| N-myristoyl transferase, putative [Q4Q5S8] | |
|---|---|
| Systematic Name | LmjF.32.0080 [Leishmania major] |
| Gene Name | NMT |
| Molecular Weight | 48514 Da |
| Protein Sequence Size | 421 |
| Function | |
| Charge | 0.5 |
| Isoelectric Point | 6.5 pH |
| Description | N-myristoyl transferase, putative (EC 2.3.1.97). |
| Subcellular Location | N.A.[Predict] |
| E. C. Number | 2.3.1.97 |
| Sequence | >tr|Q4Q5S8|Q4Q5S8_LEIMA N-myristoyl transferase, putative (EC 2.3.1.97) - Leishmania major. SRNPSNSDAAHAFWSTQPVPQTEDETEKIVFAGPMDEPKTVADIPEEPYPIASTFEWWTP NMEAADDIHAIYELLRDNYVEDDDSMFRFNYSEEFLQWALCPPNYIPDWHVAVRRKADKK LLAFIAGVPVTLRMGTPKYMKVKAQEKGEGEEAAKYDEPRHICEINFLCVHKQLREKRLA PILIKEATRRVNRTNVWQAVYTAGVLLPTPYASGQYFHRSLNPEKLVEIRFSGIPAQYQK FQNPMAMLKRNYQLPSAPKNSGLREMKPSDVPQVRRILMNYLDSFDVGPVFSDAEISHYL LPRDGVVFTYVVENDKKVTDFFSFYRIPSTVIGNSNYNLLNAAYVHYYAATSIPLHQLIL DLLIVAHSRGFDVCNMVEILDNRSFVEQLKFGAGDGHLRYYFYNWAYPKIKPSQVALVML |
| DNA Sequence | >LmjF32.0080 |NMT||N-myristoyl transferase, putative|Leishmania major|chr 32|||Manual ATGTCTCGCA ATCCATCGAA CTCCGACGCT GCGCATGCGT TCTGGAGCAC ACAGCCCGTACCGCAGACGG AAGATGAGAC GGAGAAAATT GTGTTCGCTG GTCCGATGGA CGAGCCAAAGACGGTAGCCG ATATTCCTGA GGAGCCGTAC CCGATCGCCA GCACATTTGA GTGGTGGACGCCGAACATGG AGGCGGCCGA CGACATTCAC GCAATTTACG AGCTTCTTCG GGATAACTACGTCGAAGACG ACGACAGCAT GTTTCGTTTC AACTACTCCG AGGAGTTTCT TCAGTGGGCACTATGCCCAC CGAACTACAT CCCGGACTGG CACGTTGCAG TTCGCCGAAA GGCGGATAAGAAGCTGCTGG CCTTCATTGC CGGCGTTCCC GTGACGTTGC GCATGGGCAC TCCCAAGTACATGAAGGTGA AAGCACAGGA AAAGGGCGAA GGGGAGGAGG CGGCCAAGTA TGATGAACCCCGTCACATCT GCGAAATCAA CTTTCTCTGT GTCCACAAGC AACTCCGGGA GAAGCGGCTTGCCCCGATTT TGATCAAAGA GGCGACGCGC CGCGTGAACC GCACCAACGT GTGGCAGGCGGTGTACACGG CTGGGGTGCT GCTACCCACT CCGTATGCAT CAGGGCAGTA CTTCCACCGCAGCCTGAACC CCGAGAAGCT TGTGGAGATC CGCTTCAGCG GCATTCCAGC ACAGTACCAAAAGTTTCAGA ACCCAATGGC GATGCTGAAG CGCAACTACC AGCTGCCAAG CGCGCCGAAGAACTCTGGTC TTCGTGAAAT GAAGCCGTCT GACGTTCCGC AGGTGCGGCG GATTCTCATGAACTACCTGG ACAGCTTCGA TGTAGGTCCC GTCTTTAGCG ATGCCGAGAT CAGCCACTACCTCCTTCCAC GCGACGGTGT GGTCTTCACC TACGTGGTGG AAAACGACAA GAAGGTGACCGACTTCTTTT CCTTCTATCG AATTCCGTCG ACTGTGATTG GGAACAGCAA TTACAACCTTCTGAACGCAG CTTACGTTCA CTACTATGCC GCGACGAGTA TACCTTTGCA TCAACTCATTCTCGACCTTT TGATCGTGGC GCATTCACGC GGCTTCGACG TGTGCAATAT GGTAGAGATCCTCGACAACC GGTCTTTCGT TGAGCAGCTC AAGTTTGGCG CCGGCGACGG TCATCTTCGATATTACTTCT ACAACTGGGC GTATCCAAAG ATCAAGCCTT CTCAGGTTGC CTTGGTGATGCTGTAG |
| N-myristoyl transferase, putative Q4Q5S8] | |
|---|---|
| Metabolite Information | N-terminal protein myristoylation |
| Molecular Function | |
| Biochemical Pathway | |
| Regulatory Pathway | |
| KEGG Pathways | K00671 |
| Orthologs | ||||
| Homologs | GI | Percent Identity | Evalue | Score |
| Homo sapiens | glycylpeptide N-tetradecanoyltransferase 2 [Homo sapiens] | 44 | 2e-98 | 356 |
| DEG Information | ||||
