|
Name |
Accession |
Description |
Interval |
E-value |
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
224-543 |
2.30e-144 |
|
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: 418.51 E-value: 2.30e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 224 DVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYL 303
Cdd:cd00776 3 NLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQLYK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 304 ETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFL-TFDDLLNRLEDLVCDVVDRILKSPA--GSIVHELNPNF 380
Cdd:cd00776 83 EMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAkeLELVNQLNREL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 381 QPPKRPFKRMNYSDAIVWLKEHDVKKEDgtfyEFGEDIPEAPERLMTDTI-NEPILLCRFPVEIKSFYMQRCPEDSRLTE 459
Cdd:cd00776 163 LKPLEPFPRITYDEAIELLREKGVEEEV----KWGEDLSTEHERLLGEIVkGDPVFVTDYPKEIKPFYMKPDDDNPETVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 460 SVDVLMPNVGEIVGGSMRIFDSEEILAGYKREGIDPTPYYWYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYP 539
Cdd:cd00776 239 SFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
....
gi 530414204 540 RFVQ 543
Cdd:cd00776 319 RDPK 322
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
118-547 |
4.86e-142 |
|
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: 416.76 E-value: 4.86e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 118 ALEGYRGQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLADELCQCYNGVL-LSTESSVAVYGMLNLTPKgkqAPGG 196
Cdd:COG0017 8 LLPEHVGQEVTVAGWVRTKRDSGG-ISFLILRDGSGFIQVVVKKDKLENFEEAKkLTTESSVEVTGTVVESPR---APQG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 197 HELSCDFWELIGLA----PaggadnLINEESDVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTL 272
Cdd:COG0017 84 VELQAEEIEVLGEAdepyP------LQPKRHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVEVHTPII 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 273 VQTQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTFDDLLNR 352
Cdd:COG0017 158 TASATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMALEKVYTFGPTFRAEKSNTRRHLAEFWMIEPEMAFADLEDVMDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 353 LEDLVCDVVDRILKSpAGSIVHELNPNFQP----PKRPFKRMNYSDAIVWLKEHDVKkedgtfYEFGEDI-PEApERLMT 427
Cdd:COG0017 238 AEEMLKYIIKYVLEN-CPEELEFLGRDVERlekvPESPFPRITYTEAIEILKKSGEK------VEWGDDLgTEH-ERYLG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 428 DTI-NEPILLCRFPVEIKSFYMQRCPEDSRLTESVDVLMPNVGEIVGGSMRIFDSEEILAGYKREGIDPTPYYWYTDQRK 506
Cdd:COG0017 310 EEFfKKPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAPGIGEIIGGSQREHRYDVLVERIKEKGLDPEDYEWYLDLRR 389
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 530414204 507 YGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPRFVQRCTP 547
Cdd:COG0017 390 YGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
124-547 |
1.84e-140 |
|
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: 413.70 E-value: 1.84e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 124 GQRVKVFGWVHRlRRQGKNLMFLVLRDGT--GYLQCVLADELCQCYNGVL--LSTESSVAVYGMLNLTPKGKQapgGHEL 199
Cdd:TIGR00457 16 GDEVTVSGWVRT-KRSSKKIIFLELNDGSslGPIQAVINGEDNPYLFQLLksLTTGSSVSVTGKVVESPGKGQ---PVEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 200 SCDFWELIGLAPAGGADNLInEESDVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEG 279
Cdd:TIGR00457 92 QVKKIEVVGEAEPDDYPLQK-KEHSLEFLRDIAHLRLRTNTLGAVMRVRNALSQAIHRYFQENGFTWVSPPILTSNDCEG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 280 GATLFKL---------DYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTFDDLL 350
Cdd:TIGR00457 171 AGELFRVstgnidfsqDFFGKEAYLTVSGQLYLETYALALSKVYTFGPTFRAEKSNTSRHLSEFWMIEPEMAFANLNDLL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 351 NRLEDLVCDVVDRILKSPAGSiVHELNPNFQPPKRP---------FKRMNYSDAIVWLKEHDVKKEDGTFyeFGEDIPEA 421
Cdd:TIGR00457 251 QLAETLIKYIIKAVLENCSQE-LKFLEKNFDKDLIKrleniinnkFARITYTDAIEILKESDKNFEYEDF--WGDDLQTE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 422 PERLMTDTI-NEPILLCRFPVEIKSFYMQRCpEDSRLTESVDVLMPNVGEIVGGSMRIFDSEEILAGYKREGIDPTPYYW 500
Cdd:TIGR00457 328 HERFLAEEYfKPPVFVTNYPKDIKAFYMKLN-DDGKTVAAMDLLAPGIGEIIGGSEREDDLDKLENRMKEMGLDTDALNW 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 530414204 501 YTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPRFVQRCTP 547
Cdd:TIGR00457 407 YLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGNINF 453
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
120-547 |
1.71e-107 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 328.99 E-value: 1.71e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 120 EGYRGQRVKVFGWVHRlRRQGKNLMFLVLRDGTGYLQCVL-ADELCQCYNGVL-LSTESSVAVYGMLNLTPKgkqAPGGH 197
Cdd:PRK03932 12 GKYVGQEVTVRGWVRT-KRDSGKIAFLQLRDGSCFKQLQVvKDNGEEYFEEIKkLTTGSSVIVTGTVVESPR---AGQGY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 198 ELSCDFWELIGLAPAggaDNLINE-ESDVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQ 276
Cdd:PRK03932 88 ELQATKIEVIGEDPE---DYPIQKkRHSIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVDTPIITASD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 277 VEGGATLFKL---------DYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTFD 347
Cdd:PRK03932 165 CEGAGELFRVttldldfskDFFGKEAYLTVSGQLYAEAYAMALGKVYTFGPTFRAENSNTRRHLAEFWMIEPEMAFADLE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 348 DLLNRLEDLVCDVVDRIL-----------KSPAGSIVHELNpNFQPPkrPFKRMNYSDAIVWLKEHDVKKEDGTfyEFGE 416
Cdd:PRK03932 245 DNMDLAEEMLKYVVKYVLencpddleflnRRVDKGDIERLE-NFIES--PFPRITYTEAIEILQKSGKKFEFPV--EWGD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 417 DI--PEapERLMTDTINE-PILLCRFPVEIKSFYMQRCPEDsRLTESVDVLMPNVGEIVGGSMRIFDSEEILAGYKREGI 493
Cdd:PRK03932 320 DLgsEH--ERYLAEEHFKkPVFVTNYPKDIKAFYMRLNPDG-KTVAAMDLLAPGIGEIIGGSQREERLDVLEARIKELGL 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 530414204 494 DPTPYYWYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPRFVQRCTP 547
Cdd:PRK03932 397 NKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
224-540 |
4.72e-102 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 310.27 E-value: 4.72e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 224 DVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEGGATLFKL------DYFgeeaFLTQ 297
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVpsralgKFY----ALPQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 298 SSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHLaEYTHVEAECPFLTFDDLLNRLEDLVCDVVDRILKSPAGsivhEL 376
Cdd:pfam00152 77 SPQLYKQLLMVAgFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKE----LE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 377 NPNFQPPKRPFKRMNYSDAIVWLKEHDVkkedgtfYEFGEDIPEAPERLMTD-----TINEPILLCRFPVEIKSFYMQRC 451
Cdd:pfam00152 152 GGTLLDLKKPFPRITYAEAIEKLNGKDV-------EELGYGSDKPDLRFLLElvidkNKFNPLWVTDFPAEHHPFTMPKD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 452 PEDSRLTESVDVLMPNVgEIVGGSMRIFDSEEILAGYKREGIDP----TPYYWYTDQRKYGTCPHGGYGLGLERFLTWIL 527
Cdd:pfam00152 225 EDDPALAEAFDLVLNGV-EIGGGSIRIHDPELQEERFEEQGLDPeeaeEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLT 303
|
330
....*....|...
