|
Name |
Accession |
Description |
Interval |
E-value |
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
195-514 |
5.21e-149 |
|
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: 5.21e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 195 DVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYL 274
Cdd:cd00776 3 NLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQLYK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 275 ETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFL-TFEDLLNRLEDLVCDVVDRVLKSPVASI--VYELNPNF 351
Cdd:cd00776 83 EMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAKELelVNQLNREL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 352 KPPKRPFRRMNYSDAIEWLKEHDVKKEDgtfyEFGDDIPEAPERLMTDTI-NEPILLCRFPVEIKSFYMQRCPEDPRLTE 430
Cdd:cd00776 163 LKPLEPFPRITYDEAIELLREKGVEEEV----KWGEDLSTEHERLLGEIVkGDPVFVTDYPKEIKPFYMKPDDDNPETVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 431 SVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYP 510
Cdd:cd00776 239 SFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
....
gi 1781905169 511 RFLQ 514
Cdd:cd00776 319 RDPK 322
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
85-518 |
2.96e-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: 2.96e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 85 VKIS-ALEGYRGQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQCYNGVV-LSTESSVAVYGTLNLTPKgk 162
Cdd:COG0017 3 TYIKdLLPEHVGQEVTVAGWVRTKRDSGG-ISFLILRDGSGFIQVVVKKDKLENFEEAKkLTTESSVEVTGTVVESPR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 163 qAPGGHELSCDFWELVGLA----PaggadnLINEESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEV 238
Cdd:COG0017 80 -APQGVELQAEEIEVLGEAdepyP------LQPKRHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVEV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 239 TTPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFE 318
Cdd:COG0017 153 HTPIITASATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMALEKVYTFGPTFRAEKSNTRRHLAEFWMIEPEMAFADLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 319 DLLNRLEDLVCDVVDRVLKSPVASI-VYELNPNF--KPPKRPFRRMNYSDAIEWLKEHDVKkedgtfYEFGDDI-PEApE 394
Cdd:COG0017 233 DVMDLAEEMLKYIIKYVLENCPEELeFLGRDVERleKVPESPFPRITYTEAIEILKKSGEK------VEWGDDLgTEH-E 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 395 RLMTDTI-NEPILLCRFPVEIKSFYMQRCPEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYT 473
Cdd:COG0017 306 RYLGEEFfKKPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAPGIGEIIGGSQREHRYDVLVERIKEKGLDPEDYEWYL 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1781905169 474 DQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 518
Cdd:COG0017 386 DLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
95-518 |
5.47e-144 |
|
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: 5.47e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 95 GQRVKVFGWVHRlRRQGKNLMFLVLRDGT--GYLQCVLSDDLCQCYNGVV--LSTESSVAVYGTLNLTPKGKQapgGHEL 170
Cdd:TIGR00457 16 GDEVTVSGWVRT-KRSSKKIIFLELNDGSslGPIQAVINGEDNPYLFQLLksLTTGSSVSVTGKVVESPGKGQ---PVEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 171 SCDFWELVGLAPAGGADNLInEESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEG 250
Cdd:TIGR00457 92 QVKKIEVVGEAEPDDYPLQK-KEHSLEFLRDIAHLRLRTNTLGAVMRVRNALSQAIHRYFQENGFTWVSPPILTSNDCEG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 251 GATLFKL---------DYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFEDLL 321
Cdd:TIGR00457 171 AGELFRVstgnidfsqDFFGKEAYLTVSGQLYLETYALALSKVYTFGPTFRAEKSNTSRHLSEFWMIEPEMAFANLNDLL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 322 NRLEDLVCDVVDRVLKSpVASIVYELNPNFKPPKRP---------FRRMNYSDAIEWLKEHDVKKEDGTFyeFGDDIPEA 392
Cdd:TIGR00457 251 QLAETLIKYIIKAVLEN-CSQELKFLEKNFDKDLIKrleniinnkFARITYTDAIEILKESDKNFEYEDF--WGDDLQTE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 393 PERLMTDTI-NEPILLCRFPVEIKSFYMQRCpEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYW 471
Cdd:TIGR00457 328 HERFLAEEYfKPPVFVTNYPKDIKAFYMKLN-DDGKTVAAMDLLAPGIGEIIGGSEREDDLDKLENRMKEMGLDTDALNW 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1781905169 472 YTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 518
Cdd:TIGR00457 407 YLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGNINF 453
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
91-518 |
3.17e-111 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 337.47 E-value: 3.17e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 91 EGYRGQRVKVFGWVHRlRRQGKNLMFLVLRDGTGY--LQCVLSDDLCqcYNGVV--LSTESSVAVYGTLNLTPKgkqAPG 166
Cdd:PRK03932 12 GKYVGQEVTVRGWVRT-KRDSGKIAFLQLRDGSCFkqLQVVKDNGEE--YFEEIkkLTTGSSVIVTGTVVESPR---AGQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 167 GHELSCDFWELVGLAPAggaDNLINE-ESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQ 245
Cdd:PRK03932 86 GYELQATKIEVIGEDPE---DYPIQKkRHSIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVDTPIITA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 246 TQVEGGATLFKL---------DYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLT 316
Cdd:PRK03932 163 SDCEGAGELFRVttldldfskDFFGKEAYLTVSGQLYAEAYAMALGKVYTFGPTFRAENSNTRRHLAEFWMIEPEMAFAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 317 FEDLLNRLEDLVCDVVDRVL-----------KSPVASIVYELNpNFKPPkrPFRRMNYSDAIEWLKEHDVKKEDGTfyEF 385
Cdd:PRK03932 243 LEDNMDLAEEMLKYVVKYVLencpddleflnRRVDKGDIERLE-NFIES--PFPRITYTEAIEILQKSGKKFEFPV--EW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 386 GDDI--PEapERLMTDTINE-PILLCRFPVEIKSFYMQRCPEDpRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKRE 462
Cdd:PRK03932 318 GDDLgsEH--ERYLAEEHFKkPVFVTNYPKDIKAFYMRLNPDG-KTVAAMDLLAPGIGEIIGGSQREERLDVLEARIKEL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1781905169 463 GIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 518
Cdd:PRK03932 395 GLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
195-511 |
3.62e-106 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 319.90 E-value: 3.62e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 195 DVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGATLFKL------DYFgeeaFLTQ 268
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVpsralgKFY----ALPQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 269 SSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHLaEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPvasiVYEL 347
Cdd:pfam00152 77 SPQLYKQLLMVAgFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIA----KELE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 348 NPNFKPPKRPFRRMNYSDAIEWLKEHDVkkedgtfYEFGDDIPEAPERLMTD-----TINEPILLCRFPVEIKSFYMQRC 422
Cdd:pfam00152 152 GGTLLDLKKPFPRITYAEAIEKLNGKDV-------EELGYGSDKPDLRFLLElvidkNKFNPLWVTDFPAEHHPFTMPKD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 423 PEDPRLTESVDVLMPNVgEIVGGSMRSWDSEEILEGYKREGIDP----APYYWYTDQRKYGTCPHGGYGLGLERFLSWIL 498
Cdd:pfam00152 225 EDDPALAEAFDLVLNGV-EIGGGSIRIHDPELQEERFEEQGLDPeeaeEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLT 303
|
330
....*....|...
