Primary Information |
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| BoMiProt ID | Bomi5021 |
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| Protein Name | Damage-control phosphatase ARMT1/Acidic residue methyltransferase 1/Protein-glutamate O-methyltransferase/Sugar phosphate phosphatase ARMT1 |
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| Organism | Bos taurus |
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| Uniprot ID | A3KMX8 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_001076968.1 |
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| Aminoacid Length | 441 |
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| Molecular Weight | 50964 |
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| FASTA Sequence |
Download |
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| Gene Name | ARMT1 |
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| Gene ID | 540698 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein Function | shows phosphatase activity against several substrates andshown to have O-methyltransferase activity that methylates glutamate residues of target proteins to form gamma-glutamyl methyl ester residues. |
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| Biochemical Properties | The biochemical activities of the human protein are conserved with those of a previously characterized budding yeast homolog, where an in vitro phosphatase activity is supported by divalent cations that include Co2+, Ni2+, Mn2+ or Mg2+. |
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| PTMs | Acetylation and phosphorylation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|A3KMX8|ARMT1_BOVIN Damage-control phosphatase ARMT1 OS=Bos taurus OX=9913 GN=ARMT1 PE=2 SV=1
MAGPPASLSARDVGSFAYLSVKDRSPQILTKAIDTLHRHKSEFFEKHGEKGLEAEKKAIS
LLSKLRNELQTDKPIVPLVEKFVDTDIWNQYLEYQQSLLNES*102DGKPRWFLSPWLFVECYM
YRRIHEAIIQSPPIDDFDIFKEFKDQNFFESQESIIALCTHLQELRKTIEDLDENQLKNE
FFKVLQISLWGNKCDLSLSGGEHISQKTNIMNSLEDLKPFILVNDMDRLWSLLSNCKKTR
EKESVTRVDIVLDNSGFELITDLVLADFLLSSKLATKIHFYGKTIPWFVSDTTLHDFNWI
IKQLKHSNNKWVSQCGVDWEDHVKTGRWVYLDHIFWTLPHEFSAMSQVAPDLHAALQKAH
LIFFKGDLNYRKLTGDRRWEFTVPFHEALSGFHPAPLCSIRTLKAEVQVGLQPGQGEQLT
ASEPNWLTAGKYGVFQFDGPL
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Additional Comments | The sequence around the two cysteines involved in the redox-active disulphide bond is conserved and can be used as a signature pattern. |
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| Bibliography | 1.Dennis TN, Kenjić N, Kang AS, Lowenson JD, Kirkwood JS, Clarke SG, Perry JJP. Human ARMT1 structure and substrate specificity indicates that it is a DUF89 family damage-control phosphatase. J Struct Biol. 2020 Oct 1;212(1):107576. doi: 10.1016/j.jsb.2020.107576. Epub 2020 Jul 15. PMID: 32682077. |
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