gi 530414204 528 NRYHIRDVCLYPR 540
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 ... |
126-208 |
2.34e-39 |
|
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and Saccharomyces cerevisiae cytoplasmic asparaginyl-tRNA synthetase (AsnRS), in Brugia malayai AsnRs and, in various putative bacterial AsnRSs. This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. AsnRS is immunodominant antigen of the filarial nematode B. malayai and of interest as a target for anti-parasitic drug design. Human AsnRS has been shown to be a pro-inflammatory chemokine which interacts with CCR3 chemokine receptors on T cells, immature dendritic cells and macrophages.
Pssm-ID: 239818 [Multi-domain] Cd Length: 84 Bit Score: 138.14 E-value: 2.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 126 RVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLADELCQ-CYNGVLLSTESSVAVYGMLNLTPKGKQAPGGHELSCDFW 204
Cdd:cd04323 1 RVKVFGWVHRLRSQKK-LMFLVLRDGTGFLQCVLSKKLVTeFYDAKSLTQESSVEVTGEVKEDPRAKQAPGGYELQVDYL 79
|
....
gi 530414204 205 ELIG 208
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 ... |
127-207 |
4.37e-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: 64.56 E-value: 4.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 127 VKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVL-ADELCQCYNgvLLSTESSVAVYGMLNLTPKgkqapGGHELSCDFWE 205
Cdd:pfam01336 1 VTVAGRVTSIRRSGGKLLFLTLRDGTGSIQVVVfKEEAEKLAK--KLKEGDVVRVTGKVKKRKG-----GELELVVEEIE 73
|
..
gi 530414204 206 LI 207
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 ... |
224-543 |
2.30e-144 |
|
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: 418.51 E-value: 2.30e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 224 DVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYL 303
Cdd:cd00776 3 NLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQLYK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 304 ETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFL-TFDDLLNRLEDLVCDVVDRILKSPA--GSIVHELNPNF 380
Cdd:cd00776 83 EMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAkeLELVNQLNREL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 381 QPPKRPFKRMNYSDAIVWLKEHDVKKEDgtfyEFGEDIPEAPERLMTDTI-NEPILLCRFPVEIKSFYMQRCPEDSRLTE 459
Cdd:cd00776 163 LKPLEPFPRITYDEAIELLREKGVEEEV----KWGEDLSTEHERLLGEIVkGDPVFVTDYPKEIKPFYMKPDDDNPETVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 460 SVDVLMPNVGEIVGGSMRIFDSEEILAGYKREGIDPTPYYWYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYP 539
Cdd:cd00776 239 SFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
....
gi 530414204 540 RFVQ 543
Cdd:cd00776 319 RDPK 322
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
118-547 |
4.86e-142 |
|
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: 416.76 E-value: 4.86e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 118 ALEGYRGQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLADELCQCYNGVL-LSTESSVAVYGMLNLTPKgkqAPGG 196
Cdd:COG0017 8 LLPEHVGQEVTVAGWVRTKRDSGG-ISFLILRDGSGFIQVVVKKDKLENFEEAKkLTTESSVEVTGTVVESPR---APQG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 197 HELSCDFWELIGLA----PaggadnLINEESDVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTL 272
Cdd:COG0017 84 VELQAEEIEVLGEAdepyP------LQPKRHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVEVHTPII 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 273 VQTQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTFDDLLNR 352
Cdd:COG0017 158 TASATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMALEKVYTFGPTFRAEKSNTRRHLAEFWMIEPEMAFADLEDVMDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 353 LEDLVCDVVDRILKSpAGSIVHELNPNFQP----PKRPFKRMNYSDAIVWLKEHDVKkedgtfYEFGEDI-PEApERLMT 427
Cdd:COG0017 238 AEEMLKYIIKYVLEN-CPEELEFLGRDVERlekvPESPFPRITYTEAIEILKKSGEK------VEWGDDLgTEH-ERYLG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 428 DTI-NEPILLCRFPVEIKSFYMQRCPEDSRLTESVDVLMPNVGEIVGGSMRIFDSEEILAGYKREGIDPTPYYWYTDQRK 506
Cdd:COG0017 310 EEFfKKPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAPGIGEIIGGSQREHRYDVLVERIKEKGLDPEDYEWYLDLRR 389
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 530414204 507 YGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPRFVQRCTP 547
Cdd:COG0017 390 YGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
124-547 |
1.84e-140 |
|
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: 413.70 E-value: 1.84e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 124 GQRVKVFGWVHRlRRQGKNLMFLVLRDGT--GYLQCVLADELCQCYNGVL--LSTESSVAVYGMLNLTPKGKQapgGHEL 199
Cdd:TIGR00457 16 GDEVTVSGWVRT-KRSSKKIIFLELNDGSslGPIQAVINGEDNPYLFQLLksLTTGSSVSVTGKVVESPGKGQ---PVEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 200 SCDFWELIGLAPAGGADNLInEESDVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEG 279
Cdd:TIGR00457 92 QVKKIEVVGEAEPDDYPLQK-KEHSLEFLRDIAHLRLRTNTLGAVMRVRNALSQAIHRYFQENGFTWVSPPILTSNDCEG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 280 GATLFKL---------DYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTFDDLL 350
Cdd:TIGR00457 171 AGELFRVstgnidfsqDFFGKEAYLTVSGQLYLETYALALSKVYTFGPTFRAEKSNTSRHLSEFWMIEPEMAFANLNDLL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 351 NRLEDLVCDVVDRILKSPAGSiVHELNPNFQPPKRP---------FKRMNYSDAIVWLKEHDVKKEDGTFyeFGEDIPEA 421
Cdd:TIGR00457 251 QLAETLIKYIIKAVLENCSQE-LKFLEKNFDKDLIKrleniinnkFARITYTDAIEILKESDKNFEYEDF--WGDDLQTE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 422 PERLMTDTI-NEPILLCRFPVEIKSFYMQRCpEDSRLTESVDVLMPNVGEIVGGSMRIFDSEEILAGYKREGIDPTPYYW 500
Cdd:TIGR00457 328 HERFLAEEYfKPPVFVTNYPKDIKAFYMKLN-DDGKTVAAMDLLAPGIGEIIGGSEREDDLDKLENRMKEMGLDTDALNW 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 530414204 501 YTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPRFVQRCTP 547
Cdd:TIGR00457 407 YLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGNINF 453
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
120-547 |
1.71e-107 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 328.99 E-value: 1.71e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 120 EGYRGQRVKVFGWVHRlRRQGKNLMFLVLRDGTGYLQCVL-ADELCQCYNGVL-LSTESSVAVYGMLNLTPKgkqAPGGH 197
