Glutaminyl-tRNA synthetase, putative [Q4QF36] | |
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Systematic Name | LmjF.15.1440 [Leishmania major] |
Gene Name | LMJF_15_1440 |
Molecular Weight | 66076 Da |
Protein Sequence Size | 570 |
Function | |
Charge | 4 |
Isoelectric Point | 6.9 pH |
Description | Glutaminyl-tRNA synthetase, putative. |
Subcellular Location | N.A.[Predict] |
E. C. Number | N.A. |
Sequence | >tr|Q4QF36|Q4QF36_LEIMA Glutaminyl-tRNA synthetase, putative - Leishmania major. AGPAAAEVKEMETKRDLSILQSGRPVPGCRNTRELLETHEKVTGGKPYFRFPPEPNGFLH IGHAKSMNLNFGSARAHGGKCYLRYDDTNPESEDQVYIDAIMEMVNWMGWKPDWVTFSSD YFDQLHTFAVQLIKDGKAYVDHSTPDELKQQREQREDSPWRNRSVEENLLLFKHMRQGRY AEGEATLRVKADMKSDNPNMRDFIAYRVKYVEHPHVKDKWCIYPSYDFTHCLIDSLEDID YSLCTLEFETRRESYFWLLNELNLWRPHVWEFSRLNVTGSLLSKRKINVLVRKGIVRGFD DPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCERRLMVI DPIKVVVDNWKGERIFECPNHPRKPELGGRALTFTDTFYVDRSDFRTEDNNNKFYGLAPG PRVVGLKYSGNVVCKSFEVDANGQSMVIHVDIDFERKDKPKTNISWVSATACTPVEVRLY NALLKDDRAAIDPEFLKFIDENSEVVSHGYAEKGVENFKHFESIQVERFGYFVVDPDTKV DHLVMNRVLGLREDKSKATVGEPVPTKRK |
DNA Sequence | >LmjF15.1440 |||glutaminyl-tRNA synthetase, putative|Leishmania major|chr 15|||Manual ATGGCGGGAC CGGCAGCTGC GGAAGTGAAA GAAATGGAGA CGAAGCGCGA CCTGTCGATCCTGCAGAGCG GCCGTCCCGT CCCGGGGTGC CGGAACACGC GCGAGCTGCT CGAGACGCACGAGAAGGTCA CCGGCGGGAA GCCGTACTTT CGCTTTCCTC CGGAGCCAAA TGGCTTCCTGCACATTGGCC ATGCCAAGAG CATGAACCTC AACTTCGGCA GCGCACGCGC GCACGGTGGCAAGTGCTACC TGCGCTACGA CGATACGAAC CCCGAGTCGG AGGATCAGGT CTACATTGATGCTATCATGG AGATGGTGAA CTGGATGGGG TGGAAACCGG ACTGGGTCAC CTTTTCCTCCGACTACTTCG ACCAGCTGCA CACCTTCGCC GTGCAGCTCA TCAAGGATGG GAAGGCCTACGTCGATCACA GCACGCCAGA CGAGCTGAAG CAGCAGCGGG AGCAGCGCGA GGACAGCCCGTGGCGCAACC GCAGCGTCGA GGAGAATCTG CTCCTCTTCA AGCACATGCG CCAGGGCCGTTACGCTGAGG GCGAGGCGAC GCTTCGCGTG AAGGCCGATA TGAAGAGCGA CAACCCGAACATGCGCGACT TCATTGCGTA CCGCGTCAAG TACGTCGAGC ACCCGCACGT CAAGGACAAGTGGTGCATCT ACCCAAGCTA CGACTTCACC CACTGCCTCA TCGACTCGCT CGAGGACATCGACTACAGCC TGTGTACGCT GGAGTTCGAG ACGCGCCGCG AGAGCTACTT CTGGCTGCTGAACGAGCTCA ACCTGTGGCG TCCGCACGTG TGGGAGTTCA GCCGCCTGAA CGTGACGGGCTCGCTGCTCT CGAAGCGTAA GATCAACGTG CTGGTGCGCA AGGGCATTGT CCGCGGGTTTGACGACCCCC GTCTGCTCAC CCTTGCCGGC ATGCGTCGCC GCGGGTACAC TCCGGCCGCCATTAACCGCT TCTGCGAGCT GGTTGGTATC ACCCGCTCCA TGAATGTAAT TCAGATCAGCATGCTGGAGA ACACCCTGCG CGAGGACCTC GACGAGCGCT GCGAGCGCCG GCTGATGGTGATTGACCCAA TCAAAGTGGT GGTGGACAAC TGGAAGGGCG AGCGAATCTT CGAGTGCCCGAACCATCCGC GCAAGCCTGA GCTCGGTGGC CGCGCCTTGA CATTTACGGA CACCTTCTACGTCGACCGCA GCGACTTCCG CACAGAAGAC AACAACAACA AGTTCTACGG ACTCGCCCCTGGCCCACGCG TGGTGGGCCT CAAGTACTCA GGCAACGTTG TGTGCAAGAG CTTCGAGGTGGACGCCAATG GACAGTCGAT GGTGATTCAT GTAGACATCG ACTTCGAGCG CAAGGACAAGCCGAAGACAA ATATCTCCTG GGTGAGTGCG ACGGCATGTA CGCCGGTGGA GGTGCGCTTGTACAACGCGC TCCTCAAGGA CGACCGTGCC GCCATCGATC CCGAGTTTCT CAAGTTCATCGACGAGAACA GTGAGGTGGT GTCGCACGGG TACGCGGAGA AGGGCGTCGA GAATTTCAAGCACTTCGAGT CGATCCAGGT GGAACGCTTC GGGTACTTCG TCGTCGACCC TGATACGAAGGTCGACCACC TCGTCATGAA CCGAGTGCTG GGCCTGCGCG |
Glutaminyl-tRNA synthetase, putative Q4QF36] | |
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Metabolite Information | |
