LeishBase: Leishmania Structural Database
header
Home List of Proteins How to Visualize Structures Download Contact Us
Glucose-regulated protein 78, putative [Q4Q8E6]
Systematic NameLmjF.28.1200 [Leishmania major]
Gene NameLMJF_28_1200
Molecular Weight71941 Da
Protein Sequence Size658
Function
Charge-17
Isoelectric Point4.7866 pH
DescriptionGlucose-regulated protein 78, putative.
Subcellular Locationendoplasmic reticulum[Predict]
E. C. Number N.A.
Sequence>tr|Q4Q8E6|Q4Q8E6_LEIMA Glucose-regulated protein 78, putative - Leishmania major
TRKDNLTLMAVCLVSAILVVSAAAVPDGSGKVESPCIGVDLGTTYSVAGVWQKGEVHIVT
NEMGNRITPSVVAFTDAERLVGDGAKNQLPQNPENTIYAIKRLIGRKYADPTVQNDKKLL
SYHIVADKTGKPLVQVTVKGQQKRFTPEEVSAMVLQKMKEISETFLGEKVKNAVVTVPAY
FNDAQRQATKDSGKIAGLNVVRIINEPTAAAIAYGLNKAGEKNILVFDLGGGTFDVSLLT
IDEGFFEVVATNGDTHLGGEDFDNNMMKFFVDGLKRKQNVDISNDQKALARLRKACEAAK
RQLSSHPEARVEVDSLVEGYDFSEKITRAKFEELNMALFKNTLVPVQKVLEDAKLKKSDI
DEIVLVGGSTRIPKVQQLIKDFFSGKEPNKGINPDEAVAYGAAVQAAVLTGESEVGGKVV
LVDVIPLSLGIETVGGVMTKLIERNTQIPTKKSQIFSTYQDNQPSVLIQVFEGERGMTKD
NRLLGKFDLSGIPPAPRGVPQIEVAFDVDENSILQVTASDKSSGKREEITITNDKGRLSE
EEIERMVREAAEFEDEDRKVRERVEAKNSLESIAYSLRNQINDKDKLGDKLDADDKKAIE
EAVKDALDFVDENPNADREEFEAARTKLQSVTNPIIQKVYQGTAGSGAEEADAMDDL
DNA Sequence>LmjF28.1200 |||glucose-regulated protein 78, putative|Leishmania major|chr 28|||Manual
ATGACGCGGA AAGACAACCT AACACTCATG GCCGTGTGCC TCGTGTCCGC CATACTGGTGGTGTCGGCTG CGGCTGTCCC TGATGGCAGC GGCAAGGTGG AGTCGCCGTG CATCGGCGTTGACCTGGGTA CGACGTACTC GGTTGCCGGT GTTTGGCAGA AGGGTGAGGT CCACATTGTCACGAACGAGA TGGGCAACCG CATCACCCCG TCTGTGGTCG CCTTCACCGA CGCGGAGCGTCTGGTCGGCG ATGGCGCGAA GAATCAGTTG CCGCAGAACC CGGAGAACAC CATCTACGCCATCAAGCGTC TCATCGGCCG CAAATACGCG GACCCCACCG TTCAGAATGA CAAGAAGCTGCTCTCGTACC ATATTGTGGC GGACAAAACT GGCAAGCCGC TCGTGCAGGT GACGGTGAAGGGCCAGCAGA AGCGGTTCAC GCCTGAGGAG GTGAGCGCCA TGGTGCTACA GAAGATGAAAGAGATCTCTG AGACCTTCCT CGGCGAGAAG GTGAAGAACG CCGTCGTAAC GGTGCCAGCGTACTTTAATG ATGCGCAGCG CCAGGCAACG AAGGACTCCG GTAAGATCGC CGGCCTTAACGTCGTCCGCA TCATCAACGA GCCCACAGCG GCGGCCATAG CGTACGGGCT CAACAAAGCTGGCGAGAAGA ACATCCTGGT CTTCGACCTC GGTGGCGGCA CGTTCGATGT GTCGCTGCTGACAATCGACG AGGGTTTCTT CGAGGTGGTC GCGACGAACG GTGATACCCA CCTCGGTGGTGAGGACTTCG ATAACAACAT GATGAAGTTT TTCGTGGACG GCCTCAAGCG CAAGCAGAACGTCGACATCT CGAATGACCA GAAGGCCCTG GCCCGTCTGC GCAAGGCATG CGAGGCTGCGAAGCGTCAGT TGTCGTCCCA CCCGGAGGCG CGCGTAGAGG TGGACAGCCT TGTCGAGGGCTACGACTTCA GCGAGAAGAT CACGCGGGCC AAGTTCGAGG AGCTGAACAT GGCCCTCTTCAAGAACACGC TGGTGCCTGT GCAGAAAGTG CTAGAGGATG CAAAGCTGAA GAAGAGTGACATCGACGAGA TCGTCCTGGT CGGCGGCTCG ACCCGAATTC CGAAGGTGCA ACAGCTCATCAAGGACTTCT TCAGCGGCAA GGAGCCGAAC AAGGGCATCA ACCCCGACGA GGCCGTCGCGTACGGCGCTG CGGTGCAGGC GGCCGTGCTG ACGGGCGAGA GCGAGGTGGG CGGCAAGGTCGTGCTCGTTG ATGTGATTCC CTTGTCTCTC GGCATCGAGA CCGTTGGCGG AGTCATGACGAAGCTGATCG AGCGCAACAC GCAGATCCCG ACCAAGAAGA GCCAGATCTT CTCCACCTATCAGGACAACC AACCCAGCGT GCTGATTCAG GTCTTCGAGG GCGAGCGCGG GATGACGAAAGACAACCGCT TGCTTGGCAA GTTCGACCTC TCCGGCATCC CGCCGGCGCC GCGCGGCGTGCCGCAGATCG AGGTCGCCTT CGATGTGGAC GAGAACAGCA TCCTGCAGGT GACGGCGAGCGACAAGTCCT CTGGAAAGCG GGAGGAGATC ACCATCACAA ATGACAAGGG CCGCCTCAGCGAGGAGGAGA TCGAGCGCAT GGTGCGCGAG GCTGCCGAGT TCGAGGATGA GGACCGTAAGGTGCGCGAGC GTGTCGAAGC GAAGAACTCG CTAGAGAGCA TCGCGTACTC CCTTCGCAACCAGATCAACG ACAAGGACAA GCTTGGTGAC AAGCTCGACG CGGACGACAA GAAGGCGATCGAGGAGGCTG TGAAGGATGC CCTCGACTTT GTCGACGAGA ACCCCAATGC AGACCGTGAGGAGTTCGAGG CAGCACGCAC GAAGCTGCAG AGTGTGACGA ACCCCATCAT TCAAAAGGTGTACCAGGGCA CCGCCGGCTC TGGTGCAGAA GAGGCGGACG CGATGGATGA CTTGTAG
