|
Name |
Accession |
Description |
Interval |
E-value |
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
225-544 |
2.04e-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: 418.89 E-value: 2.04e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 225 DVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYL 304
Cdd:cd00776 3 NLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQLYK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 305 ETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFL-TFDDLLNRLEDLVCDVVDRILKSPA--GSIVHELNPNF 381
Cdd:cd00776 83 EMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAkeLELVNQLNREL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 382 QPPKRPFKRMNYSDAIVWLKEHDVKKEDgtfyEFGEDIPEAPERLMTDTI-NEPILLCRFPVEIKSFYMQRCPEDSRLTE 460
Cdd:cd00776 163 LKPLEPFPRITYDEAIELLREKGVEEEV----KWGEDLSTEHERLLGEIVkGDPVFVTDYPKEIKPFYMKPDDDNPETVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 461 SVDVLMPNVGEIVGGSMRIFDSEEILAGYKREGIDPTPYYWYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYP 540
Cdd:cd00776 239 SFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
....
gi 4758762 541 RFVQ 544
Cdd:cd00776 319 RDPK 322
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
119-548 |
5.08e-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: 5.08e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 119 ALEGYRGQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLADELCQCYNGVL-LSTESSVAVYGMLNLTPKgkqAPGG 197
Cdd:COG0017 8 LLPEHVGQEVTVAGWVRTKRDSGG-ISFLILRDGSGFIQVVVKKDKLENFEEAKkLTTESSVEVTGTVVESPR---APQG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 198 HELSCDFWELIGLA----PaggadnLINEESDVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTL 273
Cdd:COG0017 84 VELQAEEIEVLGEAdepyP------LQPKRHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVEVHTPII 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 274 VQTQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTFDDLLNR 353
Cdd:COG0017 158 TASATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMALEKVYTFGPTFRAEKSNTRRHLAEFWMIEPEMAFADLEDVMDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 354 LEDLVCDVVDRILKSpAGSIVHELNPNFQP----PKRPFKRMNYSDAIVWLKEHDVKkedgtfYEFGEDI-PEApERLMT 428
Cdd:COG0017 238 AEEMLKYIIKYVLEN-CPEELEFLGRDVERlekvPESPFPRITYTEAIEILKKSGEK------VEWGDDLgTEH-ERYLG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 429 DTI-NEPILLCRFPVEIKSFYMQRCPEDSRLTESVDVLMPNVGEIVGGSMRIFDSEEILAGYKREGIDPTPYYWYTDQRK 507
Cdd:COG0017 310 EEFfKKPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAPGIGEIIGGSQREHRYDVLVERIKEKGLDPEDYEWYLDLRR 389
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 4758762 508 YGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPRFVQRCTP 548
Cdd:COG0017 390 YGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
125-548 |
1.90e-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: 1.90e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 125 GQRVKVFGWVHRlRRQGKNLMFLVLRDGT--GYLQCVLADELCQCYNGVL--LSTESSVAVYGMLNLTPKGKQapgGHEL 200
Cdd:TIGR00457 16 GDEVTVSGWVRT-KRSSKKIIFLELNDGSslGPIQAVINGEDNPYLFQLLksLTTGSSVSVTGKVVESPGKGQ---PVEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 201 SCDFWELIGLAPAGGADNLInEESDVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEG 280
Cdd:TIGR00457 92 QVKKIEVVGEAEPDDYPLQK-KEHSLEFLRDIAHLRLRTNTLGAVMRVRNALSQAIHRYFQENGFTWVSPPILTSNDCEG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 281 GATLFKL---------DYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTFDDLL 351
Cdd:TIGR00457 171 AGELFRVstgnidfsqDFFGKEAYLTVSGQLYLETYALALSKVYTFGPTFRAEKSNTSRHLSEFWMIEPEMAFANLNDLL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 352 NRLEDLVCDVVDRILKSPAGSiVHELNPNFQPPKRP---------FKRMNYSDAIVWLKEHDVKKEDGTFyeFGEDIPEA 422
Cdd:TIGR00457 251 QLAETLIKYIIKAVLENCSQE-LKFLEKNFDKDLIKrleniinnkFARITYTDAIEILKESDKNFEYEDF--WGDDLQTE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 423 PERLMTDTI-NEPILLCRFPVEIKSFYMQRCpEDSRLTESVDVLMPNVGEIVGGSMRIFDSEEILAGYKREGIDPTPYYW 501
Cdd:TIGR00457 328 HERFLAEEYfKPPVFVTNYPKDIKAFYMKLN-DDGKTVAAMDLLAPGIGEIIGGSEREDDLDKLENRMKEMGLDTDALNW 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 4758762 502 YTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPRFVQRCTP 548
Cdd:TIGR00457 407 YLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGNINF 453
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
121-548 |
1.73e-107 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 328.99 E-value: 1.73e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 121 EGYRGQRVKVFGWVHRlRRQGKNLMFLVLRDGTGYLQCVL-ADELCQCYNGVL-LSTESSVAVYGMLNLTPKgkqAPGGH 198
Cdd:PRK03932 12 GKYVGQEVTVRGWVRT-KRDSGKIAFLQLRDGSCFKQLQVvKDNGEEYFEEIKkLTTGSSVIVTGTVVESPR---AGQGY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 199 ELSCDFWELIGLAPAggaDNLINE-ESDVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQ 277
Cdd:PRK03932 88 ELQATKIEVIGEDPE---DYPIQKkRHSIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVDTPIITASD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 278 VEGGATLFKL---------DYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTFD 348
Cdd:PRK03932 165 CEGAGELFRVttldldfskDFFGKEAYLTVSGQLYAEAYAMALGKVYTFGPTFRAENSNTRRHLAEFWMIEPEMAFADLE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 349 DLLNRLEDLVCDVVDRIL-----------KSPAGSIVHELNpNFQPPkrPFKRMNYSDAIVWLKEHDVKKEDGTfyEFGE 417
Cdd:PRK03932 245 DNMDLAEEMLKYVVKYVLencpddleflnRRVDKGDIERLE-NFIES--PFPRITYTEAIEILQKSGKKFEFPV--EWGD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 418 DI--PEapERLMTDTINE-PILLCRFPVEIKSFYMQRCPEDsRLTESVDVLMPNVGEIVGGSMRIFDSEEILAGYKREGI 494
Cdd:PRK03932 320 DLgsEH--ERYLAEEHFKkPVFVTNYPKDIKAFYMRLNPDG-KTVAAMDLLAPGIGEIIGGSQREERLDVLEARIKELGL 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 4758762 495 DPTPYYWYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPRFVQRCTP 548
Cdd:PRK03932 397 NKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
225-541 |
4.18e-102 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 310.27 E-value: 4.18e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 225 DVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEGGATLFKL------DYFgeeaFLTQ 298
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVpsralgKFY----ALPQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 299 SSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHLaEYTHVEAECPFLTFDDLLNRLEDLVCDVVDRILKSPAGsivhEL 377
Cdd:pfam00152 77 SPQLYKQLLMVAgFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKE----LE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 378 NPNFQPPKRPFKRMNYSDAIVWLKEHDVkkedgtfYEFGEDIPEAPERLMTD-----TINEPILLCRFPVEIKSFYMQRC 452
Cdd:pfam00152 152 GGTLLDLKKPFPRITYAEAIEKLNGKDV-------EELGYGSDKPDLRFLLElvidkNKFNPLWVTDFPAEHHPFTMPKD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 453 PEDSRLTESVDVLMPNVgEIVGGSMRIFDSEEILAGYKREGIDP----TPYYWYTDQRKYGTCPHGGYGLGLERFLTWIL 528
Cdd:pfam00152 225 EDDPALAEAFDLVLNGV-EIGGGSIRIHDPELQEERFEEQGLDPeeaeEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLT 303
|
330
....*....|...
