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Conserved domains on  [gi|880868926|ref|XP_012966578|]
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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.
 33-212 9.39e-95

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: 281.56  E-value: 9.39e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926   33 KMLYERTFYFHFKNLHYANGRKNTFLCFEVNRMECGELVPLCQGVFRKESsNLHAEVCFLYWFhtqVLGMLPPGEKYKIT 112
Cdd:pfam18782   1 KRMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGTWLPQHRGFFRNQA-KYHAELCFLSWF---CGNQLPPYQNYQVT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926  113 WYMSWSPCSECAAEVTRFLDTHRNLSLAIFSSRLYYFWKSDYQDKLRRLNQAGAQIAAMDFPEFEKCWNKFVDNDGKSFR 192
Cdd:pfam18782  77 WYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQGEPFQ 156

                         170       180
                  ....*....|....*....|
gi 880868926  193 PWKRLKINFRNQDSTLWDIL 212
Cdd:pfam18782 157 PWDGLEENSRFLHRRLREIL 176
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 219-393 6.71e-75

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: 230.95  E-value: 6.71e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926  219 LTEDIFYMQFSNRHRVqpvqqrrYYQRKTYLCYLLEPYN--DQQPLKGCLQNKKDKHAEILFIDKMRSLELCQ---VRIT 293
Cdd:pfam18772   1 MDPKTFKFQFKNVPYA-------SGRNKTYLCYEVETRSgsDLSPDRGYLRNQAGCHAELCFLSWILPWQLDPgqkYQVT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926  294 CYLTWSPCPNCAQELAAFKKDHPDLVLRIYTSRLYFHWRRKYQEGLCSLWRSGIQVDVMDLPQFTDCWTNFVSSQS-PFR 372
Cdd:pfam18772  74 WYVSWSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDNQGrPFE 153

                         170       180
                  ....*....|....*....|.
gi 880868926  373 PWNNLEKNSRCIQRRLQRIKE 393
Cdd:pfam18772 154 PWEDLDENYEYLSRKLQEILR 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.
 33-212 9.39e-95

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: 281.56  E-value: 9.39e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926   33 KMLYERTFYFHFKNLHYANGRKNTFLCFEVNRMECGELVPLCQGVFRKESsNLHAEVCFLYWFhtqVLGMLPPGEKYKIT 112
Cdd:pfam18782   1 KRMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGTWLPQHRGFFRNQA-KYHAELCFLSWF---CGNQLPPYQNYQVT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926  113 WYMSWSPCSECAAEVTRFLDTHRNLSLAIFSSRLYYFWKSDYQDKLRRLNQAGAQIAAMDFPEFEKCWNKFVDNDGKSFR 192
Cdd:pfam18782  77 WYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQGEPFQ 156

                         170       180
                  ....*....|....*....|
gi 880868926  193 PWKRLKINFRNQDSTLWDIL 212
Cdd:pfam18782 157 PWDGLEENSRFLHRRLREIL 176
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 219-393 6.71e-75

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: 230.95  E-value: 6.71e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926  219 LTEDIFYMQFSNRHRVqpvqqrrYYQRKTYLCYLLEPYN--DQQPLKGCLQNKKDKHAEILFIDKMRSLELCQ---VRIT 293
Cdd:pfam18772   1 MDPKTFKFQFKNVPYA-------SGRNKTYLCYEVETRSgsDLSPDRGYLRNQAGCHAELCFLSWILPWQLDPgqkYQVT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926  294 CYLTWSPCPNCAQELAAFKKDHPDLVLRIYTSRLYFHWRRKYQEGLCSLWRSGIQVDVMDLPQFTDCWTNFVSSQS-PFR 372
Cdd:pfam18772  74 WYVSWSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDNQGrPFE 153

                         170       180
                  ....*....|....*....|.
gi 880868926  373 PWNNLEKNSRCIQRRLQRIKE 393
Cdd:pfam18772 154 PWEDLDENYEYLSRKLQEILR 174
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 239-337 1.30e-15

