NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|6753098|ref|NP_033824|]
View 

C-

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
46-223 8.26e-91

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: 408549 [Multi-domain]  Cd Length: 175  Bit Score: 264.13  E-value: 8.26e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753098     46 RLPVNFFKFQFRNVEYSSGRNKTFLCYVVEVQskGGQAQATQGYLEDEHAGAHAEEAFFNTI--LPAFDPALKYNVTWYV 123
Cdd:pfam18778   1 RMSPETFKFQFKNVEYASGRNKTLLCYEVKTR--GNSSSLWRGYLENENSGCHAEICFLRWIldLGLFDPSQKYTITWYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753098    124 SSSPCAACADRILKTLSKTKNLRLLILVSRLFMWEEPEVQAALKKLKEAGCKLRIMKPQDFEYIWQNFVEQEEgesKAFE 203
Cdd:pfam18778  79 SWSPCASCADKLAEFLSAYPNVTLTIFAARLYYWEDPENQEGLRSLASAGVKLRIMDYEDFEYCWQNFVDNEG---RPFT 155
                         170       180
                  ....*....|....*....|
gi 6753098    204 PWEDIQENFLYYEEKLADIL 223
Cdd:pfam18778 156 PWEDLQENSRYYHRKLARIL 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 ...
46-223 8.26e-91

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: 408549 [Multi-domain]  Cd Length: 175  Bit Score: 264.13  E-value: 8.26e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753098     46 RLPVNFFKFQFRNVEYSSGRNKTFLCYVVEVQskGGQAQATQGYLEDEHAGAHAEEAFFNTI--LPAFDPALKYNVTWYV 123
Cdd:pfam18778   1 RMSPETFKFQFKNVEYASGRNKTLLCYEVKTR--GNSSSLWRGYLENENSGCHAEICFLRWIldLGLFDPSQKYTITWYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753098    124 SSSPCAACADRILKTLSKTKNLRLLILVSRLFMWEEPEVQAALKKLKEAGCKLRIMKPQDFEYIWQNFVEQEEgesKAFE 203
Cdd:pfam18778  79 SWSPCASCADKLAEFLSAYPNVTLTIFAARLYYWEDPENQEGLRSLASAGVKLRIMDYEDFEYCWQNFVDNEG---RPFT 155
                         170       180
                  ....*....|....*....|
gi 6753098    204 PWEDIQENFLYYEEKLADIL 223
Cdd:pfam18778 156 PWEDLQENSRYYHRKLARIL 175
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
61-151 1.05e-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: 1.05e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753098   61 YSSGRNKTFLCYVVEvqsKGGQAqaTQGYLEDEHA---GAHAEEAFFNTILPAFDPalKYNVTWYVSS-----SPCAACA 132
Cdd:cd01283  12 YAPYSNFTVGAALLT---KDGRI--FTGVNVENASyglTLCAERTAIGKAVSEGLR--RYLVTWAVSDeggvwSPCGACR 84
                        90
                ....*....|....*....
gi 6753098  133 DRILKTLSKtknlRLLILV 151
Cdd:cd01283  85 QVLAEFLPS----RLYIII 99
 
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 ...
46-223 8.26e-91

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: 408549 [Multi-domain]  Cd Length: 175  Bit Score: 264.13  E-value: 8.26e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753098     46 RLPVNFFKFQFRNVEYSSGRNKTFLCYVVEVQskGGQAQATQGYLEDEHAGAHAEEAFFNTI--LPAFDPALKYNVTWYV 123
Cdd:pfam18778   1 RMSPETFKFQFKNVEYASGRNKTLLCYEVKTR--GNSSSLWRGYLENENSGCHAEICFLRWIldLGLFDPSQKYTITWYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753098    124 SSSPCAACADRILKTLSKTKNLRLLILVSRLFMWEEPEVQAALKKLKEAGCKLRIMKPQDFEYIWQNFVEQEEgesKAFE 203
Cdd:pfam18778  79 SWSPCASCADKLAEFLSAYPNVTLTIFAARLYYWEDPENQEGLRSLASAGVKLRIMDYEDFEYCWQNFVDNEG---RPFT 155
                         170       180
                  ....*....|....*....|
gi 6753098    204 PWEDIQENFLYYEEKLADIL 223
Cdd:pfam18778 156 PWEDLQENSRYYHRKLARIL 175
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
47-224 5.92e-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: 408543 [Multi-domain]  Cd Length: 174  Bit Score: 241.73  E-value: 5.92e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753098     47 LPVNFFKFQFRNVEYSSGRNKTFLCYVVEVQSkGGQAQATQGYLEDEhAGAHAEEAFFNTILP-AFDPALKYNVTWYVSS 125
Cdd:pfam18772   1 LDPKTFKFNFKNVPYASGRNKTYLCYEVETRS-GSDLSLDRGYLRNQ-AGCHAELCFLSWILPwQLDPGQKYQVTWYVSW 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753098    126 SPCAACADRILKTLSKTKNLRLLILVSRL-FMWeEPEVQAALKKLKEAGCKLRIMKPQDFEYIWQNFVEQEEgesKAFEP 204
Cdd:pfam18772  79 SPCPNCARKLAEFLAQHPNVSLTIFAARLyFFW-EPEYQEGLRRLSRAGAQVKIMTYQDFQYCWENFVDNQG---RPFEP 154
                         170       180
                  ....*....|....*....|
gi 6753098    205 WEDIQENFLYYEEKLADILK 224
Cdd:pfam18772 155 WEDLDENYQYLSRKLQEILR 174
APOBEC_N pfam08210
APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. ...
52-221 9.54e-71

