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Conserved domains on  [gi|1159731399|ref|NP_001336365|]
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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.
 184-368 9.25e-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: 270.01  E-value: 9.25e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399 184 HSMDPPTFTFNFNNEPWVRGRHETYLCYEVERMHNDTWVLlnQRRGFLCNQAphkhgfleGRHAELCFLDVIPFWKLDLD 263
Cdd:pfam18782   1 KRMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGTWLP--QHRGFFRNQA--------KYHAELCFLSWFCGNQLPPY 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399 264 QDYRVTCFTSWSPCFSCAQEMAKFISKNKHVSLCIFTARIYDDQGR-CQEGLRTLAEAGAKISIMTYSEFKHCWDTFVDH 342
Cdd:pfam18782  71 QNYQVTWYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPdYQEALRRLRQAGARVKIMDYEEFEYCWENFVYN 150

                         170       180
                  ....*....|....*....|....*.
gi 1159731399 343 QGCPFQPWDGLDEHSQDLSGRLRAIL 368
Cdd:pfam18782 151 QGEPFQPWDGLEENSRFLHRRLREIL 176
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 1-183 2.34e-86

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: 258.68  E-value: 2.34e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399   1 MYRDTFSYNFYNRPILSRRNTVWLCYEVKTKGPSrpplDAKIFRGQVYSELKYHPEMRFFHWFSKWrKLHRDQEYEVTWY 80
Cdd:pfam18772   1 MDPKTFKFQFKNVPYASGRNKTYLCYEVETRSGS----DLSPDRGYLRNQAGCHAELCFLSWILPW-QLDPGQKYQVTWY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399  81 ISWSPCTKCTRDMATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSLCQKrdgpRATMKIMNYDEFQHCWSKFVYSQREL 160
Cdd:pfam18772  76 VSWSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRA----GAQLKIMDYQDFEYCWENFVDNQGRP 151

                         170       180
                  ....*....|....*....|...
gi 1159731399 161 FEPWNNLPKYYILLHIMLGEILR 183
Cdd:pfam18772 152 FEPWEDLDENYEYLSRKLQEILR 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.
 184-368 9.25e-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: 270.01  E-value: 9.25e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399 184 HSMDPPTFTFNFNNEPWVRGRHETYLCYEVERMHNDTWVLlnQRRGFLCNQAphkhgfleGRHAELCFLDVIPFWKLDLD 263
Cdd:pfam18782   1 KRMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGTWLP--QHRGFFRNQA--------KYHAELCFLSWFCGNQLPPY 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399 264 QDYRVTCFTSWSPCFSCAQEMAKFISKNKHVSLCIFTARIYDDQGR-CQEGLRTLAEAGAKISIMTYSEFKHCWDTFVDH 342
Cdd:pfam18782  71 QNYQVTWYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPdYQEALRRLRQAGARVKIMDYEEFEYCWENFVYN 150

                         170       180
                  ....*....|....*....|....*.
gi 1159731399 343 QGCPFQPWDGLDEHSQDLSGRLRAIL 368
Cdd:pfam18782 151 QGEPFQPWDGLEENSRFLHRRLREIL 176
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 1-183 2.34e-86

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: 258.68  E-value: 2.34e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399   1 MYRDTFSYNFYNRPILSRRNTVWLCYEVKTKGPSrpplDAKIFRGQVYSELKYHPEMRFFHWFSKWrKLHRDQEYEVTWY 80
Cdd:pfam18772   1 MDPKTFKFQFKNVPYASGRNKTYLCYEVETRSGS----DLSPDRGYLRNQAGCHAELCFLSWILPW-QLDPGQKYQVTWY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399  81 ISWSPCTKCTRDMATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSLCQKrdgpRATMKIMNYDEFQHCWSKFVYSQREL 160
Cdd:pfam18772  76 VSWSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRA----GAQLKIMDYQDFEYCWENFVDNQGRP 151

