|
Name |
Accession |
Description |
Interval |
E-value |
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
236-555 |
2.11e-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: 2.11e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 236 DVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYL 315
Cdd:cd00776 3 NLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQLYK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 316 ETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFL-TFEDLLNRLEDLVCDVVDRVLKSPVASI--VYELNPNF 392
Cdd:cd00776 83 EMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAKELelVNQLNREL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 393 KPPKRPFRRMNYSDAIEWLKEHDVKKEDgtfyEFGDDIPEAPERLMTDTI-NEPILLCRFPVEIKSFYMQRCPEDPRLTE 471
Cdd:cd00776 163 LKPLEPFPRITYDEAIELLREKGVEEEV----KWGEDLSTEHERLLGEIVkGDPVFVTDYPKEIKPFYMKPDDDNPETVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 472 SVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYP 551
Cdd:cd00776 239 SFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
....
gi 193806326 552 RFLQ 555
Cdd:cd00776 319 RDPK 322
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
126-559 |
1.51e-146 |
|
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl/asparaginyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439788 [Multi-domain] Cd Length: 430 Bit Score: 428.70 E-value: 1.51e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 126 VKIS-ALEGYRGQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQCYNGVV-LSTESSVAVYGTLNLTPKgk 203
Cdd:COG0017 3 TYIKdLLPEHVGQEVTVAGWVRTKRDSGG-ISFLILRDGSGFIQVVVKKDKLENFEEAKkLTTESSVEVTGTVVESPR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 204 qAPGGHELSCDFWELVGLA----PaggadnLINEESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEV 279
Cdd:COG0017 80 -APQGVELQAEEIEVLGEAdepyP------LQPKRHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVEV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 280 TTPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFE 359
Cdd:COG0017 153 HTPIITASATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMALEKVYTFGPTFRAEKSNTRRHLAEFWMIEPEMAFADLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 360 DLLNRLEDLVCDVVDRVLKSPVASI-VYELNPNF--KPPKRPFRRMNYSDAIEWLKEHDVKkedgtfYEFGDDI-PEApE 435
Cdd:COG0017 233 DVMDLAEEMLKYIIKYVLENCPEELeFLGRDVERleKVPESPFPRITYTEAIEILKKSGEK------VEWGDDLgTEH-E 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 436 RLMTDTI-NEPILLCRFPVEIKSFYMQRCPEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYT 514
Cdd:COG0017 306 RYLGEEFfKKPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAPGIGEIIGGSQREHRYDVLVERIKEKGLDPEDYEWYL 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 193806326 515 DQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 559
Cdd:COG0017 386 DLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
136-559 |
2.18e-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: 2.18e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 136 GQRVKVFGWVHRlRRQGKNLMFLVLRDGT--GYLQCVLSDDLCQCYNGVV--LSTESSVAVYGTLNLTPKGKQapgGHEL 211
Cdd:TIGR00457 16 GDEVTVSGWVRT-KRSSKKIIFLELNDGSslGPIQAVINGEDNPYLFQLLksLTTGSSVSVTGKVVESPGKGQ---PVEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 212 SCDFWELVGLAPAGGADNLInEESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEG 291
Cdd:TIGR00457 92 QVKKIEVVGEAEPDDYPLQK-KEHSLEFLRDIAHLRLRTNTLGAVMRVRNALSQAIHRYFQENGFTWVSPPILTSNDCEG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 292 GATLFKL---------DYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFEDLL 362
Cdd:TIGR00457 171 AGELFRVstgnidfsqDFFGKEAYLTVSGQLYLETYALALSKVYTFGPTFRAEKSNTSRHLSEFWMIEPEMAFANLNDLL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 363 NRLEDLVCDVVDRVLKSpVASIVYELNPNFKPPKRP---------FRRMNYSDAIEWLKEHDVKKEDGTFyeFGDDIPEA 433
Cdd:TIGR00457 251 QLAETLIKYIIKAVLEN-CSQELKFLEKNFDKDLIKrleniinnkFARITYTDAIEILKESDKNFEYEDF--WGDDLQTE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 434 PERLMTDTI-NEPILLCRFPVEIKSFYMQRCpEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYW 512
Cdd:TIGR00457 328 HERFLAEEYfKPPVFVTNYPKDIKAFYMKLN-DDGKTVAAMDLLAPGIGEIIGGSEREDDLDKLENRMKEMGLDTDALNW 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 193806326 513 YTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 559
Cdd:TIGR00457 407 YLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGNINF 453
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
132-559 |
1.44e-110 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 337.08 E-value: 1.44e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 132 EGYRGQRVKVFGWVHRlRRQGKNLMFLVLRDGTGY--LQCVLSDDLCqcYNGVV--LSTESSVAVYGTLNLTPKgkqAPG 207
Cdd:PRK03932 12 GKYVGQEVTVRGWVRT-KRDSGKIAFLQLRDGSCFkqLQVVKDNGEE--YFEEIkkLTTGSSVIVTGTVVESPR---AGQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 208 GHELSCDFWELVGLAPAggaDNLINE-ESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQ 286
Cdd:PRK03932 86 GYELQATKIEVIGEDPE---DYPIQKkRHSIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVDTPIITA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 287 TQVEGGATLFKL---------DYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLT 357
Cdd:PRK03932 163 SDCEGAGELFRVttldldfskDFFGKEAYLTVSGQLYAEAYAMALGKVYTFGPTFRAENSNTRRHLAEFWMIEPEMAFAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 358 FEDLLNRLEDLVCDVVDRVL-----------KSPVASIVYELNpNFKPPkrPFRRMNYSDAIEWLKEHDVKKEDGTfyEF 426
Cdd:PRK03932 243 LEDNMDLAEEMLKYVVKYVLencpddleflnRRVDKGDIERLE-NFIES--PFPRITYTEAIEILQKSGKKFEFPV--EW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 427 GDDI--PEapERLMTDTINE-PILLCRFPVEIKSFYMQRCPEDpRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKRE 503
Cdd:PRK03932 318 GDDLgsEH--ERYLAEEHFKkPVFVTNYPKDIKAFYMRLNPDG-KTVAAMDLLAPGIGEIIGGSQREERLDVLEARIKEL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 193806326 504 GIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 559
Cdd:PRK03932 395 GLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
236-552 |
1.30e-105 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 319.90 E-value: 1.30e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 236 DVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGATLFKL------DYFgeeaFLTQ 309
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVpsralgKFY----ALPQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 310 SSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHLaEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPvasiVYEL 388
Cdd:pfam00152 77 SPQLYKQLLMVAgFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIA----KELE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 389 NPNFKPPKRPFRRMNYSDAIEWLKEHDVkkedgtfYEFGDDIPEAPERLMTD-----TINEPILLCRFPVEIKSFYMQRC 463
Cdd:pfam00152 152 GGTLLDLKKPFPRITYAEAIEKLNGKDV-------EELGYGSDKPDLRFLLElvidkNKFNPLWVTDFPAEHHPFTMPKD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 464 PEDPRLTESVDVLMPNVgEIVGGSMRSWDSEEILEGYKREGIDP----APYYWYTDQRKYGTCPHGGYGLGLERFLSWIL 539
Cdd:pfam00152 225 EDDPALAEAFDLVLNGV-EIGGGSIRIHDPELQEERFEEQGLDPeeaeEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLT 303
|
330
....*....|...
