| Vacuolar ATP synthase catalytic subunit a, putative [Q4Q2H7] | |
|---|---|
| Systematic Name | LmjF.34.3670 [Leishmania major] |
| Gene Name | LMJF_34_3670 |
| Molecular Weight | 67736 Da |
| Protein Sequence Size | 610 |
| Function | Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells |
| Charge | -13 |
| Isoelectric Point | 4.9 pH |
| Description | Vacuolar ATP synthase catalytic subunit a, putative (EC 3.6.3.14). |
| Subcellular Location | lysosomal hydrogen-translocating V-type ATPase complex; proton-transporting two-sector ATPase complex[Predict] |
| E. C. Number | 3.6.3.14 |
| Sequence | >tr|Q4Q2H7|Q4Q2H7_LEIMA Vacuolar ATP synthase catalytic subunit a, putative (EC 3.6.3.14) - Leishmania major. ARDQHAFESEQQMGSVKAVSGPVVIAENMSGSAMYELVQVGSFRLVGEIIRLEGDTATIQ VYEETDGLTVGDPVYCTGKPLSLELGPGIMSEIFDGIQRPLDTIYQMVQNVFIPKGVQVR ALNAQRQWDFTPSVKVGDIVTGGDVLGFVAENSLMNNHSIMVPPNMQGRVVSVQPGGNYT LDDDVVDIEYNGKRKSLRLMQRWPVRTPRPVALKESGNHPLLTGQRVLDALFPSVQGGTC SIPGAFGCGKTVISQALSKYSNSDCVIYVGCGERGNEMAEVLMDFPTLTTVIDGREESIM KRTCLVANTSNMPVAAREASIYTGITLAEYYRDMGKHIAMMADSTSRWAEALREISGRLA EMPADGGYPAYLSARLASFYERAGLVTCIGGPKRQGSVTIVGAVSPPGGDFSDPVTSATL SIVQVFWGLEKRLAQRKHFPSVNWLISYSKYLNALEPFFNTFDSDYMRLRAVVSEILQRE EELQEIVQLVGKDSLSESDKIILEVAKVIREEFLQQNAFTPYDKFCPLYKTCWMLRNIVT FYEEAQRVVAESAGDHKITWNYIREKIPTIYTGLTEMKFRDPIEGEEANTDYFKKQNEEI ISSFNSLLQ |
| DNA Sequence | >LmjF34.3670 |||vacuolar ATP synthase catalytic subunit a, putative|Leishmania major|chr 34|||Manual ATGGCCCGCG ATCAGCATGC GTTCGAGTCA GAGCAGCAGA TGGGCTCCGT CAAGGCTGTTTCCGGCCCTG TCGTGATCGC CGAAAACATG AGCGGTAGCG CGATGTACGA GCTTGTGCAGGTCGGATCGT TCCGCCTTGT CGGCGAGATC ATCCGCCTGG AGGGCGACAC GGCCACGATTCAGGTGTACG AGGAGACGGA CGGTCTGACT GTCGGTGATC CGGTCTACTG TACCGGCAAGCCTCTGTCGC TCGAGCTGGG CCCTGGCATC ATGTCGGAGA TCTTTGACGG CATTCAGCGTCCGCTCGACA CCATTTACCA GATGGTGCAG AACGTATTCA TCCCGAAAGG CGTACAGGTGCGCGCGCTCA ACGCGCAGAG GCAGTGGGAC TTCACCCCTT CTGTGAAGGT GGGCGACATAGTCACGGGCG GTGACGTCCT GGGCTTCGTC GCTGAGAACT CGCTCATGAA CAACCACAGCATTATGGTGC CGCCGAACAT GCAGGGCCGT GTGGTATCGG TCCAGCCTGG TGGCAACTACACGCTGGATG ATGACGTGGT GGATATCGAG TACAACGGCA AGAGGAAGTC CCTGCGTCTGATGCAGCGCT GGCCCGTGCG CACGCCGCGC CCGGTGGCTT TGAAAGAGTC AGGCAACCACCCCCTCCTGA CCGGCCAGCG TGTGCTGGAC GCGCTGTTCC CCTCCGTGCA GGGTGGCACGTGCTCGATCC CCGGCGCGTT CGGCTGTGGC AAGACTGTCA TTAGTCAGGC CCTCTCCAAGTACTCCAACT CCGACTGCGT CATCTATGTC GGCTGCGGCG AGCGCGGTAA TGAGATGGCTGAGGTGCTCA TGGATTTCCC AACTCTGACG ACCGTGATCG ATGGTCGCGA GGAGTCCATCATGAAGCGCA CCTGCCTCGT GGCAAACACT TCGAACATGC CAGTCGCAGC CCGCGAGGCCTCTATTTACA CCGGCATCAC CCTGGCCGAG TACTACCGTG ATATGGGCAA GCATATTGCCATGATGGCCG ACTCGACATC TCGCTGGGCC GAGGCGCTTC GTGAGATTTC CGGTCGTCTGGCGGAGATGC CAGCCGATGG TGGCTACCCT GCCTACCTCA GCGCTCGTCT CGCCTCCTTCTACGAGCGCG CCGGCCTCGT CACCTGCATC GGCGGGCCGA AGCGCCAGGG CTCCGTCACGATCGTCGGTG CTGTGTCTCC GCCGGGCGGT GACTTCTCTG ATCCCGTCAC ATCCGCCACTCTCAGCATTG TGCAGGTCTT CTGGGGTCTG GAGAAGCGCC TCGCCCAGCG CAAGCACTTCCCGTCCGTCA ACTGGCTCAT TTCCTACTCC AAATACCTGA ACGCGCTGGA GCCCTTCTTCAACACCTTCG ACTCCGACTA CATGCGCCTG CGCGCCGTCG TGTCGGAGAT TCTGCAGCGCGAGGAGGAGC TGCAGGAGAT TGTGCAGCTG GTGGGTAAGG ACTCCCTTTC CGAGTCCGACAAGATCATTC TCGAGGTGGC AAAGGTGATT CGTGAGGAGT TCCTTCAGCA GAACGCCTTCACCCCGTACG ACAAGTTTTG TCCGCTGTAC AAGACATGCT GGATGCTGCG CAACATCGTCACCTTCTACG AGGAGGCCCA GCGCGTCGTT GCCGAGTCTG CCGGCGACCA CAAGATCACGTGGAACTACA TCCGTGAGAA GATCCCGACC ATCTACACGG GCCTGACCGA AATGAAGTTCCGCGACCCCA TCGAGGGTGA GGAGGCGAAC ACGGACTACT TCAAGAAGCA GAACGAGGAGATCATCAGCT CCTTCAACTC GCTGCTACAG TAG |
| Vacuolar ATP synthase catalytic subunit a, putative Q4Q2H7] | |
|---|---|
| Metabolite Information | ATP biosynthesis; ATP synthesis coupled proton transport |
| Molecular Function | |
| Biochemical Pathway | |
| Regulatory Pathway | |
| KEGG Pathways | K02145 |
| Orthologs | ||||
| Homologs | GI | Percent Identity | Evalue | Score |
| Homo sapiens | ATPase, H+ transporting, lysosomal 70kD, V1 subunit A, isoform 1 [Homo sapiens] | 63 | 0 | 759 |
| DEG Information | ||||
| DEG Protein | DEG Organism | Percent Identity | Evalue | Bit Score |
| atpD Proton-translocating ATPase, F1 sector, beta-subunit | Streptococcus pneumoniae | 27% | 7e-27 | 116 |
| Post Translational Modification | ||||
| PTM Type | PTM Sub Type | Score | Modification Site | Prosite ID |
| PDOC00137 | ATP synthase alpha and beta subunits signature | 441-450; | PS00152 | |
| PDOC00017 | ATP/GTP-binding site motif A (P-loop) | 245-252; | PS00017 | |
| PDOC00595 | Formate--tetrahydrofolate ligase signatures | 29-32; 158-161; 179-182; 309-312; | PS00722 | |
| Acylation | N-myristoylation site | 15-20; 68-73; 177-182; 238-243; 245-250; 248-253; 276-281; 325-330; 367-372; 385-390; 409-414; | PS00008 | |
| Amidation | Amidation site | 192-195; | PS00009 | |
| Glycosylation | N-glycosylation site | 29-32; 158-161; 179-182; 309-312; | PS00001 | |
| Phosphorylation | cAMP- and cGMP-dependent protein kinase phosphorylation site | 194-197; | PS00004 | |
| Phosphorylation | Casein kinase II phosphorylation site | 70-73; 142-145; 181-184; 262-265; 291-294; 327-330; 379-382; 495-498; 497-500; 521-524; 541-544; 553-556; | PS00006 | |
| Phosphorylation | Protein kinase C phosphorylation site | 16-18; 43-45; 78-80; 134-136; 197-199; 208-210; 346-348; 357-359; 374-376; 499-501; | PS00005 | |
| Phosphorylation | Tyrosine kinase phosphorylation site | 100-106; | PS00007 | |
| Sulfation | Tyrosine sulfation site | 56-70; | PS00003 | |
| Vacuolar ATP synthase catalytic subunit a, putative [Q4Q2H7] | ||
|---|---|---|
| Model Information | ||
| Template PDB ID | 1vdzA | |
| Percent Identity | 47% | |
| Target Region | 72-602 | |
| Template Region | 62-513 | |
| Domain Information | ||
|---|---|---|
| Domains | Start | End |
| Active Site Information | ||
|---|---|---|
| Residue | Active Site Number | Functional Part |
| LYS | 180 | Unknown |
| GLU | 203 | Unknown |
| ARG | 204 | Unknown |
| Co-Factor | |
|---|---|
| Metal | Description |
| Ligands | |||||
|---|---|---|---|---|---|
| CAS number | Name | Mol. Weight | Mol. Formula | Smile Notation | PDB Reference |
| (4S)-2-METHYL-2,4-PENTANEDIOL | 118.174 | C6 H14 O2 | OC(C)CC(O)(C)C | 1vdz | |
| Mutational Information | ||
|---|---|---|
| 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/495444/Q4Q2H7.pdb 2.0 529 = residues | | = | *| Ramachandran plot: 89.1% core 9.4% allow 1.1% gener 0.4% = disall | | = | *| All Ramachandrans: 34 labelled residues (out of 527) = | +| Chi1-chi2 plots: 7 labelled residues (out of 305) = | | = | | Main-chain params: 6 better 0 inside 0 worse = | | Side-chain params: 5 better 0 inside 0 worse = | | = | *| Residue properties: Max.deviation: 7.7 Bad contacts: = 10 | *| Bond len/angle: 6.3 Morris et al class: 1 = 1 2 | +| 2 cis-peptides = | | G-factors Dihedrals: -0.02 Covalent: -0.16 Overall: = -0.07 | | = | | M/c bond lengths: 99.0% within limits 1.0% highlighted = | *| M/c bond angles: 94.1% within limits 5.9% highlighted 1 off = graph | | Planar groups: 100.0% within limits 0.0% highlighted = | | = | = +------------------------------------------------------------------------= ----+ + May be worth investigating further. * Worth investigating further. |