                         170       180
                  ....*....|....*....|...
gi 1159731399 161 FEPWNNLPKYYILLHIMLGEILR 183
Cdd:pfam18772 152 FEPWEDLDENYEYLSRKLQEILR 174
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 1-122 1.78e-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: 66.21  E-value: 1.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399   1 MYRDTFSYNFYnrpilsrRNTVWLCYEVKTKGpsrppldaKIFRGQVYSELKY----HPEMRFFHWFSKWRklhrDQEYE 76
Cdd:cd01283     5 LAAAEFAYAPY-------SNFTVGAALLTKDG--------RIFTGVNVENASYgltlCAERTAIGKAVSEG----LRRYL 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1159731399  77 VTWYIS-----WSPCTKCTRDMATFLAedpkvtltifvARLYYFWDPDYQE 122
Cdd:cd01283    66 VTWAVSdeggvWSPCGACRQVLAEFLP-----------SRLYIIIDNPKGE 105
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 200-291 8.89e-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: 47.34  E-value: 8.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399 200 WVRGRHETYLCYEVERmhNDTWVllnqrRGFLCNQAphkhGFLEGRHAELCFLDVIPfwkLDLDQDYRVTCFTS-----W 274
Cdd:cd01283    12 YAPYSNFTVGAALLTK--DGRIF-----TGVNVENA----SYGLTLCAERTAIGKAV---SEGLRRYLVTWAVSdeggvW 77

                          90
                  ....*....|....*..
gi 1159731399 275 SPCFSCAQEMAKFISKN 291
Cdd:cd01283    78 SPCGACRQVLAEFLPSR 94
 
Name Accession Description Interval E-value
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 184-368 9.25e-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: 270.01  E-value: 9.25e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399 184 HSMDPPTFTFNFNNEPWVRGRHETYLCYEVERMHNDTWVLlnQRRGFLCNQAphkhgfleGRHAELCFLDVIPFWKLDLD 263
Cdd:pfam18782   1 KRMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGTWLP--QHRGFFRNQA--------KYHAELCFLSWFCGNQLPPY 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399 264 QDYRVTCFTSWSPCFSCAQEMAKFISKNKHVSLCIFTARIYDDQGR-CQEGLRTLAEAGAKISIMTYSEFKHCWDTFVDH 342
Cdd:pfam18782  71 QNYQVTWYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPdYQEALRRLRQAGARVKIMDYEEFEYCWENFVYN 150

                         170       180
                  ....*....|....*....|....*.
gi 1159731399 343 QGCPFQPWDGLDEHSQDLSGRLRAIL 368
Cdd:pfam18782 151 QGEPFQPWDGLEENSRFLHRRLREIL 176
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 1-183 2.34e-86

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: 258.68  E-value: 2.34e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399   1 MYRDTFSYNFYNRPILSRRNTVWLCYEVKTKGPSrpplDAKIFRGQVYSELKYHPEMRFFHWFSKWrKLHRDQEYEVTWY 80
Cdd:pfam18772   1 MDPKTFKFQFKNVPYASGRNKTYLCYEVETRSGS----DLSPDRGYLRNQAGCHAELCFLSWILPW-QLDPGQKYQVTWY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399  81 ISWSPCTKCTRDMATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSLCQKrdgpRATMKIMNYDEFQHCWSKFVYSQREL 160
Cdd:pfam18772  76 VSWSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRA----GAQLKIMDYQDFEYCWENFVDNQGRP 151

                         170       180
                  ....*....|....*....|...
gi 1159731399 161 FEPWNNLPKYYILLHIMLGEILR 183
Cdd:pfam18772 152 FEPWEDLDENYEYLSRKLQEILR 174
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 186-369 1.53e-82

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: 249.05  E-value: 1.53e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399 186 MDPPTFTFNFNNEPWVRGRHETYLCYEVERMHNDTwvlLNQRRGFLCNQAphkhgfleGRHAELCFLDVIPFWKLDLDQD 265
Cdd:pfam18772   1 MDPKTFKFQFKNVPYASGRNKTYLCYEVETRSGSD---LSPDRGYLRNQA--------GCHAELCFLSWILPWQLDPGQK 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399 266 YRVTCFTSWSPCFSCAQEMAKFISKNKHVSLCIFTARIY-DDQGRCQEGLRTLAEAGAKISIMTYSEFKHCWDTFVDHQG 344
Cdd:pfam18772  70 YQVTWYVSWSPCPDCARKLAEFLARHPNLSLTIFAARLYfFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDNQG 149

                         170       180
                  ....*....|....*....|....*
gi 1159731399 345 CPFQPWDGLDEHSQDLSGRLRAILQ 369
Cdd:pfam18772 150 RPFEPWEDLDENYEYLSRKLQEILR 174
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 1-182 1.64e-81

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: 246.51  E-value: 1.64e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399   1 MYRDTFSYNFYNRPILSRRNTVWLCYEVKTKGPSRPPldaKIFRGQVYSELKYHPEMRFFHWFsKWRKLHRDQEYEVTWY 80
Cdd:pfam18782   3 MYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGTWL---PQHRGFFRNQAKYHAELCFLSWF-CGNQLPPYQNYQVTWY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399  81 ISWSPCTKCTRDMATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSLCQKrdgpRATMKIMNYDEFQHCWSKFVYSQREL 160
Cdd:pfam18782  79 VSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQA----GARVKIMDYEEFEYCWENFVYNQGEP 154

                         170       180
                  ....*....|....*....|..
gi 1159731399 161 FEPWNNLPKYYILLHIMLGEIL 182
Cdd:pfam18782 155 FQPWDGLEENSRFLHRRLREIL 176
NAD1 pfam18778
Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned ...
 184-368 1.42e-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: 236.41  E-value: 1.42e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399 184 HSMDPPTFTFNFNNEPWVRGRHETYLCYEVERmHNDTwvllNQRRGFLCNQAPhkhgfleGRHAELCFLDVIPFWKL-DL 262
Cdd:pfam18778   1 ERMSPETFKFQFKNVEYASGRNKTLLCYEVKR-GNSS----SLWRGHLRNENS-------GCHAEICFLRWFSSWRLfDP 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399 263 DQDYRVTCFTSWSPCFSCAQEMAKFISKNKHVSLCIFTARIYDDQGR-CQEGLRTLAEAGAKISIMTYSEFKHCWDTFVD 341
Cdd:pfam18778  69 SQCYTITWYLSWSPCPSCAAKLAEFLKAHPNVTLTIFAARLYYFEDPwNQEGLRSLASAGVTLSIMDYSDFEYCWENFVD 148

                         170       180
                  ....*....|....*....|....*..
gi 1159731399 342 HQGCPFQPWDGLDEHSQDLSGRLRAIL 368
Cdd:pfam18778 149 NEGRPFVPWEDLEENSRYYHRKLQRIL 175
NAD1 pfam18778
Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned ...
 1-182 2.26e-75

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: 230.63  E-value: 2.26e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399   1 MYRDTFSYNFYNRPILSRRNTVWLCYEVKTKGPSRPPLdaKIFRGQvysELKYHPEMRFFHWFSKWRKLHRDQEYEVTWY 80
Cdd:pfam18778   3 MSPETFKFQFKNVEYASGRNKTLLCYEVKRGNSSSLWR--GHLRNE---NSGCHAEICFLRWFSSWRLFDPSQCYTITWY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399  81 ISWSPCTKCTRDMATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSLCQKrdgpRATMKIMNYDEFQHCWSKFVYSQREL 160
Cdd:pfam18778  78 LSWSPCPSCAAKLAEFLKAHPNVTLTIFAARLYYFEDPWNQEGLRSLASA----GVTLSIMDYSDFEYCWENFVDNEGRP 153

                         170       180
                  ....*....|....*....|..
gi 1159731399 161 FEPWNNLPKYYILLHIMLGEIL 182
Cdd:pfam18778 154 FVPWEDLEENSRYYHRKLQRIL 175
APOBEC_N pfam08210
APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. ...
 191-365 2.73e-61

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: 194.51  E-value: 2.73e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399 191 FTFNFNNEPWVRGRHETYLCYEVERMHNDTWVLLnqrRGFLCNQAphkhgfLEGRHAELCFLDVIPFWKLDLDQDYRVTC 270
Cdd:pfam08210   1 FFFHFKNLPYASGRHETYLCYEVKRDSGGLVVED---KGYLRNQA------ASSLHAEERFLRWIHDLALDPGSNYEVTW 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399 271 FTSWSPCFSCAQEMAKFISKNKHVSLCIFTARIY---DDQGRCQEGLRTLAEAGAKISIMTYSEFKHCWDTFVDHQGCPF 347
Cdd:pfam08210  72 YVSWSPCNECASELAAFLSKHPNVRLRIFVSRLYyweEPDYWNREGLRSLAQAGVQLRPMSYKDFEYCWNNFVDHDGEPF 151

                         170
                  ....*....|....*...
gi 1159731399 348 QPWDGLDEHSQDLSGRLR 365
Cdd:pfam08210 152 KPWDGLHENSVYLARKLQ 169
SNAD4 pfam18750
Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases ...
 227-338 6.14e-46

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: 153.19  E-value: 6.14e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399 227 RRGFLCNQAphkhgfleGRHAELCFLDVIPFWKLDLDQDYRVTCFTSWSPCFSCAQEMAKFISKNKHVSLCIFTARIYDD 306
Cdd:pfam18750  13 QRGYLSNEH--------EQHAEICFLENIRSRELDPSQRYRVTWYLSWSPCPECAQKIAEFLAEHPNVTLTIFAARLYHW 84

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1159731399 307 QGRCQEGLRTLAEAGAKISIMTYSEFKHCWDT 338
Cdd:pfam18750  85 DEDNRQGLRSLAQAGVTLQIMTLEDFEYCWKN 116
APOBEC_N pfam08210
APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. ...
 6-167 9.19e-46

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: 154.45  E-value: 9.19e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399   6 FSYNFYNRPILSRRNTVWLCYEVKTKGPSRPPLDAKIFRGQVYSELkyHPEMRFFHWFSKWrKLHRDQEYEVTWYISWSP 85
Cdd:pfam08210   1 FFFHFKNLPYASGRHETYLCYEVKRDSGGLVVEDKGYLRNQAASSL--HAEERFLRWIHDL-ALDPGSNYEVTWYVSWSP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399  86 CTKCTRDMATFLAEDPKVTLTIFVARLYYFWDPDYQ--EALRSLCQKrdgpRATMKIMNYDEFQHCWSKFVYSQRELFEP 163
Cdd:pfam08210  78 CNECASELAAFLSKHPNVRLRIFVSRLYYWEEPDYWnrEGLRSLAQA----GVQLRPMSYKDFEYCWNNFVDHDGEPFKP 153


                  ....
gi 1159731399 164 WNNL 167
Cdd:pfam08210 154 WDGL 157
SNAD4 pfam18750
Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases ...
 26-152 2.41e-45

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: 151.64  E-value: 2.41e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399  26 YEVKTKGPSRPpldakIFRGQVYSELKYHPEMRFFHWFSkWRKLHRDQEYEVTWYISWSPCTKCTRDMATFLAEDPKVTL 105
Cdd:pfam18750   1 YEIKWGNGSKI-----WQRGYLSNEHEQHAEICFLENIR-SRELDPSQRYRVTWYLSWSPCPECAQKIAEFLAEHPNVTL 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1159731399 106 TIFVARLYYfWDPDYQEALRSLCQKrdgpRATMKIMNYDEFQHCWSK 152
Cdd:pfam18750  75 TIFAARLYH-WDEDNRQGLRSLAQA----GVTLQIMTLEDFEYCWKN 116
APOBEC3 pfam18771
APOBEC3; APOBEC3 deaminases act as restriction factors in the innate response to retroviruses ...
 207-348 1.17e-40

