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
125-548 |
2.06e-101 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 312.89 E-value: 2.06e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 125 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQCYNGVV--LSTESSVAVYGTLNLTPKgkqAPGGHELSC 202
Cdd:PRK05159 16 GEEVTLAGWVHEIRDLGG-IAFLILRDRSGIIQVVVKKKVDEELFETIkkLKRESVVSVTGTVKANPK---APGGVEVIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 203 DFWELVGLApaggADNL---INEES--DVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQ 277
Cdd:PRK05159 92 EEIEVLNKA----EEPLpldISGKVlaELDTRLDNRFLDLRRPRVRAIFKIRSEVLRAFREFLYENGFTEIFTPKIVASG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 278 VEGGATLFKLDYFGEEAFLTQSSQLYLETCLPALGD-VFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLT-FEDLLNRLE 355
Cdd:PRK05159 168 TEGGAELFPIDYFEKEAYLAQSPQLYKQMMVGAGFErVFEIGPVFRAEEHNTSRHLNEYTSIDVEMGFIDdHEDVMDLLE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 356 DLVCDVVDRVLKSPVASIVyELNPNFKPPKRPFRRMNYSDAIEWLKEHDVKKedgtfyEFGDDIPEAPERLMTDTINE-- 433
Cdd:PRK05159 248 NLLRYMYEDVAENCEKELE-LLGIELPVPETPIPRITYDEAIEILKSKGNEI------SWGDDLDTEGERLLGEYVKEey 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 434 ---PILLCRFPVEIKSFYMQRCPEDPRLTESVDVLMPNVgEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGT 510
Cdd:PRK05159 321 gsdFYFITDYPSEKRPFYTMPDEDDPEISKSFDLLFRGL-EITSGGQRIHRYDMLVESIKEKGLNPESFEFYLEAFKYGM 399
|
410 420 430
....*....|....*....|....*....|....*...
gi 1781914484 511 CPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 548
Cdd:PRK05159 400 PPHGGFGLGLERLTMKLLGLENIREAVLFPRDRHRLTP 437
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
76-548 |
7.84e-55 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 193.38 E-value: 7.84e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 76 KNDSREKKEAEDNLRREKNLEEAKKIIIKNDP---------------SLPEPACVKISAL-EGYRGQRVKVFGWVHRLRR 139
Cdd:PLN02850 16 KAAKKAAAKAEKLRREATAKAAAASLEDEDDPlasnygdvpleelqsKVTGREWTDVSDLgEELAGSEVLIRGRVHTIRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 140 QGKnLMFLVLRDGTGYLQCVLSDDLCQCYNGVV-----LSTESSVAVYGTLNLTPKG-KQAPGGHELSCDFWELVGLAPA 213
Cdd:PLN02850 96 KGK-SAFLVLRQSGFTVQCVVFVSEVTVSKGMVkyakqLSRESVVDVEGVVSVPKKPvKGTTQQVEIQVRKIYCVSKALA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 214 GGADNLIN---EESDV---------------DVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQ 275
Cdd:PLN02850 175 TLPFNVEDaarSESEIekalqtgeqlvrvgqDTRLNNRVLDLRTPANQAIFRIQSQVCNLFREFLLSKGFVEIHTPKLIA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 276 TQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHLAEFTHveaecpfLTFEDLLNRL 354
Cdd:PLN02850 255 GASEGGSAVFRLDYKGQPACLAQSPQLHKQMAICGdFRRVFEIGPVFRAEDSFTHRHLCEFTG-------LDLEMEIKEH 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 355 EDLVCDVVDRVLKspvaSIVYELNPN-------------FKPPK--RPFRRMNYSDAIEWLKEHDVKKEDgtfyeFGDDI 419
Cdd:PLN02850 328 YSEVLDVVDELFV----AIFDGLNERckkeleaireqypFEPLKylPKTLRLTFAEGIQMLKEAGVEVDP-----LGDLN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 420 PEApERLMTDTINEP-----ILLCRFPVEIKSFYMQRCPEDPRLTESVDVLMPNvGEIVGGSMRSWDSEEILEGYKREGI 494
Cdd:PLN02850 399 TES-ERKLGQLVKEKygtdfYILHRYPLAVRPFYTMPCPDDPKYSNSFDVFIRG-EEIISGAQRVHDPELLEKRAEECGI 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1781914484 495 DPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 548
Cdd:PLN02850 477 DVKTISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPRDPQRLAP 530
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
237-541 |
8.55e-50 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 174.82 E-value: 8.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 237 IRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLvqTQV-----EGGATL----FKLDYFGEEAFLTQSSQLYLETC 307
Cdd:PRK06462 21 ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPII--SPStdplmGLGSDLpvkqISIDFYGVEYYLADSMILHKQLA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 308 LPALGDVFCIAQSYRAEQ--SRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPVASIvYELNPNFKPPK 385
Cdd:PRK06462 99 LRMLGKIFYLSPNFRLEPvdKDTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHEDEL-EFFGRDLPHLK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 386 RPFRRMNYSDAIEWLKEHDVKKEDgtFYEFGDDIpeapERLMTDTINEPILLCRFPVEIKSFYMQRCPEDPRLTESVDVL 465
Cdd:PRK06462 178 RPFKRITHKEAVEILNEEGCRGID--LEELGSEG----EKSLSEHFEEPFWIIDIPKGSREFYDREDPERPGVLRNYDLL 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1781914484 466 MPN-VGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPR 541
Cdd:PRK06462 252 LPEgYGEAVSGGEREYEYEEIVERIREHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQPFPR 328
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
122-542 |
1.92e-49 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 179.42 E-value: 1.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 122 GYRGQRVKVFGWVHRLRRQGK-NLMFLVLRDGT--GYLQCVLSDDLCQCYNgvVLSTESSVAVYGTLNLTPKGKQAPGGH 198
Cdd:PLN02221 47 GLAGQKVRIGGWVKTGREQGKgTFAFLEVNDGScpANLQVMVDSSLYDLST--LVATGTCVTVDGVLKVPPEGKGTKQKI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 199 ELSCDFWELVGLAPAGGADnLINEESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQV 278
Cdd:PLN02221 125 ELSVEKVIDVGTVDPTKYP-LPKTKLTLEFLRDVLHLRSRTNSISAVARIRNALAFATHSFFQEHSFLYIHTPIITTSDC 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 279 EGGATLFKL----------------------------------------------------------------------- 287
