| ATPase beta subunit, putative [Q4Q9X6] | |
|---|---|
| Systematic Name | LmjF.25.1170 [Leishmania major] |
| Gene Name | LMJF_25_1170 |
| Molecular Weight | 56349 Da |
| Protein Sequence Size | 525 |
| Function | |
| Charge | -11 |
| Isoelectric Point | 4.9235 pH |
| Description | ATPase beta subunit, putative. |
| Subcellular Location | hydrogen-translocating F-type ATPase complex; integral to membrane; proton-transporting ATP synthase complex, catalytic core F(1) (sensu Eukaryota); proton-transporting two-sector ATPase complex[Predict] |
| E. C. Number | 3.6.3.14 |
| Sequence | >tr|Q4Q9X6|Q4Q9X6_LEIMA ATPase beta subunit, putative - Leishmania major LSRVQSAMIRRAAGVRAASSAVAAAAAKPAEHKGRVGYVSQVIGAVVDVHFSEGVPPVLT ALDVTEDLGRDEPLTLEIVQHLDANTGRCIAMQTTDLLKLKSKVVSTGGNISVPVGRETL GRIFNVLGDAIDQRGPVGEKMRMAIHAEAPKLADQAAEDTILTTGIKVIDLILPYCKGGK IGLFGGAGVGKTVIIMELINNVAKGHGGFSVFAGVGERTREGTDLYLEMMQSKVIDLKGE SKCVLVYGQMNEPPGARARVAQSALTMAEYFRDVEGQNVLLFIDNIFRFTQANSEVSALL GRIPAAVGYQPTLAEDLGMLQERITSTTKGSITSVQAVYVPADDITDPAPATTFSHLDAT TVLDRAVAESGIYPAVNPLECASRIMDPDVIDVDHYNVAQDIVQMLTKYKELQDIIAVLG IDELSEEDKVVVDRARKVTRFLSQPFQVAEVFTGMTGHYVQLVDTVESFSGLLMGSYDQI PEMAFYMVGGIKSVLEKAKAMAEEAAAMEKQRRARQAANASDSQ |
| DNA Sequence | >LmjF25.1170 |||ATPase beta subunit, putative|Leishmania major|chr 25|||Manual ATGCTGTCCC GTGTGCAGTC TGCGATGATT CGCCGCGCCG CTGGGGTGCG CGCTGCGTCGTCGGCGGTGG CTGCCGCTGC CGCGAAGCCT GCGGAGCACA AGGGCCGCGT CGGCTACGTGTCGCAGGTCA TTGGTGCGGT GGTGGACGTG CACTTCTCGG AGGGCGTGCC GCCCGTGCTGACGGCGCTGG ATGTGACGGA GGACCTTGGC CGTGATGAGC CGCTGACGCT GGAGATCGTGCAGCACTTGG ACGCGAACAC CGGCCGCTGC ATTGCGATGC AGACGACGGA CCTGCTGAAGCTGAAGTCGA AGGTTGTGTC GACCGGCGGC AACATCTCTG TGCCGGTGGG CCGTGAGACGCTGGGCCGCA TCTTCAACGT TCTGGGCGAT GCGATCGACC AGCGCGGCCC CGTGGGCGAGAAGATGCGCA TGGCGATCCA CGCCGAGGCC CCGAAGCTGG CGGATCAGGC CGCAGAGGACACGATCCTGA CGACCGGCAT CAAGGTGATC GACTTGATCC TGCCCTACTG CAAGGGTGGCAAGATCGGCC TGTTCGGCGG TGCCGGTGTG GGCAAGACTG TGATCATCAT GGAGCTGATCAACAATGTCG CGAAGGGCCA CGGTGGTTTC TCCGTGTTTG CCGGCGTTGG CGAGCGCACGCGCGAGGGCA CGGACCTGTA CCTGGAGATG ATGCAGTCGA AGGTGATTGA CCTGAAGGGCGAGTCGAAGT GCGTGCTTGT GTACGGGCAG ATGAACGAGC CCCCGGGTGC GCGCGCGCGCGTTGCGCAGT CTGCGCTGAC GATGGCGGAG TACTTCCGCG ACGTGGAGGG CCAGAACGTGCTGCTGTTCA TCGACAACAT CTTCCGCTTC ACGCAGGCGA ACTCCGAGGT GTCCGCGCTGCTGGGCCGCA TTCCGGCCGC CGTGGGCTAC CAGCCGACGC TTGCGGAGGA TCTTGGTATGCTGCAGGAGC GCATCACGTC GACAACGAAG GGGTCGATCA CGTCCGTGCA GGCCGTGTACGTGCCAGCGG ATGATATCAC GGATCCCGCG CCCGCGACGA CGTTCTCGCA CCTGGATGCGACGACTGTGC TGGACCGCGC GGTGGCGGAG TCGGGCATCT ACCCTGCCGT GAACCCGCTGGAGTGCGCGT CGCGTATCAT GGACCCCGAT GTGATCGATG TGGACCACTA CAACGTTGCGCAGGATATCG TGCAGATGCT GACCAAGTAC AAGGAGCTGC AGGACATCAT TGCGGTGCTTGGCATCGACG AGCTGAGCGA GGAAGACAAG GTTGTGGTGG ACCGCGCGCG CAAGGTGACCCGGTTCCTGT CGCAGCCGTT CCAGGTTGCG GAGGTGTTCA CGGGCATGAC GGGCCACTACGTGCAGCTGG TCGACACGGT GGAGTCGTTC TCTGGCCTGC TGATGGGGTC GTACGACCAGATCCCGGAGA TGGCGTTCTA CATGGTTGGC GGCATCAAGT CTGTGCTGGA GAAGGCGAAGGCCATGGCGG AGGAGGCTGC GGCGATGGAG AAGCAGCGTC GCGCGCGCCA GGCCGCGAACGCCTCGGACT CGCAGTAG |
| ATPase beta subunit, putative Q4Q9X6] | |
|---|---|
| Metabolite Information | |
| Molecular Function | ATP binding; GTP binding; hydrogen-exporting ATPase activity, phosphorylative mechanism; hydrogen-transporting ATP synthase activity, rotational mechanism; hydrogen-transporting ATPase activity, rotational mechanism; nucleoside-triphosphatase activity; nucleotide binding |
| Biochemical Pathway | ATP biosynthesis; ATP synthesis coupled proton transport |
| Regulatory Pathway | |
| KEGG Pathways | K02112 |
| Orthologs | ||||
| Homologs | GI | Percent Identity | Evalue | Score |
| Homo sapiens | ATP synthase, H+ transporting, mitochondrial F1 complex, beta subunit precursor [Homo sapiens] | 63 | 1e-163 | 571 |
| DEG Information | ||||
| DEG Protein | DEG Organism | Percent Identity | Evalue | Bit Score |
| HP1132 ATP synthase F1, subunit beta (atpD) | Helicobacter pylori | 57% | 1e-145 | 509 |
| Post Translational Modification | ||||
| PTM Type | PTM Sub Type | Score | Modification Site | Prosite ID |
| PDOC00017 | ATP/GTP-binding site motif A (P-loop) | 186-193; | PS00017 | |
| Acylation | N-myristoylation site | 15-20; 109-114; 179-184; 183-188; 187-192; 189-194; 331-336; 372-377; 472-477; 490-495; | PS00008 | |
| Glycosylation | N-glycosylation site | 111-114; 520-523; | PS00001 | |
| Phosphorylation | cAMP- and cGMP-dependent protein kinase phosphorylation site | 437-440; | PS00004 | |
| Phosphorylation | Casein kinase II phosphorylation site | 61-64; 267-270; 313-316; 356-359; 362-365; 426-429; 494-497; | PS00006 | |
| Phosphorylation | Protein kinase C phosphorylation site | 87-89; 328-330; | PS00005 | |
| Phosphorylation | Tyrosine kinase phosphorylation site | 366-374; | PS00007 | |
| Sulfation | Tyrosine sulfation site | 390-404; | PS00003 | |
| ATPase beta subunit, putative [Q4Q9X6] | ||
|---|---|---|
| Model Information | ||
| Template PDB ID | 2hldX | |
| Percent Identity | 63% | |
| Target Region | 34-505 | |
| Template Region | 7-469 | |
| Domain Information | ||
|---|---|---|
| Domains | Start | End |
| Active Site Information | ||
|---|---|---|
| Residue | Active Site Number | Functional Part |
| LYS | 159 | Sidechain |
| GLU | 185 | Sidechain |
| ARG | 186 | Sidechain |
| ARG | 352 | Sidechain |
| ILE | 353 | Sidechain (LEU 357 In Template) |
| Co-Factor | |
|---|---|
| Metal | Description |
| Ligands | |||||
|---|---|---|---|---|---|
| CAS number | Name | Mol. Weight | Mol. Formula | Smile Notation | PDB Reference |
| PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER | 506.196 | C10 H17 N6 O12 P3 | O=P(O)(O)NP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O | 2hld | |
| 7791-18-6 | MAGNESIUM ION | 24.305 | Mg | [Mg+2] | 2hld |
| 14265-44-2 | PHOSPHATE ION | 94.971 | O4 P | [O-]P([O-])([O-])=O | 2hld |
| 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/2295722/Q4Q9X6.pdb 2.0 471 = residues | | = | *| Ramachandran plot: 93.9% core 5.2% allow 0.7% gener 0.2% = disall | | = | +| All Ramachandrans: 9 labelled residues (out of 469) = | +| Chi1-chi2 plots: 4 labelled residues (out of 258) = | | = | | 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: = 5 | *| Bond len/angle: 18.4 Morris et al class: 1 = 1 2 | +| 1 cis-peptides = | | G-factors Dihedrals: 0.09 Covalent: -0.11 Overall: = 0.02 | | = | | M/c bond lengths: 99.7% within limits 0.3% highlighted = | *| M/c bond angles: 95.1% within limits 4.9% highlighted 1 off = graph | | Planar groups: 100.0% within limits 0.0% highlighted = | | = | = +------------------------------------------------------------------------= ----+ + May be worth investigating further. * Worth investigating further. |