gi 4758762 529 NRYHIRDVCLYPR 541
Cdd:pfam00152 304 GLESIREVIAFPK 316
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
127-209 |
2.35e-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: 2.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 127 RVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLADELCQ-CYNGVLLSTESSVAVYGMLNLTPKGKQAPGGHELSCDFW 205
Cdd:cd04323 1 RVKVFGWVHRLRSQKK-LMFLVLRDGTGFLQCVLSKKLVTeFYDAKSLTQESSVEVTGEVKEDPRAKQAPGGYELQVDYL 79
|
....
gi 4758762 206 ELIG 209
Cdd:cd04323 80 EIIG 83
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
128-208 |
4.38e-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: 4.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 128 VKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVL-ADELCQCYNgvLLSTESSVAVYGMLNLTPKgkqapGGHELSCDFWE 206
Cdd:pfam01336 1 VTVAGRVTSIRRSGGKLLFLTLRDGTGSIQVVVfKEEAEKLAK--KLKEGDVVRVTGKVKKRKG-----GELELVVEEIE 73
|
..
gi 4758762 207 LI 208
Cdd:pfam01336 74 LL 75
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
225-544 |
2.04e-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: 418.89 E-value: 2.04e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 225 DVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYL 304
Cdd:cd00776 3 NLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQLYK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 305 ETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFL-TFDDLLNRLEDLVCDVVDRILKSPA--GSIVHELNPNF 381
Cdd:cd00776 83 EMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAkeLELVNQLNREL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 382 QPPKRPFKRMNYSDAIVWLKEHDVKKEDgtfyEFGEDIPEAPERLMTDTI-NEPILLCRFPVEIKSFYMQRCPEDSRLTE 460
Cdd:cd00776 163 LKPLEPFPRITYDEAIELLREKGVEEEV----KWGEDLSTEHERLLGEIVkGDPVFVTDYPKEIKPFYMKPDDDNPETVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 461 SVDVLMPNVGEIVGGSMRIFDSEEILAGYKREGIDPTPYYWYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYP 540
Cdd:cd00776 239 SFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
....
gi 4758762 541 RFVQ 544
Cdd:cd00776 319 RDPK 322
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
119-548 |
5.08e-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: 5.08e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 119 ALEGYRGQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLADELCQCYNGVL-LSTESSVAVYGMLNLTPKgkqAPGG 197
Cdd:COG0017 8 LLPEHVGQEVTVAGWVRTKRDSGG-ISFLILRDGSGFIQVVVKKDKLENFEEAKkLTTESSVEVTGTVVESPR---APQG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 198 HELSCDFWELIGLA----PaggadnLINEESDVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTL 273
Cdd:COG0017 84 VELQAEEIEVLGEAdepyP------LQPKRHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVEVHTPII 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 274 VQTQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTFDDLLNR 353
Cdd:COG0017 158 TASATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMALEKVYTFGPTFRAEKSNTRRHLAEFWMIEPEMAFADLEDVMDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 354 LEDLVCDVVDRILKSpAGSIVHELNPNFQP----PKRPFKRMNYSDAIVWLKEHDVKkedgtfYEFGEDI-PEApERLMT 428
Cdd:COG0017 238 AEEMLKYIIKYVLEN-CPEELEFLGRDVERlekvPESPFPRITYTEAIEILKKSGEK------VEWGDDLgTEH-ERYLG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 429 DTI-NEPILLCRFPVEIKSFYMQRCPEDSRLTESVDVLMPNVGEIVGGSMRIFDSEEILAGYKREGIDPTPYYWYTDQRK 507
Cdd:COG0017 310 EEFfKKPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAPGIGEIIGGSQREHRYDVLVERIKEKGLDPEDYEWYLDLRR 389
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 4758762 508 YGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPRFVQRCTP 548
Cdd:COG0017 390 YGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
125-548 |
1.90e-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: 1.90e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 125 GQRVKVFGWVHRlRRQGKNLMFLVLRDGT--GYLQCVLADELCQCYNGVL--LSTESSVAVYGMLNLTPKGKQapgGHEL 200
Cdd:TIGR00457 16 GDEVTVSGWVRT-KRSSKKIIFLELNDGSslGPIQAVINGEDNPYLFQLLksLTTGSSVSVTGKVVESPGKGQ---PVEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 201 SCDFWELIGLAPAGGADNLInEESDVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEG 280
Cdd:TIGR00457 92 QVKKIEVVGEAEPDDYPLQK-KEHSLEFLRDIAHLRLRTNTLGAVMRVRNALSQAIHRYFQENGFTWVSPPILTSNDCEG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 281 GATLFKL---------DYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTFDDLL 351
Cdd:TIGR00457 171 AGELFRVstgnidfsqDFFGKEAYLTVSGQLYLETYALALSKVYTFGPTFRAEKSNTSRHLSEFWMIEPEMAFANLNDLL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 352 NRLEDLVCDVVDRILKSPAGSiVHELNPNFQPPKRP---------FKRMNYSDAIVWLKEHDVKKEDGTFyeFGEDIPEA 422
Cdd:TIGR00457 251 QLAETLIKYIIKAVLENCSQE-LKFLEKNFDKDLIKrleniinnkFARITYTDAIEILKESDKNFEYEDF--WGDDLQTE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 423 PERLMTDTI-NEPILLCRFPVEIKSFYMQRCpEDSRLTESVDVLMPNVGEIVGGSMRIFDSEEILAGYKREGIDPTPYYW 501
Cdd:TIGR00457 328 HERFLAEEYfKPPVFVTNYPKDIKAFYMKLN-DDGKTVAAMDLLAPGIGEIIGGSEREDDLDKLENRMKEMGLDTDALNW 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 4758762 502 YTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPRFVQRCTP 548
Cdd:TIGR00457 407 YLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGNINF 453
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
121-548 |
1.73e-107 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 328.99 E-value: 1.73e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 121 EGYRGQRVKVFGWVHRlRRQGKNLMFLVLRDGTGYLQCVL-ADELCQCYNGVL-LSTESSVAVYGMLNLTPKgkqAPGGH 198
Cdd:PRK03932 12 GKYVGQEVTVRGWVRT-KRDSGKIAFLQLRDGSCFKQLQVvKDNGEEYFEEIKkLTTGSSVIVTGTVVESPR---AGQGY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 199 ELSCDFWELIGLAPAggaDNLINE-ESDVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQ 277
Cdd:PRK03932 88 ELQATKIEVIGEDPE---DYPIQKkRHSIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVDTPIITASD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 278 VEGGATLFKL---------DYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTFD 348
