NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1849085983|ref|XP_034804992|]
View 

DNA dC-

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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.
 195-379 2.66e-88

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: 264.23  E-value: 2.66e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983 195 HSMDPPTFTSNFNNELWVRGRHETYLCYEVERLHNDTrvLLNQRRGFLCNQAphkhgfleGRHAELCFLDVIPFWKLDLH 274
Cdd:pfam18782   1 KRMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGT--WLPQHRGFFRNQA--------KYHAELCFLSWFCGNQLPPY 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983 275 QDYRVTCFTSWSPCFSCAQEMAKFISNNKHVSLCIFAARIYDDQGR-CQEGLRTLAKAGAEISIMTYSEFKHCWDTFVDH 353
Cdd:pfam18782  71 QNYQVTWYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPdYQEALRRLRQAGARVKIMDYEEFEYCWENFVYN 150

                         170       180
                  ....*....|....*....|....*.
gi 1849085983 354 QGCPFQPWDGLEEHSQALSERLQAIL 379
Cdd:pfam18782 151 QGEPFQPWDGLEENSRFLHRRLREIL 176
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 12-194 1.63e-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: 259.45  E-value: 1.63e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983  12 MYQDTFSDNFYNRPILSRRNTVWLCYEVKTKGPSrpplDAKIFRGQVYSKLKYHPEMRFFHWFSKWrKLHRDQEYEVTWY 91
Cdd:pfam18772   1 MDPKTFKFQFKNVPYASGRNKTYLCYEVETRSGS----DLSPDRGYLRNQAGCHAELCFLSWILPW-QLDPGQKYQVTWY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983  92 ISWSPCTKCTRDVATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSLCQKrdgpRATMKIMNYDEFQHCWSKFVYSQREL 171
Cdd:pfam18772  76 VSWSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRA----GAQLKIMDYQDFEYCWENFVDNQGRP 151

                         170       180
                  ....*....|....*....|...
gi 1849085983 172 FEPWNNLPKYYILLHIMLGEILR 194
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.
 195-379 2.66e-88

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: 264.23  E-value: 2.66e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983 195 HSMDPPTFTSNFNNELWVRGRHETYLCYEVERLHNDTrvLLNQRRGFLCNQAphkhgfleGRHAELCFLDVIPFWKLDLH 274
Cdd:pfam18782   1 KRMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGT--WLPQHRGFFRNQA--------KYHAELCFLSWFCGNQLPPY 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983 275 QDYRVTCFTSWSPCFSCAQEMAKFISNNKHVSLCIFAARIYDDQGR-CQEGLRTLAKAGAEISIMTYSEFKHCWDTFVDH 353
Cdd:pfam18782  71 QNYQVTWYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPdYQEALRRLRQAGARVKIMDYEEFEYCWENFVYN 150

                         170       180
                  ....*....|....*....|....*.
gi 1849085983 354 QGCPFQPWDGLEEHSQALSERLQAIL 379
Cdd:pfam18782 151 QGEPFQPWDGLEENSRFLHRRLREIL 176
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 12-194 1.63e-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: 259.45  E-value: 1.63e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983  12 MYQDTFSDNFYNRPILSRRNTVWLCYEVKTKGPSrpplDAKIFRGQVYSKLKYHPEMRFFHWFSKWrKLHRDQEYEVTWY 91
Cdd:pfam18772   1 MDPKTFKFQFKNVPYASGRNKTYLCYEVETRSGS----DLSPDRGYLRNQAGCHAELCFLSWILPW-QLDPGQKYQVTWY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983  92 ISWSPCTKCTRDVATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSLCQKrdgpRATMKIMNYDEFQHCWSKFVYSQREL 171
Cdd:pfam18772  76 VSWSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRA----GAQLKIMDYQDFEYCWENFVDNQGRP 151