Cdd:PRK03932 12 GKYVGQEVTVRGWVRT-KRDSGKIAFLQLRDGSCFKQLQVvKDNGEEYFEEIKkLTTGSSVIVTGTVVESPR---AGQGY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 198 ELSCDFWELIGLAPAggaDNLINE-ESDVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQ 276
Cdd:PRK03932 88 ELQATKIEVIGEDPE---DYPIQKkRHSIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVDTPIITASD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 277 VEGGATLFKL---------DYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTFD 347
Cdd:PRK03932 165 CEGAGELFRVttldldfskDFFGKEAYLTVSGQLYAEAYAMALGKVYTFGPTFRAENSNTRRHLAEFWMIEPEMAFADLE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 348 DLLNRLEDLVCDVVDRIL-----------KSPAGSIVHELNpNFQPPkrPFKRMNYSDAIVWLKEHDVKKEDGTfyEFGE 416
Cdd:PRK03932 245 DNMDLAEEMLKYVVKYVLencpddleflnRRVDKGDIERLE-NFIES--PFPRITYTEAIEILQKSGKKFEFPV--EWGD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 417 DI--PEapERLMTDTINE-PILLCRFPVEIKSFYMQRCPEDsRLTESVDVLMPNVGEIVGGSMRIFDSEEILAGYKREGI 493
Cdd:PRK03932 320 DLgsEH--ERYLAEEHFKkPVFVTNYPKDIKAFYMRLNPDG-KTVAAMDLLAPGIGEIIGGSQREERLDVLEARIKELGL 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 530414204 494 DPTPYYWYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPRFVQRCTP 547
Cdd:PRK03932 397 NKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
224-540 |
4.72e-102 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 310.27 E-value: 4.72e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 224 DVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEGGATLFKL------DYFgeeaFLTQ 297
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVpsralgKFY----ALPQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 298 SSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHLaEYTHVEAECPFLTFDDLLNRLEDLVCDVVDRILKSPAGsivhEL 376
Cdd:pfam00152 77 SPQLYKQLLMVAgFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKE----LE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 377 NPNFQPPKRPFKRMNYSDAIVWLKEHDVkkedgtfYEFGEDIPEAPERLMTD-----TINEPILLCRFPVEIKSFYMQRC 451
Cdd:pfam00152 152 GGTLLDLKKPFPRITYAEAIEKLNGKDV-------EELGYGSDKPDLRFLLElvidkNKFNPLWVTDFPAEHHPFTMPKD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 452 PEDSRLTESVDVLMPNVgEIVGGSMRIFDSEEILAGYKREGIDP----TPYYWYTDQRKYGTCPHGGYGLGLERFLTWIL 527
Cdd:pfam00152 225 EDDPALAEAFDLVLNGV-EIGGGSIRIHDPELQEERFEEQGLDPeeaeEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLT 303
|
330
....*....|...
gi 530414204 528 NRYHIRDVCLYPR 540
Cdd:pfam00152 304 GLESIREVIAFPK 316
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
124-547 |
1.99e-97 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 302.49 E-value: 1.99e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 124 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVL-ADELCQCYNGV-LLSTESSVAVYGMLNLTPKgkqAPGGHELSC 201
Cdd:PRK05159 16 GEEVTLAGWVHEIRDLGG-IAFLILRDRSGIIQVVVkKKVDEELFETIkKLKRESVVSVTGTVKANPK---APGGVEVIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 202 DFWELIGLApaggADNL---INEES--DVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQ 276
Cdd:PRK05159 92 EEIEVLNKA----EEPLpldISGKVlaELDTRLDNRFLDLRRPRVRAIFKIRSEVLRAFREFLYENGFTEIFTPKIVASG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 277 VEGGATLFKLDYFGEEAFLTQSSQLYLETCLPALGD-VFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLT-FDDLLNRLE 354
Cdd:PRK05159 168 TEGGAELFPIDYFEKEAYLAQSPQLYKQMMVGAGFErVFEIGPVFRAEEHNTSRHLNEYTSIDVEMGFIDdHEDVMDLLE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 355 DLVCDVVDRILKSPAGSIVhELNPNFQPPKRPFKRMNYSDAIvwlkehDVKKEDGTFYEFGEDIPEAPERLMTDTINE-- 432
Cdd:PRK05159 248 NLLRYMYEDVAENCEKELE-LLGIELPVPETPIPRITYDEAI------EILKSKGNEISWGDDLDTEGERLLGEYVKEey 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 433 ---PILLCRFPVEIKSFYMQRCPEDSRLTESVDVLMPNVgEIVGGSMRIFDSEEILAGYKREGIDPTPYYWYTDQRKYGT 509
Cdd:PRK05159 321 gsdFYFITDYPSEKRPFYTMPDEDDPEISKSFDLLFRGL-EITSGGQRIHRYDMLVESIKEKGLNPESFEFYLEAFKYGM 399
|
410 420 430
....*....|....*....|....*....|....*...
gi 530414204 510 CPHGGYGLGLERFLTWILNRYHIRDVCLYPRFVQRCTP 547
Cdd:PRK05159 400 PPHGGFGLGLERLTMKLLGLENIREAVLFPRDRHRLTP 437
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
75-547 |
1.10e-52 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 187.61 E-value: 1.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 75 KSESREKKEAEDSLRREKNLEEAKKITIKNDP---------------SLPEPKCVKIGAL-EGYRGQRVKVFGWVHRLRR 138
Cdd:PLN02850 16 KAAKKAAAKAEKLRREATAKAAAASLEDEDDPlasnygdvpleelqsKVTGREWTDVSDLgEELAGSEVLIRGRVHTIRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 139 QGKnLMFLVLRDGTGYLQCVL-ADELCQCYNGV----LLSTESSVAVYGMLNLTPKG-KQAPGGHELSCDFWELIGLAPA 212
Cdd:PLN02850 96 KGK-SAFLVLRQSGFTVQCVVfVSEVTVSKGMVkyakQLSRESVVDVEGVVSVPKKPvKGTTQQVEIQVRKIYCVSKALA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 213 GGADNLIN---EESDV---------------DVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQ 274
Cdd:PLN02850 175 TLPFNVEDaarSESEIekalqtgeqlvrvgqDTRLNNRVLDLRTPANQAIFRIQSQVCNLFREFLLSKGFVEIHTPKLIA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 275 TQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPfltfddlLNRL 353
Cdd:PLN02850 255 GASEGGSAVFRLDYKGQPACLAQSPQLHKQMAICGdFRRVFEIGPVFRAEDSFTHRHLCEFTGLDLEME-------IKEH 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 354 EDLVCDVVDRILKspagSIVHELNPN-------------FQPPK--RPFKRMNYSDAIVWLKEHDVKKEDgtfyefGEDI 418
Cdd:PLN02850 328 YSEVLDVVDELFV----AIFDGLNERckkeleaireqypFEPLKylPKTLRLTFAEGIQMLKEAGVEVDP------LGDL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 419 PEAPERLMTDTINEP-----ILLCRFPVEIKSFYMQRCPEDSRLTESVDVLMPNvGEIVGGSMRIFDSEEILAGYKREGI 493
Cdd:PLN02850 398 NTESERKLGQLVKEKygtdfYILHRYPLAVRPFYTMPCPDDPKYSNSFDVFIRG-EEIISGAQRVHDPELLEKRAEECGI 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 530414204 494 DPTPYYWYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPRFVQRCTP 547
Cdd:PLN02850 477 DVKTISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPRDPQRLAP 530
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
114-540 |
5.75e-48 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 175.16 E-value: 5.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 114 VKIGALEG--YRGQRVKVFGWVHRLRRQgKNLMFLVLRDGT--GYLQCVLADElCQCYNGV---LLSTESSVAVYGMLNL 186
