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Conserved domains on  [gi|115533068|ref|NP_001041054|]
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Methylated-DNA--protein-cysteine methyltransferase [Caenorhabditis elegans]

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, ...
87-171 6.41e-46

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


:

Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 148.10  E-value: 6.41e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533068  87 TAFGMQVYSAIQKIPKGETRSYSDIAREIGNPSAVRAVASACARNNLAYIVPCHRVIGSTGNLSGYRWGIAKKRRLLQAE 166
Cdd:COG0350   78 TPFQRRVWEALRKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSLGGYAGGLERKRALLELE 157

                 ....*
gi 115533068 167 GAELR 171
Cdd:COG0350  158 GALAA 162
 
Name Accession Description Interval E-value
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
87-171 6.41e-46

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


Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 148.10  E-value: 6.41e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533068  87 TAFGMQVYSAIQKIPKGETRSYSDIAREIGNPSAVRAVASACARNNLAYIVPCHRVIGSTGNLSGYRWGIAKKRRLLQAE 166
Cdd:COG0350   78 TPFQRRVWEALRKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSLGGYAGGLERKRALLELE 157

                 ....*
gi 115533068 167 GAELR 171
Cdd:COG0350  158 GALAA 162
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
88-168 5.13e-42

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: 135.18  E-value: 5.13e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533068   88 AFGMQVYSAIQKIPKGETRSYSDIAREIGNPSAVRAVASACARNNLAYIVPCHRVIGSTGNLSGYRWGIAKKRRLLQAEG 167
Cdd:pfam01035   1 PFQRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSLGGYAGGLERKRALLELEG 80

                  .
gi 115533068  168 A 168
Cdd:pfam01035  81 V 81
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
89-167 6.62e-39

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: 127.21  E-value: 6.62e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115533068  89 FGMQVYSAIQKIPKGETRSYSDIAREIGNPSAVRAVASACARNNLAYIVPCHRVIGSTGNLSGYRWGIAKKRRLLQAEG 167
Cdd:cd06445    1 FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGLGGYRGGLERKRELLELEG 79
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
87-166 2.10e-36

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: 121.27  E-value: 2.10e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533068   87 TAFGMQVYSAIQKIPKGETRSYSDIAREIGNPSAVRAVASACARNNLAYIVPCHRVIGSTGNLSGYRWGIAKKRRLLQAE 166
Cdd:TIGR00589   1 TPFQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLTGYGGGLERKEFLLEHE 80
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
45-166 2.46e-36

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


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 128.76  E-value: 2.46e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533068  45 ELHDAYPTVNFIPGKPTQSSGIVQALNTLDSTIKVNAVH---KGdTAFGMQVYSAIQKIPKGETRSYSDIAREIGNPSAV 121
Cdd:PRK15435 225 ELQQMFPAADNAPADLTFQQHVREVIASLNQRDTPLTLPldiRG-TAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAV 303
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 115533068 122 RAVASACARNNLAYIVPCHRVIGSTGNLSGYRWGIAKKRRLLQAE 166
Cdd:PRK15435 304 RAVASACAANKLAIVIPCHRVVRGDGALSGYRWGVSRKAQLLRRE 348
 
Name Accession Description Interval E-value
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
87-171 6.41e-46

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


Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 148.10  E-value: 6.41e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533068  87 TAFGMQVYSAIQKIPKGETRSYSDIAREIGNPSAVRAVASACARNNLAYIVPCHRVIGSTGNLSGYRWGIAKKRRLLQAE 166
Cdd:COG0350   78 TPFQRRVWEALRKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSLGGYAGGLERKRALLELE 157

                 ....*
gi 115533068 167 GAELR 171
Cdd:COG0350  158 GALAA 162
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
88-168 5.13e-42

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: 135.18  E-value: 5.13e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533068   88 AFGMQVYSAIQKIPKGETRSYSDIAREIGNPSAVRAVASACARNNLAYIVPCHRVIGSTGNLSGYRWGIAKKRRLLQAEG 167
Cdd:pfam01035   1 PFQRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSLGGYAGGLERKRALLELEG 80

                  .
gi 115533068  168 A 168
Cdd:pfam01035  81 V 81
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
89-167 6.62e-39

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: 127.21  E-value: 6.62e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115533068  89 FGMQVYSAIQKIPKGETRSYSDIAREIGNPSAVRAVASACARNNLAYIVPCHRVIGSTGNLSGYRWGIAKKRRLLQAEG 167
Cdd:cd06445    1 FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGLGGYRGGLERKRELLELEG 79
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
87-166 2.10e-36

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: 121.27  E-value: 2.10e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533068   87 TAFGMQVYSAIQKIPKGETRSYSDIAREIGNPSAVRAVASACARNNLAYIVPCHRVIGSTGNLSGYRWGIAKKRRLLQAE 166
Cdd:TIGR00589   1 TPFQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLTGYGGGLERKEFLLEHE 80
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
45-166 2.46e-36

