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Conserved domains on  [gi|2025768795|ref|XP_040610061|]
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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 ...
 118-292 1.71e-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: 231.33  E-value: 1.71e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025768795 118 LTEDIFYMQFSNRHRVqpvqqrrYYQRKTYLCYLLEPYN--DQQPLKGCLQNKKDKHAEILFIDKMRSLELCQ---VRIT 192
Cdd:pfam18772   1 MDPKTFKFQFKNVPYA-------SGRNKTYLCYEVETRSgsDLSPDRGYLRNQAGCHAELCFLSWILPWQLDPgqkYQVT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025768795 193 CYLTWSPCPNCAQELAAFKKDHPDLVLRIYTSRLYFHWRRKYQEGLCSLWRSGIQVDVMDLPQFTDCWTNFVSSQS-PFR 271
Cdd:pfam18772  74 WYVSWSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDNQGrPFE 153

                         170       180
                  ....*....|....*....|.
gi 2025768795 272 PWNNLEKNSRCIQRRLQRIKE 292
Cdd:pfam18772 154 PWEDLDENYEYLSRKLQEILR 174
NAD2 super family cl40079
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 1-111 3.75e-61

Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.


The actual alignment was detected with superfamily member pfam18782:

Pssm-ID: 436733 [Multi-domain]  Cd Length: 176  Bit Score: 192.58  E-value: 3.75e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025768795   1 MLPPGEKYKITWYMSWSPCSECAAEVTRFLDTHRNLSLAIFSSRLYYFWKSDYQDKLRRLNQAGAQIAAMDFPEFEKCWN 80
Cdd:pfam18782  66 QLPPYQNYQVTWYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWE 145

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2025768795  81 KFVDNDGKSFRPWKRLKINFRNQDSTLWDIL 111
Cdd:pfam18782 146 NFVYNQGEPFQPWDGLEENSRFLHRRLREIL 176
 
Name Accession Description Interval E-value
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 118-292 1.71e-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: 231.33  E-value: 1.71e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025768795 118 LTEDIFYMQFSNRHRVqpvqqrrYYQRKTYLCYLLEPYN--DQQPLKGCLQNKKDKHAEILFIDKMRSLELCQ---VRIT 192
Cdd:pfam18772   1 MDPKTFKFQFKNVPYA-------SGRNKTYLCYEVETRSgsDLSPDRGYLRNQAGCHAELCFLSWILPWQLDPgqkYQVT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025768795 193 CYLTWSPCPNCAQELAAFKKDHPDLVLRIYTSRLYFHWRRKYQEGLCSLWRSGIQVDVMDLPQFTDCWTNFVSSQS-PFR 271
Cdd:pfam18772  74 WYVSWSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDNQGrPFE 153

                         170       180
                  ....*....|....*....|.
gi 2025768795 272 PWNNLEKNSRCIQRRLQRIKE 292
Cdd:pfam18772 154 PWEDLDENYEYLSRKLQEILR 174
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 1-111 3.75e-61

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: 192.58  E-value: 3.75e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025768795   1 MLPPGEKYKITWYMSWSPCSECAAEVTRFLDTHRNLSLAIFSSRLYYFWKSDYQDKLRRLNQAGAQIAAMDFPEFEKCWN 80
Cdd:pfam18782  66 QLPPYQNYQVTWYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWE 145

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2025768795  81 KFVDNDGKSFRPWKRLKINFRNQDSTLWDIL 111
Cdd:pfam18782 146 NFVYNQGEPFQPWDGLEENSRFLHRRLREIL 176
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 138-236 1.75e-16

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: 73.91  E-value: 1.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025768795 138 QRRYYQRKTYLCYLLEpyNDQQPLKGCLQNKKD----KHAEILFIDKMRSLELCQVRITCYLT-----WSPCPNCAQELA 208
Cdd:cd01283    11 AYAPYSNFTVGAALLT--KDGRIFTGVNVENASygltLCAERTAIGKAVSEGLRRYLVTWAVSdeggvWSPCGACRQVLA 88

                          90       100
                  ....*....|....*....|....*...
gi 2025768795 209 AFKKdhpdlvlriytSRLYFHWRRKYQE 236
Cdd:cd01283    89 EFLP-----------SRLYIIIDNPKGE 105
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 5-55 9.46e-04

