| Peptidyl-prolyl cis-trans isomerase, putative [Q4Q255] | |
|---|---|
| Systematic Name | LmjF.36.0230 [Leishmania major] |
| Gene Name | LMJF_36_0230 |
| Molecular Weight | 11983 Da |
| Protein Sequence Size | 109 |
| Function | |
| Charge | 0 |
| Isoelectric Point | 6.5134 pH |
| Description | Peptidyl-prolyl cis-trans isomerase, putative. |
| Subcellular Location | N.A.[Predict] |
| E. C. Number | 5.2.1.8 |
| Sequence | >tr|Q4Q255|Q4Q255_LEIMA Peptidyl-prolyl cis-trans isomerase, putative - Leishmania major. GVIRTVMKAGSGATPKPGQTITVHCTGYLADGKKKFWSTHDDKNPFTFNVGVGQVIRGWD EGMMQMQLGETAELLMTADYAYGDRGFPAWNIPSNAALLFEIELLKIQ |
| DNA Sequence | >LmjF36.0230 |||peptidyl-prolyl cis-trans isomerase, putative|Leishmania major|chr 36|||Manual ATGGGCGTCA TTCGTACGGT CATGAAGGCG GGCAGTGGCG CCACCCCAAA GCCCGGGCAGACGATCACCG TGCACTGCAC CGGGTACTTA GCGGATGGGA AGAAGAAGTT CTGGTCCACCCATGATGACA AGAACCCGTT CACCTTTAAC GTGGGTGTCG GTCAGGTAAT TCGCGGCTGGGATGAGGGCA TGATGCAGAT GCAGCTCGGG GAGACGGCAG AGTTGCTCAT GACGGCCGACTACGCGTACG GTGATCGCGG CTTTCCTGCC TGGAACATCC CGTCAAACGC CGCACTGCTGTTCGAGATTG AGCTGCTGAA AATCCAGTAG |
| Peptidyl-prolyl cis-trans isomerase, putative Q4Q255] | |
|---|---|
| Metabolite Information | protein folding |
| Molecular Function | |
| Biochemical Pathway | |
| Regulatory Pathway | |
| KEGG Pathways | K01802 |
| Orthologs | ||||
| Homologs | GI | Percent Identity | Evalue | Score |
| Homo sapiens | FK506-binding protein 1A [Homo sapiens] | 50 | 2e-22 | 100 |
| DEG Information | ||||
| DEG Protein | DEG Organism | Percent Identity | Evalue | Bit Score |
| drm Phosphopentomutase | Staphylococcus aureus | 45% | 0.56 | 26.6 |
| Post Translational Modification | ||||
| PTM Type | PTM Sub Type | Score | Modification Site | Prosite ID |
| PDOC00426 | FKBP-type peptidyl-prolyl cis-trans isomerase profile | 25.611 | 19-109 | PS50059 |
| Acylation | N-myristoylation site | 2-7; 19-24; | PS00008 | |
| Amidation | Amidation site | 32-35; | PS00009 | |
| Phosphorylation | Casein kinase II phosphorylation site | 39-42; 40-43; | PS00006 | |
| Phosphorylation | Protein kinase C phosphorylation site | 15-17; | PS00005 | |
| Peptidyl-prolyl cis-trans isomerase, putative [Q4Q255] | ||
|---|---|---|
| Model Information | ||
| Template PDB ID | 1fklA | |
| Percent Identity | 50% | |
| Target Region | 1-109 | |
| Template Region | 1-107 | |
| Domain Information | ||
|---|---|---|
| Domains | Start | End |
| Active Site Information | ||
|---|---|---|
| Residue | Active Site Number | Functional Part |
| TRP | 38 | Sidechain (ASP 37 In Template) |
| ILE | 57 | Backbone amide |
| TYR | 83 | Sidechain |
| Co-Factor | |
|---|---|
| Metal | Description |
| Ligands | |||||
|---|---|---|---|---|---|
| CAS number | Name | Mol. Weight | Mol. Formula | Smile Notation | PDB Reference |
| RAPAMYCIN IMMUNOSUPPRESSANT DRUG | 914.172 | C51 H79 N O13 | O=C2C(C)CC(C=CC=CC=C(C)C(OC)CC4OC(O)(C(=O)C(=O)N3C(C(=O)OC(C(C)CC1CCC(O)C(OC)C1)CC(=O)C(C=C(C)C(O)C2OC)C)CCCC3)C(CC4)C)C | 1fkl | |
| 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/997005/Q4Q255.pdb 2.0 109 = residues | | = | | Ramachandran plot: 91.0% core 9.0% allow 0.0% gener 0.0% = disall | | = | +| All Ramachandrans: 3 labelled residues (out of 107) = | +| Chi1-chi2 plots: 1 labelled residues (out of 63) = | | = | | Main-chain params: 6 better 0 inside 0 worse = | | Side-chain params: 5 better 0 inside 0 worse = | | = | | Residue properties: Max.deviation: 2.8 Bad contacts: = 1 | +| Bond len/angle: 4.4 Morris et al class: 1 = 1 2 | | = | | G-factors Dihedrals: -0.08 Covalent: -0.21 Overall: = -0.12 | | = | | M/c bond lengths: 98.9% within limits 1.1% highlighted = | | M/c bond angles: 92.6% within limits 7.4% highlighted = | | Planar groups: 100.0% within limits 0.0% highlighted = | | = | = +------------------------------------------------------------------------= ----+ + May be worth investigating further. * Worth investigating further. |