gi 193806326 540 NRYHIRDVCLYPR 552
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 ... |
138-220 |
6.27e-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: 6.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 138 RVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQ-CYNGVVLSTESSVAVYGTLNLTPKGKQAPGGHELSCDFW 216
Cdd:cd04323 1 RVKVFGWVHRLRSQKK-LMFLVLRDGTGFLQCVLSKKLVTeFYDAKSLTQESSVEVTGEVKEDPRAKQAPGGYELQVDYL 79
|
....
gi 193806326 217 ELVG 220
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 ... |
139-219 |
1.11e-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: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 139 VKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVL-SDDLCQCYNgvVLSTESSVAVYGTLNLTPKgkqapGGHELSCDFWE 217
Cdd:pfam01336 1 VTVAGRVTSIRRSGGKLLFLTLRDGTGSIQVVVfKEEAEKLAK--KLKEGDVVRVTGKVKKRKG-----GELELVVEEIE 73
|
..
gi 193806326 218 LV 219
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 ... |
236-555 |
2.11e-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: 2.11e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 236 DVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYL 315
Cdd:cd00776 3 NLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQLYK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 316 ETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFL-TFEDLLNRLEDLVCDVVDRVLKSPVASI--VYELNPNF 392
Cdd:cd00776 83 EMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAKELelVNQLNREL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 393 KPPKRPFRRMNYSDAIEWLKEHDVKKEDgtfyEFGDDIPEAPERLMTDTI-NEPILLCRFPVEIKSFYMQRCPEDPRLTE 471
Cdd:cd00776 163 LKPLEPFPRITYDEAIELLREKGVEEEV----KWGEDLSTEHERLLGEIVkGDPVFVTDYPKEIKPFYMKPDDDNPETVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 472 SVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYP 551
Cdd:cd00776 239 SFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
....
gi 193806326 552 RFLQ 555
Cdd:cd00776 319 RDPK 322
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
126-559 |
1.51e-146 |
|
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl/asparaginyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439788 [Multi-domain] Cd Length: 430 Bit Score: 428.70 E-value: 1.51e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 126 VKIS-ALEGYRGQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQCYNGVV-LSTESSVAVYGTLNLTPKgk 203
Cdd:COG0017 3 TYIKdLLPEHVGQEVTVAGWVRTKRDSGG-ISFLILRDGSGFIQVVVKKDKLENFEEAKkLTTESSVEVTGTVVESPR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 204 qAPGGHELSCDFWELVGLA----PaggadnLINEESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEV 279
Cdd:COG0017 80 -APQGVELQAEEIEVLGEAdepyP------LQPKRHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVEV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 280 TTPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFE 359
Cdd:COG0017 153 HTPIITASATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMALEKVYTFGPTFRAEKSNTRRHLAEFWMIEPEMAFADLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 360 DLLNRLEDLVCDVVDRVLKSPVASI-VYELNPNF--KPPKRPFRRMNYSDAIEWLKEHDVKkedgtfYEFGDDI-PEApE 435
Cdd:COG0017 233 DVMDLAEEMLKYIIKYVLENCPEELeFLGRDVERleKVPESPFPRITYTEAIEILKKSGEK------VEWGDDLgTEH-E 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 436 RLMTDTI-NEPILLCRFPVEIKSFYMQRCPEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYT 514
Cdd:COG0017 306 RYLGEEFfKKPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAPGIGEIIGGSQREHRYDVLVERIKEKGLDPEDYEWYL 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 193806326 515 DQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 559
Cdd:COG0017 386 DLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
136-559 |
2.18e-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: 2.18e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 136 GQRVKVFGWVHRlRRQGKNLMFLVLRDGT--GYLQCVLSDDLCQCYNGVV--LSTESSVAVYGTLNLTPKGKQapgGHEL 211
Cdd:TIGR00457 16 GDEVTVSGWVRT-KRSSKKIIFLELNDGSslGPIQAVINGEDNPYLFQLLksLTTGSSVSVTGKVVESPGKGQ---PVEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 212 SCDFWELVGLAPAGGADNLInEESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEG 291
Cdd:TIGR00457 92 QVKKIEVVGEAEPDDYPLQK-KEHSLEFLRDIAHLRLRTNTLGAVMRVRNALSQAIHRYFQENGFTWVSPPILTSNDCEG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 292 GATLFKL---------DYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFEDLL 362
Cdd:TIGR00457 171 AGELFRVstgnidfsqDFFGKEAYLTVSGQLYLETYALALSKVYTFGPTFRAEKSNTSRHLSEFWMIEPEMAFANLNDLL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 363 NRLEDLVCDVVDRVLKSpVASIVYELNPNFKPPKRP---------FRRMNYSDAIEWLKEHDVKKEDGTFyeFGDDIPEA 433
Cdd:TIGR00457 251 QLAETLIKYIIKAVLEN-CSQELKFLEKNFDKDLIKrleniinnkFARITYTDAIEILKESDKNFEYEDF--WGDDLQTE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 434 PERLMTDTI-NEPILLCRFPVEIKSFYMQRCpEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYW 512
Cdd:TIGR00457 328 HERFLAEEYfKPPVFVTNYPKDIKAFYMKLN-DDGKTVAAMDLLAPGIGEIIGGSEREDDLDKLENRMKEMGLDTDALNW 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 193806326 513 YTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 559
Cdd:TIGR00457 407 YLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGNINF 453
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
132-559 |
1.44e-110 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 337.08 E-value: 1.44e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 132 EGYRGQRVKVFGWVHRlRRQGKNLMFLVLRDGTGY--LQCVLSDDLCqcYNGVV--LSTESSVAVYGTLNLTPKgkqAPG 207
Cdd:PRK03932 12 GKYVGQEVTVRGWVRT-KRDSGKIAFLQLRDGSCFkqLQVVKDNGEE--YFEEIkkLTTGSSVIVTGTVVESPR---AGQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 208 GHELSCDFWELVGLAPAggaDNLINE-ESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQ 286
Cdd:PRK03932 86 GYELQATKIEVIGEDPE---DYPIQKkRHSIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVDTPIITA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 287 TQVEGGATLFKL---------DYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLT 357
Cdd:PRK03932 163 SDCEGAGELFRVttldldfskDFFGKEAYLTVSGQLYAEAYAMALGKVYTFGPTFRAENSNTRRHLAEFWMIEPEMAFAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 358 FEDLLNRLEDLVCDVVDRVL-----------KSPVASIVYELNpNFKPPkrPFRRMNYSDAIEWLKEHDVKKEDGTfyEF 426
Cdd:PRK03932 243 LEDNMDLAEEMLKYVVKYVLencpddleflnRRVDKGDIERLE-NFIES--PFPRITYTEAIEILQKSGKKFEFPV--EW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 427 GDDI--PEapERLMTDTINE-PILLCRFPVEIKSFYMQRCPEDpRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKRE 503
Cdd:PRK03932 318 GDDLgsEH--ERYLAEEHFKkPVFVTNYPKDIKAFYMRLNPDG-KTVAAMDLLAPGIGEIIGGSQREERLDVLEARIKEL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 193806326 504 GIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 559
Cdd:PRK03932 395 GLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
236-552 |
1.30e-105 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 319.90 E-value: 1.30e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 236 DVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGATLFKL------DYFgeeaFLTQ 309
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVpsralgKFY----ALPQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 310 SSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHLaEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPvasiVYEL 388
Cdd:pfam00152 77 SPQLYKQLLMVAgFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIA----KELE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 389 NPNFKPPKRPFRRMNYSDAIEWLKEHDVkkedgtfYEFGDDIPEAPERLMTD-----TINEPILLCRFPVEIKSFYMQRC 463
Cdd:pfam00152 152 GGTLLDLKKPFPRITYAEAIEKLNGKDV-------EELGYGSDKPDLRFLLElvidkNKFNPLWVTDFPAEHHPFTMPKD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 464 PEDPRLTESVDVLMPNVgEIVGGSMRSWDSEEILEGYKREGIDP----APYYWYTDQRKYGTCPHGGYGLGLERFLSWIL 539
Cdd:pfam00152 225 EDDPALAEAFDLVLNGV-EIGGGSIRIHDPELQEERFEEQGLDPeeaeEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLT 303
|
330
....*....|...