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: 38.09  E-value: 9.46e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2025768795   5 GEKYKITWYMS-----WSPCSECAAEVTRFLDthrnlslaifsSRLYYFWKSDYQD 55
Cdd:cd01283    61 LRRYLVTWAVSdeggvWSPCGACRQVLAEFLP-----------SRLYIIIDNPKGE 105
 
Name Accession Description Interval E-value
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 118-292 1.71e-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: 231.33  E-value: 1.71e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025768795 118 LTEDIFYMQFSNRHRVqpvqqrrYYQRKTYLCYLLEPYN--DQQPLKGCLQNKKDKHAEILFIDKMRSLELCQ---VRIT 192
Cdd:pfam18772   1 MDPKTFKFQFKNVPYA-------SGRNKTYLCYEVETRSgsDLSPDRGYLRNQAGCHAELCFLSWILPWQLDPgqkYQVT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025768795 193 CYLTWSPCPNCAQELAAFKKDHPDLVLRIYTSRLYFHWRRKYQEGLCSLWRSGIQVDVMDLPQFTDCWTNFVSSQS-PFR 271
Cdd:pfam18772  74 WYVSWSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDNQGrPFE 153

                         170       180
                  ....*....|....*....|.
gi 2025768795 272 PWNNLEKNSRCIQRRLQRIKE 292
Cdd:pfam18772 154 PWEDLDENYEYLSRKLQEILR 174
NAD1 pfam18778
Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned ...
 117-291 5.53e-66

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: 204.82  E-value: 5.53e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025768795 117 LLTEDIFYMQFSNRHRVqpvqqrrYYQRKTYLCYLLEPYNDQQPLKGCLQNKK-DKHAEILFIDKMRSLELC----QVRI 191
Cdd:pfam18778   2 RMSPETFKFQFKNVEYA-------SGRNKTLLCYEVKRGNSSSLWRGHLRNENsGCHAEICFLRWFSSWRLFdpsqCYTI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025768795 192 TCYLTWSPCPNCAQELAAFKKDHPDLVLRIYTSRLYFHWRRKYQEGLCSLWRSGIQVDVMDLPQFTDCWTNFVSSQ-SPF 270
Cdd:pfam18778  75 TWYLSWSPCPSCAAKLAEFLKAHPNVTLTIFAARLYYFEDPWNQEGLRSLASAGVTLSIMDYSDFEYCWENFVDNEgRPF 154

                         170       180
                  ....*....|....*....|.
gi 2025768795 271 RPWNNLEKNSRCIQRRLQRIK 291
Cdd:pfam18778 155 VPWEDLEENSRYYHRKLQRIL 175
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 117-291 2.59e-64

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: 200.67  E-value: 2.59e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025768795 117 LLTEDIFYMQFSNRHRVqpvqqrrYYQRKTYLCYLLEPYNDQQPL---KGCLQNKKDKHAEILFIDKMRSLELC---QVR 190
Cdd:pfam18782   2 RMYPRTFYFNFNNKPIL-------YGRNKTYLCYEVERLDNGTWLpqhRGFFRNQAKYHAELCFLSWFCGNQLPpyqNYQ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025768795 191 ITCYLTWSPCPNCAQELAAFKKDHPDLVLRIYTSRLYFHWRRKYQEGLCSLWRSGIQVDVMDLPQFTDCWTNFVSSQS-P 269
Cdd:pfam18782  75 VTWYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQGeP 154

                         170       180
                  ....*....|....*....|..
gi 2025768795 270 FRPWNNLEKNSRCIQRRLQRIK 291
Cdd:pfam18782 155 FQPWDGLEENSRFLHRRLREIL 176
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 1-111 3.75e-61

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: 192.58  E-value: 3.75e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025768795   1 MLPPGEKYKITWYMSWSPCSECAAEVTRFLDTHRNLSLAIFSSRLYYFWKSDYQDKLRRLNQAGAQIAAMDFPEFEKCWN 80
Cdd:pfam18782  66 QLPPYQNYQVTWYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWE 145

