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Conserved domains on  [gi|1066543278|ref|NP_001332883|]
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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.
 10-189 3.03e-105

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: 307.37  E-value: 3.03e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278  10 ERMYQRTFYYHFENEPILYGRSYTWLCYEVKIRKDPSKLPWDTGVFRGQmyskPEHHAEMCFLSWFCGNQLPAHKRFQIT 89
Cdd:pfam18782   1 KRMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGTWLPQHRGFFRNQ----AKYHAELCFLSWFCGNQLPPYQNYQVT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278  90 WFVSWTPCPDCVAKVAEFLAEYPNVTLTISAARLYYYWETDYRRALCRLRQAGARVKIMDYEEFAYCWENCVYNGGQPFM 169
Cdd:pfam18782  77 WYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQGEPFQ 156

                         170       180
                  ....*....|....*....|
gi 1066543278 170 PWYKFDDNYAFLHHKLKEIL 189
Cdd:pfam18782 157 PWDGLEENSRFLHRRLREIL 176
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 191-377 3.06e-91

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: 271.55  E-value: 3.06e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278 191 HLMDPDTFTINFNNDLSVLGRRQTYLCYEVERLDNGTWVPMDQhwGFLCNQARnplhgvdsCHVELCFLSQVSSWQLDPA 270
Cdd:pfam18782   1 KRMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGTWLPQHR--GFFRNQAK--------YHAELCFLSWFCGNQLPPY 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278 271 QTYRVTWFISWSPCFSggCAEQVRAFLQENTHVRLCIFAARIYNY-DPLYQEALRMLRDAGAQVSIMTYEEFEYCWDTFV 349
Cdd:pfam18782  71 QNYQVTWYVSWSPCPE--CAGEVAEFLAEHPNVTLTIFAARLYYFwDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFV 148

                         170       180
                  ....*....|....*....|....*...
gi 1066543278 350 DRQGCPFQPWDGLDEHSQALSGRLRAIL 377
Cdd:pfam18782 149 YNQGEPFQPWDGLEENSRFLHRRLREIL 176
 
Name Accession Description Interval E-value
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 10-189 3.03e-105

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: 307.37  E-value: 3.03e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278  10 ERMYQRTFYYHFENEPILYGRSYTWLCYEVKIRKDPSKLPWDTGVFRGQmyskPEHHAEMCFLSWFCGNQLPAHKRFQIT 89
Cdd:pfam18782   1 KRMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGTWLPQHRGFFRNQ----AKYHAELCFLSWFCGNQLPPYQNYQVT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278  90 WFVSWTPCPDCVAKVAEFLAEYPNVTLTISAARLYYYWETDYRRALCRLRQAGARVKIMDYEEFAYCWENCVYNGGQPFM 169
Cdd:pfam18782  77 WYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQGEPFQ 156

                         170       180
                  ....*....|....*....|
gi 1066543278 170 PWYKFDDNYAFLHHKLKEIL 189
Cdd:pfam18782 157 PWDGLEENSRFLHRRLREIL 176
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 191-377 3.06e-91

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: 271.55  E-value: 3.06e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278 191 HLMDPDTFTINFNNDLSVLGRRQTYLCYEVERLDNGTWVPMDQhwGFLCNQARnplhgvdsCHVELCFLSQVSSWQLDPA 270
Cdd:pfam18782   1 KRMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGTWLPQHR--GFFRNQAK--------YHAELCFLSWFCGNQLPPY 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278 271 QTYRVTWFISWSPCFSggCAEQVRAFLQENTHVRLCIFAARIYNY-DPLYQEALRMLRDAGAQVSIMTYEEFEYCWDTFV 349
Cdd:pfam18782  71 QNYQVTWYVSWSPCPE--CAGEVAEFLAEHPNVTLTIFAARLYYFwDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFV 148

                         170       180
                  ....*....|....*....|....*...
gi 1066543278 350 DRQGCPFQPWDGLDEHSQALSGRLRAIL 377
Cdd:pfam18782 149 YNQGEPFQPWDGLEENSRFLHRRLREIL 176
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 8-158 1.43e-13

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: 66.60  E-value: 1.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278   8 PMERMYQRTFYYhfenepiLYGRSYTWLCYEVKirkdpsklpWDTGVFRGQMYSKPEH----HAEMCFLSWFCGNQlpaH 83
Cdd:cd01283     1 IEAALAAAEFAY-------APYSNFTVGAALLT---------KDGRIFTGVNVENASYgltlCAERTAIGKAVSEG---L 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278  84 KRFQITWFVS-----WTPCPDCvakvAEFLAEYpnvtltiSAARLYYYWETDYRralcrlrqagarvkimdyEEFAYCWE 158
Cdd:cd01283    62 RRYLVTWAVSdeggvWSPCGAC----RQVLAEF-------LPSRLYIIIDNPKG------------------EEFAYTLS 112
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 210-303 1.81e-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: 49.26  E-value: 1.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278 210 GRRQTYLCYEVERldngtwvPMDQHWGFLCNQARNPLHgvdsCHVELCFLSQVSSWQLdpaQTYRVTWFIS-----WSPC 284
Cdd:cd01283    15 YSNFTVGAALLTK-------DGRIFTGVNVENASYGLT----LCAERTAIGKAVSEGL---RRYLVTWAVSdeggvWSPC 80

                          90
                  ....*....|....*....
gi 1066543278 285 fsGGCAEQVRAFLQENTHV 303
Cdd:cd01283    81 --GACRQVLAEFLPSRLYI 97
 
Name Accession Description Interval E-value
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 10-189 3.03e-105

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: 307.37  E-value: 3.03e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278  10 ERMYQRTFYYHFENEPILYGRSYTWLCYEVKIRKDPSKLPWDTGVFRGQmyskPEHHAEMCFLSWFCGNQLPAHKRFQIT 89
Cdd:pfam18782   1 KRMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGTWLPQHRGFFRNQ----AKYHAELCFLSWFCGNQLPPYQNYQVT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278  90 WFVSWTPCPDCVAKVAEFLAEYPNVTLTISAARLYYYWETDYRRALCRLRQAGARVKIMDYEEFAYCWENCVYNGGQPFM 169
Cdd:pfam18782  77 WYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQGEPFQ 156

                         170       180
                  ....*....|....*....|
gi 1066543278 170 PWYKFDDNYAFLHHKLKEIL 189
Cdd:pfam18782 157 PWDGLEENSRFLHRRLREIL 176
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 12-190 5.29e-93

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: 276.02  E-value: 5.29e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278  12 MYQRTFYYHFENEPILYGRSYTWLCYEVKiRKDPSKLPWDTGVFRGQmyskPEHHAEMCFLSWFCGNQLPAHKRFQITWF 91
Cdd:pfam18772   1 MDPKTFKFQFKNVPYASGRNKTYLCYEVE-TRSGSDLSPDRGYLRNQ----AGCHAELCFLSWILPWQLDPGQKYQVTWY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278  92 VSWTPCPDCVAKVAEFLAEYPNVTLTISAARLYYYWETDYRRALCRLRQAGARVKIMDYEEFAYCWENCVYNGGQPFMPW 171
Cdd:pfam18772  76 VSWSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDNQGRPFEPW 155

                         170
                  ....*....|....*....
gi 1066543278 172 YKFDDNYAFLHHKLKEILR 190
Cdd:pfam18772 156 EDLDENYEYLSRKLQEILR 174
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 191-377 3.06e-91

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: 271.55  E-value: 3.06e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278 191 HLMDPDTFTINFNNDLSVLGRRQTYLCYEVERLDNGTWVPMDQhwGFLCNQARnplhgvdsCHVELCFLSQVSSWQLDPA 270
Cdd:pfam18782   1 KRMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGTWLPQHR--GFFRNQAK--------YHAELCFLSWFCGNQLPPY 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278 271 QTYRVTWFISWSPCFSggCAEQVRAFLQENTHVRLCIFAARIYNY-DPLYQEALRMLRDAGAQVSIMTYEEFEYCWDTFV 349
Cdd:pfam18782  71 QNYQVTWYVSWSPCPE--CAGEVAEFLAEHPNVTLTIFAARLYYFwDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFV 148

                         170       180
                  ....*....|....*....|....*...
gi 1066543278 350 DRQGCPFQPWDGLDEHSQALSGRLRAIL 377
Cdd:pfam18782 149 YNQGEPFQPWDGLEENSRFLHRRLREIL 176
NAD1 pfam18778
Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned ...
 10-189 8.11e-81

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: 244.88  E-value: 8.11e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278  10 ERMYQRTFYYHFENEPILYGRSYTWLCYEVKiRKDPSKLPWdtGVFRGQmysKPEHHAEMCFLSWFCGNQL-PAHKRFQI 88
Cdd:pfam18778   1 ERMSPETFKFQFKNVEYASGRNKTLLCYEVK-RGNSSSLWR--GHLRNE---NSGCHAEICFLRWFSSWRLfDPSQCYTI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278  89 TWFVSWTPCPDCVAKVAEFLAEYPNVTLTISAARLYYYWETDYRRALCRLRQAGARVKIMDYEEFAYCWENCVYNGGQPF 168
Cdd:pfam18778  75 TWYLSWSPCPSCAAKLAEFLKAHPNVTLTIFAARLYYFEDPWNQEGLRSLASAGVTLSIMDYSDFEYCWENFVDNEGRPF 154

                         170       180
                  ....*....|....*....|.
gi 1066543278 169 MPWYKFDDNYAFLHHKLKEIL 189
Cdd:pfam18778 155 VPWEDLEENSRYYHRKLQRIL 175
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 193-378 5.13e-79

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: 240.19  E-value: 5.13e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278 193 MDPDTFTINFNNDLSVLGRRQTYLCYEVERLDNGtwvPMDQHWGFLCNQARnplhgvdsCHVELCFLSQVSSWQLDPAQT 272
Cdd:pfam18772   1 MDPKTFKFQFKNVPYASGRNKTYLCYEVETRSGS---DLSPDRGYLRNQAG--------CHAELCFLSWILPWQLDPGQK 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278 273 YRVTWFISWSPCFSggCAEQVRAFLQENTHVRLCIFAARIYNY-DPLYQEALRMLRDAGAQVSIMTYEEFEYCWDTFVDR 351
Cdd:pfam18772  70 YQVTWYVSWSPCPD--CARKLAEFLARHPNLSLTIFAARLYFFwEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDN 147

                         170       180
                  ....*....|....*....|....*..
gi 1066543278 352 QGCPFQPWDGLDEHSQALSGRLRAILQ 378
Cdd:pfam18772 148 QGRPFEPWEDLDENYEYLSRKLQEILR 174
NAD1 pfam18778
Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned ...
 191-377 3.31e-77

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: 235.64  E-value: 3.31e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278 191 HLMDPDTFTINFNNDLSVLGRRQTYLCYEVERLDngtwvPMDQHWGFLCNQARNplhgvdsCHVELCFLSQVSSWQL-DP 269
Cdd:pfam18778   1 ERMSPETFKFQFKNVEYASGRNKTLLCYEVKRGN-----SSSLWRGHLRNENSG-------CHAEICFLRWFSSWRLfDP 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278 270 AQTYRVTWFISWSPCFSggCAEQVRAFLQENTHVRLCIFAARIYNY-DPLYQEALRMLRDAGAQVSIMTYEEFEYCWDTF 348
Cdd:pfam18778  69 SQCYTITWYLSWSPCPS--CAAKLAEFLKAHPNVTLTIFAARLYYFeDPWNQEGLRSLASAGVTLSIMDYSDFEYCWENF 146

                         170       180
                  ....*....|....*....|....*....
gi 1066543278 349 VDRQGCPFQPWDGLDEHSQALSGRLRAIL 377
Cdd:pfam18778 147 VDNEGRPFVPWEDLEENSRYYHRKLQRIL 175
APOBEC_N pfam08210
APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. ...
 198-374 1.84e-60

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: 192.58  E-value: 1.84e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278 198 FTINFNNDLSVLGRRQTYLCYEVERLDNGTWVpmdQHWGFLCNQARNplhgvdSCHVELCFLSQVSSWQLDPAQTYRVTW 277
Cdd:pfam08210   1 FFFHFKNLPYASGRHETYLCYEVKRDSGGLVV---EDKGYLRNQAAS------SLHAEERFLRWIHDLALDPGSNYEVTW 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278 278 FISWSPCFSggCAEQVRAFLQENTHVRLCIFAARIYN-YDPLYQ--EALRMLRDAGAQVSIMTYEEFEYCWDTFVDRQGC 354
Cdd:pfam08210  72 YVSWSPCNE--CASELAAFLSKHPNVRLRIFVSRLYYwEEPDYWnrEGLRSLAQAGVQLRPMSYKDFEYCWNNFVDHDGE 149

