|
Name |
Accession |
Description |
Interval |
E-value |
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
226-545 |
1.01e-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: 429.68 E-value: 1.01e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 226 DVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYL 305
Cdd:cd00776 3 NLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQLYK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 306 ETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFL-TFEDLLNRLEDLVCDVVDRVLKSPVASI--VYELNPNF 382
Cdd:cd00776 83 EMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAKELelVNQLNREL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 383 KPPKRPFRRMNYSDAIEWLKEHDVKKEDgtfyEFGDDIPEAPERLMTDTI-NEPILLCRFPVEIKSFYMQRCPEDPRLTE 461
Cdd:cd00776 163 LKPLEPFPRITYDEAIELLREKGVEEEV----KWGEDLSTEHERLLGEIVkGDPVFVTDYPKEIKPFYMKPDDDNPETVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 462 SVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYP 541
Cdd:cd00776 239 SFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
....
gi 1781913009 542 RFLQ 545
Cdd:cd00776 319 RDPK 322
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
116-549 |
7.77e-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: 429.09 E-value: 7.77e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 116 VKIS-ALEGYRGQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQCYNGVV-LSTESSVAVYGTLNLTPKgk 193
Cdd:COG0017 3 TYIKdLLPEHVGQEVTVAGWVRTKRDSGG-ISFLILRDGSGFIQVVVKKDKLENFEEAKkLTTESSVEVTGTVVESPR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 194 qAPGGHELSCDFWELVGLA----PaggadnLINEESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEV 269
Cdd:COG0017 80 -APQGVELQAEEIEVLGEAdepyP------LQPKRHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVEV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 270 TTPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFE 349
Cdd:COG0017 153 HTPIITASATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMALEKVYTFGPTFRAEKSNTRRHLAEFWMIEPEMAFADLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 350 DLLNRLEDLVCDVVDRVLKSPVASI-VYELNPNF--KPPKRPFRRMNYSDAIEWLKEHDVKkedgtfYEFGDDI-PEApE 425
Cdd:COG0017 233 DVMDLAEEMLKYIIKYVLENCPEELeFLGRDVERleKVPESPFPRITYTEAIEILKKSGEK------VEWGDDLgTEH-E 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 426 RLMTDTI-NEPILLCRFPVEIKSFYMQRCPEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYT 504
Cdd:COG0017 306 RYLGEEFfKKPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAPGIGEIIGGSQREHRYDVLVERIKEKGLDPEDYEWYL 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1781913009 505 DQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 549
Cdd:COG0017 386 DLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
126-549 |
1.56e-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: 1.56e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 126 GQRVKVFGWVHRlRRQGKNLMFLVLRDGT--GYLQCVLSDDLCQCYNGVV--LSTESSVAVYGTLNLTPKGKQapgGHEL 201
Cdd:TIGR00457 16 GDEVTVSGWVRT-KRSSKKIIFLELNDGSslGPIQAVINGEDNPYLFQLLksLTTGSSVSVTGKVVESPGKGQ---PVEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 202 SCDFWELVGLAPAGGADNLInEESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEG 281
Cdd:TIGR00457 92 QVKKIEVVGEAEPDDYPLQK-KEHSLEFLRDIAHLRLRTNTLGAVMRVRNALSQAIHRYFQENGFTWVSPPILTSNDCEG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 282 GATLFKL---------DYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFEDLL 352
Cdd:TIGR00457 171 AGELFRVstgnidfsqDFFGKEAYLTVSGQLYLETYALALSKVYTFGPTFRAEKSNTSRHLSEFWMIEPEMAFANLNDLL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 353 NRLEDLVCDVVDRVLKSpVASIVYELNPNFKPPKRP---------FRRMNYSDAIEWLKEHDVKKEDGTFyeFGDDIPEA 423
Cdd:TIGR00457 251 QLAETLIKYIIKAVLEN-CSQELKFLEKNFDKDLIKrleniinnkFARITYTDAIEILKESDKNFEYEDF--WGDDLQTE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 424 PERLMTDTI-NEPILLCRFPVEIKSFYMQRCpEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYW 502
Cdd:TIGR00457 328 HERFLAEEYfKPPVFVTNYPKDIKAFYMKLN-DDGKTVAAMDLLAPGIGEIIGGSEREDDLDKLENRMKEMGLDTDALNW 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1781913009 503 YTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 549
Cdd:TIGR00457 407 YLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGNINF 453
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
122-549 |
7.22e-111 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 337.85 E-value: 7.22e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 122 EGYRGQRVKVFGWVHRlRRQGKNLMFLVLRDGTGY--LQCVLSDDLCqcYNGVV--LSTESSVAVYGTLNLTPKgkqAPG 197
Cdd:PRK03932 12 GKYVGQEVTVRGWVRT-KRDSGKIAFLQLRDGSCFkqLQVVKDNGEE--YFEEIkkLTTGSSVIVTGTVVESPR---AGQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 198 GHELSCDFWELVGLAPAggaDNLINE-ESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQ 276
Cdd:PRK03932 86 GYELQATKIEVIGEDPE---DYPIQKkRHSIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVDTPIITA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 277 TQVEGGATLFKL---------DYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLT 347
Cdd:PRK03932 163 SDCEGAGELFRVttldldfskDFFGKEAYLTVSGQLYAEAYAMALGKVYTFGPTFRAENSNTRRHLAEFWMIEPEMAFAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 348 FEDLLNRLEDLVCDVVDRVL-----------KSPVASIVYELNpNFKPPkrPFRRMNYSDAIEWLKEHDVKKEDGTfyEF 416
Cdd:PRK03932 243 LEDNMDLAEEMLKYVVKYVLencpddleflnRRVDKGDIERLE-NFIES--PFPRITYTEAIEILQKSGKKFEFPV--EW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 417 GDDI--PEapERLMTDTINE-PILLCRFPVEIKSFYMQRCPEDpRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKRE 493
Cdd:PRK03932 318 GDDLgsEH--ERYLAEEHFKkPVFVTNYPKDIKAFYMRLNPDG-KTVAAMDLLAPGIGEIIGGSQREERLDVLEARIKEL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1781913009 494 GIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 549
Cdd:PRK03932 395 GLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
226-542 |
6.63e-106 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 320.28 E-value: 6.63e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 226 DVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGATLFKL------DYFgeeaFLTQ 299
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVpsralgKFY----ALPQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 300 SSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHLaEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPvasiVYEL 378
Cdd:pfam00152 77 SPQLYKQLLMVAgFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIA----KELE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 379 NPNFKPPKRPFRRMNYSDAIEWLKEHDVkkedgtfYEFGDDIPEAPERLMTD-----TINEPILLCRFPVEIKSFYMQRC 453
Cdd:pfam00152 152 GGTLLDLKKPFPRITYAEAIEKLNGKDV-------EELGYGSDKPDLRFLLElvidkNKFNPLWVTDFPAEHHPFTMPKD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 454 PEDPRLTESVDVLMPNVgEIVGGSMRSWDSEEILEGYKREGIDP----APYYWYTDQRKYGTCPHGGYGLGLERFLSWIL 529
Cdd:pfam00152 225 EDDPALAEAFDLVLNGV-EIGGGSIRIHDPELQEERFEEQGLDPeeaeEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLT 303
|
330
....*....|...
gi 1781913009 530 NRYHIRDVCLYPR 542
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 ... |
128-210 |
5.47e-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: 139.68 E-value: 5.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 128 RVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQ-CYNGVVLSTESSVAVYGTLNLTPKGKQAPGGHELSCDFW 206
Cdd:cd04323 1 RVKVFGWVHRLRSQKK-LMFLVLRDGTGFLQCVLSKKLVTeFYDAKSLTQESSVEVTGEVKEDPRAKQAPGGYELQVDYL 79
|
....
gi 1781913009 207 ELVG 210
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 ... |
129-209 |
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 1781913009 129 VKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVL-SDDLCQCYNgvVLSTESSVAVYGTLNLTPKgkqapGGHELSCDFWE 207
Cdd:pfam01336 1 VTVAGRVTSIRRSGGKLLFLTLRDGTGSIQVVVfKEEAEKLAK--KLKEGDVVRVTGKVKKRKG-----GELELVVEEIE 73
|
..
gi 1781913009 208 LV 209
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 ... |
226-545 |
1.01e-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: 429.68 E-value: 1.01e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 226 DVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYL 305
Cdd:cd00776 3 NLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQLYK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 306 ETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFL-TFEDLLNRLEDLVCDVVDRVLKSPVASI--VYELNPNF 382
Cdd:cd00776 83 EMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAKELelVNQLNREL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 383 KPPKRPFRRMNYSDAIEWLKEHDVKKEDgtfyEFGDDIPEAPERLMTDTI-NEPILLCRFPVEIKSFYMQRCPEDPRLTE 461
Cdd:cd00776 163 LKPLEPFPRITYDEAIELLREKGVEEEV----KWGEDLSTEHERLLGEIVkGDPVFVTDYPKEIKPFYMKPDDDNPETVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 462 SVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYP 541
Cdd:cd00776 239 SFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
....
gi 1781913009 542 RFLQ 545
Cdd:cd00776 319 RDPK 322
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
116-549 |
7.77e-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: 429.09 E-value: 7.77e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 116 VKIS-ALEGYRGQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQCYNGVV-LSTESSVAVYGTLNLTPKgk 193
Cdd:COG0017 3 TYIKdLLPEHVGQEVTVAGWVRTKRDSGG-ISFLILRDGSGFIQVVVKKDKLENFEEAKkLTTESSVEVTGTVVESPR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 194 qAPGGHELSCDFWELVGLA----PaggadnLINEESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEV 269
Cdd:COG0017 80 -APQGVELQAEEIEVLGEAdepyP------LQPKRHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVEV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 270 TTPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFE 349
Cdd:COG0017 153 HTPIITASATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMALEKVYTFGPTFRAEKSNTRRHLAEFWMIEPEMAFADLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 350 DLLNRLEDLVCDVVDRVLKSPVASI-VYELNPNF--KPPKRPFRRMNYSDAIEWLKEHDVKkedgtfYEFGDDI-PEApE 425
Cdd:COG0017 233 DVMDLAEEMLKYIIKYVLENCPEELeFLGRDVERleKVPESPFPRITYTEAIEILKKSGEK------VEWGDDLgTEH-E 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 426 RLMTDTI-NEPILLCRFPVEIKSFYMQRCPEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYT 504
Cdd:COG0017 306 RYLGEEFfKKPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAPGIGEIIGGSQREHRYDVLVERIKEKGLDPEDYEWYL 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1781913009 505 DQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 549
Cdd:COG0017 386 DLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
126-549 |
1.56e-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: 1.56e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 126 GQRVKVFGWVHRlRRQGKNLMFLVLRDGT--GYLQCVLSDDLCQCYNGVV--LSTESSVAVYGTLNLTPKGKQapgGHEL 201
Cdd:TIGR00457 16 GDEVTVSGWVRT-KRSSKKIIFLELNDGSslGPIQAVINGEDNPYLFQLLksLTTGSSVSVTGKVVESPGKGQ---PVEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 202 SCDFWELVGLAPAGGADNLInEESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEG 281
Cdd:TIGR00457 92 QVKKIEVVGEAEPDDYPLQK-KEHSLEFLRDIAHLRLRTNTLGAVMRVRNALSQAIHRYFQENGFTWVSPPILTSNDCEG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 282 GATLFKL---------DYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFEDLL 352
Cdd:TIGR00457 171 AGELFRVstgnidfsqDFFGKEAYLTVSGQLYLETYALALSKVYTFGPTFRAEKSNTSRHLSEFWMIEPEMAFANLNDLL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 353 NRLEDLVCDVVDRVLKSpVASIVYELNPNFKPPKRP---------FRRMNYSDAIEWLKEHDVKKEDGTFyeFGDDIPEA 423
Cdd:TIGR00457 251 QLAETLIKYIIKAVLEN-CSQELKFLEKNFDKDLIKrleniinnkFARITYTDAIEILKESDKNFEYEDF--WGDDLQTE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 424 PERLMTDTI-NEPILLCRFPVEIKSFYMQRCpEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYW 502
Cdd:TIGR00457 328 HERFLAEEYfKPPVFVTNYPKDIKAFYMKLN-DDGKTVAAMDLLAPGIGEIIGGSEREDDLDKLENRMKEMGLDTDALNW 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1781913009 503 YTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 549
Cdd:TIGR00457 407 YLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGNINF 453
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
122-549 |
7.22e-111 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 337.85 E-value: 7.22e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 122 EGYRGQRVKVFGWVHRlRRQGKNLMFLVLRDGTGY--LQCVLSDDLCqcYNGVV--LSTESSVAVYGTLNLTPKgkqAPG 197
Cdd:PRK03932 12 GKYVGQEVTVRGWVRT-KRDSGKIAFLQLRDGSCFkqLQVVKDNGEE--YFEEIkkLTTGSSVIVTGTVVESPR---AGQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 198 GHELSCDFWELVGLAPAggaDNLINE-ESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQ 276
Cdd:PRK03932 86 GYELQATKIEVIGEDPE---DYPIQKkRHSIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVDTPIITA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 277 TQVEGGATLFKL---------DYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLT 347
Cdd:PRK03932 163 SDCEGAGELFRVttldldfskDFFGKEAYLTVSGQLYAEAYAMALGKVYTFGPTFRAENSNTRRHLAEFWMIEPEMAFAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 348 FEDLLNRLEDLVCDVVDRVL-----------KSPVASIVYELNpNFKPPkrPFRRMNYSDAIEWLKEHDVKKEDGTfyEF 416
Cdd:PRK03932 243 LEDNMDLAEEMLKYVVKYVLencpddleflnRRVDKGDIERLE-NFIES--PFPRITYTEAIEILQKSGKKFEFPV--EW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 417 GDDI--PEapERLMTDTINE-PILLCRFPVEIKSFYMQRCPEDpRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKRE 493
Cdd:PRK03932 318 GDDLgsEH--ERYLAEEHFKkPVFVTNYPKDIKAFYMRLNPDG-KTVAAMDLLAPGIGEIIGGSQREERLDVLEARIKEL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1781913009 494 GIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 549
Cdd:PRK03932 395 GLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
226-542 |
6.63e-106 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 320.28 E-value: 6.63e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 226 DVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGATLFKL------DYFgeeaFLTQ 299
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVpsralgKFY----ALPQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 300 SSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHLaEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPvasiVYEL 378
Cdd:pfam00152 77 SPQLYKQLLMVAgFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIA----KELE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 379 NPNFKPPKRPFRRMNYSDAIEWLKEHDVkkedgtfYEFGDDIPEAPERLMTD-----TINEPILLCRFPVEIKSFYMQRC 453
Cdd:pfam00152 152 GGTLLDLKKPFPRITYAEAIEKLNGKDV-------EELGYGSDKPDLRFLLElvidkNKFNPLWVTDFPAEHHPFTMPKD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 454 PEDPRLTESVDVLMPNVgEIVGGSMRSWDSEEILEGYKREGIDP----APYYWYTDQRKYGTCPHGGYGLGLERFLSWIL 529
Cdd:pfam00152 225 EDDPALAEAFDLVLNGV-EIGGGSIRIHDPELQEERFEEQGLDPeeaeEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLT 303
|
330
....*....|...
