Aspartyl-tRNA synthetase, putative [Q4Q7R2] | |
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Systematic Name | LmjF.30.0460 [Leishmania major] |
Gene Name | LMJF_30_0460 |
Molecular Weight | 62374 Da |
Protein Sequence Size | 550 |
Function | |
Charge | 5.5 |
Isoelectric Point | 7.3 pH |
Description | Aspartyl-tRNA synthetase, putative (EC 6.1.1.12). |
Subcellular Location | cytoplasm[Predict] |
E. C. Number | 6.1.1.12 |
Sequence | >tr|Q4Q7R2|Q4Q7R2_LEIMA Aspartyl-tRNA synthetase, putative (EC 6.1.1.12) - Leishmania major SANHADAGAPAVAKKMSDKEARKAARLAEEKARADEKAALVEKYKAVFGAAPMVQSTTYK SRTHIPVSELSRPELVDKTVLIRARVSTTRKKGKMAFMVLRDGSDSVQAMAAVEGDVPKE MIDFMGQIATESIVDVEATVCKVEQPITSTSHSDIELKVKKIHTVTESLRTLPFTLEDAS RKESAEGAKVNLDTRLNSRWMDLRTLASGAIFRLQSRVCQYFRQFLIDKDFCEIHSPKII NAPSEGGANVFKLEYFNRFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNTHRHLT EFVGLDVEMRIDEHYYEVLDVAESLFNYIFERLATHTKELKNVCQQYPFEPLVWKLTPER IKELGVGVISEGVVPTDKFQARVHNMDSRMLRINYMHCIELLNTVLDEKMAPTDDINTTN EKLLGKLVKERYGTDFFISDRFPSSARPFYTMECKDDVRFTNSYDMFIRGEEISSGAQRI HDPDLLLARAKMLNVDLTPIKEYVDSFRLGAWPHGGFGIGLERVVMLYLGLSNVRLASLF PRDPQRTTP |
DNA Sequence | >LmjF30.0460 |||aspartyl-tRNA synthetase, putative|Leishmania major|chr 30|||Manual ATGAGCGCAA ACCACGCCGA TGCCGGCGCA CCAGCCGTGG CGAAGAAGAT GAGCGACAAAGAGGCGCGTA AGGCGGCGCG CCTGGCGGAG GAGAAGGCCC GCGCGGATGA AAAGGCGGCCCTTGTGGAGA AGTACAAGGC CGTGTTTGGT GCCGCACCAA TGGTGCAGTC GACGACGTACAAGTCGCGCA CGCACATCCC GGTCTCGGAG CTGTCGCGGC CGGAGTTGGT GGACAAGACGGTGCTGATCC GTGCCCGCGT GTCGACGACG CGCAAGAAGG GCAAGATGGC GTTCATGGTGCTGCGCGACG GGAGCGATTC GGTGCAGGCG ATGGCTGCCG TGGAAGGCGA TGTGCCGAAGGAGATGATCG ACTTCATGGG GCAGATCGCG ACAGAGTCGA TTGTTGATGT GGAGGCGACAGTTTGCAAGG TGGAGCAGCC CATCACGTCG ACGTCGCACT CGGACATCGA GCTGAAGGTGAAGAAGATCC ACACGGTGAC GGAGTCGCTG CGCACGCTGC CGTTCACGCT AGAGGACGCGAGCCGCAAGG AGTCGGCCGA GGGTGCGAAG GTGAACCTCG ACACGCGCCT GAATAGCCGCTGGATGGACC TGCGCACACT AGCGTCCGGC GCGATCTTCC GCCTTCAGTC GCGCGTGTGCCAGTACTTCC GCCAGTTTCT TATCGACAAG GACTTCTGTG AGATCCACTC GCCCAAGATCATCAACGCGC CGAGCGAGGG TGGCGCCAAC GTGTTCAAGC TGGAGTACTT CAACCGCTTCGCGTACCTTG CCCAGTCGCC ACAACTGTAC AAGCAGATGG TGCTGCAGGG CGATGTGCCGCGCGTGTTCG AGGTGGGACC GGTGTTCCGC TCAGAGAACA GCAACACACA CCGCCACCTGACGGAGTTTG TTGGGTTGGA CGTGGAGATG CGCATCGATG AGCACTACTA CGAGGTGCTGGATGTGGCGG AGAGCCTATT CAACTACATT TTCGAGCGCC TTGCCACTCA CACAAAGGAGCTGAAGAACG TGTGCCAGCA GTACCCCTTC GAGCCTCTCG TGTGGAAGCT CACACCGGAGAGGATAAAGG AGCTCGGCGT TGGCGTCATC TCGGAGGGCG TGGTGCCGAC AGACAAGTTTCAGGCACGCG TGCACAACAT GGATAGCCGT ATGCTGCGTA TCAACTACAT GCACTGCATTGAGCTGTTGA ACACTGTGCT GGACGAGAAG ATGGCGCCGA CGGATGACAT CAACACGACGAACGAGAAGC TGCTCGGCAA GCTTGTGAAG GAGCGCTACG GCACAGACTT CTTCATCTCGGACCGCTTTC CGTCCTCGGC GCGCCCGTTC TACACGATGG AGTGCAAGGA CGACGTGCGCTTCACGAACT CGTACGATAT GTTCATCCGC GGTGAGGAGA TCTCCAGCGG AGCGCAGCGCATCCACGACC CCGATCTGCT GCTGGCACGC GCCAAGATGC TGAACGTGGA TCTCACACCGATCAAGGAGT ACGTCGACTC CTTCCGTCTC GGTGCGTGGC CGCACGGCGG CTTCGGCATTGGGCTGGAGC GCGTGGTGAT GCTGTACCTT GGACTGAGCA ACGTGCGCCT TGCTTCGCTCTTTCCGCGTG ACCCGCAGCG CACGACGCCA TAG |
Aspartyl-tRNA synthetase, putative Q4Q7R2] | |
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Metabolite Information | |
Molecular Function | ATP binding; aminoacyl-tRNA ligase activity; asparagine-tRNA ligase activity; aspartate-tRNA ligase activity; nucleic acid binding |
