| Peptidyl-prolyl cis-trans isomerase [Q4Q424] | |
|---|---|
| Systematic Name | LmjF.33.1630 [Leishmania major] |
| Gene Name | CYP4 |
| Molecular Weight | 24091 Da |
| Protein Sequence Size | 220 |
| Function | PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides |
| Charge | 8.5 |
| Isoelectric Point | 9.282 pH |
| Description | Peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8). |
| Subcellular Location | N.A.[Predict] |
| E. C. Number | 5.2.1.8 |
| Sequence | >tr|Q4Q424|Q4Q424_LEIMA Peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8) - Leishmania major. HSEALVISYFLRSCSLKVSLPPKMLRRTFLSAERRIPFYPINSNNPIVFFDISIGSQPAG RVEMELFKDVVPKTAENFRALCTGEKGVGRSGKPLWFKGSRFHRVIPQFMCQGGDFTAGN GTGGESIYGHKFPDESFAGRAGRHFGPGTLSMANAGPNTNGSQFFICTAPTDWLDGKHVV FGQVTKGYDVIMKVETQGSQSGATRQPITVTDCGEIKQE |
| DNA Sequence | >LmjF33.1630 |||cyclophilin, putative|Leishmania major|chr 33|||Manual ATGCACTCAG AAGCACTGGT GATATCCTAT TTCTTGAGAT CTTGTTCACT GAAAGTGTCCCTCCCTCCAA AAATGCTTCG CCGTACCTTT CTAAGCGCTG AGCGCAGGAT TCCGTTCTACCCGATCAACT CGAATAACCC CATCGTGTTC TTCGACATCT CTATCGGATC GCAGCCGGCAGGGCGTGTCG AGATGGAGCT CTTCAAGGAC GTCGTGCCGA AGACGGCCGA GAACTTCCGCGCGCTTTGCA CCGGTGAGAA GGGTGTTGGC CGCTCTGGCA AGCCTCTCTG GTTCAAGGGAAGCCGTTTCC ACCGCGTTAT ACCACAGTTC ATGTGCCAGG GTGGCGATTT CACTGCCGGCAACGGCACCG GTGGCGAGTC CATCTACGGT CACAAGTTTC CTGATGAGTC CTTTGCCGGACGTGCCGGAA GGCATTTTGG CCCGGGCACG CTGTCAATGG CTAATGCCGG CCCCAACACAAACGGCTCTC AATTCTTCAT CTGCACCGCT CCCACCGACT GGCTGGACGG GAAGCATGTCGTGTTCGGCC AGGTCACCAA GGGCTATGAC GTCATCATGA AGGTGGAGAC TCAGGGCAGCCAATCTGGTG CTACCCGCCA GCCCATCACG GTCACTGACT GTGGTGAGAT CAAGCAAGAGTAG |
| Peptidyl-prolyl cis-trans isomerase Q4Q424] | |
|---|---|
| Metabolite Information | protein folding |
| Molecular Function | |
| Biochemical Pathway | |
| Regulatory Pathway | |
| KEGG Pathways | K01802 |
| Orthologs | ||||
| Homologs | GI | Percent Identity | Evalue | Score |
| Homo sapiens | peptidylprolyl isomerase F precursor [Homo sapiens] | 53 | 3e-56 | 215 |
| DEG Information | ||||
| DEG Protein | DEG Organism | Percent Identity | Evalue | Bit Score |
| ppiB PROBABLE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE B PPIB (CYCLOPHILIN) (PPIASE) (ROTAMASE) (PEPTIDYLPROLYL ISOMERASE) | Mycobacterium tuberculosis H37Rv | 29% | 0.00004 | 42.4 |
| Post Translational Modification | ||||
| PTM Type | PTM Sub Type | Score | Modification Site | Prosite ID |
| PDOC00154 | Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature & profile | 98-115; | PS00170 | |
| PDOC00154 | Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature & profile | 43.672 | 50-216 | PS50072 |
| Acylation | N-myristoylation site | 56-61; 88-93; 114-119; 120-125; 199-204; | PS00008 | |
| Glycosylation | N-glycosylation site | 121-124; 161-164; | PS00001 | |
| Phosphorylation | Casein kinase II phosphorylation site | 123-126; 210-213; | PS00006 | |
| Phosphorylation | Protein kinase C phosphorylation site | 16-18; 92-94; | PS00005 | |
| Peptidyl-prolyl cis-trans isomerase [Q4Q424] | ||
|---|---|---|
| Model Information | ||
| Template PDB ID | 2hqjA | |
| Percent Identity | 67% | |
| Target Region | 45-220 | |
| Template Region | 2-179 | |
| Domain Information | ||
|---|---|---|
| Domains | Start | End |
| Active Site Information | ||
|---|---|---|
| Residue | Active Site Number | Functional Part |
| ARG | 61 | Sidechain |
| PHE | 66 | Sidechain |
| GLN | 69 | Sidechain |
| ASN | 111 | Sidechain |
| PHE | 122 | Sidechain |
| LEU | 131 | Sidechain |
| Co-Factor | |
|---|---|
| Metal | Description |
| Ligands | |||||
|---|---|---|---|---|---|
| CAS number | Name | Mol. Weight | Mol. Formula | Smile Notation | PDB Reference |
| 14265-44-2 | PHOSPHATE ION | 94.971 | O4 P | [O-]P([O-])([O-])=O | 2hqj |
| 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/5215101/Q4Q424.pdb 2.0 176 = residues | | = | +| Ramachandran plot: 89.9% core 10.1% allow 0.0% gener 0.0% = disall | | = | +| All Ramachandrans: 4 labelled residues (out of 174) = | +| Chi1-chi2 plots: 1 labelled residues (out of 91) = | | = | | Main-chain params: 6 better 0 inside 0 worse = | | Side-chain params: 5 better 0 inside 0 worse = | | = | | Residue properties: Max.deviation: 2.4 Bad contacts: = 0 | +| Bond len/angle: 4.3 Morris et al class: 1 = 1 2 | | = | | G-factors Dihedrals: 0.05 Covalent: -0.17 Overall: = -0.03 | | = | | 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. |