gi 193806326 540 NRYHIRDVCLYPR 552
Cdd:pfam00152 304 GLESIREVIAFPK 316
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
136-559 |
3.45e-101 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 312.51 E-value: 3.45e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 136 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQCYNGVV--LSTESSVAVYGTLNLTPKgkqAPGGHELSC 213
Cdd:PRK05159 16 GEEVTLAGWVHEIRDLGG-IAFLILRDRSGIIQVVVKKKVDEELFETIkkLKRESVVSVTGTVKANPK---APGGVEVIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 214 DFWELVGLApaggADNL---INEES--DVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQ 288
Cdd:PRK05159 92 EEIEVLNKA----EEPLpldISGKVlaELDTRLDNRFLDLRRPRVRAIFKIRSEVLRAFREFLYENGFTEIFTPKIVASG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 289 VEGGATLFKLDYFGEEAFLTQSSQLYLETCLPALGD-VFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLT-FEDLLNRLE 366
Cdd:PRK05159 168 TEGGAELFPIDYFEKEAYLAQSPQLYKQMMVGAGFErVFEIGPVFRAEEHNTSRHLNEYTSIDVEMGFIDdHEDVMDLLE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 367 DLVCDVVDRVLKSPVASIVyELNPNFKPPKRPFRRMNYSDAIEWLKEHDVKKedgtfyEFGDDIPEAPERLMTDTINE-- 444
Cdd:PRK05159 248 NLLRYMYEDVAENCEKELE-LLGIELPVPETPIPRITYDEAIEILKSKGNEI------SWGDDLDTEGERLLGEYVKEey 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 445 ---PILLCRFPVEIKSFYMQRCPEDPRLTESVDVLMPNVgEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGT 521
Cdd:PRK05159 321 gsdFYFITDYPSEKRPFYTMPDEDDPEISKSFDLLFRGL-EITSGGQRIHRYDMLVESIKEKGLNPESFEFYLEAFKYGM 399
|
410 420 430
....*....|....*....|....*....|....*...
gi 193806326 522 CPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 559
Cdd:PRK05159 400 PPHGGFGLGLERLTMKLLGLENIREAVLFPRDRHRLTP 437
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
87-559 |
1.24e-54 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 193.00 E-value: 1.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 87 KNDSREKKEAEDNLRREKNLEEAKKIIIKNDP---------------SLPEPACVKISAL-EGYRGQRVKVFGWVHRLRR 150
Cdd:PLN02850 16 KAAKKAAAKAEKLRREATAKAAAASLEDEDDPlasnygdvpleelqsKVTGREWTDVSDLgEELAGSEVLIRGRVHTIRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 151 QGKnLMFLVLRDGTGYLQCVLSDDLCQCYNGVV-----LSTESSVAVYGTLNLTPKG-KQAPGGHELSCDFWELVGLAPA 224
Cdd:PLN02850 96 KGK-SAFLVLRQSGFTVQCVVFVSEVTVSKGMVkyakqLSRESVVDVEGVVSVPKKPvKGTTQQVEIQVRKIYCVSKALA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 225 GGADNLIN---EESDV---------------DVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQ 286
Cdd:PLN02850 175 TLPFNVEDaarSESEIekalqtgeqlvrvgqDTRLNNRVLDLRTPANQAIFRIQSQVCNLFREFLLSKGFVEIHTPKLIA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 287 TQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHLAEFTHveaecpfLTFEDLLNRL 365
Cdd:PLN02850 255 GASEGGSAVFRLDYKGQPACLAQSPQLHKQMAICGdFRRVFEIGPVFRAEDSFTHRHLCEFTG-------LDLEMEIKEH 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 366 EDLVCDVVDRVLKspvaSIVYELNPN-------------FKPPK--RPFRRMNYSDAIEWLKEHDVKKEDgtfyeFGDDI 430
Cdd:PLN02850 328 YSEVLDVVDELFV----AIFDGLNERckkeleaireqypFEPLKylPKTLRLTFAEGIQMLKEAGVEVDP-----LGDLN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 431 PEApERLMTDTINEP-----ILLCRFPVEIKSFYMQRCPEDPRLTESVDVLMPNvGEIVGGSMRSWDSEEILEGYKREGI 505
Cdd:PLN02850 399 TES-ERKLGQLVKEKygtdfYILHRYPLAVRPFYTMPCPDDPKYSNSFDVFIRG-EEIISGAQRVHDPELLEKRAEECGI 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 193806326 506 DPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 559
Cdd:PLN02850 477 DVKTISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPRDPQRLAP 530
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
248-552 |
1.17e-49 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 174.44 E-value: 1.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 248 IRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLvqTQV-----EGGATL----FKLDYFGEEAFLTQSSQLYLETC 318
Cdd:PRK06462 21 ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPII--SPStdplmGLGSDLpvkqISIDFYGVEYYLADSMILHKQLA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 319 LPALGDVFCIAQSYRAEQ--SRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPVASIvYELNPNFKPPK 396
Cdd:PRK06462 99 LRMLGKIFYLSPNFRLEPvdKDTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHEDEL-EFFGRDLPHLK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 397 RPFRRMNYSDAIEWLKEHDVKKEDgtFYEFGDDIpeapERLMTDTINEPILLCRFPVEIKSFYMQRCPEDPRLTESVDVL 476
Cdd:PRK06462 178 RPFKRITHKEAVEILNEEGCRGID--LEELGSEG----EKSLSEHFEEPFWIIDIPKGSREFYDREDPERPGVLRNYDLL 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193806326 477 MPN-VGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPR 552
Cdd:PRK06462 252 LPEgYGEAVSGGEREYEYEEIVERIREHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQPFPR 328
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
133-553 |
2.35e-49 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 179.42 E-value: 2.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 133 GYRGQRVKVFGWVHRLRRQGK-NLMFLVLRDGT--GYLQCVLSDDLCQCYNgvVLSTESSVAVYGTLNLTPKGKQAPGGH 209
Cdd:PLN02221 47 GLAGQKVRIGGWVKTGREQGKgTFAFLEVNDGScpANLQVMVDSSLYDLST--LVATGTCVTVDGVLKVPPEGKGTKQKI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 210 ELSCDFWELVGLAPAGGADnLINEESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQV 289
Cdd:PLN02221 125 ELSVEKVIDVGTVDPTKYP-LPKTKLTLEFLRDVLHLRSRTNSISAVARIRNALAFATHSFFQEHSFLYIHTPIITTSDC 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 290 EGGATLFKL----------------------------------------------------------------------- 298
