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Conserved domains on  [gi|119580685|gb|EAW60281|]
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apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3B, isoform CRA_c [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 10-189 1.92e-104

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: 305.06  E-value: 1.92e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685   10 ERMYRDTFYDNFENEPILYGRSYTWLCYEVKIKRGRSNLLWDTGVFRGQvyfePQYHAEMCFLSWFCGNQLPAYKCFQIT 89
Cdd:pfam18782   1 KRMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGTWLPQHRGFFRNQ----AKYHAELCFLSWFCGNQLPPYQNYQVT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685   90 WFVSWTPCPDCVAKLAEFLSEHPNVTLTISAARLYYYWERDYRRALCRLSQAGARVKIMDYEEFAYCWENFVYNEGQQFM 169
Cdd:pfam18782  77 WYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQGEPFQ 156

                         170       180
                  ....*....|....*....|
gi 119580685  170 PWYKFDENYAFLHRTLKEIL 189
Cdd:pfam18782 157 PWDGLEENSRFLHRRLREIL 176
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 191-377 3.54e-92

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: 273.86  E-value: 3.54e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685  191 YLMDPDTFTFNFNNDPLVLRRRQTYLCYEVERLDNGTWVLmdQHMGFLCNEAKnllcgfygRHAELRFLDLVPSLQLDPA 270
Cdd:pfam18782   1 KRMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGTWLP--QHRGFFRNQAK--------YHAELCFLSWFCGNQLPPY 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685  271 QIYRVTWFISWSPCFSwgCAGEVRAFLQENTHVRLRIFAARIY-DYDPLYKEALQMLRDAGAQVSIMTYDEFEYCWDTFV 349
Cdd:pfam18782  71 QNYQVTWYVSWSPCPE--CAGEVAEFLAEHPNVTLTIFAARLYyFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFV 148

                         170       180
                  ....*....|....*....|....*...
gi 119580685  350 YRQGCPFQPWDGLEEHSQALSGRLRAIL 377
Cdd:pfam18782 149 YNQGEPFQPWDGLEENSRFLHRRLREIL 176
 
Name Accession Description Interval E-value
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 10-189 1.92e-104

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: 305.06  E-value: 1.92e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685   10 ERMYRDTFYDNFENEPILYGRSYTWLCYEVKIKRGRSNLLWDTGVFRGQvyfePQYHAEMCFLSWFCGNQLPAYKCFQIT 89
Cdd:pfam18782   1 KRMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGTWLPQHRGFFRNQ----AKYHAELCFLSWFCGNQLPPYQNYQVT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685   90 WFVSWTPCPDCVAKLAEFLSEHPNVTLTISAARLYYYWERDYRRALCRLSQAGARVKIMDYEEFAYCWENFVYNEGQQFM 169
Cdd:pfam18782  77 WYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQGEPFQ 156

                         170       180
                  ....*....|....*....|
gi 119580685  170 PWYKFDENYAFLHRTLKEIL 189
Cdd:pfam18782 157 PWDGLEENSRFLHRRLREIL 176
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 191-377 3.54e-92

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: 273.86  E-value: 3.54e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685  191 YLMDPDTFTFNFNNDPLVLRRRQTYLCYEVERLDNGTWVLmdQHMGFLCNEAKnllcgfygRHAELRFLDLVPSLQLDPA 270
Cdd:pfam18782   1 KRMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGTWLP--QHRGFFRNQAK--------YHAELCFLSWFCGNQLPPY 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685  271 QIYRVTWFISWSPCFSwgCAGEVRAFLQENTHVRLRIFAARIY-DYDPLYKEALQMLRDAGAQVSIMTYDEFEYCWDTFV 349
Cdd:pfam18782  71 QNYQVTWYVSWSPCPE--CAGEVAEFLAEHPNVTLTIFAARLYyFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFV 148

                         170       180
                  ....*....|....*....|....*...
gi 119580685  350 YRQGCPFQPWDGLEEHSQALSGRLRAIL 377
Cdd:pfam18782 149 YNQGEPFQPWDGLEENSRFLHRRLREIL 176
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 8-158 8.79e-15