Cdd:PLN02603 95 VKGGEDEGlaRVGKTLNVMGWVRTLRAQ-SSVTFIEVNDGSclSNMQCVMTPD-AEGYDQVesgLITTGASVLVQGTVVS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 187 TPKGKQAPgghELSCDFWELIGlapaggadnlineESDVDVQLNNR-----------HMMIRGENMSKILKARSMVTRCF 255
Cdd:PLN02603 173 SQGGKQKV---ELKVSKIVVVG-------------KSDPSYPIQKKrvsreflrtkaHLRPRTNTFGAVARVRNALAYAT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 256 RDHFFDRGYYEVTPP-----------------TLVQTQVEGGATLFK-------------LDYFGEEAFLTQSSQLYLET 305
Cdd:PLN02603 237 HKFFQENGFVWVSSPiitasdcegageqfcvtTLIPNSAENGGSLVDdipktkdglidwsQDFFGKPAFLTVSGQLNGET 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 306 CLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTFDDLLNRLEDLVCDVVDRILKSPA-----------GSIVH 374
Cdd:PLN02603 317 YATALSDVYTFGPTFRAENSNTSRHLAEFWMIEPELAFADLNDDMACATAYLQYVVKYILENCKedmeffntwieKGIID 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 375 ELNpnfQPPKRPFKRMNYSDAIVWLKEhdVKKEDGTFYEFGEDIPEAPERLMTDTI--NEPILLCRFPVEIKSFYMqRCP 452
Cdd:PLN02603 397 RLS---DVVEKNFVQLSYTDAIELLLK--AKKKFEFPVKWGLDLQSEHERYITEEAfgGRPVIIRDYPKEIKAFYM-REN 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 453 EDSRLTESVDVLMPNVGEIVGGSMRIFDSEEILAGYKREGIDPTPYYWYTDQRKYGTCPHGGYGLGLERFLTWILNRYHI 532
Cdd:PLN02603 471 DDGKTVAAMDMLVPRVGELIGGSQREERLEYLEARLDELKLNKESYWWYLDLRRYGSVPHAGFGLGFERLVQFATGIDNI 550
|
....*...
gi 530414204 533 RDVCLYPR 540
Cdd:PLN02603 551 RDAIPFPR 558
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
121-541 |
2.39e-47 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 173.64 E-value: 2.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 121 GYRGQRVKVFGWVHRLRRQGK-NLMFLVLRDGT--GYLQCVLADELCQCYNgvLLSTESSVAVYGMLNLTPKGKQAPGGH 197
Cdd:PLN02221 47 GLAGQKVRIGGWVKTGREQGKgTFAFLEVNDGScpANLQVMVDSSLYDLST--LVATGTCVTVDGVLKVPPEGKGTKQKI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 198 ELSCDfwELIGLAPAGGAD-NLINEESDVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQ 276
Cdd:PLN02221 125 ELSVE--KVIDVGTVDPTKyPLPKTKLTLEFLRDVLHLRSRTNSISAVARIRNALAFATHSFFQEHSFLYIHTPIITTSD 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 277 VEGGATLFKL---------------------------------------------------------------------- 286
Cdd:PLN02221 203 CEGAGEMFQVttlinyterleqdlidnpppteadveaarlivkergevvaqlkaakaskeeitaavaelkiakeslahie 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 287 --------------------DYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTF 346
Cdd:PLN02221 283 ersklkpglpkkdgkidyskDFFGRQAFLTVSGQLQVETYACALSSVYTFGPTFRAENSHTSRHLAEFWMVEPEIAFADL 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 347 DDLLNRLEDLVCDVVDRILKSpAGSIVHELNPNFQP---------PKRPFKRMNYSDAIVWLKEHDVK-KEDGTFYEFGE 416
Cdd:PLN02221 363 EDDMNCAEAYVKYMCKWLLDK-CFDDMELMAKNFDSgcidrlrmvASTPFGRITYTEAIELLEEAVAKgKEFDNNVEWGI 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 417 DIPEAPERLMTDTI-NEPILLCRFPVEIKSFYMqRCPEDSRLTESVDVLMPNVGEIVGGSMRIFDSEEILAGYKREGIDP 495
Cdd:PLN02221 442 DLASEHERYLTEVLfQKPLIVYNYPKGIKAFYM-RLNDDEKTVAAMDVLVPKVGELIGGSQREERYDVIKQRIEEMGLPI 520
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 530414204 496 TPYYWYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPRF 541
Cdd:PLN02221 521 EPYEWYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPRY 566
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
236-540 |
2.29e-46 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 165.58 E-value: 2.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 236 IRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLvqTQV-----EGGATL----FKLDYFGEEAFLTQSSQLYLETC 306
Cdd:PRK06462 21 ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPII--SPStdplmGLGSDLpvkqISIDFYGVEYYLADSMILHKQLA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 307 LPALGDVFCIAQSYRAEQ--SRTRRHLAEYTHVEAECPFLTFDDLLNRLEDLVCDVVDRILKSPAGSIvHELNPNFQPPK 384
Cdd:PRK06462 99 LRMLGKIFYLSPNFRLEPvdKDTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHEDEL-EFFGRDLPHLK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 385 RPFKRMNYSDAIVWLKEHDVKKEDgtFYEFGEDIpeapERLMTDTINEPILLCRFPVEIKSFYMQRCPEDSRLTESVDVL 464
Cdd:PRK06462 178 RPFKRITHKEAVEILNEEGCRGID--LEELGSEG----EKSLSEHFEEPFWIIDIPKGSREFYDREDPERPGVLRNYDLL 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530414204 465 MPN-VGEIVGGSMRIFDSEEILAGYKREGIDPTPYYWYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPR 540
Cdd:PRK06462 252 LPEgYGEAVSGGEREYEYEEIVERIREHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQPFPR 328
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
124-547 |
4.33e-45 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 167.09 E-value: 4.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 124 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLA----------DELCQcyngvlLSTESSVAVYGMLNLTPKGKQA 193
Cdd:PTZ00401 78 DKTVLIRARVSTTRKKGK-MAFMVLRDGSDSVQAMAAvegdvpkemiDFIGQ------IPTESIVDVEATVCKVEQPITS 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 194 PGGHELSCD------FWELIGLAPAGGADNLINEESD-----VDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDR 262
Cdd:PTZ00401 151 TSHSDIELKvkkihtVTESLRTLPFTLEDASRKESDEgakvnFDTRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLIDS 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 263 GYYEVTPPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHLAEYTHVEAEC 341
Cdd:PTZ00401 231 DFCEIHSPKIINAPSEGGANVFKLEYFNRFAYLAQSPQLYKQMVLQGdVPRVFEVGPVFRSENSNTHRHLTEFVGLDVEM 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 342 PFLT-FDDLLNRLEDLVCDVVDRILKS-----------PAGSIVHELNPNFQP------------PKRPFK--------- 388
Cdd:PTZ00401 311 RINEhYYEVLDLAESLFNYIFERLATHtkelkavcqqyPFEPLVWKLTPERMKelgvgvisegvePTDKYQarvhnmdsr 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 389 --RMNYSDAIVWLKEHDVKKEDGTfyefgEDIPEAPERLMTDTINEP-----ILLCRFPVEIKSFYMQRCPEDSRLTESV 461
Cdd:PTZ00401 391 mlRINYMHCIELLNTVLEEKMAPT-----DDINTTNEKLLGKLVKERygtdfFISDRFPSSARPFYTMECKDDERFTNSY 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 462 DVLMPNvGEIVGGSMRIFDSEEILAGYKREGIDPTPYYWYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPRF 541
Cdd:PTZ00401 466 DMFIRG-EEISSGAQRIHDPDLLLARAKMLNVDLTPIKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFPRD 544
|
....*.