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2025768795  81 KFVDNDGKSFRPWKRLKINFRNQDSTLWDIL 111
Cdd:pfam18782 146 NFVYNQGEPFQPWDGLEENSRFLHRRLREIL 176
APOBEC3 pfam18771
APOBEC3; APOBEC3 deaminases act as restriction factors in the innate response to retroviruses ...
 141-271 9.89e-56

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: 177.29  E-value: 9.89e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025768795 141 YYQRKTYLCYLLEPYNDQQPLKGCLQNKKDKHAEILFIDKMRSLELCQV---RITCYLTWSPCPNCAQELAAFKKDHPDL 217
Cdd:pfam18771   1 YYDRKAYLCYQLKGRNGSALDRGYFSNKKKRHAEIRFIDKIRSLDLDNIqcyRITCYITWSPCPNCAAELVDFISLNPHL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2025768795 218 VLRIYTSRLYFHWRRKYQEGLCSLWRSGIQVDVMDLPQFTDCWTNFVSSQS-PFR 271
Cdd:pfam18771  81 KLRIFASRLYYHWERSYKEGLQKLQRAGVSVAVMTLPEFQDCWEDFVDHQEePFR 135
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 2-112 8.97e-52

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: 168.16  E-value: 8.97e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025768795   2 LPPGEKYKITWYMSWSPCSECAAEVTRFLDTHRNLSLAIFSSRLYYFWKSDYQDKLRRLNQAGAQIAAMDFPEFEKCWNK 81
Cdd:pfam18772  64 LDPGQKYQVTWYVSWSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWEN 143

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2025768795  82 FVDNDGKSFRPWKRLKINFRNQDSTLWDILR 112
Cdd:pfam18772 144 FVDNQGRPFEPWEDLDENYEYLSRKLQEILR 174
NAD1 pfam18778
Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned ...
 1-111 3.88e-49

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: 161.68  E-value: 3.88e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025768795   1 MLPPGEKYKITWYMSWSPCSECAAEVTRFLDTHRNLSLAIFSSRLYYFWKSDYQDKLRRLNQAGAQIAAMDFPEFEKCWN 80
Cdd:pfam18778  65 LFDPSQCYTITWYLSWSPCPSCAAKLAEFLKAHPNVTLTIFAARLYYFEDPWNQEGLRSLASAGVTLSIMDYSDFEYCWE 144

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2025768795  81 KFVDNDGKSFRPWKRLKINFRNQDSTLWDIL 111
Cdd:pfam18778 145 NFVDNEGRPFVPWEDLEENSRYYHRKLQRIL 175
APOBEC_N pfam08210
APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. ...
 2-109 1.88e-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: 152.13  E-value: 1.88e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025768795   2 LPPGEKYKITWYMSWSPCSECAAEVTRFLDTHRNLSLAIFSSRLYYFWKSDYQDK--LRRLNQAGAQIAAMDFPEFEKCW 79
Cdd:pfam08210  61 LDPGSNYEVTWYVSWSPCNECASELAAFLSKHPNVRLRIFVSRLYYWEEPDYWNRegLRSLAQAGVQLRPMSYKDFEYCW 140

                          90       100       110
                  ....*....|....*....|....*....|
gi 2025768795  80 NKFVDNDGKSFRPWKRLKINFRNQDSTLWD 109
Cdd:pfam08210 141 NNFVDHDGEPFKPWDGLHENSVYLARKLQE 170
SNAD4 pfam18750
Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases ...
 162-262 1.46e-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: 147.79  E-value: 1.46e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025768795 162 KGCLQNKKDKHAEILFIDKMRSLELCQV---RITCYLTWSPCPNCAQELAAFKKDHPDLVLRIYTSRLYfHWRRKYQEGL 238
Cdd:pfam18750  14 RGYLSNEHEQHAEICFLENIRSRELDPSqryRVTWYLSWSPCPECAQKIAEFLAEHPNVTLTIFAARLY-HWDEDNRQGL 92

                          90       100
                  ....*....|....*....|....
gi 2025768795 239 CSLWRSGIQVDVMDLPQFTDCWTN 262
Cdd:pfam18750  93 RSLAQAGVTLQIMTLEDFEYCWKN 116
APOBEC_N pfam08210
APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. ...
 123-289 2.63e-43

