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Vacuolar ATP synthase subunit B, putative [Q4Q821]
Systematic NameLmjF.28.2430 [Leishmania major]
Gene NameLMJF_28_2430
Molecular Weight55519 Da
Protein Sequence Size495
Function Noncatalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells
Charge-6
Isoelectric Point5.5451 pH
DescriptionVacuolar ATP synthase subunit B, putative (EC 3.6.3.14).
Subcellular Locationcytoplasm; lysosomal hydrogen-translocating V-type ATPase complex; proton-transporting two-sector ATPase complex[Predict]
E. C. Number 3.6.3.14
Sequence>tr|Q4Q821|Q4Q821_LEIMA Vacuolar ATP synthase subunit B, putative (EC 3.6.3.14) - Leishmania major
GRDEEHVRVLSKQELLATHIKELNESYSVKPHLEYTTIRAVNGPLVILEDVRKPTFAEIV
NIELADGTARRGQVLEVDGTKAVVQVFEGTSGIDVVRSKCEFTGKVMELGVSEDMLGRIF
NGSGIPIDNGPPVLPEQFRSIEGIPINPRARVYPEEMIQTGISSIDVMTSISRGQKIPLF
SGAGLPHNEIAAQIVRQAGLVKREGKTEDFCVVFAAMGVNQETARFFRTEFEQNGSMEKT
VLFLNLANDPTIERIVTPRLALTTAEYLAYDCGKHVLVILTDMSSYADALREVSAAREEV
PGRRGFPGYMYTNLACIYERAGRVLGRAGSITQIPILSMPNDDITHPIPDLTGYITEGQI
YVDRQLHNRQLYPPINILPSLSRLMKNAIGEGMTRKDHSGVSNQMYAAYAISRDILAMKA
VVGEEALSSEDLLYLEFLDKFEHKFICQGFYETRDIFQSLDLCWELLRTFPKSMLNKIDM
KTRDEFYDRHPGRK
DNA Sequence>LmjF28.2430 |||vacuolar ATP synthase subunit B, putative|Leishmania major|chr 28|||Manual
ATGGGCCGCG ATGAGGAACA TGTTCGCGTG CTGTCGAAGC AGGAGCTGCT CGCCACGCACATCAAGGAGC TCAACGAGAG CTACTCGGTG AAACCGCATC TTGAGTACAC GACGATTCGTGCCGTCAACG GTCCCCTCGT CATCCTGGAG GATGTGCGCA AGCCGACCTT CGCCGAGATCGTCAACATCG AGCTGGCCGA CGGCACCGCG CGTCGTGGCC AGGTGCTCGA GGTGGATGGCACCAAGGCCG TCGTGCAGGT CTTCGAGGGC ACCTCCGGTA TCGATGTCGT GCGCTCCAAGTGCGAGTTTA CCGGCAAGGT TATGGAGCTC GGCGTAAGCG AGGACATGCT GGGCCGCATCTTCAACGGTT CCGGCATCCC GATCGATAAC GGCCCACCGG TGCTGCCGGA GCAGTTCCGCAGTATCGAGG GTATTCCAAT CAACCCGCGT GCGCGTGTCT ACCCGGAGGA GATGATCCAGACGGGTATCT CGTCCATCGA CGTCATGACC TCCATCTCGC GCGGCCAGAA GATTCCGCTCTTCTCCGGCG CTGGGCTGCC GCACAATGAA ATCGCCGCGC AGATTGTGCG TCAGGCCGGTCTCGTGAAGC GCGAGGGCAA GACGGAGGAC TTCTGTGTCG TCTTCGCCGC CATGGGTGTGAACCAGGAGA CGGCCCGCTT TTTCCGCACA GAGTTCGAGC AGAACGGCTC GATGGAGAAGACCGTCCTCT TCCTGAACCT GGCGAACGAC CCGACCATTG AGCGCATCGT GACGCCGCGTCTGGCCCTCA CTACTGCTGA GTACCTCGCC TACGACTGCG GTAAGCACGT GCTCGTCATTCTGACCGACA TGTCCTCGTA CGCCGATGCC CTGCGTGAGG TGTCCGCCGC CCGTGAGGAGGTGCCCGGCC GCCGAGGTTT CCCTGGCTAC ATGTACACGA ATCTGGCGTG CATCTACGAGCGTGCAGGCC GTGTGCTGGG CCGCGCCGGC TCCATCACCC AGATCCCGAT TCTGTCCATGCCGAACGATG ATATCACCCA CCCCATTCCA GATCTCACCG GGTACATTAC AGAAGGCCAGATCTACGTGG ACCGCCAGCT GCACAACCGG CAGCTGTACC CGCCGATTAA TATTCTGCCGTCGCTGTCGC GTCTGATGAA GAACGCCATT GGTGAGGGCA TGACCCGCAA GGATCACAGCGGCGTGAGCA ACCAAATGTA CGCCGCCTAC GCCATCAGTC GTGATATTCT CGCCATGAAGGCCGTCGTTG GCGAGGAGGC GTTGAGTAGC GAGGATCTGC TGTACCTCGA GTTTCTCGACAAGTTCGAGC ACAAGTTCAT CTGCCAAGGC TTCTACGAAA CACGCGATAT CTTCCAAAGCCTTGACCTGT GCTGGGAACT GCTGCGCACG TTCCCCAAGA GCATGCTGAA CAAGATCGACATGAAGACCC GTGATGAGTT TTATGACCGC CACCCGGGCC GCAAGTAA
