| Peptidyl-prolyl cis-trans isomerase [Q4QBK4] | |
|---|---|
| Systematic Name | LmjF.22.1430 [Leishmania major] |
| Gene Name | LMJF_22_1430 |
| Molecular Weight | 11839 Da |
| Protein Sequence Size | 111 |
| Function | |
| Charge | -3 |
| Isoelectric Point | 4.5743 pH |
| Description | Peptidyl-prolyl cis-trans isomerase. |
| Subcellular Location | N.A.[Predict] |
| E. C. Number | 5.2.1.8 |
| Sequence | >tr|Q4QBK4|Q4QBK4_LEIMA Peptidyl-prolyl cis-trans isomerase - Leishmania major PSDAVVMDKIIEGDGKTIPRSGSVVTLDYIGYLEDGSKFDSTLERGKPFVFRVGCGEVIK GWDAGIIQMSKGERSKLTMPPTLAYGGTGFPGLIPPNATIVFEVTLLDVA |
| DNA Sequence | >LmjF22.1430 |||fk506-binding protein 1-like protein|Leishmania major|chr 22|||Manual ATGCCCAGCG ACGCAGTGGT GATGGATAAG ATTATCGAGG GCGATGGCAA GACGATTCCTCGATCTGGCA GTGTTGTGAC ACTAGACTAT ATTGGTTATC TGGAGGACGG AAGCAAGTTCGACTCAACGC TGGAGCGCGG GAAGCCTTTC GTGTTTCGCG TTGGGTGCGG TGAGGTGATCAAGGGCTGGG ACGCGGGTAT TATTCAGATG TCCAAGGGCG AGCGTAGCAA GCTGACGATGCCGCCGACTC TCGCCTACGG CGGCACAGGG TTTCCGGGGC TCATCCCCCC CAACGCGACCATTGTGTTTG AGGTAACGCT GCTCGATGTA GCGTAG |
| Peptidyl-prolyl cis-trans isomerase Q4QBK4] | |
|---|---|
| Metabolite Information | |
| Molecular Function | FK506 binding; peptidyl-prolyl cis-trans isomerase activity |
| Biochemical Pathway | protein folding |
| Regulatory Pathway | |
| KEGG Pathways | K01802 |
| Orthologs | ||||
| Homologs | GI | Percent Identity | Evalue | Score |
| Homo sapiens | FK506-binding protein 1A [Homo sapiens] | 54 | 5e-29 | 122 |
| DEG Information | ||||
| DEG Protein | DEG Organism | Percent Identity | Evalue | Bit Score |
| YDL195w component of the COPII coat of ER-golgi vesicles | Saccharomyces cerevisiae | 26% | 0.15 | 28.5 |
| Post Translational Modification | ||||
| PTM Type | PTM Sub Type | Score | Modification Site | Prosite ID |
| PDOC00426 | FKBP-type peptidyl-prolyl cis-trans isomerase profile | 30.368 | 23-111 | PS50059 |
| Acylation | N-myristoylation site | 23-28; | PS00008 | |
| Glycosylation | N-glycosylation site | 98-101; | PS00001 | |
| Phosphorylation | Casein kinase II phosphorylation site | 38-41; 42-45; 71-74; 106-109; | PS00006 | |
| Sulfation | Tyrosine sulfation site | 26-40; | PS00003 | |
| Peptidyl-prolyl cis-trans isomerase [Q4QBK4] | ||
|---|---|---|
| Model Information | ||
| Template PDB ID | 1yatA | |
| Percent Identity | 56% | |
| Target Region | 1-111 | |
| Template Region | 1-113 | |
| Domain Information | ||
|---|---|---|
| Domains | Start | End |
| Active Site Information | ||
|---|---|---|
| Residue | Active Site Number | Functional Part |
| ASP | 41 | Sidechain |
| ILE | 60 | Backbone amide |
| TYR | 86 | Sidechain |
| Co-Factor | |
|---|---|
| Metal | Description |
| Ligands | |||||
|---|---|---|---|---|---|
| CAS number | Name | Mol. Weight | Mol. Formula | Smile Notation | PDB Reference |
| 8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN | 804.018 | C44 H69 N O12 | O=C3C(=O)N1CCCCC1C(=O)OC(C(=C/C2CCC(O)C(OC)C2)/C)C(C)C(O)CC(=O)C(C=C(CC(CC(OC)C4OC3(O)C(C)CC4OC)C)C)C\C=C | 1yat | |
| 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/137977/Q4QBK4.pdb 2.0 111 = residues | | = | | Ramachandran plot: 97.7% core 2.3% allow 0.0% gener 0.0% = disall | | = | +| All Ramachandrans: 1 labelled residues (out of 109) = | | Chi1-chi2 plots: 0 labelled residues (out of 57) = | | = | | Main-chain params: 6 better 0 inside 0 worse = | | Side-chain params: 5 better 0 inside 0 worse = | | = | *| Residue properties: Max.deviation: 2.9 Bad contacts: = 0 | *| Bond len/angle: 5.3 Morris et al class: 1 = 1 3 | | = | | G-factors Dihedrals: -0.01 Covalent: -0.20 Overall: = -0.08 | | = | | M/c bond lengths: 99.1% within limits 0.9% highlighted = | | M/c bond angles: 92.3% within limits 7.7% highlighted = | | Planar groups: 100.0% within limits 0.0% highlighted = | | = | = +------------------------------------------------------------------------= ----+ + May be worth investigating further. * Worth investigating further. |