| AP-Endonuclease [O15922] | |
|---|---|
| Systematic Name | LmjF.16.0680 [Leishmania major] |
| Gene Name | LMAP |
| Molecular Weight | 43121 Da |
| Protein Sequence Size | 447 |
| Function | |
| Charge | 9 |
| Isoelectric Point | 8.6824 pH |
| Description | AP-Endonuclease (Apurinic/apyrimidinic endonuclease-redox protein (Ap-endonuclease) (EC 4.2.99.18)). |
| Subcellular Location | nucleus[Predict] |
| E. C. Number | 4.2.99.18 |
| Sequence | >tr|O15922|O15922_LEIMA AP-Endonuclease (Apurinic/apyrimidinic endonuclease-redox protein (Ap- endonuclease) (EC 4.2.99.18)) - Leishmania major. ASKRCRQCSGDSASSSTSSLSPSELPPSKKAAGGQRVTAEVEVAPITTDATSATVTAAGG AKKKATTGSPARRTSSAAKITNGDAGELIRTAEALAALNAKKSEKEIWSDVVPFVRRTTD SDFDPSRMYKFITWNVAGLRGLLKKNASALRAFMEAEKPDVLCLQETKLNVDEADANATL GVVDGYSFVDHPCAFKRGYSGTRTYMKNSTTVKGLHARCTRGFALPSEPQADAAAGSRVL VEGAGDEEGRVLTTFLSPDPDSASSSSRIALVNTYVANSGMGLTRLPYRVQSFDPSMREY LHRLDTWATENAAVPSAAAMGSGSSPHGFIWAGDLNVAERDYDRYYAGTFKSMQECSGFA PEERMSFRETMQRTNSVDIFRQLYPQAGPVYSFWSQRINGRPRNLGWRLDYFVVSSRLAS YVVDCFPMPTVMGSDHCPFQMWMRHP |
| DNA Sequence | >LmjF16.0680 |||apurinic/apyrimidinic endonuclease-redox protein|Leishmania major|chr 16|||Manual ATGGCCTCGA AGCGATGCCG GCAGTGCAGC GGCGACTCTG CGTCCTCATC GACCTCGTCGTTGTCACCAT CCGAGCTGCC GCCCTCGAAG AAGGCGGCTG GCGGTCAGCG AGTCACGGCGGAAGTTGAAG TGGCGCCCAT CACAACGGAC GCTACGTCTG CCACTGTCAC GGCTGCAGGCGGCGCGAAGA AAAAGGCGAC GACGGGGAGC CCCGCACGTC GCACGAGCAG CGCGGCAAAGATCACGAACG GTGACGCCGG TGAGCTGATC CGCACCGCGG AGGCCCTCGC CGCTCTCAACGCGAAGAAGT CCGAGAAGGA GATTTGGTCT GACGTGGTGC CGTTCGTGCG CAGGACCACGGACAGCGACT TCGACCCGTC GCGCATGTAC AAGTTCATTA CGTGGAACGT AGCCGGCCTACGCGGGCTGC TGAAGAAGAA CGCCTCGGCG CTGAGAGCGT TCATGGAGGC CGAGAAGCCGGATGTTCTGT GCCTGCAGGA GACCAAGCTG AACGTCGACG AGGCCGATGC CAATGCGACCCTCGGCGTGG TGGACGGCTA CTCCTTTGTG GACCACCCGT GCGCCTTCAA GCGGGGCTACTCGGGCACCC GCACCTACAT GAAGAACAGC ACCACTGTGA AAGGGCTGCA CGCACGGTGCACTCGTGGCT TTGCATTGCC GTCCGAACCA CAGGCAGACG CGGCCGCCGG CTCACGGGTGCTGGTAGAAG GCGCTGGCGA CGAGGAGGGC CGCGTGTTGA CTACATTCCT CTCTCCGGATCCGGACTCTG CATCGTCGTC GTCGCGCATC GCCCTCGTGA ACACCTACGT GGCGAACAGCGGCATGGGAC TGACGCGGCT GCCTTACCGC GTCCAATCCT TTGATCCCAG CATGAGGGAGTACCTTCACC GGCTGGACAC CTGGGCCACA GAAAATGCCG CCGTCCCGTC GGCGGCGGCGATGGGCAGCG GCAGCAGCCC GCACGGCTTT ATCTGGGCTG GCGACCTCAA CGTGGCGGAGCGGGACTACG ACCGTTACTA CGCCGGTACG TTCAAGTCAA TGCAGGAGTG CAGCGGCTTTGCACCTGAGG AGCGGATGTC TTTTCGCGAG ACGATGCAGC GGACGAATTC GGTGGACATCTTTCGCCAGC TCTACCCCCA GGCAGGCCCG GTCTACTCCT TCTGGTCTCA GCGTATCAACGGTCGCCCGA GAAACTTGGG GTGGCGCTTG GACTACTTCG TTGTTTCCTC GCGACTTGCATCGTACGTCG TGGACTGCTT CCCGATGCCG ACGGTGATGG GCAGCGATCA CTGTCCGTTCCAGATGTGGA TGCGACACCC ATGA |
| AP-Endonuclease O15922] | |
|---|---|
| Metabolite Information | |
| Molecular Function | molecular function unknown; nuclease activity |
| Biochemical Pathway | DNA repair |
| Regulatory Pathway | |