gi 1781905169 499 NRYHIRDVCLYPR 511
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 ... |
97-179 |
5.76e-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: 139.29 E-value: 5.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 97 RVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQ-CYNGVVLSTESSVAVYGTLNLTPKGKQAPGGHELSCDFW 175
Cdd:cd04323 1 RVKVFGWVHRLRSQKK-LMFLVLRDGTGFLQCVLSKKLVTeFYDAKSLTQESSVEVTGEVKEDPRAKQAPGGYELQVDYL 79
|
....
gi 1781905169 176 ELVG 179
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 ... |
98-178 |
1.02e-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: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 98 VKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVL-SDDLCQCYNgvVLSTESSVAVYGTLNLTPKgkqapGGHELSCDFWE 176
Cdd:pfam01336 1 VTVAGRVTSIRRSGGKLLFLTLRDGTGSIQVVVfKEEAEKLAK--KLKEGDVVRVTGKVKKRKG-----GELELVVEEIE 73
|
..
gi 1781905169 177 LV 178
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 ... |
195-514 |
5.21e-149 |
|
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: 5.21e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 195 DVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYL 274
Cdd:cd00776 3 NLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQLYK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 275 ETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFL-TFEDLLNRLEDLVCDVVDRVLKSPVASI--VYELNPNF 351
Cdd:cd00776 83 EMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAKELelVNQLNREL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 352 KPPKRPFRRMNYSDAIEWLKEHDVKKEDgtfyEFGDDIPEAPERLMTDTI-NEPILLCRFPVEIKSFYMQRCPEDPRLTE 430
Cdd:cd00776 163 LKPLEPFPRITYDEAIELLREKGVEEEV----KWGEDLSTEHERLLGEIVkGDPVFVTDYPKEIKPFYMKPDDDNPETVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 431 SVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYP 510
Cdd:cd00776 239 SFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
....
gi 1781905169 511 RFLQ 514
Cdd:cd00776 319 RDPK 322
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
85-518 |
2.96e-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: 2.96e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 85 VKIS-ALEGYRGQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQCYNGVV-LSTESSVAVYGTLNLTPKgk 162
Cdd:COG0017 3 TYIKdLLPEHVGQEVTVAGWVRTKRDSGG-ISFLILRDGSGFIQVVVKKDKLENFEEAKkLTTESSVEVTGTVVESPR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 163 qAPGGHELSCDFWELVGLA----PaggadnLINEESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEV 238
Cdd:COG0017 80 -APQGVELQAEEIEVLGEAdepyP------LQPKRHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVEV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 239 TTPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFE 318
Cdd:COG0017 153 HTPIITASATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMALEKVYTFGPTFRAEKSNTRRHLAEFWMIEPEMAFADLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 319 DLLNRLEDLVCDVVDRVLKSPVASI-VYELNPNF--KPPKRPFRRMNYSDAIEWLKEHDVKkedgtfYEFGDDI-PEApE 394
Cdd:COG0017 233 DVMDLAEEMLKYIIKYVLENCPEELeFLGRDVERleKVPESPFPRITYTEAIEILKKSGEK------VEWGDDLgTEH-E 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 395 RLMTDTI-NEPILLCRFPVEIKSFYMQRCPEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYT 473
Cdd:COG0017 306 RYLGEEFfKKPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAPGIGEIIGGSQREHRYDVLVERIKEKGLDPEDYEWYL 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1781905169 474 DQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 518
Cdd:COG0017 386 DLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
95-518 |
5.47e-144 |
|
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: 5.47e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 95 GQRVKVFGWVHRlRRQGKNLMFLVLRDGT--GYLQCVLSDDLCQCYNGVV--LSTESSVAVYGTLNLTPKGKQapgGHEL 170
Cdd:TIGR00457 16 GDEVTVSGWVRT-KRSSKKIIFLELNDGSslGPIQAVINGEDNPYLFQLLksLTTGSSVSVTGKVVESPGKGQ---PVEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 171 SCDFWELVGLAPAGGADNLInEESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEG 250
Cdd:TIGR00457 92 QVKKIEVVGEAEPDDYPLQK-KEHSLEFLRDIAHLRLRTNTLGAVMRVRNALSQAIHRYFQENGFTWVSPPILTSNDCEG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 251 GATLFKL---------DYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFEDLL 321
Cdd:TIGR00457 171 AGELFRVstgnidfsqDFFGKEAYLTVSGQLYLETYALALSKVYTFGPTFRAEKSNTSRHLSEFWMIEPEMAFANLNDLL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 322 NRLEDLVCDVVDRVLKSpVASIVYELNPNFKPPKRP---------FRRMNYSDAIEWLKEHDVKKEDGTFyeFGDDIPEA 392
Cdd:TIGR00457 251 QLAETLIKYIIKAVLEN-CSQELKFLEKNFDKDLIKrleniinnkFARITYTDAIEILKESDKNFEYEDF--WGDDLQTE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 393 PERLMTDTI-NEPILLCRFPVEIKSFYMQRCpEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYW 471
Cdd:TIGR00457 328 HERFLAEEYfKPPVFVTNYPKDIKAFYMKLN-DDGKTVAAMDLLAPGIGEIIGGSEREDDLDKLENRMKEMGLDTDALNW 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1781905169 472 YTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 518
Cdd:TIGR00457 407 YLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGNINF 453
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
91-518 |
3.17e-111 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 337.47 E-value: 3.17e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 91 EGYRGQRVKVFGWVHRlRRQGKNLMFLVLRDGTGY--LQCVLSDDLCqcYNGVV--LSTESSVAVYGTLNLTPKgkqAPG 166
Cdd:PRK03932 12 GKYVGQEVTVRGWVRT-KRDSGKIAFLQLRDGSCFkqLQVVKDNGEE--YFEEIkkLTTGSSVIVTGTVVESPR---AGQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 167 GHELSCDFWELVGLAPAggaDNLINE-ESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQ 245
Cdd:PRK03932 86 GYELQATKIEVIGEDPE---DYPIQKkRHSIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVDTPIITA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 246 TQVEGGATLFKL---------DYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLT 316
Cdd:PRK03932 163 SDCEGAGELFRVttldldfskDFFGKEAYLTVSGQLYAEAYAMALGKVYTFGPTFRAENSNTRRHLAEFWMIEPEMAFAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 317 FEDLLNRLEDLVCDVVDRVL-----------KSPVASIVYELNpNFKPPkrPFRRMNYSDAIEWLKEHDVKKEDGTfyEF 385
Cdd:PRK03932 243 LEDNMDLAEEMLKYVVKYVLencpddleflnRRVDKGDIERLE-NFIES--PFPRITYTEAIEILQKSGKKFEFPV--EW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 386 GDDI--PEapERLMTDTINE-PILLCRFPVEIKSFYMQRCPEDpRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKRE 462
Cdd:PRK03932 318 GDDLgsEH--ERYLAEEHFKkPVFVTNYPKDIKAFYMRLNPDG-KTVAAMDLLAPGIGEIIGGSQREERLDVLEARIKEL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1781905169 463 GIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 518
Cdd:PRK03932 395 GLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
195-511 |
3.62e-106 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 319.90 E-value: 3.62e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 195 DVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGATLFKL------DYFgeeaFLTQ 268
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVpsralgKFY----ALPQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 269 SSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHLaEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPvasiVYEL 347
Cdd:pfam00152 77 SPQLYKQLLMVAgFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIA----KELE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 348 NPNFKPPKRPFRRMNYSDAIEWLKEHDVkkedgtfYEFGDDIPEAPERLMTD-----TINEPILLCRFPVEIKSFYMQRC 422
Cdd:pfam00152 152 GGTLLDLKKPFPRITYAEAIEKLNGKDV-------EELGYGSDKPDLRFLLElvidkNKFNPLWVTDFPAEHHPFTMPKD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 423 PEDPRLTESVDVLMPNVgEIVGGSMRSWDSEEILEGYKREGIDP----APYYWYTDQRKYGTCPHGGYGLGLERFLSWIL 498
Cdd:pfam00152 225 EDDPALAEAFDLVLNGV-EIGGGSIRIHDPELQEERFEEQGLDPeeaeEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLT 303
|
330
....*....|...
gi 1781905169 499 NRYHIRDVCLYPR 511
Cdd:pfam00152 304 GLESIREVIAFPK 316
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
95-518 |
4.63e-102 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 313.67 E-value: 4.63e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 95 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQCYNGVV--LSTESSVAVYGTLNLTPKgkqAPGGHELSC 172
Cdd:PRK05159 16 GEEVTLAGWVHEIRDLGG-IAFLILRDRSGIIQVVVKKKVDEELFETIkkLKRESVVSVTGTVKANPK---APGGVEVIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 173 DFWELVGLApaggADNL---INEES--DVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQ 247
Cdd:PRK05159 92 EEIEVLNKA----EEPLpldISGKVlaELDTRLDNRFLDLRRPRVRAIFKIRSEVLRAFREFLYENGFTEIFTPKIVASG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 248 VEGGATLFKLDYFGEEAFLTQSSQLYLETCLPALGD-VFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLT-FEDLLNRLE 325
Cdd:PRK05159 168 TEGGAELFPIDYFEKEAYLAQSPQLYKQMMVGAGFErVFEIGPVFRAEEHNTSRHLNEYTSIDVEMGFIDdHEDVMDLLE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 326 DLVCDVVDRVLKSPVASIVyELNPNFKPPKRPFRRMNYSDAIEWLKEHDVKKedgtfyEFGDDIPEAPERLMTDTINE-- 403
Cdd:PRK05159 248 NLLRYMYEDVAENCEKELE-LLGIELPVPETPIPRITYDEAIEILKSKGNEI------SWGDDLDTEGERLLGEYVKEey 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 404 ---PILLCRFPVEIKSFYMQRCPEDPRLTESVDVLMPNVgEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGT 480
Cdd:PRK05159 321 gsdFYFITDYPSEKRPFYTMPDEDDPEISKSFDLLFRGL-EITSGGQRIHRYDMLVESIKEKGLNPESFEFYLEAFKYGM 399
|
410 420 430
....*....|....*....|....*....|....*...
gi 1781905169 481 CPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP 518
Cdd:PRK05159 400 PPHGGFGLGLERLTMKLLGLENIREAVLFPRDRHRLTP 437
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
73-518 |
9.10e-56 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 195.31 E-value: 9.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 73 EQMKNDSREKKEVKISAL-EGYRGQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQCYNGVV-----LSTE 146
Cdd:PLN02850 58 EELQSKVTGREWTDVSDLgEELAGSEVLIRGRVHTIRGKGK-SAFLVLRQSGFTVQCVVFVSEVTVSKGMVkyakqLSRE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 147 SSVAVYGTLNLTPKG-KQAPGGHELSCDFWELVGLAPAGGADNLIN---EESDV---------------DVQLNNRHMMI 207
Cdd:PLN02850 137 SVVDVEGVVSVPKKPvKGTTQQVEIQVRKIYCVSKALATLPFNVEDaarSESEIekalqtgeqlvrvgqDTRLNNRVLDL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 208 RGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPA-LGDVFC 286
Cdd:PLN02850 217 RTPANQAIFRIQSQVCNLFREFLLSKGFVEIHTPKLIAGASEGGSAVFRLDYKGQPACLAQSPQLHKQMAICGdFRRVFE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 287 IAQSYRAEQSRTRRHLAEFTHveaecpfLTFEDLLNRLEDLVCDVVDRVLKspvaSIVYELNPN-------------FKP 353
Cdd:PLN02850 297 IGPVFRAEDSFTHRHLCEFTG-------LDLEMEIKEHYSEVLDVVDELFV----AIFDGLNERckkeleaireqypFEP 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 354 PK--RPFRRMNYSDAIEWLKEHDVKKEDgtfyeFGDDIPEApERLMTDTINEP-----ILLCRFPVEIKSFYMQRCPEDP 426
Cdd:PLN02850 366 LKylPKTLRLTFAEGIQMLKEAGVEVDP-----LGDLNTES-ERKLGQLVKEKygtdfYILHRYPLAVRPFYTMPCPDDP 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 427 RLTESVDVLMPNvGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDV 506
Cdd:PLN02850 440 KYSNSFDVFIRG-EEIISGAQRVHDPELLEKRAEECGIDVKTISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKT 518
|
490
....*....|..
gi 1781905169 507 CLYPRFLQRCRP 518
Cdd:PLN02850 519 SLFPRDPQRLAP 530
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
207-511 |
3.26e-50 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 175.21 E-value: 3.26e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 207 IRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLvqTQV-----EGGATL----FKLDYFGEEAFLTQSSQLYLETC 277
Cdd:PRK06462 21 ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPII--SPStdplmGLGSDLpvkqISIDFYGVEYYLADSMILHKQLA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 278 LPALGDVFCIAQSYRAEQ--SRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPVASIvYELNPNFKPPK 355
Cdd:PRK06462 99 LRMLGKIFYLSPNFRLEPvdKDTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHEDEL-EFFGRDLPHLK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 356 RPFRRMNYSDAIEWLKEHDVKKEDgtFYEFGDDIpeapERLMTDTINEPILLCRFPVEIKSFYMQRCPEDPRLTESVDVL 435
Cdd:PRK06462 178 RPFKRITHKEAVEILNEEGCRGID--LEELGSEG----EKSLSEHFEEPFWIIDIPKGSREFYDREDPERPGVLRNYDLL 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1781905169 436 MPN-VGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPR 511
Cdd:PRK06462 252 LPEgYGEAVSGGEREYEYEEIVERIREHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQPFPR 328
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
92-512 |
1.08e-49 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 179.42 E-value: 1.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 92 GYRGQRVKVFGWVHRLRRQGK-NLMFLVLRDGT--GYLQCVLSDDLCQCYNgvVLSTESSVAVYGTLNLTPKGKQAPGGH 168