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: 70.06  E-value: 8.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685   8 PMERMYRDTFYdnfenepILYGRSYTWLCYEVKikrgrsnllWDTGVFRGQVYFEPQY----HAEMCFLSWFCGNQlpaY 83
Cdd:cd01283    1 IEAALAAAEFA-------YAPYSNFTVGAALLT---------KDGRIFTGVNVENASYgltlCAERTAIGKAVSEG---L 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685  84 KCFQITWFVS-----WTPCPDCVAKLAEFLSehpnvtltisaARLYYYWERDYRralcrlsqagarvkimdyEEFAYCWE 158
Cdd:cd01283   62 RRYLVTWAVSdeggvWSPCGACRQVLAEFLP-----------SRLYIIIDNPKG------------------EEFAYTLS 112
 
Name Accession Description Interval E-value
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 10-189 1.92e-104

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: 305.06  E-value: 1.92e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685   10 ERMYRDTFYDNFENEPILYGRSYTWLCYEVKIKRGRSNLLWDTGVFRGQvyfePQYHAEMCFLSWFCGNQLPAYKCFQIT 89
Cdd:pfam18782   1 KRMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGTWLPQHRGFFRNQ----AKYHAELCFLSWFCGNQLPPYQNYQVT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685   90 WFVSWTPCPDCVAKLAEFLSEHPNVTLTISAARLYYYWERDYRRALCRLSQAGARVKIMDYEEFAYCWENFVYNEGQQFM 169
Cdd:pfam18782  77 WYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQGEPFQ 156

                         170       180
                  ....*....|....*....|
gi 119580685  170 PWYKFDENYAFLHRTLKEIL 189
Cdd:pfam18782 157 PWDGLEENSRFLHRRLREIL 176
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 12-190 4.11e-95

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: 281.41  E-value: 4.11e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685   12 MYRDTFYDNFENEPILYGRSYTWLCYEVKiKRGRSNLLWDTGVFRGQvyfePQYHAEMCFLSWFCGNQLPAYKCFQITWF 91
Cdd:pfam18772   1 MDPKTFKFQFKNVPYASGRNKTYLCYEVE-TRSGSDLSPDRGYLRNQ----AGCHAELCFLSWILPWQLDPGQKYQVTWY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685   92 VSWTPCPDCVAKLAEFLSEHPNVTLTISAARLYYYWERDYRRALCRLSQAGARVKIMDYEEFAYCWENFVYNEGQQFMPW 171
Cdd:pfam18772  76 VSWSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDNQGRPFEPW 155

                         170
                  ....*....|....*....
gi 119580685  172 YKFDENYAFLHRTLKEILR 190
Cdd:pfam18772 156 EDLDENYEYLSRKLQEILR 174
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 191-377 3.54e-92

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: 273.86  E-value: 3.54e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685  191 YLMDPDTFTFNFNNDPLVLRRRQTYLCYEVERLDNGTWVLmdQHMGFLCNEAKnllcgfygRHAELRFLDLVPSLQLDPA 270
Cdd:pfam18782   1 KRMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGTWLP--QHRGFFRNQAK--------YHAELCFLSWFCGNQLPPY 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685  271 QIYRVTWFISWSPCFSwgCAGEVRAFLQENTHVRLRIFAARIY-DYDPLYKEALQMLRDAGAQVSIMTYDEFEYCWDTFV 349
Cdd:pfam18782  71 QNYQVTWYVSWSPCPE--CAGEVAEFLAEHPNVTLTIFAARLYyFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFV 148

                         170       180
                  ....*....|....*....|....*...
gi 119580685  350 YRQGCPFQPWDGLEEHSQALSGRLRAIL 377
Cdd:pfam18782 149 YNQGEPFQPWDGLEENSRFLHRRLREIL 176
NAD1 pfam18778
Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned ...
 10-189 2.08e-85