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: 400493 [Multi-domain]  Cd Length: 170  Bit Score: 213.37  E-value: 9.54e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753098     52 FKFQFRNVEYSSGRNKTFLCYVVEVQSKGGQAQaTQGYLEDEHA-GAHAEEAFFNTI-LPAFDPALKYNVTWYVSSSPCA 129
Cdd:pfam08210   1 FYFHFKNLPYASGRHKTFLCYEVKRSSGGLVVS-DKGVLRNQVAsSCHAEERFLRWIhDLILDPGSSYEVTWYVSWSPCN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753098    130 ACADRILKTLSKTKNLRLLILVSRLFMWEEPEVQA--ALKKLKEAGCKLRIMKPQDFEYIWQNFVEQEEgesKAFEPWED 207
Cdd:pfam08210  80 ECASELAAFLAKHPNVRLRIFVSRLYYWEEPDYAEreGLRSLAQAGVQLEPMSYKDFKYCWQNFVENEG---EPFKPWDG 156
                         170
                  ....*....|....
gi 6753098    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 ...
87-190 5.04e-40

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: 408522  Cd Length: 104  Bit Score: 132.74  E-value: 5.04e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753098     87 QGYLEDEHaGAHAEEAFFNTIL-PAFDPALKYNVTWYVSSSPCAACADRILKTLSKTKNLRLLILVSRLFMWEEPEvQAA 165
Cdd:pfam18750   2 RGFLSNEH-GSHAEICFLENIDsKLLDPVTCYRVTWYLSWSPCAECAQKIAEFLREHPNVTLRIFAARLYHWDELY-REG 79
                          90       100
                  ....*....|....*....|....*
gi 6753098    166 LKKLKEAGCKLRIMKPQDFEYIWQN 190
Cdd:pfam18750  80 LRSLHQAGVTLRIMTYEDFTYCWDN 104
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
52-223 8.74e-39

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


Pssm-ID: 408553 [Multi-domain]  Cd Length: 179  Bit Score: 132.11  E-value: 8.74e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753098     52 FKFQFRNVEYSSGRNKTFLCYvvEVQSKGGQAQAT---QGYLEDE-HAGAHAEEAFFNTILP-AFDPALKYNVTWYVSSS 126
Cdd:pfam18782   8 FYFNFNNKPILYGRNKTWLCY--EVERKDGGTWVVplhRGFFRNQvKSKYHAELCFLSWFCGnQLPPYQDYRVTWYVSWS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753098    127 PCAACADRILKTLSKTKNLRLLILVSRLFMWEEPEVQAALKKLKEAGCKLRIMKPQDFEYIWQNFVeqeEGESKAFEPWE 206
Cdd:pfam18782  86 PCPDCAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYPEFEYCWENFV---YNQGEPFQPWK 162
                         170
                  ....*....|....*..
gi 6753098    207 DIQENFLYYEEKLADIL 223
Cdd:pfam18782 163 GLEINSRFLHRTLREIL 179
APOBEC_C pfam05240
APOBEC-like C-terminal domain; This domain is found at the C-termini of the Apolipoprotein B ...
143-223 3.48e-34

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


Pssm-ID: 398766  Cd Length: 78  Bit Score: 116.80  E-value: 3.48e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753098    143 KNLRLLILVSRLFMWEEPEVQAALKKLKEAGCKLRIMKPQDFEYIWQNFVEQEEgesKAFEPWEDIQENFLYYEEKLADI 222
Cdd:pfam05240   1 PNVSLTIFAARLYYHWDPEYQQGLRRLVQAGAQVAIMSYKEFEYCWDNFVDNQG---RPFQPWEGLNENSQYLSRRLQEI 77

                  .
gi 6753098    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 6.77e-18

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: 408546  Cd Length: 74  Bit Score: 74.68  E-value: 6.77e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6753098    119 VTWYVSSSPCAACADRILKTLSKTKNLRLLILVSRLFMWEEPEVQAALKKLKEAGCKLRIMKPQDFEYIWQNFV 192
Cdd:pfam18775   1 VTLYLSWSPCGECCEKIQEFLKKHPNVNLDIYFAQLYYTEAEDNRQGLRSLVEKGVTLSVMSGEDYIYCWRTFV 74
APOBEC4_like pfam18774
APOBEC4-like -AID/APOBEC-deaminase; Cnidarian and Algal homologs of the APOBEC4-like AID ...
98-193 6.74e-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  Cd Length: 131  Bit Score: 74.14  E-value: 6.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753098     98 HAEEAFFNTILPAfDPALKYNVTWYVSSSPCAACADRILKTLSKTKNLRLLILVSRLFMWEEPEVQAALKKLKEAGCKLR 177
Cdd:pfam18774  36 HAEVNFLENFRSE-RPSRSCTITWYLSWSPCWECSGRILEFLSRHPNVTLGIYVARLFMHDDDRNRQGLRILQMNGVTIQ 114
                          90
                  ....*....|....*.
gi 6753098    178 IMKPQDFEYIWQNFVE 193
Cdd:pfam18774 115 VMMNKDYCYCWKAFKN 130
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
61-151 1.05e-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: 1.05e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753098   61 YSSGRNKTFLCYVVEvqsKGGQAqaTQGYLEDEHA---GAHAEEAFFNTILPAFDPalKYNVTWYVSS-----SPCAACA 132
Cdd:cd01283  12 YAPYSNFTVGAALLT---KDGRI--FTGVNVENASyglTLCAERTAIGKAVSEGLR--RYLVTWAVSDeggvwSPCGACR 84
                        90
                ....*....|....*....
gi 6753098  133 DRILKTLSKtknlRLLILV 151
Cdd:cd01283  85 QVLAEFLPS----RLYIII 99
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH