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Conserved domains on  [gi|1039749735|ref|XP_017172295|]
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DNA dC-

Protein Classification

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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 ...
 32-209 5.79e-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: 248.28  E-value: 5.79e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735  32 ISQETFKFHFKNLGYAKGRKDTFLCYEVTRKDCdSPVSLHHGVFKNKDNIHAEICFLYWFHDKVLkvlSPREEFKITWYM 111
Cdd:pfam18772   1 MDPKTFKFQFKNVPYASGRNKTYLCYEVETRSG-SDLSPDRGYLRNQAGCHAELCFLSWILPWQL---DPGQKYQVTWYV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735 112 SWSPCFECAEQIVRFLATHHNLSLDIFSSRLYNVQDPETQQNLCRLVQEGAQVAAMDLYEFKKCWKKFVDNGGRRFRPWK 191
Cdd:pfam18772  77 SWSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDNQGRPFEPWE 156

                         170
                  ....*....|....*...
gi 1039749735 192 RLLTNFRYQDSKLQEILR 209
Cdd:pfam18772 157 DLDENYEYLSRKLQEILR 174
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 212-374 8.25e-70

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: 217.23  E-value: 8.25e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735 212 DPLSEEEFYSQFYNqrvKHLcYYHRMKPYLCYQLEQFNGQAPL---KGCLLSEKgKQHAEILFLDKIRSMELS---QVTI 285
Cdd:pfam18782   1 KRMYPRTFYFNFNN---KPI-LYGRNKTYLCYEVERLDNGTWLpqhRGFFRNQA-KYHAELCFLSWFCGNQLPpyqNYQV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735 286 TCYLTWSPCPNCAWQLAAFKRDRPDLILHIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFVNPK-RPF 364
Cdd:pfam18782  76 TWYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQgEPF 155

                         170
                  ....*....|
gi 1039749735 365 WPWKGLEIIS 374
Cdd:pfam18782 156 QPWDGLEENS 165
 
Name Accession Description Interval E-value
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 32-209 5.79e-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: 248.28  E-value: 5.79e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735  32 ISQETFKFHFKNLGYAKGRKDTFLCYEVTRKDCdSPVSLHHGVFKNKDNIHAEICFLYWFHDKVLkvlSPREEFKITWYM 111
Cdd:pfam18772   1 MDPKTFKFQFKNVPYASGRNKTYLCYEVETRSG-SDLSPDRGYLRNQAGCHAELCFLSWILPWQL---DPGQKYQVTWYV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735 112 SWSPCFECAEQIVRFLATHHNLSLDIFSSRLYNVQDPETQQNLCRLVQEGAQVAAMDLYEFKKCWKKFVDNGGRRFRPWK 191
Cdd:pfam18772  77 SWSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDNQGRPFEPWE 156

                         170
                  ....*....|....*...
gi 1039749735 192 RLLTNFRYQDSKLQEILR 209
Cdd:pfam18772 157 DLDENYEYLSRKLQEILR 174
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 212-374 8.25e-70

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: 217.23  E-value: 8.25e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735 212 DPLSEEEFYSQFYNqrvKHLcYYHRMKPYLCYQLEQFNGQAPL---KGCLLSEKgKQHAEILFLDKIRSMELS---QVTI 285
Cdd:pfam18782   1 KRMYPRTFYFNFNN---KPI-LYGRNKTYLCYEVERLDNGTWLpqhRGFFRNQA-KYHAELCFLSWFCGNQLPpyqNYQV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735 286 TCYLTWSPCPNCAWQLAAFKRDRPDLILHIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFVNPK-RPF 364
Cdd:pfam18782  76 TWYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQgEPF 155

                         170
                  ....*....|
gi 1039749735 365 WPWKGLEIIS 374
Cdd:pfam18782 156 QPWDGLEENS 165
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 46-152 6.68e-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: 67.37  E-value: 6.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735  46 YAKGRKDTFLCYEVTRKdcdspVSLHHGVFKNK----DNIHAEICFLYWFHDKVLKvlspreEFKITWYMS-----WSPC 116
Cdd:cd01283    12 YAPYSNFTVGAALLTKD-----GRIFTGVNVENasygLTLCAERTAIGKAVSEGLR------RYLVTWAVSdeggvWSPC 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1039749735 117 FECAEQIVRFLathhnlsldifSSRLYNVQDPETQQ 152
Cdd:cd01283    81 GACRQVLAEFL-----------PSRLYIIIDNPKGE 105
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 232-330 3.34e-13