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: 146.36  E-value: 2.63e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025768795 123 FYMQFSNRHRVqpvqqrrYYQRKTYLCYLLE--PYNDQQPLKGCLQNKKDK--HAEILFIDKMRSLELCQV---RITCYL 195
Cdd:pfam08210   1 FFFHFKNLPYA-------SGRHETYLCYEVKrdSGGLVVEDKGYLRNQAASslHAEERFLRWIHDLALDPGsnyEVTWYV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025768795 196 TWSPCPNCAQELAAFKKDHPDLVLRIYTSRLYFHWRRKYQ--EGLCSLWRSGIQVDVMDLPQFTDCWTNFVSSQS-PFRP 272
Cdd:pfam08210  74 SWSPCNECASELAAFLSKHPNVRLRIFVSRLYYWEEPDYWnrEGLRSLAQAGVQLRPMSYKDFEYCWNNFVDHDGePFKP 153

                         170
                  ....*....|....*..
gi 2025768795 273 WNNLEKNSRCIQRRLQR 289
Cdd:pfam08210 154 WDGLHENSVYLARKLQE 170
SNAD4 pfam18750
Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases ...
 2-81 1.85e-35

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: 124.30  E-value: 1.85e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025768795   2 LPPGEKYKITWYMSWSPCSECAAEVTRFLDTHRNLSLAIFSSRLYYfWKSDYQDKLRRLNQAGAQIAAMDFPEFEKCWNK 81
Cdd:pfam18750  38 LDPSQRYRVTWYLSWSPCPECAQKIAEFLAEHPNVTLTIFAARLYH-WDEDNRQGLRSLAQAGVTLQIMTLEDFEYCWKN 116
APOBEC_C pfam05240
APOBEC-like C-terminal domain; This domain is found at the C-termini of the Apolipoprotein B ...
 34-111 1.09e-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: 1.09e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2025768795  34 RNLSLAIFSSRLYYFWKSDYQDKLRRLNQAGAQIAAMDFPEFEKCWNKFVDNDGKSFRPWKRLKINFRNQDSTLWDIL 111
Cdd:pfam05240   1 PNVSLTIFAARLYYHWDPEYQQGLRRLVQAGAQVAIMSYKEFEYCWDNFVDNQGRPFQPWEGLEENSQLLSRRLQEIL 78
APOBEC_C pfam05240
APOBEC-like C-terminal domain; This domain is found at the C-termini of the Apolipoprotein B ...
 215-290 8.69e-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: 116.04  E-value: 8.69e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2025768795 215 PDLVLRIYTSRLYFHWRRKYQEGLCSLWRSGIQVDVMDLPQFTDCWTNFVSSQ-SPFRPWNNLEKNSRCIQRRLQRI 290
Cdd:pfam05240   1 PNVSLTIFAARLYYHWDPEYQQGLRRLVQAGAQVAIMSYKEFEYCWDNFVDNQgRPFQPWEGLEENSQLLSRRLQEI 77
APOBEC3 pfam18771
APOBEC3; APOBEC3 deaminases act as restriction factors in the innate response to retroviruses ...
 2-91 1.44e-29

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: 109.50  E-value: 1.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025768795   2 LPPGEKYKITWYMSWSPCSECAAEVTRFLDTHRNLSLAIFSSRLYYFWKSDYQDKLRRLNQAGAQIAAMDFPEFEKCWNK 81
Cdd:pfam18771  46 LDNIQCYRITCYITWSPCPNCAAELVDFISLNPHLKLRIFASRLYYHWERSYKEGLQKLQRAGVSVAVMTLPEFQDCWED 125

                          90
                  ....*....|
gi 2025768795  82 FVDNDGKSFR 91
Cdd:pfam18771 126 FVDHQEEPFR 135
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 138-236 1.75e-16

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: 73.91  E-value: 1.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025768795 138 QRRYYQRKTYLCYLLEpyNDQQPLKGCLQNKKD----KHAEILFIDKMRSLELCQVRITCYLT-----WSPCPNCAQELA 208
Cdd:cd01283    11 AYAPYSNFTVGAALLT--KDGRIFTGVNVENASygltLCAERTAIGKAVSEGLRRYLVTWAVSdeggvWSPCGACRQVLA 88