Vacuolar ATP synthase subunit B, putative Q4Q821]
Metabolite Information
Molecular FunctionATP binding; hydrogen-exporting ATPase activity, phosphorylative mechanism; hydrogen-transporting ATP synthase activity, rotational mechanism; hydrogen-transporting ATPase activity, rotational mechanism
Biochemical PathwayATP biosynthesis; ATP hydrolysis coupled proton transport; ATP synthesis coupled proton transport; energy coupled proton transport, against electrochemical gradient
Regulatory Pathway
KEGG PathwaysK02147
Orthologs
Homologs GI Percent Identity Evalue Score
Homo sapiensATPase, H+ transporting, lysosomal 56/58kD, V1 subunit B, isoform 2 [Homo sapiens]730695
DEG Information
DEG Protein DEG Organism Percent Identity Evalue Bit Score
HP1132 ATP synthase F1, subunit beta (atpD)Helicobacter pylori27%1e-32135
Post Translational Modification
PTM Type PTM Sub Type Score Modification Site Prosite ID
PDOC00137ATP synthase alpha and beta subunits signature373-382; PS00152
AcylationN-myristoylation site184-189; PS00008
AmidationAmidation site301-304; 491-494; PS00009
GlycosylationN-glycosylation site25-28; 121-124; 234-237; PS00001
PhosphorylationcAMP- and cGMP-dependent protein kinase phosphorylation site53-56; PS00004
PhosphorylationCasein kinase II phosphorylation site12-15; 56-59; 91-94; 98-101; 163-166; 229-232; 263-266; 285-288; 394-397; 428-431; 482-485; PS00006
PhosphorylationProtein kinase C phosphorylation site29-31; 38-40; 68-70; 103-105; 223-225; 257-259; 394-396; PS00005
PhosphorylationTyrosine kinase phosphorylation site481-487; PS00007
Vacuolar ATP synthase subunit B, putative [Q4Q821]
Model Information
Template PDB ID2c61B
Percent Identity56%
Target Region44-495
Template Region13-425
Domain Information
Domains Start End
Active Site Information
Residue Active Site Number Functional Part
ARG341Unknown
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/2309040/Q4Q821.pdb 2.0 452 = residues | | = | *| Ramachandran plot: 91.0% core 6.6% allow 1.8% gener 0.5% = disall | | = | +| All Ramachandrans: 13 labelled residues (out of 450) = | +| Chi1-chi2 plots: 7 labelled residues (out of 275) = | | = | | Main-chain params: 6 better 0 inside 0 worse = | | Side-chain params: 5 better 0 inside 0 worse = | | = | *| Residue properties: Max.deviation: 4.9 Bad contacts: = 11 | *| Bond len/angle: 18.3 Morris et al class: 1 = 1 2 | +| 2 cis-peptides = | +| G-factors Dihedrals: -0.01 Covalent: -0.52 Overall: = -0.20 | | = | *| M/c bond lengths: 98.0% within limits 2.0% highlighted 10 off = graph | *| M/c bond angles: 92.5% within limits 7.5% highlighted 7 off = graph | | 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