damage-control phosphatase ARMT1 isoform X2 [Mus musculus]
Protein Classification
damage-control phosphatase ARMT1 family protein( domain architecture ID 10487715)
damage-control phosphatase ARMT1 family protein is a metal-dependent phosphatase implicated in metabolite damage-control, similar to Homo sapiens acidic residue methyltransferase 1 (ARMT1) that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| ARMT1-like_dom | pfam01937 | Damage-control phosphatase ARMT1-like domain; This domain is widely distributed in all domains ... |
1-298 | 6.54e-87 | |||||
Damage-control phosphatase ARMT1-like domain; This domain is widely distributed in all domains of life and occur in stand-alone form and as C-terminal fusions to pantothenate kinase (PanK) in plants and animals. They are metal-dependent phosphatases involved in metabolic damage-control processes termed "damage pre-emption" or "housecleaning". S.cerevisiae Damage-control phosphatase YMR027W and the human orthologue Damage-control phosphatase ARMT1 (also known as C6orf211) are involved in response to DNA damage, a damage pre-emption function. Crystal structure of Damage-control phosphatase At2g17340 from Arabidopsis revealed a novel protein fold and several conserved residues coordinating a metal ion (probably Mg2+), which exhibits a high degree of conservation, suggesting that the metal-binding site is central for the function. : Pssm-ID: 396496 Cd Length: 303 Bit Score: 262.97 E-value: 6.54e-87
|
|||||||||
| Name | Accession | Description | Interval | E-value | |||||
| ARMT1-like_dom | pfam01937 | Damage-control phosphatase ARMT1-like domain; This domain is widely distributed in all domains ... |
1-298 | 6.54e-87 | |||||
Damage-control phosphatase ARMT1-like domain; This domain is widely distributed in all domains of life and occur in stand-alone form and as C-terminal fusions to pantothenate kinase (PanK) in plants and animals. They are metal-dependent phosphatases involved in metabolic damage-control processes termed "damage pre-emption" or "housecleaning". S.cerevisiae Damage-control phosphatase YMR027W and the human orthologue Damage-control phosphatase ARMT1 (also known as C6orf211) are involved in response to DNA damage, a damage pre-emption function. Crystal structure of Damage-control phosphatase At2g17340 from Arabidopsis revealed a novel protein fold and several conserved residues coordinating a metal ion (probably Mg2+), which exhibits a high degree of conservation, suggesting that the metal-binding site is central for the function. Pssm-ID: 396496 Cd Length: 303 Bit Score: 262.97 E-value: 6.54e-87
|
|||||||||
| Name | Accession | Description | Interval | E-value | |||||
| ARMT1-like_dom | pfam01937 | Damage-control phosphatase ARMT1-like domain; This domain is widely distributed in all domains ... |
1-298 | 6.54e-87 | |||||
Damage-control phosphatase ARMT1-like domain; This domain is widely distributed in all domains of life and occur in stand-alone form and as C-terminal fusions to pantothenate kinase (PanK) in plants and animals. They are metal-dependent phosphatases involved in metabolic damage-control processes termed "damage pre-emption" or "housecleaning". S.cerevisiae Damage-control phosphatase YMR027W and the human orthologue Damage-control phosphatase ARMT1 (also known as C6orf211) are involved in response to DNA damage, a damage pre-emption function. Crystal structure of Damage-control phosphatase At2g17340 from Arabidopsis revealed a novel protein fold and several conserved residues coordinating a metal ion (probably Mg2+), which exhibits a high degree of conservation, suggesting that the metal-binding site is central for the function. Pssm-ID: 396496 Cd Length: 303 Bit Score: 262.97 E-value: 6.54e-87
|
|||||||||
| Blast search parameters | ||||
|
