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Conserved domains on  [gi|1910379707|ref|XP_036093401|]
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DNA dC-

Protein Classification

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List of domain hits

 Name Accession Description Interval E-value
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 25-199 6.90e-76

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: 233.65  E-value: 6.90e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707  25 LDPETFSYEFQNLDFAYGRKDTYLCFQVKReQHSSPEPSDCGVLKNQEASHAEICFLTWFHAEKLSPHEHYDVTWFLSWS 104
Cdd:pfam18772   1 MDPKTFKFQFKNVPYASGRNKTYLCYEVET-RSGSDLSPDRGYLRNQAGCHAELCFLSWILPWQLDPGQKYQVTWYVSWS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707 105 PCAICAKKVAIFLRNHENVRLSIFVSRIYMFQKPEVQQALRDLNCLGVKLDAMCFDEFKYCWENFVHNQGKPFMCWENVH 184
Cdd:pfam18772  80 PCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDNQGRPFEPWEDLD 159

                         170
                  ....*....|....*
gi 1910379707 185 RNSQSMSRELNEILR 199
Cdd:pfam18772 160 ENYEYLSRKLQEILR 174
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 205-378 2.93e-67

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: 211.30  E-value: 2.93e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707 205 LSEQTFNYQFGNQRRVKepqGRRKTYLCYKLK---LLNETLDKGYFMEKKKNHAEICFINKISKLDLDPNQSYEITCYTT 281
Cdd:pfam18772   1 MDPKTFKFQFKNVPYAS---GRNKTYLCYEVEtrsGSDLSPDRGYLRNQAGCHAELCFLSWILPWQLDPGQKYQVTWYVS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707 282 WSPCPDCAGKLAALVEGCPQLRLRIFASRLHFHWRWQYQEGLRCLQKINIPVLVMKEPEFAYCWDNFADNQGRRFRPWDK 361
Cdd:pfam18772  78 WSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDNQGRPFEPWED 157

                         170
                  ....*....|....*..
gi 1910379707 362 LTQYSNCAERRLEKILQ 378
Cdd:pfam18772 158 LDENYEYLSRKLQEILR 174
 
Name Accession Description Interval E-value
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 25-199 6.90e-76

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: 233.65  E-value: 6.90e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707  25 LDPETFSYEFQNLDFAYGRKDTYLCFQVKReQHSSPEPSDCGVLKNQEASHAEICFLTWFHAEKLSPHEHYDVTWFLSWS 104
Cdd:pfam18772   1 MDPKTFKFQFKNVPYASGRNKTYLCYEVET-RSGSDLSPDRGYLRNQAGCHAELCFLSWILPWQLDPGQKYQVTWYVSWS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707 105 PCAICAKKVAIFLRNHENVRLSIFVSRIYMFQKPEVQQALRDLNCLGVKLDAMCFDEFKYCWENFVHNQGKPFMCWENVH 184
Cdd:pfam18772  80 PCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDNQGRPFEPWEDLD 159

                         170
                  ....*....|....*
gi 1910379707 185 RNSQSMSRELNEILR 199
Cdd:pfam18772 160 ENYEYLSRKLQEILR 174
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 205-378 2.93e-67

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: 211.30  E-value: 2.93e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707 205 LSEQTFNYQFGNQRRVKepqGRRKTYLCYKLK---LLNETLDKGYFMEKKKNHAEICFINKISKLDLDPNQSYEITCYTT 281
Cdd:pfam18772   1 MDPKTFKFQFKNVPYAS---GRNKTYLCYEVEtrsGSDLSPDRGYLRNQAGCHAELCFLSWILPWQLDPGQKYQVTWYVS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707 282 WSPCPDCAGKLAALVEGCPQLRLRIFASRLHFHWRWQYQEGLRCLQKINIPVLVMKEPEFAYCWDNFADNQGRRFRPWDK 361
Cdd:pfam18772  78 WSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDNQGRPFEPWED 157

                         170
                  ....*....|....*..
gi 1910379707 362 LTQYSNCAERRLEKILQ 378
Cdd:pfam18772 158 LDENYEYLSRKLQEILR 174
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 21-167 2.93e-07

