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Conserved domains on  [gi|1067605039|ref|NP_001332929|]
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apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3C [Papio anubis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 12-190 2.89e-98

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: 281.80  E-value: 2.89e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605039  12 MDPDTFYFQFKNLWEANNRNETWLCFTVEViKQRSTVSWERGVFQNQvdpkSHCHAERCFLSWFCEDILSPNTDYQVTWY 91
Cdd:pfam18772   1 MDPKTFKFQFKNVPYASGRNKTYLCYEVET-RSGSDLSPDRGYLRNQ----AGCHAELCFLSWILPWQLDPGQKYQVTWY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605039  92 TSWSPCPECAGEVAEFLARHNNVMLTIYTARLYYSQDPNYQQGLRSLSEKGVSVKIMDYEDFKYCWEKFVYDDGEPFKPW 171
Cdd:pfam18772  76 VSWSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDNQGRPFEPW 155

                         170
                  ....*....|....*....
gi 1067605039 172 KGINTNFRFLKRRLREILQ 190
Cdd:pfam18772 156 EDLDENYEYLSRKLQEILR 174
 
Name Accession Description Interval E-value
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 12-190 2.89e-98

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: 281.80  E-value: 2.89e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605039  12 MDPDTFYFQFKNLWEANNRNETWLCFTVEViKQRSTVSWERGVFQNQvdpkSHCHAERCFLSWFCEDILSPNTDYQVTWY 91
Cdd:pfam18772   1 MDPKTFKFQFKNVPYASGRNKTYLCYEVET-RSGSDLSPDRGYLRNQ----AGCHAELCFLSWILPWQLDPGQKYQVTWY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605039  92 TSWSPCPECAGEVAEFLARHNNVMLTIYTARLYYSQDPNYQQGLRSLSEKGVSVKIMDYEDFKYCWEKFVYDDGEPFKPW 171
Cdd:pfam18772  76 VSWSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDNQGRPFEPW 155

                         170
                  ....*....|....*....
gi 1067605039 172 KGINTNFRFLKRRLREILQ 190
Cdd:pfam18772 156 EDLDENYEYLSRKLQEILR 174
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 8-158 3.87e-14

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: 65.44  E-value: 3.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605039   8 PIKAMDPDTFYfqfknlwEANNRNETWLCFTVEvikqrSTVSWERGVFQNQVDPKSHCHAERCFLSWFCEDILspnTDYQ 87
Cdd:cd01283     1 IEAALAAAEFA-------YAPYSNFTVGAALLT-----KDGRIFTGVNVENASYGLTLCAERTAIGKAVSEGL---RRYL 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067605039  88 VTWYTS-----WSPCPECAGEVAEFLArhnnvmltiytARLYYSQDPNYQQglrslsekgvsvkimdyeDFKYCWE 158
Cdd:cd01283    66 VTWAVSdeggvWSPCGACRQVLAEFLP-----------SRLYIIIDNPKGE------------------EFAYTLS 112
 
Name Accession Description Interval E-value
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 12-190 2.89e-98

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: 281.80  E-value: 2.89e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605039  12 MDPDTFYFQFKNLWEANNRNETWLCFTVEViKQRSTVSWERGVFQNQvdpkSHCHAERCFLSWFCEDILSPNTDYQVTWY 91
Cdd:pfam18772   1 MDPKTFKFQFKNVPYASGRNKTYLCYEVET-RSGSDLSPDRGYLRNQ----AGCHAELCFLSWILPWQLDPGQKYQVTWY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605039  92 TSWSPCPECAGEVAEFLARHNNVMLTIYTARLYYSQDPNYQQGLRSLSEKGVSVKIMDYEDFKYCWEKFVYDDGEPFKPW 171
Cdd:pfam18772  76 VSWSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDNQGRPFEPW 155

                         170
                  ....*....|....*....
gi 1067605039 172 KGINTNFRFLKRRLREILQ 190
Cdd:pfam18772 156 EDLDENYEYLSRKLQEILR 174
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 10-189 1.59e-90