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: 72.37  E-value: 1.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926 239 QRRYYQRKTYLCYLLEpyNDQQPLKGCLQNKKD----KHAEILFIDKMRSLELCQVRITCYLT-----WSPCPNCAQELA 309
Cdd:cd01283   11 AYAPYSNFTVGAALLT--KDGRIFTGVNVENASygltLCAERTAIGKAVSEGLRRYLVTWAVSdeggvWSPCGACRQVLA 88

                         90       100
                 ....*....|....*....|....*...
gi 880868926 310 AFKKdhpdlvlriytSRLYFHWRRKYQE 337
Cdd:cd01283   89 EFLP-----------SRLYIIIDNPKGE 105
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 31-156 1.09e-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: 52.73  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926  31 PIKMLYERTFYfhfknlhYANGRKNTFLCFEVnrMECGELVplcQGVFRKESS---NLHAEVCFLYWFHTQVLGmlppge 107
Cdd:cd01283    1 IEAALAAAEFA-------YAPYSNFTVGAALL--TKDGRIF---TGVNVENASyglTLCAERTAIGKAVSEGLR------ 62

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 880868926 108 KYKITWYMS-----WSPCSECAAEVTRFLDthrnlslaifsSRLYYFWKSDYQD 156
Cdd:cd01283   63 RYLVTWAVSdeggvWSPCGACRQVLAEFLP-----------SRLYIIIDNPKGE 105
 
Name Accession Description Interval E-value
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 33-212 9.39e-95

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: 281.56  E-value: 9.39e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926   33 KMLYERTFYFHFKNLHYANGRKNTFLCFEVNRMECGELVPLCQGVFRKESsNLHAEVCFLYWFhtqVLGMLPPGEKYKIT 112
Cdd:pfam18782   1 KRMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGTWLPQHRGFFRNQA-KYHAELCFLSWF---CGNQLPPYQNYQVT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926  113 WYMSWSPCSECAAEVTRFLDTHRNLSLAIFSSRLYYFWKSDYQDKLRRLNQAGAQIAAMDFPEFEKCWNKFVDNDGKSFR 192
Cdd:pfam18782  77 WYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQGEPFQ 156

                         170       180
                  ....*....|....*....|
gi 880868926  193 PWKRLKINFRNQDSTLWDIL 212
Cdd:pfam18782 157 PWDGLEENSRFLHRRLREIL 176
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 219-393 6.71e-75

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: 230.95  E-value: 6.71e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926  219 LTEDIFYMQFSNRHRVqpvqqrrYYQRKTYLCYLLEPYN--DQQPLKGCLQNKKDKHAEILFIDKMRSLELCQ---VRIT 293
Cdd:pfam18772   1 MDPKTFKFQFKNVPYA-------SGRNKTYLCYEVETRSgsDLSPDRGYLRNQAGCHAELCFLSWILPWQLDPgqkYQVT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926  294 CYLTWSPCPNCAQELAAFKKDHPDLVLRIYTSRLYFHWRRKYQEGLCSLWRSGIQVDVMDLPQFTDCWTNFVSSQS-PFR 372
Cdd:pfam18772  74 WYVSWSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDNQGrPFE 153

                         170       180
                  ....*....|....*....|.
gi 880868926  373 PWNNLEKNSRCIQRRLQRIKE 393
Cdd:pfam18772 154 PWEDLDENYEYLSRKLQEILR 174
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 35-213 1.59e-74

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: 229.79  E-value: 1.59e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926   35 LYERTFYFHFKNLHYANGRKNTFLCFEVNRMECGELVPLcQGVFRKESSNlHAEVCFLYWFHTqvlGMLPPGEKYKITWY 114
Cdd:pfam18772   1 MDPKTFKFQFKNVPYASGRNKTYLCYEVETRSGSDLSPD-RGYLRNQAGC-HAELCFLSWILP---WQLDPGQKYQVTWY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926  115 MSWSPCSECAAEVTRFLDTHRNLSLAIFSSRLYYFWKSDYQDKLRRLNQAGAQIAAMDFPEFEKCWNKFVDNDGKSFRPW 194
Cdd:pfam18772  76 VSWSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDNQGRPFEPW 155

                         170
                  ....*....|....*....
gi 880868926  195 KRLKINFRNQDSTLWDILR 213
Cdd:pfam18772 156 EDLDENYEYLSRKLQEILR 174
NAD1 pfam18778
Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned ...
 35-212 1.04e-71

