| Calmodulin, putative [Q4Q148] | |
|---|---|
| Systematic Name | LmjF.36.3675 [Leishmania major] |
| Gene Name | LMJF_36_3675 |
| Molecular Weight | 17306 Da |
| Protein Sequence Size | 155 |
| Function | |
| Charge | -13.5 |
| Isoelectric Point | 4.1 pH |
| Description | Calmodulin, putative. |
| Subcellular Location | N.A.[Predict] |
| E. C. Number | N.A. |
| Sequence | >tr|Q4Q148|Q4Q148_LEIMA Calmodulin, putative - Leishmania major ADLLSLQQITELKEAFSAFDADCDGSITVDDLEQVFSSIGHKVSRKKLQSILCEADLDSN GVIDFPEFLTLVATKLNDPEEKELEMRRAFRMYDLGNTGFITVPNLRFVMGRLGCFLTTE QAFDMISEADADGDGKLSFDDFRRVMTEGWGATP |
| DNA Sequence | >LmjF36.3675 |||calmodulin, putative|Leishmania major|chr 36|||Manual ATGGCGGACC TTCTTTCGCT TCAACAAATT ACTGAGCTTA AAGAAGCCTT TTCCGCATTTGATGCTGATT GTGATGGTAG CATTACTGTC GATGATTTGG AGCAAGTGTT CAGCTCCATTGGTCACAAAG TGTCCAGGAA AAAACTGCAG TCGATTTTGT GTGAAGCTGA CCTAGACTCTAACGGGGTAA TCGACTTCCC GGAGTTTCTC ACGCTTGTGG CCACTAAGCT GAATGACCCGGAGGAAAAAG AGCTTGAAAT GCGTCGTGCG TTTCGCATGT ACGACTTAGG AAACACTGGGTTCATCACTG TACCAAATCT GCGCTTTGTG ATGGGGCGCC TTGGCTGTTT CCTGACAACAGAACAGGCAT TCGACATGAT CAGTGAGGCG GATGCGGATG GTGACGGAAA GCTCAGCTTTGACGATTTTC GCCGTGTGAT GACTGAGGGA TGGGGCGCGA CGCCTTGA |
| Calmodulin, putative Q4Q148] | |
|---|---|
| Metabolite Information | biological process unknown |
| Molecular Function | |
| Biochemical Pathway | |
| Regulatory Pathway | |
| KEGG Pathways | |
| Orthologs | ||||
| Homologs | GI | Percent Identity | Evalue | Score |
| Homo sapiens | calmodulin 3 [Homo sapiens] | 47 | 1e-33 | 139 |
| DEG Information | ||||
| DEG Protein | DEG Organism | Percent Identity | Evalue | Bit Score |
| YBR109c calmodulin | Saccharomyces cerevisiae | 33% | 7e-20 | 90.5 |
| Post Translational Modification | ||||
| PTM Type | PTM Sub Type | Score | Modification Site | Prosite ID |
| PDOC00018 | EF-hand calcium-binding domain signature and profile | 21-33; 57-69; 131-143; | PS00018 | |
| Acylation | N-myristoylation site | 115-120; | PS00008 | |
| Phosphorylation | Casein kinase II phosphorylation site | 18-21; 29-32; 128-131; 139-142; | PS00006 | |
| Phosphorylation | Protein kinase C phosphorylation site | 45-47; | PS00005 | |
| Calmodulin, putative [Q4Q148] | ||
|---|---|---|
| Model Information | ||
| Template PDB ID | 2vasB | |
| Percent Identity | 48% | |
| Target Region | 1-149 | |
| Template Region | 4-141 | |
| 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 |
| 58-64-0 | ADENOSINE-5'-DIPHOSPHATE | 427.201 | C10 H15 N5 O10 P2 | O=P(O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O | 2vas |
| BERYLLIUM TRIFLUORIDE ION | 66.007 | Be F3 | F[Be-](F)F | 2vas | |
| 17787-72-3 | CALCIUM ION | 40.078 | Ca | [Ca+2] | 2vas |
| 7791-18-6 | MAGNESIUM ION | 24.305 | Mg | [Mg+2] | 2vas |
| 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/5315128/Q4Q148.pdb 2.0 149 = residues | | = | *| Ramachandran plot: 90.4% core 8.9% allow 0.0% gener 0.7% = disall | | = | +| All Ramachandrans: 3 labelled residues (out of 147) = | | Chi1-chi2 plots: 0 labelled residues (out of 89) = | | = | | 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: = 4 | +| Bond len/angle: 4.8 Morris et al class: 1 = 1 2 | | = | | G-factors Dihedrals: 0.20 Covalent: -0.03 Overall: = 0.11 | | = | | M/c bond lengths: 99.9% within limits 0.1% highlighted = | | M/c bond angles: 95.7% within limits 4.3% highlighted = | | Planar groups: 100.0% within limits 0.0% highlighted = | | = | = +------------------------------------------------------------------------= ----+ + May be worth investigating further. * Worth investigating further. |