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Conserved domains on  [gi|1676317112|ref|NP_001257340|]
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DNA dC-

Protein Classification

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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 1.04e-103

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: 302.36  E-value: 1.04e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112  10 ERMYRDTFYDNFENEPILYGRSYTWLCYEVKIKRGRSNLLWDTGVFRGQvyfkPQYHAEMCFLSWFCGNQLPAYKCFQIT 89
Cdd:pfam18782   1 KRMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGTWLPQHRGFFRNQ----AKYHAELCFLSWFCGNQLPPYQNYQVT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112  90 WFVSWTPCPDCVAKLAEFLSEHPNVTLTISAARLYYYWERDYRRALCRLSQAGARVTIMDYEEFAYCWENFVYNEGQQFM 169
Cdd:pfam18782  77 WYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQGEPFQ 156

                         170       180
                  ....*....|....*....|
gi 1676317112 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.
 191-352 1.17e-81

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: 246.51  E-value: 1.17e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112 191 YLMDPDTFTFNFNNDPLVLRRRQTYLCYEVERLDNGTWVLmdQHMGFLCNE-----------------LDPAQIYRVTWF 253
Cdd:pfam18782   1 KRMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGTWLP--QHRGFFRNQakyhaelcflswfcgnqLPPYQNYQVTWY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112 254 ISWSPCFSwgCAGEVRAFLQENTHVRLRIFAARIY-DYDPLYKEALQMLRDAGAQVSIMTYDEFEYCWDTFVYRQGCPFQ 332
Cdd:pfam18782  79 VSWSPCPE--CAGEVAEFLAEHPNVTLTIFAARLYyFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQGEPFQ 156

                         170       180
                  ....*....|....*....|
gi 1676317112 333 PWDGLEEHSQALSGRLRAIL 352
Cdd:pfam18782 157 PWDGLEENSRFLHRRLREIL 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 1.04e-103

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: 302.36  E-value: 1.04e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112  10 ERMYRDTFYDNFENEPILYGRSYTWLCYEVKIKRGRSNLLWDTGVFRGQvyfkPQYHAEMCFLSWFCGNQLPAYKCFQIT 89
Cdd:pfam18782   1 KRMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGTWLPQHRGFFRNQ----AKYHAELCFLSWFCGNQLPPYQNYQVT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112  90 WFVSWTPCPDCVAKLAEFLSEHPNVTLTISAARLYYYWERDYRRALCRLSQAGARVTIMDYEEFAYCWENFVYNEGQQFM 169
Cdd:pfam18782  77 WYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQGEPFQ 156

                         170       180
                  ....*....|....*....|
gi 1676317112 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.
 191-352 1.17e-81

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: 246.51  E-value: 1.17e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112 191 YLMDPDTFTFNFNNDPLVLRRRQTYLCYEVERLDNGTWVLmdQHMGFLCNE-----------------LDPAQIYRVTWF 253
Cdd:pfam18782   1 KRMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGTWLP--QHRGFFRNQakyhaelcflswfcgnqLPPYQNYQVTWY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112 254 ISWSPCFSwgCAGEVRAFLQENTHVRLRIFAARIY-DYDPLYKEALQMLRDAGAQVSIMTYDEFEYCWDTFVYRQGCPFQ 332
Cdd:pfam18782  79 VSWSPCPE--CAGEVAEFLAEHPNVTLTIFAARLYyFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQGEPFQ 156

                         170       180
                  ....*....|....*....|
gi 1676317112 333 PWDGLEEHSQALSGRLRAIL 352
Cdd:pfam18782 157 PWDGLEENSRFLHRRLREIL 176
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 8-158 6.73e-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: 6.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112   8 PMERMYRDTFYdnfenepILYGRSYTWLCYEVKikrgrsnllWDTGVFRGQVYFKPQY----HAEMCFLSWFCGNQlpaY 83
Cdd:cd01283     1 IEAALAAAEFA-------YAPYSNFTVGAALLT---------KDGRIFTGVNVENASYgltlCAERTAIGKAVSEG---L 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112  84 KCFQITWFVS-----WTPCPDCVAKLAEFLSehpnvtltisaARLYYYWERDYRralcrlsqagarvtimdyEEFAYCWE 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 1.04e-103