gi 530414204 542 VQRCTP 547
Cdd:PTZ00401 545 PQRTTP 550
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
284-541 |
8.76e-41 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 155.57 E-value: 8.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 284 FKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTFDDLLNRLEDLVCDVVDR 363
Cdd:PTZ00425 317 YKKDFFSKQAFLTVSGQLSLENLCSSMGDVYTFGPTFRAENSHTSRHLAEFWMIEPEIAFADLYDNMELAESYIKYCIGY 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 364 ILKSPAGSIVH-ELNPNFQPPKR-------PFKRMNYSDAIVWLKEHDVKKEdgTFYEFGEDIPEAPERLMTDTI-NEPI 434
Cdd:PTZ00425 397 VLNNNFDDIYYfEENVETGLISRlknildeDFAKITYTNVIDLLQPYSDSFE--VPVKWGMDLQSEHERFVAEQIfKKPV 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 435 LLCRFPVEIKSFYMqRCPEDSRLTESVDVLMPNVGEIVGGSMRIFDSEEILAGYKREGIDPTPYYWYTDQRKYGTCPHGG 514
Cdd:PTZ00425 475 IVYNYPKDLKAFYM-KLNEDQKTVAAMDVLVPKIGEVIGGSQREDNLERLDKMIKEKKLNMESYWWYRQLRKFGSHPHAG 553
|
250 260
....*....|....*....|....*..
gi 530414204 515 YGLGLERFLTWILNRYHIRDVCLYPRF 541
Cdd:PTZ00425 554 FGLGFERLIMLVTGVDNIKDTIPFPRY 580
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
126-208 |
2.34e-39 |
|
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and Saccharomyces cerevisiae cytoplasmic asparaginyl-tRNA synthetase (AsnRS), in Brugia malayai AsnRs and, in various putative bacterial AsnRSs. This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. AsnRS is immunodominant antigen of the filarial nematode B. malayai and of interest as a target for anti-parasitic drug design. Human AsnRS has been shown to be a pro-inflammatory chemokine which interacts with CCR3 chemokine receptors on T cells, immature dendritic cells and macrophages.
Pssm-ID: 239818 [Multi-domain] Cd Length: 84 Bit Score: 138.14 E-value: 2.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 126 RVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLADELCQ-CYNGVLLSTESSVAVYGMLNLTPKGKQAPGGHELSCDFW 204
Cdd:cd04323 1 RVKVFGWVHRLRSQKK-LMFLVLRDGTGFLQCVLSKKLVTeFYDAKSLTQESSVEVTGEVKEDPRAKQAPGGYELQVDYL 79
|
....
gi 530414204 205 ELIG 208
Cdd:cd04323 80 EIIG 83
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
245-540 |
2.76e-37 |
|
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: 138.76 E-value: 2.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 245 LKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEGGATLFKLDYF--GEEAFLTQSSQLYLETCLPA-LGDVFCIAQSYR 321
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNalGLDYYLRISPQLFKKRLMVGgLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 322 AEQSRTRrHLAEYTHVEAECPFLTFDDLLNRLEDLVCDVVDRILkspaGSIVHELNPNFQPPKRPFKRMNYSDAIvwlke 401
Cdd:cd00669 81 NEDLRAR-HQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVL----GVTAVTYGFELEDFGLPFPRLTYREAL----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 402 hdvkkedgtfyefgedipeapERLmtdtiNEPILLCRFPVEIKSFYMQRCPEDSRLTESVDVLMPNVgEIVGGSMRIFDS 481
Cdd:cd00669 151 ---------------------ERY-----GQPLFLTDYPAEMHSPLASPHDVNPEIADAFDLFINGV-EVGNGSSRLHDP 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530414204 482 EEILAGYKREGIDPTP----YYWYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPR 540
Cdd:cd00669 204 DIQAEVFQEQGINKEAgmeyFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPK 266
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
284-540 |
9.39e-27 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 114.58 E-value: 9.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 284 FKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTFDDLLNRLEDLVCDVVDR 363
Cdd:PLN02532 363 FSKDFFSRPTYLTVSGRLHLESYACALGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAFSELEDAMNCAEDYFKFLCKW 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 364 ILKSPAGSIvhelnpNFQpPKR---------------PFKRMNYSDAIVWLKEH-DVKKEdgTFYEFGedIPEAPERL-- 425
Cdd:PLN02532 443 VLENCSEDM------KFV-SKRidktistrleaiissSLQRISYTEAVDLLKQAtDKKFE--TKPEWG--IALTTEHLsy 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 426 MTDTI-NEPILLCRFPVEIKSFYMqRCPEDSRLTESVDVLMPNVGEIVGGS-----MRIFDSEEILAGYKREgidptPYY 499
Cdd:PLN02532 512 LADEIyKKPVIIYNYPKELKPFYV-RLNDDGKTVAAFDLVVPKVGTVITGSqneerMDILNARIEELGLPRE-----QYE 585
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 530414204 500 WYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPR 540
Cdd:PLN02532 586 WYLDLRRHGTVKHSGFSLGFELMVLFATGLPDVRDAIPFPR 626
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
126-208 |
1.83e-23 |
|
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: 94.17 E-value: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 126 RVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLADELCQ--CYNGVLLSTESSVAVYGMLNLTPKGKQAPGGHELSCDF 203
Cdd:cd04100 1 EVTLAGWVHSRRDHGG-LIFIDLRDGSGIVQVVVNKEELGefFEEAEKLRTESVVGVTGTVVKRPEGNLATGEIELQAEE 79
|
....*
gi 530414204 204 WELIG 208
Cdd:cd04100 80 LEVLS 84
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
124-396 |
3.81e-21 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 97.17 E-value: 3.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 124 GQRVKVFGWVHRLRRQGkNLMFLVLRDGTGYLQCV-LADELCQCYNGVL-LSTESSVAVYGMLNLTPKG----KQAPGGH 197
Cdd:PLN02903 72 GSRVTLCGWVDLHRDMG-GLTFLDVRDHTGIVQVVtLPDEFPEAHRTANrLRNEYVVAVEGTVRSRPQEspnkKMKTGSV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 198 ELSCDFWELIG---------LAPAGGADNLINEEsdvdVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDR-GYYEV 267
Cdd:PLN02903 151 EVVAESVDILNvvtkslpflVTTADEQKDSIKEE----VRLRYRVLDLRRPQMNANLRLRHRVVKLIRRYLEDVhGFVEI 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 268 TPPTLVQTQVEGGatlfkLDYF-------GEEAFLTQSSQLYLETCLPALGD-VFCIAQSYRAEQSRTRRHlAEYTHVEA 339
Cdd:PLN02903 227 ETPILSRSTPEGA-----RDYLvpsrvqpGTFYALPQSPQLFKQMLMVSGFDrYYQIARCFRDEDLRADRQ-PEFTQLDM 300
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 530414204 340 ECPFLTFDDLLNRLEDLVCDVVDRILkspagsivhelnpNFQPPkRPFKRMNYSDAI 396
Cdd:PLN02903 301 ELAFTPLEDMLKLNEDLIRQVFKEIK-------------GVQLP-NPFPRLTYAEAM 343
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
245-539 |
1.31e-16 |
|
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: 80.31 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 245 LKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEGGAtlfklDYF-------GEEAFLTQSSQLYLETCLPA-LGDVFCI 316
