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ATP synthase alpha chain [Q4QJF1]
Systematic NameLmjF.05.0500 [Leishmania major]
Gene NameLMJF_05_0500
Molecular Weight62549 Da
Protein Sequence Size574
Function
Charge30.5
Isoelectric Point10.12 pH
DescriptionATP synthase alpha chain.
Subcellular Locationproton-transporting ATP synthase complex, catalytic core F(1)[Predict]
E. C. Number N.A.
Sequence>tr|Q4QJF1|Q4QJF1_LEIMA ATP synthase alpha chain - Leishmania major.
RRFVAQYVAPAMGRLASTAAAGKSAAPGQKSFFKATEMIGYVHSIDGTIATLIPAPGNPG
VAYNTIIMIQVSPTTFAAGLVFNLEKDGRIGIILMDNITEVQSGQKVMATGKLLYIPVGA
GVLGKVVNPLGHEVPVGLLTRSRALLESEQTLGKVDAGAPNIVSRSPVNYNLLTGFKAVD
TMIPIGRGQRELIVGDRQTGKTSIAVSTIINQVRSNQQILSKNAVISIYVSIGQRCSNVA
RIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQ
AVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDV
TAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAMKAVAGKLKGIL
AEYRKLAADSVGGSQVQTVPMIRGARFVALFNQKNPSFFMNALVSLYACLNGYLDDVKVN
YAKLYEYLLVNKDLSVMYGTATNKFFYMYVQQLNYVIRFFTLNHPILNAEVEEMLKQHTH
LFLQHYQSKMNAIKTEKEIKALKNLLYSCKRAV
DNA Sequence>LmjF05.0500 |||ATPase alpha subunit|Leishmania major|chr 5|||Manual
ATGCGCCGCT TCGTGGCCCA GTACGTGGCG CCCGCCATGG GACGCCTTGC GTCGACGGCTGCTGCCGGCA AGTCTGCCGC GCCGGGCCAG AAGTCGTTCT TCAAGGCGAC GGAGATGATCGGCTACGTGC ACTCGATCGA CGGCACGATC GCGACGCTGA TCCCCGCGCC GGGCAACCCCGGCGTTGCGT ACAACACGAT CATCATGATC CAGGTGAGCC CGACGACGTT CGCGGCGGGGCTTGTGTTCA ACCTGGAGAA GGACGGCCGG ATAGGCATCA TCCTGATGGA TAACATCACGGAGGTGCAGT CCGGCCAGAA GGTGATGGCG ACGGGCAAGC TGCTGTACAT CCCCGTGGGTGCGGGCGTGC TGGGCAAGGT GGTGAACCCG CTGGGCCACG AGGTGCCGGT GGGGCTGTTGACGCGGTCGC GCGCGCTGCT GGAGAGCGAA CAGACGCTGG GCAAGGTGGA CGCCGGCGCGCCGAACATCG TGTCGCGCTC GCCAGTGAAC TACAACCTGC TGACCGGCTT CAAGGCAGTGGACACGATGA TCCCGATCGG GCGCGGCCAG CGCGAGCTGA TCGTGGGTGA CCGCCAGACCGGCAAGACGT CGATCGCGGT GTCGACGATC ATCAACCAGG TGCGCAGCAA CCAGCAGATCCTATCGAAGA ACGCGGTCAT CTCGATCTAC GTGTCGATCG GGCAGCGCTG CTCCAACGTCGCGCGCATCC ACCGCCTGCT GCGCTCGTAC GGCGCGCTGC GCTACACGAC GGTGATGGCTGCGACGGCCG CGGAGCCGGC GGGGCTGCAG TACCTCGCGC CGTACTCGGG CGTGACAATGGGCGAGTACT TCATGAACCG CGGCCGCCAC TGCCTGTGTG TGTACGACGA CCTGTCGAAGCAAGCCGTTG CGTACCGCCA GATCTCGCTG CTGCTGCGCC GCCCGCCGGG CCGCGAGGCGTACCCTGGTG ATGTGTTCTA CCTGCACTCG CGCCTGCTGG AGCGCGCCGC GATGCTGTCGCCTGGCAAGG GCGGCGGCTC CGTGACGGCG CTGCCGATCG TGGAGACGCT GTCGAACGATGTGACGGCGT ACATCGTCAC GAACGTCATC TCCATCACGG ACGGCCAGAT CTACCTGGACACGAAGCTGT TCACCGGCGG CCAGCGCCCG GCCGTGAACA TCGGCCTGTC CGTGTCGCGCGTCGGCTCGT CCGCGCAGAA CGTGGCGATG AAGGCGGTGG CCGGCAAGCT GAAGGGCATCCTCGCGGAGT ACCGCAAGCT GGCGGCGGAC TCGGTGGGCG GGAGCCAGGT GCAGACGGTGCCGATGATCC GCGGCGCGCG CTTCGTCGCG CTGTTCAACC AGAAGAACCC GTCCTTCTTCATGAACGCGC TCGTGTCGCT GTACGCGTGC CTGAACGGGT ACCTGGACGA CGTGAAGGTGAACTACGCGA AGCTCTACGA GTACCTGCTG GTGAACAAGG ACCTGAGCGT GATGTACGGGACAGCGACGA ACAAGTTCTT CTACATGTAC GTGCAGCAGC TGAACTACGT GATCCGCTTCTTCACGCTGA ACCACCCGAT CCTGAACGCG GAGGTGGAGG AGATGCTGAA GCAGCACACGCACCTGTTCC TGCAGCACTA CCAGTCGAAG ATGAACGCGA TCAAGACGGA GAAGGAGATCAAGGCGCTCA AGAACCTGCT GTACTCATGC AAGCGCGCCG TCTAA
ATP synthase alpha chain Q4QJF1]
Metabolite Information
Molecular FunctionATP binding; hydrogen-transporting ATP synthase activity, rotational mechanism; hydrogen-transporting ATPase activity, rotational mechanism; hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
Biochemical PathwayATP biosynthesis; ATP synthesis coupled proton transport
Regulatory Pathway
KEGG PathwaysK02111
Orthologs
Homologs GI Percent Identity Evalue Score
Homo sapiensATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit precursor [Homo sapiens]521e-109392
DEG Information
DEG Protein DEG Organism Percent Identity Evalue Bit Score
atpA ATP synthase subunit AMycobacterium tuberculosis H37Rv48%1e-103370
Post Translational Modification
PTM Type PTM Sub Type Score Modification Site Prosite ID
PDOC00137ATP synthase alpha and beta subunits signature390-399; PS00152
PDOC00017ATP/GTP-binding site motif A (P-loop)196-203; PS00017
AcylationN-myristoylation site48-53; 61-66; 80-85; 234-239; 277-282; 345-350; 346-351; 387-392; 395-400; 500-505; PS00008
GlycosylationN-glycosylation site98-101; PS00001
PhosphorylationCasein kinase II phosphorylation site262-265; 279-282; 371-374; 556-559; PS00006
PhosphorylationProtein kinase C phosphorylation site111-113; 200-202; 503-505; 556-558; 569-571; PS00005
PhosphorylationTyrosine kinase phosphorylation site35-42; PS00007
ATP synthase alpha chain [Q4QJF1]
Model Information
Template PDB ID2qe7C
Percent Identity52%
Target Region29-574
Template Region27-474
Domain Information
Domains Start End
Active Site Information
Residue Active Site Number Functional Part
LYS174Unknown
GLN207Unknown
ARG208Unknown (LYS 201 In Template)
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/402825/Q4QJF1.pdb 2.0 546 = residues | | = | *| Ramachandran plot: 87.7% core 9.2% allow 2.5% gener 0.6% = disall | | = | *| All Ramachandrans: 27 labelled residues (out of 544) = | +| Chi1-chi2 plots: 3 labelled residues (out of 310) = | | = | | Main-chain params: 6 better 0 inside 0 worse = | | Side-chain params: 5 better 0 inside 0 worse = | | = | *| Residue properties: Max.deviation: 4.0 Bad contacts: = 10 | *| Bond len/angle: 6.7 Morris et al class: 1 = 1 2 | +| 1 cis-peptides = | | G-factors Dihedrals: -0.07 Covalent: -0.25 Overall: = -0.13 | | = | | M/c bond lengths: 99.4% within limits 0.6% highlighted = | | M/c bond angles: 92.2% within limits 7.8% 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