activation-induced cytidine deaminase [Homo sapiens]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| NAD1 super family | cl40077 | Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned ... |
5-53 | 1.11e-15 | ||
Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned fishes, the coelacanth, amphibians, lizards, and marsupials. The actual alignment was detected with superfamily member pfam18778: Pssm-ID: 465865 [Multi-domain] Cd Length: 175 Bit Score: 66.53 E-value: 1.11e-15
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| Name | Accession | Description | Interval | E-value | ||
| NAD1 | pfam18778 | Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned ... |
5-53 | 1.11e-15 | ||
Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned fishes, the coelacanth, amphibians, lizards, and marsupials. Pssm-ID: 465865 [Multi-domain] Cd Length: 175 Bit Score: 66.53 E-value: 1.11e-15
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| Name | Accession | Description | Interval | E-value | ||
| NAD1 | pfam18778 | Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned ... |
5-53 | 1.11e-15 | ||
Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned fishes, the coelacanth, amphibians, lizards, and marsupials. Pssm-ID: 465865 [Multi-domain] Cd Length: 175 Bit Score: 66.53 E-value: 1.11e-15
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| APOBEC2 | pfam18772 | APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ... |
6-55 | 3.66e-15 | ||
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most vertebrates including cartilaginous fishes. APOBEC2 is poorly understood in terms of their molecular functions and substrate specificity. Pssm-ID: 465863 [Multi-domain] Cd Length: 174 Bit Score: 65.31 E-value: 3.66e-15
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| APOBEC_N | pfam08210 | APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. ... |
11-53 | 1.33e-12 | ||
APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. Members of this family are C-to-U editing enzymes. The N-terminal domain of APOBEC-1 like proteins is the catalytic domain, while the C-terminal domain is a pseudocatalyitc domain. More specifically, the catalytic domain is a zinc dependent deaminases domain and is essential for cytidine deamination.APOBEC-3 like members contain two copies of this domain. RNA editing by APOBEC-1 requires homodimerization and this complex interacts with RNA binding proteins to from the editosome (and references therein). This family also includes the functionally homologous activation induced deaminase (AID), which is essential for the development of antibody diversity in B lymphocytes, and the sea lamprey PmCDA1 and PmCDA2, which are predicted to play an AID-like role in the adaptive immune response of jawless vertebrates. Divergent members of this family are present in various eukaryotes such as Nematostella, C. elegans, Micromonas and Emiliania, and prokaryotes such as Wolbachia and Pseudomonas brassicacearum. Pssm-ID: 462396 [Multi-domain] Cd Length: 170 Bit Score: 58.53 E-value: 1.33e-12
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| Blast search parameters | ||||
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