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: 302.36  E-value: 1.04e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112  10 ERMYRDTFYDNFENEPILYGRSYTWLCYEVKIKRGRSNLLWDTGVFRGQvyfkPQYHAEMCFLSWFCGNQLPAYKCFQIT 89
Cdd:pfam18782   1 KRMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGTWLPQHRGFFRNQ----AKYHAELCFLSWFCGNQLPPYQNYQVT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112  90 WFVSWTPCPDCVAKLAEFLSEHPNVTLTISAARLYYYWERDYRRALCRLSQAGARVTIMDYEEFAYCWENFVYNEGQQFM 169
Cdd:pfam18782  77 WYVSWSPCPECAGEVAEFLAEHPNVTLTIFAARLYYFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQGEPFQ 156

                         170       180
                  ....*....|....*....|
gi 1676317112 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 5.64e-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: 280.25  E-value: 5.64e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112  12 MYRDTFYDNFENEPILYGRSYTWLCYEVKiKRGRSNLLWDTGVFRGQvyfkPQYHAEMCFLSWFCGNQLPAYKCFQITWF 91
Cdd:pfam18772   1 MDPKTFKFQFKNVPYASGRNKTYLCYEVE-TRSGSDLSPDRGYLRNQ----AGCHAELCFLSWILPWQLDPGQKYQVTWY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112  92 VSWTPCPDCVAKLAEFLSEHPNVTLTISAARLYYYWERDYRRALCRLSQAGARVTIMDYEEFAYCWENFVYNEGQQFMPW 171
Cdd:pfam18772  76 VSWSPCPDCARKLAEFLARHPNLSLTIFAARLYFFWEPEYQEGLRRLKRAGAQLKIMDYQDFEYCWENFVDNQGRPFEPW 155

                         170
                  ....*....|....*....
gi 1676317112 172 YKFDENYAFLHRTLKEILR 190
Cdd:pfam18772 156 EDLDENYEYLSRKLQEILR 174
NAD1 pfam18778
Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned ...
 10-189 2.61e-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: 255.67  E-value: 2.61e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112  10 ERMYRDTFYDNFENEPILYGRSYTWLCYEVKikRGRSNLLWdTGVFRGQvyfKPQYHAEMCFLSWFCGNQL-PAYKCFQI 88
Cdd:pfam18778   1 ERMSPETFKFQFKNVEYASGRNKTLLCYEVK--RGNSSSLW-RGHLRNE---NSGCHAEICFLRWFSSWRLfDPSQCYTI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112  89 TWFVSWTPCPDCVAKLAEFLSEHPNVTLTISAARLYYYWERDYRRALCRLSQAGARVTIMDYEEFAYCWENFVYNEGQQF 168
Cdd:pfam18778  75 TWYLSWSPCPSCAAKLAEFLKAHPNVTLTIFAARLYYFEDPWNQEGLRSLASAGVTLSIMDYSDFEYCWENFVDNEGRPF 154

                         170       180
                  ....*....|....*....|.
gi 1676317112 169 MPWYKFDENYAFLHRTLKEIL 189
Cdd:pfam18778 155 VPWEDLEENSRYYHRKLQRIL 175
NAD2 pfam18782
Novel AID APOBEC clade 2; A distnct family of AID/APOBEC deaminases found only in Amphibians.
 191-352 1.17e-81

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: 246.51  E-value: 1.17e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112 191 YLMDPDTFTFNFNNDPLVLRRRQTYLCYEVERLDNGTWVLmdQHMGFLCNE-----------------LDPAQIYRVTWF 253
Cdd:pfam18782   1 KRMYPRTFYFNFNNKPILYGRNKTYLCYEVERLDNGTWLP--QHRGFFRNQakyhaelcflswfcgnqLPPYQNYQVTWY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112 254 ISWSPCFSwgCAGEVRAFLQENTHVRLRIFAARIY-DYDPLYKEALQMLRDAGAQVSIMTYDEFEYCWDTFVYRQGCPFQ 332
Cdd:pfam18782  79 VSWSPCPE--CAGEVAEFLAEHPNVTLTIFAARLYyFWDPDYQEALRRLRQAGARVKIMDYEEFEYCWENFVYNQGEPFQ 156

