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Conserved domains on  [gi|74198961|dbj|BAE30699|]
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unnamed protein product [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NAD1 pfam18778
Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned ...
 16-186 4.80e-67

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: 204.43  E-value: 4.80e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74198961    16 RRIEPHEFEVFFDPRE---LRKETCLLYEINWGGRHSVWR-HTS-QNTSNHVEVNFLEKFTTERYFRPNTRCSITWFLSW 90
Cdd:pfam18778   1 ERMSPETFKFQFKNVEyasGRNKTLLCYEVKRGNSSSLWRgHLRnENSGCHAEICFLRWFSSWRLFDPSQCYTITWYLSW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74198961    91 SPCGECSRAITEFLSRHPYVTLFIYIARLYHHTDQRNRQGLRDLISSGVTIQIMTEQEYCYCWRNFVNYPPSNEAYWPRy 170
Cdd:pfam18778  81 SPCPSCAAKLAEFLKAHPNVTLTIFAARLYYFEDPWNQEGLRSLASAGVTLSIMDYSDFEYCWENFVDNEGRPFVPWED- 159

                         170
                  ....*....|....*.
gi 74198961   171 PHLWVKLYVLELYCII 186
Cdd:pfam18778 160 LEENSRYYHRKLQRIL 175
 
Name Accession Description Interval E-value
NAD1 pfam18778
Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned ...
 16-186 4.80e-67

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: 204.43  E-value: 4.80e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74198961    16 RRIEPHEFEVFFDPRE---LRKETCLLYEINWGGRHSVWR-HTS-QNTSNHVEVNFLEKFTTERYFRPNTRCSITWFLSW 90
Cdd:pfam18778   1 ERMSPETFKFQFKNVEyasGRNKTLLCYEVKRGNSSSLWRgHLRnENSGCHAEICFLRWFSSWRLFDPSQCYTITWYLSW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74198961    91 SPCGECSRAITEFLSRHPYVTLFIYIARLYHHTDQRNRQGLRDLISSGVTIQIMTEQEYCYCWRNFVNYPPSNEAYWPRy 170
Cdd:pfam18778  81 SPCPSCAAKLAEFLKAHPNVTLTIFAARLYYFEDPWNQEGLRSLASAGVTLSIMDYSDFEYCWENFVDNEGRPFVPWED- 159

                         170
                  ....*....|....*.
gi 74198961   171 PHLWVKLYVLELYCII 186
Cdd:pfam18778 160 LEENSRYYHRKLQRIL 175
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 14-129 1.75e-10

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: 56.58  E-value: 1.75e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74198961  14 LRRRIEPHEFEvffdPRELRKETCLLYEINWGGRhsVWR-----HTSQNTSNHVEVNFLEKFTTERYfrpnTRCSITWFL 88
Cdd:cd01283   1 IEAALAAAEFA----YAPYSNFTVGAALLTKDGR--IFTgvnveNASYGLTLCAERTAIGKAVSEGL----RRYLVTWAV 70

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 74198961  89 S-----WSPCGECSRAITEFLSrhpyvtlfiyiARLYHHTDQRNRQ 129
Cdd:cd01283  71 SdeggvWSPCGACRQVLAEFLP-----------SRLYIIIDNPKGE 105
 
Name Accession Description Interval E-value
NAD1 pfam18778
Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned ...
 16-186 4.80e-67

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: 204.43  E-value: 4.80e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74198961    16 RRIEPHEFEVFFDPRE---LRKETCLLYEINWGGRHSVWR-HTS-QNTSNHVEVNFLEKFTTERYFRPNTRCSITWFLSW 90
Cdd:pfam18778   1 ERMSPETFKFQFKNVEyasGRNKTLLCYEVKRGNSSSLWRgHLRnENSGCHAEICFLRWFSSWRLFDPSQCYTITWYLSW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74198961    91 SPCGECSRAITEFLSRHPYVTLFIYIARLYHHTDQRNRQGLRDLISSGVTIQIMTEQEYCYCWRNFVNYPPSNEAYWPRy 170
Cdd:pfam18778  81 SPCPSCAAKLAEFLKAHPNVTLTIFAARLYYFEDPWNQEGLRSLASAGVTLSIMDYSDFEYCWENFVDNEGRPFVPWED- 159

