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Conserved domains on  [gi|1102130411|ref|NP_001333970|]
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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.
 102-264 3.28e-71

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: 217.62  E-value: 3.28e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102130411 102 DPLSEEEFYSQFYNqrvKHLcYYHRMKPYLCYQLEQFNGQAPL---KGCLLSEKgKQHAEILFLDKIRSMELS---QVTI 175
Cdd:pfam18782   1 KRMYPRTFYFNFNN---KPI-LYGRNKTYLCYEVERLDNGTWLpqhRGFFRNQA-KYHAELCFLSWFCGNQLPpyqNYQV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102130411 176 TCYLTWSPCPNCAWQLAAFKRDRPDLILHIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFVNPK-RPF 254
Cdd:pfam18782  76 TWYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQgEPF 155

                         170
                  ....*....|
gi 1102130411 255 WPWKGLEIIS 264
Cdd:pfam18782 156 QPWDGLEENS 165
APOBEC2 super family cl40073
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 1-99 6.64e-46

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.


The actual alignment was detected with superfamily member pfam18772:

Pssm-ID: 465863 [Multi-domain]  Cd Length: 174  Bit Score: 152.75  E-value: 6.64e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102130411   1 MSWSPCFECAEQIVRFLATHHNLSLDIFSSRLYNVQDPETQQNLCRLVQEGAQVAAMDLYEFKKCWKKFVDNGGRRFRPW 80
Cdd:pfam18772  76 VSWSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDNQGRPFEPW 155

                          90
                  ....*....|....*....
gi 1102130411  81 KRLLTNFRYQDSKLQEILR 99
Cdd:pfam18772 156 EDLDENYEYLSRKLQEILR 174
 
Name Accession Description Interval E-value
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 102-264 3.28e-71

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: 217.62  E-value: 3.28e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102130411 102 DPLSEEEFYSQFYNqrvKHLcYYHRMKPYLCYQLEQFNGQAPL---KGCLLSEKgKQHAEILFLDKIRSMELS---QVTI 175
Cdd:pfam18782   1 KRMYPRTFYFNFNN---KPI-LYGRNKTYLCYEVERLDNGTWLpqhRGFFRNQA-KYHAELCFLSWFCGNQLPpyqNYQV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102130411 176 TCYLTWSPCPNCAWQLAAFKRDRPDLILHIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFVNPK-RPF 254
Cdd:pfam18782  76 TWYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQgEPF 155

                         170
                  ....*....|
gi 1102130411 255 WPWKGLEIIS 264
Cdd:pfam18782 156 QPWDGLEENS 165
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 1-99 6.64e-46

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: 152.75  E-value: 6.64e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102130411   1 MSWSPCFECAEQIVRFLATHHNLSLDIFSSRLYNVQDPETQQNLCRLVQEGAQVAAMDLYEFKKCWKKFVDNGGRRFRPW 80
Cdd:pfam18772  76 VSWSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDNQGRPFEPW 155

                          90
                  ....*....|....*....
gi 1102130411  81 KRLLTNFRYQDSKLQEILR 99
Cdd:pfam18772 156 EDLDENYEYLSRKLQEILR 174
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 122-220 3.79e-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: 67.37  E-value: 3.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102130411 122 CYYHRmKPYLCYQLEqfNGQAPLKGCLL---SEKGKQHAEILFLDKIRSMELSQVTITCYLT-----WSPCPNCAWQLAA 193
Cdd:cd01283    13 APYSN-FTVGAALLT--KDGRIFTGVNVenaSYGLTLCAERTAIGKAVSEGLRRYLVTWAVSdeggvWSPCGACRQVLAE 89

                          90       100
                  ....*....|....*....|....*..
gi 1102130411 194 FKRdrpdlilhiytSRLYFHWKRPFQK 220
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.
 102-264 3.28e-71

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: 217.62  E-value: 3.28e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102130411 102 DPLSEEEFYSQFYNqrvKHLcYYHRMKPYLCYQLEQFNGQAPL---KGCLLSEKgKQHAEILFLDKIRSMELS---QVTI 175
Cdd:pfam18782   1 KRMYPRTFYFNFNN---KPI-LYGRNKTYLCYEVERLDNGTWLpqhRGFFRNQA-KYHAELCFLSWFCGNQLPpyqNYQV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102130411 176 TCYLTWSPCPNCAWQLAAFKRDRPDLILHIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFVNPK-RPF 254
Cdd:pfam18782  76 TWYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQgEPF 155