Cdd:PLN02221 204 EGAGEMFQVttlinyterleqdlidnpppteadveaarlivkergevvaqlkaakaskeeitaavaelkiakeslahiee 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 288 -------------------DYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFE 348
Cdd:PLN02221 284 rsklkpglpkkdgkidyskDFFGRQAFLTVSGQLQVETYACALSSVYTFGPTFRAENSHTSRHLAEFWMVEPEIAFADLE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 349 DLLNRLEDLVCDVVDRVLKSPVASIvyEL-NPNFKP---------PKRPFRRMNYSDAIEWLKEHDVK-KEDGTFYEFGD 417
Cdd:PLN02221 364 DDMNCAEAYVKYMCKWLLDKCFDDM--ELmAKNFDSgcidrlrmvASTPFGRITYTEAIELLEEAVAKgKEFDNNVEWGI 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 418 DIPEAPERLMTDTI-NEPILLCRFPVEIKSFYMqRCPEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDP 496
Cdd:PLN02221 442 DLASEHERYLTEVLfQKPLIVYNYPKGIKAFYM-RLNDDEKTVAAMDVLVPKVGELIGGSQREERYDVIKQRIEEMGLPI 520
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1781914484 497 APYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRF 542
Cdd:PLN02221 521 EPYEWYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPRY 566
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
125-541 |
4.14e-49 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 178.63 E-value: 4.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 125 GQRVKVFGWVHRLRRQgKNLMFLVLRDGT--GYLQCVLSDDlCQCYNGV---VLSTESSVAVYGTLNLTPKGKQAPgghE 199
Cdd:PLN02603 107 GKTLNVMGWVRTLRAQ-SSVTFIEVNDGSclSNMQCVMTPD-AEGYDQVesgLITTGASVLVQGTVVSSQGGKQKV---E 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 200 LSCDFWELVGlapaggadnlineESDVDVQLNNR-----------HMMIRGENMSKILKARSMITRCFRDHFFDRGYCEV 268
Cdd:PLN02603 182 LKVSKIVVVG-------------KSDPSYPIQKKrvsreflrtkaHLRPRTNTFGAVARVRNALAYATHKFFQENGFVWV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 269 TTP-----------------TLVQTQVEGGATLFK-------------LDYFGEEAFLTQSSQLYLETCLPALGDVFCIA 318
Cdd:PLN02603 249 SSPiitasdcegageqfcvtTLIPNSAENGGSLVDdipktkdglidwsQDFFGKPAFLTVSGQLNGETYATALSDVYTFG 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 319 QSYRAEQSRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPV-----------ASIVYELNpnfKPPKRP 387
Cdd:PLN02603 329 PTFRAENSNTSRHLAEFWMIEPELAFADLNDDMACATAYLQYVVKYILENCKedmeffntwieKGIIDRLS---DVVEKN 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 388 FRRMNYSDAIEWLKEhdVKKEDGTFYEFGDDIPEAPERLMTDTI--NEPILLCRFPVEIKSFYMqRCPEDPRLTESVDVL 465
Cdd:PLN02603 406 FVQLSYTDAIELLLK--AKKKFEFPVKWGLDLQSEHERYITEEAfgGRPVIIRDYPKEIKAFYM-RENDDGKTVAAMDML 482
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1781914484 466 MPNVGEIVGGSMRSwDSEEILEGYKRE-GIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPR 541
Cdd:PLN02603 483 VPRVGELIGGSQRE-ERLEYLEARLDElKLNKESYWWYLDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFPR 558
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
125-548 |
6.69e-46 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 169.40 E-value: 6.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 125 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCV--LSDDLCQCYNGVV--LSTESSVAVYGTLNLT--PKGKQAPGGH 198
Cdd:PTZ00401 78 DKTVLIRARVSTTRKKGK-MAFMVLRDGSDSVQAMaaVEGDVPKEMIDFIgqIPTESIVDVEATVCKVeqPITSTSHSDI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 199 ELSCDFWELVG---------LAPAGGADNLINEESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVT 269
Cdd:PTZ00401 157 ELKVKKIHTVTeslrtlpftLEDASRKESDEGAKVNFDTRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLIDSDFCEIH 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 270 TPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLT-F 347
Cdd:PTZ00401 237 SPKIINAPSEGGANVFKLEYFNRFAYLAQSPQLYKQMVLQGdVPRVFEVGPVFRSENSNTHRHLTEFVGLDVEMRINEhY 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 348 EDLLNRLEDLVCDVVDRVLKS-----------PVASIVYELNP-------------NFKPPKR----------PFRRMNY 393
Cdd:PTZ00401 317 YEVLDLAESLFNYIFERLATHtkelkavcqqyPFEPLVWKLTPermkelgvgviseGVEPTDKyqarvhnmdsRMLRINY 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 394 SDAIEWLKEHDVKKEDGTfyefgDDIPEAPERLMTDTINEP-----ILLCRFPVEIKSFYMQRCPEDPRLTESVDVLMPN 468
Cdd:PTZ00401 397 MHCIELLNTVLEEKMAPT-----DDINTTNEKLLGKLVKERygtdfFISDRFPSSARPFYTMECKDDERFTNSYDMFIRG 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 469 vGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 548
Cdd:PTZ00401 472 -EEISSGAQRIHDPDLLLARAKMLNVDLTPIKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFPRDPQRTTP 550
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
285-542 |
1.06e-43 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 163.66 E-value: 1.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 285 FKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDR 364
Cdd:PTZ00425 317 YKKDFFSKQAFLTVSGQLSLENLCSSMGDVYTFGPTFRAENSHTSRHLAEFWMIEPEIAFADLYDNMELAESYIKYCIGY 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 365 VLKSPVASIVY-ELNPNFKPPKR-------PFRRMNYSDAIEWLKEHDVKKEdgTFYEFGDDIPEAPERLMTDTI-NEPI 435
Cdd:PTZ00425 397 VLNNNFDDIYYfEENVETGLISRlknildeDFAKITYTNVIDLLQPYSDSFE--VPVKWGMDLQSEHERFVAEQIfKKPV 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 436 LLCRFPVEIKSFYMqRCPEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGG 515
Cdd:PTZ00425 475 IVYNYPKDLKAFYM-KLNEDQKTVAAMDVLVPKIGEVIGGSQREDNLERLDKMIKEKKLNMESYWWYRQLRKFGSHPHAG 553
|
250 260
....*....|....*....|....*..