Cdd:PRK03932 165 CEGAGELFRVttldldfskDFFGKEAYLTVSGQLYAEAYAMALGKVYTFGPTFRAENSNTRRHLAEFWMIEPEMAFADLE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 349 DLLNRLEDLVCDVVDRIL-----------KSPAGSIVHELNpNFQPPkrPFKRMNYSDAIVWLKEHDVKKEDGTfyEFGE 417
Cdd:PRK03932 245 DNMDLAEEMLKYVVKYVLencpddleflnRRVDKGDIERLE-NFIES--PFPRITYTEAIEILQKSGKKFEFPV--EWGD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 418 DI--PEapERLMTDTINE-PILLCRFPVEIKSFYMQRCPEDsRLTESVDVLMPNVGEIVGGSMRIFDSEEILAGYKREGI 494
Cdd:PRK03932 320 DLgsEH--ERYLAEEHFKkPVFVTNYPKDIKAFYMRLNPDG-KTVAAMDLLAPGIGEIIGGSQREERLDVLEARIKELGL 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 4758762 495 DPTPYYWYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPRFVQRCTP 548
Cdd:PRK03932 397 NKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
225-541 |
4.18e-102 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 310.27 E-value: 4.18e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 225 DVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEGGATLFKL------DYFgeeaFLTQ 298
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVpsralgKFY----ALPQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 299 SSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHLaEYTHVEAECPFLTFDDLLNRLEDLVCDVVDRILKSPAGsivhEL 377
Cdd:pfam00152 77 SPQLYKQLLMVAgFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKE----LE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 378 NPNFQPPKRPFKRMNYSDAIVWLKEHDVkkedgtfYEFGEDIPEAPERLMTD-----TINEPILLCRFPVEIKSFYMQRC 452
Cdd:pfam00152 152 GGTLLDLKKPFPRITYAEAIEKLNGKDV-------EELGYGSDKPDLRFLLElvidkNKFNPLWVTDFPAEHHPFTMPKD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 453 PEDSRLTESVDVLMPNVgEIVGGSMRIFDSEEILAGYKREGIDP----TPYYWYTDQRKYGTCPHGGYGLGLERFLTWIL 528
Cdd:pfam00152 225 EDDPALAEAFDLVLNGV-EIGGGSIRIHDPELQEERFEEQGLDPeeaeEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLT 303
|
330
....*....|...
gi 4758762 529 NRYHIRDVCLYPR 541
Cdd:pfam00152 304 GLESIREVIAFPK 316
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
125-548 |
1.84e-97 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 302.49 E-value: 1.84e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 125 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVL-ADELCQCYNGV-LLSTESSVAVYGMLNLTPKgkqAPGGHELSC 202
Cdd:PRK05159 16 GEEVTLAGWVHEIRDLGG-IAFLILRDRSGIIQVVVkKKVDEELFETIkKLKRESVVSVTGTVKANPK---APGGVEVIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 203 DFWELIGLApaggADNL---INEES--DVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQ 277
Cdd:PRK05159 92 EEIEVLNKA----EEPLpldISGKVlaELDTRLDNRFLDLRRPRVRAIFKIRSEVLRAFREFLYENGFTEIFTPKIVASG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 278 VEGGATLFKLDYFGEEAFLTQSSQLYLETCLPALGD-VFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLT-FDDLLNRLE 355
Cdd:PRK05159 168 TEGGAELFPIDYFEKEAYLAQSPQLYKQMMVGAGFErVFEIGPVFRAEEHNTSRHLNEYTSIDVEMGFIDdHEDVMDLLE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 356 DLVCDVVDRILKSPAGSIVhELNPNFQPPKRPFKRMNYSDAIvwlkehDVKKEDGTFYEFGEDIPEAPERLMTDTINE-- 433
Cdd:PRK05159 248 NLLRYMYEDVAENCEKELE-LLGIELPVPETPIPRITYDEAI------EILKSKGNEISWGDDLDTEGERLLGEYVKEey 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 434 ---PILLCRFPVEIKSFYMQRCPEDSRLTESVDVLMPNVgEIVGGSMRIFDSEEILAGYKREGIDPTPYYWYTDQRKYGT 510
Cdd:PRK05159 321 gsdFYFITDYPSEKRPFYTMPDEDDPEISKSFDLLFRGL-EITSGGQRIHRYDMLVESIKEKGLNPESFEFYLEAFKYGM 399
|
410 420 430
....*....|....*....|....*....|....*...
gi 4758762 511 CPHGGYGLGLERFLTWILNRYHIRDVCLYPRFVQRCTP 548
Cdd:PRK05159 400 PPHGGFGLGLERLTMKLLGLENIREAVLFPRDRHRLTP 437
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
76-548 |
1.03e-52 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 187.61 E-value: 1.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 76 KSESREKKEAEDSLRREKNLEEAKKITIKNDP---------------SLPEPKCVKIGAL-EGYRGQRVKVFGWVHRLRR 139
Cdd:PLN02850 16 KAAKKAAAKAEKLRREATAKAAAASLEDEDDPlasnygdvpleelqsKVTGREWTDVSDLgEELAGSEVLIRGRVHTIRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 140 QGKnLMFLVLRDGTGYLQCVL-ADELCQCYNGV----LLSTESSVAVYGMLNLTPKG-KQAPGGHELSCDFWELIGLAPA 213
Cdd:PLN02850 96 KGK-SAFLVLRQSGFTVQCVVfVSEVTVSKGMVkyakQLSRESVVDVEGVVSVPKKPvKGTTQQVEIQVRKIYCVSKALA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 214 GGADNLIN---EESDV---------------DVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQ 275
Cdd:PLN02850 175 TLPFNVEDaarSESEIekalqtgeqlvrvgqDTRLNNRVLDLRTPANQAIFRIQSQVCNLFREFLLSKGFVEIHTPKLIA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 276 TQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPfltfddlLNRL 354
Cdd:PLN02850 255 GASEGGSAVFRLDYKGQPACLAQSPQLHKQMAICGdFRRVFEIGPVFRAEDSFTHRHLCEFTGLDLEME-------IKEH 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 355 EDLVCDVVDRILKspagSIVHELNPN-------------FQPPK--RPFKRMNYSDAIVWLKEHDVKKEDgtfyefGEDI 419
Cdd:PLN02850 328 YSEVLDVVDELFV----AIFDGLNERckkeleaireqypFEPLKylPKTLRLTFAEGIQMLKEAGVEVDP------LGDL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 420 PEAPERLMTDTINEP-----ILLCRFPVEIKSFYMQRCPEDSRLTESVDVLMPNvGEIVGGSMRIFDSEEILAGYKREGI 494
Cdd:PLN02850 398 NTESERKLGQLVKEKygtdfYILHRYPLAVRPFYTMPCPDDPKYSNSFDVFIRG-EEIISGAQRVHDPELLEKRAEECGI 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 4758762 495 DPTPYYWYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPRFVQRCTP 548
Cdd:PLN02850 477 DVKTISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPRDPQRLAP 530
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
115-541 |
5.86e-48 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 175.16 E-value: 5.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 115 VKIGALEG--YRGQRVKVFGWVHRLRRQgKNLMFLVLRDGT--GYLQCVLADElCQCYNGV---LLSTESSVAVYGMLNL 187
Cdd:PLN02603 95 VKGGEDEGlaRVGKTLNVMGWVRTLRAQ-SSVTFIEVNDGSclSNMQCVMTPD-AEGYDQVesgLITTGASVLVQGTVVS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 188 TPKGKQAPgghELSCDFWELIGlapaggadnlineESDVDVQLNNR-----------HMMIRGENMSKILKARSMVTRCF 256