                         170
                  ....*....|....*.
gi 74198961   171 PHLWVKLYVLELYCII 186
Cdd:pfam18778 160 LEENSRYYHRKLQRIL 175
APOBEC1 pfam18769
APOBEC1; APOBEC1 deaminates cytosine both in RNA and ssDNA and has roles in both mRNA editing ...
 44-144 5.69e-64

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: 193.88  E-value: 5.69e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74198961    44 WGGRHSVWRHTSQNTSNHVEVNFLEKFTTERYFRPNTRCSITWFLSWSPCGECSRAITEFLSRHPYVTLFIYIARLYHHT 123
Cdd:pfam18769   1 WGRRGTIWRNCGNNTTQHAEVNFLEKFFSERHFDPSVSCSITWFLSWSPCGECSKAIGEFLSQHPNVTLVIYAARLFKHL 80

                          90       100
                  ....*....|....*....|.
gi 74198961   124 DQRNRQGLRDLISSGVTIQIM 144
Cdd:pfam18769  81 DIRNRQGLRDLAMSGVTIQIM 101
APOBEC4_like pfam18774
APOBEC4-like -AID/APOBEC-deaminase; Cnidarian and Algal homologs of the APOBEC4-like AID ...
 26-159 3.99e-58

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: 180.07  E-value: 3.99e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74198961    26 FFDPRELRKETCLLYEINWGgRHSVWRH-TSQNTSNHVEVNFLEKFTTERyfrPNTRCSITWFLSWSPCGECSRAITEFL 104
Cdd:pfam18774   1 NFDPNNHKKEICLLYEIQWG-RGTIWRNwTENNCTEHAEVNFLENFRSER---PSRSCTITWYLSWSPCWECSGRILEFL 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 74198961   105 SRHPYVTLFIYIARLYHHTDQRNRQGLRDLISSGVTIQIMTEQEYCYCWRNFVNY 159
Cdd:pfam18774  77 SRHPNVTLGIYVARLFMHDDDRNRQGLRILQMNGVTIQVMMNKDYCYCWKAFKNY 131
SNAD4 pfam18750
Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases ...
 40-155 6.87e-53

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


Pssm-ID: 465854 [Multi-domain]  Cd Length: 116  Bit Score: 166.28  E-value: 6.87e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74198961    40 YEINWGGRHSVW-RHTSQNTSN-HVEVNFLEKFTtERYFRPNTRCSITWFLSWSPCGECSRAITEFLSRHPYVTLFIYIA 117
Cdd:pfam18750   1 YEIKWGNGSKIWqRGYLSNEHEqHAEICFLENIR-SRELDPSQRYRVTWYLSWSPCPECAQKIAEFLAEHPNVTLTIFAA 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 74198961   118 RLYHHtDQRNRQGLRDLISSGVTIQIMTEQEYCYCWRN 155
Cdd:pfam18750  80 RLYHW-DEDNRQGLRSLAQAGVTLQIMTLEDFEYCWKN 116
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 33-157 1.35e-33

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: 118.86  E-value: 1.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74198961    33 RKETCLLYEINWGGRHSVWRHTSQ---NTSNHVEVNFLEKFTTERYfRPNTRCSITWFLSWSPCGECSRAITEFLSRHPY 109
Cdd:pfam18772  19 RNKTYLCYEVETRSGSDLSPDRGYlrnQAGCHAELCFLSWILPWQL-DPGQKYQVTWYVSWSPCPDCARKLAEFLARHPN 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 74198961   110 VTLFIYIARLYHHTDQRNRQGLRDLISSGVTIQIMTEQEYCYCWRNFV 157
Cdd:pfam18772  98 LSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFV 145
APOBEC4 pfam18775
APOBEC4; A member of the AID/APOBEC family of cytosine deaminases. The biological function of ...
 84-157 6.19e-32