                         170       180
                  ....*....|....*....|...
gi 1849085983 172 FEPWNNLPKYYILLHIMLGEILR 194
Cdd:pfam18772 152 FEPWEDLDENYEYLSRKLQEILR 174
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 19-133 4.24e-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: 65.06  E-value: 4.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983  19 DNFYNRPIlsrRNTVWLCYEVKTKGpsrppldaKIFRGQVYSKLKY----HPEMRFFHWFSKWRklhrDQEYEVTWYIS- 93
Cdd:cd01283     8 AEFAYAPY---SNFTVGAALLTKDG--------RIFTGVNVENASYgltlCAERTAIGKAVSEG----LRRYLVTWAVSd 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1849085983  94 ----WSPCTKCTRDVATFLAedpkvtltifvARLYYFWDPDYQE 133
Cdd:cd01283    73 eggvWSPCGACRQVLAEFLP-----------SRLYIIIDNPKGE 105
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 208-302 4.44e-08

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: 50.80  E-value: 4.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983 208 NELWVRGRHETYLCYEVERlhnDTRVLlnqrRGFLCNQAphkhGFLEGRHAELCFLDVIPfwkLDLHQDYRVTCFTS--- 284
Cdd:cd01283     9 EFAYAPYSNFTVGAALLTK---DGRIF----TGVNVENA----SYGLTLCAERTAIGKAV---SEGLRRYLVTWAVSdeg 74

                          90       100
                  ....*....|....*....|
gi 1849085983 285 --WSPCFSCAQEMAKFISNN 302
Cdd:cd01283    75 gvWSPCGACRQVLAEFLPSR 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.
 195-379 2.66e-88

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: 264.23  E-value: 2.66e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983 195 HSMDPPTFTSNFNNELWVRGRHETYLCYEVERLHNDTrvLLNQRRGFLCNQAphkhgfleGRHAELCFLDVIPFWKLDLH 274
Cdd:pfam18782   1 KRMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGT--WLPQHRGFFRNQA--------KYHAELCFLSWFCGNQLPPY 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983 275 QDYRVTCFTSWSPCFSCAQEMAKFISNNKHVSLCIFAARIYDDQGR-CQEGLRTLAKAGAEISIMTYSEFKHCWDTFVDH 353
Cdd:pfam18782  71 QNYQVTWYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPdYQEALRRLRQAGARVKIMDYEEFEYCWENFVYN 150

                         170       180
                  ....*....|....*....|....*.
gi 1849085983 354 QGCPFQPWDGLEEHSQALSERLQAIL 379
Cdd:pfam18782 151 QGEPFQPWDGLEENSRFLHRRLREIL 176
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 12-194 1.63e-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: 259.45  E-value: 1.63e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983  12 MYQDTFSDNFYNRPILSRRNTVWLCYEVKTKGPSrpplDAKIFRGQVYSKLKYHPEMRFFHWFSKWrKLHRDQEYEVTWY 91
Cdd:pfam18772   1 MDPKTFKFQFKNVPYASGRNKTYLCYEVETRSGS----DLSPDRGYLRNQAGCHAELCFLSWILPW-QLDPGQKYQVTWY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983  92 ISWSPCTKCTRDVATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSLCQKrdgpRATMKIMNYDEFQHCWSKFVYSQREL 171
Cdd:pfam18772  76 VSWSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRA----GAQLKIMDYQDFEYCWENFVDNQGRP 151

                         170       180
                  ....*....|....*....|...
gi 1849085983 172 FEPWNNLPKYYILLHIMLGEILR 194
Cdd:pfam18772 152 FEPWEDLDENYEYLSRKLQEILR 174
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 10-193 2.14e-82

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: 249.21  E-value: 2.14e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983  10 ERMYQDTFSDNFYNRPILSRRNTVWLCYEVKTKGPSRPPldaKIFRGQVYSKLKYHPEMRFFHWFsKWRKLHRDQEYEVT 89
Cdd:pfam18782   1 KRMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGTWL---PQHRGFFRNQAKYHAELCFLSWF-CGNQLPPYQNYQVT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983  90 WYISWSPCTKCTRDVATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSLCQKrdgpRATMKIMNYDEFQHCWSKFVYSQR 169
Cdd:pfam18782  77 WYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQA----GARVKIMDYEEFEYCWENFVYNQG 152