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: 3.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735 232 CYYHRmKPYLCYQLEqfNGQAPLKGCLL---SEKGKQHAEILFLDKIRSMELSQVTITCYLT-----WSPCPNCAWQLAA 303
Cdd:cd01283    13 APYSN-FTVGAALLT--KDGRIFTGVNVenaSYGLTLCAERTAIGKAVSEGLRRYLVTWAVSdeggvWSPCGACRQVLAE 89

                          90       100
                  ....*....|....*....|....*..
gi 1039749735 304 FKRdrpdlilhiytSRLYFHWKRPFQK 330
Cdd:cd01283    90 FLP-----------SRLYIIIDNPKGE 105
 
Name Accession Description Interval E-value
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 32-209 5.79e-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: 248.28  E-value: 5.79e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735  32 ISQETFKFHFKNLGYAKGRKDTFLCYEVTRKDCdSPVSLHHGVFKNKDNIHAEICFLYWFHDKVLkvlSPREEFKITWYM 111
Cdd:pfam18772   1 MDPKTFKFQFKNVPYASGRNKTYLCYEVETRSG-SDLSPDRGYLRNQAGCHAELCFLSWILPWQL---DPGQKYQVTWYV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735 112 SWSPCFECAEQIVRFLATHHNLSLDIFSSRLYNVQDPETQQNLCRLVQEGAQVAAMDLYEFKKCWKKFVDNGGRRFRPWK 191
Cdd:pfam18772  77 SWSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDNQGRPFEPWE 156

                         170
                  ....*....|....*...
gi 1039749735 192 RLLTNFRYQDSKLQEILR 209
Cdd:pfam18772 157 DLDENYEYLSRKLQEILR 174
NAD1 pfam18778
Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned ...
 31-208 5.84e-77

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: 235.64  E-value: 5.84e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735  31 LISQETFKFHFKNLGYAKGRKDTFLCYEVTRKdcdSPVSLHHGVFKNKDN-IHAEICFLYWFHDkvLKVLSPREEFKITW 109
Cdd:pfam18778   2 RMSPETFKFQFKNVEYASGRNKTLLCYEVKRG---NSSSLWRGHLRNENSgCHAEICFLRWFSS--WRLFDPSQCYTITW 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735 110 YMSWSPCFECAEQIVRFLATHHNLSLDIFSSRLYNVQDPETQQNLCRLVQEGAQVAAMDLYEFKKCWKKFVDNGGRRFRP 189
Cdd:pfam18778  77 YLSWSPCPSCAAKLAEFLKAHPNVTLTIFAARLYYFEDPWNQEGLRSLASAGVTLSIMDYSDFEYCWENFVDNEGRPFVP 156

                         170
                  ....*....|....*....
gi 1039749735 190 WKRLLTNFRYQDSKLQEIL 208
Cdd:pfam18778 157 WEDLEENSRYYHRKLQRIL 175
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 31-208 3.16e-73

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: 226.09  E-value: 3.16e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735  31 LISQETFKFHFKNLGYAKGRKDTFLCYEVTRKDCDSPVSLHHGVFKNKDNIHAEICFLYWFhdkVLKVLSPREEFKITWY 110
Cdd:pfam18782   2 RMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGTWLPQHRGFFRNQAKYHAELCFLSWF---CGNQLPPYQNYQVTWY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735 111 MSWSPCFECAEQIVRFLATHHNLSLDIFSSRLYNVQDPETQQNLCRLVQEGAQVAAMDLYEFKKCWKKFVDNGGRRFRPW 190
Cdd:pfam18782  79 VSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQGEPFQPW 158

                         170
                  ....*....|....*...
gi 1039749735 191 KRLLTNFRYQDSKLQEIL 208
Cdd:pfam18782 159 DGLEENSRFLHRRLREIL 176
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 212-374 8.25e-70

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: 217.23  E-value: 8.25e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735 212 DPLSEEEFYSQFYNqrvKHLcYYHRMKPYLCYQLEQFNGQAPL---KGCLLSEKgKQHAEILFLDKIRSMELS---QVTI 285
Cdd:pfam18782   1 KRMYPRTFYFNFNN---KPI-LYGRNKTYLCYEVERLDNGTWLpqhRGFFRNQA-KYHAELCFLSWFCGNQLPpyqNYQV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735 286 TCYLTWSPCPNCAWQLAAFKRDRPDLILHIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFVNPK-RPF 364
Cdd:pfam18782  76 TWYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQgEPF 155

                         170
                  ....*....|
gi 1039749735 365 WPWKGLEIIS 374
Cdd:pfam18782 156 QPWDGLEENS 165
NAD1 pfam18778
Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned ...
 212-374 8.30e-64

