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Conserved domains on  [gi|1958768299|ref|XP_038963038|]
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Protein Classification

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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 ...
 86-256 1.92e-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: 218.30  E-value: 1.92e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768299  86 RRIEPHEFEVFFDPRE---LRKETCLLYEINWGGRHSIWR-HTS-QNTNKHVEVNFIEKFTTERYFCPNTRCSITWFLSW 160
Cdd:pfam18778   1 ERMSPETFKFQFKNVEyasGRNKTLLCYEVKRGNSSSLWRgHLRnENSGCHAEICFLRWFSSWRLFDPSQCYTITWYLSW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768299 161 SPCGECSRAITEFLSRYPHVTLFIYIARLYHHADPRNRQGLRDLISSGVTIQIMTEQESGYCWRNFVNYSPSNEAHWPRy 240
Cdd:pfam18778  81 SPCPSCAAKLAEFLKAHPNVTLTIFAARLYYFEDPWNQEGLRSLASAGVTLSIMDYSDFEYCWENFVDNEGRPFVPWED- 159

                         170
                  ....*....|....*.
gi 1958768299 241 PHLWVRLYVLELYCII 256
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 ...
 86-256 1.92e-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: 218.30  E-value: 1.92e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768299  86 RRIEPHEFEVFFDPRE---LRKETCLLYEINWGGRHSIWR-HTS-QNTNKHVEVNFIEKFTTERYFCPNTRCSITWFLSW 160
Cdd:pfam18778   1 ERMSPETFKFQFKNVEyasGRNKTLLCYEVKRGNSSSLWRgHLRnENSGCHAEICFLRWFSSWRLFDPSQCYTITWYLSW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768299 161 SPCGECSRAITEFLSRYPHVTLFIYIARLYHHADPRNRQGLRDLISSGVTIQIMTEQESGYCWRNFVNYSPSNEAHWPRy 240
Cdd:pfam18778  81 SPCPSCAAKLAEFLKAHPNVTLTIFAARLYYFEDPWNQEGLRSLASAGVTLSIMDYSDFEYCWENFVDNEGRPFVPWED- 159

                         170
                  ....*....|....*.
gi 1958768299 241 PHLWVRLYVLELYCII 256
Cdd:pfam18778 160 LEENSRYYHRKLQRIL 175
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 84-199 2.08e-11

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: 59.66  E-value: 2.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768299  84 LRRRIEPHEFEvffdPRELRKETCLLYEINWGGRhsIWR-----HTSQNTNKHVEVNFIEKFTTERYfcpnTRCSITWFL 158
Cdd:cd01283     1 IEAALAAAEFA----YAPYSNFTVGAALLTKDGR--IFTgvnveNASYGLTLCAERTAIGKAVSEGL----RRYLVTWAV 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958768299 159 S-----WSPCGECSRAITEFLSryphvtlfiyiARLYHHADPRNRQ 199
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 ...
 86-256 1.92e-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: 218.30  E-value: 1.92e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768299  86 RRIEPHEFEVFFDPRE---LRKETCLLYEINWGGRHSIWR-HTS-QNTNKHVEVNFIEKFTTERYFCPNTRCSITWFLSW 160
Cdd:pfam18778   1 ERMSPETFKFQFKNVEyasGRNKTLLCYEVKRGNSSSLWRgHLRnENSGCHAEICFLRWFSSWRLFDPSQCYTITWYLSW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768299 161 SPCGECSRAITEFLSRYPHVTLFIYIARLYHHADPRNRQGLRDLISSGVTIQIMTEQESGYCWRNFVNYSPSNEAHWPRy 240
Cdd:pfam18778  81 SPCPSCAAKLAEFLKAHPNVTLTIFAARLYYFEDPWNQEGLRSLASAGVTLSIMDYSDFEYCWENFVDNEGRPFVPWED- 159