Cdd:PLN02603 173 SQGGKQKV---ELKVSKIVVVG-------------KSDPSYPIQKKrvsreflrtkaHLRPRTNTFGAVARVRNALAYAT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 257 RDHFFDRGYYEVTPP-----------------TLVQTQVEGGATLFK-------------LDYFGEEAFLTQSSQLYLET 306
Cdd:PLN02603 237 HKFFQENGFVWVSSPiitasdcegageqfcvtTLIPNSAENGGSLVDdipktkdglidwsQDFFGKPAFLTVSGQLNGET 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 307 CLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTFDDLLNRLEDLVCDVVDRILKSPA-----------GSIVH 375
Cdd:PLN02603 317 YATALSDVYTFGPTFRAENSNTSRHLAEFWMIEPELAFADLNDDMACATAYLQYVVKYILENCKedmeffntwieKGIID 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 376 ELNpnfQPPKRPFKRMNYSDAIVWLKEhdVKKEDGTFYEFGEDIPEAPERLMTDTI--NEPILLCRFPVEIKSFYMqRCP 453
Cdd:PLN02603 397 RLS---DVVEKNFVQLSYTDAIELLLK--AKKKFEFPVKWGLDLQSEHERYITEEAfgGRPVIIRDYPKEIKAFYM-REN 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 454 EDSRLTESVDVLMPNVGEIVGGSMRIFDSEEILAGYKREGIDPTPYYWYTDQRKYGTCPHGGYGLGLERFLTWILNRYHI 533
Cdd:PLN02603 471 DDGKTVAAMDMLVPRVGELIGGSQREERLEYLEARLDELKLNKESYWWYLDLRRYGSVPHAGFGLGFERLVQFATGIDNI 550
|
....*...
gi 4758762 534 RDVCLYPR 541
Cdd:PLN02603 551 RDAIPFPR 558
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
122-542 |
2.43e-47 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 173.64 E-value: 2.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 122 GYRGQRVKVFGWVHRLRRQGK-NLMFLVLRDGT--GYLQCVLADELCQCYNgvLLSTESSVAVYGMLNLTPKGKQAPGGH 198
Cdd:PLN02221 47 GLAGQKVRIGGWVKTGREQGKgTFAFLEVNDGScpANLQVMVDSSLYDLST--LVATGTCVTVDGVLKVPPEGKGTKQKI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 199 ELSCDfwELIGLAPAGGAD-NLINEESDVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQ 277
Cdd:PLN02221 125 ELSVE--KVIDVGTVDPTKyPLPKTKLTLEFLRDVLHLRSRTNSISAVARIRNALAFATHSFFQEHSFLYIHTPIITTSD 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 278 VEGGATLFKL---------------------------------------------------------------------- 287
Cdd:PLN02221 203 CEGAGEMFQVttlinyterleqdlidnpppteadveaarlivkergevvaqlkaakaskeeitaavaelkiakeslahie 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 288 --------------------DYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTF 347
Cdd:PLN02221 283 ersklkpglpkkdgkidyskDFFGRQAFLTVSGQLQVETYACALSSVYTFGPTFRAENSHTSRHLAEFWMVEPEIAFADL 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 348 DDLLNRLEDLVCDVVDRILKSpAGSIVHELNPNFQP---------PKRPFKRMNYSDAIVWLKEHDVK-KEDGTFYEFGE 417
Cdd:PLN02221 363 EDDMNCAEAYVKYMCKWLLDK-CFDDMELMAKNFDSgcidrlrmvASTPFGRITYTEAIELLEEAVAKgKEFDNNVEWGI 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 418 DIPEAPERLMTDTI-NEPILLCRFPVEIKSFYMqRCPEDSRLTESVDVLMPNVGEIVGGSMRIFDSEEILAGYKREGIDP 496
Cdd:PLN02221 442 DLASEHERYLTEVLfQKPLIVYNYPKGIKAFYM-RLNDDEKTVAAMDVLVPKVGELIGGSQREERYDVIKQRIEEMGLPI 520
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 4758762 497 TPYYWYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPRF 542
Cdd:PLN02221 521 EPYEWYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPRY 566
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
237-541 |
1.82e-46 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 165.58 E-value: 1.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 237 IRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLvqTQV-----EGGATL----FKLDYFGEEAFLTQSSQLYLETC 307
Cdd:PRK06462 21 ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPII--SPStdplmGLGSDLpvkqISIDFYGVEYYLADSMILHKQLA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 308 LPALGDVFCIAQSYRAEQ--SRTRRHLAEYTHVEAECPFLTFDDLLNRLEDLVCDVVDRILKSPAGSIvHELNPNFQPPK 385
Cdd:PRK06462 99 LRMLGKIFYLSPNFRLEPvdKDTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHEDEL-EFFGRDLPHLK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 386 RPFKRMNYSDAIVWLKEHDVKKEDgtFYEFGEDIpeapERLMTDTINEPILLCRFPVEIKSFYMQRCPEDSRLTESVDVL 465
Cdd:PRK06462 178 RPFKRITHKEAVEILNEEGCRGID--LEELGSEG----EKSLSEHFEEPFWIIDIPKGSREFYDREDPERPGVLRNYDLL 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4758762 466 MPN-VGEIVGGSMRIFDSEEILAGYKREGIDPTPYYWYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPR 541
Cdd:PRK06462 252 LPEgYGEAVSGGEREYEYEEIVERIREHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQPFPR 328
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
125-548 |
4.40e-45 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 167.09 E-value: 4.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 125 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLA----------DELCQcyngvlLSTESSVAVYGMLNLTPKGKQA 194
Cdd:PTZ00401 78 DKTVLIRARVSTTRKKGK-MAFMVLRDGSDSVQAMAAvegdvpkemiDFIGQ------IPTESIVDVEATVCKVEQPITS 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 195 PGGHELSCD------FWELIGLAPAGGADNLINEESD-----VDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDR 263
Cdd:PTZ00401 151 TSHSDIELKvkkihtVTESLRTLPFTLEDASRKESDEgakvnFDTRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLIDS 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 264 GYYEVTPPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHLAEYTHVEAEC 342
Cdd:PTZ00401 231 DFCEIHSPKIINAPSEGGANVFKLEYFNRFAYLAQSPQLYKQMVLQGdVPRVFEVGPVFRSENSNTHRHLTEFVGLDVEM 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 343 PFLT-FDDLLNRLEDLVCDVVDRILKS-----------PAGSIVHELNPNFQP------------PKRPFK--------- 389
Cdd:PTZ00401 311 RINEhYYEVLDLAESLFNYIFERLATHtkelkavcqqyPFEPLVWKLTPERMKelgvgvisegvePTDKYQarvhnmdsr 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 390 --RMNYSDAIVWLKEHDVKKEDGTfyefgEDIPEAPERLMTDTINEP-----ILLCRFPVEIKSFYMQRCPEDSRLTESV 462
Cdd:PTZ00401 391 mlRINYMHCIELLNTVLEEKMAPT-----DDINTTNEKLLGKLVKERygtdfFISDRFPSSARPFYTMECKDDERFTNSY 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 463 DVLMPNvGEIVGGSMRIFDSEEILAGYKREGIDPTPYYWYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPRF 542
Cdd:PTZ00401 466 DMFIRG-EEISSGAQRIHDPDLLLARAKMLNVDLTPIKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFPRD 544
|
....*.