                         170       180
                  ....*....|....*....|
gi 1676317112 333 PWDGLEEHSQALSGRLRAIL 352
Cdd:pfam18782 157 PWDGLEENSRFLHRRLREIL 176
NAD1 pfam18778
Novel AID APOBEC clade 1; A distinct family of AID/APOBEC-like deaminases found in ray-finned ...
 191-352 9.03e-65

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: 203.28  E-value: 9.03e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112 191 YLMDPDTFTFNFNNDPLVLRRRQTYLCYEVERL-DNGTW--VLMDQHMG----------FLCNEL-DPAQIYRVTWFISW 256
Cdd:pfam18778   1 ERMSPETFKFQFKNVEYASGRNKTLLCYEVKRGnSSSLWrgHLRNENSGchaeicflrwFSSWRLfDPSQCYTITWYLSW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112 257 SPCFSwgCAGEVRAFLQENTHVRLRIFAARIYDY-DPLYKEALQMLRDAGAQVSIMTYDEFEYCWDTFVYRQGCPFQPWD 335
Cdd:pfam18778  81 SPCPS--CAAKLAEFLKAHPNVTLTIFAARLYYFeDPWNQEGLRSLASAGVTLSIMDYSDFEYCWENFVDNEGRPFVPWE 158

                         170
                  ....*....|....*..
gi 1676317112 336 GLEEHSQALSGRLRAIL 352
Cdd:pfam18778 159 DLEENSRYYHRKLQRIL 175
SNAD4 pfam18750
Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases ...
 39-159 8.80e-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: 177.84  E-value: 8.80e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112  39 VKIKRGRSNLLWDTGVFRGqvyfKPQYHAEMCFLSWFCGNQLPAYKCFQITWFVSWTPCPDCVAKLAEFLSEHPNVTLTI 118
Cdd:pfam18750   1 YEIKWGNGSKIWQRGYLSN----EHEQHAEICFLENIRSRELDPSQRYRVTWYLSWSPCPECAQKIAEFLAEHPNVTLTI 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1676317112 119 SAARLyYYWERDYRRALCRLSQAGARVTIMDYEEFAYCWEN 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 3.24e-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: 178.33  E-value: 3.24e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112  17 FYDNFENEPILYGRSYTWLCYEVKIKRGrSNLLWDTGVFRGQVYFKPqyHAEMCFLSWFCGNQLPAYKCFQITWFVSWTP 96
Cdd:pfam08210   1 FFFHFKNLPYASGRHETYLCYEVKRDSG-GLVVEDKGYLRNQAASSL--HAEERFLRWIHDLALDPGSNYEVTWYVSWSP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112  97 CPDCVAKLAEFLSEHPNVTLTISAARLYYYWERDY--RRALCRLSQAGARVTIMDYEEFAYCWENFVYNEGQQFMPWYKF 174
Cdd:pfam08210  78 CNECASELAAFLSKHPNVRLRIFVSRLYYWEEPDYwnREGLRSLAQAGVQLRPMSYKDFEYCWNNFVDHDGEPFKPWDGL 157

                         170
                  ....*....|...
gi 1676317112 175 DENYAFLHRTLKE 187
Cdd:pfam08210 158 HENSVYLARKLQE 170
APOBEC_N pfam08210
APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. ...
 198-349 3.78e-53

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: 173.32  E-value: 3.78e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112 198 FTFNFNNDPLVLRRRQTYLCYEVERLDNGTWVlmdQHMGFLCNE-------------------LDPAQIYRVTWFISWSP 258
Cdd:pfam08210   1 FFFHFKNLPYASGRHETYLCYEVKRDSGGLVV---EDKGYLRNQaasslhaeerflrwihdlaLDPGSNYEVTWYVSWSP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112 259 CFSwgCAGEVRAFLQENTHVRLRIFAARIY-DYDPLY--KEALQMLRDAGAQVSIMTYDEFEYCWDTFVYRQGCPFQPWD 335
Cdd:pfam08210  78 CNE--CASELAAFLSKHPNVRLRIFVSRLYyWEEPDYwnREGLRSLAQAGVQLRPMSYKDFEYCWNNFVDHDGEPFKPWD 155

                         170
                  ....*....|....
gi 1676317112 336 GLEEHSQALSGRLR 349
Cdd:pfam08210 156 GLHENSVYLARKLQ 169
APOBEC_C pfam05240
APOBEC-like C-terminal domain; This domain is found at the C-termini of the Apolipoprotein B ...
 112-189 7.57e-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: 135.30  E-value: 7.57e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1676317112 112 PNVTLTISAARLYYYWERDYRRALCRLSQAGARVTIMDYEEFAYCWENFVYNEGQQFMPWYKFDENYAFLHRTLKEIL 189
Cdd:pfam05240   1 PNVSLTIFAARLYYHWDPEYQQGLRRLVQAGAQVAIMSYKEFEYCWDNFVDNQGRPFQPWEGLEENSQLLSRRLQEIL 78
SNAD4 pfam18750
Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases ...
 237-322 4.76e-38

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: 132.00  E-value: 4.76e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112 237 FLCNELDPAQIYRVTWFISWSPCFSwgCAGEVRAFLQENTHVRLRIFAARIYDYDPLYKEALQMLRDAGAQVSIMTYDEF 316
Cdd:pfam18750  33 IRSRELDPSQRYRVTWYLSWSPCPE--CAQKIAEFLAEHPNVTLTIFAARLYHWDEDNRQGLRSLAQAGVTLQIMTLEDF 110


                  ....*.
gi 1676317112 317 EYCWDT 322
Cdd:pfam18750 111 EYCWKN 116
APOBEC_C pfam05240
APOBEC-like C-terminal domain; This domain is found at the C-termini of the Apolipoprotein B ...
 277-352 8.78e-37

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: 8.78e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1676317112 277 HVRLRIFAARIYD-YDPLYKEALQMLRDAGAQVSIMTYDEFEYCWDTFVYRQGCPFQPWDGLEEHSQALSGRLRAIL 352
Cdd:pfam05240   2 NVSLTIFAARLYYhWDPEYQQGLRRLVQAGAQVAIMSYKEFEYCWDNFVDNQGRPFQPWEGLEENSQLLSRRLQEIL 78
APOBEC3 pfam18771
APOBEC3; APOBEC3 deaminases act as restriction factors in the innate response to retroviruses ...
 33-168 5.10e-34

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: 122.21  E-value: 5.10e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112  33 TWLCYEVKikrGRSNLLWDTGVFRGqvyfKPQYHAEMCFLSWFCGNQLPAYKCFQITWFVSWTPCPDCVAKLAEFLSEHP 112
Cdd:pfam18771   6 AYLCYQLK---GRNGSALDRGYFSN----KKKRHAEIRFIDKIRSLDLDNIQCYRITCYITWSPCPNCAAELVDFISLNP 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1676317112 113 NVTLTISAARLYYYWERDYRRALCRLSQAGARVTIMDYEEFAYCWENFVYNEGQQF 168
Cdd:pfam18771  79 HLKLRIFASRLYYHWERSYKEGLQKLQRAGVSVAVMTLPEFQDCWEDFVDHQEEPF 134
APOBEC3 pfam18771
APOBEC3; APOBEC3 deaminases act as restriction factors in the innate response to retroviruses ...
 211-332 1.72e-29

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: 110.27  E-value: 1.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112 211 RRQTYLCYEVERLDNGTWVlmdqhMGFLCNE-----------------LDPAQIYRVTWFISWSPCFSwgCAGEVRAFLQ 273
Cdd:pfam18771   3 DRKAYLCYQLKGRNGSALD-----RGYFSNKkkrhaeirfidkirsldLDNIQCYRITCYITWSPCPN--CAAELVDFIS 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112 274 ENTHVRLRIFAARIYDYD-PLYKEALQMLRDAGAQVSIMTYDEFEYCWDTFVYRQGCPFQ 332
Cdd:pfam18771  76 LNPHLKLRIFASRLYYHWeRSYKEGLQKLQRAGVSVAVMTLPEFQDCWEDFVDHQEEPFR 135
APOBEC4_like pfam18774
APOBEC4-like -AID/APOBEC-deaminase; Cnidarian and Algal homologs of the APOBEC4-like AID ...
 33-161 1.19e-20

