| Farnesyltransferase, putative [Q4Q5W4] | |
|---|---|
| Systematic Name | LmjF.31.2940 [Leishmania major] |
| Gene Name | LMJF_31_2940 |
| Molecular Weight | 47121 Da |
| Protein Sequence Size | 414 |
| Function | |
| Charge | -3.5 |
| Isoelectric Point | 5.7 pH |
| Description | Farnesyltransferase, putative (EC 2.5.1.21). |
| Subcellular Location | integral to membrane[Predict] |
| E. C. Number | 2.5.1.21 |
| Sequence | >tr|Q4Q5W4|Q4Q5W4_LEIMA Farnesyltransferase, putative (EC 2.5.1.21) - Leishmania major. GFFSDSVAMMRVKWQMRSVKIQVPPEETDLRFCYDIMNDVSRSFAVVVAQLADQQLRDAI CIFYLVLRALDTLEDDMSVPVDVKLKELPKFHTHTSDMSWCMSGVGEGRERELLAKYPCV SREFKKLKKEYQDVIANICERMANGMCEFLKRPVVTKDDYNQYCHYVAGLVGHGLTQLFA RCGFEDPSLDDDLTSSNHMGLFLQKTNIIRDYYEDIREEPPRMFWPKEIWGTYVTELKEL KSESNNAAAVQCLNAMVADALVHVPYIVDYLSALRDPSVFRFCAIPQVMAIATLKEVYNN PDTFQVKVKVSRPESCRIMLKATTLYSSLSMFRDYCVELQEKLDMQDASSVSIANSLAAA IERIDLQLKKCQDVSYTRSLLARYPGLGGQFLLTVMDTVAGFFGGRKEIAGHA |
| DNA Sequence | >LmjF31.2940 |||farnesyltransferase, putative|Leishmania major|chr 31|||Manual ATGGGGTTCT TCTCGGATTC GGTAGCGATG ATGCGTGTAA AGTGGCAGAT GCGCTCTGTGAAGATTCAGG TGCCGCCGGA AGAGACGGAC TTACGCTTCT GCTACGATAT CATGAACGACGTCTCTCGTT CCTTCGCGGT TGTCGTGGCG CAGCTCGCAG ACCAGCAGCT CCGTGATGCCATCTGCATCT TCTACCTTGT CCTCCGTGCG CTGGATACCT TGGAGGATGA CATGAGCGTTCCGGTAGACG TTAAGCTGAA GGAGCTTCCG AAGTTCCACA CGCACACGAG CGACATGAGCTGGTGCATGA GCGGCGTCGG TGAGGGACGC GAGCGCGAAC TGCTGGCGAA ATACCCGTGCGTCTCGCGCG AATTCAAGAA GCTGAAGAAG GAGTATCAGG ACGTCATCGC AAATATCTGCGAGCGCATGG CAAACGGCAT GTGCGAGTTC TTGAAGCGCC CAGTGGTCAC AAAGGACGACTACAACCAGT ACTGCCACTA TGTCGCCGGC CTCGTCGGCC ACGGCCTCAC CCAGCTCTTCGCCCGCTGCG GCTTCGAGGA CCCGAGCCTG GACGACGATC TCACCAGTTC CAACCACATGGGTCTCTTCC TGCAGAAGAC AAACATCATC CGCGACTACT ACGAGGACAT CCGAGAGGAGCCGCCGCGGA TGTTCTGGCC GAAGGAGATC TGGGGCACGT ACGTGACGGA GCTGAAGGAGCTGAAAAGTG AGTCGAACAA TGCGGCAGCG GTGCAGTGCC TGAACGCCAT GGTGGCCGACGCTCTCGTGC ATGTCCCCTA CATCGTGGAC TACCTCTCCG CTCTGCGCGA CCCGTCCGTGTTCCGCTTTT GCGCCATTCC TCAGGTGATG GCCATTGCGA CGCTGAAAGA GGTGTACAACAACCCCGACA CGTTCCAGGT CAAGGTGAAG GTGTCACGGC CGGAGTCGTG CCGTATCATGCTCAAGGCCA CGACCCTCTA CAGCTCCCTC AGCATGTTCC GCGACTACTG CGTGGAGCTGCAGGAGAAGC TAGACATGCA AGACGCCAGC TCCGTATCGA TCGCCAACTC GCTTGCGGCGGCGATTGAGC GGATCGACCT GCAGCTGAAG AAGTGCCAGG ACGTCTCCTA CACCCGCAGCCTCCTCGCCC GCTACCCAGG CCTCGGTGGT CAGTTCCTTC TCACCGTCAT GGATACCGTCGCTGGTTTCT TTGGTGGCCG CAAGGAGATT GCCGGCCACG CGTAA |
| Farnesyltransferase, putative Q4Q5W4] | |
|---|---|
| Metabolite Information | biosynthesis; lipid biosynthesis |
| Molecular Function | |
| Biochemical Pathway | |
| Regulatory Pathway | |
| KEGG Pathways | K00801 |
| Orthologs | ||||
