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Conserved domains on  [gi|6678878|ref|NP_032624|]
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methylated-DNA--protein-cysteine methyltransferase isoform 1 [Mus musculus]

Protein Classification

methylated-DNA--[protein]-cysteine S-methyltransferase( domain architecture ID 11417447)

methylated-DNA--[protein]-cysteine S-methyltransferase is involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA; it repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
7-179 7.53e-56

DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, recombination and repair];


:

Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 174.68  E-value: 7.53e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678878    7 MKYSVLDSPLGKMELSGCERGLHGIRLlsgktpnTDPTEAPATPEVLGGPEGVPEPLVQCTAWLEAYFREPAATEGLPLp 86
Cdd:COG0350   2 IRYAIFDTPLGPLLIAATDRGLCALSF-------GDDREEALLARFPAALREDPPLLAEAARQLDAYFAGERKDFDLPL- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678878   87 ALHHPVFQQdsftrQVlWKLLKVVKFGETVSYQQLAALAGNPKAARAVGGAMRSNPVPILIPCHRVVRSDGAIGHYSgGG 166
Cdd:COG0350  74 DLRGTPFQR-----RV-WEALRKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSLGGYA-GG 146
                       170
                ....*....|...
gi 6678878  167 QAVKEWLLAHEGI 179
Cdd:COG0350 147 LERKRALLELEGA 159
 
Name Accession Description Interval E-value
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
7-179 7.53e-56

DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, recombination and repair];


Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 174.68  E-value: 7.53e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678878    7 MKYSVLDSPLGKMELSGCERGLHGIRLlsgktpnTDPTEAPATPEVLGGPEGVPEPLVQCTAWLEAYFREPAATEGLPLp 86
Cdd:COG0350   2 IRYAIFDTPLGPLLIAATDRGLCALSF-------GDDREEALLARFPAALREDPPLLAEAARQLDAYFAGERKDFDLPL- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678878   87 ALHHPVFQQdsftrQVlWKLLKVVKFGETVSYQQLAALAGNPKAARAVGGAMRSNPVPILIPCHRVVRSDGAIGHYSgGG 166
Cdd:COG0350  74 DLRGTPFQR-----RV-WEALRKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSLGGYA-GG 146
                       170
                ....*....|...
gi 6678878  167 QAVKEWLLAHEGI 179
Cdd:COG0350 147 LERKRALLELEGA 159
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
97-177 1.50e-40

O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are known are involved alkyl-DNA transferases which remove alkyl groups from DNA as part of alkylation DNA repair. Some of the proteins in this family are also transcription regulators and have a distinct transcription regulatory domain. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273157  Cd Length: 80  Bit Score: 132.82  E-value: 1.50e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678878     97 SFTRQVLWKLLKVVKFGETVSYQQLAALAGNPKAARAVGGAMRSNPVPILIPCHRVVRSDGAIGHYsGGGQAVKEWLLAH 176
Cdd:TIGR00589   1 TPFQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLTGY-GGGLERKEFLLEH 79

                  .
gi 6678878    177 E 177
Cdd:TIGR00589  80 E 80
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
97-179 1.01e-39

6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal DNA-binding domain of 6-O-methylguanine-DNA methyltransferases.


Pssm-ID: 460036  Cd Length: 81  Bit Score: 130.94  E-value: 1.01e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678878     97 SFTRQVlWKLLKVVKFGETVSYQQLAALAGNPKAARAVGGAMRSNPVPILIPCHRVVRSDGAIGHYSGGGqAVKEWLLAH 176
Cdd:pfam01035   1 PFQRRV-WEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSLGGYAGGL-ERKRALLEL 78

                  ...
gi 6678878    177 EGI 179
Cdd:pfam01035  79 EGV 81
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
98-178 6.56e-38

The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT and MGMT) reverses O6-alkylation DNA damage by transferring O6-alkyl adducts to an active site cysteine irreversibly, without inducing DNA strand breaks. ATases are specific for repair of guanines with O6-alkyl adducts, however human ATase is not limited to O6-methylguanine, repairing many other adducts at the O6-position of guanine as well. ATase is widely distributed among species. Most ATases have N- and C-terminal domains. The C-terminal domain contains the conserved active-site cysteine motif (PCHR), the O6-alkylguanine binding channel, and the helix-turn-helix (HTH) DNA-binding motif. The active site is located near the recognition helix of the HTH motif. While the C-terminal domain of ATase contains residues that are necessary for DNA binding and alkyl transfer, the function of the N-terminal domain is still unknown. Removal of the N-terminal domain abolishes the activity of the C-terminal domain, suggesting an important structural role for the N-terminal domain in orienting the C-terminal domain for proper catalysis. Some ATase C-terminal domain homologs are either single-domain proteins that lack an N-terminal domain, or have a tryptophan substituted in place of the acceptor cysteine (i.e. the motif PCHR is replaced by PWHR). ATase null mutant mice are viable, fertile, and have a normal lifespan.


Pssm-ID: 119438 [Multi-domain]  Cd Length: 79  Bit Score: 126.06  E-value: 6.56e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678878   98 FTRQVlWKLLKVVKFGETVSYQQLAALAGNPKAARAVGGAMRSNPVPILIPCHRVVRSDGAIGHYSgGGQAVKEWLLAHE 177
Cdd:cd06445   1 FQRRV-WEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGLGGYR-GGLERKRELLELE 78

                .
gi 6678878  178 G 178
Cdd:cd06445  79 G 79
PRK00901 PRK00901
methylated-DNA--protein-cysteine methyltransferase; Provisional
70-178 6.63e-25

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 234860 [Multi-domain]  Cd Length: 155  Bit Score: 95.12  E-value: 6.63e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678878    70 LEAYFREPAATEGLPL-PalhhpvfQQDSFTRQVlWKLLKVVKFGETVSYQQLAALAGNPKAARAVGGAMRSNPVPILIP 148
Cdd:PRK00901  52 LEEYFEGKRKKFDLPLaP-------QGTEFQKKV-WKALQEIPYGETRSYKEIAVNIGNPKACRAVGLANNKNPIPIFIP 123
                         90       100       110
                 ....*....|....*....|....*....|
gi 6678878   149 CHRVVRSDGAIGHYSGGGQaVKEWLLAHEG 178
Cdd:PRK00901 124 CHRVIGANGKLVGYAGGLD-IKEKLLKLEK 152
 
Name Accession Description Interval E-value
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
7-179 7.53e-56

DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, recombination and repair];


Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 174.68  E-value: 7.53e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678878    7 MKYSVLDSPLGKMELSGCERGLHGIRLlsgktpnTDPTEAPATPEVLGGPEGVPEPLVQCTAWLEAYFREPAATEGLPLp 86
Cdd:COG0350   2 IRYAIFDTPLGPLLIAATDRGLCALSF-------GDDREEALLARFPAALREDPPLLAEAARQLDAYFAGERKDFDLPL- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678878   87 ALHHPVFQQdsftrQVlWKLLKVVKFGETVSYQQLAALAGNPKAARAVGGAMRSNPVPILIPCHRVVRSDGAIGHYSgGG 166
Cdd:COG0350  74 DLRGTPFQR-----RV-WEALRKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSLGGYA-GG 146
                       170
                ....*....|...
gi 6678878  167 QAVKEWLLAHEGI 179
Cdd:COG0350 147 LERKRALLELEGA 159
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
97-177 1.50e-40

O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are known are involved alkyl-DNA transferases which remove alkyl groups from DNA as part of alkylation DNA repair. Some of the proteins in this family are also transcription regulators and have a distinct transcription regulatory domain. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273157  Cd Length: 80  Bit Score: 132.82  E-value: 1.50e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678878     97 SFTRQVLWKLLKVVKFGETVSYQQLAALAGNPKAARAVGGAMRSNPVPILIPCHRVVRSDGAIGHYsGGGQAVKEWLLAH 176
Cdd:TIGR00589   1 TPFQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLTGY-GGGLERKEFLLEH 79

                  .
gi 6678878    177 E 177
Cdd:TIGR00589  80 E 80
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
97-179 1.01e-39

6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal DNA-binding domain of 6-O-methylguanine-DNA methyltransferases.