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: 256.82  E-value: 2.08e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685   10 ERMYRDTFYDNFENEPILYGRSYTWLCYEVKikRGRSNLLWdTGVFRGQvyfEPQYHAEMCFLSWFCGNQL-PAYKCFQI 88
Cdd:pfam18778   1 ERMSPETFKFQFKNVEYASGRNKTLLCYEVK--RGNSSSLW-RGHLRNE---NSGCHAEICFLRWFSSWRLfDPSQCYTI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685   89 TWFVSWTPCPDCVAKLAEFLSEHPNVTLTISAARLYYYWERDYRRALCRLSQAGARVKIMDYEEFAYCWENFVYNEGQQF 168
Cdd:pfam18778  75 TWYLSWSPCPSCAAKLAEFLKAHPNVTLTIFAARLYYFEDPWNQEGLRSLASAGVTLSIMDYSDFEYCWENFVDNEGRPF 154

                         170       180
                  ....*....|....*....|.
gi 119580685  169 MPWYKFDENYAFLHRTLKEIL 189
Cdd:pfam18778 155 VPWEDLEENSRYYHRKLQRIL 175
APOBEC2 pfam18772
APOBEC2; APOBEC2 is a highly conserved (slow-evolving) family of AID/APOBECs found in most ...
 193-378 4.55e-75

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: 230.18  E-value: 4.55e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685  193 MDPDTFTFNFNNDPLVLRRRQTYLCYEVERLDNGTwVLMDQhmGFLCNEAknllcgfyGRHAELRFLDLVPSLQLDPAQI 272
Cdd:pfam18772   1 MDPKTFKFQFKNVPYASGRNKTYLCYEVETRSGSD-LSPDR--GYLRNQA--------GCHAELCFLSWILPWQLDPGQK 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685  273 YRVTWFISWSPCFSwgCAGEVRAFLQENTHVRLRIFAARIYDY-DPLYKEALQMLRDAGAQVSIMTYDEFEYCWDTFVYR 351
Cdd:pfam18772  70 YQVTWYVSWSPCPD--CARKLAEFLARHPNLSLTIFAARLYFFwEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDN 147

                         170       180
                  ....*....|....*....|....*..
gi 119580685  352 QGCPFQPWDGLEEHSQALSGRLRAILQ 378
Cdd:pfam18772 148 QGRPFEPWEDLDENYEYLSRKLQEILR 174
NAD1 pfam18778
Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned ...
 191-377 2.76e-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: 220.61  E-value: 2.76e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685  191 YLMDPDTFTFNFNNDPLVLRRRQTYLCYEVERL-DNGTWVlmdqhmGFLCNEAKnllcgfyGRHAELRFLDLVPSLQL-D 268
Cdd:pfam18778   1 ERMSPETFKFQFKNVEYASGRNKTLLCYEVKRGnSSSLWR------GHLRNENS-------GCHAEICFLRWFSSWRLfD 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685  269 PAQIYRVTWFISWSPCFSwgCAGEVRAFLQENTHVRLRIFAARIYDY-DPLYKEALQMLRDAGAQVSIMTYDEFEYCWDT 347
Cdd:pfam18778  68 PSQCYTITWYLSWSPCPS--CAAKLAEFLKAHPNVTLTIFAARLYYFeDPWNQEGLRSLASAGVTLSIMDYSDFEYCWEN 145

                         170       180       190
                  ....*....|....*....|....*....|
gi 119580685  348 FVYRQGCPFQPWDGLEEHSQALSGRLRAIL 377
Cdd:pfam18778 146 FVDNEGRPFVPWEDLEENSRYYHRKLQRIL 175
APOBEC_N pfam08210
APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. ...
 198-374 1.14e-60