                          90       100
                  ....*....|....*....|....*...
gi 2025768795 209 AFKKdhpdlvlriytSRLYFHWRRKYQE 236
Cdd:cd01283    89 EFLP-----------SRLYIIIDNPKGE 105
APOBEC4_like pfam18774
APOBEC4-like -AID/APOBEC-deaminase; Cnidarian and Algal homologs of the APOBEC4-like AID ...
 167-264 4.82e-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: 73.37  E-value: 4.82e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025768795 167 NKKDKHAEILFIDKMRS-LELCQVRITCYLTWSPCPNCAQELAAFKKDHPDLVLRIYTSRLYFHWRRKYQEGLCSLWRSG 245
Cdd:pfam18774  31 NNCTEHAEVNFLENFRSeRPSRSCTITWYLSWSPCWECSGRILEFLSRHPNVTLGIYVARLFMHDDDRNRQGLRILQMNG 110

                          90
                  ....*....|....*....
gi 2025768795 246 IQVDVMDLPQFTDCWTNFV 264
Cdd:pfam18774 111 VTIQVMMNKDYCYCWKAFK 129
APOBEC4 pfam18775
APOBEC4; A member of the AID/APOBEC family of cytosine deaminases. The biological function of ...
 191-264 1.24e-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: 70.44  E-value: 1.24e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2025768795 191 ITCYLTWSPCPNCAQELAAFKKDHPDLVLRIYTSRLYFHWRRKYQEGLCSLWRSGIQVDVMDLPQFTDCWTNFV 264
Cdd:pfam18775   1 VTLYLSWSPCNECSEKIQEFLKKHPKVNLDIYFAQLYHTEEEDNRQGLRSLVEKGVTLSVMSGEDWIYCLRTFV 74
APOBEC4 pfam18775
APOBEC4; A member of the AID/APOBEC family of cytosine deaminases. The biological function of ...
 10-83 7.01e-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: 68.52  E-value: 7.01e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2025768795  10 ITWYMSWSPCSECAAEVTRFLDTHRNLSLAIFSSRLYYFWKSDYQDKLRRLNQAGAQIAAMDFPEFEKCWNKFV 83
Cdd:pfam18775   1 VTLYLSWSPCNECSEKIQEFLKKHPKVNLDIYFAQLYHTEEEDNRQGLRSLVEKGVTLSVMSGEDWIYCLRTFV 74
APOBEC4_like pfam18774
APOBEC4-like -AID/APOBEC-deaminase; Cnidarian and Algal homologs of the APOBEC4-like AID ...
 9-84 7.28e-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: 67.21  E-value: 7.28e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2025768795   9 KITWYMSWSPCSECAAEVTRFLDTHRNLSLAIFSSRLYYFWKSDYQDKLRRLNQAGAQIAAMDFPEFEKCWNKFVD 84
Cdd:pfam18774  55 TITWYLSWSPCWECSGRILEFLSRHPNVTLGIYVARLFMHDDDRNRQGLRILQMNGVTIQVMMNKDYCYCWKAFKN 130
APOBEC1 pfam18769
APOBEC1; APOBEC1 deaminates cytosine both in RNA and ssDNA and has roles in both mRNA editing ...
 10-70 2.37e-11

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: 59.44  E-value: 2.37e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2025768795  10 ITWYMSWSPCSECAAEVTRFLDTHRNLSLAIFSSRLyyFWKSDYQDK--LRRLNQAGAQIAAM 70
Cdd:pfam18769  41 ITWFLSWSPCGECSKAIGEFLSQHPNVTLVIYAARL--FKHLDIRNRqgLRDLAMSGVTIQIM 101
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 5-55 9.46e-04

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: 38.09  E-value: 9.46e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2025768795   5 GEKYKITWYMS-----WSPCSECAAEVTRFLDthrnlslaifsSRLYYFWKSDYQD 55
Cdd:cd01283    61 LRRYLVTWAVSdeggvWSPCGACRQVLAEFLP-----------SRLYIIIDNPKGE 105
 
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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