Cdd:PLN02221 204 EGAGEMFQVttlinyterleqdlidnpppteadveaarlivkergevvaqlkaakaskeeitaavaelkiakeslahiee 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 299 -------------------DYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFE 359
Cdd:PLN02221 284 rsklkpglpkkdgkidyskDFFGRQAFLTVSGQLQVETYACALSSVYTFGPTFRAENSHTSRHLAEFWMVEPEIAFADLE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 360 DLLNRLEDLVCDVVDRVLKSPVASIvyEL-NPNFKP---------PKRPFRRMNYSDAIEWLKEHDVK-KEDGTFYEFGD 428
Cdd:PLN02221 364 DDMNCAEAYVKYMCKWLLDKCFDDM--ELmAKNFDSgcidrlrmvASTPFGRITYTEAIELLEEAVAKgKEFDNNVEWGI 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 429 DIPEAPERLMTDTI-NEPILLCRFPVEIKSFYMqRCPEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDP 507
Cdd:PLN02221 442 DLASEHERYLTEVLfQKPLIVYNYPKGIKAFYM-RLNDDEKTVAAMDVLVPKVGELIGGSQREERYDVIKQRIEEMGLPI 520
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 193806326 508 APYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRF 553
Cdd:PLN02221 521 EPYEWYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPRY 566
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
136-552 |
5.06e-49 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 178.63 E-value: 5.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 136 GQRVKVFGWVHRLRRQgKNLMFLVLRDGT--GYLQCVLSDDlCQCYNGV---VLSTESSVAVYGTLNLTPKGKQAPgghE 210
Cdd:PLN02603 107 GKTLNVMGWVRTLRAQ-SSVTFIEVNDGSclSNMQCVMTPD-AEGYDQVesgLITTGASVLVQGTVVSSQGGKQKV---E 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 211 LSCDFWELVGlapaggadnlineESDVDVQLNNR-----------HMMIRGENMSKILKARSMITRCFRDHFFDRGYCEV 279
Cdd:PLN02603 182 LKVSKIVVVG-------------KSDPSYPIQKKrvsreflrtkaHLRPRTNTFGAVARVRNALAYATHKFFQENGFVWV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 280 TTP-----------------TLVQTQVEGGATLFK-------------LDYFGEEAFLTQSSQLYLETCLPALGDVFCIA 329
Cdd:PLN02603 249 SSPiitasdcegageqfcvtTLIPNSAENGGSLVDdipktkdglidwsQDFFGKPAFLTVSGQLNGETYATALSDVYTFG 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 330 QSYRAEQSRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPV-----------ASIVYELNpnfKPPKRP 398
Cdd:PLN02603 329 PTFRAENSNTSRHLAEFWMIEPELAFADLNDDMACATAYLQYVVKYILENCKedmeffntwieKGIIDRLS---DVVEKN 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 399 FRRMNYSDAIEWLKEhdVKKEDGTFYEFGDDIPEAPERLMTDTI--NEPILLCRFPVEIKSFYMqRCPEDPRLTESVDVL 476
Cdd:PLN02603 406 FVQLSYTDAIELLLK--AKKKFEFPVKWGLDLQSEHERYITEEAfgGRPVIIRDYPKEIKAFYM-RENDDGKTVAAMDML 482
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193806326 477 MPNVGEIVGGSMRSwDSEEILEGYKRE-GIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPR 552
Cdd:PLN02603 483 VPRVGELIGGSQRE-ERLEYLEARLDElKLNKESYWWYLDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFPR 558
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
136-559 |
8.05e-46 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 169.40 E-value: 8.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 136 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCV--LSDDLCQCYNGVV--LSTESSVAVYGTLNLT--PKGKQAPGGH 209
Cdd:PTZ00401 78 DKTVLIRARVSTTRKKGK-MAFMVLRDGSDSVQAMaaVEGDVPKEMIDFIgqIPTESIVDVEATVCKVeqPITSTSHSDI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 210 ELSCDFWELVG---------LAPAGGADNLINEESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVT 280
Cdd:PTZ00401 157 ELKVKKIHTVTeslrtlpftLEDASRKESDEGAKVNFDTRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLIDSDFCEIH 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 281 TPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLT-F 358
Cdd:PTZ00401 237 SPKIINAPSEGGANVFKLEYFNRFAYLAQSPQLYKQMVLQGdVPRVFEVGPVFRSENSNTHRHLTEFVGLDVEMRINEhY 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 359 EDLLNRLEDLVCDVVDRVLKS-----------PVASIVYELNP-------------NFKPPKR----------PFRRMNY 404
Cdd:PTZ00401 317 YEVLDLAESLFNYIFERLATHtkelkavcqqyPFEPLVWKLTPermkelgvgviseGVEPTDKyqarvhnmdsRMLRINY 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 405 SDAIEWLKEHDVKKEDGTfyefgDDIPEAPERLMTDTINEP-----ILLCRFPVEIKSFYMQRCPEDPRLTESVDVLMPN 479
Cdd:PTZ00401 397 MHCIELLNTVLEEKMAPT-----DDINTTNEKLLGKLVKERygtdfFISDRFPSSARPFYTMECKDDERFTNSYDMFIRG 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 480 vGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 559
Cdd:PTZ00401 472 -EEISSGAQRIHDPDLLLARAKMLNVDLTPIKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFPRDPQRTTP 550
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
296-553 |
1.26e-43 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 163.66 E-value: 1.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 296 FKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDR 375
Cdd:PTZ00425 317 YKKDFFSKQAFLTVSGQLSLENLCSSMGDVYTFGPTFRAENSHTSRHLAEFWMIEPEIAFADLYDNMELAESYIKYCIGY 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 376 VLKSPVASIVY-ELNPNFKPPKR-------PFRRMNYSDAIEWLKEHDVKKEdgTFYEFGDDIPEAPERLMTDTI-NEPI 446
Cdd:PTZ00425 397 VLNNNFDDIYYfEENVETGLISRlknildeDFAKITYTNVIDLLQPYSDSFE--VPVKWGMDLQSEHERFVAEQIfKKPV 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 447 LLCRFPVEIKSFYMqRCPEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGG 526
Cdd:PTZ00425 475 IVYNYPKDLKAFYM-KLNEDQKTVAAMDVLVPKIGEVIGGSQREDNLERLDKMIKEKKLNMESYWWYRQLRKFGSHPHAG 553
|
250 260
....*....|....*....|....*..