gi 1781914484 516 YGLGLERFLSWILNRYHIRDVCLYPRF 542
Cdd:PTZ00425 554 FGLGFERLIMLVTGVDNIKDTIPFPRY 580
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
246-541 |
3.04e-41 |
|
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: 149.55 E-value: 3.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 246 LKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGATLFKLDYF--GEEAFLTQSSQLYLETCLPA-LGDVFCIAQSYR 322
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNalGLDYYLRISPQLFKKRLMVGgLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 323 AEQSRTRrHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLkspvasIVYELNPNFKP--PKRPFRRMNYSDAIEWL 400
Cdd:cd00669 81 NEDLRAR-HQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVL------GVTAVTYGFELedFGLPFPRLTYREALERY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 401 KEhdvkkedgtfyefgddipeaperlmtdtinePILLCRFPVEIKSFYMQRCPEDPRLTESVDVLMPNVgEIVGGSMRSW 480
Cdd:cd00669 154 GQ-------------------------------PLFLTDYPAEMHSPLASPHDVNPEIADAFDLFINGV-EVGNGSSRLH 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1781914484 481 DSEEILEGYKREGIDPAP----YYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPR 541
Cdd:cd00669 202 DPDIQAEVFQEQGINKEAgmeyFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPK 266
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
127-209 |
5.08e-40 |
|
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: 140.06 E-value: 5.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 127 RVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQ-CYNGVVLSTESSVAVYGTLNLTPKGKQAPGGHELSCDFW 205
Cdd:cd04323 1 RVKVFGWVHRLRSQKK-LMFLVLRDGTGFLQCVLSKKLVTeFYDAKSLTQESSVEVTGEVKEDPRAKQAPGGYELQVDYL 79
|
....
gi 1781914484 206 ELVG 209
Cdd:cd04323 80 EIIG 83
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
285-541 |
2.54e-27 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 116.51 E-value: 2.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 285 FKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDR 364
Cdd:PLN02532 363 FSKDFFSRPTYLTVSGRLHLESYACALGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAFSELEDAMNCAEDYFKFLCKW 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 365 VLKSPVA-----------SIVYELNPNFkppKRPFRRMNYSDAIEWLKEH-DVKKEdgTFYEFGddIPEAPERL--MTDT 430
Cdd:PLN02532 443 VLENCSEdmkfvskridkTISTRLEAII---SSSLQRISYTEAVDLLKQAtDKKFE--TKPEWG--IALTTEHLsyLADE 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 431 I-NEPILLCRFPVEIKSFYMqRCPEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYG 509
Cdd:PLN02532 516 IyKKPVIIYNYPKELKPFYV-RLNDDGKTVAAFDLVVPKVGTVITGSQNEERMDILNARIEELGLPREQYEWYLDLRRHG 594
|
250 260 270
....*....|....*....|....*....|..