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: 48.49  E-value: 2.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707  21 PMERLDPETFSYefqnldfAYGRKDTYLCFQVKReqhsspepsDCGVLK--NQEAS------HAEICFLTWFHAEKlspH 92
Cdd:cd01283     1 IEAALAAAEFAY-------APYSNFTVGAALLTK---------DGRIFTgvNVENAsygltlCAERTAIGKAVSEG---L 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707  93 EHYDVTWFLS-----WSPCAICAKKVAIFLRnhenvrlsifvSRIYMFQKPEVQQalrdlnclgvkldamcfdEFKYCWE 167
Cdd:cd01283    62 RRYLVTWAVSdeggvWSPCGACRQVLAEFLP-----------SRLYIIIDNPKGE------------------EFAYTLS 112
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 225-315 4.66e-05

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: 42.33  E-value: 4.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707 225 GRRKTYLCYKLKLLNETLdKGYFMEKK----KNHAEICFINKISKLDLdpnQSYEITCYTT-----WSPCPDCAGKLAAL 295
Cdd:cd01283    15 YSNFTVGAALLTKDGRIF-TGVNVENAsyglTLCAERTAIGKAVSEGL---RRYLVTWAVSdeggvWSPCGACRQVLAEF 90

                          90       100
                  ....*....|....*....|
gi 1910379707 296 vegcpqlrlriFASRLHFHW 315
Cdd:cd01283    91 -----------LPSRLYIII 99
 
Name Accession Description Interval E-value
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 25-199 6.90e-76

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: 233.65  E-value: 6.90e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707  25 LDPETFSYEFQNLDFAYGRKDTYLCFQVKReQHSSPEPSDCGVLKNQEASHAEICFLTWFHAEKLSPHEHYDVTWFLSWS 104
Cdd:pfam18772   1 MDPKTFKFQFKNVPYASGRNKTYLCYEVET-RSGSDLSPDRGYLRNQAGCHAELCFLSWILPWQLDPGQKYQVTWYVSWS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707 105 PCAICAKKVAIFLRNHENVRLSIFVSRIYMFQKPEVQQALRDLNCLGVKLDAMCFDEFKYCWENFVHNQGKPFMCWENVH 184
Cdd:pfam18772  80 PCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDNQGRPFEPWEDLD 159

                         170
                  ....*....|....*
gi 1910379707 185 RNSQSMSRELNEILR 199
Cdd:pfam18772 160 ENYEYLSRKLQEILR 174
NAD1 pfam18778
Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned ...
 23-198 2.44e-70

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: 219.46  E-value: 2.44e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707  23 ERLDPETFSYEFQNLDFAYGRKDTYLCFQVKReqhSSPEPSDCGVLKNQEA-SHAEICFLTWFHAEKL-SPHEHYDVTWF 100
Cdd:pfam18778   1 ERMSPETFKFQFKNVEYASGRNKTLLCYEVKR---GNSSSLWRGHLRNENSgCHAEICFLRWFSSWRLfDPSQCYTITWY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707 101 LSWSPCAICAKKVAIFLRNHENVRLSIFVSRIYMFQKPEVQQALRDLNCLGVKLDAMCFDEFKYCWENFVHNQGKPFMCW 180
Cdd:pfam18778  78 LSWSPCPSCAAKLAEFLKAHPNVTLTIFAARLYYFEDPWNQEGLRSLASAGVTLSIMDYSDFEYCWENFVDNEGRPFVPW 157

                         170
                  ....*....|....*...
gi 1910379707 181 ENVHRNSQSMSRELNEIL 198
Cdd:pfam18778 158 EDLEENSRYYHRKLQRIL 175
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 23-198 2.65e-70