Cdd:PLN02221 47 GLAGQKVRIGGWVKTGREQGKgTFAFLEVNDGScpANLQVMVDSSLYDLST--LVATGTCVTVDGVLKVPPEGKGTKQKI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 169 ELSCDFWELVGLAPAGGADnLINEESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQV 248
Cdd:PLN02221 125 ELSVEKVIDVGTVDPTKYP-LPKTKLTLEFLRDVLHLRSRTNSISAVARIRNALAFATHSFFQEHSFLYIHTPIITTSDC 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 249 EGGATLFKL----------------------------------------------------------------------- 257
Cdd:PLN02221 204 EGAGEMFQVttlinyterleqdlidnpppteadveaarlivkergevvaqlkaakaskeeitaavaelkiakeslahiee 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 258 -------------------DYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFE 318
Cdd:PLN02221 284 rsklkpglpkkdgkidyskDFFGRQAFLTVSGQLQVETYACALSSVYTFGPTFRAENSHTSRHLAEFWMVEPEIAFADLE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 319 DLLNRLEDLVCDVVDRVLKSPVASIvyEL-NPNFKP---------PKRPFRRMNYSDAIEWLKEHDVK-KEDGTFYEFGD 387
Cdd:PLN02221 364 DDMNCAEAYVKYMCKWLLDKCFDDM--ELmAKNFDSgcidrlrmvASTPFGRITYTEAIELLEEAVAKgKEFDNNVEWGI 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 388 DIPEAPERLMTDTI-NEPILLCRFPVEIKSFYMqRCPEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDP 466
Cdd:PLN02221 442 DLASEHERYLTEVLfQKPLIVYNYPKGIKAFYM-RLNDDEKTVAAMDVLVPKVGELIGGSQREERYDVIKQRIEEMGLPI 520
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1781905169 467 APYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRF 512
Cdd:PLN02221 521 EPYEWYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPRY 566
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
82-511 |
1.30e-49 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 179.01 E-value: 1.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 82 KKEVKISALEG-------YRGQRVKVFGWVHRLRRQgKNLMFLVLRDGT--GYLQCVLSDDlCQCYNGV---VLSTESSV 149
Cdd:PLN02603 87 RKKLRIADVKGgedeglaRVGKTLNVMGWVRTLRAQ-SSVTFIEVNDGSclSNMQCVMTPD-AEGYDQVesgLITTGASV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 150 AVYGTLNLTPKGKQAPgghELSCDFWELVGlapaggadnlineESDVDVQLNNR-----------HMMIRGENMSKILKA 218
Cdd:PLN02603 165 LVQGTVVSSQGGKQKV---ELKVSKIVVVG-------------KSDPSYPIQKKrvsreflrtkaHLRPRTNTFGAVARV 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 219 RSMITRCFRDHFFDRGYCEVTTP-----------------TLVQTQVEGGATLFK-------------LDYFGEEAFLTQ 268
Cdd:PLN02603 229 RNALAYATHKFFQENGFVWVSSPiitasdcegageqfcvtTLIPNSAENGGSLVDdipktkdglidwsQDFFGKPAFLTV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 269 SSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPV-------- 340
Cdd:PLN02603 309 SGQLNGETYATALSDVYTFGPTFRAENSNTSRHLAEFWMIEPELAFADLNDDMACATAYLQYVVKYILENCKedmeffnt 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 341 ---ASIVYELNpnfKPPKRPFRRMNYSDAIEWLKEhdVKKEDGTFYEFGDDIPEAPERLMTDTI--NEPILLCRFPVEIK 415
Cdd:PLN02603 389 wieKGIIDRLS---DVVEKNFVQLSYTDAIELLLK--AKKKFEFPVKWGLDLQSEHERYITEEAfgGRPVIIRDYPKEIK 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 416 SFYMqRCPEDPRLTESVDVLMPNVGEIVGGSMRSwDSEEILEGYKRE-GIDPAPYYWYTDQRKYGTCPHGGYGLGLERFL 494
Cdd:PLN02603 464 AFYM-RENDDGKTVAAMDMLVPRVGELIGGSQRE-ERLEYLEARLDElKLNKESYWWYLDLRRYGSVPHAGFGLGFERLV 541
|
490
....*....|....*..
gi 1781905169 495 SWILNRYHIRDVCLYPR 511
Cdd:PLN02603 542 QFATGIDNIRDAIPFPR 558
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
79-518 |
1.51e-46 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 170.56 E-value: 1.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 79 SREKKEVKISALEGYRGQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCV--LSDDLCQCYNGVV--LSTESSVAVYGT 154
Cdd:PTZ00401 62 SRTFIPVAVLSKPELVDKTVLIRARVSTTRKKGK-MAFMVLRDGSDSVQAMaaVEGDVPKEMIDFIgqIPTESIVDVEAT 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 155 LNLT--PKGKQAPGGHELSCDFWELVG---------LAPAGGADNLINEESDVDVQLNNRHMMIRGENMSKILKARSMIT 223
Cdd:PTZ00401 141 VCKVeqPITSTSHSDIELKVKKIHTVTeslrtlpftLEDASRKESDEGAKVNFDTRLNSRWMDLRTPASGAIFRLQSRVC 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 224 RCFRDHFFDRGYCEVTTPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHL 302
Cdd:PTZ00401 221 QYFRQFLIDSDFCEIHSPKIINAPSEGGANVFKLEYFNRFAYLAQSPQLYKQMVLQGdVPRVFEVGPVFRSENSNTHRHL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 303 AEFTHVEAECPFLT-FEDLLNRLEDLVCDVVDRVLKS-----------PVASIVYELNP-------------NFKPPKR- 356
Cdd:PTZ00401 301 TEFVGLDVEMRINEhYYEVLDLAESLFNYIFERLATHtkelkavcqqyPFEPLVWKLTPermkelgvgviseGVEPTDKy 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 357 ---------PFRRMNYSDAIEWLKEHDVKKEDGTfyefgDDIPEAPERLMTDTINEP-----ILLCRFPVEIKSFYMQRC 422
Cdd:PTZ00401 381 qarvhnmdsRMLRINYMHCIELLNTVLEEKMAPT-----DDINTTNEKLLGKLVKERygtdfFISDRFPSSARPFYTMEC 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 423 PEDPRLTESVDVLMPNvGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYH 502
Cdd:PTZ00401 456 KDDERFTNSYDMFIRG-EEISSGAQRIHDPDLLLARAKMLNVDLTPIKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSN 534
|
490
....*....|....*.