gi 1781914484 510 TCPHGGYGLGLERFLSWILNRYHIRDVCLYPR 541
Cdd:PLN02532 595 TVKHSGFSLGFELMVLFATGLPDVRDAIPFPR 626
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
127-209 |
2.73e-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: 96.48 E-value: 2.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 127 RVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQCYNGVV--LSTESSVAVYGTLNLTPKGKQAPGGHELSCDF 204
Cdd:cd04100 1 EVTLAGWVHSRRDHGG-LIFIDLRDGSGIVQVVVNKEELGEFFEEAekLRTESVVGVTGTVVKRPEGNLATGEIELQAEE 79
|
....*
gi 1781914484 205 WELVG 209
Cdd:cd04100 80 LEVLS 84
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
125-398 |
1.66e-23 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 104.49 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 125 GQRVKVFGWVHRLRRQGkNLMFLVLRDGTGYLQCVLSDDLCQCYNGVV--LSTESSVAVYGTLNLTPKG----KQAPGGH 198
Cdd:PLN02903 72 GSRVTLCGWVDLHRDMG-GLTFLDVRDHTGIVQVVTLPDEFPEAHRTAnrLRNEYVVAVEGTVRSRPQEspnkKMKTGSV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 199 EL---SCDFWELVGLA------PAGGADNLINEEsdvdVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDR-GYCEV 268
Cdd:PLN02903 151 EVvaeSVDILNVVTKSlpflvtTADEQKDSIKEE----VRLRYRVLDLRRPQMNANLRLRHRVVKLIRRYLEDVhGFVEI 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 269 TTPTLVQTQVEGGatlfkLDYF-------GEEAFLTQSSQLYLETCLPALGD-VFCIAQSYRAEQSRTRRHlAEFTHVEA 340
Cdd:PLN02903 227 ETPILSRSTPEGA-----RDYLvpsrvqpGTFYALPQSPQLFKQMLMVSGFDrYYQIARCFRDEDLRADRQ-PEFTQLDM 300
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1781914484 341 ECPFLTFEDLLNRLEDLVCDVVDRVLKSPVAsivyelnpnfkppkRPFRRMNYSDAIE 398
Cdd:PLN02903 301 ELAFTPLEDMLKLNEDLIRQVFKEIKGVQLP--------------NPFPRLTYAEAMS 344
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
125-399 |
1.69e-19 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 92.05 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 125 GQRVKVFGWVHRLRRQGkNLMFLVLRDGTGYLQCVLSDDLCQCYNGVVLSTESSVAVYGTLNLTPKG----KQAPGGHEL 200
Cdd:PRK00476 17 GQTVTLCGWVHRRRDHG-GLIFIDLRDREGIVQVVFDPDAEAFEVAESLRSEYVIQVTGTVRARPEGtvnpNLPTGEIEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 201 SCDFWELvgLAPaggADNL---INEESDV--DVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQ 275
Cdd:PRK00476 96 LASELEV--LNK---SKTLpfpIDDEEDVseELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDDNGFLEIETPILTK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 276 TQVEgGATlfklDYF-------GEeaF--LTQSSQL------------YletclpalgdvFCIAQSYRAEQSRTRRhLAE 334
Cdd:PRK00476 171 STPE-GAR----DYLvpsrvhpGK--FyaLPQSPQLfkqllmvagfdrY-----------YQIARCFRDEDLRADR-QPE 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1781914484 335 FTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPVasivyelnpnfkppKRPFRRMNYSDAIEW 399
Cdd:PRK00476 232 FTQIDIEMSFVTQEDVMALMEGLIRHVFKEVLGVDL--------------PTPFPRMTYAEAMRR 282
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
125-540 |
6.67e-19 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 89.76 E-value: 6.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 125 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLS-DDLCQCYNGVVLSTESS--VAVYGTLNLTPKGkqapgghELS 201
Cdd:PRK00484 54 EIEVSVAGRVMLKRVMGK-ASFATLQDGSGRIQLYVSkDDVGEEALEAFKKLDLGdiIGVEGTLFKTKTG-------ELS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 202 --CDFWELV------------GLapaggadnlineeSDVDVQLNNRHM-MIRGENMSKILKARSMITRCFRDHFFDRGYC 266
Cdd:PRK00484 126 vkATELTLLtkslrplpdkfhGL-------------TDVETRYRQRYVdLIVNPESRETFRKRSKIISAIRRFLDNRGFL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 267 EVTTPTLvQTqVEGGATL--FK--LDYFGEEAFLTQSSQLYLETCLpaLGD---VFCIAQSYRAEQSRTrRHLAEFTHVE 339
Cdd:PRK00484 193 EVETPML-QP-IAGGAAArpFIthHNALDIDLYLRIAPELYLKRLI--VGGferVYEIGRNFRNEGIDT-RHNPEFTMLE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 340 AECPFLTFEDLLNRLEDLVCDVVDRVLKSPVasIVY---ELnpNFKPpkrPFRRMNYSDAI-----------------EW 399
Cdd:PRK00484 268 FYQAYADYNDMMDLTEELIRHLAQAVLGTTK--VTYqgtEI--DFGP---PFKRLTMVDAIkeytgvdfddmtdeearAL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 400 LKEHDVKKEDgtFYEFGDDIPEAPERLMTDTINEPILLCRFPVEI----KsfymqRCPEDPRLTESVDVlmpnvgeIVGG 475
Cdd:PRK00484 341 AKELGIEVEK--SWGLGKLINELFEEFVEPKLIQPTFITDYPVEIsplaK-----RHREDPGLTERFEL-------FIGG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 476 SmrswdseEILEGYKrEGIDPApyywytDQRK----------------------------YGTCPHGGYGLGLERFLSWI 527
Cdd:PRK00484 407 R-------EIANAFS-ELNDPI------DQRErfeaqveakeagddeamfmdedflraleYGMPPTGGLGIGIDRLVMLL 472
|
490
....*....|...