                         170
                  ....*....|....*.
gi 1958768299 241 PHLWVRLYVLELYCII 256
Cdd:pfam18778 160 LEENSRYYHRKLQRIL 175
APOBEC1 pfam18769
APOBEC1; APOBEC1 deaminates cytosine both in RNA and ssDNA and has roles in both mRNA editing ...
 114-214 2.84e-61

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: 189.64  E-value: 2.84e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768299 114 WGGRHSIWRHTSQNTNKHVEVNFIEKFTTERYFCPNTRCSITWFLSWSPCGECSRAITEFLSRYPHVTLFIYIARLYHHA 193
Cdd:pfam18769   1 WGRRGTIWRNCGNNTTQHAEVNFLEKFFSERHFDPSVSCSITWFLSWSPCGECSKAIGEFLSQHPNVTLVIYAARLFKHL 80

                          90       100
                  ....*....|....*....|.
gi 1958768299 194 DPRNRQGLRDLISSGVTIQIM 214
Cdd:pfam18769  81 DIRNRQGLRDLAMSGVTIQIM 101
APOBEC4_like pfam18774
APOBEC4-like -AID/APOBEC-deaminase; Cnidarian and Algal homologs of the APOBEC4-like AID ...
 96-229 5.03e-55

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: 174.68  E-value: 5.03e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768299  96 FFDPRELRKETCLLYEINWGgRHSIWRH-TSQNTNKHVEVNFIEKFTTERyfcPNTRCSITWFLSWSPCGECSRAITEFL 174
Cdd:pfam18774   1 NFDPNNHKKEICLLYEIQWG-RGTIWRNwTENNCTEHAEVNFLENFRSER---PSRSCTITWYLSWSPCWECSGRILEFL 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958768299 175 SRYPHVTLFIYIARLYHHADPRNRQGLRDLISSGVTIQIMTEQESGYCWRNFVNY 229
Cdd:pfam18774  77 SRHPNVTLGIYVARLFMHDDDRNRQGLRILQMNGVTIQVMMNKDYCYCWKAFKNY 131
SNAD4 pfam18750
Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases ...
 110-225 7.88e-52

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: 165.90  E-value: 7.88e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768299 110 YEINWGGRHSIW-RHTSQN-TNKHVEVNFIEKFTtERYFCPNTRCSITWFLSWSPCGECSRAITEFLSRYPHVTLFIYIA 187
Cdd:pfam18750   1 YEIKWGNGSKIWqRGYLSNeHEQHAEICFLENIR-SRELDPSQRYRVTWYLSWSPCPECAQKIAEFLAEHPNVTLTIFAA 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958768299 188 RLYHHaDPRNRQGLRDLISSGVTIQIMTEQESGYCWRN 225
Cdd:pfam18750  80 RLYHW-DEDNRQGLRSLAQAGVTLQIMTLEDFEYCWKN 116
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 103-227 1.92e-32

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: 118.09  E-value: 1.92e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768299 103 RKETCLLYEINWGGRHSIWRHTSQNTNK---HVEVNFIEKFTTERYfCPNTRCSITWFLSWSPCGECSRAITEFLSRYPH 179
Cdd:pfam18772  19 RNKTYLCYEVETRSGSDLSPDRGYLRNQagcHAELCFLSWILPWQL-DPGQKYQVTWYVSWSPCPDCARKLAEFLARHPN 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958768299 180 VTLFIYIARLYHHADPRNRQGLRDLISSGVTIQIMTEQESGYCWRNFV 227
Cdd:pfam18772  98 LSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFV 145
APOBEC_N pfam08210
APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. ...
 103-239 2.34e-31