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTPEGAR-----DFLvpsrlhpGKFYALPQSPQLFKQLLMVSgFDRYFQI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 317 AQSYRAEQSRTRRHlAEYTHVEAECPFLTFDDLLNRLEDLVCDVVDRILKspagsivhelnpnfQPPKRPFKRMNYSDAI 396
Cdd:cd00777 76 ARCFRDEDLRADRQ-PEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG--------------VELTTPFPRMTYAEAM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 397 -------VW-----LKEHDvkKEDGTfYEFGEDIPEAPERLMTDTINEpillcrFPVEIKSfymqrcpedsrltESVDVL 464
Cdd:cd00777 141 erygfkfLWivdfpLFEWD--EEEGR-LVSAHHPFTAPKEEDLDLLEK------DPEDARA-------------QAYDLV 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530414204 465 MpNVGEIVGGSMRIFDSEEILAGYKREGIDPTPYY----WYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYP 539
Cdd:cd00777 199 L-NGVELGGGSIRIHDPDIQEKVFEILGLSEEEAEekfgFLLEAFKYGAPPHGGIALGLDRLVMLLTGSESIRDVIAFP 276
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
124-396 |
5.55e-15 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 78.10 E-value: 5.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 124 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLADELC--QCYN-GVLLSTESSVAVYGMLNLTPKGKQAP----GG 196
Cdd:PRK12820 18 GREVCLAGWVDAFRDHGE-LLFIHLRDRNGFIQAVFSPEAApaDVYElAASLRAEFCVALQGEVQKRLEETENPhietGD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 197 HELSCDfwELIGLAPA------------------GGADNlINEesdvDVQLNNRHMMIRGENMSKILKARSMVTRCFRDH 258
Cdd:PRK12820 97 IEVFVR--ELSILAASealpfaisdkamtagagsAGADA-VNE----DLRLQYRYLDIRRPAMQDHLAKRHRIIKCARDF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 259 FFDRGYYEVTPPTLVQTQVEGGATLFKLDYFGEEAF--LTQSSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHlAEYT 335
Cdd:PRK12820 170 LDSRGFLEIETPILTKSTPEGARDYLVPSRIHPKEFyaLPQSPQLFKQLLMIAgFERYFQLARCFRDEDLRPNRQ-PEFT 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530414204 336 HVEAECPFLTFDDLLNRLEDLVCDVVDrilkspAGSIvhELNpnfqppkRPFKRMNYSDAI 396
Cdd:PRK12820 249 QLDIEASFIDEEFIFELIEELTARMFA------IGGI--ALP-------RPFPRMPYAEAM 294
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
124-396 |
6.27e-15 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 77.42 E-value: 6.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 124 GQRVKVFGWVHRLRRQGkNLMFLVLRDGTGYLQCVlADELCQCYNGVL-LSTESSVAVYGMLNLTPKG----KQAPGGHE 198
Cdd:PRK00476 17 GQTVTLCGWVHRRRDHG-GLIFIDLRDREGIVQVV-FDPDAEAFEVAEsLRSEYVIQVTGTVRARPEGtvnpNLPTGEIE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 199 LSCDFWELIglapaGGADNL---INEESDV--DVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLV 273
Cdd:PRK00476 95 VLASELEVL-----NKSKTLpfpIDDEEDVseELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDDNGFLEIETPILT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 274 QTQVEgGATlfklDYF-------GEeaF--LTQSSQL------------YletclpalgdvFCIAQSYRAEQSRTRRhLA 332
Cdd:PRK00476 170 KSTPE-GAR----DYLvpsrvhpGK--FyaLPQSPQLfkqllmvagfdrY-----------YQIARCFRDEDLRADR-QP 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530414204 333 EYTHVEAECPFLTFDDLLNRLEDLVCDVVDRILKspagsivHELnpnfqppKRPFKRMNYSDAI 396
Cdd:PRK00476 231 EFTQIDIEMSFVTQEDVMALMEGLIRHVFKEVLG-------VDL-------PTPFPRMTYAEAM 280
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
127-207 |
4.37e-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: 64.56 E-value: 4.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 127 VKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVL-ADELCQCYNgvLLSTESSVAVYGMLNLTPKgkqapGGHELSCDFWE 205
Cdd:pfam01336 1 VTVAGRVTSIRRSGGKLLFLTLRDGTGSIQVVVfKEEAEKLAK--KLKEGDVVRVTGKVKKRKG-----GELELVVEEIE 73
|
..
gi 530414204 206 LI 207
Cdd:pfam01336 74 LL 75
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
124-396 |
4.68e-12 |
|
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: 68.49 E-value: 4.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 124 GQRVKVFGWVHRLRRQGkNLMFLVLRDGTGYLQCV-----------LADElcqcyngvlLSTESSVAVYGMLNLTPKG-- 190
Cdd:COG0173 16 GQEVTLSGWVHRRRDHG-GLIFIDLRDRYGITQVVfdpddsaeafeKAEK---------LRSEYVIAVTGKVRARPEGtv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 191 --KQAPGGHELSCDfwELIGLAPaggADNL---INEESDV--DVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRG 263
Cdd:COG0173 86 npKLPTGEIEVLAS--ELEILNK---AKTPpfqIDDDTDVseELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDENG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 264 YYEVTPPTLVQTQVEgGATlfklDYF-------GEeaF--LTQSSQL------------YletclpalgdvFCIAQSYRA 322
Cdd:COG0173 161 FLEIETPILTKSTPE-GAR----DYLvpsrvhpGK--FyaLPQSPQLfkqllmvsgfdrY-----------FQIARCFRD 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530414204 323 EQSRTRRHlAEYTHVEAECPFLTFDDLLNRLEDLVCDVVDRILKspagsivHELnpnfqppKRPFKRMNYSDAI 396
Cdd:COG0173 223 EDLRADRQ-PEFTQLDIEMSFVDQEDVFELMEGLIRHLFKEVLG-------VEL-------PTPFPRMTYAEAM 281
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
124-539 |
3.92e-11 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 65.50 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 124 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLA-DELCQCYNGVLLSTESS--VAVYGMLNLTPKGkqapgghELS 200
Cdd:PRK00484 54 EIEVSVAGRVMLKRVMGK-ASFATLQDGSGRIQLYVSkDDVGEEALEAFKKLDLGdiIGVEGTLFKTKTG-------ELS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 201 --CDFWELI------------GLapaggadnlineeSDVDVQLNNRHM-MIRGENMSKILKARSMVTRCFRDHFFDRGYY 265
Cdd:PRK00484 126 vkATELTLLtkslrplpdkfhGL-------------TDVETRYRQRYVdLIVNPESRETFRKRSKIISAIRRFLDNRGFL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 266 EVTPPTLvQTqVEGGATL--FK--LDYFGEEAFLTQSSQLYLETCLpaLGD---VFCIAQSYRAEQSRTrRHLAEYTHVE 338
Cdd:PRK00484 193 EVETPML-QP-IAGGAAArpFIthHNALDIDLYLRIAPELYLKRLI--VGGferVYEIGRNFRNEGIDT-RHNPEFTMLE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 339 AECPFLTFDDLLNRLEDLVCDVVDRILkspaGSIV-----HELnpNFQPpkrPFKRMNYSDAIV---------------- 397
Cdd:PRK00484 268 FYQAYADYNDMMDLTEELIRHLAQAVL----GTTKvtyqgTEI--DFGP---PFKRLTMVDAIKeytgvdfddmtdeear 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 398 -WLKEHDVKKEDgtFYEFGEDIPEAPERLMTDTINEPILLCRFPVEI----KsfymqRCPEDSRLTESVDVlmpnvgeIV 472
Cdd:PRK00484 339 aLAKELGIEVEK--SWGLGKLINELFEEFVEPKLIQPTFITDYPVEIsplaK-----RHREDPGLTERFEL-------FI 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 473 GGSmrifdseEILAGYKrEGIDPtpyywyTDQRK----------------------------YGTCPHGGYGLGLER--- 521
Cdd:PRK00484 405 GGR-------EIANAFS-ELNDP------IDQRErfeaqveakeagddeamfmdedflraleYGMPPTGGLGIGIDRlvm 470
|
490
....*....|....*...