| KEGG Pathways | K01142 |
| Orthologs | ||||
| Homologs | GI | Percent Identity | Evalue | Score |
| Homo sapiens | APEX nuclease [Homo sapiens] | 30 | 1e-30 | 131 |
| DEG Information | ||||
| DEG Protein | DEG Organism | Percent Identity | Evalue | Bit Score |
| xthA exodeoxyribonuclease III | Haemophilus influenzae | 23% | 0.0000001 | 52 |
| Post Translational Modification | ||||
| PTM Type | PTM Sub Type | Score | Modification Site | Prosite ID |
| PDOC00598 | AP endonucleases family 1 signatures | 160-169 | PS00726 | |
| PDOC00598 | AP endonucleases family 1 signatures | 405-416 | PS00728 | |
| PDOC00595 | Formate--tetrahydrofolate ligase signatures | 147-150; 178-181; 209-212 | PS00722 | |
| Acylation | N-myristoylation site | 35-40; 182-187; 281-286; 349-354 | PS00008 | |
| Glycosylation | N-glycosylation site | 147-150; 178-181; 209-212 | PS00001 | |
| Phosphorylation | cAMP- and cGMP-dependent protein kinase phosphorylation site | 64-67; 73-76; 117-120 | PS00004 | |
| Phosphorylation | Casein kinase II phosphorylation site | 22-25; 82-85; 104-107; 120-123; 122-125; 188-191; 297-300; 353-356; 367-370 | PS00006 | |
| Phosphorylation | Protein kinase C phosphorylation site | 3-5; 29-31; 104-106; 212-214; 267-269; 297-299; 350-352; 367-369; 396-398; 416-418 | PS00005 | |
| Phosphorylation | Tyrosine kinase phosphorylation site | 341-347 | PS00007 | |
| AP-Endonuclease [O15922] | ||
|---|---|---|
| Model Information | ||
| Template PDB ID | 2j63B | |
| Percent Identity | 84% | |
| Target Region | 90-447 | |
| Template Region | 90-333 | |
| Domain Information | ||
|---|---|---|
| Domains | Start | End |
| Active Site Information | ||
|---|---|---|
| Residue | Active Site Number | Functional Part |
| TYR | 187 | Sidechain |
| ASP | 246 | Sidechain |
| ASP | 322 | Sidechain |
| HIS | 348 | Sidechain |
| Co-Factor | |
|---|---|
| Metal | Description |
| Ligands | |||||
|---|---|---|---|---|---|
| CAS number | Name | Mol. Weight | Mol. Formula | Smile Notation | PDB Reference |
| 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/2701713/O15922.pdb 2.0 358 = residues | | = | *| Ramachandran plot: 92.0% core 7.3% allow 0.3% gener 0.3% = disall | | = | +| All Ramachandrans: 6 labelled residues (out of 356) = | +| Chi1-chi2 plots: 3 labelled residues (out of 193) = | | = | | 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: 5.7 Morris et al class: 1 = 1 2 | +| 1 cis-peptides = | | G-factors Dihedrals: -0.01 Covalent: -0.16 Overall: = -0.06 | | = | | M/c bond lengths: 99.0% within limits 1.0% highlighted = | | M/c bond angles: 93.4% within limits 6.6% highlighted = | | Planar groups: 100.0% within limits 0.0% highlighted = | | = | = +------------------------------------------------------------------------= ----+ + May be worth investigating further. * Worth investigating further. |