| Metallo-peptidase, Clan MA(E), Family M3 [Q4FYX2] | |
|---|---|
| Systematic Name | LMJ_0159 [Leishmania major] |
| Gene Name | |
| Molecular Weight | 76568 Da |
| Protein Sequence Size | 678 |
| Function | |
| Charge | |
| Isoelectric Point | pH |
| Description | Metallo-peptidase, Clan MA(E), Family M3. |
| Subcellular Location | N.A.[Predict] |
| E. C. Number | N.A. |
| Sequence | >tr|Q4FYX2|Q4FYX2_LEIMA Metallo-peptidase, Clan MA(E), Family M3 - Leishmania major SANPLLQQSPLQYQHPPFDQITMEHYAPAFEQGMAEQMAEIEAIKSNPDAPTLENTVVAL ERSGAQLKRARLVFQNLCSAHTNPEMQNLEQAYAPKFSVHTDKIYLDGALYNRIKAVWDE RASLAGEDLRLVEHYEREFRKAGAGLHDADKEKLKQVNERLATLESDFAKKVMGTRKTAS LVVDNVAELEGLSEDEIATAQMEAESLGHPGKYALIIVNTTQQPLLASLRSRETRRRLFE ASVQRAARGDENDTSAIIVEIAQLRLKKAKLLGRKCFAEWQLQNQMADPASAEALLRDMG NAAASKAKKEAADIKQMIREEGGDFELAPWDWRYYAERVRKQRYDLDENETKPYFELNNV LERGVFYTAAKLYGVTMRRRTDLPVYHPDVLSFEMFDCTGESLAIFCLDPYARASKRGGA WMTFYVRQSSLLGQKPVVYNVLNIVKPAEGKPTLLSRSDVTTLFHEFGHGLHGMLSNLKY STLSGTSVARDFLEFPSQINEHWAMYDAVLKNYALHYETKEPIPQALVDRMKAAETYGAG FHTIEVVKAAYLDLCWHLVAEETAFLPPAQMEEAAMRSFGVGMTEVPPRYHSGYFMHTFS GGYASNYYVYQWARVLDCDGFEWFLENGGLTRENGDHLRACVLSVGNSVDANVAYEKFAG RKANMKAFLRINGLLDE |
| DNA Sequence | |
| Metallo-peptidase, Clan MA(E), Family M3 Q4FYX2] | |
|---|---|
| Metabolite Information | |
| Molecular Function | |
| Biochemical Pathway | |
| Regulatory Pathway | |
| KEGG Pathways | K01284 |
| Orthologs | ||||
| Homologs | GI | Percent Identity | Evalue | Score |
| Homo sapiens | thimet oligopeptidase 1 [Homo sapiens] | 27 | 2e-47 | 188 |
| DEG Information | ||||
| DEG Protein | DEG Organism | Percent Identity | Evalue | Bit Score |
| ptrBa PROBABLE PROTEASE II PTRBA [FIRST PART] (OLIGOPEPTIDASE B) | Mycobacterium tuberculosis H37Rv | 40% | 2.3 | 28.5 |
| Post Translational Modification | ||||
| PTM Type | PTM Sub Type | Score | Modification Site | Prosite ID |
| PDOC00016 | Cell attachment sequence | 249-251 | PS00016 | |
| PDOC00129 | Neutral zinc metallopeptidases, zinc-binding region signature | 463-472; | PS00142 | |
| Acylation | N-myristoylation site | 109-114; 146-151; 175-180; 301-306; 365-370; 420-425; 474-479; 486-491; 581-586; 602-607; | PS00008 | |
| Amidation | Amidation site | 273-276; 660-663; | PS00009 | |
| Glycosylation | N-glycosylation site | 220-223; 253-256; 350-353; | PS00001 | |
| Phosphorylation | cAMP- and cGMP-dependent protein kinase phosphorylation site | 379-382; | PS00004 | |
| Phosphorylation | Casein kinase II phosphorylation site | 47-50; 83-86; 194-197; 457-460; | PS00006 | |
| Phosphorylation | Protein kinase C phosphorylation site | 102-104; 176-178; 229-231; 235-237; 377-379; 416-418; | PS00005 | |
| Phosphorylation | Tyrosine kinase phosphorylation site | 104-112; 379-387; | PS00007 | |
| Metallo-peptidase, Clan MA(E), Family M3 [Q4FYX2] | ||
|---|---|---|
| Model Information | ||
| Template PDB ID | 1y791 | |
| Percent Identity | 44% | |
| Target Region | 1-677 | |
| Template Region | 1-680 | |
| Domain Information | ||
|---|---|---|
| Domains | Start | End |
| Active Site Information | ||
|---|---|---|
| Residue | Active Site Number | Functional Part |
| GLU | 495 | Sidechain |
| TYR | 611 | Sidechain |
| Co-Factor | |
|---|---|
| Metal | Description |
| Zn | Binds 1 zinc ion |
| Ligands | |||||
|---|---|---|---|---|---|
| CAS number | Name | Mol. Weight | Mol. Formula | Smile Notation | PDB Reference |
| 87867-94-5 | GLYCINE | 75.067 | C2 H5 N O2 | O=C(O)CN | 1y79 |
| 05-06-6899 00:00:00 | LYSINE | 147.195 | C6 H15 N2 O2 | O=C(O)C(N)CCCC[NH3+] | 1y79 |
| 23713-49-7 | ZINC ION | 65.409 | Zn | [Zn+2] | 1y79 |
| 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/1107085/Q4FYX2.pdb 2.0 677 = residues | | = | *| Ramachandran plot: 95.2% core 4.6% allow 0.0% gener 0.2% = disall | | = | +| All Ramachandrans: 6 labelled residues (out of 675) = | +| Chi1-chi2 plots: 9 labelled residues (out of 405) = | | = | | Main-chain params: 6 better 0 inside 0 worse = | | Side-chain params: 5 better 0 inside 0 worse = | | = | *| Residue properties: Max.deviation: 4.2 Bad contacts: = 4 | *| Bond len/angle: 8.3 Morris et al class: 1 = 1 2 | | = | | G-factors Dihedrals: 0.09 Covalent: -0.15 Overall: = 0.00 | | = | | M/c bond lengths: 99.6% within limits 0.4% highlighted = | | M/c bond angles: 93.6% within limits 6.4% highlighted = | | Planar groups: 100.0% within limits 0.0% highlighted = | | = | = +------------------------------------------------------------------------= ----+ + May be worth investigating further. * Worth investigating further. |