gi 530414204 522 FLTwilNRYHIRDVCLYP 539
Cdd:PRK00484 471 LLT---DSPSIRDVILFP 485
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
126-234 |
4.12e-11 |
|
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus horikoshii AsnRS asparaginyl-tRNA synthetase (AsnRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The archeal enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose.
Pssm-ID: 239814 [Multi-domain] Cd Length: 103 Bit Score: 59.85 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 126 RVKVFGWVHRLRRQGKNLmFLVLRDGTGYLQCVLADELC-QCYNGVL-LSTESSVAVYGMLNLTPKgkqAPGGHELSCDF 203
Cdd:cd04319 1 KVTLAGWVYRKREVGKKA-FIVLRDSTGIVQAVFSKDLNeEAYREAKkVGIESSVIVEGAVKADPR---APGGAEVHGEK 76
|
90 100 110
....*....|....*....|....*....|..
gi 530414204 204 WELIGLapaggADNL-INEESDVDVQLNNRHM 234
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 ... |
124-199 |
1.42e-10 |
|
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: 58.48 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 124 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLA-----DELCQCYNGvlLSTESSVAVYGMLNLTPKgkqAPGGHE 198
Cdd:cd04316 12 GEEVTVAGWVHEIRDLGG-IKFVILRDREGIVQVTAPkkkvdKELFKTVRK--LSRESVISVTGTVKAEPK---APNGVE 85
|
.
gi 530414204 199 L 199
Cdd:cd04316 86 I 86
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
127-202 |
3.31e-09 |
|
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: 53.72 E-value: 3.31e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530414204 127 VKVFGWVhRLRRQGKNLMFLVLRDGTGY--LQCVLADELCQCYNGVLLSTESSVAVYGMLNLTPKGKQApggHELSCD 202
Cdd:cd04318 2 VTVNGWV-RSVRDSKKISFIELNDGSCLknLQVVVDKELTNFKEILKLSTGSSIRVEGVLVKSPGAKQP---FELQAE 75
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
66-539 |
6.21e-09 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 58.48 E-value: 6.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 66 KKMWHREQMKSESREKkEAEDSLR-----REKNLEEAKKITIKNDP-------SLPE--PKCVKIGALEGYRGQRVKVFG 131
Cdd:PTZ00417 61 KKVRSVQASKDKKKEE-EAEVDPRlyyenRSKFIQEQKAKGINPYPhkfertiTVPEfvEKYQDLASGEHLEDTILNVTG 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 132 WVHRLRRQGKNLMFLVLRDGTGYLQcVLAD---------ELCQCYNGVLLSTessvaVYGMLNLTPKGKQApgghELSCD 202
Cdd:PTZ00417 140 RIMRVSASGQKLRFFDLVGDGAKIQ-VLANfafhdhtksNFAECYDKIRRGD-----IVGIVGFPGKSKKG----ELSIF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 203 FWELIGLAPAGGADNLINEESDVDVQLNNRHM-MIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLvqTQVEGGA 281
Cdd:PTZ00417 210 PKETIILSPCLHMLPMKYGLKDTEIRYRQRYLdLMINESTRSTFITRTKIINYLRNFLNDRGFIEVETPTM--NLVAGGA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 282 TlfkldyfgEEAFLTQSSQLYLE------TCLP-------ALGDVFCIAQSYRAEqSRTRRHLAEYTHVEAECPFLTFDD 348
Cdd:PTZ00417 288 N--------ARPFITHHNDLDLDlylriaTELPlkmlivgGIDKVYEIGKVFRNE-GIDNTHNPEFTSCEFYWAYADFYD 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 349 LLNRLEDLVCDVV------DRILKSPAGSIVHELNPNFQPP------------------KRPFKRMNYSDAIVWL-KEHD 403
Cdd:PTZ00417 359 LIKWSEDFFSQLVmhlfgtYKILYNKDGPEKDPIEIDFTPPypkvsiveelekltntklEQPFDSPETINKMINLiKENK 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 404 VkkedgtfyefgeDIPEAP------ERLMTDTI-----NEPILLCRFPvEIKSFYMQRCPEDSRLTESVDVLMPNvGEIV 472
Cdd:PTZ00417 439 I------------EMPNPPtaakllDQLASHFIenkypNKPFFIIEHP-QIMSPLAKYHRSKPGLTERLEMFICG-KEVL 504
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530414204 473 GGSMRI---FDSEEILAGYK--REGIDPTPYYW---YTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYP 539
Cdd:PTZ00417 505 NAYTELndpFKQKECFSAQQkdREKGDAEAFQFdaaFCTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFP 579
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
224-539 |
6.32e-09 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 58.53 E-value: 6.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 224 DVDVQLNNRHM-MIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLvqTQVEGGAT----LFKLDYFGEEAFLTQS 298
Cdd:PRK12445 162 DQEVRYRQRYLdLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMM--QVIPGGASarpfITHHNALDLDMYLRIA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 299 SQLYLET-CLPALGDVFCIAQSYRAEqSRTRRHLAEYTHVEAECPFLTFDDLLNRLEDLVCDVVDRIL---KSPAGSIVH 374
Cdd:PRK12445 240 PELYLKRlVVGGFERVFEINRNFRNE-GISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLgttKVTYGEHVF 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 375 ELNpnfqppkRPFKRMNYSDAIvwlKEHDVKKEDGTFYEF------GEDIPEAPE------RLMTDTINE--------PI 434
Cdd:PRK12445 319 DFG-------KPFEKLTMREAI---KKYRPETDMADLDNFdaakalAESIGITVEkswglgRIVTEIFDEvaeahliqPT 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 435 LLCRFPVEIKSFyMQRCPEDSRLTESVDVLMPNvGEIVGGSMRIFDSEEILAGY------KREGIDPTPYYW--YTDQRK 506
Cdd:PRK12445 389 FITEYPAEVSPL-ARRNDVNPEITDRFEFFIGG-REIGNGFSELNDAEDQAERFqeqvnaKAAGDDEAMFYDedYVTALE 466
|
330 340 350
....*....|....*....|....*....|...