Pssm-ID: 460036  Cd Length: 81  Bit Score: 130.94  E-value: 1.01e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678878     97 SFTRQVlWKLLKVVKFGETVSYQQLAALAGNPKAARAVGGAMRSNPVPILIPCHRVVRSDGAIGHYSGGGqAVKEWLLAH 176
Cdd:pfam01035   1 PFQRRV-WEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSLGGYAGGL-ERKRALLEL 78

                  ...
gi 6678878    177 EGI 179
Cdd:pfam01035  79 EGV 81
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
98-178 6.56e-38

The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT and MGMT) reverses O6-alkylation DNA damage by transferring O6-alkyl adducts to an active site cysteine irreversibly, without inducing DNA strand breaks. ATases are specific for repair of guanines with O6-alkyl adducts, however human ATase is not limited to O6-methylguanine, repairing many other adducts at the O6-position of guanine as well. ATase is widely distributed among species. Most ATases have N- and C-terminal domains. The C-terminal domain contains the conserved active-site cysteine motif (PCHR), the O6-alkylguanine binding channel, and the helix-turn-helix (HTH) DNA-binding motif. The active site is located near the recognition helix of the HTH motif. While the C-terminal domain of ATase contains residues that are necessary for DNA binding and alkyl transfer, the function of the N-terminal domain is still unknown. Removal of the N-terminal domain abolishes the activity of the C-terminal domain, suggesting an important structural role for the N-terminal domain in orienting the C-terminal domain for proper catalysis. Some ATase C-terminal domain homologs are either single-domain proteins that lack an N-terminal domain, or have a tryptophan substituted in place of the acceptor cysteine (i.e. the motif PCHR is replaced by PWHR). ATase null mutant mice are viable, fertile, and have a normal lifespan.


Pssm-ID: 119438 [Multi-domain]  Cd Length: 79  Bit Score: 126.06  E-value: 6.56e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678878   98 FTRQVlWKLLKVVKFGETVSYQQLAALAGNPKAARAVGGAMRSNPVPILIPCHRVVRSDGAIGHYSgGGQAVKEWLLAHE 177
Cdd:cd06445   1 FQRRV-WEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGLGGYR-GGLERKRELLELE 78

                .
gi 6678878  178 G 178
Cdd:cd06445  79 G 79
PRK00901 PRK00901
methylated-DNA--protein-cysteine methyltransferase; Provisional
70-178 6.63e-25

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 234860 [Multi-domain]  Cd Length: 155  Bit Score: 95.12  E-value: 6.63e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678878    70 LEAYFREPAATEGLPL-PalhhpvfQQDSFTRQVlWKLLKVVKFGETVSYQQLAALAGNPKAARAVGGAMRSNPVPILIP 148
Cdd:PRK00901  52 LEEYFEGKRKKFDLPLaP-------QGTEFQKKV-WKALQEIPYGETRSYKEIAVNIGNPKACRAVGLANNKNPIPIFIP 123
                         90       100       110
                 ....*....|....*....|....*....|
gi 6678878   149 CHRVVRSDGAIGHYSGGGQaVKEWLLAHEG 178
Cdd:PRK00901 124 CHRVIGANGKLVGYAGGLD-IKEKLLKLEK 152
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
7-177 2.33e-22

bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 92.93  E-value: 2.33e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678878     7 MKYSVLDSPLGKMELSGCERGLHGIRL----------LSGKTPNTDptEAPATPEVlggpegvPEPLVQCTAWLEAYFRE 76
Cdd:PRK15435 189 VRYALADCELGRCLVAESERGICAILLgdddaaliseLQQMFPAAD--NAPADLTF-------QQHVREVIASLNQRDTP 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678878    77 PAategLPLPaLHHPVFQQdsftrQVlWKLLKVVKFGETVSYQQLAALAGNPKAARAVGGAMRSNPVPILIPCHRVVRSD 156
Cdd:PRK15435 260 LT----LPLD-IRGTAFQQ-----QV-WQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIVIPCHRVVRGD 328
                        170       180
                 ....*....|....*....|.
gi 6678878   157 GAIGHYSgGGQAVKEWLLAHE 177
Cdd:PRK15435 329 GALSGYR-WGVSRKAQLLRRE 348
PRK10286 PRK10286
methylated-DNA--[protein]-cysteine S-methyltransferase;
77-178 2.72e-22

methylated-DNA--[protein]-cysteine S-methyltransferase;


Pssm-ID: 182355 [Multi-domain]  Cd Length: 171  Bit Score: 88.77  E-value: 2.72e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678878    77 PAATEGLPlpalhhpvfqqdsFTRQVlWKLLKVVKFGETVSYQQLAALAGNPKAARAVGGAMRSNPVPILIPCHRVVRSD 156
Cdd:PRK10286  81 PTATGGTP-------------FQREV-WQTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIGRN 146
                         90       100
                 ....*....|....*....|..
gi 6678878   157 GAIGHYSGGGQAvKEWLLAHEG 178
Cdd:PRK10286 147 GTMTGYAGGVQR-KEWLLRHEG 167
Atl1 COG3695
Alkylated DNA nucleotide flippase Atl1, participates in nucleotide excision repair, Ada-like ...
95-180 7.79e-21

Alkylated DNA nucleotide flippase Atl1, participates in nucleotide excision repair, Ada-like DNA-binding domain [Transcription];


Pssm-ID: 442910  Cd Length: 104  Bit Score: 82.93  E-value: 7.79e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678878   95 QDSFTRQVlWKLLKVVKFGETVSYQQLAALAGNPKAARAVGGAMRSNPVPILIPCHRVVRSDGAIGHYSGGGQAVKEWLL 174
Cdd:COG3695   3 MEEFYERV-YEVVAQIPPGRVATYGDIAALAGLPRGARQVGRALRALPEGSDLPWHRVVNADGRLSPGHAGGAEEQRELL 81

                ....*.
gi 6678878  175 AHEGIP 180
Cdd:COG3695  82 EAEGVP 87
Methyltransf_1N pfam02870
6-O-methylguanine DNA methyltransferase, ribonuclease-like domain; This entry represents the ...
6-94 5.23e-18

6-O-methylguanine DNA methyltransferase, ribonuclease-like domain; This entry represents the N-terminal ribonuclease-like domain associated with 6-O-methylguanine DNA methyltransferase activity. The repair of DNA containing O6-alkylated guanine is carried out by DNA-[protein]-cysteine S-methyltransferase (also known as O-6-methylguanine-DNA-alkyltransferase)


Pssm-ID: 397139 [Multi-domain]  Cd Length: 77  Bit Score: 75.09  E-value: 5.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678878      6 KMKYSVLDSPLGKMELSGCERGLHGIRLLSGKTPntdptEAPATPEVLGGPEgvpepLVQCTAWLEAYFREPAATEGlpL 85
Cdd:pfam02870   1 ALYYTLIDSPLGRLLLAGDERGLTAIDFLDKDYA-----LRKELPKVLPQPE-----LLPALALLVQALEEYFAGEL--K 68

                  ....*....
gi 6678878     86 PALHHPVFQ 94
Cdd:pfam02870  69 PEFTLPLDQ 77
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
58-186 2.68e-17

Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), contains Zn-binding and two AraC-type DNA-binding domains [Replication, recombination and repair];


Pssm-ID: 441772 [Multi-domain]  Cd Length: 358  Bit Score: 78.94  E-value: 2.68e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678878   58 GVPEPLVQCTAWLEAYFREPAATEGLPLPALHHPVFQQDsftrqvlWKLLKVVKFGETVSYQQLAALAGNPKAARAVGGA 137
Cdd:COG2169 238 GGDAAFEQLVAEVVGFVEGPLLGLDLPLDLRGTAFQQRV-------WQALRAIPAGETASYAEIAARIGAPKAVRAVAAA 310
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 6678878  138 MRSNPVPILIPCHRVVRSDGAIGHYsGGGQAVKEWLLAHEGIPTGQPAS 186
Cdd:COG2169 311 CAANQLAVAIPCHRVVRADGALSGY-RWGVERKRALLEREAAAAAAAAA 358
PRK03887 PRK03887
methylated-DNA--protein-cysteine methyltransferase; Provisional
97-181 1.43e-16

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 167628 [Multi-domain]  Cd Length: 175  Bit Score: 74.00  E-value: 1.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678878    97 SFTRQVLWKLLKVVKFGETVSYQQLA-ALAGNPkaaRAVGGAMRSNPVPILIPCHRVVRSDGaIGHYSGGGQAvKEWLLA 175
Cdd:PRK03887  92 PFERKVYEWLTKNVKRGEVITYGELAkALNTSP---RAVGGAMKRNPYPIIVPCHRVVGRKN-PGLYTPKPEY-KKFLLE 166

                 ....*.
gi 6678878   176 HEGIPT 181
Cdd:PRK03887 167 VEGVKE 172
 
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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