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


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 128.76  E-value: 2.46e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533068  45 ELHDAYPTVNFIPGKPTQSSGIVQALNTLDSTIKVNAVH---KGdTAFGMQVYSAIQKIPKGETRSYSDIAREIGNPSAV 121
Cdd:PRK15435 225 ELQQMFPAADNAPADLTFQQHVREVIASLNQRDTPLTLPldiRG-TAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAV 303
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 115533068 122 RAVASACARNNLAYIVPCHRVIGSTGNLSGYRWGIAKKRRLLQAE 166
Cdd:PRK15435 304 RAVASACAANKLAIVIPCHRVVRGDGALSGYRWGVSRKAQLLRRE 348
PRK00901 PRK00901
methylated-DNA--protein-cysteine methyltransferase; Provisional
87-167 1.43e-28

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 234860 [Multi-domain]  Cd Length: 155  Bit Score: 103.59  E-value: 1.43e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533068  87 TAFGMQVYSAIQKIPKGETRSYSDIAREIGNPSAVRAVASACARNNLAYIVPCHRVIGSTGNLSGYRWGIAKKRRLLQAE 166
Cdd:PRK00901  72 TEFQKKVWKALQEIPYGETRSYKEIAVNIGNPKACRAVGLANNKNPIPIFIPCHRVIGANGKLVGYAGGLDIKEKLLKLE 151

                 .
gi 115533068 167 G 167
Cdd:PRK00901 152 K 152
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
86-171 5.38e-25

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: 98.59  E-value: 5.38e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533068  86 DTAFGMQVYSAIQKIPKGETRSYSDIAREIGNPSAVRAVASACARNNLAYIVPCHRVIGSTGNLSGYRWGIAKKRRLLQA 165
Cdd:COG2169  269 GTAFQQRVWQALRAIPAGETASYAEIAARIGAPKAVRAVAAACAANQLAVAIPCHRVVRADGALSGYRWGVERKRALLER 348

                 ....*.
gi 115533068 166 EGAELR 171
Cdd:COG2169  349 EAAAAA 354
PRK10286 PRK10286
methylated-DNA--[protein]-cysteine S-methyltransferase;
42-167 3.44e-20

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


Pssm-ID: 182355 [Multi-domain]  Cd Length: 171  Bit Score: 82.22  E-value: 3.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533068  42 QMEELHDA-YPTVNFIPGKPTQSSGIVQALNTLD----STIKVNAVHKGDTAFGMQVYSAIQKIPKGETRSYSDIAREIG 116
Cdd:PRK10286  37 RMVQLLDIhYRKEGYERISATNPGGLSDKLRDYFagnlSIIDTLPTATGGTPFQREVWQTLRTIPCGQVMHYGQLAEQLG 116
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 115533068 117 NPSAVRAVASACARNNLAYIVPCHRVIGSTGNLSGYRWGIAKKRRLLQAEG 167
Cdd:PRK10286 117 RPGAARAVGAANGSNPISIVVPCHRVIGRNGTMTGYAGGVQRKEWLLRHEG 167
Atl1 COG3695
Alkylated DNA nucleotide flippase Atl1, participates in nucleotide excision repair, Ada-like ...
86-171 8.73e-18

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


Pssm-ID: 442910  Cd Length: 104  Bit Score: 74.07  E-value: 8.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533068  86 DTAFGMQVYSAIQKIPKGETRSYSDIAREIGNPSAVRAVASACARNNLAYIVPCHRVIGSTGNLS-GYRWGIAKKRRLLQ 164
Cdd:COG3695    3 MEEFYERVYEVVAQIPPGRVATYGDIAALAGLPRGARQVGRALRALPEGSDLPWHRVVNADGRLSpGHAGGAEEQRELLE 82

                 ....*..
gi 115533068 165 AEGAELR 171
Cdd:COG3695   83 AEGVPVV 89
PRK03887 PRK03887
methylated-DNA--protein-cysteine methyltransferase; Provisional
85-169 3.22e-10

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 167628 [Multi-domain]  Cd Length: 175  Bit Score: 55.90  E-value: 3.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533068  85 GDTAFGMQVYSAIQK-IPKGETRSYSDIAREIGnpSAVRAVASACARNNLAYIVPCHRVIGSTgNLSGYRWGIAKKRRLL 163
Cdd:PRK03887  89 GLTPFERKVYEWLTKnVKRGEVITYGELAKALN--TSPRAVGGAMKRNPYPIIVPCHRVVGRK-NPGLYTPKPEYKKFLL 165

                 ....*.
gi 115533068 164 QAEGAE 169
Cdd:PRK03887 166 EVEGVK 171
 
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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