gi 4758762 543 VQRCTP 548
Cdd:PTZ00401 545 PQRTTP 550
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
285-542 |
8.89e-41 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 155.57 E-value: 8.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 285 FKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTFDDLLNRLEDLVCDVVDR 364
Cdd:PTZ00425 317 YKKDFFSKQAFLTVSGQLSLENLCSSMGDVYTFGPTFRAENSHTSRHLAEFWMIEPEIAFADLYDNMELAESYIKYCIGY 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 365 ILKSPAGSIVH-ELNPNFQPPKR-------PFKRMNYSDAIVWLKEHDVKKEdgTFYEFGEDIPEAPERLMTDTI-NEPI 435
Cdd:PTZ00425 397 VLNNNFDDIYYfEENVETGLISRlknildeDFAKITYTNVIDLLQPYSDSFE--VPVKWGMDLQSEHERFVAEQIfKKPV 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 436 LLCRFPVEIKSFYMqRCPEDSRLTESVDVLMPNVGEIVGGSMRIFDSEEILAGYKREGIDPTPYYWYTDQRKYGTCPHGG 515
Cdd:PTZ00425 475 IVYNYPKDLKAFYM-KLNEDQKTVAAMDVLVPKIGEVIGGSQREDNLERLDKMIKEKKLNMESYWWYRQLRKFGSHPHAG 553
|
250 260
....*....|....*....|....*..
gi 4758762 516 YGLGLERFLTWILNRYHIRDVCLYPRF 542
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 ... |
127-209 |
2.35e-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: 2.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 127 RVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLADELCQ-CYNGVLLSTESSVAVYGMLNLTPKGKQAPGGHELSCDFW 205
Cdd:cd04323 1 RVKVFGWVHRLRSQKK-LMFLVLRDGTGFLQCVLSKKLVTeFYDAKSLTQESSVEVTGEVKEDPRAKQAPGGYELQVDYL 79
|
....
gi 4758762 206 ELIG 209
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 ... |
246-541 |
2.69e-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: 2.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 246 LKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEGGATLFKLDYF--GEEAFLTQSSQLYLETCLPA-LGDVFCIAQSYR 322
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNalGLDYYLRISPQLFKKRLMVGgLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 323 AEQSRTRrHLAEYTHVEAECPFLTFDDLLNRLEDLVCDVVDRILkspaGSIVHELNPNFQPPKRPFKRMNYSDAIvwlke 402
Cdd:cd00669 81 NEDLRAR-HQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVL----GVTAVTYGFELEDFGLPFPRLTYREAL----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 403 hdvkkedgtfyefgedipeapERLmtdtiNEPILLCRFPVEIKSFYMQRCPEDSRLTESVDVLMPNVgEIVGGSMRIFDS 482
Cdd:cd00669 151 ---------------------ERY-----GQPLFLTDYPAEMHSPLASPHDVNPEIADAFDLFINGV-EVGNGSSRLHDP 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4758762 483 EEILAGYKREGIDPTP----YYWYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPR 541
Cdd:cd00669 204 DIQAEVFQEQGINKEAgmeyFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPK 266
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
285-541 |
9.47e-27 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 114.58 E-value: 9.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 285 FKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTFDDLLNRLEDLVCDVVDR 364
Cdd:PLN02532 363 FSKDFFSRPTYLTVSGRLHLESYACALGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAFSELEDAMNCAEDYFKFLCKW 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 365 ILKSPAGSIvhelnpNFQpPKR---------------PFKRMNYSDAIVWLKEH-DVKKEdgTFYEFGedIPEAPERL-- 426
Cdd:PLN02532 443 VLENCSEDM------KFV-SKRidktistrleaiissSLQRISYTEAVDLLKQAtDKKFE--TKPEWG--IALTTEHLsy 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 427 MTDTI-NEPILLCRFPVEIKSFYMqRCPEDSRLTESVDVLMPNVGEIVGGS-----MRIFDSEEILAGYKREgidptPYY 500
Cdd:PLN02532 512 LADEIyKKPVIIYNYPKELKPFYV-RLNDDGKTVAAFDLVVPKVGTVITGSqneerMDILNARIEELGLPRE-----QYE 585
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 4758762 501 WYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPR 541
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 ... |
127-209 |
1.84e-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: 1.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 127 RVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLADELCQ--CYNGVLLSTESSVAVYGMLNLTPKGKQAPGGHELSCDF 204
Cdd:cd04100 1 EVTLAGWVHSRRDHGG-LIFIDLRDGSGIVQVVVNKEELGefFEEAEKLRTESVVGVTGTVVKRPEGNLATGEIELQAEE 79
|
....*
gi 4758762 205 WELIG 209
Cdd:cd04100 80 LEVLS 84
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
125-397 |
3.84e-21 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 97.17 E-value: 3.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 125 GQRVKVFGWVHRLRRQGkNLMFLVLRDGTGYLQCV-LADELCQCYNGVL-LSTESSVAVYGMLNLTPKG----KQAPGGH 198
Cdd:PLN02903 72 GSRVTLCGWVDLHRDMG-GLTFLDVRDHTGIVQVVtLPDEFPEAHRTANrLRNEYVVAVEGTVRSRPQEspnkKMKTGSV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 199 ELSCDFWELIG---------LAPAGGADNLINEEsdvdVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDR-GYYEV 268
Cdd:PLN02903 151 EVVAESVDILNvvtkslpflVTTADEQKDSIKEE----VRLRYRVLDLRRPQMNANLRLRHRVVKLIRRYLEDVhGFVEI 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 269 TPPTLVQTQVEGGatlfkLDYF-------GEEAFLTQSSQLYLETCLPALGD-VFCIAQSYRAEQSRTRRHlAEYTHVEA 340
Cdd:PLN02903 227 ETPILSRSTPEGA-----RDYLvpsrvqpGTFYALPQSPQLFKQMLMVSGFDrYYQIARCFRDEDLRADRQ-PEFTQLDM 300
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 4758762 341 ECPFLTFDDLLNRLEDLVCDVVDRILkspagsivhelnpNFQPPkRPFKRMNYSDAI 397
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 ... |
246-540 |
1.23e-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: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 246 LKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEGGAtlfklDYF-------GEEAFLTQSSQLYLETCLPA-LGDVFCI 317
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTPEGAR-----DFLvpsrlhpGKFYALPQSPQLFKQLLMVSgFDRYFQI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 318 AQSYRAEQSRTRRHlAEYTHVEAECPFLTFDDLLNRLEDLVCDVVDRILKspagsivhelnpnfQPPKRPFKRMNYSDAI 397
Cdd:cd00777 76 ARCFRDEDLRADRQ-PEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG--------------VELTTPFPRMTYAEAM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 398 -------VW-----LKEHDvkKEDGTfYEFGEDIPEAPERLMTDTINEpillcrFPVEIKSfymqrcpedsrltESVDVL 465
