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Conserved domains on  [gi|23396445|sp|Q9WV35|]
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RecName: Full=C-

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 ...
 47-224 2.75e-82

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: 242.50  E-value: 2.75e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396445    47 LPVNFFKFQFRNVEYSSGRNKTFLCYVVEVQSkGGQAQATQGYLEDEhAGAHAEEAFFNTILP-AFDPALKYNVTWYVSS 125
Cdd:pfam18772   1 MDPKTFKFQFKNVPYASGRNKTYLCYEVETRS-GSDLSPDRGYLRNQ-AGCHAELCFLSWILPwQLDPGQKYQVTWYVSW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396445   126 SPCAACADRILKTLSKTKNLRLLILVSRLFMWEEPEVQAALKKLKEAGCKLRIMKPQDFEYIWQNFVEQEEgesKAFEPW 205
Cdd:pfam18772  79 SPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDNQG---RPFEPW 155

                         170
                  ....*....|....*....
gi 23396445   206 EDIQENFLYYEEKLADILK 224
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 ...
 47-224 2.75e-82

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: 242.50  E-value: 2.75e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396445    47 LPVNFFKFQFRNVEYSSGRNKTFLCYVVEVQSkGGQAQATQGYLEDEhAGAHAEEAFFNTILP-AFDPALKYNVTWYVSS 125
Cdd:pfam18772   1 MDPKTFKFQFKNVPYASGRNKTYLCYEVETRS-GSDLSPDRGYLRNQ-AGCHAELCFLSWILPwQLDPGQKYQVTWYVSW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396445   126 SPCAACADRILKTLSKTKNLRLLILVSRLFMWEEPEVQAALKKLKEAGCKLRIMKPQDFEYIWQNFVEQEEgesKAFEPW 205
Cdd:pfam18772  79 SPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDNQG---RPFEPW 155

                         170
                  ....*....|....*....
gi 23396445   206 EDIQENFLYYEEKLADILK 224
Cdd:pfam18772 156 EDLDENYEYLSRKLQEILR 174
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 61-151 1.11e-07

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: 48.88  E-value: 1.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396445  61 YSSGRNKTFLCYVVEvqsKGGQAqaTQGYLEDEHA---GAHAEEAFFNTILPAFDPalKYNVTWYVSS-----SPCAACA 132
Cdd:cd01283  12 YAPYSNFTVGAALLT---KDGRI--FTGVNVENASyglTLCAERTAIGKAVSEGLR--RYLVTWAVSDeggvwSPCGACR 84

                        90
                ....*....|....*....
gi 23396445 133 DRILKTLSKtknlRLLILV 151
Cdd:cd01283  85 QVLAEFLPS----RLYIII 99
 
Name Accession Description Interval E-value
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 47-224 2.75e-82

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: 242.50  E-value: 2.75e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396445    47 LPVNFFKFQFRNVEYSSGRNKTFLCYVVEVQSkGGQAQATQGYLEDEhAGAHAEEAFFNTILP-AFDPALKYNVTWYVSS 125
Cdd:pfam18772   1 MDPKTFKFQFKNVPYASGRNKTYLCYEVETRS-GSDLSPDRGYLRNQ-AGCHAELCFLSWILPwQLDPGQKYQVTWYVSW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396445   126 SPCAACADRILKTLSKTKNLRLLILVSRLFMWEEPEVQAALKKLKEAGCKLRIMKPQDFEYIWQNFVEQEEgesKAFEPW 205
Cdd:pfam18772  79 SPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDNQG---RPFEPW 155

                         170
                  ....*....|....*....
gi 23396445   206 EDIQENFLYYEEKLADILK 224
Cdd:pfam18772 156 EDLDENYEYLSRKLQEILR 174
NAD1 pfam18778
Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned ...
 46-223 2.15e-79

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: 235.25  E-value: 2.15e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396445    46 RLPVNFFKFQFRNVEYSSGRNKTFLCYVVEVQSKGGQaqaTQGYLEDEHAGAHAEEAFFNTI--LPAFDPALKYNVTWYV 123
Cdd:pfam18778   2 RMSPETFKFQFKNVEYASGRNKTLLCYEVKRGNSSSL---WRGHLRNENSGCHAEICFLRWFssWRLFDPSQCYTITWYL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396445   124 SSSPCAACADRILKTLSKTKNLRLLILVSRLFMWEEPEVQAALKKLKEAGCKLRIMKPQDFEYIWQNFVEQEEgesKAFE 203
Cdd:pfam18778  79 SWSPCPSCAAKLAEFLKAHPNVTLTIFAARLYYFEDPWNQEGLRSLASAGVTLSIMDYSDFEYCWENFVDNEG---RPFV 155

                         170       180
                  ....*....|....*....|
gi 23396445   204 PWEDIQENFLYYEEKLADIL 223
Cdd:pfam18778 156 PWEDLEENSRYYHRKLQRIL 175
APOBEC_N pfam08210
APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. ...
 52-221 7.86e-72

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: 216.08  E-value: 7.86e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396445    52 FKFQFRNVEYSSGRNKTFLCYVVEVQSKGGQAQaTQGYLEDEHA-GAHAEEAFFNTI-LPAFDPALKYNVTWYVSSSPCA 129
Cdd:pfam08210   1 FFFHFKNLPYASGRHETYLCYEVKRDSGGLVVE-DKGYLRNQAAsSLHAEERFLRWIhDLALDPGSNYEVTWYVSWSPCN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396445   130 ACADRILKTLSKTKNLRLLILVSRLFMWEEPEVQA--ALKKLKEAGCKLRIMKPQDFEYIWQNFVEQEEgesKAFEPWED 207
Cdd:pfam08210  80 ECASELAAFLSKHPNVRLRIFVSRLYYWEEPDYWNreGLRSLAQAGVQLRPMSYKDFEYCWNNFVDHDG---EPFKPWDG 156