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: 139.93  E-value: 1.17e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399 207 TYLCYEVERMHNDTWVllnqrRGFLCNQAPhkhgflegRHAELCFLDVIPFWKLDLDQDYRVTCFTSWSPCFSCAQEMAK 286
Cdd:pfam18771   6 AYLCYQLKGRNGSALD-----RGYFSNKKK--------RHAEIRFIDKIRSLDLDNIQCYRITCYITWSPCPNCAAELVD 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1159731399 287 FISKNKHVSLCIFTARIYDDQGRC-QEGLRTLAEAGAKISIMTYSEFKHCWDTFVDHQGCPFQ 348
Cdd:pfam18771  73 FISLNPHLKLRIFASRLYYHWERSyKEGLQKLQRAGVSVAVMTLPEFQDCWEDFVDHQEEPFR 135
APOBEC_C pfam05240
APOBEC-like C-terminal domain; This domain is found at the C-termini of the Apolipoprotein B ...
 292-368 5.47e-37

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: 128.37  E-value: 5.47e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1159731399 292 KHVSLCIFTARIYDDQ-GRCQEGLRTLAEAGAKISIMTYSEFKHCWDTFVDHQGCPFQPWDGLDEHSQDLSGRLRAIL 368
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 ...
 101-182 6.31e-35

APOBEC-like C-terminal domain; This domain is found at the C-termini of the Apolipoprotein B mRNA editing enzyme.


Pssm-ID: 461599  Cd Length: 78  Bit Score: 122.98  E-value: 6.31e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399 101 PKVTLTIFVARLYYFWDPDYQEALRSLCQKRdgprATMKIMNYDEFQHCWSKFVYSQRELFEPWNNLPKYYILLHIMLGE 180
Cdd:pfam05240   1 PNVSLTIFAARLYYHWDPEYQQGLRRLVQAG----AQVAIMSYKEFEYCWDNFVDNQGRPFQPWEGLEENSQLLSRRLQE 76


                  ..
gi 1159731399 181 IL 182
Cdd:pfam05240  77 IL 78
APOBEC3 pfam18771
APOBEC3; APOBEC3 deaminases act as restriction factors in the innate response to retroviruses ...
 23-161 2.27e-24

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: 96.79  E-value: 2.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399  23 WLCYEVKtkgpsrPPLDAKIFRGQVYSELKYHPEMRFFhwfSKWRKLHRD--QEYEVTWYISWSPCTKCTRDMATFLAED 100
Cdd:pfam18771   7 YLCYQLK------GRNGSALDRGYFSNKKKRHAEIRFI---DKIRSLDLDniQCYRITCYITWSPCPNCAAELVDFISLN 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159731399 101 PKVTLTIFVARLYYFWDPDYQEALRSLCQKrdgpRATMKIMNYDEFQHCWSKFVYSQRELF 161
Cdd:pfam18771  78 PHLKLRIFASRLYYHWERSYKEGLQKLQRA----GVSVAVMTLPEFQDCWEDFVDHQEEPF 134
APOBEC4 pfam18775
APOBEC4; A member of the AID/APOBEC family of cytosine deaminases. The biological function of ...
 77-154 3.02e-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: 72.75  E-value: 3.02e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1159731399  77 VTWYISWSPCTKCTRDMATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSLCQKrdgpRATMKIMNYDEFQHCWSKFV 154
Cdd:pfam18775   1 VTLYLSWSPCNECSEKIQEFLKKHPKVNLDIYFAQLYHTEEEDNRQGLRSLVEK----GVTLSVMSGEDWIYCLRTFV 74
APOBEC4_like pfam18774
APOBEC4-like -AID/APOBEC-deaminase; Cnidarian and Algal homologs of the APOBEC4-like AID ...
 61-154 9.15e-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: 9.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399  61 HWFSKWRKLHRDQEYEVTWYISWSPCTKCTRDMATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSLCQKrdgpRATMKI 140
Cdd:pfam18774  40 NFLENFRSERPSRSCTITWYLSWSPCWECSGRILEFLSRHPNVTLGIYVARLFMHDDDRNRQGLRILQMN----GVTIQV 115

                          90
                  ....*....|....
gi 1159731399 141 MNYDEFQHCWSKFV 154
Cdd:pfam18774 116 MMNKDYCYCWKAFK 129
APOBEC4 pfam18775
APOBEC4; A member of the AID/APOBEC family of cytosine deaminases. The biological function of ...
 268-340 7.00e-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: 7.00e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1159731399 268 VTCFTSWSPCFSCAQEMAKFISKNKHVSLCIFTARIYDDQGRC-QEGLRTLAEAGAKISIMTYSEFKHCWDTFV 340
Cdd:pfam18775   1 VTLYLSWSPCNECSEKIQEFLKKHPKVNLDIYFAQLYHTEEEDnRQGLRSLVEKGVTLSVMSGEDWIYCLRTFV 74
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 1-122 1.78e-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: 66.21  E-value: 1.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399   1 MYRDTFSYNFYnrpilsrRNTVWLCYEVKTKGpsrppldaKIFRGQVYSELKY----HPEMRFFHWFSKWRklhrDQEYE 76
Cdd:cd01283     5 LAAAEFAYAPY-------SNFTVGAALLTKDG--------RIFTGVNVENASYgltlCAERTAIGKAVSEG----LRRYL 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1159731399  77 VTWYIS-----WSPCTKCTRDMATFLAedpkvtltifvARLYYFWDPDYQE 122
Cdd:cd01283    66 VTWAVSdeggvWSPCGACRQVLAEFLP-----------SRLYIIIDNPKGE 105
APOBEC1 pfam18769
APOBEC1; APOBEC1 deaminates cytosine both in RNA and ssDNA and has roles in both mRNA editing ...
 54-127 7.90e-13

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: 64.06  E-value: 7.90e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1159731399  54 HPEMRFFHWFSKWRKLHRDQEYEVTWYISWSPCTKCTRDMATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSL 127
Cdd:pfam18769  18 HAEVNFLEKFFSERHFDPSVSCSITWFLSWSPCGECSKAIGEFLSQHPNVTLVIYAARLFKHLDIRNRQGLRDL 91
APOBEC4_like pfam18774
APOBEC4-like -AID/APOBEC-deaminase; Cnidarian and Algal homologs of the APOBEC4-like AID ...
 237-341 1.97e-12

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: 63.74  E-value: 1.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399 237 HKHGFLEGRHAELCFLDvipfwKLDLDQDYR---VTCFTSWSPCFSCAQEMAKFISKNKHVSLCIFTARIY---DDQGRc 310
Cdd:pfam18774  27 NWTENNCTEHAEVNFLE-----NFRSERPSRsctITWYLSWSPCWECSGRILEFLSRHPNVTLGIYVARLFmhdDDRNR- 100

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1159731399 311 qEGLRTLAEAGAKISIMTYSEFKHCWDTFVD 341
Cdd:pfam18774 101 -QGLRILQMNGVTIQVMMNKDYCYCWKAFKN 130
AID pfam18767
Activation induced deaminase; The activation induced deaminase is a vertebrate-specific member ...
 1-47 2.12e-11

Activation induced deaminase; The activation induced deaminase is a vertebrate-specific member of the classical AID/APOBEC cytosine deaminases that is involved in antibody diversification.


Pssm-ID: 408538  Cd Length: 90  Bit Score: 59.49  E-value: 2.12e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1159731399   1 MYRDTFSYNFynRPILSRRNTVWL-------CYEVKTKGPSRPPLDAKIFRGQV 47
Cdd:pfam18767   5 IHAEIFFIDD--NKDPSRITELWIknspchrCSEVLLKHFSRPPLKPTIHIGRI 56
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 200-291 8.89e-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: 47.34  E-value: 8.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159731399 200 WVRGRHETYLCYEVERmhNDTWVllnqrRGFLCNQAphkhGFLEGRHAELCFLDVIPfwkLDLDQDYRVTCFTS-----W 274
Cdd:cd01283    12 YAPYSNFTVGAALLTK--DGRIF-----TGVNVENA----SYGLTLCAERTAIGKAV---SEGLRRYLVTWAVSdeggvW 77

                          90
                  ....*....|....*..
gi 1159731399 275 SPCFSCAQEMAKFISKN 291
Cdd:cd01283    78 SPCGACRQVLAEFLPSR 94
 
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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