Cdd:cd00777 141 erygfkfLWivdfpLFEWD--EEEGR-LVSAHHPFTAPKEEDLDLLEK------DPEDARA-------------QAYDLV 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4758762 466 MpNVGEIVGGSMRIFDSEEILAGYKREGIDPTPYY----WYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYP 540
Cdd:cd00777 199 L-NGVELGGGSIRIHDPDIQEKVFEILGLSEEEAEekfgFLLEAFKYGAPPHGGIALGLDRLVMLLTGSESIRDVIAFP 276
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
125-397 |
5.88e-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: 5.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 125 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLADELC--QCYN-GVLLSTESSVAVYGMLNLTPKGKQAP----GG 197
Cdd:PRK12820 18 GREVCLAGWVDAFRDHGE-LLFIHLRDRNGFIQAVFSPEAApaDVYElAASLRAEFCVALQGEVQKRLEETENPhietGD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 198 HELSCDfwELIGLAPA------------------GGADNlINEesdvDVQLNNRHMMIRGENMSKILKARSMVTRCFRDH 259
Cdd:PRK12820 97 IEVFVR--ELSILAASealpfaisdkamtagagsAGADA-VNE----DLRLQYRYLDIRRPAMQDHLAKRHRIIKCARDF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 260 FFDRGYYEVTPPTLVQTQVEGGATLFKLDYFGEEAF--LTQSSQLYLETCLPA-LGDVFCIAQSYRAEQSRTRRHlAEYT 336
Cdd:PRK12820 170 LDSRGFLEIETPILTKSTPEGARDYLVPSRIHPKEFyaLPQSPQLFKQLLMIAgFERYFQLARCFRDEDLRPNRQ-PEFT 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4758762 337 HVEAECPFLTFDDLLNRLEDLVCDVVDrilkspAGSIvhELNpnfqppkRPFKRMNYSDAI 397
Cdd:PRK12820 249 QLDIEASFIDEEFIFELIEELTARMFA------IGGI--ALP-------RPFPRMPYAEAM 294
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
125-397 |
6.19e-15 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 77.80 E-value: 6.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 125 GQRVKVFGWVHRLRRQGkNLMFLVLRDGTGYLQCVlADELCQCYNGVL-LSTESSVAVYGMLNLTPKG----KQAPGGHE 199
Cdd:PRK00476 17 GQTVTLCGWVHRRRDHG-GLIFIDLRDREGIVQVV-FDPDAEAFEVAEsLRSEYVIQVTGTVRARPEGtvnpNLPTGEIE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 200 LSCDFWELIglapaGGADNL---INEESDV--DVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLV 274
Cdd:PRK00476 95 VLASELEVL-----NKSKTLpfpIDDEEDVseELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDDNGFLEIETPILT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 275 QTQVEgGATlfklDYF-------GEeaF--LTQSSQL------------YletclpalgdvFCIAQSYRAEQSRTRRhLA 333
Cdd:PRK00476 170 KSTPE-GAR----DYLvpsrvhpGK--FyaLPQSPQLfkqllmvagfdrY-----------YQIARCFRDEDLRADR-QP 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4758762 334 EYTHVEAECPFLTFDDLLNRLEDLVCDVVDRILKspagsivHELnpnfqppKRPFKRMNYSDAI 397
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 ... |
128-208 |
4.38e-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: 4.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 128 VKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVL-ADELCQCYNgvLLSTESSVAVYGMLNLTPKgkqapGGHELSCDFWE 206
Cdd:pfam01336 1 VTVAGRVTSIRRSGGKLLFLTLRDGTGSIQVVVfKEEAEKLAK--KLKEGDVVRVTGKVKKRKG-----GELELVVEEIE 73
|
..
gi 4758762 207 LI 208
Cdd:pfam01336 74 LL 75
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
125-397 |
4.78e-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: 4.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 125 GQRVKVFGWVHRLRRQGkNLMFLVLRDGTGYLQCV-----------LADElcqcyngvlLSTESSVAVYGMLNLTPKG-- 191
Cdd:COG0173 16 GQEVTLSGWVHRRRDHG-GLIFIDLRDRYGITQVVfdpddsaeafeKAEK---------LRSEYVIAVTGKVRARPEGtv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 192 --KQAPGGHELSCDfwELIGLAPaggADNL---INEESDV--DVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRG 264
Cdd:COG0173 86 npKLPTGEIEVLAS--ELEILNK---AKTPpfqIDDDTDVseELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDENG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 265 YYEVTPPTLVQTQVEgGATlfklDYF-------GEeaF--LTQSSQL------------YletclpalgdvFCIAQSYRA 323
Cdd:COG0173 161 FLEIETPILTKSTPE-GAR----DYLvpsrvhpGK--FyaLPQSPQLfkqllmvsgfdrY-----------FQIARCFRD 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4758762 324 EQSRTRRHlAEYTHVEAECPFLTFDDLLNRLEDLVCDVVDRILKspagsivHELnpnfqppKRPFKRMNYSDAI 397
Cdd:COG0173 223 EDLRADRQ-PEFTQLDIEMSFVDQEDVFELMEGLIRHLFKEVLG-------VEL-------PTPFPRMTYAEAM 281
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
125-540 |
3.76e-11 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 65.50 E-value: 3.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 125 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLA-DELCQCYNGVLLSTESS--VAVYGMLNLTPKGkqapgghELS 201
Cdd:PRK00484 54 EIEVSVAGRVMLKRVMGK-ASFATLQDGSGRIQLYVSkDDVGEEALEAFKKLDLGdiIGVEGTLFKTKTG-------ELS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 202 --CDFWELI------------GLapaggadnlineeSDVDVQLNNRHM-MIRGENMSKILKARSMVTRCFRDHFFDRGYY 266
Cdd:PRK00484 126 vkATELTLLtkslrplpdkfhGL-------------TDVETRYRQRYVdLIVNPESRETFRKRSKIISAIRRFLDNRGFL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 267 EVTPPTLvQTqVEGGATL--FK--LDYFGEEAFLTQSSQLYLETCLpaLGD---VFCIAQSYRAEQSRTrRHLAEYTHVE 339
Cdd:PRK00484 193 EVETPML-QP-IAGGAAArpFIthHNALDIDLYLRIAPELYLKRLI--VGGferVYEIGRNFRNEGIDT-RHNPEFTMLE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 340 AECPFLTFDDLLNRLEDLVCDVVDRILkspaGSIV-----HELnpNFQPpkrPFKRMNYSDAIV---------------- 398
Cdd:PRK00484 268 FYQAYADYNDMMDLTEELIRHLAQAVL----GTTKvtyqgTEI--DFGP---PFKRLTMVDAIKeytgvdfddmtdeear 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 399 -WLKEHDVKKEDgtFYEFGEDIPEAPERLMTDTINEPILLCRFPVEI----KsfymqRCPEDSRLTESVDVlmpnvgeIV 473
Cdd:PRK00484 339 aLAKELGIEVEK--SWGLGKLINELFEEFVEPKLIQPTFITDYPVEIsplaK-----RHREDPGLTERFEL-------FI 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 474 GGSmrifdseEILAGYKrEGIDPtpyywyTDQRK----------------------------YGTCPHGGYGLGLER--- 522
Cdd:PRK00484 405 GGR-------EIANAFS-ELNDP------IDQRErfeaqveakeagddeamfmdedflraleYGMPPTGGLGIGIDRlvm 470
|
490
....*....|....*...