Molecular Function | ATP binding; glutamate-tRNA ligase activity; glutamine-tRNA ligase activity |
Biochemical Pathway | glutamyl-tRNA aminoacylation |
Regulatory Pathway | |
KEGG Pathways | K01886 |
Orthologs | ||||
Homologs | GI | Percent Identity | Evalue | Score |
Homo sapiens | glutaminyl-tRNA synthetase [Homo sapiens] | 43 | 1e-116 | 415 |
DEG Information | ||||
DEG Protein | DEG Organism | Percent Identity | Evalue | Bit Score |
YOR168w glutaminyl-tRNA synthetase | Saccharomyces cerevisiae | 43% | 1e-124 | 440 |
Post Translational Modification | ||||
PTM Type | PTM Sub Type | Score | Modification Site | Prosite ID |
PDOC00161 | Aminoacyl-transfer RNA synthetases class-I signature | 54-65; | PS00178 | |
Acylation | N-myristoylation site | 29-34; 73-78; 280-285; 295-300; 329-334; 426-431; 431-436; | PS00008 | |
Glycosylation | N-glycosylation site | 163-166; 277-280; 464-467; | PS00001 | |
Phosphorylation | cAMP- and cGMP-dependent protein kinase phosphorylation site | 252-255; | PS00004 | |
Phosphorylation | Casein kinase II phosphorylation site | 14-17; 89-92; 144-147; 145-148; 165-168; 236-239; 251-254; 340-343; 345-348; 394-397; 474-477; 539-542; 560-563; | PS00006 | |
Phosphorylation | Protein kinase C phosphorylation site | 14-16; 23-25; 74-76; 187-189; 251-253; 284-286; 345-347; 567-569; | PS00005 | |
Sulfation | Tyrosine sulfation site | 393-407; | PS00003 |
Glutaminyl-tRNA synthetase, putative [Q4QF36] | ||
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Model Information | ||
Template PDB ID | 1qrsA | |
Percent Identity | 44% | |
Target Region | 47-578 | |
Template Region | 26-511 |
Domain Information | ||
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Domains | Start | End |
Active Site Information | ||
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Residue | Active Site Number | Functional Part |
GLU | 9 | Sidechain |
ARG | 229 | Sidechain |
LYS | 239 | 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 |
84412-18-0 | ADENOSINE-5'-TRIPHOSPHATE | 507.181 | C10 H16 N5 O13 P3 | O=P(O)(O)OP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O | 1qrs |
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/12493/Q4QF36.pdb 2.0 524 = residues | | = | +| Ramachandran plot: 91.2% core 8.3% allow 0.4% gener 0.0% = disall | | = | +| All Ramachandrans: 15 labelled residues (out of 522) = | +| Chi1-chi2 plots: 1 labelled residues (out of 344) = | | = | | Main-chain params: 6 better 0 inside 0 worse = | | Side-chain params: 5 better 0 inside 0 worse = | | = | *| Residue properties: Max.deviation: 5.3 Bad contacts: = 6 | *| Bond len/angle: 10.3 Morris et al class: 1 = 1 2 | | = | | G-factors Dihedrals: -0.01 Covalent: -0.23 Overall: = -0.09 | | = | *| M/c bond lengths: 98.8% within limits 1.2% highlighted 2 off = graph | *| M/c bond angles: 92.2% within limits 7.8% highlighted 2 off = graph | | Planar groups: 100.0% within limits 0.0% highlighted = | | = | = +------------------------------------------------------------------------= ----+ + May be worth investigating further. * Worth investigating further. |