gi 193806326 527 YGLGLERFLSWILNRYHIRDVCLYPRF 553
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 ... |
257-552 |
3.52e-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: 3.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 257 LKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGATLFKLDYF--GEEAFLTQSSQLYLETCLPA-LGDVFCIAQSYR 333
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNalGLDYYLRISPQLFKKRLMVGgLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 334 AEQSRTRrHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLkspvasIVYELNPNFKP--PKRPFRRMNYSDAIEWL 411
Cdd:cd00669 81 NEDLRAR-HQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVL------GVTAVTYGFELedFGLPFPRLTYREALERY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 412 KEhdvkkedgtfyefgddipeaperlmtdtinePILLCRFPVEIKSFYMQRCPEDPRLTESVDVLMPNVgEIVGGSMRSW 491
Cdd:cd00669 154 GQ-------------------------------PLFLTDYPAEMHSPLASPHDVNPEIADAFDLFINGV-EVGNGSSRLH 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193806326 492 DSEEILEGYKREGIDPAP----YYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPR 552
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 ... |
138-220 |
6.27e-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: 6.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 138 RVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQ-CYNGVVLSTESSVAVYGTLNLTPKGKQAPGGHELSCDFW 216
Cdd:cd04323 1 RVKVFGWVHRLRSQKK-LMFLVLRDGTGFLQCVLSKKLVTeFYDAKSLTQESSVEVTGEVKEDPRAKQAPGGYELQVDYL 79
|
....
gi 193806326 217 ELVG 220
Cdd:cd04323 80 EIIG 83
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
296-552 |
2.79e-27 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 116.51 E-value: 2.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 296 FKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDR 375
Cdd:PLN02532 363 FSKDFFSRPTYLTVSGRLHLESYACALGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAFSELEDAMNCAEDYFKFLCKW 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 376 VLKSPVA-----------SIVYELNPNFkppKRPFRRMNYSDAIEWLKEH-DVKKEdgTFYEFGddIPEAPERL--MTDT 441
Cdd:PLN02532 443 VLENCSEdmkfvskridkTISTRLEAII---SSSLQRISYTEAVDLLKQAtDKKFE--TKPEWG--IALTTEHLsyLADE 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 442 I-NEPILLCRFPVEIKSFYMqRCPEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYG 520
Cdd:PLN02532 516 IyKKPVIIYNYPKELKPFYV-RLNDDGKTVAAFDLVVPKVGTVITGSQNEERMDILNARIEELGLPREQYEWYLDLRRHG 594
|
250 260 270
....*....|....*....|....*....|..
gi 193806326 521 TCPHGGYGLGLERFLSWILNRYHIRDVCLYPR 552
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 ... |
138-220 |
2.84e-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: 2.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 138 RVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQCYNGVV--LSTESSVAVYGTLNLTPKGKQAPGGHELSCDF 215
Cdd:cd04100 1 EVTLAGWVHSRRDHGG-LIFIDLRDGSGIVQVVVNKEELGEFFEEAekLRTESVVGVTGTVVKRPEGNLATGEIELQAEE 79
|
....*
gi 193806326 216 WELVG 220
Cdd:cd04100 80 LEVLS 84
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
136-409 |
1.79e-23 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 104.49 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 136 GQRVKVFGWVHRLRRQGkNLMFLVLRDGTGYLQCVLSDDLCQCYNGVV--LSTESSVAVYGTLNLTPKG----KQAPGGH 209
Cdd:PLN02903 72 GSRVTLCGWVDLHRDMG-GLTFLDVRDHTGIVQVVTLPDEFPEAHRTAnrLRNEYVVAVEGTVRSRPQEspnkKMKTGSV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 210 EL---SCDFWELVGLA------PAGGADNLINEEsdvdVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDR-GYCEV 279
Cdd:PLN02903 151 EVvaeSVDILNVVTKSlpflvtTADEQKDSIKEE----VRLRYRVLDLRRPQMNANLRLRHRVVKLIRRYLEDVhGFVEI 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 280 TTPTLVQTQVEGGatlfkLDYF-------GEEAFLTQSSQLYLETCLPALGD-VFCIAQSYRAEQSRTRRHlAEFTHVEA 351
Cdd:PLN02903 227 ETPILSRSTPEGA-----RDYLvpsrvqpGTFYALPQSPQLFKQMLMVSGFDrYYQIARCFRDEDLRADRQ-PEFTQLDM 300
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 193806326 352 ECPFLTFEDLLNRLEDLVCDVVDRVLKSPVAsivyelnpnfkppkRPFRRMNYSDAIE 409
Cdd:PLN02903 301 ELAFTPLEDMLKLNEDLIRQVFKEIKGVQLP--------------NPFPRLTYAEAMS 344
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
136-410 |
1.77e-19 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 92.05 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 136 GQRVKVFGWVHRLRRQGkNLMFLVLRDGTGYLQCVLSDDLCQCYNGVVLSTESSVAVYGTLNLTPKG----KQAPGGHEL 211
Cdd:PRK00476 17 GQTVTLCGWVHRRRDHG-GLIFIDLRDREGIVQVVFDPDAEAFEVAESLRSEYVIQVTGTVRARPEGtvnpNLPTGEIEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 212 SCDFWELvgLAPaggADNL---INEESDV--DVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQ 286
Cdd:PRK00476 96 LASELEV--LNK---SKTLpfpIDDEEDVseELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDDNGFLEIETPILTK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 287 TQVEgGATlfklDYF-------GEeaF--LTQSSQL------------YletclpalgdvFCIAQSYRAEQSRTRRhLAE 345
Cdd:PRK00476 171 STPE-GAR----DYLvpsrvhpGK--FyaLPQSPQLfkqllmvagfdrY-----------YQIARCFRDEDLRADR-QPE 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193806326 346 FTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPVasivyelnpnfkppKRPFRRMNYSDAIEW 410
Cdd:PRK00476 232 FTQIDIEMSFVTQEDVMALMEGLIRHVFKEVLGVDL--------------PTPFPRMTYAEAMRR 282
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
257-551 |