gi 4758762 523 FLTwilNRYHIRDVCLYP 540
Cdd:PRK00484 471 LLT---DSPSIRDVILFP 485
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
127-235 |
4.13e-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: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 127 RVKVFGWVHRLRRQGKNLmFLVLRDGTGYLQCVLADELC-QCYNGVL-LSTESSVAVYGMLNLTPKgkqAPGGHELSCDF 204
Cdd:cd04319 1 KVTLAGWVYRKREVGKKA-FIVLRDSTGIVQAVFSKDLNeEAYREAKkVGIESSVIVEGAVKADPR---APGGAEVHGEK 76
|
90 100 110
....*....|....*....|....*....|..
gi 4758762 205 WELIGLapaggADNL-INEESDVDVQLNNRHM 235
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 ... |
125-200 |
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 4758762 125 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLA-----DELCQCYNGvlLSTESSVAVYGMLNLTPKgkqAPGGHE 199
Cdd:cd04316 12 GEEVTVAGWVHEIRDLGG-IKFVILRDREGIVQVTAPkkkvdKELFKTVRK--LSRESVISVTGTVKAEPK---APNGVE 85
|
.
gi 4758762 200 L 200
Cdd:cd04316 86 I 86
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
128-203 |
3.32e-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: 3.32e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4758762 128 VKVFGWVhRLRRQGKNLMFLVLRDGTGY--LQCVLADELCQCYNGVLLSTESSVAVYGMLNLTPKGKQApggHELSCD 203
Cdd:cd04318 2 VTVNGWV-RSVRDSKKISFIELNDGSCLknLQVVVDKELTNFKEILKLSTGSSIRVEGVLVKSPGAKQP---FELQAE 75
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
67-540 |
6.23e-09 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 58.48 E-value: 6.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 67 KKMWHREQMKSESREKkEAEDSLR-----REKNLEEAKKITIKNDP-------SLPE--PKCVKIGALEGYRGQRVKVFG 132
Cdd:PTZ00417 61 KKVRSVQASKDKKKEE-EAEVDPRlyyenRSKFIQEQKAKGINPYPhkfertiTVPEfvEKYQDLASGEHLEDTILNVTG 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 133 WVHRLRRQGKNLMFLVLRDGTGYLQcVLAD---------ELCQCYNGVLLSTessvaVYGMLNLTPKGKQApgghELSCD 203
Cdd:PTZ00417 140 RIMRVSASGQKLRFFDLVGDGAKIQ-VLANfafhdhtksNFAECYDKIRRGD-----IVGIVGFPGKSKKG----ELSIF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 204 FWELIGLAPAGGADNLINEESDVDVQLNNRHM-MIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLvqTQVEGGA 282
Cdd:PTZ00417 210 PKETIILSPCLHMLPMKYGLKDTEIRYRQRYLdLMINESTRSTFITRTKIINYLRNFLNDRGFIEVETPTM--NLVAGGA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 283 TlfkldyfgEEAFLTQSSQLYLE------TCLP-------ALGDVFCIAQSYRAEqSRTRRHLAEYTHVEAECPFLTFDD 349
Cdd:PTZ00417 288 N--------ARPFITHHNDLDLDlylriaTELPlkmlivgGIDKVYEIGKVFRNE-GIDNTHNPEFTSCEFYWAYADFYD 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 350 LLNRLEDLVCDVV------DRILKSPAGSIVHELNPNFQPP------------------KRPFKRMNYSDAIVWL-KEHD 404
Cdd:PTZ00417 359 LIKWSEDFFSQLVmhlfgtYKILYNKDGPEKDPIEIDFTPPypkvsiveelekltntklEQPFDSPETINKMINLiKENK 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 405 VkkedgtfyefgeDIPEAP------ERLMTDTI-----NEPILLCRFPvEIKSFYMQRCPEDSRLTESVDVLMPNvGEIV 473
Cdd:PTZ00417 439 I------------EMPNPPtaakllDQLASHFIenkypNKPFFIIEHP-QIMSPLAKYHRSKPGLTERLEMFICG-KEVL 504
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4758762 474 GGSMRI---FDSEEILAGYK--REGIDPTPYYW---YTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYP 540
Cdd:PTZ00417 505 NAYTELndpFKQKECFSAQQkdREKGDAEAFQFdaaFCTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFP 579
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
225-540 |
6.34e-09 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 58.53 E-value: 6.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 225 DVDVQLNNRHM-MIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLvqTQVEGGAT----LFKLDYFGEEAFLTQS 299
Cdd:PRK12445 162 DQEVRYRQRYLdLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMM--QVIPGGASarpfITHHNALDLDMYLRIA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 300 SQLYLET-CLPALGDVFCIAQSYRAEqSRTRRHLAEYTHVEAECPFLTFDDLLNRLEDLVCDVVDRIL---KSPAGSIVH 375
Cdd:PRK12445 240 PELYLKRlVVGGFERVFEINRNFRNE-GISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLgttKVTYGEHVF 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 376 ELNpnfqppkRPFKRMNYSDAIvwlKEHDVKKEDGTFYEF------GEDIPEAPE------RLMTDTINE--------PI 435
Cdd:PRK12445 319 DFG-------KPFEKLTMREAI---KKYRPETDMADLDNFdaakalAESIGITVEkswglgRIVTEIFDEvaeahliqPT 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 436 LLCRFPVEIKSFyMQRCPEDSRLTESVDVLMPNvGEIVGGSMRIFDSEEILAGY------KREGIDPTPYYW--YTDQRK 507
Cdd:PRK12445 389 FITEYPAEVSPL-ARRNDVNPEITDRFEFFIGG-REIGNGFSELNDAEDQAERFqeqvnaKAAGDDEAMFYDedYVTALE 466
|
330 340 350
....*....|....*....|....*....|...