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: 262.30  E-value: 1.59e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605039  10 KAMDPDTFYFQFKNLWEANNRNETWLCFTVEVIKQRSTVSWERGVFQNQvdpkSHCHAERCFLSWFCEDILSPNTDYQVT 89
Cdd:pfam18782   1 KRMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGTWLPQHRGFFRNQ----AKYHAELCFLSWFCGNQLPPYQNYQVT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605039  90 WYTSWSPCPECAGEVAEFLARHNNVMLTIYTARLYYSQDPNYQQGLRSLSEKGVSVKIMDYEDFKYCWEKFVYDDGEPFK 169
Cdd:pfam18782  77 WYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQGEPFQ 156

                         170       180
                  ....*....|....*....|
gi 1067605039 170 PWKGINTNFRFLKRRLREIL 189
Cdd:pfam18782 157 PWDGLEENSRFLHRRLREIL 176
NAD1 pfam18778
Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned ...
 10-189 5.39e-88

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: 255.67  E-value: 5.39e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605039  10 KAMDPDTFYFQFKNLWEANNRNETWLCFTVEviKQRSTVSWeRGVFQNQvdpKSHCHAERCFLSWFC-EDILSPNTDYQV 88
Cdd:pfam18778   1 ERMSPETFKFQFKNVEYASGRNKTLLCYEVK--RGNSSSLW-RGHLRNE---NSGCHAEICFLRWFSsWRLFDPSQCYTI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605039  89 TWYTSWSPCPECAGEVAEFLARHNNVMLTIYTARLYYSQDPNYQQGLRSLSEKGVSVKIMDYEDFKYCWEKFVYDDGEPF 168
Cdd:pfam18778  75 TWYLSWSPCPSCAAKLAEFLKAHPNVTLTIFAARLYYFEDPWNQEGLRSLASAGVTLSIMDYSDFEYCWENFVDNEGRPF 154

                         170       180
                  ....*....|....*....|.
gi 1067605039 169 KPWKGINTNFRFLKRRLREIL 189
Cdd:pfam18778 155 VPWEDLEENSRYYHRKLQRIL 175
APOBEC_N pfam08210
APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. ...
 17-187 5.21e-77

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: 227.63  E-value: 5.21e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605039  17 FYFQFKNLWEANNRNETWLCFTVEViKQRSTVSWERGVFQNQVDPksHCHAERCFLSWFCEDILSPNTDYQVTWYTSWSP 96
Cdd:pfam08210   1 FFFHFKNLPYASGRHETYLCYEVKR-DSGGLVVEDKGYLRNQAAS--SLHAEERFLRWIHDLALDPGSNYEVTWYVSWSP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605039  97 CPECAGEVAEFLARHNNVMLTIYTARLYYSQDPNYQ--QGLRSLSEKGVSVKIMDYEDFKYCWEKFVYDDGEPFKPWKGI 174
Cdd:pfam08210  78 CNECASELAAFLSKHPNVRLRIFVSRLYYWEEPDYWnrEGLRSLAQAGVQLRPMSYKDFEYCWNNFVDHDGEPFKPWDGL 157

                         170
                  ....*....|...
gi 1067605039 175 NTNFRFLKRRLRE 187
Cdd:pfam08210 158 HENSVYLARKLQE 170
SNAD4 pfam18750
Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases ...
 39-159 2.90e-58

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: 178.22  E-value: 2.90e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605039  39 VEVIKQRSTVSWERGVFQNqvdpKSHCHAERCFLSWFCEDILSPNTDYQVTWYTSWSPCPECAGEVAEFLARHNNVMLTI 118
Cdd:pfam18750   1 YEIKWGNGSKIWQRGYLSN----EHEQHAEICFLENIRSRELDPSQRYRVTWYLSWSPCPECAQKIAEFLAEHPNVTLTI 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1067605039 119 YTARLYYsQDPNYQQGLRSLSEKGVSVKIMDYEDFKYCWEK 159
Cdd:pfam18750  77 FAARLYH-WDEDNRQGLRSLAQAGVTLQIMTLEDFEYCWKN 116
APOBEC_C pfam05240
APOBEC-like C-terminal domain; This domain is found at the C-termini of the Apolipoprotein B ...
 113-189 1.24e-39