                         170
                  ....*....|....
gi 23396445   208 IQENFLYYEEKLAD 221
Cdd:pfam08210 157 LHENSVYLARKLQE 170
SNAD4 pfam18750
Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases ...
 74-190 3.51e-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: 141.24  E-value: 3.51e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396445    74 VEVQSKGGQAQATQGYLEDEHaGAHAEEAFFNTILP-AFDPALKYNVTWYVSSSPCAACADRILKTLSKTKNLRLLILVS 152
Cdd:pfam18750   1 YEIKWGNGSKIWQRGYLSNEH-EQHAEICFLENIRSrELDPSQRYRVTWYLSWSPCPECAQKIAEFLAEHPNVTLTIFAA 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 23396445   153 RLFMWEEPEvQAALKKLKEAGCKLRIMKPQDFEYIWQN 190
Cdd:pfam18750  80 RLYHWDEDN-RQGLRSLAQAGVTLQIMTLEDFEYCWKN 116
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 52-223 1.41e-38

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: 131.72  E-value: 1.41e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396445    52 FKFQFRNVEYSSGRNKTFLCYVVEVQSKGGQAQATQGYLEDEhAGAHAEEAFFNTI-LPAFDPALKYNVTWYVSSSPCAA 130
Cdd:pfam18782   8 FYFNFNNKPILYGRNKTYLCYEVERLDNGTWLPQHRGFFRNQ-AKYHAELCFLSWFcGNQLPPYQNYQVTWYVSWSPCPE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396445   131 CADRILKTLSKTKNLRLLILVSRLFMWEEPEVQAALKKLKEAGCKLRIMKPQDFEYIWQNFVeqeEGESKAFEPWEDIQE 210
Cdd:pfam18782  87 CAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFV---YNQGEPFQPWDGLEE 163

                         170
                  ....*....|...
gi 23396445   211 NFLYYEEKLADIL 223
Cdd:pfam18782 164 NSRFLHRRLREIL 176
APOBEC_C pfam05240
APOBEC-like C-terminal domain; This domain is found at the C-termini of the Apolipoprotein B ...
 143-223 1.54e-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: 112.96  E-value: 1.54e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396445   143 KNLRLLILVSRLFMWEEPEVQAALKKLKEAGCKLRIMKPQDFEYIWQNFVEQEEgesKAFEPWEDIQENFLYYEEKLADI 222
Cdd:pfam05240   1 PNVSLTIFAARLYYHWDPEYQQGLRRLVQAGAQVAIMSYKEFEYCWDNFVDNQG---RPFQPWEGLEENSQLLSRRLQEI 77


                  .
gi 23396445   223 L 223
Cdd:pfam05240  78 L 78
APOBEC4 pfam18775
APOBEC4; A member of the AID/APOBEC family of cytosine deaminases. The biological function of ...
 119-192 3.32e-17

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: 73.14  E-value: 3.32e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23396445   119 VTWYVSSSPCAACADRILKTLSKTKNLRLLILVSRLFMWEEPEVQAALKKLKEAGCKLRIMKPQDFEYIWQNFV 192
Cdd:pfam18775   1 VTLYLSWSPCNECSEKIQEFLKKHPKVNLDIYFAQLYHTEEEDNRQGLRSLVEKGVTLSVMSGEDWIYCLRTFV 74
APOBEC4_like pfam18774
APOBEC4-like -AID/APOBEC-deaminase; Cnidarian and Algal homologs of the APOBEC4-like AID ...
 98-193 7.12e-17

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: 74.14  E-value: 7.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396445    98 HAEEAFFNTILPAfDPALKYNVTWYVSSSPCAACADRILKTLSKTKNLRLLILVSRLFMWEEPEVQAALKKLKEAGCKLR 177
Cdd:pfam18774  36 HAEVNFLENFRSE-RPSRSCTITWYLSWSPCWECSGRILEFLSRHPNVTLGIYVARLFMHDDDRNRQGLRILQMNGVTIQ 114

                          90
                  ....*....|....*.
gi 23396445   178 IMKPQDFEYIWQNFVE 193
Cdd:pfam18774 115 VMMNKDYCYCWKAFKN 130
APOBEC1 pfam18769
APOBEC1; APOBEC1 deaminates cytosine both in RNA and ssDNA and has roles in both mRNA editing ...
 98-179 3.85e-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: 63.29  E-value: 3.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396445    98 HAEEAFFNTILPA--FDPALKYNVTWYVSSSPCAACADRILKTLSKTKNLRLLILVSRLFMWEEPEVQAALKKLKEAGCK 175
Cdd:pfam18769  18 HAEVNFLEKFFSErhFDPSVSCSITWFLSWSPCGECSKAIGEFLSQHPNVTLVIYAARLFKHLDIRNRQGLRDLAMSGVT 97


                  ....
gi 23396445   176 LRIM 179
Cdd:pfam18769  98 IQIM 101
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 61-151 1.11e-07

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: 48.88  E-value: 1.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396445  61 YSSGRNKTFLCYVVEvqsKGGQAqaTQGYLEDEHA---GAHAEEAFFNTILPAFDPalKYNVTWYVSS-----SPCAACA 132
Cdd:cd01283  12 YAPYSNFTVGAALLT---KDGRI--FTGVNVENASyglTLCAERTAIGKAVSEGLR--RYLVTWAVSDeggvwSPCGACR 84

                        90
                ....*....|....*....
gi 23396445 133 DRILKTLSKtknlRLLILV 151
Cdd:cd01283  85 QVLAEFLPS----RLYIII 99
 
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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