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: 222.92  E-value: 1.04e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926   35 LYERTFYFHFKNLHYANGRKNTFLCFEVNRmecGELVPLCQGVFRKESSNLHAEVCFLYWFHTqvLGMLPPGEKYKITWY 114
Cdd:pfam18778   3 MSPETFKFQFKNVEYASGRNKTLLCYEVKR---GNSSSLWRGHLRNENSGCHAEICFLRWFSS--WRLFDPSQCYTITWY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926  115 MSWSPCSECAAEVTRFLDTHRNLSLAIFSSRLYYFWKSDYQDKLRRLNQAGAQIAAMDFPEFEKCWNKFVDNDGKSFRPW 194
Cdd:pfam18778  78 LSWSPCPSCAAKLAEFLKAHPNVTLTIFAARLYYFEDPWNQEGLRSLASAGVTLSIMDYSDFEYCWENFVDNEGRPFVPW 157

                         170
                  ....*....|....*...
gi 880868926  195 KRLKINFRNQDSTLWDIL 212
Cdd:pfam18778 158 EDLEENSRYYHRKLQRIL 175
APOBEC_N pfam08210
APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. ...
 40-210 1.35e-69

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: 217.23  E-value: 1.35e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926   40 FYFHFKNLHYANGRKNTFLCFEVNRMECGELVpLCQGVFRKE-SSNLHAEVCFLYWFHTQVLgmlPPGEKYKITWYMSWS 118
Cdd:pfam08210   1 FFFHFKNLPYASGRHETYLCYEVKRDSGGLVV-EDKGYLRNQaASSLHAEERFLRWIHDLAL---DPGSNYEVTWYVSWS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926  119 PCSECAAEVTRFLDTHRNLSLAIFSSRLYYFWKSDYQDK--LRRLNQAGAQIAAMDFPEFEKCWNKFVDNDGKSFRPWKR 196
Cdd:pfam08210  77 PCNECASELAAFLSKHPNVRLRIFVSRLYYWEEPDYWNRegLRSLAQAGVQLRPMSYKDFEYCWNNFVDHDGEPFKPWDG 156

                         170
                  ....*....|....
gi 880868926  197 LKINFRNQDSTLWD 210
Cdd:pfam08210 157 LHENSVYLARKLQE 170
NAD1 pfam18778
Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned ...
 218-392 2.67e-64

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: 203.66  E-value: 2.67e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926  218 LLTEDIFYMQFSNRHRVqpvqqrrYYQRKTYLCYLLEPYNDQQPLKGCLQNKK-DKHAEILFIDKMRSLELC----QVRI 292
Cdd:pfam18778   2 RMSPETFKFQFKNVEYA-------SGRNKTLLCYEVKRGNSSSLWRGHLRNENsGCHAEICFLRWFSSWRLFdpsqCYTI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926  293 TCYLTWSPCPNCAQELAAFKKDHPDLVLRIYTSRLYFHWRRKYQEGLCSLWRSGIQVDVMDLPQFTDCWTNFVSSQ-SPF 371
Cdd:pfam18778  75 TWYLSWSPCPSCAAKLAEFLKAHPNVTLTIFAARLYYFEDPWNQEGLRSLASAGVTLSIMDYSDFEYCWENFVDNEgRPF 154

                         170       180
                  ....*....|....*....|.
gi 880868926  372 RPWNNLEKNSRCIQRRLQRIK 392
Cdd:pfam18778 155 VPWEDLEENSRYYHRKLQRIL 175
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 218-392 5.52e-63

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


Pssm-ID: 436733 [Multi-domain]  Cd Length: 176  Bit Score: 200.29  E-value: 5.52e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926  218 LLTEDIFYMQFSNRHRVqpvqqrrYYQRKTYLCYLLEPYNDQQPL---KGCLQNKKDKHAEILFIDKMRSLELC---QVR 291
Cdd:pfam18782   2 RMYPRTFYFNFNNKPIL-------YGRNKTYLCYEVERLDNGTWLpqhRGFFRNQAKYHAELCFLSWFCGNQLPpyqNYQ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926  292 ITCYLTWSPCPNCAQELAAFKKDHPDLVLRIYTSRLYFHWRRKYQEGLCSLWRSGIQVDVMDLPQFTDCWTNFVSSQS-P 370
Cdd:pfam18782  75 VTWYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQGeP 154