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: 219.16  E-value: 2.65e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707  23 ERLDPETFSYEFQNLDFAYGRKDTYLCFQVKREQHSSPEPSDCGVLKNQEASHAEICFLTWFHAEKLSPHEHYDVTWFLS 102
Cdd:pfam18782   1 KRMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGTWLPQHRGFFRNQAKYHAELCFLSWFCGNQLPPYQNYQVTWYVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707 103 WSPCAICAKKVAIFLRNHENVRLSIFVSRIYMFQKPEVQQALRDLNCLGVKLDAMCFDEFKYCWENFVHNQGKPFMCWEN 182
Cdd:pfam18782  81 WSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQGEPFQPWDG 160

                         170
                  ....*....|....*.
gi 1910379707 183 VHRNSQSMSRELNEIL 198
Cdd:pfam18782 161 LEENSRFLHRRLREIL 176
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 205-378 2.93e-67

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: 211.30  E-value: 2.93e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707 205 LSEQTFNYQFGNQRRVKepqGRRKTYLCYKLK---LLNETLDKGYFMEKKKNHAEICFINKISKLDLDPNQSYEITCYTT 281
Cdd:pfam18772   1 MDPKTFKFQFKNVPYAS---GRNKTYLCYEVEtrsGSDLSPDRGYLRNQAGCHAELCFLSWILPWQLDPGQKYQVTWYVS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707 282 WSPCPDCAGKLAALVEGCPQLRLRIFASRLHFHWRWQYQEGLRCLQKINIPVLVMKEPEFAYCWDNFADNQGRRFRPWDK 361
Cdd:pfam18772  78 WSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDNQGRPFEPWED 157

                         170
                  ....*....|....*..
gi 1910379707 362 LTQYSNCAERRLEKILQ 378
Cdd:pfam18772 158 LDENYEYLSRKLQEILR 174
NAD1 pfam18778
Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned ...
 205-377 1.92e-61

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: 196.35  E-value: 1.92e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707 205 LSEQTFNYQFGNQRRVKepqGRRKTYLCYKLKLLNE-TLDKGYFM-EKKKNHAEICFINKISKLDL-DPNQSYEITCYTT 281
Cdd:pfam18778   3 MSPETFKFQFKNVEYAS---GRNKTLLCYEVKRGNSsSLWRGHLRnENSGCHAEICFLRWFSSWRLfDPSQCYTITWYLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707 282 WSPCPDCAGKLAALVEGCPQLRLRIFASRLHFHWRWQYQEGLRCLQKINIPVLVMKEPEFAYCWDNFADNQGRRFRPWDK 361
Cdd:pfam18778  80 WSPCPSCAAKLAEFLKAHPNVTLTIFAARLYYFEDPWNQEGLRSLASAGVTLSIMDYSDFEYCWENFVDNEGRPFVPWED 159

                         170
                  ....*....|....*.
gi 1910379707 362 LTQYSNCAERRLEKIL 377
Cdd:pfam18778 160 LEENSRYYHRKLQRIL 175
APOBEC_N pfam08210
APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. ...
 30-196 7.45e-58

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: 187.19  E-value: 7.45e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707  30 FSYEFQNLDFAYGRKDTYLCFQVKREQHSSPEpSDCGVLKNQEAS--HAEICFLTWFHAEKLSPHEHYDVTWFLSWSPCA 107
Cdd:pfam08210   1 FFFHFKNLPYASGRHETYLCYEVKRDSGGLVV-EDKGYLRNQAASslHAEERFLRWIHDLALDPGSNYEVTWYVSWSPCN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707 108 ICAKKVAIFLRNHENVRLSIFVSRIYMFQKPEVQ--QALRDLNCLGVKLDAMCFDEFKYCWENFVHNQGKPFMCWENVHR 185
Cdd:pfam08210  80 ECASELAAFLSKHPNVRLRIFVSRLYYWEEPDYWnrEGLRSLAQAGVQLRPMSYKDFEYCWNNFVDHDGEPFKPWDGLHE 159

                         170
                  ....*....|.
gi 1910379707 186 NSQSMSRELNE 196
Cdd:pfam08210 160 NSVYLARKLQE 170
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 204-377 4.81e-57