                         170       180
                  ....*....|....*....|....
gi 1849085983 170 ELFEPWNNLPKYYILLHIMLGEIL 193
Cdd:pfam18782 153 EPFQPWDGLEENSRFLHRRLREIL 176
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 197-380 1.52e-81

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: 246.74  E-value: 1.52e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983 197 MDPPTFTSNFNNELWVRGRHETYLCYEVERLHNDTrvlLNQRRGFLCNQAphkhgfleGRHAELCFLDVIPFWKLDLHQD 276
Cdd:pfam18772   1 MDPKTFKFQFKNVPYASGRNKTYLCYEVETRSGSD---LSPDRGYLRNQA--------GCHAELCFLSWILPWQLDPGQK 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983 277 YRVTCFTSWSPCFSCAQEMAKFISNNKHVSLCIFAARIY-DDQGRCQEGLRTLAKAGAEISIMTYSEFKHCWDTFVDHQG 355
Cdd:pfam18772  70 YQVTWYVSWSPCPDCARKLAEFLARHPNLSLTIFAARLYfFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDNQG 149

                         170       180
                  ....*....|....*....|....*
gi 1849085983 356 CPFQPWDGLEEHSQALSERLQAILQ 380
Cdd:pfam18772 150 RPFEPWEDLDENYEYLSRKLQEILR 174
NAD1 pfam18778
Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned ...
 195-379 6.90e-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: 234.87  E-value: 6.90e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983 195 HSMDPPTFTSNFNNELWVRGRHETYLCYEVERlhndtRVLLNQRRGFLCNQAPhkhgfleGRHAELCFLDVIPFWKL-DL 273
Cdd:pfam18778   1 ERMSPETFKFQFKNVEYASGRNKTLLCYEVKR-----GNSSSLWRGHLRNENS-------GCHAEICFLRWFSSWRLfDP 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983 274 HQDYRVTCFTSWSPCFSCAQEMAKFISNNKHVSLCIFAARIYDDQGR-CQEGLRTLAKAGAEISIMTYSEFKHCWDTFVD 352
Cdd:pfam18778  69 SQCYTITWYLSWSPCPSCAAKLAEFLKAHPNVTLTIFAARLYYFEDPwNQEGLRSLASAGVTLSIMDYSDFEYCWENFVD 148

                         170       180
                  ....*....|....*....|....*..
gi 1849085983 353 HQGCPFQPWDGLEEHSQALSERLQAIL 379
Cdd:pfam18778 149 NEGRPFVPWEDLEENSRYYHRKLQRIL 175
NAD1 pfam18778
Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned ...
 10-193 1.26e-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: 231.78  E-value: 1.26e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983  10 ERMYQDTFSDNFYNRPILSRRNTVWLCYEVKTKGPSRPPLdaKIFRGQvysKLKYHPEMRFFHWFSKWRKLHRDQEYEVT 89
Cdd:pfam18778   1 ERMSPETFKFQFKNVEYASGRNKTLLCYEVKRGNSSSLWR--GHLRNE---NSGCHAEICFLRWFSSWRLFDPSQCYTIT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983  90 WYISWSPCTKCTRDVATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSLCQKrdgpRATMKIMNYDEFQHCWSKFVYSQR 169
Cdd:pfam18778  76 WYLSWSPCPSCAAKLAEFLKAHPNVTLTIFAARLYYFEDPWNQEGLRSLASA----GVTLSIMDYSDFEYCWENFVDNEG 151