gi 4758762 508 YGTCPHGGYGLGLERFLTWILNRYHIRDVCLYP 540
Cdd:PRK12445 467 YGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
225-544 |
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 4758762 225 DVDVQLNNRHM-MIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEGGATLFKLDYFGEEA--FLTQSSQ 301
Cdd:PTZ00385 211 DNDVKYRYRFTdMMTNPCVIETIKKRHVMLQALRDYFNERNFVEVETPVLHTVASGANAKSFVTHHNANAMdlFLRVAPE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 302 LYLETCL-PALGDVFCIAQSYRAEQSrTRRHLAEYTHVEAECPFLTFDDLLNRLEDLVCDVVDRILKSPAGSIVHEL--- 377
Cdd:PTZ00385 291 LHLKQCIvGGMERIYEIGKVFRNEDA-DRSHNPEFTSCEFYAAYHTYEDLMPMTEDIFRQLAMRVNGTTVVQIYPENahg 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 378 NPNFQPPKRPFKRMNYSDAIVWLK------EHDVKKEDGTFY----EFGEDIPEAPER------------LMTDTINEPI 435
Cdd:PTZ00385 370 NPVTVDLGKPFRRVSVYDEIQRMSgvefppPNELNTPKGIAYmsvvMLRYNIPLPPVRtaakmfeklidfFITDRVVEPT 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 436 LLCRFPVEIKSFYMQrcpEDSR--LTESVDVLMPNVgEIVGGSMRIFDSEEILAGYKREGID-------PTPY-YWYTDQ 505
Cdd:PTZ00385 450 FVMDHPLFMSPLAKE---QVSRpgLAERFELFVNGI-EYCNAYSELNDPHEQYHRFQQQLVDrqggdeeAMPLdETFLKS 525
|
330 340 350
....*....|....*....|....*....|....*....
gi 4758762 506 RKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPRFVQ 544
Cdd:PTZ00385 526 LQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFPLLRQ 564
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
125-230 |
1.66e-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: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 125 GQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLADELCQCYNGVL-LSTESSVAVYGMLNLTPKG----KQAPGGHE 199
Cdd:cd04317 14 GQEVTLCGWVQRRRDHGG-LIFIDLRDRYGIVQVVFDPEEAPEFELAEkLRNESVIQVTGKVRARPEGtvnpKLPTGEIE 92
|
90 100 110
....*....|....*....|....*....|....
gi 4758762 200 LSCDFWELIGLapaggADNL---INEESDVDVQL 230
Cdd:cd04317 93 VVASELEVLNK-----AKTLpfeIDDDVNVSEEL 121
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
119-340 |
1.57e-07 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 54.58 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 119 ALEGYRGQRVKVFGWVHRLRRQGKnLMFLVLRDGTGYLQCVLADELCQCYNGVLLSTESS----VAVYGMLNLTPKGkqa 194
Cdd:PRK02983 645 ALDAPTGEEVSVSGRVLRIRDYGG-VLFADLRDWSGELQVLLDASRLEQGSLADFRAAVDlgdlVEVTGTMGTSRNG--- 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 195 pgghELS--CDFWELIG--LAPaggadnLINEE---SDVDVQLNNRHM--MIRGENMSkILKARSMVTRCFRDHFFDRGY 265
Cdd:PRK02983 721 ----TLSllVTSWRLAGkcLRP------LPDKWkglTDPEARVRQRYLdlAVNPEARD-LLRARSAVVRAVRETLVARGF 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 266 YEVTPPTLvQtQVEGGAT----LFKLDYFGEEAFLTQSSQLYLET-CLPALGDVFCIAQSYRAE-QSRTrrHLAEYTHVE 339
Cdd:PRK02983 790 LEVETPIL-Q-QVHGGANarpfVTHINAYDMDLYLRIAPELYLKRlCVGGVERVFELGRNFRNEgVDAT--HNPEFTLLE 865
|
.
gi 4758762 340 A 340
Cdd:PRK02983 866 A 866
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
128-190 |
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 4758762 128 VKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVLA-------DELCQCYNGvlLSTESSVAVYGMLNLTPK 190
Cdd:cd04320 2 VLIRARVHTSRAQGAKLAFLVLRQQGYTIQGVLAasaegvsKQMVKWAGS--LSKESIVDVEGTVKKPEE 69
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
242-536 |
4.41e-06 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 48.77 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 242 MSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQ-TQVEGGATLFKLDYFGEEAflTQSSQLYLETC--------LPAL- 311
Cdd:PRK09350 1 SIPNLLKRAKIIAEIRRFFADRGVLEVETPILSQaTVTDIHLVPFETRFVGPGA--SQGKTLWLMTSpeyhmkrlLAAGs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 312 GDVFCIAQSYRAEQSrTRRHLAEYTHVEAECPFLTFDDLLNRLEDLV-----CDVVDRILKSPAGSIVHELNPnFQPPKR 386
Cdd:PRK09350 79 GPIFQICKSFRNEEA-GRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLqqvldCEPAESLSYQQAFLRYLGIDP-LSADKT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 387 PFKrmnysDAIVWLKEHDVKKEDgtfyefgEDIPEAPERLMTDTI------NEPILLCRFPVEIKSfYMQRCPEDSRLTE 460
Cdd:PRK09350 157 QLR-----EVAAKLGLSNIADEE-------EDRDTLLQLLFTFGVepnigkEKPTFVYHFPASQAA-LAKISTEDHRVAE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 461 SVDVLMPNVgEIVGGSMRIFDSEEILAGYKR-------EGIDPTPyywyTDQR-----KYGTCPHGGYGLGLERFLTWIL 528
Cdd:PRK09350 224 RFEVYFKGI-ELANGFHELTDAREQRQRFEQdnrkraaRGLPQQP----IDENliaalEAGLPDCSGVALGVDRLIMLAL 298
|
....*...
gi 4758762 529 NRYHIRDV 536
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 ... |
249-341 |
6.84e-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: 6.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758762 249 RSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEGGATLFKLD------YFGEEAFLTQSSQLYLET----CLPALGD-VFCI 317
Cdd:cd00768 2 RSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHEPKDllpvgaENEEDLYLRPTLEPGLVRlfvsHIRKLPLrLAEI 81
|
90 100
....*....|....*....|....*
gi 4758762 318 AQSYRAEQSRTR-RHLAEYTHVEAE 341
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 ... |
127-207 |
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 4758762 127 RVKVFGWVHRLRRQGKNLMFLVLRDGTGY-LQCVLADElcqcyNGVL-----LSTESSVAVYGMLNLtpkgKQAPGGHEL 200
Cdd:cd04321 1 KVTLNGWIDRKPRIVKKLSFADLRDPNGDiIQLVSTAK-----KDAFsllksITAESPVQVRGKLQL----KEAKSSEKN 71
|
....*..
gi 4758762 201 SCdfWEL 207
Cdd:cd04321 72 DE--WEL 76
|
|
| |