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: 193.35  E-value: 1.14e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685  198 FTFNFNNDPLVLRRRQTYLCYEVERLDNGTWVlmdQHMGFLCNEAKNllcgfyGRHAELRFLDLVPSLQLDPAQIYRVTW 277
Cdd:pfam08210   1 FFFHFKNLPYASGRHETYLCYEVKRDSGGLVV---EDKGYLRNQAAS------SLHAEERFLRWIHDLALDPGSNYEVTW 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685  278 FISWSPCFSwgCAGEVRAFLQENTHVRLRIFAARIY-DYDPLY--KEALQMLRDAGAQVSIMTYDEFEYCWDTFVYRQGC 354
Cdd:pfam08210  72 YVSWSPCNE--CASELAAFLSKHPNVRLRIFVSRLYyWEEPDYwnREGLRSLAQAGVQLRPMSYKDFEYCWNNFVDHDGE 149

                         170       180
                  ....*....|....*....|
gi 119580685  355 PFQPWDGLEEHSQALSGRLR 374
Cdd:pfam08210 150 PFKPWDGLHENSVYLARKLQ 169
SNAD4 pfam18750
Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases ...
 39-159 4.52e-56

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: 179.38  E-value: 4.52e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685   39 VKIKRGRSNLLWDTGVFRGqvyfEPQYHAEMCFLSWFCGNQLPAYKCFQITWFVSWTPCPDCVAKLAEFLSEHPNVTLTI 118
Cdd:pfam18750   1 YEIKWGNGSKIWQRGYLSN----EHEQHAEICFLENIRSRELDPSQRYRVTWYLSWSPCPECAQKIAEFLAEHPNVTLTI 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 119580685  119 SAARLyYYWERDYRRALCRLSQAGARVKIMDYEEFAYCWEN 159
Cdd:pfam18750  77 FAARL-YHWDEDNRQGLRSLAQAGVTLQIMTLEDFEYCWKN 116
APOBEC_N pfam08210
APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. ...
 17-187 4.21e-55

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: 179.10  E-value: 4.21e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685   17 FYDNFENEPILYGRSYTWLCYEVKIKRGrSNLLWDTGVFRGQVyfEPQYHAEMCFLSWFCGNQLPAYKCFQITWFVSWTP 96
Cdd:pfam08210   1 FFFHFKNLPYASGRHETYLCYEVKRDSG-GLVVEDKGYLRNQA--ASSLHAEERFLRWIHDLALDPGSNYEVTWYVSWSP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685   97 CPDCVAKLAEFLSEHPNVTLTISAARLYYYWERDY--RRALCRLSQAGARVKIMDYEEFAYCWENFVYNEGQQFMPWYKF 174
Cdd:pfam08210  78 CNECASELAAFLSKHPNVRLRIFVSRLYYWEEPDYwnREGLRSLAQAGVQLRPMSYKDFEYCWNNFVDHDGEPFKPWDGL 157

                         170
                  ....*....|...
gi 119580685  175 DENYAFLHRTLKE 187
Cdd:pfam08210 158 HENSVYLARKLQE 170
SNAD4 pfam18750
Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases ...
 243-347 1.58e-44

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: 149.72  E-value: 1.58e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685  243 KNLLCGFYGRHAELRFLDLVPSLQLDPAQIYRVTWFISWSPCFSwgCAGEVRAFLQENTHVRLRIFAARIYDYDPLYKEA 322
Cdd:pfam18750  14 RGYLSNEHEQHAEICFLENIRSRELDPSQRYRVTWYLSWSPCPE--CAQKIAEFLAEHPNVTLTIFAARLYHWDEDNRQG 91

                          90       100
                  ....*....|....*....|....*
gi 119580685  323 LQMLRDAGAQVSIMTYDEFEYCWDT 347
Cdd:pfam18750  92 LRSLAQAGVTLQIMTLEDFEYCWKN 116
APOBEC_C pfam05240
APOBEC-like C-terminal domain; This domain is found at the C-termini of the Apolipoprotein B ...
 112-189 9.91e-40

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: 135.69  E-value: 9.91e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119580685  112 PNVTLTISAARLYYYWERDYRRALCRLSQAGARVKIMDYEEFAYCWENFVYNEGQQFMPWYKFDENYAFLHRTLKEIL 189
Cdd:pfam05240   1 PNVSLTIFAARLYYHWDPEYQQGLRRLVQAGAQVAIMSYKEFEYCWDNFVDNQGRPFQPWEGLEENSQLLSRRLQEIL 78
APOBEC3 pfam18771
APOBEC3; APOBEC3 deaminases act as restriction factors in the innate response to retroviruses ...
 211-357 5.86e-38

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: 133.38  E-value: 5.86e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685  211 RRQTYLCYEVERLDNGTWVlmdqhMGFLCNEAKnllcgfygRHAELRFLDLVPSLQLDPAQIYRVTWFISWSPCFSwgCA 290
Cdd:pfam18771   3 DRKAYLCYQLKGRNGSALD-----RGYFSNKKK--------RHAEIRFIDKIRSLDLDNIQCYRITCYITWSPCPN--CA 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119580685  291 GEVRAFLQENTHVRLRIFAARIYDYD-PLYKEALQMLRDAGAQVSIMTYDEFEYCWDTFVYRQGCPFQ 357
Cdd:pfam18771  68 AELVDFISLNPHLKLRIFASRLYYHWeRSYKEGLQKLQRAGVSVAVMTLPEFQDCWEDFVDHQEEPFR 135
APOBEC_C pfam05240
APOBEC-like C-terminal domain; This domain is found at the C-termini of the Apolipoprotein B ...
 302-377 1.32e-36

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: 127.60  E-value: 1.32e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119580685  302 HVRLRIFAARIYD-YDPLYKEALQMLRDAGAQVSIMTYDEFEYCWDTFVYRQGCPFQPWDGLEEHSQALSGRLRAIL 377
Cdd:pfam05240   2 NVSLTIFAARLYYhWDPEYQQGLRRLVQAGAQVAIMSYKEFEYCWDNFVDNQGRPFQPWEGLEENSQLLSRRLQEIL 78
APOBEC3 pfam18771
APOBEC3; APOBEC3 deaminases act as restriction factors in the innate response to retroviruses ...
 33-168 1.06e-33

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: 121.83  E-value: 1.06e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685   33 TWLCYEVKikrGRSNLLWDTGVFRGqvyfEPQYHAEMCFLSWFCGNQLPAYKCFQITWFVSWTPCPDCVAKLAEFLSEHP 112
Cdd:pfam18771   6 AYLCYQLK---GRNGSALDRGYFSN----KKKRHAEIRFIDKIRSLDLDNIQCYRITCYITWSPCPNCAAELVDFISLNP 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 119580685  113 NVTLTISAARLYYYWERDYRRALCRLSQAGARVKIMDYEEFAYCWENFVYNEGQQF 168
Cdd:pfam18771  79 HLKLRIFASRLYYHWERSYKEGLQKLQRAGVSVAVMTLPEFQDCWEDFVDHQEEPF 134
APOBEC4_like pfam18774
APOBEC4-like -AID/APOBEC-deaminase; Cnidarian and Algal homologs of the APOBEC4-like AID ...
 33-161 6.01e-21

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: 87.62  E-value: 6.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685   33 TWLCYEVKIKRGRsnllwdtgVFRGQVYFEPQYHAEMCFLSWFCGnQLPAYKCfQITWFVSWTPCPDCVAKLAEFLSEHP 112
Cdd:pfam18774  11 ICLLYEIQWGRGT--------IWRNWTENNCTEHAEVNFLENFRS-ERPSRSC-TITWYLSWSPCWECSGRILEFLSRHP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 119580685  113 NVTLTISAARLYYYWERDYRRALCRLSQAGARVKIMDYEEFAYCWENFV 161
Cdd:pfam18774  81 NVTLGIYVARLFMHDDDRNRQGLRILQMNGVTIQVMMNKDYCYCWKAFK 129
APOBEC4 pfam18775
APOBEC4; A member of the AID/APOBEC family of cytosine deaminases. The biological function of ...
 88-161 4.13e-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: 75.07  E-value: 4.13e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119580685   88 ITWFVSWTPCPDCVAKLAEFLSEHPNVTLTISAARLYYYWERDYRRALCRLSQAGARVKIMDYEEFAYCWENFV 161
Cdd:pfam18775   1 VTLYLSWSPCNECSEKIQEFLKKHPKVNLDIYFAQLYHTEEEDNRQGLRSLVEKGVTLSVMSGEDWIYCLRTFV 74
APOBEC1 pfam18769
APOBEC1; APOBEC1 deaminates cytosine both in RNA and ssDNA and has roles in both mRNA editing ...
 66-148 1.02e-16