                         170       180
                  ....*....|....*....|....
gi 1849085983 170 ELFEPWNNLPKYYILLHIMLGEIL 193
Cdd:pfam18778 152 RPFVPWEDLEENSRYYHRKLQRIL 175
APOBEC_N pfam08210
APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. ...
 202-376 5.02e-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: 181.41  E-value: 5.02e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983 202 FTSNFNNELWVRGRHETYLCYEVERlhnDTRVLLNQRRGFLCNQAphkhgfLEGRHAELCFLDVIPFWKLDLHQDYRVTC 281
Cdd:pfam08210   1 FFFHFKNLPYASGRHETYLCYEVKR---DSGGLVVEDKGYLRNQA------ASSLHAEERFLRWIHDLALDPGSNYEVTW 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983 282 FTSWSPCFSCAQEMAKFISNNKHVSLCIFAARIY---DDQGRCQEGLRTLAKAGAEISIMTYSEFKHCWDTFVDHQGCPF 358
Cdd:pfam08210  72 YVSWSPCNECASELAAFLSKHPNVRLRIFVSRLYyweEPDYWNREGLRSLAQAGVQLRPMSYKDFEYCWNNFVDHDGEPF 151

                         170
                  ....*....|....*...
gi 1849085983 359 QPWDGLEEHSQALSERLQ 376
Cdd:pfam08210 152 KPWDGLHENSVYLARKLQ 169
SNAD4 pfam18750
Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases ...
 222-349 4.34e-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: 153.57  E-value: 4.34e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983 222 YEVERlHNDTRVLlnqRRGFLCNQAphkhgfleGRHAELCFLDVIPFWKLDLHQDYRVTCFTSWSPCFSCAQEMAKFISN 301
Cdd:pfam18750   1 YEIKW-GNGSKIW---QRGYLSNEH--------EQHAEICFLENIRSRELDPSQRYRVTWYLSWSPCPECAQKIAEFLAE 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1849085983 302 NKHVSLCIFAARIYDDQGRCQEGLRTLAKAGAEISIMTYSEFKHCWDT 349
Cdd:pfam18750  69 HPNVTLTIFAARLYHWDEDNRQGLRSLAQAGVTLQIMTLEDFEYCWKN 116
SNAD4 pfam18750
Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases ...
 37-163 2.32e-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: 152.03  E-value: 2.32e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983  37 YEVKTKGPSRPpldakIFRGQVYSKLKYHPEMRFFHWFSkWRKLHRDQEYEVTWYISWSPCTKCTRDVATFLAEDPKVTL 116
Cdd:pfam18750   1 YEIKWGNGSKI-----WQRGYLSNEHEQHAEICFLENIR-SRELDPSQRYRVTWYLSWSPCPECAQKIAEFLAEHPNVTL 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1849085983 117 TIFVARLYYfWDPDYQEALRSLCQKrdgpRATMKIMNYDEFQHCWSK 163
Cdd:pfam18750  75 TIFAARLYH-WDEDNRQGLRSLAQA----GVTLQIMTLEDFEYCWKN 116
APOBEC_N pfam08210
APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. ...
 20-178 1.56e-44

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: 151.75  E-value: 1.56e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983  20 NFYNRPILSRRNTVWLCYEVKTKGPSRPPLDAKIFRGQVYSKLkyHPEMRFFHWFSKWrKLHRDQEYEVTWYISWSPCTK 99
Cdd:pfam08210   4 HFKNLPYASGRHETYLCYEVKRDSGGLVVEDKGYLRNQAASSL--HAEERFLRWIHDL-ALDPGSNYEVTWYVSWSPCNE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983 100 CTRDVATFLAEDPKVTLTIFVARLYYFWDPDYQ--EALRSLCQKrdgpRATMKIMNYDEFQHCWSKFVYSQRELFEPWNN 177
Cdd:pfam08210  81 CASELAAFLSKHPNVRLRIFVSRLYYWEEPDYWnrEGLRSLAQA----GVQLRPMSYKDFEYCWNNFVDHDGEPFKPWDG 156


                  .
gi 1849085983 178 L 178
Cdd:pfam08210 157 L 157
APOBEC3 pfam18771
APOBEC3; APOBEC3 deaminases act as restriction factors in the innate response to retroviruses ...
 218-359 3.68e-41

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: 141.47  E-value: 3.68e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983 218 TYLCYEVERLHNDTRVllnqrRGFLCNQAPhkhgflegRHAELCFLDVIPFWKLDLHQDYRVTCFTSWSPCFSCAQEMAK 297
Cdd:pfam18771   6 AYLCYQLKGRNGSALD-----RGYFSNKKK--------RHAEIRFIDKIRSLDLDNIQCYRITCYITWSPCPNCAAELVD 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1849085983 298 FISNNKHVSLCIFAARIYDDQGRC-QEGLRTLAKAGAEISIMTYSEFKHCWDTFVDHQGCPFQ 359
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 ...
 303-379 4.27e-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: 131.45  E-value: 4.27e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1849085983 303 KHVSLCIFAARIYDDQ-GRCQEGLRTLAKAGAEISIMTYSEFKHCWDTFVDHQGCPFQPWDGLEEHSQALSERLQAIL 379
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 ...
 112-193 5.49e-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: 123.36  E-value: 5.49e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983 112 PKVTLTIFVARLYYFWDPDYQEALRSLCQKRdgprATMKIMNYDEFQHCWSKFVYSQRELFEPWNNLPKYYILLHIMLGE 191
Cdd:pfam05240   1 PNVSLTIFAARLYYHWDPEYQQGLRRLVQAG----AQVAIMSYKEFEYCWDNFVDNQGRPFQPWEGLEENSQLLSRRLQE 76


                  ..
gi 1849085983 192 IL 193
Cdd:pfam05240  77 IL 78
APOBEC3 pfam18771
APOBEC3; APOBEC3 deaminases act as restriction factors in the innate response to retroviruses ...
 34-172 1.72e-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: 97.56  E-value: 1.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983  34 WLCYEVKtkgpsrPPLDAKIFRGQVYSKLKYHPEMRFFhwfSKWRKLHRD--QEYEVTWYISWSPCTKCTRDVATFLAED 111
Cdd:pfam18771   7 YLCYQLK------GRNGSALDRGYFSNKKKRHAEIRFI---DKIRSLDLDniQCYRITCYITWSPCPNCAAELVDFISLN 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1849085983 112 PKVTLTIFVARLYYFWDPDYQEALRSLCQKrdgpRATMKIMNYDEFQHCWSKFVYSQRELF 172
Cdd:pfam18771  78 PHLKLRIFASRLYYHWERSYKEGLQKLQRA----GVSVAVMTLPEFQDCWEDFVDHQEEPF 134
APOBEC4 pfam18775
APOBEC4; A member of the AID/APOBEC family of cytosine deaminases. The biological function of ...
 88-165 3.85e-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: 72.37  E-value: 3.85e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1849085983  88 VTWYISWSPCTKCTRDVATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSLCQKrdgpRATMKIMNYDEFQHCWSKFV 165
Cdd:pfam18775   1 VTLYLSWSPCNECSEKIQEFLKKHPKVNLDIYFAQLYHTEEEDNRQGLRSLVEK----GVTLSVMSGEDWIYCLRTFV 74
APOBEC4_like pfam18774
APOBEC4-like -AID/APOBEC-deaminase; Cnidarian and Algal homologs of the APOBEC4-like AID ...
 72-165 6.28e-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: 73.75  E-value: 6.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983  72 HWFSKWRKLHRDQEYEVTWYISWSPCTKCTRDVATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSLCQKrdgpRATMKI 151
Cdd:pfam18774  40 NFLENFRSERPSRSCTITWYLSWSPCWECSGRILEFLSRHPNVTLGIYVARLFMHDDDRNRQGLRILQMN----GVTIQV 115

