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single-stranded DNA cytosine deaminase isoform 2 [Homo sapiens]
List of domain hits
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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 ... |
5-170 | 1.08e-79 | ||||
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: 234.48 E-value: 1.08e-79
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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 ... |
5-170 | 1.08e-79 | ||||
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: 234.48 E-value: 1.08e-79
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cytidine_deaminase | cd01283 | Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ... |
5-129 | 1.50e-12 | ||||
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on the substrate. Cytidine deaminases catalyze the deamination of cytidine to uridine and are important in the pyrimadine salvage pathway in many cell types, from bacteria to humans. This family also includes the apoBec proteins, which are a mammal specific expansion of RNA editing enzymes, and the closely related phorbolins, and the AID (activation-induced) enzymes. Pssm-ID: 238610 [Multi-domain] Cd Length: 112 Bit Score: 61.20 E-value: 1.50e-12
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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 ... |
5-170 | 1.08e-79 | ||||
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: 234.48 E-value: 1.08e-79
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APOBEC2 | pfam18772 | APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ... |
6-170 | 3.83e-77 | ||||
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: 228.25 E-value: 3.83e-77
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APOBEC_N | pfam08210 | APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. ... |
11-168 | 1.71e-70 | ||||
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: 211.07 E-value: 1.71e-70
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NAD2 | pfam18782 | Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians. |
5-170 | 5.93e-60 | ||||
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians. Pssm-ID: 436733 [Multi-domain] Cd Length: 176 Bit Score: 184.88 E-value: 5.93e-60
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SNAD4 | pfam18750 | Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases ... |
31-143 | 2.07e-47 | ||||
Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases found only in sponges that often shows lineage-specific expansions. Pssm-ID: 465854 [Multi-domain] Cd Length: 116 Bit Score: 150.87 E-value: 2.07e-47
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APOBEC3 | pfam18771 | APOBEC3; APOBEC3 deaminases act as restriction factors in the innate response to retroviruses ... |
24-143 | 3.30e-36 | ||||
APOBEC3; APOBEC3 deaminases act as restriction factors in the innate response to retroviruses and various retroelements. Pssm-ID: 465862 [Multi-domain] Cd Length: 135 Bit Score: 122.98 E-value: 3.30e-36
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APOBEC_C | pfam05240 | APOBEC-like C-terminal domain; This domain is found at the C-termini of the Apolipoprotein B ... |
102-170 | 9.33e-27 | ||||
APOBEC-like C-terminal domain; This domain is found at the C-termini of the Apolipoprotein B mRNA editing enzyme. Pssm-ID: 461599 Cd Length: 78 Bit Score: 96.78 E-value: 9.33e-27
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APOBEC1 | pfam18769 | APOBEC1; APOBEC1 deaminates cytosine both in RNA and ssDNA and has roles in both mRNA editing ... |
56-139 | 5.89e-18 | ||||
APOBEC1; APOBEC1 deaminates cytosine both in RNA and ssDNA and has roles in both mRNA editing and ssDNA mutagenesis as part of the defense against retroviruses and genomic retrotransposons. Pssm-ID: 408540 Cd Length: 101 Bit Score: 74.85 E-value: 5.89e-18
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APOBEC4_like | pfam18774 | APOBEC4-like -AID/APOBEC-deaminase; Cnidarian and Algal homologs of the APOBEC4-like AID ... |
50-151 | 1.58e-16 | ||||
APOBEC4-like -AID/APOBEC-deaminase; Cnidarian and Algal homologs of the APOBEC4-like AID/APOBEC-like deaminases characterized by a distinct Zn chelating site involving residues from the conserved loops 1 and 3. Pssm-ID: 408545 [Multi-domain] Cd Length: 131 Bit Score: 72.21 E-value: 1.58e-16
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APOBEC4 | pfam18775 | APOBEC4; A member of the AID/APOBEC family of cytosine deaminases. The biological function of ... |
78-142 | 4.36e-13 | ||||
APOBEC4; A member of the AID/APOBEC family of cytosine deaminases. The biological function of APOBEC4 is poorly understood. However, it is widely conserved across vertebrates. Pssm-ID: 436728 Cd Length: 74 Bit Score: 61.58 E-value: 4.36e-13
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cytidine_deaminase | cd01283 | Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ... |
5-129 | 1.50e-12 | ||||
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on the substrate. Cytidine deaminases catalyze the deamination of cytidine to uridine and are important in the pyrimadine salvage pathway in many cell types, from bacteria to humans. This family also includes the apoBec proteins, which are a mammal specific expansion of RNA editing enzymes, and the closely related phorbolins, and the AID (activation-induced) enzymes. Pssm-ID: 238610 [Multi-domain] Cd Length: 112 Bit Score: 61.20 E-value: 1.50e-12
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Blast search parameters | ||||
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