                         170
                  ....*....|
gi 1102130411 255 WPWKGLEIIS 264
Cdd:pfam18782 156 QPWDGLEENS 165
NAD1 pfam18778
Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned ...
 102-264 1.61e-65

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: 202.89  E-value: 1.61e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102130411 102 DPLSEEEFYSQFYNQRVKhlcyYHRMKPYLCYQLEQFNGQAPLKGCLLSEKGKQHAEILFLDKIRSMEL----SQVTITC 177
Cdd:pfam18778   1 ERMSPETFKFQFKNVEYA----SGRNKTLLCYEVKRGNSSSLWRGHLRNENSGCHAEICFLRWFSSWRLfdpsQCYTITW 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102130411 178 YLTWSPCPNCAWQLAAFKRDRPDLILHIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFVNPK-RPFWP 256
Cdd:pfam18778  77 YLSWSPCPSCAAKLAEFLKAHPNVTLTIFAARLYYFEDPWNQEGLRSLASAGVTLSIMDYSDFEYCWENFVDNEgRPFVP 156


                  ....*...
gi 1102130411 257 WKGLEIIS 264
Cdd:pfam18778 157 WEDLEENS 164
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 104-261 1.54e-55

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: 177.41  E-value: 1.54e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102130411 104 LSEEEFYSQFYNQRVKhlcyYHRMKPYLCYQLEQFNGQA--PLKGCLLSEKGKqHAEILFLDKIRSMELSQ---VTITCY 178
Cdd:pfam18772   1 MDPKTFKFQFKNVPYA----SGRNKTYLCYEVETRSGSDlsPDRGYLRNQAGC-HAELCFLSWILPWQLDPgqkYQVTWY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102130411 179 LTWSPCPNCAWQLAAFKRDRPDLILHIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFV-NPKRPFWPW 257
Cdd:pfam18772  76 VSWSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVdNQGRPFEPW 155


                  ....
gi 1102130411 258 KGLE 261
Cdd:pfam18772 156 EDLD 159
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 1-99 6.64e-46

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: 152.75  E-value: 6.64e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102130411   1 MSWSPCFECAEQIVRFLATHHNLSLDIFSSRLYNVQDPETQQNLCRLVQEGAQVAAMDLYEFKKCWKKFVDNGGRRFRPW 80
Cdd:pfam18772  76 VSWSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDNQGRPFEPW 155

                          90
                  ....*....|....*....
gi 1102130411  81 KRLLTNFRYQDSKLQEILR 99
Cdd:pfam18772 156 EDLDENYEYLSRKLQEILR 174
APOBEC3 pfam18771
APOBEC3; APOBEC3 deaminases act as restriction factors in the innate response to retroviruses ...
 124-253 1.49e-45

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: 150.72  E-value: 1.49e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102130411 124 YHRMKPYLCYQLEQFNGQAPLKGCLlSEKGKQHAEILFLDKIRSMELSQV---TITCYLTWSPCPNCAWQLAAFKRDRPD 200
Cdd:pfam18771   1 YYDRKAYLCYQLKGRNGSALDRGYF-SNKKKRHAEIRFIDKIRSLDLDNIqcyRITCYITWSPCPNCAAELVDFISLNPH 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1102130411 201 LILHIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFVNPKRP 253
Cdd:pfam18771  80 LKLRIFASRLYYHWERSYKEGLQKLQRAGVSVAVMTLPEFQDCWEDFVDHQEE 132
SNAD4 pfam18750
Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases ...
 133-246 5.96e-43

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: 143.17  E-value: 5.96e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102130411 133 YQLEQFNGQAPL-KGCLLSEKGkQHAEILFLDKIRSMELSQVT---ITCYLTWSPCPNCAWQLAAFKRDRPDLILHIYTS 208
Cdd:pfam18750   1 YEIKWGNGSKIWqRGYLSNEHE-QHAEICFLENIRSRELDPSQryrVTWYLSWSPCPECAQKIAEFLAEHPNVTLTIFAA 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1102130411 209 RLYfHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTN 246
Cdd:pfam18750  80 RLY-HWDEDNRQGLRSLAQAGVTLQIMTLEDFEYCWKN 116
NAD1 pfam18778
Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned ...
 1-98 1.25e-42