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: 111.27  E-value: 6.19e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74198961    84 ITWFLSWSPCGECSRAITEFLSRHPYVTLFIYIARLYHHTDQRNRQGLRDLISSGVTIQIMTEQEYCYCWRNFV 157
Cdd:pfam18775   1 VTLYLSWSPCNECSEKIQEFLKKHPKVNLDIYFAQLYHTEEEDNRQGLRSLVEKGVTLSVMSGEDWIYCLRTFV 74
APOBEC_N pfam08210
APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. ...
 33-169 1.46e-30

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: 110.92  E-value: 1.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74198961    33 RKETCLLYEINWGGRHSVWRH----TSQNTSN-HVEVNFLEKFTTERyFRPNTRCSITWFLSWSPCGECSRAITEFLSRH 107
Cdd:pfam08210  14 RHETYLCYEVKRDSGGLVVEDkgylRNQAASSlHAEERFLRWIHDLA-LDPGSNYEVTWYVSWSPCNECASELAAFLSKH 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74198961   108 PYVTLFIYIARLYHH--TDQRNRQGLRDLISSGVTIQIMTEQEYCYCWRNFVNYPPSNEAYWPR 169
Cdd:pfam08210  93 PNVRLRIFVSRLYYWeePDYWNREGLRSLAQAGVQLRPMSYKDFEYCWNNFVDHDGEPFKPWDG 156
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 17-168 1.72e-26

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: 100.52  E-value: 1.72e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74198961    17 RIEPHEFEVFFDPREL---RKETCLLYEIN-WGGRHSVWRHTS--QNTSN-HVEVNFLEKFTTeRYFRPNTRCSITWFLS 89
Cdd:pfam18782   2 RMYPRTFYFNFNNKPIlygRNKTYLCYEVErLDNGTWLPQHRGffRNQAKyHAELCFLSWFCG-NQLPPYQNYQVTWYVS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74198961    90 WSPCGECSRAITEFLSRHPYVTLFIYIARLYHHTDQRNRQGLRDLISSGVTIQIMTEQEYCYCWRNFVNypPSNEAYWP 168
Cdd:pfam18782  81 WSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVY--NQGEPFQP 157
APOBEC_C pfam05240
APOBEC-like C-terminal domain; This domain is found at the C-termini of the Apolipoprotein B ...
 108-186 2.62e-24

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: 91.78  E-value: 2.62e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74198961   108 PYVTLFIYIARLYHHTDQRNRQGLRDLISSGVTIQIMTEQEYCYCWRNFVNYppSNEAYWPryphlWVKL------YVLE 181
Cdd:pfam05240   1 PNVSLTIFAARLYYHWDPEYQQGLRRLVQAGAQVAIMSYKEFEYCWDNFVDN--QGRPFQP-----WEGLeensqlLSRR 73


                  ....*
gi 74198961   182 LYCII 186
Cdd:pfam05240  74 LQEIL 78
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 14-129 1.75e-10

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: 56.58  E-value: 1.75e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74198961  14 LRRRIEPHEFEvffdPRELRKETCLLYEINWGGRhsVWR-----HTSQNTSNHVEVNFLEKFTTERYfrpnTRCSITWFL 88
Cdd:cd01283   1 IEAALAAAEFA----YAPYSNFTVGAALLTKDGR--IFTgvnveNASYGLTLCAERTAIGKAVSEGL----RRYLVTWAV 70

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 74198961  89 S-----WSPCGECSRAITEFLSrhpyvtlfiyiARLYHHTDQRNRQ 129
Cdd:cd01283  71 SdeggvWSPCGACRQVLAEFLP-----------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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