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Aspartyl-tRNA synthetase, putative [Q4Q7R2]
Systematic NameLmjF.30.0460 [Leishmania major]
Gene NameLMJF_30_0460
Molecular Weight62374 Da
Protein Sequence Size550
Function
Charge5.5
Isoelectric Point7.3 pH
DescriptionAspartyl-tRNA synthetase, putative (EC 6.1.1.12).
Subcellular Locationcytoplasm[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]
Metabolite Information
Molecular FunctionATP binding; aminoacyl-tRNA ligase activity; asparagine-tRNA ligase activity; aspartate-tRNA ligase activity; nucleic acid binding
Biochemical Pathwayasparaginyl-tRNA aminoacylation; aspartyl-tRNA aminoacylation; protein complex assembly; tRNA aminoacylation for protein translation
Regulatory Pathway
KEGG PathwaysK01876
Orthologs
Homologs GI Percent Identity Evalue Score
Homo sapiensaspartyl-tRNA synthetase [Homo sapiens]491e-122437
DEG Information
DEG Protein DEG Organism Percent Identity Evalue Bit Score
YLL018c aspartyl-tRNA synthetase, cytosolicSaccharomyces cerevisiae45%1e-116413
Post Translational Modification
PTM Type PTM Sub Type Score Modification Site Prosite ID
PDOC00363Aminoacyl-transfer RNA synthetases class-II profiles21.197213-542PS50862
AcylationN-myristoylation site127-132; 188-193; 373-378; PS00008
GlycosylationN-glycosylation site418-421; PS00001
PhosphorylationcAMP- and cGMP-dependent protein kinase phosphorylation site15-18; 182-185; PS00004
PhosphorylationCasein kinase II phosphorylation site18-21; 72-75; 133-136; 152-155; 154-157; 165-168; 176-179; 181-184; 405-408; 419-422; PS00006
PhosphorylationProtein kinase C phosphorylation site18-20; 59-61; 89-91; 90-92; 169-171; 181-183; 237-239; 296-298; 377-379; 440-442; 446-448; 507-509; PS00005
PhosphorylationTyrosine kinase phosphorylation site311-317; PS00007
Aspartyl-tRNA synthetase, putative [Q4Q7R2]
Model Information
Template PDB ID1eovA
Percent Identity45%
Target Region1-559
Template Region71-487
Domain Information
Domains Start End
Active Site Information
Residue Active Site Number Functional Part
ARG290Sidechain
ASP307Sidechain
ARG524Sidechain
Co-Factor
Metal Description
Ligands
CAS number Name Mol. Weight Mol. Formula Smile Notation PDB Reference
Mutational Information
Residue Feature Description
Modeled Protein Template Structure
+----------<<< 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.
Overlapped Structure Procheck Summary
LeishBase: Leishmania Structural Database