gi 530414204 507 YGTCPHGGYGLGLERFLTWILNRYHIRDVCLYP 539
Cdd:PRK12445 467 YGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
224-543 |
1.49e-08 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 57.35 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 224 DVDVQLNNRHM-MIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEGGATLFKLDYFGEEA--FLTQSSQ 300
Cdd:PTZ00385 211 DNDVKYRYRFTdMMTNPCVIETIKKRHVMLQALRDYFNERNFVEVETPVLHTVASGANAKSFVTHHNANAMdlFLRVAPE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 301 LYLETCL-PALGDVFCIAQSYRAEQSrTRRHLAEYTHVEAECPFLTFDDLLNRLEDLVCDVVDRILKSPAGSIVHEL--- 376
Cdd:PTZ00385 291 LHLKQCIvGGMERIYEIGKVFRNEDA-DRSHNPEFTSCEFYAAYHTYEDLMPMTEDIFRQLAMRVNGTTVVQIYPENahg 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 377 NPNFQPPKRPFKRMNYSDAIVWLK------EHDVKKEDGTFY----EFGEDIPEAPER------------LMTDTINEPI 434
Cdd:PTZ00385 370 NPVTVDLGKPFRRVSVYDEIQRMSgvefppPNELNTPKGIAYmsvvMLRYNIPLPPVRtaakmfeklidfFITDRVVEPT 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 435 LLCRFPVEIKSFYMQrcpEDSR--LTESVDVLMPNVgEIVGGSMRIFDSEEILAGYKREGID-------PTPY-YWYTDQ 504
Cdd:PTZ00385 450 FVMDHPLFMSPLAKE---QVSRpgLAERFELFVNGI-EYCNAYSELNDPHEQYHRFQQQLVDrqggdeeAMPLdETFLKS 525
|
330 340 350
....*....|....*....|....*....|....*....
gi 530414204 505 RKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPRFVQ 543
Cdd:PTZ00385 526 LQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFPLLRQ 564
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
124-229 |
1.72e-08 |
|
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: 53.29 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 124 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLADELCQCYNGVL-LSTESSVAVYGMLNLTPKG----KQAPGGHE 198
Cdd:cd04317 14 GQEVTLCGWVQRRRDHGG-LIFIDLRDRYGIVQVVFDPEEAPEFELAEkLRNESVIQVTGKVRARPEGtvnpKLPTGEIE 92
|
90 100 110
....*....|....*....|....*....|....
gi 530414204 199 LSCDFWELIGLapaggADNL---INEESDVDVQL 229
Cdd:cd04317 93 VVASELEVLNK-----AKTLpfeIDDDVNVSEEL 121
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
118-339 |
1.56e-07 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 54.58 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 118 ALEGYRGQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLADELCQCYNGVLLSTESS----VAVYGMLNLTPKGkqa 193
Cdd:PRK02983 645 ALDAPTGEEVSVSGRVLRIRDYGG-VLFADLRDWSGELQVLLDASRLEQGSLADFRAAVDlgdlVEVTGTMGTSRNG--- 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 194 pgghELS--CDFWELIG--LAPaggadnLINEE---SDVDVQLNNRHM--MIRGENMSkILKARSMVTRCFRDHFFDRGY 264
Cdd:PRK02983 721 ----TLSllVTSWRLAGkcLRP------LPDKWkglTDPEARVRQRYLdlAVNPEARD-LLRARSAVVRAVRETLVARGF 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 265 YEVTPPTLvQtQVEGGAT----LFKLDYFGEEAFLTQSSQLYLET-CLPALGDVFCIAQSYRAE-QSRTrrHLAEYTHVE 338
Cdd:PRK02983 790 LEVETPIL-Q-QVHGGANarpfVTHINAYDMDLYLRIAPELYLKRlCVGGVERVFELGRNFRNEgVDAT--HNPEFTLLE 865
|
.
gi 530414204 339 A 339
Cdd:PRK02983 866 A 866
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
127-189 |
2.20e-06 |
|
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: 46.40 E-value: 2.20e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 127 VKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVLA-------DELCQCYNGvlLSTESSVAVYGMLNLTPK 189
Cdd:cd04320 2 VLIRARVHTSRAQGAKLAFLVLRQQGYTIQGVLAasaegvsKQMVKWAGS--LSKESIVDVEGTVKKPEE 69
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
241-535 |
4.44e-06 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 48.77 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 241 MSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQ-TQVEGGATLFKLDYFGEEAflTQSSQLYLETC--------LPAL- 310
Cdd:PRK09350 1 SIPNLLKRAKIIAEIRRFFADRGVLEVETPILSQaTVTDIHLVPFETRFVGPGA--SQGKTLWLMTSpeyhmkrlLAAGs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 311 GDVFCIAQSYRAEQSrTRRHLAEYTHVEAECPFLTFDDLLNRLEDLV-----CDVVDRILKSPAGSIVHELNPnFQPPKR 385
Cdd:PRK09350 79 GPIFQICKSFRNEEA-GRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLqqvldCEPAESLSYQQAFLRYLGIDP-LSADKT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 386 PFKrmnysDAIVWLKEHDVKKEDgtfyefgEDIPEAPERLMTDTI------NEPILLCRFPVEIKSfYMQRCPEDSRLTE 459
Cdd:PRK09350 157 QLR-----EVAAKLGLSNIADEE-------EDRDTLLQLLFTFGVepnigkEKPTFVYHFPASQAA-LAKISTEDHRVAE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 460 SVDVLMPNVgEIVGGSMRIFDSEEILAGYKR-------EGIDPTPyywyTDQR-----KYGTCPHGGYGLGLERFLTWIL 527
Cdd:PRK09350 224 RFEVYFKGI-ELANGFHELTDAREQRQRFEQdnrkraaRGLPQQP----IDENliaalEAGLPDCSGVALGVDRLIMLAL 298
|
....*...
gi 530414204 528 NRYHIRDV 535
Cdd:PRK09350 299 GAESISEV 306
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
248-340 |
7.08e-05 |
|
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: 44.03 E-value: 7.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 248 RSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEGGATLFKLD------YFGEEAFLTQSSQLYLET----CLPALGD-VFCI 316
Cdd:cd00768 2 RSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHEPKDllpvgaENEEDLYLRPTLEPGLVRlfvsHIRKLPLrLAEI 81
|
90 100
....*....|....*....|....*
gi 530414204 317 AQSYRAEQSRTR-RHLAEYTHVEAE 340
Cdd:cd00768 82 GPAFRNEGGRRGlRRVREFTQLEGE 106
|
|
| ScAspRS_mt_like_N |
cd04321 |
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
126-206 |
2.91e-03 |
|
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: 36.91 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414204 126 RVKVFGWVHRLRRQGKNLMFLVLRDGTGY-LQCVLADElcqcyNGVL-----LSTESSVAVYGMLNLtpkgKQAPGGHEL 199
Cdd:cd04321 1 KVTLNGWIDRKPRIVKKLSFADLRDPNGDiIQLVSTAK-----KDAFsllksITAESPVQVRGKLQL----KEAKSSEKN 71
|
....*..
gi 530414204 200 SCdfWEL 206
Cdd:cd04321 72 DE--WEL 76
|
|
| |