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: 201.74  E-value: 8.30e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735 212 DPLSEEEFYSQFYNQRVKhlcyYHRMKPYLCYQLEQFNGQAPLKGCLLSEKGKQHAEILFLDKIRSMEL----SQVTITC 287
Cdd:pfam18778   1 ERMSPETFKFQFKNVEYA----SGRNKTLLCYEVKRGNSSSLWRGHLRNENSGCHAEICFLRWFSSWRLfdpsQCYTITW 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735 288 YLTWSPCPNCAWQLAAFKRDRPDLILHIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFVNPK-RPFWP 366
Cdd:pfam18778  77 YLSWSPCPSCAAKLAEFLKAHPNVTLTIFAARLYYFEDPWNQEGLRSLASAGVTLSIMDYSDFEYCWENFVDNEgRPFVP 156


                  ....*...
gi 1039749735 367 WKGLEIIS 374
Cdd:pfam18778 157 WEDLEENS 164
APOBEC_N pfam08210
APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. ...
 37-206 1.72e-59

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: 190.65  E-value: 1.72e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735  37 FKFHFKNLGYAKGRKDTFLCYEVTRKDCDSPVsLHHGVFKNK--DNIHAEICFLYWFHDKVLkvlSPREEFKITWYMSWS 114
Cdd:pfam08210   1 FFFHFKNLPYASGRHETYLCYEVKRDSGGLVV-EDKGYLRNQaaSSLHAEERFLRWIHDLAL---DPGSNYEVTWYVSWS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735 115 PCFECAEQIVRFLATHHNLSLDIFSSRLYNVQDPE--TQQNLCRLVQEGAQVAAMDLYEFKKCWKKFVDNGGRRFRPWKR 192
Cdd:pfam08210  77 PCNECASELAAFLSKHPNVRLRIFVSRLYYWEEPDywNREGLRSLAQAGVQLRPMSYKDFEYCWNNFVDHDGEPFKPWDG 156

                         170
                  ....*....|....
gi 1039749735 193 LLTNFRYQDSKLQE 206
Cdd:pfam08210 157 LHENSVYLARKLQE 170
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 214-371 3.93e-54

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: 176.64  E-value: 3.93e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735 214 LSEEEFYSQFYNQRVKhlcyYHRMKPYLCYQLEQFNGQA--PLKGCLLSEKGKqHAEILFLDKIRSMELSQ---VTITCY 288
Cdd:pfam18772   1 MDPKTFKFQFKNVPYA----SGRNKTYLCYEVETRSGSDlsPDRGYLRNQAGC-HAELCFLSWILPWQLDPgqkYQVTWY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735 289 LTWSPCPNCAWQLAAFKRDRPDLILHIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFV-NPKRPFWPW 367
Cdd:pfam18772  76 VSWSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVdNQGRPFEPW 155


                  ....
gi 1039749735 368 KGLE 371
Cdd:pfam18772 156 EDLD 159
SNAD4 pfam18750
Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases ...
 57-178 7.61e-46

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: 153.19  E-value: 7.61e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735  57 YEVTRKDcdSPVSLHHGVFKNKDNIHAEICFLYWFHDKVLkvlSPREEFKITWYMSWSPCFECAEQIVRFLATHHNLSLD 136
Cdd:pfam18750   1 YEIKWGN--GSKIWQRGYLSNEHEQHAEICFLENIRSREL---DPSQRYRVTWYLSWSPCPECAQKIAEFLAEHPNVTLT 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1039749735 137 IFSSRLYNvQDPETQQNLCRLVQEGAQVAAMDLYEFKKCWKK 178
Cdd:pfam18750  76 IFAARLYH-WDEDNRQGLRSLAQAGVTLQIMTLEDFEYCWKN 116
APOBEC3 pfam18771
APOBEC3; APOBEC3 deaminases act as restriction factors in the innate response to retroviruses ...
 234-363 3.66e-44

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: 149.56  E-value: 3.66e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735 234 YHRMKPYLCYQLEQFNGQAPLKGCLlSEKGKQHAEILFLDKIRSMELSQV---TITCYLTWSPCPNCAWQLAAFKRDRPD 310
Cdd:pfam18771   1 YYDRKAYLCYQLKGRNGSALDRGYF-SNKKKRHAEIRFIDKIRSLDLDNIqcyRITCYITWSPCPNCAAELVDFISLNPH 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039749735 311 LILHIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFVNPKRP 363
Cdd:pfam18771  80 LKLRIFASRLYYHWERSYKEGLQKLQRAGVSVAVMTLPEFQDCWEDFVDHQEE 132
SNAD4 pfam18750
Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases ...
 243-356 1.48e-41