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: 185.26  E-value: 4.81e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707 204 PLSEQTFNYQFGNQRRVKepqGRRKTYLCYKLKLLNE----TLDKGYFMEKKKNHAEICFINKISKLDLDPNQSYEITCY 279
Cdd:pfam18782   2 RMYPRTFYFNFNNKPILY---GRNKTYLCYEVERLDNgtwlPQHRGFFRNQAKYHAELCFLSWFCGNQLPPYQNYQVTWY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707 280 TTWSPCPDCAGKLAALVEGCPQLRLRIFASRLHFHWRWQYQEGLRCLQKINIPVLVMKEPEFAYCWDNFADNQGRRFRPW 359
Cdd:pfam18782  79 VSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQGEPFQPW 158

                         170
                  ....*....|....*...
gi 1910379707 360 DKLTQYSNCAERRLEKIL 377
Cdd:pfam18782 159 DGLEENSRFLHRRLREIL 176
APOBEC3 pfam18771
APOBEC3; APOBEC3 deaminases act as restriction factors in the innate response to retroviruses ...
 226-357 7.79e-55

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: 178.07  E-value: 7.79e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707 226 RRKTYLCYKLKLLN-ETLDKGYFMEKKKNHAEICFINKISKLDLDPNQSYEITCYTTWSPCPDCAGKLAALVEGCPQLRL 304
Cdd:pfam18771   3 DRKAYLCYQLKGRNgSALDRGYFSNKKKRHAEIRFIDKIRSLDLDNIQCYRITCYITWSPCPNCAAELVDFISLNPHLKL 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1910379707 305 RIFASRLHFHWRWQYQEGLRCLQKINIPVLVMKEPEFAYCWDNFADNQGRRFR 357
Cdd:pfam18771  83 RIFASRLYYHWERSYKEGLQKLQRAGVSVAVMTLPEFQDCWEDFVDHQEEPFR 135
APOBEC_N pfam08210
APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. ...
 210-379 7.96e-45

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: 153.29  E-value: 7.96e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707 210 FNYQFGNQRRVKepqGRRKTYLCYKLKLLNE---TLDKGYFMEKKKN--HAEICFINKISKLDLDPNQSYEITCYTTWSP 284
Cdd:pfam08210   1 FFFHFKNLPYAS---GRHETYLCYEVKRDSGglvVEDKGYLRNQAASslHAEERFLRWIHDLALDPGSNYEVTWYVSWSP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707 285 CPDCAGKLAALVEGCPQLRLRIFASRLHFHWR--WQYQEGLRCLQKINIPVLVMKEPEFAYCWDNFADNQGRRFRPWDKL 362
Cdd:pfam08210  78 CNECASELAAFLSKHPNVRLRIFVSRLYYWEEpdYWNREGLRSLAQAGVQLRPMSYKDFEYCWNNFVDHDGEPFKPWDGL 157

                         170
                  ....*....|....*..
gi 1910379707 363 TQYSncaeRRLEKILQI 379
Cdd:pfam08210 158 HENS----VYLARKLQE 170
SNAD4 pfam18750
Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases ...
 55-168 1.01e-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: 150.87  E-value: 1.01e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707  55 EQHSSPEPSDCGVLKNQEASHAEICFLTWFHAEKLSPHEHYDVTWFLSWSPCAICAKKVAIFLRNHENVRLSIFVSRIYm 134
Cdd:pfam18750   4 KWGNGSKIWQRGYLSNEHEQHAEICFLENIRSRELDPSQRYRVTWYLSWSPCPECAQKIAEFLAEHPNVTLTIFAARLY- 82

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1910379707 135 FQKPEVQQALRDLNCLGVKLDAMCFDEFKYCWEN 168
Cdd:pfam18750  83 HWDEDNRQGLRSLAQAGVTLQIMTLEDFEYCWKN 116
SNAD4 pfam18750
Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases ...
 242-347 6.09e-42

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: 143.56  E-value: 6.09e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707 242 LDKGYFMEKKKNHAEICFINKISKLDLDPNQSYEITCYTTWSPCPDCAGKLAALVEGCPQLRLRIFASRLhFHWRWQYQE 321
Cdd:pfam18750  12 WQRGYLSNEHEQHAEICFLENIRSRELDPSQRYRVTWYLSWSPCPECAQKIAEFLAEHPNVTLTIFAARL-YHWDEDNRQ 90

