cysteine-rich/transmembrane domain A-like protein [Arabidopsis thaliana]
Protein Classification
CYSTM domain-containing protein( domain architecture ID 10579196)
CYSTM domain-containing protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| CYSTM | pfam12734 | Cysteine-rich TM module stress tolerance; The members of this family are short cysteine-rich ... |
41-71 | 7.35e-07 | ||
Cysteine-rich TM module stress tolerance; The members of this family are short cysteine-rich membrane proteins that most probably dimerize together to form a transmembrane sulfhydryl-lined pore. The CYSTM module is always present at the extreme C-terminus of the protein in which it is present. Furthermore, like the yeast prototypes, the majority of the proteins also possess a proline/glutamine-rich segment upstream of the CYSTM module that is likely to form a polar, disordered head in the cytoplasm. The presence of an atypical well-conserved acidic residue at the C-terminal end of the TM helix suggests that this might interact with a positively charged moiety in the lipid head group. Consistently across the eukaryotes, the different versions of the CYSTM module appear to have roles in stress-response or stress-tolerance, and, more specifically, in resistance to deleterious substances, implying that these might be general functions of the whole family. : Pssm-ID: 403822 Cd Length: 37 Bit Score: 41.10 E-value: 7.35e-07
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| Name | Accession | Description | Interval | E-value | ||
| CYSTM | pfam12734 | Cysteine-rich TM module stress tolerance; The members of this family are short cysteine-rich ... |
41-71 | 7.35e-07 | ||
Cysteine-rich TM module stress tolerance; The members of this family are short cysteine-rich membrane proteins that most probably dimerize together to form a transmembrane sulfhydryl-lined pore. The CYSTM module is always present at the extreme C-terminus of the protein in which it is present. Furthermore, like the yeast prototypes, the majority of the proteins also possess a proline/glutamine-rich segment upstream of the CYSTM module that is likely to form a polar, disordered head in the cytoplasm. The presence of an atypical well-conserved acidic residue at the C-terminal end of the TM helix suggests that this might interact with a positively charged moiety in the lipid head group. Consistently across the eukaryotes, the different versions of the CYSTM module appear to have roles in stress-response or stress-tolerance, and, more specifically, in resistance to deleterious substances, implying that these might be general functions of the whole family. Pssm-ID: 403822 Cd Length: 37 Bit Score: 41.10 E-value: 7.35e-07
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| Name | Accession | Description | Interval | E-value | ||
| CYSTM | pfam12734 | Cysteine-rich TM module stress tolerance; The members of this family are short cysteine-rich ... |
41-71 | 7.35e-07 | ||
Cysteine-rich TM module stress tolerance; The members of this family are short cysteine-rich membrane proteins that most probably dimerize together to form a transmembrane sulfhydryl-lined pore. The CYSTM module is always present at the extreme C-terminus of the protein in which it is present. Furthermore, like the yeast prototypes, the majority of the proteins also possess a proline/glutamine-rich segment upstream of the CYSTM module that is likely to form a polar, disordered head in the cytoplasm. The presence of an atypical well-conserved acidic residue at the C-terminal end of the TM helix suggests that this might interact with a positively charged moiety in the lipid head group. Consistently across the eukaryotes, the different versions of the CYSTM module appear to have roles in stress-response or stress-tolerance, and, more specifically, in resistance to deleterious substances, implying that these might be general functions of the whole family. Pssm-ID: 403822 Cd Length: 37 Bit Score: 41.10 E-value: 7.35e-07
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