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: 142.01  E-value: 1.48e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735 243 YQLEQFNGQAPL-KGCLLSEKGkQHAEILFLDKIRSMELSQVT---ITCYLTWSPCPNCAWQLAAFKRDRPDLILHIYTS 318
Cdd:pfam18750   1 YEIKWGNGSKIWqRGYLSNEHE-QHAEICFLENIRSRELDPSQryrVTWYLSWSPCPECAQKIAEFLAEHPNVTLTIFAA 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1039749735 319 RLYfHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTN 356
Cdd:pfam18750  80 RLY-HWDEDNRQGLRSLAQAGVTLQIMTLEDFEYCWKN 116
APOBEC_C pfam05240
APOBEC-like C-terminal domain; This domain is found at the C-termini of the Apolipoprotein B ...
 131-208 1.89e-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: 116.81  E-value: 1.89e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039749735 131 HNLSLDIFSSRLYNVQDPETQQNLCRLVQEGAQVAAMDLYEFKKCWKKFVDNGGRRFRPWKRLLTNFRYQDSKLQEIL 208
Cdd:pfam05240   1 PNVSLTIFAARLYYHWDPEYQQGLRRLVQAGAQVAIMSYKEFEYCWDNFVDNQGRPFQPWEGLEENSQLLSRRLQEIL 78
APOBEC_N pfam08210
APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. ...
 219-372 1.85e-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: 117.47  E-value: 1.85e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735 219 FYSQFYNQRvkhlCYYHRMKPYLCYQLEQFNGQAPL--KGCLLSEKGKQ-HAEILFLDKIRSMELSQV---TITCYLTWS 292
Cdd:pfam08210   1 FFFHFKNLP----YASGRHETYLCYEVKRDSGGLVVedKGYLRNQAASSlHAEERFLRWIHDLALDPGsnyEVTWYVSWS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735 293 PCPNCAWQLAAFKRDRPDLILHIYTSRLYFHWKR--PFQKGLCSLWQSGILVDVMDLPQFTDCWTNFVNPK-RPFWPWKG 369
Cdd:pfam08210  77 PCNECASELAAFLSKHPNVRLRIFVSRLYYWEEPdyWNREGLRSLAQAGVQLRPMSYKDFEYCWNNFVDHDgEPFKPWDG 156


                  ...
gi 1039749735 370 LEI 372
Cdd:pfam08210 157 LHE 159
APOBEC3 pfam18771
APOBEC3; APOBEC3 deaminases act as restriction factors in the innate response to retroviruses ...
 50-188 1.18e-30

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: 114.12  E-value: 1.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735  50 RKDTFLCYEVTRKDCDSPVSlhhGVFKNKDNIHAEICFLywfhDKVLKV-LSPREEFKITWYMSWSPCFECAEQIVRFLA 128
Cdd:pfam18771   3 DRKAYLCYQLKGRNGSALDR---GYFSNKKKRHAEIRFI----DKIRSLdLDNIQCYRITCYITWSPCPNCAAELVDFIS 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735 129 THHNLSLDIFSSRLYNVQDPETQQNLCRLVQEGAQVAAMDLYEFKKCWKKFVDNGGRRFR 188
Cdd:pfam18771  76 LNPHLKLRIFASRLYYHWERSYKEGLQKLQRAGVSVAVMTLPEFQDCWEDFVDHQEEPFR 135
APOBEC_C pfam05240
APOBEC-like C-terminal domain; This domain is found at the C-termini of the Apolipoprotein B ...
 309-374 2.70e-25

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: 97.94  E-value: 2.70e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039749735 309 PDLILHIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFVNPK-RPFWPWKGLEIIS 374
Cdd:pfam05240   1 PNVSLTIFAARLYYHWDPEYQQGLRRLVQAGAQVAIMSYKEFEYCWDNFVDNQgRPFQPWEGLEENS 67
APOBEC4 pfam18775
APOBEC4; A member of the AID/APOBEC family of cytosine deaminases. The biological function of ...
 107-180 2.20e-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: 436728  Cd Length: 74  Bit Score: 78.92  E-value: 2.20e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039749735 107 ITWYMSWSPCFECAEQIVRFLATHHNLSLDIFSSRLYNVQDPETQQNLCRLVQEGAQVAAMDLYEFKKCWKKFV 180
Cdd:pfam18775   1 VTLYLSWSPCNECSEKIQEFLKKHPKVNLDIYFAQLYHTEEEDNRQGLRSLVEKGVTLSVMSGEDWIYCLRTFV 74
APOBEC4_like pfam18774
APOBEC4-like -AID/APOBEC-deaminase; Cnidarian and Algal homologs of the APOBEC4-like AID ...
 235-359 7.48e-18