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: 86.47  E-value: 1.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112  33 TWLCYEVKIKRGRsnllwdtgVFRGQVYFKPQYHAEMCFLSWFCGnQLPAYKCfQITWFVSWTPCPDCVAKLAEFLSEHP 112
Cdd:pfam18774  11 ICLLYEIQWGRGT--------IWRNWTENNCTEHAEVNFLENFRS-ERPSRSC-TITWYLSWSPCWECSGRILEFLSRHP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1676317112 113 NVTLTISAARLYYYWERDYRRALCRLSQAGARVTIMDYEEFAYCWENFV 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 1.62e-16

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: 1.62e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1676317112  88 ITWFVSWTPCPDCVAKLAEFLSEHPNVTLTISAARLYYYWERDYRRALCRLSQAGARVTIMDYEEFAYCWENFV 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 2.44e-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: 73.69  E-value: 2.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112  66 HAEMCFLSWFCGNQ--LPAYKCfQITWFVSWTPCPDCVAKLAEFLSEHPNVTLTISAARLYYYWERDYRRALCRLSQAGA 143
Cdd:pfam18769  18 HAEVNFLEKFFSERhfDPSVSC-SITWFLSWSPCGECSKAIGEFLSQHPNVTLVIYAARLFKHLDIRNRQGLRDLAMSGV 96


                  ....*
gi 1676317112 144 RVTIM 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 6.73e-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: 6.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112   8 PMERMYRDTFYdnfenepILYGRSYTWLCYEVKikrgrsnllWDTGVFRGQVYFKPQY----HAEMCFLSWFCGNQlpaY 83
Cdd:cd01283     1 IEAALAAAEFA-------YAPYSNFTVGAALLT---------KDGRIFTGVNVENASYgltlCAERTAIGKAVSEG---L 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317112  84 KCFQITWFVS-----WTPCPDCVAKLAEFLSehpnvtltisaARLYYYWERDYRralcrlsqagarvtimdyEEFAYCWE 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 ...
 250-324 6.20e-13

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: 65.28  E-value: 6.20e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1676317112 250 VTWFISWSPCfsWGCAGEVRAFLQENTHVRLRIFAARIYDY-DPLYKEALQMLRDAGAQVSIMTYDEFEYCWDTFV 324
Cdd:pfam18774  56 ITWYLSWSPC--WECSGRILEFLSRHPNVTLGIYVARLFMHdDDRNRQGLRILQMNGVTIQVMMNKDYCYCWKAFK 129
APOBEC4 pfam18775
APOBEC4; A member of the AID/APOBEC family of cytosine deaminases. The biological function of ...
 250-324 1.34e-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: 1.34e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1676317112 250 VTWFISWSPCfsWGCAGEVRAFLQENTHVRLRIFAARIYDYDPLY-KEALQMLRDAGAQVSIMTYDEFEYCWDTFV 324
Cdd:pfam18775   1 VTLYLSWSPC--NECSEKIQEFLKKHPKVNLDIYFAQLYHTEEEDnRQGLRSLVEKGVTLSVMSGEDWIYCLRTFV 74
APOBEC1 pfam18769
APOBEC1; APOBEC1 deaminates cytosine both in RNA and ssDNA and has roles in both mRNA editing ...
 250-311 6.58e-09

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: 52.89  E-value: 6.58e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1676317112 250 VTWFISWSPCfsWGCAGEVRAFLQENTHVRLRIFAARIYDY-DPLYKEALQMLRDAGAQVSIM 311
Cdd:pfam18769  41 ITWFLSWSPC--GECSKAIGEFLSQHPNVTLVIYAARLFKHlDIRNRQGLRDLAMSGVTIQIM 101
 
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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