gi 1781905169 503 IRDVCLYPRFLQRCRP 518
Cdd:PTZ00401 535 VRLASLFPRDPQRTTP 550
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
59-512 |
2.90e-44 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 164.81 E-value: 2.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 59 SKSQMKNIKKMWHREQMKNDSREKKEvkisalegYRGQRVKVFGWVHRLRRQGKN-LMFLVLRDGTGYL-------QCVL 130
Cdd:PTZ00425 53 SRIRICNVLNVPKSEKEFNDNSRKNK--------YIDQIITVCGWSKAVRKQGGGrFCFVNLNDGSCHLnlqiivdQSIE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 131 S-DDLCQCYNGVVLSTESSVAVYGTLNLTPKG--KQapgGHELSCDFWELVGLAPAGgaDNLINEESDVDVQLNNR---- 203
Cdd:PTZ00425 125 NyEKLLKCGVGCCFRFTGKLIISPVQNENKKGllKE---NVELALKDNSIHNFEIYG--ENLDPQKYPLSKKNHGKeflr 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 204 ---HMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGATLF------------------------- 255
Cdd:PTZ00425 200 evaHLRPRSYFISSVIRIRNALAIATHLFFQSRGFLYIHTPLITTSDCEGGGEMFtvttllgedadyraiprvnkknkkg 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 256 --------------------------------------KLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSR 297
Cdd:PTZ00425 280 ekredilntcnannnngnssssnavsspaypdqylidyKKDFFSKQAFLTVSGQLSLENLCSSMGDVYTFGPTFRAENSH 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 298 TRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPVASIVY-ELNPNFKPPKR-------PFRRMNYSDAIEW 369
Cdd:PTZ00425 360 TSRHLAEFWMIEPEIAFADLYDNMELAESYIKYCIGYVLNNNFDDIYYfEENVETGLISRlknildeDFAKITYTNVIDL 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 370 LKEHDVKKEdgTFYEFGDDIPEAPERLMTDTI-NEPILLCRFPVEIKSFYMqRCPEDPRLTESVDVLMPNVGEIVGGSMR 448
Cdd:PTZ00425 440 LQPYSDSFE--VPVKWGMDLQSEHERFVAEQIfKKPVIVYNYPKDLKAFYM-KLNEDQKTVAAMDVLVPKIGEVIGGSQR 516
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1781905169 449 SWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRF 512
Cdd:PTZ00425 517 EDNLERLDKMIKEKKLNMESYWWYRQLRKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFPRY 580
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
216-511 |
1.63e-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: 1.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 216 LKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGATLFKLDYF--GEEAFLTQSSQLYLETCLPA-LGDVFCIAQSYR 292
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNalGLDYYLRISPQLFKKRLMVGgLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 293 AEQSRTRrHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLkspvasIVYELNPNFKP--PKRPFRRMNYSDAIEWL 370
Cdd:cd00669 81 NEDLRAR-HQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVL------GVTAVTYGFELedFGLPFPRLTYREALERY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 371 KEhdvkkedgtfyefgddipeaperlmtdtinePILLCRFPVEIKSFYMQRCPEDPRLTESVDVLMPNVgEIVGGSMRSW 450
Cdd:cd00669 154 GQ-------------------------------PLFLTDYPAEMHSPLASPHDVNPEIADAFDLFINGV-EVGNGSSRLH 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1781905169 451 DSEEILEGYKREGIDPAP----YYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPR 511
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 ... |
97-179 |
5.76e-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: 139.29 E-value: 5.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 97 RVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQ-CYNGVVLSTESSVAVYGTLNLTPKGKQAPGGHELSCDFW 175
Cdd:cd04323 1 RVKVFGWVHRLRSQKK-LMFLVLRDGTGFLQCVLSKKLVTeFYDAKSLTQESSVEVTGEVKEDPRAKQAPGGYELQVDYL 79
|
....
gi 1781905169 176 ELVG 179
Cdd:cd04323 80 EIIG 83
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
255-511 |
1.92e-27 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 116.51 E-value: 1.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 255 FKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDR 334
Cdd:PLN02532 363 FSKDFFSRPTYLTVSGRLHLESYACALGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAFSELEDAMNCAEDYFKFLCKW 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 335 VLKSPVA-----------SIVYELNPNFkppKRPFRRMNYSDAIEWLKEH-DVKKEdgTFYEFGddIPEAPERL--MTDT 400
Cdd:PLN02532 443 VLENCSEdmkfvskridkTISTRLEAII---SSSLQRISYTEAVDLLKQAtDKKFE--TKPEWG--IALTTEHLsyLADE 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 401 I-NEPILLCRFPVEIKSFYMqRCPEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYG 479
Cdd:PLN02532 516 IyKKPVIIYNYPKELKPFYV-RLNDDGKTVAAFDLVVPKVGTVITGSQNEERMDILNARIEELGLPREQYEWYLDLRRHG 594
|
250 260 270
....*....|....*....|....*....|..
gi 1781905169 480 TCPHGGYGLGLERFLSWILNRYHIRDVCLYPR 511
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 ... |
97-179 |
2.42e-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: 2.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 97 RVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQCYNGVV--LSTESSVAVYGTLNLTPKGKQAPGGHELSCDF 174
Cdd:cd04100 1 EVTLAGWVHSRRDHGG-LIFIDLRDGSGIVQVVVNKEELGEFFEEAekLRTESVVGVTGTVVKRPEGNLATGEIELQAEE 79
|
....*
gi 1781905169 175 WELVG 179
Cdd:cd04100 80 LEVLS 84
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
95-368 |
1.32e-23 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 104.49 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 95 GQRVKVFGWVHRLRRQGkNLMFLVLRDGTGYLQCVLSDDLCQCYNGVV--LSTESSVAVYGTLNLTPKG----KQAPGGH 168
Cdd:PLN02903 72 GSRVTLCGWVDLHRDMG-GLTFLDVRDHTGIVQVVTLPDEFPEAHRTAnrLRNEYVVAVEGTVRSRPQEspnkKMKTGSV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 169 EL---SCDFWELVGLA------PAGGADNLINEEsdvdVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDR-GYCEV 238
Cdd:PLN02903 151 EVvaeSVDILNVVTKSlpflvtTADEQKDSIKEE----VRLRYRVLDLRRPQMNANLRLRHRVVKLIRRYLEDVhGFVEI 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 239 TTPTLVQTQVEGGatlfkLDYF-------GEEAFLTQSSQLYLETCLPALGD-VFCIAQSYRAEQSRTRRHlAEFTHVEA 310
Cdd:PLN02903 227 ETPILSRSTPEGA-----RDYLvpsrvqpGTFYALPQSPQLFKQMLMVSGFDrYYQIARCFRDEDLRADRQ-PEFTQLDM 300
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1781905169 311 ECPFLTFEDLLNRLEDLVCDVVDRVLKSPVAsivyelnpnfkppkRPFRRMNYSDAIE 368
Cdd:PLN02903 301 ELAFTPLEDMLKLNEDLIRQVFKEIKGVQLP--------------NPFPRLTYAEAMS 344
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
30-510 |
1.12e-19 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 91.69 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 30 LKALMTVGKEPFPtiyvdsqkenERWDVISKSqmKNIKKmwhreqmKNDSREKKEVKisalegYRGQRVKVFGWVHRLRR 109
Cdd:PRK00484 14 LAELREQGIDPYP----------NKFERTHTA--AELRA-------KYDDKEKEELE------ELEIEVSVAGRVMLKRV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 110 QGKnLMFLVLRDGTGYLQCVLS-DDLCQCYNGVVLSTESS--VAVYGTLNLTPKGkqapgghELS--CDFWELV------ 178
Cdd:PRK00484 69 MGK-ASFATLQDGSGRIQLYVSkDDVGEEALEAFKKLDLGdiIGVEGTLFKTKTG-------ELSvkATELTLLtkslrp 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 179 ------GLapaggadnlineeSDVDVQLNNRHM-MIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLvQTqVEGG 251
Cdd:PRK00484 141 lpdkfhGL-------------TDVETRYRQRYVdLIVNPESRETFRKRSKIISAIRRFLDNRGFLEVETPML-QP-IAGG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 252 ATL--FK--LDYFGEEAFLTQSSQLYLETCLpaLGD---VFCIAQSYRAEQSRTrRHLAEFTHVEAECPFLTFEDLLNRL 324
Cdd:PRK00484 206 AAArpFIthHNALDIDLYLRIAPELYLKRLI--VGGferVYEIGRNFRNEGIDT-RHNPEFTMLEFYQAYADYNDMMDLT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 325 EDLVCDVVDRVLKSPVasIVY---ELnpNFKPpkrPFRRMNYSDAI-----------------EWLKEHDVKKEDgtFYE 384
Cdd:PRK00484 283 EELIRHLAQAVLGTTK--VTYqgtEI--DFGP---PFKRLTMVDAIkeytgvdfddmtdeearALAKELGIEVEK--SWG 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 385 FGDDIPEAPERLMTDTINEPILLCRFPVEI----KsfymqRCPEDPRLTESVDVlmpnvgeIVGGSmrswdseEILEGYK 460
Cdd:PRK00484 354 LGKLINELFEEFVEPKLIQPTFITDYPVEIsplaK-----RHREDPGLTERFEL-------FIGGR-------EIANAFS 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1781905169 461 rEGIDPApyywytDQRK----------------------------YGTCPHGGYGLGLERFLSWILNRYHIRDVCLYP 510
Cdd:PRK00484 415 -ELNDPI------DQRErfeaqveakeagddeamfmdedflraleYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
95-369 |
1.12e-19 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 92.44 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 95 GQRVKVFGWVHRLRRQGkNLMFLVLRDGTGYLQCVLSDDLCQCYNGVVLSTESSVAVYGTLNLTPKG----KQAPGGHEL 170
Cdd:PRK00476 17 GQTVTLCGWVHRRRDHG-GLIFIDLRDREGIVQVVFDPDAEAFEVAESLRSEYVIQVTGTVRARPEGtvnpNLPTGEIEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 171 SCDFWELvgLAPaggADNL---INEESDV--DVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQ 245
Cdd:PRK00476 96 LASELEV--LNK---SKTLpfpIDDEEDVseELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDDNGFLEIETPILTK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 246 TQVEgGATlfklDYF-------GEeaF--LTQSSQL------------YletclpalgdvFCIAQSYRAEQSRTRRhLAE 304
Cdd:PRK00476 171 STPE-GAR----DYLvpsrvhpGK--FyaLPQSPQLfkqllmvagfdrY-----------YQIARCFRDEDLRADR-QPE 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1781905169 305 FTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPVasivyelnpnfkppKRPFRRMNYSDAIEW 369
Cdd:PRK00476 232 FTQIDIEMSFVTQEDVMALMEGLIRHVFKEVLGVDL--------------PTPFPRMTYAEAMRR 282
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
216-510 |
6.32e-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: 6.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 216 LKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGAtlfklDYF-------GEEAFLTQSSQLYLETCLPA-LGDVFCI 287
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTPEGAR-----DFLvpsrlhpGKFYALPQSPQLFKQLLMVSgFDRYFQI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 288 AQSYRAEQSRTRRHlAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKspvasivyelnpnfKPPKRPFRRMNYSDAI 367
Cdd:cd00777 76 ARCFRDEDLRADRQ-PEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG--------------VELTTPFPRMTYAEAM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 368 E-------W-----LKEHDvkKEDGTfYEFGDDIPEAPERLMTDTINEpillcrFPVEIKSfymqrcpedprltESVDVL 435
Cdd:cd00777 141 ErygfkflWivdfpLFEWD--EEEGR-LVSAHHPFTAPKEEDLDLLEK------DPEDARA-------------QAYDLV 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1781905169 436 MpNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYY----WYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYP 510
Cdd:cd00777 199 L-NGVELGGGSIRIHDPDIQEKVFEILGLSEEEAEekfgFLLEAFKYGAPPHGGIALGLDRLVMLLTGSESIRDVIAFP 276
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
95-368 |
8.88e-18 |
|
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: 8.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 95 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLC--QCYN-GVVLSTESSVAVYGTLNLTPKGKQAP----GG 167
Cdd:PRK12820 18 GREVCLAGWVDAFRDHGE-LLFIHLRDRNGFIQAVFSPEAApaDVYElAASLRAEFCVALQGEVQKRLEETENPhietGD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 168 HELSCDfwELVGLAPA------------------GGADNlINEesdvDVQLNNRHMMIRGENMSKILKARSMITRCFRDH 229
Cdd:PRK12820 97 IEVFVR--ELSILAASealpfaisdkamtagagsAGADA-VNE----DLRLQYRYLDIRRPAMQDHLAKRHRIIKCARDF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 230 FFDRGYCEVTTPTLVQTQVEGGATLFKLDYFGEEAF--LTQSSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHlAEFT 306
Cdd:PRK12820 170 LDSRGFLEIETPILTKSTPEGARDYLVPSRIHPKEFyaLPQSPQLFKQLLMIAgFERYFQLARCFRDEDLRPNRQ-PEFT 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1781905169 307 HVEAECPFLTFEDLLNRLEDLVCDVVDrvlkspVASIvyELNpnfkppkRPFRRMNYSDAIE 368
Cdd:PRK12820 249 QLDIEASFIDEEFIFELIEELTARMFA------IGGI--ALP-------RPFPRMPYAEAMD 295
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
95-369 |
1.66e-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: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 95 GQRVKVFGWVHRLRRQGkNLMFLVLRDGTGYLQCVLSDDlcqcYNGVVLST------ESSVAVYGTLNLTPKG----KQA 164
Cdd:COG0173 16 GQEVTLSGWVHRRRDHG-GLIFIDLRDRYGITQVVFDPD----DSAEAFEKaeklrsEYVIAVTGKVRARPEGtvnpKLP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 165 PGGHELSCDfwELVGLAPaggADNL---INEESDV--DVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVT 239
Cdd:COG0173 91 TGEIEVLAS--ELEILNK---AKTPpfqIDDDTDVseELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDENGFLEIE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 240 TPTLVQTQVEgGATlfklDYF-------GEeaF--LTQSSQL------------YletclpalgdvFCIAQSYRAEQSRT 298
Cdd:COG0173 166 TPILTKSTPE-GAR----DYLvpsrvhpGK--FyaLPQSPQLfkqllmvsgfdrY-----------FQIARCFRDEDLRA 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1781905169 299 RRHlAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKspvasivYELnpnfkppKRPFRRMNYSDAIEW 369
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 ... |
98-178 |
1.02e-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: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 98 VKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVL-SDDLCQCYNgvVLSTESSVAVYGTLNLTPKgkqapGGHELSCDFWE 176
Cdd:pfam01336 1 VTVAGRVTSIRRSGGKLLFLTLRDGTGSIQVVVfKEEAEKLAK--KLKEGDVVRVTGKVKKRKG-----GELELVVEEIE 73
|
..
