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Conserved domains on  [gi|1850727247|ref|WP_173380738|]
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MULTISPECIES: methylated-DNA--[protein]-cysteine S-methyltransferase [unclassified Fibrobacter]

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

CATH:  3.30.160.70|1.10.10.10
EC:  2.1.1.63
Gene Ontology:  GO:0003908|GO:0003677|GO:0046872|GO:0006281|GO:0032259
PubMed:  17500045|17485252
SCOP:  4000565|4000678

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, ...
 17-177 8.00e-55

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


:

Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 171.21  E-value: 8.00e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850727247  17 WGEWTFTFEGNTLCGLRFSGSGESSIVPSSVKACAYATADTDiplkrstakaynNVVKELNQYLAGKITEFTVPIAIHGT 96
Cdd:COG0350    11 LGPLLIAATDRGLCALSFGDDREEALLARFPAALREDPPLLA------------EAARQLDAYFAGERKDFDLPLDLRGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850727247  97 EFQVSVLEATRKIPYGKTWTYKQVAEAIGHPNAERAVGNTLHNNPLQVIIPCHRVVTSKGKIGGYALGTDLKRRLLCMEG 176
Cdd:COG0350    79 PFQRRVWEALRKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSLGGYAGGLERKRALLELEG 158


                  .
gi 1850727247 177 A 177
Cdd:COG0350   159 A 159
 
Name Accession Description Interval E-value
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
 17-177 8.00e-55

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


Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 171.21  E-value: 8.00e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850727247  17 WGEWTFTFEGNTLCGLRFSGSGESSIVPSSVKACAYATADTDiplkrstakaynNVVKELNQYLAGKITEFTVPIAIHGT 96
Cdd:COG0350    11 LGPLLIAATDRGLCALSFGDDREEALLARFPAALREDPPLLA------------EAARQLDAYFAGERKDFDLPLDLRGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850727247  97 EFQVSVLEATRKIPYGKTWTYKQVAEAIGHPNAERAVGNTLHNNPLQVIIPCHRVVTSKGKIGGYALGTDLKRRLLCMEG 176
Cdd:COG0350    79 PFQRRVWEALRKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSLGGYAGGLERKRALLELEG 158


                  .
gi 1850727247 177 A 177
Cdd:COG0350   159 A 159
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
 97-177 2.80e-40

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: 131.33  E-value: 2.80e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850727247  97 EFQVSVLEATRKIPYGKTWTYKQVAEAIGHPNAERAVGNTLHNNPLQVIIPCHRVVTSKGKIGGYALGTDLKRRLLCMEG 176
Cdd:pfam01035   1 PFQRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSLGGYAGGLERKRALLELEG 80


                  .
gi 1850727247 177 A 177
Cdd:pfam01035  81 V 81
PRK00901 PRK00901
methylated-DNA--protein-cysteine methyltransferase; Provisional
 74-176 2.31e-38

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 234860 [Multi-domain]  Cd Length: 155  Bit Score: 129.02  E-value: 2.31e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850727247  74 KELNQYLAGKITEFTVPIAIHGTEFQVSVLEATRKIPYGKTWTYKQVAEAIGHPNAERAVGNTLHNNPLQVIIPCHRVVT 153
Cdd:PRK00901   50 KQLEEYFEGKRKKFDLPLAPQGTEFQKKVWKALQEIPYGETRSYKEIAVNIGNPKACRAVGLANNKNPIPIFIPCHRVIG 129

                          90       100
                  ....*....|....*....|...
gi 1850727247 154 SKGKIGGYALGTDLKRRLLCMEG 176
Cdd:PRK00901  130 ANGKLVGYAGGLDIKEKLLKLEK 152
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
 98-176 2.76e-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: 2.76e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1850727247  98 FQVSVLEATRKIPYGKTWTYKQVAEAIGHPNAERAVGNTLHNNPLQVIIPCHRVVTSKGKIGGYALGTDLKRRLLCMEG 176
Cdd:cd06445     1 FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGLGGYRGGLERKRELLELEG 79
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
 96-175 3.63e-30

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: 105.47  E-value: 3.63e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850727247  96 TEFQVSVLEATRKIPYGKTWTYKQVAEAIGHPNAERAVGNTLHNNPLQVIIPCHRVVTSKGKIGGYALGTDLKRRLLCME 175
Cdd:TIGR00589   1 TPFQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLTGYGGGLERKEFLLEHE 80
 
Name Accession Description Interval E-value
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
 17-177 8.00e-55

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


Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 171.21  E-value: 8.00e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850727247  17 WGEWTFTFEGNTLCGLRFSGSGESSIVPSSVKACAYATADTDiplkrstakaynNVVKELNQYLAGKITEFTVPIAIHGT 96
Cdd:COG0350    11 LGPLLIAATDRGLCALSFGDDREEALLARFPAALREDPPLLA------------EAARQLDAYFAGERKDFDLPLDLRGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850727247  97 EFQVSVLEATRKIPYGKTWTYKQVAEAIGHPNAERAVGNTLHNNPLQVIIPCHRVVTSKGKIGGYALGTDLKRRLLCMEG 176
Cdd:COG0350    79 PFQRRVWEALRKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSLGGYAGGLERKRALLELEG 158


                  .
gi 1850727247 177 A 177
Cdd:COG0350   159 A 159
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
 97-177 2.80e-40

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: 131.33  E-value: 2.80e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850727247  97 EFQVSVLEATRKIPYGKTWTYKQVAEAIGHPNAERAVGNTLHNNPLQVIIPCHRVVTSKGKIGGYALGTDLKRRLLCMEG 176
Cdd:pfam01035   1 PFQRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSLGGYAGGLERKRALLELEG 80


                  .
gi 1850727247 177 A 177
Cdd:pfam01035  81 V 81
PRK00901 PRK00901
methylated-DNA--protein-cysteine methyltransferase; Provisional
 74-176 2.31e-38

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 234860 [Multi-domain]  Cd Length: 155  Bit Score: 129.02  E-value: 2.31e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850727247  74 KELNQYLAGKITEFTVPIAIHGTEFQVSVLEATRKIPYGKTWTYKQVAEAIGHPNAERAVGNTLHNNPLQVIIPCHRVVT 153
Cdd:PRK00901   50 KQLEEYFEGKRKKFDLPLAPQGTEFQKKVWKALQEIPYGETRSYKEIAVNIGNPKACRAVGLANNKNPIPIFIPCHRVIG 129

                          90       100
                  ....*....|....*....|...
gi 1850727247 154 SKGKIGGYALGTDLKRRLLCMEG 176
Cdd:PRK00901  130 ANGKLVGYAGGLDIKEKLLKLEK 152
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
 98-176 2.76e-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: 2.76e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1850727247  98 FQVSVLEATRKIPYGKTWTYKQVAEAIGHPNAERAVGNTLHNNPLQVIIPCHRVVTSKGKIGGYALGTDLKRRLLCMEG 176
Cdd:cd06445     1 FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGLGGYRGGLERKRELLELEG 79
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
 96-175 3.63e-30

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: 105.47  E-value: 3.63e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850727247  96 TEFQVSVLEATRKIPYGKTWTYKQVAEAIGHPNAERAVGNTLHNNPLQVIIPCHRVVTSKGKIGGYALGTDLKRRLLCME 175
Cdd:TIGR00589   1 TPFQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLTGYGGGLERKEFLLEHE 80
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
73-179 1.43e-25

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


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 100.64  E-value: 1.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850727247  73 VKELNQYLAGKITEFTVPIAIHGTEFQVSVLEATRKIPYGKTWTYKQVAEAIGHPNAERAVGNTLHNNPLQVIIPCHRVV 152
Cdd:PRK15435  246 VREVIASLNQRDTPLTLPLDIRGTAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIVIPCHRVV 325

                          90       100
                  ....*....|....*....|....*..
gi 1850727247 153 TSKGKIGGYALGTDLKRRLLCMEGAIQ 179
Cdd:PRK15435  326 RGDGALSGYRWGVSRKAQLLRREAENE 352
PRK10286 PRK10286
methylated-DNA--[protein]-cysteine S-methyltransferase;
62-176 5.13e-23

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


Pssm-ID: 182355 [Multi-domain]  Cd Length: 171  Bit Score: 89.93  E-value: 5.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850727247  62 KRSTAKAYNNVVKELNQYLAGKITEF-TVPIAIHGTEFQVSVLEATRKIPYGKTWTYKQVAEAIGHPNAERAVGNTLHNN 140
Cdd:PRK10286   52 ERISATNPGGLSDKLRDYFAGNLSIIdTLPTATGGTPFQREVWQTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSN 131

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1850727247 141 PLQVIIPCHRVVTSKGKIGGYALGTDLKRRLLCMEG 176
Cdd:PRK10286  132 PISIVVPCHRVIGRNGTMTGYAGGVQRKEWLLRHEG 167
Atl1 COG3695
Alkylated DNA nucleotide flippase Atl1, participates in nucleotide excision repair, Ada-like ...
 96-176 4.04e-20

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


Pssm-ID: 442910  Cd Length: 104  Bit Score: 80.61  E-value: 4.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850727247  96 TEFQVSVLEATRKIPYGKTWTYKQVAEAIGHPNAERAVGNTLHNNPLQVIIPCHRVVTSKGKI-GGYALGTDLKRRLLCM 174
Cdd:COG3695     4 EEFYERVYEVVAQIPPGRVATYGDIAALAGLPRGARQVGRALRALPEGSDLPWHRVVNADGRLsPGHAGGAEEQRELLEA 83


                  ..
gi 1850727247 175 EG 176
Cdd:COG3695    84 EG 85
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 72-172 7.88e-19

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: 82.41  E-value: 7.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850727247  72 VVKELNQYLAGKITEFTVPIAIHGTEFQVSVLEATRKIPYGKTWTYKQVAEAIGHPNAERAVGNTLHNNPLQVIIPCHRV 151
Cdd:COG2169   246 LVAEVVGFVEGPLLGLDLPLDLRGTAFQQRVWQALRAIPAGETASYAEIAARIGAPKAVRAVAAACAANQLAVAIPCHRV 325

                          90       100
                  ....*....|....*....|.
gi 1850727247 152 VTSKGKIGGYALGTDLKRRLL 172
Cdd:COG2169   326 VRADGALSGYRWGVERKRALL 346
PRK03887 PRK03887
methylated-DNA--protein-cysteine methyltransferase; Provisional
 96-176 1.99e-10

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 167628 [Multi-domain]  Cd Length: 175  Bit Score: 56.67  E-value: 1.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850727247  96 TEFQVSVLE-ATRKIPYGKTWTYKQVAEAIGhpNAERAVGNTLHNNPLQVIIPCHRVVTSKGkIGGYALGTDLKRRLLCM 174
Cdd:PRK03887   91 TPFERKVYEwLTKNVKRGEVITYGELAKALN--TSPRAVGGAMKRNPYPIIVPCHRVVGRKN-PGLYTPKPEYKKFLLEV 167


                  ..
gi 1850727247 175 EG 176
Cdd:PRK03887  168 EG 169
 
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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