                         170       180
                  ....*....|....*....|..
gi 880868926  371 FRPWNNLEKNSRCIQRRLQRIK 392
Cdd:pfam18782 155 FQPWDGLEENSRFLHRRLREIL 176
APOBEC3 pfam18771
APOBEC3; APOBEC3 deaminases act as restriction factors in the innate response to retroviruses ...
 242-372 1.30e-54

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


Pssm-ID: 465862 [Multi-domain]  Cd Length: 135  Bit Score: 177.29  E-value: 1.30e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926  242 YYQRKTYLCYLLEPYNDQQPLKGCLQNKKDKHAEILFIDKMRSLELCQV---RITCYLTWSPCPNCAQELAAFKKDHPDL 318
Cdd:pfam18771   1 YYDRKAYLCYQLKGRNGSALDRGYFSNKKKRHAEIRFIDKIRSLDLDNIqcyRITCYITWSPCPNCAAELVDFISLNPHL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 880868926  319 VLRIYTSRLYFHWRRKYQEGLCSLWRSGIQVDVMDLPQFTDCWTNFVSSQS-PFR 372
Cdd:pfam18771  81 KLRIFASRLYYHWERSYKEGLQKLQRAGVSVAVMTLPEFQDCWEDFVDHQEePFR 135
SNAD4 pfam18750
Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases ...
 263-363 1.72e-43

Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases found only in sponges that often shows lineage-specific expansions.


Pssm-ID: 465854 [Multi-domain]  Cd Length: 116  Bit Score: 147.79  E-value: 1.72e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926  263 KGCLQNKKDKHAEILFIDKMRSLELCQV---RITCYLTWSPCPNCAQELAAFKKDHPDLVLRIYTSRLYfHWRRKYQEGL 339
Cdd:pfam18750  14 RGYLSNEHEQHAEICFLENIRSRELDPSqryRVTWYLSWSPCPECAQKIAEFLAEHPNVTLTIFAARLY-HWDEDNRQGL 92

                          90       100
                  ....*....|....*....|....
gi 880868926  340 CSLWRSGIQVDVMDLPQFTDCWTN 363
Cdd:pfam18750  93 RSLAQAGVTLQIMTLEDFEYCWKN 116
APOBEC_N pfam08210
APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. ...
 224-390 1.25e-41

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: 144.82  E-value: 1.25e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926  224 FYMQFSNRHRVqpvqqrrYYQRKTYLCYLLE--PYNDQQPLKGCLQNKKDK--HAEILFIDKMRSLELCQV---RITCYL 296
Cdd:pfam08210   1 FFFHFKNLPYA-------SGRHETYLCYEVKrdSGGLVVEDKGYLRNQAASslHAEERFLRWIHDLALDPGsnyEVTWYV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926  297 TWSPCPNCAQELAAFKKDHPDLVLRIYTSRLYFHWRRKYQ--EGLCSLWRSGIQVDVMDLPQFTDCWTNFVSSQS-PFRP 373
Cdd:pfam08210  74 SWSPCNECASELAAFLSKHPNVRLRIFVSRLYYWEEPDYWnrEGLRSLAQAGVQLRPMSYKDFEYCWNNFVDHDGePFKP 153

                         170
                  ....*....|....*..
gi 880868926  374 WNNLEKNSRCIQRRLQR 390
Cdd:pfam08210 154 WDGLHENSVYLARKLQE 170
SNAD4 pfam18750
Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases ...
 71-182 1.68e-41

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: 142.40  E-value: 1.68e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926   71 VPLCQGVFRKESsNLHAEVCFLYWFHTQVLgmlPPGEKYKITWYMSWSPCSECAAEVTRFLDTHRNLSLAIFSSRLYYfW 150
Cdd:pfam18750  10 KIWQRGYLSNEH-EQHAEICFLENIRSREL---DPSQRYRVTWYLSWSPCPECAQKIAEFLAEHPNVTLTIFAARLYH-W 84