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: 144.34  E-value: 1.25e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102130411   1 MSWSPCFECAEQIVRFLATHHNLSLDIFSSRLYNVQDPETQQNLCRLVQEGAQVAAMDLYEFKKCWKKFVDNGGRRFRPW 80
Cdd:pfam18778  78 LSWSPCPSCAAKLAEFLKAHPNVTLTIFAARLYYFEDPWNQEGLRSLASAGVTLSIMDYSDFEYCWENFVDNEGRPFVPW 157

                          90
                  ....*....|....*...
gi 1102130411  81 KRLLTNFRYQDSKLQEIL 98
Cdd:pfam18778 158 EDLEENSRYYHRKLQRIL 175
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 1-98 1.47e-39

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: 136.34  E-value: 1.47e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102130411   1 MSWSPCFECAEQIVRFLATHHNLSLDIFSSRLYNVQDPETQQNLCRLVQEGAQVAAMDLYEFKKCWKKFVDNGGRRFRPW 80
Cdd:pfam18782  79 VSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQGEPFQPW 158

                          90
                  ....*....|....*...
gi 1102130411  81 KRLLTNFRYQDSKLQEIL 98
Cdd:pfam18782 159 DGLEENSRFLHRRLREIL 176
APOBEC_C pfam05240
APOBEC-like C-terminal domain; This domain is found at the C-termini of the Apolipoprotein B ...
 21-98 4.28e-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: 116.43  E-value: 4.28e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1102130411  21 HNLSLDIFSSRLYNVQDPETQQNLCRLVQEGAQVAAMDLYEFKKCWKKFVDNGGRRFRPWKRLLTNFRYQDSKLQEIL 98
Cdd:pfam05240   1 PNVSLTIFAARLYYHWDPEYQQGLRRLVQAGAQVAIMSYKEFEYCWDNFVDNQGRPFQPWEGLEENSQLLSRRLQEIL 78
APOBEC_N pfam08210
APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. ...
 109-262 6.35e-33

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: 119.01  E-value: 6.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102130411 109 FYSQFYNQRvkhlCYYHRMKPYLCYQLEQFNGQAPL--KGCLLSEKGKQ-HAEILFLDKIRSMELSQV---TITCYLTWS 182
Cdd:pfam08210   1 FFFHFKNLP----YASGRHETYLCYEVKRDSGGLVVedKGYLRNQAASSlHAEERFLRWIHDLALDPGsnyEVTWYVSWS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102130411 183 PCPNCAWQLAAFKRDRPDLILHIYTSRLYFHWKR--PFQKGLCSLWQSGILVDVMDLPQFTDCWTNFVNPK-RPFWPWKG 259
Cdd:pfam08210  77 PCNECASELAAFLSKHPNVRLRIFVSRLYYWEEPdyWNREGLRSLAQAGVQLRPMSYKDFEYCWNNFVDHDgEPFKPWDG 156


                  ...
gi 1102130411 260 LEI 262
Cdd:pfam08210 157 LHE 159
APOBEC_N pfam08210
APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. ...
 1-96 1.18e-32

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: 118.24  E-value: 1.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102130411   1 MSWSPCFECAEQIVRFLATHHNLSLDIFSSRLYNVQDPE--TQQNLCRLVQEGAQVAAMDLYEFKKCWKKFVDNGGRRFR 78
Cdd:pfam08210  73 VSWSPCNECASELAAFLSKHPNVRLRIFVSRLYYWEEPDywNREGLRSLAQAGVQLRPMSYKDFEYCWNNFVDHDGEPFK 152

                          90
                  ....*....|....*...
gi 1102130411  79 PWKRLLTNFRYQDSKLQE 96
Cdd:pfam08210 153 PWDGLHENSVYLARKLQE 170
SNAD4 pfam18750
Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases ...
 1-68 1.26e-27

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: 103.49  E-value: 1.26e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1102130411   1 MSWSPCFECAEQIVRFLATHHNLSLDIFSSRLYNvQDPETQQNLCRLVQEGAQVAAMDLYEFKKCWKK 68
Cdd:pfam18750  50 LSWSPCPECAQKIAEFLAEHPNVTLTIFAARLYH-WDEDNRQGLRSLAQAGVTLQIMTLEDFEYCWKN 116
APOBEC_C pfam05240
APOBEC-like C-terminal domain; This domain is found at the C-termini of the Apolipoprotein B ...
 199-264 8.01e-26

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: 97.55  E-value: 8.01e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1102130411 199 PDLILHIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFVNPK-RPFWPWKGLEIIS 264
Cdd:pfam05240   1 PNVSLTIFAARLYYHWDPEYQQGLRRLVQAGAQVAIMSYKEFEYCWDNFVDNQgRPFQPWEGLEENS 67
APOBEC3 pfam18771
APOBEC3; APOBEC3 deaminases act as restriction factors in the innate response to retroviruses ...
 1-78 6.91e-19

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: 80.99  E-value: 6.91e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1102130411   1 MSWSPCFECAEQIVRFLATHHNLSLDIFSSRLYNVQDPETQQNLCRLVQEGAQVAAMDLYEFKKCWKKFVDNGGRRFR 78
Cdd:pfam18771  58 ITWSPCPNCAAELVDFISLNPHLKLRIFASRLYYHWERSYKEGLQKLQRAGVSVAVMTLPEFQDCWEDFVDHQEEPFR 135
APOBEC4_like pfam18774
APOBEC4-like -AID/APOBEC-deaminase; Cnidarian and Algal homologs of the APOBEC4-like AID ...
 125-249 1.11e-18

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: 80.30  E-value: 1.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102130411 125 HRMKPYLCYQLEQFNGQAPLKGCllSEKGKQHAEILFLDKIRS-MELSQVTITCYLTWSPCPNCAWQLAAFKRDRPDLIL 203
Cdd:pfam18774   7 HKKEICLLYEIQWGRGTIWRNWT--ENNCTEHAEVNFLENFRSeRPSRSCTITWYLSWSPCWECSGRILEFLSRHPNVTL 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1102130411 204 HIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFVN 249
Cdd:pfam18774  85 GIYVARLFMHDDDRNRQGLRILQMNGVTIQVMMNKDYCYCWKAFKN 130
APOBEC4 pfam18775
APOBEC4; A member of the AID/APOBEC family of cytosine deaminases. The biological function of ...
 1-70 3.73e-15

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: 68.90  E-value: 3.73e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102130411   1 MSWSPCFECAEQIVRFLATHHNLSLDIFSSRLYNVQDPETQQNLCRLVQEGAQVAAMDLYEFKKCWKKFV 70
Cdd:pfam18775   5 LSWSPCNECSEKIQEFLKKHPKVNLDIYFAQLYHTEEEDNRQGLRSLVEKGVTLSVMSGEDWIYCLRTFV 74
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 122-220 3.79e-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: 67.37  E-value: 3.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102130411 122 CYYHRmKPYLCYQLEqfNGQAPLKGCLL---SEKGKQHAEILFLDKIRSMELSQVTITCYLT-----WSPCPNCAWQLAA 193
Cdd:cd01283    13 APYSN-FTVGAALLT--KDGRIFTGVNVenaSYGLTLCAERTAIGKAVSEGLRRYLVTWAVSdeggvWSPCGACRQVLAE 89

                          90       100
                  ....*....|....*....|....*..
gi 1102130411 194 FKRdrpdlilhiytSRLYFHWKRPFQK 220
Cdd:cd01283    90 FLP-----------SRLYIIIDNPKGE 105
APOBEC4 pfam18775
APOBEC4; A member of the AID/APOBEC family of cytosine deaminases. The biological function of ...
 175-248 2.38e-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: 2.38e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1102130411 175 ITCYLTWSPCPNCAWQLAAFKRDRPDLILHIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFV 248
Cdd:pfam18775   1 VTLYLSWSPCNECSEKIQEFLKKHPKVNLDIYFAQLYHTEEEDNRQGLRSLVEKGVTLSVMSGEDWIYCLRTFV 74
APOBEC4_like pfam18774
APOBEC4-like -AID/APOBEC-deaminase; Cnidarian and Algal homologs of the APOBEC4-like AID ...
 1-71 4.49e-11

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: 59.50  E-value: 4.49e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1102130411   1 MSWSPCFECAEQIVRFLATHHNLSLDIFSSRLYNVQDPETQQNLCRLVQEGAQVAAMDLYEFKKCWKKFVD 71
Cdd:pfam18774  60 LSWSPCWECSGRILEFLSRHPNVTLGIYVARLFMHDDDRNRQGLRILQMNGVTIQVMMNKDYCYCWKAFKN 130
 
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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