| DEG Protein | DEG Organism | Percent Identity | Evalue | Bit Score |
| YLR195c N-myristoyltransferase | Saccharomyces cerevisiae | 41% | 3e-86 | 312 |
| Post Translational Modification | ||||
| PTM Type | PTM Sub Type | Score | Modification Site | Prosite ID |
| PDOC00595 | Formate--tetrahydrofolate ligase signatures | 91-94; 193-196; 383-386; | PS00722 | |
| PDOC00752 | Myristoyl-CoA:protein N-myristoyltransferase signatures | 165-173; | PS00975 | |
| PDOC00752 | Myristoyl-CoA:protein N-myristoyltransferase signatures | 391-397; | PS00976 | |
| PDOC00015 | The rule PS00015 has been deleted from the PROSITE database and replaced by the following motif: PS50079 (Bipartite nuclear localization signal profile | 178-194; | PS00015 | |
| Acylation | N-myristoylation site | 128-133; 306-311; 393-398; | PS00008 | |
| Phosphorylation | cAMP- and cGMP-dependent protein kinase phosphorylation site | 317-320; | PS00004 | |
| Phosphorylation | Casein kinase II phosphorylation site | 6-9; 23-26; 41-44; 54-57; 293-296; 385-388; | PS00006 | |
| Phosphorylation | Protein kinase C phosphorylation site | 27-29; 132-134; 137-139; 189-191; | PS00005 | |
| Sulfation | Tyrosine sulfation site | 73-87; | PS00003 | |
| N-myristoyl transferase, putative [Q4Q5S8] | ||
|---|---|---|
| Model Information | ||
| Template PDB ID | 1rxtD | |
| Percent Identity | 42% | |
| Target Region | 66-422 | |
| Template Region | 89-326 | |
| Domain Information | ||
|---|---|---|
| Domains | Start | End |
| Active Site Information | ||
|---|---|---|
| Residue | Active Site Number | Functional Part |
| Co-Factor | |
|---|---|
| Metal | Description |
| Ligands | |||||
|---|---|---|---|---|---|
| CAS number | Name | Mol. Weight | Mol. Formula | Smile Notation | PDB Reference |
| 22541-53-3 | COBALT (II) ION | 58.933 | Co | [Co+2] | 1rxt |
| 14808-79-8 | SULFATE ION | 96.063 | O4 S | [O-]S([O-])(=O)=O | 1rxt |
| Mutational Information | ||
|---|---|---|
| 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/3112857/Q4Q5S8.pdb 2.0 356 = residues | | = | *| Ramachandran plot: 79.8% core 17.7% allow 1.9% gener 0.6% = disall | | = | *| All Ramachandrans: 31 labelled residues (out of 354) = | +| Chi1-chi2 plots: 1 labelled residues (out of 231) = | | = | | Main-chain params: 6 better 0 inside 0 worse = | | Side-chain params: 5 better 0 inside 0 worse = | | = | *| Residue properties: Max.deviation: 4.0 Bad contacts: = 18 | *| Bond len/angle: 6.8 Morris et al class: 1 = 1 3 | | = | | G-factors Dihedrals: -0.21 Covalent: -0.26 Overall: = -0.22 | | = | | M/c bond lengths: 98.9% within limits 1.1% highlighted = | | M/c bond angles: 91.1% within limits 8.9% highlighted = | | Planar groups: 100.0% within limits 0.0% highlighted = | | = | = +------------------------------------------------------------------------= ----+ + May be worth investigating further. * Worth investigating further. |