gi 1781914484 528 LNRYHIRDVCLYP 540
Cdd:PRK00484 473 TDSPSIRDVILFP 485
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
246-540 |
6.97e-19 |
|
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: 86.86 E-value: 6.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 246 LKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGAtlfklDYF-------GEEAFLTQSSQLYLETCLPA-LGDVFCI 317
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTPEGAR-----DFLvpsrlhpGKFYALPQSPQLFKQLLMVSgFDRYFQI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 318 AQSYRAEQSRTRRHlAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKspvasivyelnpnfKPPKRPFRRMNYSDAI 397
Cdd:cd00777 76 ARCFRDEDLRADRQ-PEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG--------------VELTTPFPRMTYAEAM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 398 E-------W-----LKEHDvkKEDGTfYEFGDDIPEAPERLMTDTINEpillcrFPVEIKSfymqrcpedprltESVDVL 465
Cdd:cd00777 141 ErygfkflWivdfpLFEWD--EEEGR-LVSAHHPFTAPKEEDLDLLEK------DPEDARA-------------QAYDLV 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1781914484 466 MpNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYY----WYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYP 540
Cdd:cd00777 199 L-NGVELGGGSIRIHDPDIQEKVFEILGLSEEEAEekfgFLLEAFKYGAPPHGGIALGLDRLVMLLTGSESIRDVIAFP 276
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
125-398 |
1.39e-17 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 86.19 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 125 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLC--QCYN-GVVLSTESSVAVYGTLNLTPKGKQAP----GG 197
Cdd:PRK12820 18 GREVCLAGWVDAFRDHGE-LLFIHLRDRNGFIQAVFSPEAApaDVYElAASLRAEFCVALQGEVQKRLEETENPhietGD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 198 HELSCDfwELVGLAPA------------------GGADNlINEesdvDVQLNNRHMMIRGENMSKILKARSMITRCFRDH 259
Cdd:PRK12820 97 IEVFVR--ELSILAASealpfaisdkamtagagsAGADA-VNE----DLRLQYRYLDIRRPAMQDHLAKRHRIIKCARDF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 260 FFDRGYCEVTTPTLVQTQVEGGATLFKLDYFGEEAF--LTQSSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHlAEFT 336
Cdd:PRK12820 170 LDSRGFLEIETPILTKSTPEGARDYLVPSRIHPKEFyaLPQSPQLFKQLLMIAgFERYFQLARCFRDEDLRPNRQ-PEFT 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1781914484 337 HVEAECPFLTFEDLLNRLEDLVCDVVDrvlkspVASIvyELNpnfkppkRPFRRMNYSDAIE 398
Cdd:PRK12820 249 QLDIEASFIDEEFIFELIEELTARMFA------IGGI--ALP-------RPFPRMPYAEAMD 295
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
125-399 |
2.45e-17 |
|
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: 85.05 E-value: 2.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 125 GQRVKVFGWVHRLRRQGkNLMFLVLRDGTGYLQCVLSDDlcqcYNGVVLST------ESSVAVYGTLNLTPKG----KQA 194
Cdd:COG0173 16 GQEVTLSGWVHRRRDHG-GLIFIDLRDRYGITQVVFDPD----DSAEAFEKaeklrsEYVIAVTGKVRARPEGtvnpKLP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 195 PGGHELSCDfwELVGLAPaggADNL---INEESDV--DVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVT 269
Cdd:COG0173 91 TGEIEVLAS--ELEILNK---AKTPpfqIDDDTDVseELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDENGFLEIE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 270 TPTLVQTQVEgGATlfklDYF-------GEeaF--LTQSSQL------------YletclpalgdvFCIAQSYRAEQSRT 328
Cdd:COG0173 166 TPILTKSTPE-GAR----DYLvpsrvhpGK--FyaLPQSPQLfkqllmvsgfdrY-----------FQIARCFRDEDLRA 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1781914484 329 RRHlAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKspvasivYELnpnfkppKRPFRRMNYSDAIEW 399
Cdd:COG0173 228 DRQ-PEFTQLDIEMSFVDQEDVFELMEGLIRHLFKEVLG-------VEL-------PTPFPRMTYAEAMER 283
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
128-208 |
1.09e-13 |
|
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: 66.10 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 128 VKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVL-SDDLCQCYNgvVLSTESSVAVYGTLNLTPKgkqapGGHELSCDFWE 206
Cdd:pfam01336 1 VTVAGRVTSIRRSGGKLLFLTLRDGTGSIQVVVfKEEAEKLAK--KLKEGDVVRVTGKVKKRKG-----GELELVVEEIE 73
|
..
gi 1781914484 207 LV 208
Cdd:pfam01336 74 LL 75
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
128-547 |
1.87e-13 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 73.14 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 128 VKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLS-------DDLCQCYngVVLSTESSVAVYGTLNLTPKGkqapgghEL 200
Cdd:PTZ00385 110 VRVAGRVTSVRDIGK-IIFVTIRSNGNELQVVGQvgehftrEDLKKLK--VSLRVGDIIGADGVPCRMQRG-------EL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 201 SCDFWELVGLAPAGGADNLINEE-------SDVDVQLNNRHM-MIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPT 272
Cdd:PTZ00385 180 SVAASRMLILSPYVCTDQVVCPNlrgftvlQDNDVKYRYRFTdMMTNPCVIETIKKRHVMLQALRDYFNERNFVEVETPV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 273 LVQTQVEGGATLFKLDYFGEEA--FLTQSSQLYLETCL-PALGDVFCIAQSYRAEQSrTRRHLAEFTHVEAECPFLTFED 349
Cdd:PTZ00385 260 LHTVASGANAKSFVTHHNANAMdlFLRVAPELHLKQCIvGGMERIYEIGKVFRNEDA-DRSHNPEFTSCEFYAAYHTYED 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 350 LLNRLEDLVCDVVDRVLKSPVASIVYEL---NPNFKPPKRPFRRMNYSDAI------EWLKEHDVKKEDGTFY----EFG 416
Cdd:PTZ00385 339 LMPMTEDIFRQLAMRVNGTTVVQIYPENahgNPVTVDLGKPFRRVSVYDEIqrmsgvEFPPPNELNTPKGIAYmsvvMLR 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 417 DDIPEAPER------------LMTDTINEPILLCRFPVEIKSFYMQRCPEdPRLTESVDVLMPNVgEIVGGSMRSWDSEE 484
Cdd:PTZ00385 419 YNIPLPPVRtaakmfeklidfFITDRVVEPTFVMDHPLFMSPLAKEQVSR-PGLAERFELFVNGI-EYCNAYSELNDPHE 496
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1781914484 485 ILEGYKREGID-------PAPY-YWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCR 547
Cdd:PTZ00385 497 QYHRFQQQLVDrqggdeeAMPLdETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFPLLRQDIR 567
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
127-235 |
8.20e-12 |
|
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: 61.77 E-value: 8.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 127 RVKVFGWVHRLRRQGKNLmFLVLRDGTGYLQCVLSDDLCQ--CYNGVVLSTESSVAVYGTLNLTPKgkqAPGGHELSCDF 204
Cdd:cd04319 1 KVTLAGWVYRKREVGKKA-FIVLRDSTGIVQAVFSKDLNEeaYREAKKVGIESSVIVEGAVKADPR---APGGAEVHGEK 76
|
90 100 110
....*....|....*....|....*....|..