                          90       100
                  ....*....|....*....|....*.
gi 1910379707 322 GLRCLQKINIPVLVMKEPEFAYCWDN 347
Cdd:pfam18750  91 GLRSLAQAGVTLQIMTLEDFEYCWKN 116
APOBEC_C pfam05240
APOBEC-like C-terminal domain; This domain is found at the C-termini of the Apolipoprotein B ...
 122-198 5.92e-35

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: 124.13  E-value: 5.92e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1910379707 122 NVRLSIFVSRIYMFQKPEVQQALRDLNCLGVKLDAMCFDEFKYCWENFVHNQGKPFMCWENVHRNSQSMSRELNEIL 198
Cdd:pfam05240   2 NVSLTIFAARLYYHWDPEYQQGLRRLVQAGAQVAIMSYKEFEYCWDNFVDNQGRPFQPWEGLEENSQLLSRRLQEIL 78
APOBEC_C pfam05240
APOBEC-like C-terminal domain; This domain is found at the C-termini of the Apolipoprotein B ...
 300-377 8.25e-33

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: 118.35  E-value: 8.25e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1910379707 300 PQLRLRIFASRLHFHWRWQYQEGLRCLQKINIPVLVMKEPEFAYCWDNFADNQGRRFRPWDKLTQYSNCAERRLEKIL 377
Cdd:pfam05240   1 PNVSLTIFAARLYYHWDPEYQQGLRRLVQAGAQVAIMSYKEFEYCWDNFVDNQGRPFQPWEGLEENSQLLSRRLQEIL 78
APOBEC3 pfam18771
APOBEC3; APOBEC3 deaminases act as restriction factors in the innate response to retroviruses ...
 41-177 2.36e-31

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: 116.43  E-value: 2.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707  41 YGRKDTYLCFQVKREQHSSPepsDCGVLKNQEASHAEICFLTWFHAEKLSPHEHYDVTWFLSWSPCAICAKKVAIFLRNH 120
Cdd:pfam18771   1 YYDRKAYLCYQLKGRNGSAL---DRGYFSNKKKRHAEIRFIDKIRSLDLDNIQCYRITCYITWSPCPNCAAELVDFISLN 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1910379707 121 ENVRLSIFVSRIYMFQKPEVQQALRDLNCLGVKLDAMCFDEFKYCWENFVHNQGKPF 177
Cdd:pfam18771  78 PHLKLRIFASRLYYHWERSYKEGLQKLQRAGVSVAVMTLPEFQDCWEDFVDHQEEPF 134
APOBEC4_like pfam18774
APOBEC4-like -AID/APOBEC-deaminase; Cnidarian and Algal homologs of the APOBEC4-like AID ...
 36-170 9.60e-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: 81.84  E-value: 9.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707  36 NLDFAYGRKDTYLCFQVKREQHSsPEPSDCGvlkNQEASHAEICFLTWFHAEKLSPHEhyDVTWFLSWSPCAICAKKVAI 115
Cdd:pfam18774   1 NFDPNNHKKEICLLYEIQWGRGT-IWRNWTE---NNCTEHAEVNFLENFRSERPSRSC--TITWYLSWSPCWECSGRILE 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1910379707 116 FLRNHENVRLSIFVSRIYMFQKPEVQQALRDLNCLGVKLDAMCFDEFKYCWENFV 170
Cdd:pfam18774  75 FLSRHPNVTLGIYVARLFMHDDDRNRQGLRILQMNGVTIQVMMNKDYCYCWKAFK 129
APOBEC4 pfam18775
APOBEC4; A member of the AID/APOBEC family of cytosine deaminases. The biological function of ...
 97-170 1.10e-18

