Tryparedoxin peroxidase [Q4QF80] | |
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Systematic Name | LmjF.15.1040 [Leishmania major] |
Gene Name | TRYP |
Molecular Weight | 22099 Da |
Protein Sequence Size | 199 |
Function | |
Charge | 0.5 |
Isoelectric Point | 6.7596 pH |
Description | Tryparedoxin peroxidase. |
Subcellular Location | N.A.[Predict] |
E. C. Number | N.A. |
Sequence | >tr|Q4QF80|Q4QF80_LEIMA Tryparedoxin peroxidase - Leishmania major. SCGNAKINSPAPSFEEVALMPNGSFKKISLSSYKGKWVVLFFYPLDFSFVCPTEVIAFSD SVSRFNELNCEVLACSIDSEYAHLQWTLQDRKKGGLGTMAIPMLADKTKSIARSYGVLEE SQGVAYRGLFIIDPHGMLRQITVNDMPVGRSVEEVLRLLEAFQFVEKHGEVCPANWKKGA PTMKPEPNASVEGYFSKL |
DNA Sequence | >LmjF15.1040 |TRYP1||tryparedoxin peroxidase|Leishmania major|chr 15|||Manual ATGTCCTGCG GTAACGCCAA GATCAACTCT CCCGCGCCGT CCTTCGAGGA GGTGGCGCTCATGCCCAACG GCAGCTTCAA GAAGATCAGC CTCTCCTCCT ACAAGGGCAA GTGGGTCGTGCTCTTCTTCT ACCCGCTCGA CTTTAGCTTC GTGTGCCCGA CAGAGGTCAT CGCGTTCTCCGACAGCGTGA GTCGCTTCAA CGAGCTCAAC TGCGAGGTCC TCGCGTGCTC GATAGACAGCGAGTACGCGC ACCTGCAGTG GACGCTGCAG GACCGCAAGA AGGGCGGCCT CGGGACCATGGCGATCCCAA TGCTAGCCGA CAAGACCAAG AGCATCGCTC GTTCCTACGG CGTGCTGGAGGAGAGCCAGG GCGTGGCCTA CCGCGGTCTC TTCATCATCG ACCCCCATGG CATGCTGCGTCAGATCACCG TCAATGACAT GCCGGTGGGC CGCAGCGTGG AGGAGGTTCT ACGCCTGCTGGAGGCTTTTC AGTTCGTGGA GAAGCACGGC GAGGTGTGCC CCGCGAACTG GAAGAAGGGCGCCCCCACGA TGAAGCCGGA ACCGAATGCG TCTGTCGAGG GATACTTCAG CAAGCTCTGA |
Tryparedoxin peroxidase Q4QF80] | |
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Metabolite Information | |
Molecular Function | |
Biochemical Pathway | |
Regulatory Pathway | |
KEGG Pathways | K03386 |
Orthologs | ||||
Homologs | GI | Percent Identity | Evalue | Score |
Homo sapiens | peroxiredoxin 1 [Homo sapiens] | 61 | 3e-71 | 264 |
DEG Information | ||||
DEG Protein | DEG Organism | Percent Identity | Evalue | Bit Score |
YOL066c DRAP deaminase | Saccharomyces cerevisiae | 32% | 2.3 | 26.2 |
Post Translational Modification | ||||
PTM Type | PTM Sub Type | Score | Modification Site | Prosite ID |
PDOC00595 | Formate--tetrahydrofolate ligase signatures | 23-26; 189-192; | PS00722 | |
PDOC00299 | Microbodies C-terminal targeting signal | 197-199; | PS00342 | |
Acylation | N-myristoylation site | 95-100; | PS00008 | |
Glycosylation | N-glycosylation site | 23-26; 189-192; | PS00001 | |
Phosphorylation | cAMP- and cGMP-dependent protein kinase phosphorylation site | 27-30; | PS00004 | |
Phosphorylation | Casein kinase II phosphorylation site | 14-17; 88-91; 143-146; 152-155; | PS00006 | |
Phosphorylation | Protein kinase C phosphorylation site | 25-27; 33-35; 183-185; | PS00005 |
Tryparedoxin peroxidase [Q4QF80] | ||
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Model Information | ||
Template PDB ID | 1e2yJ | |
Percent Identity | 76% | |
Target Region | 1-170 | |
Template Region | 5-166 |
Domain Information | ||
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Domains | Start | End |
Active Site Information | ||
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Residue | Active Site Number | Functional Part |
Co-Factor | |
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Metal | Description |
Ligands | |||||
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CAS number | Name | Mol. Weight | Mol. Formula | Smile Notation | PDB Reference |
16887-00-6 | CHLORIDE ION | 35.453 | Cl | [Cl-] | 1e2y |
Mutational Information | ||
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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/481878/Q4QF80.pdb 2.0 170 = residues | | = | | Ramachandran plot: 93.3% core 6.7% allow 0.0% gener 0.0% = disall | | = | +| All Ramachandrans: 3 labelled residues (out of 168) = | *| Chi1-chi2 plots: 3 labelled residues (out of 99) = | | = | | Main-chain params: 6 better 0 inside 0 worse = | | Side-chain params: 5 better 0 inside 0 worse = | | = | +| Residue properties: Max.deviation: 3.6 Bad contacts: = 1 | +| Bond len/angle: 4.8 Morris et al class: 1 = 1 2 | | = | | G-factors Dihedrals: 0.01 Covalent: -0.12 Overall: = -0.04 | | = | | M/c bond lengths: 99.6% within limits 0.4% highlighted = | | M/c bond angles: 94.2% within limits 5.8% highlighted = | | Planar groups: 100.0% within limits 0.0% highlighted = | | = | = +------------------------------------------------------------------------= ----+ + May be worth investigating further. * Worth investigating further. |