6.95e-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: 6.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 257 LKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGAtlfklDYF-------GEEAFLTQSSQLYLETCLPA-LGDVFCI 328
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTPEGAR-----DFLvpsrlhpGKFYALPQSPQLFKQLLMVSgFDRYFQI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 329 AQSYRAEQSRTRRHlAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKspvasivyelnpnfKPPKRPFRRMNYSDAI 408
Cdd:cd00777 76 ARCFRDEDLRADRQ-PEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG--------------VELTTPFPRMTYAEAM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 409 E-------W-----LKEHDvkKEDGTfYEFGDDIPEAPERLMTDTINEpillcrFPVEIKSfymqrcpedprltESVDVL 476
Cdd:cd00777 141 ErygfkflWivdfpLFEWD--EEEGR-LVSAHHPFTAPKEEDLDLLEK------DPEDARA-------------QAYDLV 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193806326 477 MpNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYY----WYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYP 551
Cdd:cd00777 199 L-NGVELGGGSIRIHDPDIQEKVFEILGLSEEEAEekfgFLLEAFKYGAPPHGGIALGLDRLVMLLTGSESIRDVIAFP 276
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
136-551 |
7.95e-19 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 89.38 E-value: 7.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 136 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLS-DDLCQCYNGVVLSTESS--VAVYGTLNLTPKGkqapgghELS 212
Cdd:PRK00484 54 EIEVSVAGRVMLKRVMGK-ASFATLQDGSGRIQLYVSkDDVGEEALEAFKKLDLGdiIGVEGTLFKTKTG-------ELS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 213 --CDFWELV------------GLapaggadnlineeSDVDVQLNNRHM-MIRGENMSKILKARSMITRCFRDHFFDRGYC 277
Cdd:PRK00484 126 vkATELTLLtkslrplpdkfhGL-------------TDVETRYRQRYVdLIVNPESRETFRKRSKIISAIRRFLDNRGFL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 278 EVTTPTLvQTqVEGGATL--FK--LDYFGEEAFLTQSSQLYLETCLpaLGD---VFCIAQSYRAEQSRTrRHLAEFTHVE 350
Cdd:PRK00484 193 EVETPML-QP-IAGGAAArpFIthHNALDIDLYLRIAPELYLKRLI--VGGferVYEIGRNFRNEGIDT-RHNPEFTMLE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 351 AECPFLTFEDLLNRLEDLVCDVVDRVLKSPVasIVY---ELnpNFKPpkrPFRRMNYSDAI-----------------EW 410
Cdd:PRK00484 268 FYQAYADYNDMMDLTEELIRHLAQAVLGTTK--VTYqgtEI--DFGP---PFKRLTMVDAIkeytgvdfddmtdeearAL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 411 LKEHDVKKEDgtFYEFGDDIPEAPERLMTDTINEPILLCRFPVEI----KsfymqRCPEDPRLTESVDVlmpnvgeIVGG 486
Cdd:PRK00484 341 AKELGIEVEK--SWGLGKLINELFEEFVEPKLIQPTFITDYPVEIsplaK-----RHREDPGLTERFEL-------FIGG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 487 SmrswdseEILEGYKrEGIDPApyywytDQRK----------------------------YGTCPHGGYGLGLERFLSWI 538
Cdd:PRK00484 407 R-------EIANAFS-ELNDPI------DQRErfeaqveakeagddeamfmdedflraleYGMPPTGGLGIGIDRLVMLL 472
|
490
....*....|...
gi 193806326 539 LNRYHIRDVCLYP 551
Cdd:PRK00484 473 TDSPSIRDVILFP 485
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
136-409 |
1.56e-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: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 136 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLC--QCYN-GVVLSTESSVAVYGTLNLTPKGKQAP----GG 208
Cdd:PRK12820 18 GREVCLAGWVDAFRDHGE-LLFIHLRDRNGFIQAVFSPEAApaDVYElAASLRAEFCVALQGEVQKRLEETENPhietGD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 209 HELSCDfwELVGLAPA------------------GGADNlINEesdvDVQLNNRHMMIRGENMSKILKARSMITRCFRDH 270
Cdd:PRK12820 97 IEVFVR--ELSILAASealpfaisdkamtagagsAGADA-VNE----DLRLQYRYLDIRRPAMQDHLAKRHRIIKCARDF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 271 FFDRGYCEVTTPTLVQTQVEGGATLFKLDYFGEEAF--LTQSSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHlAEFT 347
Cdd:PRK12820 170 LDSRGFLEIETPILTKSTPEGARDYLVPSRIHPKEFyaLPQSPQLFKQLLMIAgFERYFQLARCFRDEDLRPNRQ-PEFT 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193806326 348 HVEAECPFLTFEDLLNRLEDLVCDVVDrvlkspVASIvyELNpnfkppkRPFRRMNYSDAIE 409
Cdd:PRK12820 249 QLDIEASFIDEEFIFELIEELTARMFA------IGGI--ALP-------RPFPRMPYAEAMD 295
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
136-410 |
2.58e-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: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 136 GQRVKVFGWVHRLRRQGkNLMFLVLRDGTGYLQCVLSDDlcqcYNGVVLST------ESSVAVYGTLNLTPKG----KQA 205
Cdd:COG0173 16 GQEVTLSGWVHRRRDHG-GLIFIDLRDRYGITQVVFDPD----DSAEAFEKaeklrsEYVIAVTGKVRARPEGtvnpKLP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 206 PGGHELSCDfwELVGLAPaggADNL---INEESDV--DVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVT 280
Cdd:COG0173 91 TGEIEVLAS--ELEILNK---AKTPpfqIDDDTDVseELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDENGFLEIE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 281 TPTLVQTQVEgGATlfklDYF-------GEeaF--LTQSSQL------------YletclpalgdvFCIAQSYRAEQSRT 339
Cdd:COG0173 166 TPILTKSTPE-GAR----DYLvpsrvhpGK--FyaLPQSPQLfkqllmvsgfdrY-----------FQIARCFRDEDLRA 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193806326 340 RRHlAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKspvasivYELnpnfkppKRPFRRMNYSDAIEW 410
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 ... |
139-219 |
1.11e-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: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 139 VKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVL-SDDLCQCYNgvVLSTESSVAVYGTLNLTPKgkqapGGHELSCDFWE 217
Cdd:pfam01336 1 VTVAGRVTSIRRSGGKLLFLTLRDGTGSIQVVVfKEEAEKLAK--KLKEGDVVRVTGKVKKRKG-----GELELVVEEIE 73
|
..
gi 193806326 218 LV 219
Cdd:pfam01336 74 LL 75
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
139-558 |
1.95e-13 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 73.14 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 139 VKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLS-------DDLCQCYngVVLSTESSVAVYGTLNLTPKGkqapgghEL 211
Cdd:PTZ00385 110 VRVAGRVTSVRDIGK-IIFVTIRSNGNELQVVGQvgehftrEDLKKLK--VSLRVGDIIGADGVPCRMQRG-------EL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 212 SCDFWELVGLAPAGGADNLINEE-------SDVDVQLNNRHM-MIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPT 283
Cdd:PTZ00385 180 SVAASRMLILSPYVCTDQVVCPNlrgftvlQDNDVKYRYRFTdMMTNPCVIETIKKRHVMLQALRDYFNERNFVEVETPV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 284 LVQTQVEGGATLFKLDYFGEEA--FLTQSSQLYLETCL-PALGDVFCIAQSYRAEQSrTRRHLAEFTHVEAECPFLTFED 360
Cdd:PTZ00385 260 LHTVASGANAKSFVTHHNANAMdlFLRVAPELHLKQCIvGGMERIYEIGKVFRNEDA-DRSHNPEFTSCEFYAAYHTYED 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 361 LLNRLEDLVCDVVDRVLKSPVASIVYEL---NPNFKPPKRPFRRMNYSDAI------EWLKEHDVKKEDGTFY----EFG 427
Cdd:PTZ00385 339 LMPMTEDIFRQLAMRVNGTTVVQIYPENahgNPVTVDLGKPFRRVSVYDEIqrmsgvEFPPPNELNTPKGIAYmsvvMLR 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 428 DDIPEAPER------------LMTDTINEPILLCRFPVEIKSFYMQRCPEdPRLTESVDVLMPNVgEIVGGSMRSWDSEE 495
Cdd:PTZ00385 419 YNIPLPPVRtaakmfeklidfFITDRVVEPTFVMDHPLFMSPLAKEQVSR-PGLAERFELFVNGI-EYCNAYSELNDPHE 496
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193806326 496 ILEGYKREGID-------PAPY-YWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCR 558
Cdd:PTZ00385 497 QYHRFQQQLVDrqggdeeAMPLdETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFPLLRQDIR 567
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
236-551 |
8.32e-12 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 67.78 E-value: 8.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 236 DVDVQLNNRHM-MIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLvqTQVEGGAT----LFKLDYFGEEAFLTQS 310
Cdd:PRK12445 162 DQEVRYRQRYLdLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMM--QVIPGGASarpfITHHNALDLDMYLRIA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 311 SQLYLET-CLPALGDVFCIAQSYRAEqSRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVL---KSPVASIVY 386
Cdd:PRK12445 240 PELYLKRlVVGGFERVFEINRNFRNE-GISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLgttKVTYGEHVF 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 387 ELNPNFKP-----------PKRPFRRMNYSDAIEWLKEH---DVKKEDGtfyeFGDDIPEAPERLMTDTINEPILLCRFP 452
Cdd:PRK12445 319 DFGKPFEKltmreaikkyrPETDMADLDNFDAAKALAESigiTVEKSWG----LGRIVTEIFDEVAEAHLIQPTFITEYP 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 453 VEIKSFyMQRCPEDPRLTESVDVLMPNvGEIVGGSMRSWDSEEILEGY------KREGIDPAPYYW--YTDQRKYGTCPH 524
Cdd:PRK12445 395 AEVSPL-ARRNDVNPEITDRFEFFIGG-REIGNGFSELNDAEDQAERFqeqvnaKAAGDDEAMFYDedYVTALEYGLPPT 472
|
330 340
....*....|....*....|....*..
gi 193806326 525 GGYGLGLERFLSWILNRYHIRDVCLYP 551
Cdd:PRK12445 473 AGLGIGIDRMIMLFTNSHTIRDVILFP 499
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
138-246 |
9.33e-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: 9.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 138 RVKVFGWVHRLRRQGKNLmFLVLRDGTGYLQCVLSDDLCQ--CYNGVVLSTESSVAVYGTLNLTPKgkqAPGGHELSCDF 215
Cdd:cd04319 1 KVTLAGWVYRKREVGKKA-FIVLRDSTGIVQAVFSKDLNEeaYREAKKVGIESSVIVEGAVKADPR---APGGAEVHGEK 76
|
90 100 110
....*....|....*....|....*....|..
gi 193806326 216 WELVGLapaggADNL-INEESDVDVQLNNRHM 246
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 ... |
136-211 |
1.48e-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: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 136 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVL-----SDDLCQCYNGvvLSTESSVAVYGTLNLTPKgkqAPGGHE 210
Cdd:cd04316 12 GEEVTVAGWVHEIRDLGG-IKFVILRDREGIVQVTApkkkvDKELFKTVRK--LSRESVISVTGTVKAEPK---APNGVE 85
|
.
gi 193806326 211 L 211
Cdd:cd04316 86 I 86
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
257-471 |
1.58e-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: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 257 LKARSMITRCFRDHFFDRGYCEVTTPTLVQTqvegGAT-----LFKLDYFGEEAfltQSSQLYLETC--------LPA-L 322
Cdd:COG2269 6 LRARARLLAAIRAFFAERGVLEVETPALSVA----PGTdphldSFATEFIGPDG---GGRPLYLHTSpefamkrlLAAgS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 323 GDVFCIAQSYRAEQsRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSpvasivyelnpnfkppkrPFRRM 402
Cdd:COG2269 79 GPIYQIAKVFRNGE-RGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAAGFA------------------PAERL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 403 NYSDA-----------------IEWLKEHDVKKEDgtfyefGDDIPEAPERLMTDTI------NEPILLCRFPVEiksfy 459
Cdd:COG2269 140 SYQEAflrylgidpltadldelAAAAAAAGLRVAD------DDDRDDLLDLLLSERVepqlgrDRPTFLYDYPAS----- 208
|
250
....*....|....*..
gi 193806326 460 mQ-----RCPEDPRLTE 471
Cdd:COG2269 209 -QaalarISPDDPRVAE 224
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
139-214 |
1.94e-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: 1.94e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193806326 139 VKVFGWVhRLRRQGKNLMFLVLRDGTGY--LQCVLSDDLCQCYNGVVLSTESSVAVYGTLNLTPKGKQApggHELSCD 214
Cdd:cd04318 2 VTVNGWV-RSVRDSKKISFIELNDGSCLknLQVVVDKELTNFKEILKLSTGSSIRVEGVLVKSPGAKQP---FELQAE 75
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
130-351 |
1.17e-09 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 61.13 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 130 ALEGYRGQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQCYN----GVVLSTESSVAVYGTLNLTPKGkqa 205
Cdd:PRK02983 645 ALDAPTGEEVSVSGRVLRIRDYGG-VLFADLRDWSGELQVLLDASRLEQGSladfRAAVDLGDLVEVTGTMGTSRNG--- 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 206 pgghELS--CDFWELVG--LAPaggadnLINEE---SDVDVQLNNRHM--MIRGENMSkILKARSMITRCFRDHFFDRGY 276
Cdd:PRK02983 721 ----TLSllVTSWRLAGkcLRP------LPDKWkglTDPEARVRQRYLdlAVNPEARD-LLRARSAVVRAVRETLVARGF 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 277 CEVTTPTLvQtQVEGGAT----LFKLDYFGEEAFLTQSSQLYLET-CLPALGDVFCIAQSYRAE-QSRTrrHLAEFTHVE 350
Cdd:PRK02983 790 LEVETPIL-Q-QVHGGANarpfVTHINAYDMDLYLRIAPELYLKRlCVGGVERVFELGRNFRNEgVDAT--HNPEFTLLE 865
|
.
gi 193806326 351 A 351
Cdd:PRK02983 866 A 866
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
139-551 |
1.23e-09 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 60.77 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 139 VKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVL----SDDLCQCYNGVVLSTESS--VAVYGTLNLTPKGkqapgghELS 212
Cdd:PLN02502 111 VSVAGRIMAKRAFGK-LAFYDLRDDGGKIQLYAdkkrLDLDEEEFEKLHSLVDRGdiVGVTGTPGKTKKG-------ELS 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 213 CDFWELVGLAPA-----GGADNLineeSDVDVQLNNRHM-MIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLvQ 286
Cdd:PLN02502 183 IFPTSFEVLTKCllmlpDKYHGL----TDQETRYRQRYLdLIANPEVRDIFRTRAKIISYIRRFLDDRGFLEVETPML-N 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 287 TQVeGGATL--FKLDY--FGEEAFLTQSSQLYL-ETCLPALGDVFCIAQSYRAEQSRTrRHLAEFTHVEAECPFLTFEDL 361
Cdd:PLN02502 258 MIA-GGAAArpFVTHHndLNMDLYLRIATELHLkRLVVGGFERVYEIGRQFRNEGIST-RHNPEFTTCEFYQAYADYNDM 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 362 LNRLEDLVCdvvdrvlkspvaSIVYELNPNFKPP--------KRPFRRMnysDAIEWLKE-------HDVKKEDGTFY-- 424
Cdd:PLN02502 336 MELTEEMVS------------GMVKELTGSYKIKyhgieidfTPPFRRI---SMISLVEEatgidfpADLKSDEANAYli 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 425 ----EFGDDIPEAP----------ERLMTDTINEPILLCRFPVEIkSFYMQRCPEDPRLTESVDVLmpnvgeIVGgsmrs 490
Cdd:PLN02502 401 aaceKFDVKCPPPQttgrllnelfEEFLEETLVQPTFVLDHPVEM-SPLAKPHRSKPGLTERFELF------ING----- 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 491 wdsEEILEGYKrEGIDPapyywyTDQRK----------------------------YGTCPHGGYGLGLERFLSWILNRY 542
Cdd:PLN02502 469 ---RELANAFS-ELTDP------VDQRErfeeqvkqhnagddeamaldedfctaleYGLPPTGGWGLGIDRLVMLLTDSA 538
|
....*....
gi 193806326 543 HIRDVCLYP 551
Cdd:PLN02502 539 SIRDVIAFP 547
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
136-202 |
2.32e-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: 2.32e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193806326 136 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQCYNGVV-LSTESSVAVYGTLNLTPKG 202
Cdd:cd04317 14 GQEVTLCGWVQRRRDHGG-LIFIDLRDRYGIVQVVFDPEEAPEFELAEkLRNESVIQVTGKVRARPEG 80
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
253-547 |
1.39e-08 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 56.48 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 253 MSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQ-TQVEGGATLFKLDYFGEEAflTQSSQLYLETC--------LPAL- 322
Cdd:PRK09350 1 SIPNLLKRAKIIAEIRRFFADRGVLEVETPILSQaTVTDIHLVPFETRFVGPGA--SQGKTLWLMTSpeyhmkrlLAAGs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 323 GDVFCIAQSYRAEQSrTRRHLAEFTHVEAECPFLTFEDLLNRLEDLvcdvVDRVLKSPVA-SIVYE--------LNPnFK 393
Cdd:PRK09350 79 GPIFQICKSFRNEEA-GRYHNPEFTMLEWYRPHYDMYRLMNEVDDL----LQQVLDCEPAeSLSYQqaflrylgIDP-LS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 394 PPKRPFRrmnysDAIEWLKEHDVKKEDgtfyefgDDIPEAPERLMTDTI------NEPILLCRFPVEIKSfYMQRCPEDP 467
Cdd:PRK09350 153 ADKTQLR-----EVAAKLGLSNIADEE-------EDRDTLLQLLFTFGVepnigkEKPTFVYHFPASQAA-LAKISTEDH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 468 RLTESVDVLMPNVgEIVGGSMRSWDSEEILEGYKR-------EGIDPAPyywyTDQR-----KYGTCPHGGYGLGLERFL 535
Cdd:PRK09350 220 RVAERFEVYFKGI-ELANGFHELTDAREQRQRFEQdnrkraaRGLPQQP----IDENliaalEAGLPDCSGVALGVDRLI 294
|
330
....*....|..
gi 193806326 536 SWILNRYHIRDV 547
Cdd:PRK09350 295 MLALGAESISEV 306
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
139-201 |
5.51e-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: 5.51e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193806326 139 VKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVLSDDlcqcyNGVV----------LSTESSVAVYGTLNLTPK 201
Cdd:cd04320 2 VLIRARVHTSRAQGAKLAFLVLRQQGYTIQGVLAAS-----AEGVskqmvkwagsLSKESIVDVEGTVKKPEE 69
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
271-471 |
9.29e-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: 9.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 271 FFDRGYCEVTTPTLVQtqveGGATLFKLDYF--GEEAFLTQSSQLYLET----CLPAL-----GDVFCIAQSYRAEQsRT 339
Cdd:TIGR00462 2 FAERGVLEVETPLLSP----APVTDPHLDAFatEFVGPDGQGRPLYLQTspeyAMKRLlaagsGPIFQICKVFRNGE-RG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 340 RRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVvdrvlkspvasivyelnpnFKPPKRPFRRMNYSDA-IEWLKEHDVKK 418
Cdd:TIGR00462 77 RRHNPEFTMLEWYRPGFDYHDLMDEVEALLQEL-------------------LGDPFAPAERLSYQEAfLRYAGIDPLTA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193806326 419 EDGTFYE----FGDDIPEAP------ERLMTDTI------NEPILLCRFPVEIKSFyMQRCPEDPRLTE 471
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 ... |
260-361 |
1.38e-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: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 260 RSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGATLFKLD------YFGEEAFLTQSSQLYLET----CLPALGD-VFCI 328
Cdd:cd00768 2 RSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHEPKDllpvgaENEEDLYLRPTLEPGLVRlfvsHIRKLPLrLAEI 81
|
90 100 110
....*....|....*....|....*....|....
gi 193806326 329 AQSYRAEQSRTR-RHLAEFTHVEAECPFLTFEDL 361
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 ... |
138-219 |
1.98e-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: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193806326 138 RVKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVLSDDLCQCYNGV-VLSTESSVAVYGTLNLtpkgKQAPGGHELSCdfW 216
Cdd:cd04321 1 KVTLNGWIDRKPRIVKKLSFADLRDPNGDIIQLVSTAKKDAFSLLkSITAESPVQVRGKLQL----KEAKSSEKNDE--W 74
|
...
gi 193806326 217 ELV 219
Cdd:cd04321 75 ELV 77
|
|
| |