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: 79.15  E-value: 7.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735 235 HRMKPYLCYQLEQFNGQAPLKGCllSEKGKQHAEILFLDKIRS-MELSQVTITCYLTWSPCPNCAWQLAAFKRDRPDLIL 313
Cdd:pfam18774   7 HKKEICLLYEIQWGRGTIWRNWT--ENNCTEHAEVNFLENFRSeRPSRSCTITWYLSWSPCWECSGRILEFLSRHPNVTL 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1039749735 314 HIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFVN 359
Cdd:pfam18774  85 GIYVARLFMHDDDRNRQGLRILQMNGVTIQVMMNKDYCYCWKAFKN 130
APOBEC4_like pfam18774
APOBEC4-like -AID/APOBEC-deaminase; Cnidarian and Algal homologs of the APOBEC4-like AID ...
 82-181 4.03e-15

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: 71.44  E-value: 4.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735  82 HAEICFLYWFHDKvlkvlSPREEFKITWYMSWSPCFECAEQIVRFLATHHNLSLDIFSSRLYNVQDPETQQNLCRLVQEG 161
Cdd:pfam18774  36 HAEVNFLENFRSE-----RPSRSCTITWYLSWSPCWECSGRILEFLSRHPNVTLGIYVARLFMHDDDRNRQGLRILQMNG 110

                          90       100
                  ....*....|....*....|
gi 1039749735 162 AQVAAMDLYEFKKCWKKFVD 181
Cdd:pfam18774 111 VTIQVMMNKDYCYCWKAFKN 130
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 46-152 6.68e-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: 67.37  E-value: 6.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735  46 YAKGRKDTFLCYEVTRKdcdspVSLHHGVFKNK----DNIHAEICFLYWFHDKVLKvlspreEFKITWYMS-----WSPC 116
Cdd:cd01283    12 YAPYSNFTVGAALLTKD-----GRIFTGVNVENasygLTLCAERTAIGKAVSEGLR------RYLVTWAVSdeggvWSPC 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1039749735 117 FECAEQIVRFLathhnlsldifSSRLYNVQDPETQQ 152
Cdd:cd01283    81 GACRQVLAEFL-----------PSRLYIIIDNPKGE 105
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 232-330 3.34e-13

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: 3.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735 232 CYYHRmKPYLCYQLEqfNGQAPLKGCLL---SEKGKQHAEILFLDKIRSMELSQVTITCYLT-----WSPCPNCAWQLAA 303
Cdd:cd01283    13 APYSN-FTVGAALLT--KDGRIFTGVNVenaSYGLTLCAERTAIGKAVSEGLRRYLVTWAVSdeggvWSPCGACRQVLAE 89

                          90       100
                  ....*....|....*....|....*..
gi 1039749735 304 FKRdrpdlilhiytSRLYFHWKRPFQK 330
Cdd:cd01283    90 FLP-----------SRLYIIIDNPKGE 105
APOBEC1 pfam18769
APOBEC1; APOBEC1 deaminates cytosine both in RNA and ssDNA and has roles in both mRNA editing ...
 77-167 7.59e-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: 64.06  E-value: 7.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749735  77 NKDNIHAEICFLYWFHDKvlKVLSPREEFKITWYMSWSPCFECAEQIVRFLATHHNLSLDIFSSRLYNVQDPETQQNLCR 156
Cdd:pfam18769  13 NNTTQHAEVNFLEKFFSE--RHFDPSVSCSITWFLSWSPCGECSKAIGEFLSQHPNVTLVIYAARLFKHLDIRNRQGLRD 90

                          90
                  ....*....|.
gi 1039749735 157 LVQEGAQVAAM 167
Cdd:pfam18769  91 LAMSGVTIQIM 101
APOBEC4 pfam18775
APOBEC4; A member of the AID/APOBEC family of cytosine deaminases. The biological function of ...
 285-358 3.02e-12

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: 61.58  E-value: 3.02e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039749735 285 ITCYLTWSPCPNCAWQLAAFKRDRPDLILHIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFV 358
Cdd:pfam18775   1 VTLYLSWSPCNECSEKIQEFLKKHPKVNLDIYFAQLYHTEEEDNRQGLRSLVEKGVTLSVMSGEDWIYCLRTFV 74
 
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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