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Eukaryotic initiation factor 5a, putative [Q4QA21]
Systematic NameLmjF.25.0720 [Leishmania major]
Gene NameEIF5A2
Molecular Weight17812 Da
Protein Sequence Size166
FunctionThe precise role of eIF-5A in protein biosynthesis is not known but it functions by promoting the formation of the first peptide bond
Charge-8
Isoelectric Point4.6159 pH
DescriptionEukaryotic initiation factor 5a, putative.
Subcellular Locationcytoplasm[Predict]
E. C. Number N.A.
Sequence>tr|Q4QA21|Q4QA21_LEIMA Eukaryotic initiation factor 5a, putative - Leishmania major
SDEDHDFSHQGGGDNASKTYPLPAGALKKGGYVCINGRPCKVIDLSVSKTGKHGHAKVSI
VATDIFTGNRLEDQAPSTHNVEVPFVKTFTYSVLDIQPNEDSSLPSHLSLMDDEGESRED
LDMPPDAALAAQIKEQFDSGKEVLVVVVSAMGTEQVLQTKNAAEK
DNA Sequence>LmjF25.0720 |EIF5A1||eukaryotic initiation factor 5a, putative|Leishmania major|chr 25|||Manual
ATGTCTGACG AGGACCATGA CTTCTCGCAC CAGGGAGGTG GCGACAACGC GTCAAAGACGTATCCCTTGC CCGCTGGCGC CCTGAAGAAG GGTGGCTACG TGTGCATCAA CGGCCGTCCGTGCAAGGTGA TCGACCTGTC TGTGTCGAAG ACCGGCAAGC ACGGTCACGC TAAGGTGAGCATTGTCGCGA CCGACATTTT CACTGGAAAC CGCCTCGAGG ATCAGGCCCC GTCCACGCACAATGTAGAGG TGCCGTTTGT GAAGACCTTC ACATACAGCG TGTTGGATAT CCAACCCAACGAAGACTCCT CTCTTCCATC TCATTTGTCG CTGATGGACG ATGAGGGCGA GAGCCGCGAGGATCTCGATA TGCCCCCGGA CGCGGCCCTG GCAGCGCAAA TCAAGGAGCA GTTCGACTCCGGCAAGGAGG TGCTAGTTGT GGTTGTGTCT GCAATGGGCA CTGAGCAGGT GTTGCAGACGAAGAATGCTG CGGAGAAGTA G
Eukaryotic initiation factor 5a, putative Q4QA21]
Metabolite Information
Molecular Functionnucleic acid binding; translation initiation factor activity
Biochemical Pathwaytranslational initiation
Regulatory Pathway
KEGG PathwaysK03263
Orthologs
Homologs GI Percent Identity Evalue Score
Homo sapienseukaryotic translation initiation factor 5A [Homo sapiens]415e-31130
DEG Information
DEG Protein DEG Organism Percent Identity Evalue Bit Score
Post Translational Modification
PTM Type PTM Sub Type Score Modification Site Prosite ID
PDOC00274Eukaryotic initiation factor 5A hypusine signature51-58; PS00302
PDOC00595Formate--tetrahydrofolate ligase signatures16-19; PS00722
AcylationN-myristoylation site12-17; 13-18; 31-36; PS00008
GlycosylationN-glycosylation site16-19; PS00001
PhosphorylationCasein kinase II phosphorylation site2-5; 93-96; 110-113; 118-121; 140-143; PS00006
PhosphorylationProtein kinase C phosphorylation site51-53; 140-142; PS00005
Eukaryotic initiation factor 5a, putative [Q4QA21]
Model Information
Template PDB ID1xtdA
Percent Identity90%
Target Region16-166
Template Region24-149
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
Mutational Information
Residue Feature Description
Modeled Protein Template Structure
+----------<<< P R O C H E C K S U M = M A R Y >>>----------+ | = | | /var/www/html/Services/SAVES_3/jobs/2198215/Q4QA21.pdb 2.0 151 = residues | | = | +| Ramachandran plot: 95.4% core 3.8% allow 0.8% gener 0.0% = disall | | = | +| All Ramachandrans: 1 labelled residues (out of 149) = | +| Chi1-chi2 plots: 1 labelled residues (out of 80) = | | = | | Main-chain params: 6 better 0 inside 0 worse = | | Side-chain params: 5 better 0 inside 0 worse = | | = | *| Residue properties: Max.deviation: 2.0 Bad contacts: = 0 | *| Bond len/angle: 5.3 Morris et al class: 1 = 1 2 | | = | | G-factors Dihedrals: 0.06 Covalent: -0.13 Overall: = -0.01 | | = | | M/c bond lengths: 99.9% within limits 0.1% 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.
Overlapped Structure Procheck Summary
LeishBase: Leishmania Structural Database