gi 1781914484 205 WELVGLapaggADNL-INEESDVDVQLNNRHM 235
Cdd:cd04319 77 LEIIQN-----VEFFpITEDASDEFLLDVRHL 103
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
225-540 |
8.45e-12 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 67.39 E-value: 8.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 225 DVDVQLNNRHM-MIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLvqTQVEGGAT----LFKLDYFGEEAFLTQS 299
Cdd:PRK12445 162 DQEVRYRQRYLdLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMM--QVIPGGASarpfITHHNALDLDMYLRIA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 300 SQLYLET-CLPALGDVFCIAQSYRAEqSRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVL---KSPVASIVY 375
Cdd:PRK12445 240 PELYLKRlVVGGFERVFEINRNFRNE-GISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLgttKVTYGEHVF 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 376 ELNPNFKP-----------PKRPFRRMNYSDAIEWLKEH---DVKKEDGtfyeFGDDIPEAPERLMTDTINEPILLCRFP 441
Cdd:PRK12445 319 DFGKPFEKltmreaikkyrPETDMADLDNFDAAKALAESigiTVEKSWG----LGRIVTEIFDEVAEAHLIQPTFITEYP 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 442 VEIKSFyMQRCPEDPRLTESVDVLMPNvGEIVGGSMRSWDSEEILEGY------KREGIDPAPYYW--YTDQRKYGTCPH 513
Cdd:PRK12445 395 AEVSPL-ARRNDVNPEITDRFEFFIGG-REIGNGFSELNDAEDQAERFqeqvnaKAAGDDEAMFYDedYVTALEYGLPPT 472
|
330 340
....*....|....*....|....*..
gi 1781914484 514 GGYGLGLERFLSWILNRYHIRDVCLYP 540
Cdd:PRK12445 473 AGLGIGIDRMIMLFTNSHTIRDVILFP 499
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
125-200 |
1.44e-11 |
|
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: 61.18 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 125 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVL-----SDDLCQCYNGvvLSTESSVAVYGTLNLTPKgkqAPGGHE 199
Cdd:cd04316 12 GEEVTVAGWVHEIRDLGG-IKFVILRDREGIVQVTApkkkvDKELFKTVRK--LSRESVISVTGTVKAEPK---APNGVE 85
|
.
gi 1781914484 200 L 200
Cdd:cd04316 86 I 86
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
246-460 |
1.52e-10 |
|
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441870 [Multi-domain] Cd Length: 309 Bit Score: 62.43 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 246 LKARSMITRCFRDHFFDRGYCEVTTPTLVQTqvegGAT-----LFKLDYFGEEAfltQSSQLYLETC--------LPA-L 311
Cdd:COG2269 6 LRARARLLAAIRAFFAERGVLEVETPALSVA----PGTdphldSFATEFIGPDG---GGRPLYLHTSpefamkrlLAAgS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 312 GDVFCIAQSYRAEQsRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSpvasivyelnpnfkppkrPFRRM 391
Cdd:COG2269 79 GPIYQIAKVFRNGE-RGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAAGFA------------------PAERL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 392 NYSDA-----------------IEWLKEHDVKKEDgtfyefGDDIPEAPERLMTDTI------NEPILLCRFPVEiksfy 448
Cdd:COG2269 140 SYQEAflrylgidpltadldelAAAAAAAGLRVAD------DDDRDDLLDLLLSERVepqlgrDRPTFLYDYPAS----- 208
|
250
....*....|....*..