| Homologs | GI | Percent Identity | Evalue | Score |
| Homo sapiens | farnesyl-diphosphate farnesyltransferase 1 [Homo sapiens] | 46 | 5e-81 | 298 |
| DEG Information | ||||
| DEG Protein | DEG Organism | Percent Identity | Evalue | Bit Score |
| YHR190w farnesyl-diphosphate farnesyltransferase | Saccharomyces cerevisiae | 41% | 3e-70 | 259 |
| Post Translational Modification | ||||
| PTM Type | PTM Sub Type | Score | Modification Site | Prosite ID |
| PDOC00299 | Microbodies C-terminal targeting signal | 412-414; | PS00342 | |
| PDOC00802 | Squalene and phytoene synthases signatures | 164-179; | PS01044 | |
| PDOC00802 | Squalene and phytoene synthases signatures | 200-227; | PS01045 | |
| Acylation | N-myristoylation site | 105-110; 232-237; | PS00008 | |
| Amidation | Amidation site | 405-408; | PS00009 | |
| Phosphorylation | Casein kinase II phosphorylation site | 73-76; 157-160; 189-192; 294-297; 312-315; 395-398; | PS00006 | |
| Phosphorylation | Protein kinase C phosphorylation site | 19-21; 294-296; 316-318; | PS00005 | |
| Phosphorylation | Tyrosine kinase phosphorylation site | 370-377; | PS00007 | |
| Farnesyltransferase, putative [Q4Q5W4] | ||
|---|---|---|
| Model Information | ||
| Template PDB ID | 1ezfC | |
| Percent Identity | 47% | |
| Target Region | 29-365 | |
| Template Region | 38-320 | |
| 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 |
| N-{2-[TRANS-7-CHLORO-1-(2,2-DIMETHYL-PROPYL) - 5-NAPHTHALEN-1-YL-2-OXO-1,2,3,5-TETRAHYDRO- BENZO[E] [1,4]OXAZEPIN-3-YL]-ACETYL}-ASPARTIC ACID | 567.029 | C30 H31 Cl N2 O7 | O=C(O)CC(C(=O)O)NC(=O)CC1OC(c2cc(Cl)ccc2N(C1=O)CC(C)(C)C)c4c3ccccc3ccc4 | 1ezf | |
| 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/351380/Q4Q5W4.pdb 2.0 337 = residues | | = | *| Ramachandran plot: 95.5% core 3.8% allow 0.3% gener 0.3% = disall | | = | +| All Ramachandrans: 6 labelled residues (out of 335) = | +| Chi1-chi2 plots: 3 labelled residues (out of 210) = | | = | | Main-chain params: 6 better 0 inside 0 worse = | | Side-chain params: 5 better 0 inside 0 worse = | | = | *| Residue properties: Max.deviation: 16.4 Bad contacts: = 6 | *| Bond len/angle: 21.9 Morris et al class: 1 = 1 2 | | = | | G-factors Dihedrals: 0.19 Covalent: -0.33 Overall: = -0.01 | | = | *| M/c bond lengths: 98.1% within limits 1.9% highlighted 5 off = graph | *| M/c bond angles: 94.8% within limits 5.2% highlighted 5 off = graph | | Planar groups: 100.0% within limits 0.0% highlighted = | | = | = +------------------------------------------------------------------------= ----+ + May be worth investigating further. * Worth investigating further. |