gi 1781905169 177 LV 178
Cdd:pfam01336 74 LL 75
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
98-517 |
1.65e-13 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 73.14 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 98 VKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLS-------DDLCQCYngVVLSTESSVAVYGTLNLTPKGkqapgghEL 170
Cdd:PTZ00385 110 VRVAGRVTSVRDIGK-IIFVTIRSNGNELQVVGQvgehftrEDLKKLK--VSLRVGDIIGADGVPCRMQRG-------EL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 171 SCDFWELVGLAPAGGADNLINEE-------SDVDVQLNNRHM-MIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPT 242
Cdd:PTZ00385 180 SVAASRMLILSPYVCTDQVVCPNlrgftvlQDNDVKYRYRFTdMMTNPCVIETIKKRHVMLQALRDYFNERNFVEVETPV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 243 LVQTQVEGGATLFKLDYFGEEA--FLTQSSQLYLETCL-PALGDVFCIAQSYRAEQSrTRRHLAEFTHVEAECPFLTFED 319
Cdd:PTZ00385 260 LHTVASGANAKSFVTHHNANAMdlFLRVAPELHLKQCIvGGMERIYEIGKVFRNEDA-DRSHNPEFTSCEFYAAYHTYED 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 320 LLNRLEDLVCDVVDRVLKSPVASIVYEL---NPNFKPPKRPFRRMNYSDAI------EWLKEHDVKKEDGTFY----EFG 386
Cdd:PTZ00385 339 LMPMTEDIFRQLAMRVNGTTVVQIYPENahgNPVTVDLGKPFRRVSVYDEIqrmsgvEFPPPNELNTPKGIAYmsvvMLR 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 387 DDIPEAPER------------LMTDTINEPILLCRFPVEIKSFYMQRCPEdPRLTESVDVLMPNVgEIVGGSMRSWDSEE 454
Cdd:PTZ00385 419 YNIPLPPVRtaakmfeklidfFITDRVVEPTFVMDHPLFMSPLAKEQVSR-PGLAERFELFVNGI-EYCNAYSELNDPHE 496
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1781905169 455 ILEGYKREGID-------PAPY-YWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCR 517
Cdd:PTZ00385 497 QYHRFQQQLVDrqggdeeAMPLdETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFPLLRQDIR 567
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
195-510 |
5.19e-12 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 68.16 E-value: 5.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 195 DVDVQLNNRHM-MIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLvqTQVEGGAT----LFKLDYFGEEAFLTQS 269
Cdd:PRK12445 162 DQEVRYRQRYLdLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMM--QVIPGGASarpfITHHNALDLDMYLRIA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 270 SQLYLET-CLPALGDVFCIAQSYRAEqSRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVL---KSPVASIVY 345
Cdd:PRK12445 240 PELYLKRlVVGGFERVFEINRNFRNE-GISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLgttKVTYGEHVF 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 346 ELNPNFKP-----------PKRPFRRMNYSDAIEWLKEH---DVKKEDGtfyeFGDDIPEAPERLMTDTINEPILLCRFP 411
Cdd:PRK12445 319 DFGKPFEKltmreaikkyrPETDMADLDNFDAAKALAESigiTVEKSWG----LGRIVTEIFDEVAEAHLIQPTFITEYP 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 412 VEIKSFyMQRCPEDPRLTESVDVLMPNvGEIVGGSMRSWDSEEILEGY------KREGIDPAPYYW--YTDQRKYGTCPH 483
Cdd:PRK12445 395 AEVSPL-ARRNDVNPEITDRFEFFIGG-REIGNGFSELNDAEDQAERFqeqvnaKAAGDDEAMFYDedYVTALEYGLPPT 472
|
330 340
....*....|....*....|....*..
gi 1781905169 484 GGYGLGLERFLSWILNRYHIRDVCLYP 510
Cdd:PRK12445 473 AGLGIGIDRMIMLFTNSHTIRDVILFP 499
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
97-205 |
6.22e-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: 62.16 E-value: 6.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 97 RVKVFGWVHRLRRQGKNLmFLVLRDGTGYLQCVLSDDLCQ--CYNGVVLSTESSVAVYGTLNLTPKgkqAPGGHELSCDF 174
Cdd:cd04319 1 KVTLAGWVYRKREVGKKA-FIVLRDSTGIVQAVFSKDLNEeaYREAKKVGIESSVIVEGAVKADPR---APGGAEVHGEK 76
|
90 100 110
....*....|....*....|....*....|..
gi 1781905169 175 WELVGLapaggADNL-INEESDVDVQLNNRHM 205
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 ... |
95-170 |
1.36e-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: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 95 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVL-----SDDLCQCYNGvvLSTESSVAVYGTLNLTPKgkqAPGGHE 169
Cdd:cd04316 12 GEEVTVAGWVHEIRDLGG-IKFVILRDREGIVQVTApkkkvDKELFKTVRK--LSRESVISVTGTVKAEPK---APNGVE 85
|
.
gi 1781905169 170 L 170
Cdd:cd04316 86 I 86
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
216-430 |
1.31e-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: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 216 LKARSMITRCFRDHFFDRGYCEVTTPTLVQTqvegGAT-----LFKLDYFGEEAfltQSSQLYLETC--------LPA-L 281
Cdd:COG2269 6 LRARARLLAAIRAFFAERGVLEVETPALSVA----PGTdphldSFATEFIGPDG---GGRPLYLHTSpefamkrlLAAgS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 282 GDVFCIAQSYRAEQsRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSpvasivyelnpnfkppkrPFRRM 361
Cdd:COG2269 79 GPIYQIAKVFRNGE-RGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAAGFA------------------PAERL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 362 NYSDA-----------------IEWLKEHDVKKEDgtfyefGDDIPEAPERLMTDTI------NEPILLCRFPVEiksfy 418
Cdd:COG2269 140 SYQEAflrylgidpltadldelAAAAAAAGLRVAD------DDDRDDLLDLLLSERVepqlgrDRPTFLYDYPAS----- 208
|
250
....*....|....*..
gi 1781905169 419 mQ-----RCPEDPRLTE 430
Cdd:COG2269 209 -QaalarISPDDPRVAE 224
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
98-173 |
1.79e-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: 1.79e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1781905169 98 VKVFGWVhRLRRQGKNLMFLVLRDGTGY--LQCVLSDDLCQCYNGVVLSTESSVAVYGTLNLTPKGKQApggHELSCD 173
Cdd:cd04318 2 VTVNGWV-RSVRDSKKISFIELNDGSCLknLQVVVDKELTNFKEILKLSTGSSIRVEGVLVKSPGAKQP---FELQAE 75
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
98-510 |
6.01e-10 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 61.55 E-value: 6.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 98 VKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVL----SDDLCQCYNGVVLSTESS--VAVYGTLNLTPKGkqapgghELS 171
Cdd:PLN02502 111 VSVAGRIMAKRAFGK-LAFYDLRDDGGKIQLYAdkkrLDLDEEEFEKLHSLVDRGdiVGVTGTPGKTKKG-------ELS 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 172 CDFWELVGLAPA-----GGADNLineeSDVDVQLNNRHM-MIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLvQ 245
Cdd:PLN02502 183 IFPTSFEVLTKCllmlpDKYHGL----TDQETRYRQRYLdLIANPEVRDIFRTRAKIISYIRRFLDDRGFLEVETPML-N 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 246 TQVeGGATL--FKLDY--FGEEAFLTQSSQLYL-ETCLPALGDVFCIAQSYRAEQSRTrRHLAEFTHVEAECPFLTFEDL 320
Cdd:PLN02502 258 MIA-GGAAArpFVTHHndLNMDLYLRIATELHLkRLVVGGFERVYEIGRQFRNEGIST-RHNPEFTTCEFYQAYADYNDM 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 321 LNRLEDLVCdvvdrvlkspvaSIVYELNPNFKPP--------KRPFRRMnysDAIEWLKE-------HDVKKEDGTFY-- 383
Cdd:PLN02502 336 MELTEEMVS------------GMVKELTGSYKIKyhgieidfTPPFRRI---SMISLVEEatgidfpADLKSDEANAYli 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 384 ----EFGDDIPEAP----------ERLMTDTINEPILLCRFPVEIkSFYMQRCPEDPRLTESVDVLmpnvgeIVGgsmrs 449
Cdd:PLN02502 401 aaceKFDVKCPPPQttgrllnelfEEFLEETLVQPTFVLDHPVEM-SPLAKPHRSKPGLTERFELF------ING----- 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 450 wdsEEILEGYKrEGIDPapyywyTDQRK----------------------------YGTCPHGGYGLGLERFLSWILNRY 501
Cdd:PLN02502 469 ---RELANAFS-ELTDP------VDQRErfeeqvkqhnagddeamaldedfctaleYGLPPTGGWGLGIDRLVMLLTDSA 538
|
....*....
