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Conserved domains on  [gi|568993659|ref|XP_006521616|]
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DNA dC-

Protein Classification

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List of domain hits

 Name Accession Description Interval E-value
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 54-216 7.16e-73

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: 219.93  E-value: 7.16e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993659   54 DPLSEEEFYSQFYNqrvKHLcYYHRMKPYLCYQLEQFNGQAPL---KGCLLSEKgKQHAEILFLDKIRSMELS---QVTI 127
Cdd:pfam18782   1 KRMYPRTFYFNFNN---KPI-LYGRNKTYLCYEVERLDNGTWLpqhRGFFRNQA-KYHAELCFLSWFCGNQLPpyqNYQV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993659  128 TCYLTWSPCPNCAWQLAAFKRDRPDLILHIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFVNPK-RPF 206
Cdd:pfam18782  76 TWYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQgEPF 155

                         170
                  ....*....|
gi 568993659  207 WPWKGLEIIS 216
Cdd:pfam18782 156 QPWDGLEENS 165
 
Name Accession Description Interval E-value
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 54-216 7.16e-73

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: 219.93  E-value: 7.16e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993659   54 DPLSEEEFYSQFYNqrvKHLcYYHRMKPYLCYQLEQFNGQAPL---KGCLLSEKgKQHAEILFLDKIRSMELS---QVTI 127
Cdd:pfam18782   1 KRMYPRTFYFNFNN---KPI-LYGRNKTYLCYEVERLDNGTWLpqhRGFFRNQA-KYHAELCFLSWFCGNQLPpyqNYQV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993659  128 TCYLTWSPCPNCAWQLAAFKRDRPDLILHIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFVNPK-RPF 206
Cdd:pfam18782  76 TWYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQgEPF 155

                         170
                  ....*....|
gi 568993659  207 WPWKGLEIIS 216
Cdd:pfam18782 156 QPWDGLEENS 165
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 74-172 1.28e-14

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: 67.75  E-value: 1.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993659  74 CYYHRmKPYLCYQLEqfNGQAPLKGCLL---SEKGKQHAEILFLDKIRSMELSQVTITCYLT-----WSPCPNCAWQLAA 145
Cdd:cd01283   13 APYSN-FTVGAALLT--KDGRIFTGVNVenaSYGLTLCAERTAIGKAVSEGLRRYLVTWAVSdeggvWSPCGACRQVLAE 89

                         90       100
                 ....*....|....*....|....*..
gi 568993659 146 FKRdrpdlilhiytSRLYFHWKRPFQK 172
Cdd:cd01283   90 FLP-----------SRLYIIIDNPKGE 105
 
Name Accession Description Interval E-value
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 54-216 7.16e-73

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: 219.93  E-value: 7.16e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993659   54 DPLSEEEFYSQFYNqrvKHLcYYHRMKPYLCYQLEQFNGQAPL---KGCLLSEKgKQHAEILFLDKIRSMELS---QVTI 127
Cdd:pfam18782   1 KRMYPRTFYFNFNN---KPI-LYGRNKTYLCYEVERLDNGTWLpqhRGFFRNQA-KYHAELCFLSWFCGNQLPpyqNYQV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993659  128 TCYLTWSPCPNCAWQLAAFKRDRPDLILHIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFVNPK-RPF 206
Cdd:pfam18782  76 TWYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQgEPF 155

                         170
                  ....*....|
gi 568993659  207 WPWKGLEIIS 216
Cdd:pfam18782 156 QPWDGLEENS 165
NAD1 pfam18778
Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned ...
 51-216 3.16e-67

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: 205.59  E-value: 3.16e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993659   51 KRMDPlseEEFYSQFYNQRVKhlcyYHRMKPYLCYQLEQFNGQAPLKGCLLSEKGKQHAEILFLDKIRSMEL----SQVT 126
Cdd:pfam18778   1 ERMSP---ETFKFQFKNVEYA----SGRNKTLLCYEVKRGNSSSLWRGHLRNENSGCHAEICFLRWFSSWRLfdpsQCYT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993659  127 ITCYLTWSPCPNCAWQLAAFKRDRPDLILHIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFVNPK-RP 205
Cdd:pfam18778  74 ITWYLSWSPCPSCAAKLAEFLKAHPNVTLTIFAARLYYFEDPWNQEGLRSLASAGVTLSIMDYSDFEYCWENFVDNEgRP 153

                         170
                  ....*....|.
gi 568993659  206 FWPWKGLEIIS 216
Cdd:pfam18778 154 FVPWEDLEENS 164
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 56-213 3.05e-57

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: 180.10  E-value: 3.05e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993659   56 LSEEEFYSQFYNQRVKhlcyYHRMKPYLCYQLEQFNGQA--PLKGCLLSEKGKqHAEILFLDKIRSMELSQ---VTITCY 130
Cdd:pfam18772   1 MDPKTFKFQFKNVPYA----SGRNKTYLCYEVETRSGSDlsPDRGYLRNQAGC-HAELCFLSWILPWQLDPgqkYQVTWY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993659  131 LTWSPCPNCAWQLAAFKRDRPDLILHIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFV-NPKRPFWPW 209
Cdd:pfam18772  76 VSWSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVdNQGRPFEPW 155


                  ....
gi 568993659  210 KGLE 213
Cdd:pfam18772 156 EDLD 159
APOBEC3 pfam18771
APOBEC3; APOBEC3 deaminases act as restriction factors in the innate response to retroviruses ...
 76-205 1.17e-46

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: 151.87  E-value: 1.17e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993659   76 YHRMKPYLCYQLEQFNGQAPLKGCLlSEKGKQHAEILFLDKIRSMELSQV---TITCYLTWSPCPNCAWQLAAFKRDRPD 152
Cdd:pfam18771   1 YYDRKAYLCYQLKGRNGSALDRGYF-SNKKKRHAEIRFIDKIRSLDLDNIqcyRITCYITWSPCPNCAAELVDFISLNPH 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568993659  153 LILHIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFVNPKRP 205
Cdd:pfam18771  80 LKLRIFASRLYYHWERSYKEGLQKLQRAGVSVAVMTLPEFQDCWEDFVDHQEE 132
SNAD4 pfam18750
Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases ...
 85-198 4.53e-44

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: 144.33  E-value: 4.53e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993659   85 YQLEQFNGQAPL-KGCLLSEKGkQHAEILFLDKIRSMELSQVT---ITCYLTWSPCPNCAWQLAAFKRDRPDLILHIYTS 160
Cdd:pfam18750   1 YEIKWGNGSKIWqRGYLSNEHE-QHAEICFLENIRSRELDPSQryrVTWYLSWSPCPECAQKIAEFLAEHPNVTLTIFAA 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568993659  161 RLYfHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTN 198
Cdd:pfam18750  80 RLY-HWDEDNRQGLRSLAQAGVTLQIMTLEDFEYCWKN 116
APOBEC_N pfam08210
APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. ...
 61-214 3.83e-34

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: 120.93  E-value: 3.83e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993659   61 FYSQFYNQRvkhlCYYHRMKPYLCYQLEQFNGQAPL--KGCLLSEKGKQ-HAEILFLDKIRSMELSQV---TITCYLTWS 134
Cdd:pfam08210   1 FFFHFKNLP----YASGRHETYLCYEVKRDSGGLVVedKGYLRNQAASSlHAEERFLRWIHDLALDPGsnyEVTWYVSWS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993659  135 PCPNCAWQLAAFKRDRPDLILHIYTSRLYFHWKR--PFQKGLCSLWQSGILVDVMDLPQFTDCWTNFVNPK-RPFWPWKG 211
Cdd:pfam08210  77 PCNECASELAAFLSKHPNVRLRIFVSRLYYWEEPdyWNREGLRSLAQAGVQLRPMSYKDFEYCWNNFVDHDgEPFKPWDG 156


                  ...
gi 568993659  212 LEI 214
Cdd:pfam08210 157 LHE 159
APOBEC_C pfam05240
APOBEC-like C-terminal domain; This domain is found at the C-termini of the Apolipoprotein B ...
 151-216 8.31e-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: 98.71  E-value: 8.31e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568993659  151 PDLILHIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFVNPK-RPFWPWKGLEIIS 216
Cdd:pfam05240   1 PNVSLTIFAARLYYHWDPEYQQGLRRLVQAGAQVAIMSYKEFEYCWDNFVDNQgRPFQPWEGLEENS 67
APOBEC4_like pfam18774
APOBEC4-like -AID/APOBEC-deaminase; Cnidarian and Algal homologs of the APOBEC4-like AID ...
 77-201 1.55e-19

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: 81.46  E-value: 1.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993659   77 HRMKPYLCYQLEQFNGQAPLKGCllSEKGKQHAEILFLDKIRS-MELSQVTITCYLTWSPCPNCAWQLAAFKRDRPDLIL 155
Cdd:pfam18774   7 HKKEICLLYEIQWGRGTIWRNWT--ENNCTEHAEVNFLENFRSeRPSRSCTITWYLSWSPCWECSGRILEFLSRHPNVTL 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568993659  156 HIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFVN 201
Cdd:pfam18774  85 GIYVARLFMHDDDRNRQGLRILQMNGVTIQVMMNKDYCYCWKAFKN 130
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 74-172 1.28e-14

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: 67.75  E-value: 1.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993659  74 CYYHRmKPYLCYQLEqfNGQAPLKGCLL---SEKGKQHAEILFLDKIRSMELSQVTITCYLT-----WSPCPNCAWQLAA 145
Cdd:cd01283   13 APYSN-FTVGAALLT--KDGRIFTGVNVenaSYGLTLCAERTAIGKAVSEGLRRYLVTWAVSdeggvWSPCGACRQVLAE 89

                         90       100
                 ....*....|....*....|....*..
gi 568993659 146 FKRdrpdlilhiytSRLYFHWKRPFQK 172
Cdd:cd01283   90 FLP-----------SRLYIIIDNPKGE 105
APOBEC4 pfam18775
APOBEC4; A member of the AID/APOBEC family of cytosine deaminases. The biological function of ...
 127-200 1.36e-12

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: 61.20  E-value: 1.36e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568993659  127 ITCYLTWSPCPNCAWQLAAFKRDRPDLILHIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFV 200
Cdd:pfam18775   1 VTLYLSWSPCNECSEKIQEFLKKHPKVNLDIYFAQLYHTEEEDNRQGLRSLVEKGVTLSVMSGEDWIYCLRTFV 74
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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