gi 1781914484 449 mQ-----RCPEDPRLTE 460
Cdd:COG2269 209 -QaalarISPDDPRVAE 224
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
128-203 |
1.90e-10 |
|
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: 57.19 E-value: 1.90e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1781914484 128 VKVFGWVhRLRRQGKNLMFLVLRDGTGY--LQCVLSDDLCQCYNGVVLSTESSVAVYGTLNLTPKGKQApggHELSCD 203
Cdd:cd04318 2 VTVNGWV-RSVRDSKKISFIELNDGSCLknLQVVVDKELTNFKEILKLSTGSSIRVEGVLVKSPGAKQP---FELQAE 75
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
128-540 |
9.03e-10 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 61.16 E-value: 9.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 128 VKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVL----SDDLCQCYNGVVLSTESS--VAVYGTLNLTPKGkqapgghELS 201
Cdd:PLN02502 111 VSVAGRIMAKRAFGK-LAFYDLRDDGGKIQLYAdkkrLDLDEEEFEKLHSLVDRGdiVGVTGTPGKTKKG-------ELS 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 202 CDFWELVGLAPA-----GGADNLineeSDVDVQLNNRHM-MIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLvQ 275
Cdd:PLN02502 183 IFPTSFEVLTKCllmlpDKYHGL----TDQETRYRQRYLdLIANPEVRDIFRTRAKIISYIRRFLDDRGFLEVETPML-N 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 276 TQVeGGATL--FKLDY--FGEEAFLTQSSQLYL-ETCLPALGDVFCIAQSYRAEQSRTrRHLAEFTHVEAECPFLTFEDL 350
Cdd:PLN02502 258 MIA-GGAAArpFVTHHndLNMDLYLRIATELHLkRLVVGGFERVYEIGRQFRNEGIST-RHNPEFTTCEFYQAYADYNDM 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 351 LNRLEDLVCdvvdrvlkspvaSIVYELNPNFKPP--------KRPFRRMnysDAIEWLKE-------HDVKKEDGTFY-- 413
Cdd:PLN02502 336 MELTEEMVS------------GMVKELTGSYKIKyhgieidfTPPFRRI---SMISLVEEatgidfpADLKSDEANAYli 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 414 ----EFGDDIPEAP----------ERLMTDTINEPILLCRFPVEIkSFYMQRCPEDPRLTESVDVLmpnvgeIVGgsmrs 479
Cdd:PLN02502 401 aaceKFDVKCPPPQttgrllnelfEEFLEETLVQPTFVLDHPVEM-SPLAKPHRSKPGLTERFELF------ING----- 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 480 wdsEEILEGYKrEGIDPapyywyTDQRK----------------------------YGTCPHGGYGLGLERFLSWILNRY 531
Cdd:PLN02502 469 ---RELANAFS-ELTDP------VDQRErfeeqvkqhnagddeamaldedfctaleYGLPPTGGWGLGIDRLVMLLTDSA 538
|
....*....
gi 1781914484 532 HIRDVCLYP 540
Cdd:PLN02502 539 SIRDVIAFP 547
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
119-340 |
1.13e-09 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 61.13 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 119 ALEGYRGQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQCYN----GVVLSTESSVAVYGTLNLTPKGkqa 194
Cdd:PRK02983 645 ALDAPTGEEVSVSGRVLRIRDYGG-VLFADLRDWSGELQVLLDASRLEQGSladfRAAVDLGDLVEVTGTMGTSRNG--- 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 195 pgghELS--CDFWELVG--LAPaggadnLINEE---SDVDVQLNNRHM--MIRGENMSkILKARSMITRCFRDHFFDRGY 265
Cdd:PRK02983 721 ----TLSllVTSWRLAGkcLRP------LPDKWkglTDPEARVRQRYLdlAVNPEARD-LLRARSAVVRAVRETLVARGF 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 266 CEVTTPTLvQtQVEGGAT----LFKLDYFGEEAFLTQSSQLYLET-CLPALGDVFCIAQSYRAE-QSRTrrHLAEFTHVE 339
Cdd:PRK02983 790 LEVETPIL-Q-QVHGGANarpfVTHINAYDMDLYLRIAPELYLKRlCVGGVERVFELGRNFRNEgVDAT--HNPEFTLLE 865
|
.
gi 1781914484 340 A 340
Cdd:PRK02983 866 A 866
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
125-191 |
2.20e-09 |
|
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: 55.61 E-value: 2.20e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1781914484 125 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQCYNGVV-LSTESSVAVYGTLNLTPKG 191
Cdd:cd04317 14 GQEVTLCGWVQRRRDHGG-LIFIDLRDRYGIVQVVFDPEEAPEFELAEkLRNESVIQVTGKVRARPEG 80
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
63-540 |
2.88e-09 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 59.64 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 63 MKNIKKMWHREQMKnDSREKKEAEDNLR-----REKNLEEAKKIIIKNDPSLPEPACVKISALEGYR----GQRVK---- 129
Cdd:PTZ00417 57 MEGEKKVRSVQASK-DKKKEEEAEVDPRlyyenRSKFIQEQKAKGINPYPHKFERTITVPEFVEKYQdlasGEHLEdtil 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 130 -VFGWVHRLRRQGKNLMFLVLRDGTGYLQcVLSD---------DLCQCYNGVVLSTessvaVYGTLNLTPKGKQApgghE 199
Cdd:PTZ00417 136 nVTGRIMRVSASGQKLRFFDLVGDGAKIQ-VLANfafhdhtksNFAECYDKIRRGD-----IVGIVGFPGKSKKG----E 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 200 LSCDFWELVGLAPAGGADNLINEESDVDVQLNNRHM-MIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLvqTQV 278
Cdd:PTZ00417 206 LSIFPKETIILSPCLHMLPMKYGLKDTEIRYRQRYLdLMINESTRSTFITRTKIINYLRNFLNDRGFIEVETPTM--NLV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 279 EGGATlfkldyfgEEAFLTQSSQLYLE------TCLP-------ALGDVFCIAQSYRAEqSRTRRHLAEFTHVEAECPFL 345
Cdd:PTZ00417 284 AGGAN--------ARPFITHHNDLDLDlylriaTELPlkmlivgGIDKVYEIGKVFRNE-GIDNTHNPEFTSCEFYWAYA 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 346 TFEDLLNRLEDLVCDVVDRVLKSpvASIVY-----ELNP---NFKPpkrPFRRMNYSDAIEWLKE----------HDVKK 407