gi 1781905169 502 HIRDVCLYP 510
Cdd:PLN02502 539 SIRDVIAFP 547
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
89-310 |
1.01e-09 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 61.13 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 89 ALEGYRGQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQCYN----GVVLSTESSVAVYGTLNLTPKGkqa 164
Cdd:PRK02983 645 ALDAPTGEEVSVSGRVLRIRDYGG-VLFADLRDWSGELQVLLDASRLEQGSladfRAAVDLGDLVEVTGTMGTSRNG--- 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 165 pgghELS--CDFWELVG--LAPaggadnLINEE---SDVDVQLNNRHM--MIRGENMSkILKARSMITRCFRDHFFDRGY 235
Cdd:PRK02983 721 ----TLSllVTSWRLAGkcLRP------LPDKWkglTDPEARVRQRYLdlAVNPEARD-LLRARSAVVRAVRETLVARGF 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 236 CEVTTPTLvQtQVEGGAT----LFKLDYFGEEAFLTQSSQLYLET-CLPALGDVFCIAQSYRAE-QSRTrrHLAEFTHVE 309
Cdd:PRK02983 790 LEVETPIL-Q-QVHGGANarpfVTHINAYDMDLYLRIAPELYLKRlCVGGVERVFELGRNFRNEgVDAT--HNPEFTLLE 865
|
.
gi 1781905169 310 A 310
Cdd:PRK02983 866 A 866
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
95-161 |
1.78e-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: 1.78e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1781905169 95 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLSDDLCQCYNGVV-LSTESSVAVYGTLNLTPKG 161
Cdd:cd04317 14 GQEVTLCGWVQRRRDHGG-LIFIDLRDRYGIVQVVFDPEEAPEFELAEkLRNESVIQVTGKVRARPEG 80
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
195-510 |
4.83e-09 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 58.87 E-value: 4.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 195 DVDVQLNNRHM-MIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLvqTQVEGGATlfkldyfgEEAFLTQSSQLY 273
Cdd:PTZ00417 231 DTEIRYRQRYLdLMINESTRSTFITRTKIINYLRNFLNDRGFIEVETPTM--NLVAGGAN--------ARPFITHHNDLD 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 274 LE------TCLP-------ALGDVFCIAQSYRAEqSRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSpv 340
Cdd:PTZ00417 301 LDlylriaTELPlkmlivgGIDKVYEIGKVFRNE-GIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHLFGT-- 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 341 ASIVY-----ELNP---NFKPpkrPFRRMNYSDAIEWLKE----------HDVKKEDGTFYEFGDDIPEAP------ERL 396
Cdd:PTZ00417 378 YKILYnkdgpEKDPieiDFTP---PYPKVSIVEELEKLTNtkleqpfdspETINKMINLIKENKIEMPNPPtaakllDQL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 397 MTDTI-----NEPILLCRFPvEIKSFYMQRCPEDPRLTESVDVLMPNvGEIVGGSMRSWDSEEILEGYK-----REGIDP 466
Cdd:PTZ00417 455 ASHFIenkypNKPFFIIEHP-QIMSPLAKYHRSKPGLTERLEMFICG-KEVLNAYTELNDPFKQKECFSaqqkdREKGDA 532
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1781905169 467 APYYW---YTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYP 510
Cdd:PTZ00417 533 EAFQFdaaFCTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFP 579
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
212-506 |
9.69e-09 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 56.86 E-value: 9.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 212 MSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQ-TQVEGGATLFKLDYFGEEAflTQSSQLYLETC--------LPAL- 281
Cdd:PRK09350 1 SIPNLLKRAKIIAEIRRFFADRGVLEVETPILSQaTVTDIHLVPFETRFVGPGA--SQGKTLWLMTSpeyhmkrlLAAGs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 282 GDVFCIAQSYRAEQSrTRRHLAEFTHVEAECPFLTFEDLLNRLEDLvcdvVDRVLKS-PVASIVYE--------LNPnFK 352
Cdd:PRK09350 79 GPIFQICKSFRNEEA-GRYHNPEFTMLEWYRPHYDMYRLMNEVDDL----LQQVLDCePAESLSYQqaflrylgIDP-LS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 353 PPKRPFRrmnysDAIEWLKEHDVKKEDgtfyefgDDIPEAPERLMTDTI------NEPILLCRFPVEIKSfYMQRCPEDP 426
Cdd:PRK09350 153 ADKTQLR-----EVAAKLGLSNIADEE-------EDRDTLLQLLFTFGVepnigkEKPTFVYHFPASQAA-LAKISTEDH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 427 RLTESVDVLMPNVgEIVGGSMRSWDSEEILEGYKR-------EGIDPAPyywyTDQR-----KYGTCPHGGYGLGLERFL 494
Cdd:PRK09350 220 RVAERFEVYFKGI-ELANGFHELTDAREQRQRFEQdnrkraaRGLPQQP----IDENliaalEAGLPDCSGVALGVDRLI 294
|
330
....*....|..
gi 1781905169 495 SWILNRYHIRDV 506
Cdd:PRK09350 295 MLALGAESISEV 306
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
98-160 |
5.07e-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: 5.07e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1781905169 98 VKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVLSDDlcqcyNGVV----------LSTESSVAVYGTLNLTPK 160
Cdd:cd04320 2 VLIRARVHTSRAQGAKLAFLVLRQQGYTIQGVLAAS-----AEGVskqmvkwagsLSKESIVDVEGTVKKPEE 69
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
230-430 |
7.20e-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: 7.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 230 FFDRGYCEVTTPTLVQtqveGGATLFKLDYF--GEEAFLTQSSQLYLET----CLPAL-----GDVFCIAQSYRAEQsRT 298
Cdd:TIGR00462 2 FAERGVLEVETPLLSP----APVTDPHLDAFatEFVGPDGQGRPLYLQTspeyAMKRLlaagsGPIFQICKVFRNGE-RG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 299 RRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVvdrvlkspvasivyelnpnFKPPKRPFRRMNYSDA-IEWLKEHDVKK 377
Cdd:TIGR00462 77 RRHNPEFTMLEWYRPGFDYHDLMDEVEALLQEL-------------------LGDPFAPAERLSYQEAfLRYAGIDPLTA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1781905169 378 EDGTFYE----FGDDIPEAP------ERLMTDTI------NEPILLCRFPVEIKSFyMQRCPEDPRLTE 430
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 ... |
219-320 |
1.53e-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: 49.04 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 219 RSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGATLFKLD------YFGEEAFLTQSSQLYLET----CLPALGD-VFCI 287
Cdd:cd00768 2 RSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHEPKDllpvgaENEEDLYLRPTLEPGLVRlfvsHIRKLPLrLAEI 81
|
90 100 110
....*....|....*....|....*....|....
gi 1781905169 288 AQSYRAEQSRTR-RHLAEFTHVEAECPFLTFEDL 320
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 ... |
97-178 |
1.82e-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: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781905169 97 RVKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVLSDDLCQCYNGV-VLSTESSVAVYGTLNLtpkgKQAPGGHELSCdfW 175
Cdd:cd04321 1 KVTLNGWIDRKPRIVKKLSFADLRDPNGDIIQLVSTAKKDAFSLLkSITAESPVQVRGKLQL----KEAKSSEKNDE--W 74
|
...
gi 1781905169 176 ELV 178
Cdd:cd04321 75 ELV 77
|
|
| |