Glucose-regulated protein 78, putative Q4Q8E6]
Metabolite Information
Molecular FunctionATP binding; molecular function unknown
Biochemical PathwaySRP-dependent cotranslational protein targeting to membrane; protein folding
Regulatory Pathway
KEGG PathwaysK09490
Orthologs
Homologs GI Percent Identity Evalue Score
Homo sapiensheat shock 70kDa protein 5 (glucose-regulated protein, 78kDa) [Homo sapiens]590718
DEG Information
DEG Protein DEG Organism Percent Identity Evalue Bit Score
YJL034w nuclear fusion proteinSaccharomyces cerevisiae57%0687
Post Translational Modification
PTM Type PTM Sub Type Score Modification Site Prosite ID
PDOC00269Heat shock hsp70 proteins family signatures40-47; PS00297
PDOC00269Heat shock hsp70 proteins family signatures227-240; PS00329
PDOC00269Heat shock hsp70 proteins family signatures364-378; PS01036
AcylationN-myristoylation site39-44; 43-48; 216-221; 436-441; 643-648; 648-653; PS00008
AmidationAmidation site105-108; 524-527; PS00009
GlycosylationN-glycosylation site6-9; PS00001
PhosphorylationcAMP- and cGMP-dependent protein kinase phosphorylation site144-147; PS00004
PhosphorylationCasein kinase II phosphorylation site2-5; 76-79; 147-150; 241-244; 252-255; 306-309; 316-319; 359-362; 385-388; 459-462; 518-521; 540-543; 647-650; PS00006
PhosphorylationProtein kinase C phosphorylation site2-4; 30-32; 130-132; 138-140; 193-195; 324-326; 370-372; 385-387; 451-453; 520-522; 524-526; 577-579; PS00005
PhosphorylationTyrosine kinase phosphorylation site568-576; PS00007
SulfationTyrosine sulfation site314-328; PS00003
Glucose-regulated protein 78, putative [Q4Q8E6]
Model Information
Template PDB ID1yuwA
Percent Identity63%
Target Region33-586
Template Region2-554
Domain Information
Domains Start End
Active Site Information
Residue Active Site Number Functional Part
LYS70Sidechain
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/626418/Q4Q8E6.pdb 2.0 551 = residues | | = | *| Ramachandran plot: 89.9% core 8.4% allow 1.2% gener 0.4% = disall | | = | *| All Ramachandrans: 21 labelled residues (out of 549) = | +| Chi1-chi2 plots: 3 labelled residues (out of 328) = | | = | | Main-chain params: 6 better 0 inside 0 worse = | | Side-chain params: 5 better 0 inside 0 worse = | | = | *| Residue properties: Max.deviation: 6.9 Bad contacts: = 4 | *| Bond len/angle: 7.2 Morris et al class: 1 = 1 2 | | = | | G-factors Dihedrals: 0.01 Covalent: -0.15 Overall: = -0.04 | | = | | 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.
Overlapped Structure Procheck Summary
LeishBase: Leishmania Structural Database