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: 74.85  E-value: 1.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685   66 HAEMCFLSWFCGNQ--LPAYKCfQITWFVSWTPCPDCVAKLAEFLSEHPNVTLTISAARLYYYWERDYRRALCRLSQAGA 143
Cdd:pfam18769  18 HAEVNFLEKFFSERhfDPSVSC-SITWFLSWSPCGECSKAIGEFLSQHPNVTLVIYAARLFKHLDIRNRQGLRDLAMSGV 96


                  ....*
gi 119580685  144 RVKIM 148
Cdd:pfam18769  97 TIQIM 101
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 8-158 8.79e-15

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: 70.06  E-value: 8.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685   8 PMERMYRDTFYdnfenepILYGRSYTWLCYEVKikrgrsnllWDTGVFRGQVYFEPQY----HAEMCFLSWFCGNQlpaY 83
Cdd:cd01283    1 IEAALAAAEFA-------YAPYSNFTVGAALLT---------KDGRIFTGVNVENASYgltlCAERTAIGKAVSEG---L 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685  84 KCFQITWFVS-----WTPCPDCVAKLAEFLSehpnvtltisaARLYYYWERDYRralcrlsqagarvkimdyEEFAYCWE 158
Cdd:cd01283   62 RRYLVTWAVSdeggvWSPCGACRQVLAEFLP-----------SRLYIIIDNPKG------------------EEFAYTLS 112
APOBEC4_like pfam18774
APOBEC4-like -AID/APOBEC-deaminase; Cnidarian and Algal homologs of the APOBEC4-like AID ...
 253-349 6.56e-14

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: 67.98  E-value: 6.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685  253 HAELRFLDLVPSLQldPAQIYRVTWFISWSPCfsWGCAGEVRAFLQENTHVRLRIFAARIYDY-DPLYKEALQMLRDAGA 331
Cdd:pfam18774  36 HAEVNFLENFRSER--PSRSCTITWYLSWSPC--WECSGRILEFLSRHPNVTLGIYVARLFMHdDDRNRQGLRILQMNGV 111

                          90
                  ....*....|....*...
gi 119580685  332 QVSIMTYDEFEYCWDTFV 349
Cdd:pfam18774 112 TIQVMMNKDYCYCWKAFK 129
APOBEC1 pfam18769
APOBEC1; APOBEC1 deaminates cytosine both in RNA and ssDNA and has roles in both mRNA editing ...
 252-336 2.90e-11

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: 59.83  E-value: 2.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580685  252 RHAELRFLD-LVPSLQLDPAQIYRVTWFISWSPCfsWGCAGEVRAFLQENTHVRLRIFAARIYDY-DPLYKEALQMLRDA 329
Cdd:pfam18769  17 QHAEVNFLEkFFSERHFDPSVSCSITWFLSWSPC--GECSKAIGEFLSQHPNVTLVIYAARLFKHlDIRNRQGLRDLAMS 94


                  ....*..
gi 119580685  330 GAQVSIM 336
Cdd:pfam18769  95 GVTIQIM 101
APOBEC4 pfam18775
APOBEC4; A member of the AID/APOBEC family of cytosine deaminases. The biological function of ...
 275-349 1.41e-10

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: 56.96  E-value: 1.41e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119580685  275 VTWFISWSPCfsWGCAGEVRAFLQENTHVRLRIFAARIYDYDPLY-KEALQMLRDAGAQVSIMTYDEFEYCWDTFV 349
Cdd:pfam18775   1 VTLYLSWSPC--NECSEKIQEFLKKHPKVNLDIYFAQLYHTEEEDnRQGLRSLVEKGVTLSVMSGEDWIYCLRTFV 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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