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: 79.69  E-value: 1.10e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1910379707  97 VTWFLSWSPCAICAKKVAIFLRNHENVRLSIFVSRIYMFQKPEVQQALRDLNCLGVKLDAMCFDEFKYCWENFV 170
Cdd:pfam18775   1 VTLYLSWSPCNECSEKIQEFLKKHPKVNLDIYFAQLYHTEEEDNRQGLRSLVEKGVTLSVMSGEDWIYCLRTFV 74
APOBEC1 pfam18769
APOBEC1; APOBEC1 deaminates cytosine both in RNA and ssDNA and has roles in both mRNA editing ...
 70-157 1.40e-16

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: 1.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707  70 NQEASHAEICFLTWFHAEK-LSPHEHYDVTWFLSWSPCAICAKKVAIFLRNHENVRLSIFVSRIYMFQKPEVQQALRDLN 148
Cdd:pfam18769  13 NNTTQHAEVNFLEKFFSERhFDPSVSCSITWFLSWSPCGECSKAIGEFLSQHPNVTLVIYAARLFKHLDIRNRQGLRDLA 92


                  ....*....
gi 1910379707 149 CLGVKLDAM 157
Cdd:pfam18769  93 MSGVTIQIM 101
APOBEC4_like pfam18774
APOBEC4-like -AID/APOBEC-deaminase; Cnidarian and Algal homologs of the APOBEC4-like AID ...
 226-348 1.09e-14

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: 70.29  E-value: 1.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707 226 RRKTYLCYKLKLLNETLDKGYFMEKKKNHAEICFINKISklDLDPNQSYEITCYTTWSPCPDCAGKLAALVEGCPQLRLR 305
Cdd:pfam18774   8 KKEICLLYEIQWGRGTIWRNWTENNCTEHAEVNFLENFR--SERPSRSCTITWYLSWSPCWECSGRILEFLSRHPNVTLG 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1910379707 306 IFASRLHFHWRWQYQEGLRCLQKINIPVLVMKEPEFAYCWDNF 348
Cdd:pfam18774  86 IYVARLFMHDDDRNRQGLRILQMNGVTIQVMMNKDYCYCWKAF 128
APOBEC4 pfam18775
APOBEC4; A member of the AID/APOBEC family of cytosine deaminases. The biological function of ...
 276-348 8.26e-08

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: 49.26  E-value: 8.26e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1910379707 276 ITCYTTWSPCPDCAGKLAALVEGCPQLRLRIFASRLHFHWRWQYQEGLRCLQKINIPVLVMKEPEFAYCWDNF 348
Cdd:pfam18775   1 VTLYLSWSPCNECSEKIQEFLKKHPKVNLDIYFAQLYHTEEEDNRQGLRSLVEKGVTLSVMSGEDWIYCLRTF 73
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 21-167 2.93e-07

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: 48.49  E-value: 2.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707  21 PMERLDPETFSYefqnldfAYGRKDTYLCFQVKReqhsspepsDCGVLK--NQEAS------HAEICFLTWFHAEKlspH 92
Cdd:cd01283     1 IEAALAAAEFAY-------APYSNFTVGAALLTK---------DGRIFTgvNVENAsygltlCAERTAIGKAVSEG---L 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707  93 EHYDVTWFLS-----WSPCAICAKKVAIFLRnhenvrlsifvSRIYMFQKPEVQQalrdlnclgvkldamcfdEFKYCWE 167
Cdd:cd01283    62 RRYLVTWAVSdeggvWSPCGACRQVLAEFLP-----------SRLYIIIDNPKGE------------------EFAYTLS 112
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 225-315 4.66e-05

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: 42.33  E-value: 4.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910379707 225 GRRKTYLCYKLKLLNETLdKGYFMEKK----KNHAEICFINKISKLDLdpnQSYEITCYTT-----WSPCPDCAGKLAAL 295
Cdd:cd01283    15 YSNFTVGAALLTKDGRIF-TGVNVENAsyglTLCAERTAIGKAVSEGL---RRYLVTWAVSdeggvWSPCGACRQVLAEF 90

                          90       100
                  ....*....|....*....|
gi 1910379707 296 vegcpqlrlriFASRLHFHW 315
Cdd:cd01283    91 -----------LPSRLYIII 99
 
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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