Biochemical Pathway | asparaginyl-tRNA aminoacylation; aspartyl-tRNA aminoacylation; protein complex assembly; tRNA aminoacylation for protein translation |
Regulatory Pathway | |
KEGG Pathways | K01876 |
Orthologs | ||||
Homologs | GI | Percent Identity | Evalue | Score |
Homo sapiens | aspartyl-tRNA synthetase [Homo sapiens] | 49 | 1e-122 | 437 |
DEG Information | ||||
DEG Protein | DEG Organism | Percent Identity | Evalue | Bit Score |
YLL018c aspartyl-tRNA synthetase, cytosolic | Saccharomyces cerevisiae | 45% | 1e-116 | 413 |
Post Translational Modification | ||||
PTM Type | PTM Sub Type | Score | Modification Site | Prosite ID |
PDOC00363 | Aminoacyl-transfer RNA synthetases class-II profiles | 21.197 | 213-542 | PS50862 |
Acylation | N-myristoylation site | 127-132; 188-193; 373-378; | PS00008 | |
Glycosylation | N-glycosylation site | 418-421; | PS00001 | |
Phosphorylation | cAMP- and cGMP-dependent protein kinase phosphorylation site | 15-18; 182-185; | PS00004 | |
Phosphorylation | Casein kinase II phosphorylation site | 18-21; 72-75; 133-136; 152-155; 154-157; 165-168; 176-179; 181-184; 405-408; 419-422; | PS00006 | |
Phosphorylation | Protein kinase C phosphorylation site | 18-20; 59-61; 89-91; 90-92; 169-171; 181-183; 237-239; 296-298; 377-379; 440-442; 446-448; 507-509; | PS00005 | |
Phosphorylation | Tyrosine kinase phosphorylation site | 311-317; | PS00007 |
Aspartyl-tRNA synthetase, putative [Q4Q7R2] | ||
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Model Information | ||
Template PDB ID | 1eovA | |
Percent Identity | 45% | |
Target Region | 1-559 | |
Template Region | 71-487 |
Domain Information | ||
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Domains | Start | End |
Active Site Information | ||
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Residue | Active Site Number | Functional Part |
ARG | 290 | Sidechain |
ASP | 307 | Sidechain |
ARG | 524 | Sidechain |
Co-Factor | |
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Metal | Description |
Ligands | |||||
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CAS number | Name | Mol. Weight | Mol. Formula | Smile Notation | PDB Reference |
Mutational Information | ||
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Residue | Feature | Description |
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Modeled Protein | Template Structure |
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+----------<<< P R O C H E C K S U M = M A R Y >>>----------+ | = | | /var/www/html/Services/SAVES_3/jobs/3197808/Q4Q7R2.pdb 2.0 550 = residues | | = | +| Ramachandran plot: 93.4% core 6.4% allow 0.2% gener 0.0% = disall | | = | +| All Ramachandrans: 14 labelled residues (out of 548) = | +| Chi1-chi2 plots: 1 labelled residues (out of 337) = | | = | | Main-chain params: 6 better 0 inside 0 worse = | | Side-chain params: 5 better 0 inside 0 worse = | | = | *| Residue properties: Max.deviation: 3.0 Bad contacts: = 8 | *| Bond len/angle: 5.0 Morris et al class: 1 = 1 2 | +| 1 cis-peptides = | | G-factors Dihedrals: 0.09 Covalent: -0.13 Overall: = 0.01 | | = | | M/c bond lengths: 99.4% within limits 0.6% highlighted = | | M/c bond angles: 94.6% within limits 5.4% highlighted = | | Planar groups: 100.0% within limits 0.0% highlighted = | | = | = +------------------------------------------------------------------------= ----+ + May be worth investigating further. * Worth investigating further. |