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: 115.16  E-value: 2.34e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768299 103 RKETCLLYEINWGGRHSIWRHTSQNTNK-----HVEVNFIEKFTTERyFCPNTRCSITWFLSWSPCGECSRAITEFLSRY 177
Cdd:pfam08210  14 RHETYLCYEVKRDSGGLVVEDKGYLRNQaasslHAEERFLRWIHDLA-LDPGSNYEVTWYVSWSPCNECASELAAFLSKH 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958768299 178 PHVTLFIYIARLYHHADP--RNRQGLRDLISSGVTIQIMTEQESGYCWRNFVNYSPSNEAHWPR 239
Cdd:pfam08210  93 PNVRLRIFVSRLYYWEEPdyWNREGLRSLAQAGVQLRPMSYKDFEYCWNNFVDHDGEPFKPWDG 156
APOBEC4 pfam18775
APOBEC4; A member of the AID/APOBEC family of cytosine deaminases. The biological function of ...
 154-227 6.38e-30

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: 108.19  E-value: 6.38e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958768299 154 ITWFLSWSPCGECSRAITEFLSRYPHVTLFIYIARLYHHADPRNRQGLRDLISSGVTIQIMTEQESGYCWRNFV 227
Cdd:pfam18775   1 VTLYLSWSPCNECSEKIQEFLKKHPKVNLDIYFAQLYHTEEEDNRQGLRSLVEKGVTLSVMSGEDWIYCLRTFV 74
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 87-228 1.82e-25

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: 99.75  E-value: 1.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768299  87 RIEPHEFEVFFDPREL---RKETCLLYEIN-WGGRHSIWRHTSQNTNK---HVEVNFIEKFTTeRYFCPNTRCSITWFLS 159
Cdd:pfam18782   2 RMYPRTFYFNFNNKPIlygRNKTYLCYEVErLDNGTWLPQHRGFFRNQakyHAELCFLSWFCG-NQLPPYQNYQVTWYVS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958768299 160 WSPCGECSRAITEFLSRYPHVTLFIYIARLYHHADPRNRQGLRDLISSGVTIQIMTEQESGYCWRNFVN 228
Cdd:pfam18782  81 WSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVY 149
APOBEC_C pfam05240
APOBEC-like C-terminal domain; This domain is found at the C-termini of the Apolipoprotein B ...
 178-256 1.39e-23

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: 1.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768299 178 PHVTLFIYIARLYHHADPRNRQGLRDLISSGVTIQIMTEQESGYCWRNFVNYspsneAHWPRYP----HLWVRLYVLELY 253
Cdd:pfam05240   1 PNVSLTIFAARLYYHWDPEYQQGLRRLVQAGAQVAIMSYKEFEYCWDNFVDN-----QGRPFQPweglEENSQLLSRRLQ 75


                  ...
gi 1958768299 254 CII 256
Cdd:pfam05240  76 EIL 78
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 84-199 2.08e-11

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: 59.66  E-value: 2.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768299  84 LRRRIEPHEFEvffdPRELRKETCLLYEINWGGRhsIWR-----HTSQNTNKHVEVNFIEKFTTERYfcpnTRCSITWFL 158
Cdd:cd01283     1 IEAALAAAEFA----YAPYSNFTVGAALLTKDGR--IFTgvnveNASYGLTLCAERTAIGKAVSEGL----RRYLVTWAV 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958768299 159 S-----WSPCGECSRAITEFLSryphvtlfiyiARLYHHADPRNRQ 199
Cdd:cd01283    71 SdeggvWSPCGACRQVLAEFLP-----------SRLYIIIDNPKGE 105
AID pfam18767
Activation induced deaminase; The activation induced deaminase is a vertebrate-specific member ...
 161-223 4.64e-03

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: 35.61  E-value: 4.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958768299 161 SPCGECSRAITEFLSRYPhVTLFIYIARLYHHADPRNRQGLRDLISSGVTIQIMTEQESGYCW 223
Cdd:pfam18767  29 SPCHRCSEVLLKHFSRPP-LKPTIHIGRISRSFDSDDDKGLIQLLKNGFNIKVWPHLTALVCW 90
 
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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