Cdd:PTZ00417 355 DFYDLIKWSEDFFSQLVMHLFGT--YKILYnkdgpEKDPieiDFTP---PYPKVSIVEELEKLTNtkleqpfdspETINK 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 408 EDGTFYEFGDDIPEAP------ERLMTDTI-----NEPILLCRFPvEIKSFYMQRCPEDPRLTESVDVLMPNvGEIVGGS 476
Cdd:PTZ00417 430 MINLIKENKIEMPNPPtaakllDQLASHFIenkypNKPFFIIEHP-QIMSPLAKYHRSKPGLTERLEMFICG-KEVLNAY 507
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1781914484 477 MRSWDSEEILEGYK-----REGIDPAPYYW---YTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYP 540
Cdd:PTZ00417 508 TELNDPFKQKECFSaqqkdREKGDAEAFQFdaaFCTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFP 579
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
242-536 |
1.35e-08 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 56.48 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 242 MSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQ-TQVEGGATLFKLDYFGEEAflTQSSQLYLETC--------LPAL- 311
Cdd:PRK09350 1 SIPNLLKRAKIIAEIRRFFADRGVLEVETPILSQaTVTDIHLVPFETRFVGPGA--SQGKTLWLMTSpeyhmkrlLAAGs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 312 GDVFCIAQSYRAEQSrTRRHLAEFTHVEAECPFLTFEDLLNRLEDLvcdvVDRVLKSPVA-SIVYE--------LNPnFK 382
Cdd:PRK09350 79 GPIFQICKSFRNEEA-GRYHNPEFTMLEWYRPHYDMYRLMNEVDDL----LQQVLDCEPAeSLSYQqaflrylgIDP-LS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 383 PPKRPFRrmnysDAIEWLKEHDVKKEDgtfyefgDDIPEAPERLMTDTI------NEPILLCRFPVEIKSfYMQRCPEDP 456
Cdd:PRK09350 153 ADKTQLR-----EVAAKLGLSNIADEE-------EDRDTLLQLLFTFGVepnigkEKPTFVYHFPASQAA-LAKISTEDH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 457 RLTESVDVLMPNVgEIVGGSMRSWDSEEILEGYKR-------EGIDPAPyywyTDQR-----KYGTCPHGGYGLGLERFL 524
Cdd:PRK09350 220 RVAERFEVYFKGI-ELANGFHELTDAREQRQRFEQdnrkraaRGLPQQP----IDENliaalEAGLPDCSGVALGVDRLI 294
|
330
....*....|..
gi 1781914484 525 SWILNRYHIRDV 536
Cdd:PRK09350 295 MLALGAESISEV 306
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
128-190 |
5.39e-08 |
|
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: 51.02 E-value: 5.39e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1781914484 128 VKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVLSDDlcqcyNGVV----------LSTESSVAVYGTLNLTPK 190
Cdd:cd04320 2 VLIRARVHTSRAQGAKLAFLVLRQQGYTIQGVLAAS-----AEGVskqmvkwagsLSKESIVDVEGTVKKPEE 69
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
260-460 |
9.03e-08 |
|
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous to the C-terminal region of lysyl-tRNA synthetase (LysS). Multiple sequence alignment of these proteins with the homologous regions of collected LysS proteins shows that these proteins form a distinct set rather than just similar truncations of LysS. The protein is termed GenX after its designation in E. coli. Interestingly, genX often is located near a homolog of lysine-2,3-aminomutase. Its function is unknown. [Unknown function, General]
Pssm-ID: 273090 [Multi-domain] Cd Length: 290 Bit Score: 53.71 E-value: 9.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 260 FFDRGYCEVTTPTLVQtqveGGATLFKLDYF--GEEAFLTQSSQLYLET----CLPAL-----GDVFCIAQSYRAEQsRT 328
Cdd:TIGR00462 2 FAERGVLEVETPLLSP----APVTDPHLDAFatEFVGPDGQGRPLYLQTspeyAMKRLlaagsGPIFQICKVFRNGE-RG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 329 RRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVvdrvlkspvasivyelnpnFKPPKRPFRRMNYSDA-IEWLKEHDVKK 407
Cdd:TIGR00462 77 RRHNPEFTMLEWYRPGFDYHDLMDEVEALLQEL-------------------LGDPFAPAERLSYQEAfLRYAGIDPLTA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1781914484 408 EDGTFYE----FGDDIPEAP------ERLMTDTI------NEPILLCRFPVEIKSFyMQRCPEDPRLTE 460
Cdd:TIGR00462 138 SLAELQAaaaaHGIRASEEDdrddllDLLFSEKVephlgfGRPTFLYDYPASQAAL-ARISPDDPRVAE 205
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
249-350 |
1.33e-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: 49.42 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 249 RSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGATLFKLD------YFGEEAFLTQSSQLYLET----CLPALGD-VFCI 317
Cdd:cd00768 2 RSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHEPKDllpvgaENEEDLYLRPTLEPGLVRlfvsHIRKLPLrLAEI 81
|
90 100 110
....*....|....*....|....*....|....
gi 1781914484 318 AQSYRAEQSRTR-RHLAEFTHVEAECPFLTFEDL 350
Cdd:cd00768 82 GPAFRNEGGRRGlRRVREFTQLEGEVFGEDGEEA 115
|
|
| ScAspRS_mt_like_N |
cd04321 |
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
127-208 |
1.93e-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: 40.38 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781914484 127 RVKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVLSDDLCQCYNGV-VLSTESSVAVYGTLNLtpkgKQAPGGHELSCdfW 205
Cdd:cd04321 1 KVTLNGWIDRKPRIVKKLSFADLRDPNGDIIQLVSTAKKDAFSLLkSITAESPVQVRGKLQL----KEAKSSEKNDE--W 74
|
...
gi 1781914484 206 ELV 208
Cdd:cd04321 75 ELV 77
|
|
| |