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: 129.91  E-value: 1.24e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067605039 113 NVMLTIYTARLYYSQDPNYQQGLRSLSEKGVSVKIMDYEDFKYCWEKFVYDDGEPFKPWKGINTNFRFLKRRLREIL 189
Cdd:pfam05240   2 NVSLTIFAARLYYHWDPEYQQGLRRLVQAGAQVAIMSYKEFEYCWDNFVDNQGRPFQPWEGLEENSQLLSRRLQEIL 78
APOBEC3 pfam18771
APOBEC3; APOBEC3 deaminases act as restriction factors in the innate response to retroviruses ...
 33-169 1.41e-34

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: 118.74  E-value: 1.41e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605039  33 TWLCFTVeviKQRSTVSWERGVFQNqvdpKSHCHAERCFLSWFCEDILSPNTDYQVTWYTSWSPCPECAGEVAEFLARHN 112
Cdd:pfam18771   6 AYLCYQL---KGRNGSALDRGYFSN----KKKRHAEIRFIDKIRSLDLDNIQCYRITCYITWSPCPNCAAELVDFISLNP 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1067605039 113 NVMLTIYTARLYYSQDPNYQQGLRSLSEKGVSVKIMDYEDFKYCWEKFVYDDGEPFK 169
Cdd:pfam18771  79 HLKLRIFASRLYYHWERSYKEGLQKLQRAGVSVAVMTLPEFQDCWEDFVDHQEEPFR 135
APOBEC4 pfam18775
APOBEC4; A member of the AID/APOBEC family of cytosine deaminases. The biological function of ...
 88-161 8.57e-26

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: 94.33  E-value: 8.57e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067605039  88 VTWYTSWSPCPECAGEVAEFLARHNNVMLTIYTARLYYSQDPNYQQGLRSLSEKGVSVKIMDYEDFKYCWEKFV 161
Cdd:pfam18775   1 VTLYLSWSPCNECSEKIQEFLKKHPKVNLDIYFAQLYHTEEEDNRQGLRSLVEKGVTLSVMSGEDWIYCLRTFV 74
APOBEC4_like pfam18774
APOBEC4-like -AID/APOBEC-deaminase; Cnidarian and Algal homologs of the APOBEC4-like AID ...
 41-161 3.10e-25

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: 94.94  E-value: 3.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605039  41 VIKQRSTVSWERGV-FQNQVDPKSHCHAERCFLSWFCEDilSPNTDYQVTWYTSWSPCPECAGEVAEFLARHNNVMLTIY 119
Cdd:pfam18774  10 EICLLYEIQWGRGTiWRNWTENNCTEHAEVNFLENFRSE--RPSRSCTITWYLSWSPCWECSGRILEFLSRHPNVTLGIY 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1067605039 120 TARLYYSQDPNYQQGLRSLSEKGVSVKIMDYEDFKYCWEKFV 161
Cdd:pfam18774  88 VARLFMHDDDRNRQGLRILQMNGVTIQVMMNKDYCYCWKAFK 129
APOBEC1 pfam18769
APOBEC1; APOBEC1 deaminates cytosine both in RNA and ssDNA and has roles in both mRNA editing ...
 66-148 2.83e-21

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: 83.71  E-value: 2.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605039  66 HAERCFL-SWFCEDILSPNTDYQVTWYTSWSPCPECAGEVAEFLARHNNVMLTIYTARLYYSQDPNYQQGLRSLSEKGVS 144
Cdd:pfam18769  18 HAEVNFLeKFFSERHFDPSVSCSITWFLSWSPCGECSKAIGEFLSQHPNVTLVIYAARLFKHLDIRNRQGLRDLAMSGVT 97


                  ....
gi 1067605039 145 VKIM 148
Cdd:pfam18769  98 IQIM 101
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 8-158 3.87e-14

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: 65.44  E-value: 3.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605039   8 PIKAMDPDTFYfqfknlwEANNRNETWLCFTVEvikqrSTVSWERGVFQNQVDPKSHCHAERCFLSWFCEDILspnTDYQ 87
Cdd:cd01283     1 IEAALAAAEFA-------YAPYSNFTVGAALLT-----KDGRIFTGVNVENASYGLTLCAERTAIGKAVSEGL---RRYL 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067605039  88 VTWYTS-----WSPCPECAGEVAEFLArhnnvmltiytARLYYSQDPNYQQglrslsekgvsvkimdyeDFKYCWE 158
Cdd:cd01283    66 VTWAVSdeggvWSPCGACRQVLAEFLP-----------SRLYIIIDNPKGE------------------EFAYTLS 112
 
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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