                          90       100       110
                  ....*....|....*....|....*....|..
gi 880868926  151 KSDYQDKLRRLNQAGAQIAAMDFPEFEKCWNK 182
Cdd:pfam18750  85 DEDNRQGLRSLAQAGVTLQIMTLEDFEYCWKN 116
APOBEC_C pfam05240
APOBEC-like C-terminal domain; This domain is found at the C-termini of the Apolipoprotein B ...
 135-212 5.19e-33

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


Pssm-ID: 461599  Cd Length: 78  Bit Score: 118.74  E-value: 5.19e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 880868926  135 RNLSLAIFSSRLYYFWKSDYQDKLRRLNQAGAQIAAMDFPEFEKCWNKFVDNDGKSFRPWKRLKINFRNQDSTLWDIL 212
Cdd:pfam05240   1 PNVSLTIFAARLYYHWDPEYQQGLRRLVQAGAQVAIMSYKEFEYCWDNFVDNQGRPFQPWEGLEENSQLLSRRLQEIL 78
APOBEC3 pfam18771
APOBEC3; APOBEC3 deaminases act as restriction factors in the innate response to retroviruses ...
 53-192 8.57e-33

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: 120.29  E-value: 8.57e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926   53 RKNTFLCFEVnrmECGELVPLCQGVFRKESSNlHAEVCFLYwfHTQVLGmLPPGEKYKITWYMSWSPCSECAAEVTRFLD 132
Cdd:pfam18771   3 DRKAYLCYQL---KGRNGSALDRGYFSNKKKR-HAEIRFID--KIRSLD-LDNIQCYRITCYITWSPCPNCAAELVDFIS 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926  133 THRNLSLAIFSSRLYYFWKSDYQDKLRRLNQAGAQIAAMDFPEFEKCWNKFVDNDGKSFR 192
Cdd:pfam18771  76 LNPHLKLRIFASRLYYHWERSYKEGLQKLQRAGVSVAVMTLPEFQDCWEDFVDHQEEPFR 135
APOBEC_C pfam05240
APOBEC-like C-terminal domain; This domain is found at the C-termini of the Apolipoprotein B ...
 316-391 3.95e-32

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


Pssm-ID: 461599  Cd Length: 78  Bit Score: 116.43  E-value: 3.95e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 880868926  316 PDLVLRIYTSRLYFHWRRKYQEGLCSLWRSGIQVDVMDLPQFTDCWTNFVSSQ-SPFRPWNNLEKNSRCIQRRLQRI 391
Cdd:pfam05240   1 PNVSLTIFAARLYYHWDPEYQQGLRRLVQAGAQVAIMSYKEFEYCWDNFVDNQgRPFQPWEGLEENSQLLSRRLQEI 77
APOBEC4_like pfam18774
APOBEC4-like -AID/APOBEC-deaminase; Cnidarian and Algal homologs of the APOBEC4-like AID ...
 268-365 1.19e-15

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: 72.98  E-value: 1.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926  268 NKKDKHAEILFIDKMRS-LELCQVRITCYLTWSPCPNCAQELAAFKKDHPDLVLRIYTSRLYFHWRRKYQEGLCSLWRSG 346
Cdd:pfam18774  31 NNCTEHAEVNFLENFRSeRPSRSCTITWYLSWSPCWECSGRILEFLSRHPNVTLGIYVARLFMHDDDRNRQGLRILQMNG 110

                          90
                  ....*....|....*....
gi 880868926  347 IQVDVMDLPQFTDCWTNFV 365
Cdd:pfam18774 111 VTIQVMMNKDYCYCWKAFK 129
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 239-337 1.30e-15

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: 72.37  E-value: 1.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926 239 QRRYYQRKTYLCYLLEpyNDQQPLKGCLQNKKD----KHAEILFIDKMRSLELCQVRITCYLT-----WSPCPNCAQELA 309
Cdd:cd01283   11 AYAPYSNFTVGAALLT--KDGRIFTGVNVENASygltLCAERTAIGKAVSEGLRRYLVTWAVSdeggvWSPCGACRQVLA 88

                         90       100
                 ....*....|....*....|....*...
gi 880868926 310 AFKKdhpdlvlriytSRLYFHWRRKYQE 337
Cdd:cd01283   89 EFLP-----------SRLYIIIDNPKGE 105
APOBEC4 pfam18775
APOBEC4; A member of the AID/APOBEC family of cytosine deaminases. The biological function of ...
 292-365 1.74e-15

APOBEC4; A member of the AID/APOBEC family of cytosine deaminases. The biological function of APOBEC4 is poorly understood. However, it is widely conserved across vertebrates.