                         170       180
                  ....*....|....*....|
gi 1066543278 355 PFQPWDGLDEHSQALSGRLR 374
Cdd:pfam08210 150 PFKPWDGLHENSVYLARKLQ 169
APOBEC_N pfam08210
APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. ...
 17-187 2.87e-56

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: 181.79  E-value: 2.87e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278  17 FYYHFENEPILYGRSYTWLCYEVKIRKDPSKLpWDTGVFRGQMYSKPehHAEMCFLSWFCGNQLPAHKRFQITWFVSWTP 96
Cdd:pfam08210   1 FFFHFKNLPYASGRHETYLCYEVKRDSGGLVV-EDKGYLRNQAASSL--HAEERFLRWIHDLALDPGSNYEVTWYVSWSP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278  97 CPDCVAKVAEFLAEYPNVTLTISAARLYYYWETDY--RRALCRLRQAGARVKIMDYEEFAYCWENCVYNGGQPFMPWYKF 174
Cdd:pfam08210  78 CNECASELAAFLSKHPNVRLRIFVSRLYYWEEPDYwnREGLRSLAQAGVQLRPMSYKDFEYCWNNFVDHDGEPFKPWDGL 157

                         170
                  ....*....|...
gi 1066543278 175 DDNYAFLHHKLKE 187
Cdd:pfam08210 158 HENSVYLARKLQE 170
SNAD4 pfam18750
Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases ...
 39-159 3.10e-53

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: 172.06  E-value: 3.10e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278  39 VKIRKDPSKLPWDTGVFRGqmysKPEHHAEMCFLSWFCGNQLPAHKRFQITWFVSWTPCPDCVAKVAEFLAEYPNVTLTI 118
Cdd:pfam18750   1 YEIKWGNGSKIWQRGYLSN----EHEQHAEICFLENIRSRELDPSQRYRVTWYLSWSPCPECAQKIAEFLAEHPNVTLTI 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1066543278 119 SAARLyYYWETDYRRALCRLRQAGARVKIMDYEEFAYCWEN 159
Cdd:pfam18750  77 FAARL-YHWDEDNRQGLRSLAQAGVTLQIMTLEDFEYCWKN 116
SNAD4 pfam18750
Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases ...
 243-347 1.51e-49

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: 162.82  E-value: 1.51e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278 243 RNPLHGVDSCHVELCFLSQVSSWQLDPAQTYRVTWFISWSPCFSggCAEQVRAFLQENTHVRLCIFAARIYNYDPLYQEA 322
Cdd:pfam18750  14 RGYLSNEHEQHAEICFLENIRSRELDPSQRYRVTWYLSWSPCPE--CAQKIAEFLAEHPNVTLTIFAARLYHWDEDNRQG 91

                          90       100
                  ....*....|....*....|....*
gi 1066543278 323 LRMLRDAGAQVSIMTYEEFEYCWDT 347
Cdd:pfam18750  92 LRSLAQAGVTLQIMTLEDFEYCWKN 116
APOBEC_C pfam05240
APOBEC-like C-terminal domain; This domain is found at the C-termini of the Apolipoprotein B ...
 302-377 2.29e-38

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: 132.22  E-value: 2.29e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1066543278 302 HVRLCIFAARIYN-YDPLYQEALRMLRDAGAQVSIMTYEEFEYCWDTFVDRQGCPFQPWDGLDEHSQALSGRLRAIL 377
Cdd:pfam05240   2 NVSLTIFAARLYYhWDPEYQQGLRRLVQAGAQVAIMSYKEFEYCWDNFVDNQGRPFQPWEGLEENSQLLSRRLQEIL 78
APOBEC3 pfam18771
APOBEC3; APOBEC3 deaminases act as restriction factors in the innate response to retroviruses ...
 211-357 2.26e-36

APOBEC3; APOBEC3 deaminases act as restriction factors in the innate response to retroviruses and various retroelements.


Pssm-ID: 465862 [Multi-domain]  Cd Length: 135  Bit Score: 129.14  E-value: 2.26e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278 211 RRQTYLCYEVERLDNGTWVPmdqhwGFLCNQARNplhgvdscHVELCFLSQVSSWQLDPAQTYRVTWFISWSPCFSggCA 290
Cdd:pfam18771   3 DRKAYLCYQLKGRNGSALDR-----GYFSNKKKR--------HAEIRFIDKIRSLDLDNIQCYRITCYITWSPCPN--CA 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1066543278 291 EQVRAFLQENTHVRLCIFAARIYNYD-PLYQEALRMLRDAGAQVSIMTYEEFEYCWDTFVDRQGCPFQ 357
Cdd:pfam18771  68 AELVDFISLNPHLKLRIFASRLYYHWeRSYKEGLQKLQRAGVSVAVMTLPEFQDCWEDFVDHQEEPFR 135
APOBEC_C pfam05240
APOBEC-like C-terminal domain; This domain is found at the C-termini of the Apolipoprotein B ...
 112-189 2.43e-36

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: 126.83  E-value: 2.43e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1066543278 112 PNVTLTISAARLYYYWETDYRRALCRLRQAGARVKIMDYEEFAYCWENCVYNGGQPFMPWYKFDDNYAFLHHKLKEIL 189
Cdd:pfam05240   1 PNVSLTIFAARLYYHWDPEYQQGLRRLVQAGAQVAIMSYKEFEYCWDNFVDNQGRPFQPWEGLEENSQLLSRRLQEIL 78
APOBEC3 pfam18771
APOBEC3; APOBEC3 deaminases act as restriction factors in the innate response to retroviruses ...
 33-168 5.62e-30

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: 112.20  E-value: 5.62e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278  33 TWLCYEVKIRKDpskLPWDTGVFRGQMYSkpehHAEMCFLSWFCGNQLPAHKRFQITWFVSWTPCPDCVAKVAEFLAEYP 112
Cdd:pfam18771   6 AYLCYQLKGRNG---SALDRGYFSNKKKR----HAEIRFIDKIRSLDLDNIQCYRITCYITWSPCPNCAAELVDFISLNP 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1066543278 113 NVTLTISAARLYYYWETDYRRALCRLRQAGARVKIMDYEEFAYCWENCVYNGGQPF 168
Cdd:pfam18771  79 HLKLRIFASRLYYHWERSYKEGLQKLQRAGVSVAVMTLPEFQDCWEDFVDHQEEPF 134
APOBEC4_like pfam18774
APOBEC4-like -AID/APOBEC-deaminase; Cnidarian and Algal homologs of the APOBEC4-like AID ...
 46-159 7.24e-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: 79.15  E-value: 7.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278  46 SKLPWDTGVFRGQMYSKPEH-HAEMCFLSWFCGNQlpAHKRFQITWFVSWTPCPDCVAKVAEFLAEYPNVTLTISAARLY 124
Cdd:pfam18774  15 YEIQWGRGTIWRNWTENNCTeHAEVNFLENFRSER--PSRSCTITWYLSWSPCWECSGRILEFLSRHPNVTLGIYVARLF 92

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1066543278 125 YYWETDYRRALCRLRQAGARVKIMDYEEFAYCWEN 159
Cdd:pfam18774  93 MHDDDRNRQGLRILQMNGVTIQVMMNKDYCYCWKA 127
APOBEC4 pfam18775
APOBEC4; A member of the AID/APOBEC family of cytosine deaminases. The biological function of ...
 88-157 4.98e-16

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: 71.98  E-value: 4.98e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278  88 ITWFVSWTPCPDCVAKVAEFLAEYPNVTLTISAARLYYYWETDYRRALCRLRQAGARVKIMDYEEFAYCW 157
Cdd:pfam18775   1 VTLYLSWSPCNECSEKIQEFLKKHPKVNLDIYFAQLYHTEEEDNRQGLRSLVEKGVTLSVMSGEDWIYCL 70
APOBEC4 pfam18775
APOBEC4; A member of the AID/APOBEC family of cytosine deaminases. The biological function of ...
 275-349 7.63e-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: 7.63e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1066543278 275 VTWFISWSPCfsGGCAEQVRAFLQENTHVRLCIFAARIYNYDPLY-QEALRMLRDAGAQVSIMTYEEFEYCWDTFV 349
Cdd:pfam18775   1 VTLYLSWSPC--NECSEKIQEFLKKHPKVNLDIYFAQLYHTEEEDnRQGLRSLVEKGVTLSVMSGEDWIYCLRTFV 74
APOBEC4_like pfam18774
APOBEC4-like -AID/APOBEC-deaminase; Cnidarian and Algal homologs of the APOBEC4-like AID ...
 252-350 6.18e-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: 67.98  E-value: 6.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278 252 CHVELCFLSQVSSWQldPAQTYRVTWFISWSPCfsGGCAEQVRAFLQENTHVRLCIFAARIYNY-DPLYQEALRMLRDAG 330
Cdd:pfam18774  35 EHAEVNFLENFRSER--PSRSCTITWYLSWSPC--WECSGRILEFLSRHPNVTLGIYVARLFMHdDDRNRQGLRILQMNG 110

                          90       100
                  ....*....|....*....|
gi 1066543278 331 AQVSIMTYEEFEYCWDTFVD 350
Cdd:pfam18774 111 VTIQVMMNKDYCYCWKAFKN 130
APOBEC1 pfam18769
APOBEC1; APOBEC1 deaminates cytosine both in RNA and ssDNA and has roles in both mRNA editing ...
 63-148 7.91e-14

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: 66.76  E-value: 7.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278  63 PEHHAEMCFL-SWFCGNQLPAHKRFQITWFVSWTPCPDCVAKVAEFLAEYPNVTLTISAARLYYYWETDYRRALCRLRQA 141
Cdd:pfam18769  15 TTQHAEVNFLeKFFSERHFDPSVSCSITWFLSWSPCGECSKAIGEFLSQHPNVTLVIYAARLFKHLDIRNRQGLRDLAMS 94


                  ....*..
gi 1066543278 142 GARVKIM 148
Cdd:pfam18769  95 GVTIQIM 101
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 8-158 1.43e-13

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: 66.60  E-value: 1.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278   8 PMERMYQRTFYYhfenepiLYGRSYTWLCYEVKirkdpsklpWDTGVFRGQMYSKPEH----HAEMCFLSWFCGNQlpaH 83
Cdd:cd01283     1 IEAALAAAEFAY-------APYSNFTVGAALLT---------KDGRIFTGVNVENASYgltlCAERTAIGKAVSEG---L 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278  84 KRFQITWFVS-----WTPCPDCvakvAEFLAEYpnvtltiSAARLYYYWETDYRralcrlrqagarvkimdyEEFAYCWE 158
Cdd:cd01283    62 RRYLVTWAVSdeggvWSPCGAC----RQVLAEF-------LPSRLYIIIDNPKG------------------EEFAYTLS 112
APOBEC1 pfam18769
APOBEC1; APOBEC1 deaminates cytosine both in RNA and ssDNA and has roles in both mRNA editing ...
 240-336 2.79e-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: 59.83  E-value: 2.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278 240 NQARNPlhgvdSCHVELCFLSQVSS-WQLDPAQTYRVTWFISWSPCfsGGCAEQVRAFLQENTHVRLCIFAARIYNY-DP 317
Cdd:pfam18769  10 NCGNNT-----TQHAEVNFLEKFFSeRHFDPSVSCSITWFLSWSPC--GECSKAIGEFLSQHPNVTLVIYAARLFKHlDI 82

                          90
                  ....*....|....*....
gi 1066543278 318 LYQEALRMLRDAGAQVSIM 336
Cdd:pfam18769  83 RNRQGLRDLAMSGVTIQIM 101
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 210-303 1.81e-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: 49.26  E-value: 1.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1066543278 210 GRRQTYLCYEVERldngtwvPMDQHWGFLCNQARNPLHgvdsCHVELCFLSQVSSWQLdpaQTYRVTWFIS-----WSPC 284
Cdd:cd01283    15 YSNFTVGAALLTK-------DGRIFTGVNVENASYGLT----LCAERTAIGKAVSEGL---RRYLVTWAVSdeggvWSPC 80

                          90
                  ....*....|....*....
gi 1066543278 285 fsGGCAEQVRAFLQENTHV 303
Cdd:cd01283    81 --GACRQVLAEFLPSRLYI 97
 
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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