gi 1781913009 530 NRYHIRDVCLYPR 542
Cdd:pfam00152 304 GLESIREVIAFPK 316
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
126-549 |
1.79e-101 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 312.89 E-value: 1.79e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 126 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQCYNGVV--LSTESSVAVYGTLNLTPKgkqAPGGHELSC 203
Cdd:PRK05159 16 GEEVTLAGWVHEIRDLGG-IAFLILRDRSGIIQVVVKKKVDEELFETIkkLKRESVVSVTGTVKANPK---APGGVEVIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 204 DFWELVGLApaggADNL---INEES--DVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQ 278
Cdd:PRK05159 92 EEIEVLNKA----EEPLpldISGKVlaELDTRLDNRFLDLRRPRVRAIFKIRSEVLRAFREFLYENGFTEIFTPKIVASG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 279 VEGGATLFKLDYFGEEAFLTQSSQLYLETCLPALGD-VFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLT-FEDLLNRLE 356
Cdd:PRK05159 168 TEGGAELFPIDYFEKEAYLAQSPQLYKQMMVGAGFErVFEIGPVFRAEEHNTSRHLNEYTSIDVEMGFIDdHEDVMDLLE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 357 DLVCDVVDRVLKSPVASIVyELNPNFKPPKRPFRRMNYSDAIEWLKEHDVKKedgtfyEFGDDIPEAPERLMTDTINE-- 434
Cdd:PRK05159 248 NLLRYMYEDVAENCEKELE-LLGIELPVPETPIPRITYDEAIEILKSKGNEI------SWGDDLDTEGERLLGEYVKEey 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 435 ---PILLCRFPVEIKSFYMQRCPEDPRLTESVDVLMPNVgEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGT 511
Cdd:PRK05159 321 gsdFYFITDYPSEKRPFYTMPDEDDPEISKSFDLLFRGL-EITSGGQRIHRYDMLVESIKEKGLNPESFEFYLEAFKYGM 399
|
410 420 430
....*....|....*....|....*....|....*...
gi 1781913009 512 CPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 549
Cdd:PRK05159 400 PPHGGFGLGLERLTMKLLGLENIREAVLFPRDRHRLTP 437
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
47-549 |
4.33e-55 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 194.15 E-value: 4.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 47 DSQKENEVGWDVISKSQMKnikkmwhreqmkndsREKKEAEDNLRREKNLEEAKKIIIKNDP---------------SLP 111
Cdd:PLN02850 1 SSQEAVEESGEKISKKAAK---------------KAAAKAEKLRREATAKAAAASLEDEDDPlasnygdvpleelqsKVT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 112 EPACVKISAL-EGYRGQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQCYNGVV-----LSTESSVAVYGT 185
Cdd:PLN02850 66 GREWTDVSDLgEELAGSEVLIRGRVHTIRGKGK-SAFLVLRQSGFTVQCVVFVSEVTVSKGMVkyakqLSRESVVDVEGV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 186 LNLTPKG-KQAPGGHELSCDFWELVGLAPAGGADNLIN---EESDV---------------DVQLNNRHMMIRGENMSKI 246
Cdd:PLN02850 145 VSVPKKPvKGTTQQVEIQVRKIYCVSKALATLPFNVEDaarSESEIekalqtgeqlvrvgqDTRLNNRVLDLRTPANQAI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 247 LKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPA-LGDVFCIAQSYRAE 325
Cdd:PLN02850 225 FRIQSQVCNLFREFLLSKGFVEIHTPKLIAGASEGGSAVFRLDYKGQPACLAQSPQLHKQMAICGdFRRVFEIGPVFRAE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 326 QSRTRRHLAEFTHveaecpfLTFEDLLNRLEDLVCDVVDRVLKspvaSIVYELNPN-------------FKPPK--RPFR 390
Cdd:PLN02850 305 DSFTHRHLCEFTG-------LDLEMEIKEHYSEVLDVVDELFV----AIFDGLNERckkeleaireqypFEPLKylPKTL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 391 RMNYSDAIEWLKEHDVKKEDgtfyeFGDDIPEApERLMTDTINEP-----ILLCRFPVEIKSFYMQRCPEDPRLTESVDV 465
Cdd:PLN02850 374 RLTFAEGIQMLKEAGVEVDP-----LGDLNTES-ERKLGQLVKEKygtdfYILHRYPLAVRPFYTMPCPDDPKYSNSFDV 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 466 LMPNvGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQ 545
Cdd:PLN02850 448 FIRG-EEIISGAQRVHDPELLEKRAEECGIDVKTISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPRDPQ 526
|
....
gi 1781913009 546 RCRP 549
Cdd:PLN02850 527 RLAP 530
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
238-542 |
6.72e-50 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 174.82 E-value: 6.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 238 IRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLvqTQV-----EGGATL----FKLDYFGEEAFLTQSSQLYLETC 308
Cdd:PRK06462 21 ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPII--SPStdplmGLGSDLpvkqISIDFYGVEYYLADSMILHKQLA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 309 LPALGDVFCIAQSYRAEQ--SRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPVASIvYELNPNFKPPK 386
Cdd:PRK06462 99 LRMLGKIFYLSPNFRLEPvdKDTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHEDEL-EFFGRDLPHLK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 387 RPFRRMNYSDAIEWLKEHDVKKEDgtFYEFGDDIpeapERLMTDTINEPILLCRFPVEIKSFYMQRCPEDPRLTESVDVL 466
Cdd:PRK06462 178 RPFKRITHKEAVEILNEEGCRGID--LEELGSEG----EKSLSEHFEEPFWIIDIPKGSREFYDREDPERPGVLRNYDLL 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1781913009 467 MPN-VGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPR 542
Cdd:PRK06462 252 LPEgYGEAVSGGEREYEYEEIVERIREHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQPFPR 328
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
123-543 |
1.96e-49 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 179.42 E-value: 1.96e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 123 GYRGQRVKVFGWVHRLRRQGK-NLMFLVLRDGT--GYLQCVLSDDLCQCYNgvVLSTESSVAVYGTLNLTPKGKQAPGGH 199
Cdd:PLN02221 47 GLAGQKVRIGGWVKTGREQGKgTFAFLEVNDGScpANLQVMVDSSLYDLST--LVATGTCVTVDGVLKVPPEGKGTKQKI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 200 ELSCDFWELVGLAPAGGADnLINEESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQV 279
Cdd:PLN02221 125 ELSVEKVIDVGTVDPTKYP-LPKTKLTLEFLRDVLHLRSRTNSISAVARIRNALAFATHSFFQEHSFLYIHTPIITTSDC 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 280 EGGATLFKL----------------------------------------------------------------------- 288
Cdd:PLN02221 204 EGAGEMFQVttlinyterleqdlidnpppteadveaarlivkergevvaqlkaakaskeeitaavaelkiakeslahiee 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 289 -------------------DYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFE 349
Cdd:PLN02221 284 rsklkpglpkkdgkidyskDFFGRQAFLTVSGQLQVETYACALSSVYTFGPTFRAENSHTSRHLAEFWMVEPEIAFADLE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 350 DLLNRLEDLVCDVVDRVLKSPVASIvyEL-NPNFKP---------PKRPFRRMNYSDAIEWLKEHDVK-KEDGTFYEFGD 418
Cdd:PLN02221 364 DDMNCAEAYVKYMCKWLLDKCFDDM--ELmAKNFDSgcidrlrmvASTPFGRITYTEAIELLEEAVAKgKEFDNNVEWGI 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 419 DIPEAPERLMTDTI-NEPILLCRFPVEIKSFYMqRCPEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDP 497
Cdd:PLN02221 442 DLASEHERYLTEVLfQKPLIVYNYPKGIKAFYM-RLNDDEKTVAAMDVLVPKVGELIGGSQREERYDVIKQRIEEMGLPI 520
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1781913009 498 APYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRF 543
Cdd:PLN02221 521 EPYEWYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPRY 566
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
126-542 |
4.22e-49 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 178.63 E-value: 4.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 126 GQRVKVFGWVHRLRRQgKNLMFLVLRDGT--GYLQCVLSDDlCQCYNGV---VLSTESSVAVYGTLNLTPKGKQAPgghE 200
Cdd:PLN02603 107 GKTLNVMGWVRTLRAQ-SSVTFIEVNDGSclSNMQCVMTPD-AEGYDQVesgLITTGASVLVQGTVVSSQGGKQKV---E 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 201 LSCDFWELVGlapaggadnlineESDVDVQLNNR-----------HMMIRGENMSKILKARSMITRCFRDHFFDRGYCEV 269
Cdd:PLN02603 182 LKVSKIVVVG-------------KSDPSYPIQKKrvsreflrtkaHLRPRTNTFGAVARVRNALAYATHKFFQENGFVWV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 270 TTP-----------------TLVQTQVEGGATLFK-------------LDYFGEEAFLTQSSQLYLETCLPALGDVFCIA 319
Cdd:PLN02603 249 SSPiitasdcegageqfcvtTLIPNSAENGGSLVDdipktkdglidwsQDFFGKPAFLTVSGQLNGETYATALSDVYTFG 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 320 QSYRAEQSRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPV-----------ASIVYELNpnfKPPKRP 388
Cdd:PLN02603 329 PTFRAENSNTSRHLAEFWMIEPELAFADLNDDMACATAYLQYVVKYILENCKedmeffntwieKGIIDRLS---DVVEKN 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 389 FRRMNYSDAIEWLKEhdVKKEDGTFYEFGDDIPEAPERLMTDTI--NEPILLCRFPVEIKSFYMqRCPEDPRLTESVDVL 466
Cdd:PLN02603 406 FVQLSYTDAIELLLK--AKKKFEFPVKWGLDLQSEHERYITEEAfgGRPVIIRDYPKEIKAFYM-RENDDGKTVAAMDML 482
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1781913009 467 MPNVGEIVGGSMRSwDSEEILEGYKRE-GIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPR 542
Cdd:PLN02603 483 VPRVGELIGGSQRE-ERLEYLEARLDElKLNKESYWWYLDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFPR 558
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
126-549 |
6.80e-46 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 169.40 E-value: 6.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 126 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCV--LSDDLCQCYNGVV--LSTESSVAVYGTLNLT--PKGKQAPGGH 199
Cdd:PTZ00401 78 DKTVLIRARVSTTRKKGK-MAFMVLRDGSDSVQAMaaVEGDVPKEMIDFIgqIPTESIVDVEATVCKVeqPITSTSHSDI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 200 ELSCDFWELVG---------LAPAGGADNLINEESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVT 270
Cdd:PTZ00401 157 ELKVKKIHTVTeslrtlpftLEDASRKESDEGAKVNFDTRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLIDSDFCEIH 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 271 TPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLT-F 348
Cdd:PTZ00401 237 SPKIINAPSEGGANVFKLEYFNRFAYLAQSPQLYKQMVLQGdVPRVFEVGPVFRSENSNTHRHLTEFVGLDVEMRINEhY 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 349 EDLLNRLEDLVCDVVDRVLKS-----------PVASIVYELNP-------------NFKPPKR----------PFRRMNY 394
Cdd:PTZ00401 317 YEVLDLAESLFNYIFERLATHtkelkavcqqyPFEPLVWKLTPermkelgvgviseGVEPTDKyqarvhnmdsRMLRINY 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 395 SDAIEWLKEHDVKKEDGTfyefgDDIPEAPERLMTDTINEP-----ILLCRFPVEIKSFYMQRCPEDPRLTESVDVLMPN 469
Cdd:PTZ00401 397 MHCIELLNTVLEEKMAPT-----DDINTTNEKLLGKLVKERygtdfFISDRFPSSARPFYTMECKDDERFTNSYDMFIRG 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 470 vGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 549
Cdd:PTZ00401 472 -EEISSGAQRIHDPDLLLARAKMLNVDLTPIKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFPRDPQRTTP 550
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
286-543 |
1.08e-43 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 163.66 E-value: 1.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 286 FKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDR 365
Cdd:PTZ00425 317 YKKDFFSKQAFLTVSGQLSLENLCSSMGDVYTFGPTFRAENSHTSRHLAEFWMIEPEIAFADLYDNMELAESYIKYCIGY 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 366 VLKSPVASIVY-ELNPNFKPPKR-------PFRRMNYSDAIEWLKEHDVKKEdgTFYEFGDDIPEAPERLMTDTI-NEPI 436
Cdd:PTZ00425 397 VLNNNFDDIYYfEENVETGLISRlknildeDFAKITYTNVIDLLQPYSDSFE--VPVKWGMDLQSEHERFVAEQIfKKPV 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 437 LLCRFPVEIKSFYMqRCPEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGG 516
Cdd:PTZ00425 475 IVYNYPKDLKAFYM-KLNEDQKTVAAMDVLVPKIGEVIGGSQREDNLERLDKMIKEKKLNMESYWWYRQLRKFGSHPHAG 553
|
250 260
....*....|....*....|....*..
gi 1781913009 517 YGLGLERFLSWILNRYHIRDVCLYPRF 543
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 ... |
247-542 |
2.31e-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: 149.93 E-value: 2.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 247 LKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGATLFKLDYF--GEEAFLTQSSQLYLETCLPA-LGDVFCIAQSYR 323
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNalGLDYYLRISPQLFKKRLMVGgLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 324 AEQSRTRrHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLkspvasIVYELNPNFKP--PKRPFRRMNYSDAIEWL 401
Cdd:cd00669 81 NEDLRAR-HQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVL------GVTAVTYGFELedFGLPFPRLTYREALERY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 402 KEhdvkkedgtfyefgddipeaperlmtdtinePILLCRFPVEIKSFYMQRCPEDPRLTESVDVLMPNVgEIVGGSMRSW 481
Cdd:cd00669 154 GQ-------------------------------PLFLTDYPAEMHSPLASPHDVNPEIADAFDLFINGV-EVGNGSSRLH 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1781913009 482 DSEEILEGYKREGIDPAP----YYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPR 542
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 ... |
128-210 |
5.47e-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: 139.68 E-value: 5.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 128 RVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQ-CYNGVVLSTESSVAVYGTLNLTPKGKQAPGGHELSCDFW 206
Cdd:cd04323 1 RVKVFGWVHRLRSQKK-LMFLVLRDGTGFLQCVLSKKLVTeFYDAKSLTQESSVEVTGEVKEDPRAKQAPGGYELQVDYL 79
|
....
gi 1781913009 207 ELVG 210
Cdd:cd04323 80 EIIG 83
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
286-542 |
2.56e-27 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 116.51 E-value: 2.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 286 FKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDR 365
Cdd:PLN02532 363 FSKDFFSRPTYLTVSGRLHLESYACALGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAFSELEDAMNCAEDYFKFLCKW 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 366 VLKSPVA-----------SIVYELNPNFkppKRPFRRMNYSDAIEWLKEH-DVKKEdgTFYEFGddIPEAPERL--MTDT 431
Cdd:PLN02532 443 VLENCSEdmkfvskridkTISTRLEAII---SSSLQRISYTEAVDLLKQAtDKKFE--TKPEWG--IALTTEHLsyLADE 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 432 I-NEPILLCRFPVEIKSFYMqRCPEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYG 510
Cdd:PLN02532 516 IyKKPVIIYNYPKELKPFYV-RLNDDGKTVAAFDLVVPKVGTVITGSQNEERMDILNARIEELGLPREQYEWYLDLRRHG 594
|
250 260 270
....*....|....*....|....*....|..
gi 1781913009 511 TCPHGGYGLGLERFLSWILNRYHIRDVCLYPR 542
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 ... |
128-210 |
2.74e-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: 2.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 128 RVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQCYNGVV--LSTESSVAVYGTLNLTPKGKQAPGGHELSCDF 205
Cdd:cd04100 1 EVTLAGWVHSRRDHGG-LIFIDLRDGSGIVQVVVNKEELGEFFEEAekLRTESVVGVTGTVVKRPEGNLATGEIELQAEE 79
|
....*
gi 1781913009 206 WELVG 210
Cdd:cd04100 80 LEVLS 84
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
126-399 |
1.67e-23 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 104.49 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 126 GQRVKVFGWVHRLRRQGkNLMFLVLRDGTGYLQCVLSDDLCQCYNGVV--LSTESSVAVYGTLNLTPKG----KQAPGGH 199
Cdd:PLN02903 72 GSRVTLCGWVDLHRDMG-GLTFLDVRDHTGIVQVVTLPDEFPEAHRTAnrLRNEYVVAVEGTVRSRPQEspnkKMKTGSV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 200 EL---SCDFWELVGLA------PAGGADNLINEEsdvdVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDR-GYCEV 269
Cdd:PLN02903 151 EVvaeSVDILNVVTKSlpflvtTADEQKDSIKEE----VRLRYRVLDLRRPQMNANLRLRHRVVKLIRRYLEDVhGFVEI 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 270 TTPTLVQTQVEGGatlfkLDYF-------GEEAFLTQSSQLYLETCLPALGD-VFCIAQSYRAEQSRTRRHlAEFTHVEA 341
Cdd:PLN02903 227 ETPILSRSTPEGA-----RDYLvpsrvqpGTFYALPQSPQLFKQMLMVSGFDrYYQIARCFRDEDLRADRQ-PEFTQLDM 300
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1781913009 342 ECPFLTFEDLLNRLEDLVCDVVDRVLKSPVAsivyelnpnfkppkRPFRRMNYSDAIE 399
Cdd:PLN02903 301 ELAFTPLEDMLKLNEDLIRQVFKEIKGVQLP--------------NPFPRLTYAEAMS 344
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
126-400 |
1.58e-19 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 92.05 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 126 GQRVKVFGWVHRLRRQGkNLMFLVLRDGTGYLQCVLSDDLCQCYNGVVLSTESSVAVYGTLNLTPKG----KQAPGGHEL 201
Cdd:PRK00476 17 GQTVTLCGWVHRRRDHG-GLIFIDLRDREGIVQVVFDPDAEAFEVAESLRSEYVIQVTGTVRARPEGtvnpNLPTGEIEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 202 SCDFWELvgLAPaggADNL---INEESDV--DVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQ 276
Cdd:PRK00476 96 LASELEV--LNK---SKTLpfpIDDEEDVseELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDDNGFLEIETPILTK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 277 TQVEgGATlfklDYF-------GEeaF--LTQSSQL------------YletclpalgdvFCIAQSYRAEQSRTRRhLAE 335
Cdd:PRK00476 171 STPE-GAR----DYLvpsrvhpGK--FyaLPQSPQLfkqllmvagfdrY-----------YQIARCFRDEDLRADR-QPE 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1781913009 336 FTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPVasivyelnpnfkppKRPFRRMNYSDAIEW 400
Cdd:PRK00476 232 FTQIDIEMSFVTQEDVMALMEGLIRHVFKEVLGVDL--------------PTPFPRMTYAEAMRR 282
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
126-541 |
6.41e-19 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 89.76 E-value: 6.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 126 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLS-DDLCQCYNGVVLSTESS--VAVYGTLNLTPKGkqapgghELS 202
Cdd:PRK00484 54 EIEVSVAGRVMLKRVMGK-ASFATLQDGSGRIQLYVSkDDVGEEALEAFKKLDLGdiIGVEGTLFKTKTG-------ELS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 203 --CDFWELV------------GLapaggadnlineeSDVDVQLNNRHM-MIRGENMSKILKARSMITRCFRDHFFDRGYC 267
Cdd:PRK00484 126 vkATELTLLtkslrplpdkfhGL-------------TDVETRYRQRYVdLIVNPESRETFRKRSKIISAIRRFLDNRGFL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 268 EVTTPTLvQTqVEGGATL--FK--LDYFGEEAFLTQSSQLYLETCLpaLGD---VFCIAQSYRAEQSRTrRHLAEFTHVE 340
Cdd:PRK00484 193 EVETPML-QP-IAGGAAArpFIthHNALDIDLYLRIAPELYLKRLI--VGGferVYEIGRNFRNEGIDT-RHNPEFTMLE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 341 AECPFLTFEDLLNRLEDLVCDVVDRVLKSPVasIVY---ELnpNFKPpkrPFRRMNYSDAI-----------------EW 400
Cdd:PRK00484 268 FYQAYADYNDMMDLTEELIRHLAQAVLGTTK--VTYqgtEI--DFGP---PFKRLTMVDAIkeytgvdfddmtdeearAL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 401 LKEHDVKKEDgtFYEFGDDIPEAPERLMTDTINEPILLCRFPVEI----KsfymqRCPEDPRLTESVDVlmpnvgeIVGG 476
Cdd:PRK00484 341 AKELGIEVEK--SWGLGKLINELFEEFVEPKLIQPTFITDYPVEIsplaK-----RHREDPGLTERFEL-------FIGG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 477 SmrswdseEILEGYKrEGIDPApyywytDQRK----------------------------YGTCPHGGYGLGLERFLSWI 528
Cdd:PRK00484 407 R-------EIANAFS-ELNDPI------DQRErfeaqveakeagddeamfmdedflraleYGMPPTGGLGIGIDRLVMLL 472
|
490
....*....|...
gi 1781913009 529 LNRYHIRDVCLYP 541
Cdd:PRK00484 473 TDSPSIRDVILFP 485
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
247-541 |
6.54e-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: 6.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 247 LKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGAtlfklDYF-------GEEAFLTQSSQLYLETCLPA-LGDVFCI 318
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTPEGAR-----DFLvpsrlhpGKFYALPQSPQLFKQLLMVSgFDRYFQI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 319 AQSYRAEQSRTRRHlAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKspvasivyelnpnfKPPKRPFRRMNYSDAI 398
Cdd:cd00777 76 ARCFRDEDLRADRQ-PEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG--------------VELTTPFPRMTYAEAM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 399 E-------W-----LKEHDvkKEDGTfYEFGDDIPEAPERLMTDTINEpillcrFPVEIKSfymqrcpedprltESVDVL 466
Cdd:cd00777 141 ErygfkflWivdfpLFEWD--EEEGR-LVSAHHPFTAPKEEDLDLLEK------DPEDARA-------------QAYDLV 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1781913009 467 MpNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYY----WYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYP 541
Cdd:cd00777 199 L-NGVELGGGSIRIHDPDIQEKVFEILGLSEEEAEekfgFLLEAFKYGAPPHGGIALGLDRLVMLLTGSESIRDVIAFP 276
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
126-399 |
1.17e-17 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 86.58 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 126 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLC--QCYN-GVVLSTESSVAVYGTLNLTPKGKQAP----GG 198
Cdd:PRK12820 18 GREVCLAGWVDAFRDHGE-LLFIHLRDRNGFIQAVFSPEAApaDVYElAASLRAEFCVALQGEVQKRLEETENPhietGD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 199 HELSCDfwELVGLAPA------------------GGADNlINEesdvDVQLNNRHMMIRGENMSKILKARSMITRCFRDH 260
Cdd:PRK12820 97 IEVFVR--ELSILAASealpfaisdkamtagagsAGADA-VNE----DLRLQYRYLDIRRPAMQDHLAKRHRIIKCARDF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 261 FFDRGYCEVTTPTLVQTQVEGGATLFKLDYFGEEAF--LTQSSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHlAEFT 337
Cdd:PRK12820 170 LDSRGFLEIETPILTKSTPEGARDYLVPSRIHPKEFyaLPQSPQLFKQLLMIAgFERYFQLARCFRDEDLRPNRQ-PEFT 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1781913009 338 HVEAECPFLTFEDLLNRLEDLVCDVVDrvlkspVASIvyELNpnfkppkRPFRRMNYSDAIE 399
Cdd:PRK12820 249 QLDIEASFIDEEFIFELIEELTARMFA------IGGI--ALP-------RPFPRMPYAEAMD 295
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
126-400 |
2.14e-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: 85.44 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 126 GQRVKVFGWVHRLRRQGkNLMFLVLRDGTGYLQCVLSDDlcqcYNGVVLST------ESSVAVYGTLNLTPKG----KQA 195
Cdd:COG0173 16 GQEVTLSGWVHRRRDHG-GLIFIDLRDRYGITQVVFDPD----DSAEAFEKaeklrsEYVIAVTGKVRARPEGtvnpKLP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 196 PGGHELSCDfwELVGLAPaggADNL---INEESDV--DVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVT 270
Cdd:COG0173 91 TGEIEVLAS--ELEILNK---AKTPpfqIDDDTDVseELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDENGFLEIE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 271 TPTLVQTQVEgGATlfklDYF-------GEeaF--LTQSSQL------------YletclpalgdvFCIAQSYRAEQSRT 329
Cdd:COG0173 166 TPILTKSTPE-GAR----DYLvpsrvhpGK--FyaLPQSPQLfkqllmvsgfdrY-----------FQIARCFRDEDLRA 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1781913009 330 RRHlAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKspvasivYELnpnfkppKRPFRRMNYSDAIEW 400
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 ... |
129-209 |
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 1781913009 129 VKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVL-SDDLCQCYNgvVLSTESSVAVYGTLNLTPKgkqapGGHELSCDFWE 207
Cdd:pfam01336 1 VTVAGRVTSIRRSGGKLLFLTLRDGTGSIQVVVfKEEAEKLAK--KLKEGDVVRVTGKVKKRKG-----GELELVVEEIE 73
|
..
gi 1781913009 208 LV 209
Cdd:pfam01336 74 LL 75
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
129-548 |
1.88e-13 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 73.14 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 129 VKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLS-------DDLCQCYngVVLSTESSVAVYGTLNLTPKGkqapgghEL 201
Cdd:PTZ00385 110 VRVAGRVTSVRDIGK-IIFVTIRSNGNELQVVGQvgehftrEDLKKLK--VSLRVGDIIGADGVPCRMQRG-------EL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 202 SCDFWELVGLAPAGGADNLINEE-------SDVDVQLNNRHM-MIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPT 273
Cdd:PTZ00385 180 SVAASRMLILSPYVCTDQVVCPNlrgftvlQDNDVKYRYRFTdMMTNPCVIETIKKRHVMLQALRDYFNERNFVEVETPV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 274 LVQTQVEGGATLFKLDYFGEEA--FLTQSSQLYLETCL-PALGDVFCIAQSYRAEQSrTRRHLAEFTHVEAECPFLTFED 350
Cdd:PTZ00385 260 LHTVASGANAKSFVTHHNANAMdlFLRVAPELHLKQCIvGGMERIYEIGKVFRNEDA-DRSHNPEFTSCEFYAAYHTYED 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 351 LLNRLEDLVCDVVDRVLKSPVASIVYEL---NPNFKPPKRPFRRMNYSDAI------EWLKEHDVKKEDGTFY----EFG 417
Cdd:PTZ00385 339 LMPMTEDIFRQLAMRVNGTTVVQIYPENahgNPVTVDLGKPFRRVSVYDEIqrmsgvEFPPPNELNTPKGIAYmsvvMLR 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 418 DDIPEAPER------------LMTDTINEPILLCRFPVEIKSFYMQRCPEdPRLTESVDVLMPNVgEIVGGSMRSWDSEE 485
Cdd:PTZ00385 419 YNIPLPPVRtaakmfeklidfFITDRVVEPTFVMDHPLFMSPLAKEQVSR-PGLAERFELFVNGI-EYCNAYSELNDPHE 496
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1781913009 486 ILEGYKREGID-------PAPY-YWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCR 548
Cdd:PTZ00385 497 QYHRFQQQLVDrqggdeeAMPLdETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFPLLRQDIR 567
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
226-541 |
6.69e-12 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 67.78 E-value: 6.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 226 DVDVQLNNRHM-MIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLvqTQVEGGAT----LFKLDYFGEEAFLTQS 300
Cdd:PRK12445 162 DQEVRYRQRYLdLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMM--QVIPGGASarpfITHHNALDLDMYLRIA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 301 SQLYLET-CLPALGDVFCIAQSYRAEqSRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVL---KSPVASIVY 376
Cdd:PRK12445 240 PELYLKRlVVGGFERVFEINRNFRNE-GISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLgttKVTYGEHVF 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 377 ELNPNFKP-----------PKRPFRRMNYSDAIEWLKEH---DVKKEDGtfyeFGDDIPEAPERLMTDTINEPILLCRFP 442
Cdd:PRK12445 319 DFGKPFEKltmreaikkyrPETDMADLDNFDAAKALAESigiTVEKSWG----LGRIVTEIFDEVAEAHLIQPTFITEYP 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 443 VEIKSFyMQRCPEDPRLTESVDVLMPNvGEIVGGSMRSWDSEEILEGY------KREGIDPAPYYW--YTDQRKYGTCPH 514
Cdd:PRK12445 395 AEVSPL-ARRNDVNPEITDRFEFFIGG-REIGNGFSELNDAEDQAERFqeqvnaKAAGDDEAMFYDedYVTALEYGLPPT 472
|
330 340
....*....|....*....|....*..
gi 1781913009 515 GGYGLGLERFLSWILNRYHIRDVCLYP 541
Cdd:PRK12445 473 AGLGIGIDRMIMLFTNSHTIRDVILFP 499
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
128-236 |
8.22e-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: 8.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 128 RVKVFGWVHRLRRQGKNLmFLVLRDGTGYLQCVLSDDLCQ--CYNGVVLSTESSVAVYGTLNLTPKgkqAPGGHELSCDF 205
Cdd:cd04319 1 KVTLAGWVYRKREVGKKA-FIVLRDSTGIVQAVFSKDLNEeaYREAKKVGIESSVIVEGAVKADPR---APGGAEVHGEK 76
|
90 100 110
....*....|....*....|....*....|..
gi 1781913009 206 WELVGLapaggADNL-INEESDVDVQLNNRHM 236
Cdd:cd04319 77 LEIIQN-----VEFFpITEDASDEFLLDVRHL 103
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
126-201 |
1.45e-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: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 126 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVL-----SDDLCQCYNGvvLSTESSVAVYGTLNLTPKgkqAPGGHE 200
Cdd:cd04316 12 GEEVTVAGWVHEIRDLGG-IKFVILRDREGIVQVTApkkkvDKELFKTVRK--LSRESVISVTGTVKAEPK---APNGVE 85
|
.
gi 1781913009 201 L 201
Cdd:cd04316 86 I 86
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
247-461 |
1.43e-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: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 247 LKARSMITRCFRDHFFDRGYCEVTTPTLVQTqvegGAT-----LFKLDYFGEEAfltQSSQLYLETC--------LPA-L 312
Cdd:COG2269 6 LRARARLLAAIRAFFAERGVLEVETPALSVA----PGTdphldSFATEFIGPDG---GGRPLYLHTSpefamkrlLAAgS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 313 GDVFCIAQSYRAEQsRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSpvasivyelnpnfkppkrPFRRM 392
Cdd:COG2269 79 GPIYQIAKVFRNGE-RGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAAGFA------------------PAERL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 393 NYSDA-----------------IEWLKEHDVKKEDgtfyefGDDIPEAPERLMTDTI------NEPILLCRFPVEiksfy 449
Cdd:COG2269 140 SYQEAflrylgidpltadldelAAAAAAAGLRVAD------DDDRDDLLDLLLSERVepqlgrDRPTFLYDYPAS----- 208
|
250
....*....|....*..
gi 1781913009 450 mQ-----RCPEDPRLTE 461
Cdd:COG2269 209 -QaalarISPDDPRVAE 224
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
129-204 |
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 1781913009 129 VKVFGWVhRLRRQGKNLMFLVLRDGTGY--LQCVLSDDLCQCYNGVVLSTESSVAVYGTLNLTPKGKQApggHELSCD 204
Cdd:cd04318 2 VTVNGWV-RSVRDSKKISFIELNDGSCLknLQVVVDKELTNFKEILKLSTGSSIRVEGVLVKSPGAKQP---FELQAE 75
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
129-541 |
7.68e-10 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 61.55 E-value: 7.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 129 VKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVL----SDDLCQCYNGVVLSTESS--VAVYGTLNLTPKGkqapgghELS 202
Cdd:PLN02502 111 VSVAGRIMAKRAFGK-LAFYDLRDDGGKIQLYAdkkrLDLDEEEFEKLHSLVDRGdiVGVTGTPGKTKKG-------ELS 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 203 CDFWELVGLAPA-----GGADNLineeSDVDVQLNNRHM-MIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLvQ 276
Cdd:PLN02502 183 IFPTSFEVLTKCllmlpDKYHGL----TDQETRYRQRYLdLIANPEVRDIFRTRAKIISYIRRFLDDRGFLEVETPML-N 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 277 TQVeGGATL--FKLDY--FGEEAFLTQSSQLYL-ETCLPALGDVFCIAQSYRAEQSRTrRHLAEFTHVEAECPFLTFEDL 351
Cdd:PLN02502 258 MIA-GGAAArpFVTHHndLNMDLYLRIATELHLkRLVVGGFERVYEIGRQFRNEGIST-RHNPEFTTCEFYQAYADYNDM 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 352 LNRLEDLVCdvvdrvlkspvaSIVYELNPNFKPP--------KRPFRRMnysDAIEWLKE-------HDVKKEDGTFY-- 414
Cdd:PLN02502 336 MELTEEMVS------------GMVKELTGSYKIKyhgieidfTPPFRRI---SMISLVEEatgidfpADLKSDEANAYli 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 415 ----EFGDDIPEAP----------ERLMTDTINEPILLCRFPVEIkSFYMQRCPEDPRLTESVDVLmpnvgeIVGgsmrs 480
Cdd:PLN02502 401 aaceKFDVKCPPPQttgrllnelfEEFLEETLVQPTFVLDHPVEM-SPLAKPHRSKPGLTERFELF------ING----- 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 481 wdsEEILEGYKrEGIDPapyywyTDQRK----------------------------YGTCPHGGYGLGLERFLSWILNRY 532
Cdd:PLN02502 469 ---RELANAFS-ELTDP------VDQRErfeeqvkqhnagddeamaldedfctaleYGLPPTGGWGLGIDRLVMLLTDSA 538
|
....*....
gi 1781913009 533 HIRDVCLYP 541
Cdd:PLN02502 539 SIRDVIAFP 547
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
120-341 |
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 1781913009 120 ALEGYRGQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQCYN----GVVLSTESSVAVYGTLNLTPKGkqa 195
Cdd:PRK02983 645 ALDAPTGEEVSVSGRVLRIRDYGG-VLFADLRDWSGELQVLLDASRLEQGSladfRAAVDLGDLVEVTGTMGTSRNG--- 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 196 pgghELS--CDFWELVG--LAPaggadnLINEE---SDVDVQLNNRHM--MIRGENMSkILKARSMITRCFRDHFFDRGY 266
Cdd:PRK02983 721 ----TLSllVTSWRLAGkcLRP------LPDKWkglTDPEARVRQRYLdlAVNPEARD-LLRARSAVVRAVRETLVARGF 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 267 CEVTTPTLvQtQVEGGAT----LFKLDYFGEEAFLTQSSQLYLET-CLPALGDVFCIAQSYRAE-QSRTrrHLAEFTHVE 340
Cdd:PRK02983 790 LEVETPIL-Q-QVHGGANarpfVTHINAYDMDLYLRIAPELYLKRlCVGGVERVFELGRNFRNEgVDAT--HNPEFTLLE 865
|
.
gi 1781913009 341 A 341
Cdd:PRK02983 866 A 866
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
126-192 |
2.02e-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: 55.99 E-value: 2.02e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1781913009 126 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQCYNGVV-LSTESSVAVYGTLNLTPKG 192
Cdd:cd04317 14 GQEVTLCGWVQRRRDHGG-LIFIDLRDRYGIVQVVFDPEEAPEFELAEkLRNESVIQVTGKVRARPEG 80
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
64-541 |
2.89e-09 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 59.64 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 64 MKNIKKMWHREQMKnDSREKKEAEDNLR-----REKNLEEAKKIIIKNDPSLPEPACVKISALEGYR----GQRVK---- 130
Cdd:PTZ00417 57 MEGEKKVRSVQASK-DKKKEEEAEVDPRlyyenRSKFIQEQKAKGINPYPHKFERTITVPEFVEKYQdlasGEHLEdtil 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 131 -VFGWVHRLRRQGKNLMFLVLRDGTGYLQcVLSD---------DLCQCYNGVVLSTessvaVYGTLNLTPKGKQApgghE 200
Cdd:PTZ00417 136 nVTGRIMRVSASGQKLRFFDLVGDGAKIQ-VLANfafhdhtksNFAECYDKIRRGD-----IVGIVGFPGKSKKG----E 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 201 LSCDFWELVGLAPAGGADNLINEESDVDVQLNNRHM-MIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLvqTQV 279
Cdd:PTZ00417 206 LSIFPKETIILSPCLHMLPMKYGLKDTEIRYRQRYLdLMINESTRSTFITRTKIINYLRNFLNDRGFIEVETPTM--NLV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 280 EGGATlfkldyfgEEAFLTQSSQLYLE------TCLP-------ALGDVFCIAQSYRAEqSRTRRHLAEFTHVEAECPFL 346
Cdd:PTZ00417 284 AGGAN--------ARPFITHHNDLDLDlylriaTELPlkmlivgGIDKVYEIGKVFRNE-GIDNTHNPEFTSCEFYWAYA 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 347 TFEDLLNRLEDLVCDVVDRVLKSpvASIVY-----ELNP---NFKPpkrPFRRMNYSDAIEWLKE----------HDVKK 408
Cdd:PTZ00417 355 DFYDLIKWSEDFFSQLVMHLFGT--YKILYnkdgpEKDPieiDFTP---PYPKVSIVEELEKLTNtkleqpfdspETINK 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 409 EDGTFYEFGDDIPEAP------ERLMTDTI-----NEPILLCRFPvEIKSFYMQRCPEDPRLTESVDVLMPNvGEIVGGS 477
Cdd:PTZ00417 430 MINLIKENKIEMPNPPtaakllDQLASHFIenkypNKPFFIIEHP-QIMSPLAKYHRSKPGLTERLEMFICG-KEVLNAY 507
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1781913009 478 MRSWDSEEILEGYK-----REGIDPAPYYW---YTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYP 541
Cdd:PTZ00417 508 TELNDPFKQKECFSaqqkdREKGDAEAFQFdaaFCTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFP 579
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
243-537 |
1.20e-08 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 56.48 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 243 MSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQ-TQVEGGATLFKLDYFGEEAflTQSSQLYLETC--------LPAL- 312
Cdd:PRK09350 1 SIPNLLKRAKIIAEIRRFFADRGVLEVETPILSQaTVTDIHLVPFETRFVGPGA--SQGKTLWLMTSpeyhmkrlLAAGs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 313 GDVFCIAQSYRAEQSrTRRHLAEFTHVEAECPFLTFEDLLNRLEDLvcdvVDRVLKS-PVASIVYE--------LNPnFK 383
Cdd:PRK09350 79 GPIFQICKSFRNEEA-GRYHNPEFTMLEWYRPHYDMYRLMNEVDDL----LQQVLDCePAESLSYQqaflrylgIDP-LS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 384 PPKRPFRrmnysDAIEWLKEHDVKKEDgtfyefgDDIPEAPERLMTDTI------NEPILLCRFPVEIKSfYMQRCPEDP 457
Cdd:PRK09350 153 ADKTQLR-----EVAAKLGLSNIADEE-------EDRDTLLQLLFTFGVepnigkEKPTFVYHFPASQAA-LAKISTEDH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 458 RLTESVDVLMPNVgEIVGGSMRSWDSEEILEGYKR-------EGIDPAPyywyTDQR-----KYGTCPHGGYGLGLERFL 525
Cdd:PRK09350 220 RVAERFEVYFKGI-ELANGFHELTDAREQRQRFEQdnrkraaRGLPQQP----IDENliaalEAGLPDCSGVALGVDRLI 294
|
330
....*....|..
gi 1781913009 526 SWILNRYHIRDV 537
Cdd:PRK09350 295 MLALGAESISEV 306
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
129-191 |
5.40e-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: 5.40e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1781913009 129 VKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVLSDDlcqcyNGVV----------LSTESSVAVYGTLNLTPK 191
Cdd:cd04320 2 VLIRARVHTSRAQGAKLAFLVLRQQGYTIQGVLAAS-----AEGVskqmvkwagsLSKESIVDVEGTVKKPEE 69
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
261-461 |
7.83e-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: 54.09 E-value: 7.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 261 FFDRGYCEVTTPTLVQtqveGGATLFKLDYF--GEEAFLTQSSQLYLET----CLPAL-----GDVFCIAQSYRAEQsRT 329
Cdd:TIGR00462 2 FAERGVLEVETPLLSP----APVTDPHLDAFatEFVGPDGQGRPLYLQTspeyAMKRLlaagsGPIFQICKVFRNGE-RG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 330 RRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVvdrvlkspvasivyelnpnFKPPKRPFRRMNYSDA-IEWLKEHDVKK 408
Cdd:TIGR00462 77 RRHNPEFTMLEWYRPGFDYHDLMDEVEALLQEL-------------------LGDPFAPAERLSYQEAfLRYAGIDPLTA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1781913009 409 EDGTFYE----FGDDIPEAP------ERLMTDTI------NEPILLCRFPVEIKSFyMQRCPEDPRLTE 461
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 ... |
250-351 |
1.21e-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: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 250 RSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGATLFKLD------YFGEEAFLTQSSQLYLET----CLPALGD-VFCI 318
Cdd:cd00768 2 RSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHEPKDllpvgaENEEDLYLRPTLEPGLVRlfvsHIRKLPLrLAEI 81
|
90 100 110
....*....|....*....|....*....|....
gi 1781913009 319 AQSYRAEQSRTR-RHLAEFTHVEAECPFLTFEDL 351
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 ... |
128-209 |
1.94e-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: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781913009 128 RVKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVLSDDLCQCYNGV-VLSTESSVAVYGTLNLtpkgKQAPGGHELSCdfW 206
Cdd:cd04321 1 KVTLNGWIDRKPRIVKKLSFADLRDPNGDIIQLVSTAKKDAFSLLkSITAESPVQVRGKLQL----KEAKSSEKNDE--W 74
|
...
gi 1781913009 207 ELV 209
Cdd:cd04321 75 ELV 77
|
|
| |