Pssm-ID: 436728  Cd Length: 74  Bit Score: 70.83  E-value: 1.74e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 880868926  292 ITCYLTWSPCPNCAQELAAFKKDHPDLVLRIYTSRLYFHWRRKYQEGLCSLWRSGIQVDVMDLPQFTDCWTNFV 365
Cdd:pfam18775   1 VTLYLSWSPCNECSEKIQEFLKKHPKVNLDIYFAQLYHTEEEDNRQGLRSLVEKGVTLSVMSGEDWIYCLRTFV 74
APOBEC4 pfam18775
APOBEC4; A member of the AID/APOBEC family of cytosine deaminases. The biological function of ...
 111-184 9.36e-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: 9.36e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 880868926  111 ITWYMSWSPCSECAAEVTRFLDTHRNLSLAIFSSRLYYFWKSDYQDKLRRLNQAGAQIAAMDFPEFEKCWNKFV 184
Cdd:pfam18775   1 VTLYLSWSPCNECSEKIQEFLKKHPKVNLDIYFAQLYHTEEEDNRQGLRSLVEKGVTLSVMSGEDWIYCLRTFV 74
APOBEC4_like pfam18774
APOBEC4-like -AID/APOBEC-deaminase; Cnidarian and Algal homologs of the APOBEC4-like AID ...
 81-185 4.41e-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: 68.75  E-value: 4.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926   81 ESSNLHAEVCFLYWFHTQvlgmlPPGEKYKITWYMSWSPCSECAAEVTRFLDTHRNLSLAIFSSRLYYFWKSDYQDKLRR 160
Cdd:pfam18774  31 NNCTEHAEVNFLENFRSE-----RPSRSCTITWYLSWSPCWECSGRILEFLSRHPNVTLGIYVARLFMHDDDRNRQGLRI 105

                          90       100
                  ....*....|....*....|....*
gi 880868926  161 LNQAGAQIAAMDFPEFEKCWNKFVD 185
Cdd:pfam18774 106 LQMNGVTIQVMMNKDYCYCWKAFKN 130
APOBEC1 pfam18769
APOBEC1; APOBEC1 deaminates cytosine both in RNA and ssDNA and has roles in both mRNA editing ...
 83-171 3.58e-12

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: 62.52  E-value: 3.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926   83 SNLHAEVCFLYWFHTQVlgMLPPGEKYKITWYMSWSPCSECAAEVTRFLDTHRNLSLAIFSSRLyyFWKSDYQDK--LRR 160
Cdd:pfam18769  15 TTQHAEVNFLEKFFSER--HFDPSVSCSITWFLSWSPCGECSKAIGEFLSQHPNVTLVIYAARL--FKHLDIRNRqgLRD 90

                          90
                  ....*....|.
gi 880868926  161 LNQAGAQIAAM 171
Cdd:pfam18769  91 LAMSGVTIQIM 101
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 31-156 1.09e-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: 52.73  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880868926  31 PIKMLYERTFYfhfknlhYANGRKNTFLCFEVnrMECGELVplcQGVFRKESS---NLHAEVCFLYWFHTQVLGmlppge 107
Cdd:cd01283    1 IEAALAAAEFA-------YAPYSNFTVGAALL--TKDGRIF---TGVNVENASyglTLCAERTAIGKAVSEGLR------ 62

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 880868926 108 KYKITWYMS-----WSPCSECAAEVTRFLDthrnlslaifsSRLYYFWKSDYQD 156
Cdd:cd01283   63 RYLVTWAVSdeggvWSPCGACRQVLAEFLP-----------SRLYIIIDNPKGE 105
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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