                          90
                  ....*....|....
gi 1849085983 152 MNYDEFQHCWSKFV 165
Cdd:pfam18774 116 MMNKDYCYCWKAFK 129
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 19-133 4.24e-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: 65.06  E-value: 4.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983  19 DNFYNRPIlsrRNTVWLCYEVKTKGpsrppldaKIFRGQVYSKLKY----HPEMRFFHWFSKWRklhrDQEYEVTWYIS- 93
Cdd:cd01283     8 AEFAYAPY---SNFTVGAALLTKDG--------RIFTGVNVENASYgltlCAERTAIGKAVSEG----LRRYLVTWAVSd 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1849085983  94 ----WSPCTKCTRDVATFLAedpkvtltifvARLYYFWDPDYQE 133
Cdd:cd01283    73 eggvWSPCGACRQVLAEFLP-----------SRLYIIIDNPKGE 105
APOBEC1 pfam18769
APOBEC1; APOBEC1 deaminates cytosine both in RNA and ssDNA and has roles in both mRNA editing ...
 65-138 5.76e-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: 64.45  E-value: 5.76e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1849085983  65 HPEMRFFHWFSKWRKLHRDQEYEVTWYISWSPCTKCTRDVATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSL 138
Cdd:pfam18769  18 HAEVNFLEKFFSERHFDPSVSCSITWFLSWSPCGECSKAIGEFLSQHPNVTLVIYAARLFKHLDIRNRQGLRDL 91
APOBEC4 pfam18775
APOBEC4; A member of the AID/APOBEC family of cytosine deaminases. The biological function of ...
 279-351 6.34e-13

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: 63.51  E-value: 6.34e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1849085983 279 VTCFTSWSPCFSCAQEMAKFISNNKHVSLCIFAARIYDDQGRC-QEGLRTLAKAGAEISIMTYSEFKHCWDTFV 351
Cdd:pfam18775   1 VTLYLSWSPCNECSEKIQEFLKKHPKVNLDIYFAQLYHTEEEDnRQGLRSLVEKGVTLSVMSGEDWIYCLRTFV 74
APOBEC4_like pfam18774
APOBEC4-like -AID/APOBEC-deaminase; Cnidarian and Algal homologs of the APOBEC4-like AID ...
 248-352 1.84e-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: 64.12  E-value: 1.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983 248 HKHGFLEGRHAELCFLDVipFWKLDLHQDYRVTCFTSWSPCFSCAQEMAKFISNNKHVSLCIFAARIY---DDQGRcqEG 324
Cdd:pfam18774  27 NWTENNCTEHAEVNFLEN--FRSERPSRSCTITWYLSWSPCWECSGRILEFLSRHPNVTLGIYVARLFmhdDDRNR--QG 102

                          90       100
                  ....*....|....*....|....*...
gi 1849085983 325 LRTLAKAGAEISIMTYSEFKHCWDTFVD 352
Cdd:pfam18774 103 LRILQMNGVTIQVMMNKDYCYCWKAFKN 130
AID pfam18767
Activation induced deaminase; The activation induced deaminase is a vertebrate-specific member ...
 9-58 6.72e-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: 58.34  E-value: 6.72e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1849085983   9 VERMYQDTFSDNFynRPILSRRNTVWL-------CYEVKTKGPSRPPLDAKIFRGQV 58
Cdd:pfam18767   2 VDRIHAEIFFIDD--NKDPSRITELWIknspchrCSEVLLKHFSRPPLKPTIHIGRI 56
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 208-302 4.44e-08

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: 50.80  E-value: 4.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849085983 208 NELWVRGRHETYLCYEVERlhnDTRVLlnqrRGFLCNQAphkhGFLEGRHAELCFLDVIPfwkLDLHQDYRVTCFTS--- 284
Cdd:cd01283     9 EFAYAPYSNFTVGAALLTK---DGRIF----TGVNVENA----SYGLTLCAERTAIGKAV---SEGLRRYLVTWAVSdeg 74

                          90       100
                  ....*....|....*....|
gi 1849085983 285 --WSPCFSCAQEMAKFISNN 302
Cdd:cd01283    75 gvWSPCGACRQVLAEFLPSR 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH