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Conserved domains on  [gi|705454223|ref|WP_033520416|]
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MGMT family protein [Bifidobacterium bohemicum]

Protein Classification

MGMT family protein( domain architecture ID 10790320)

MGMT (O-6-methylguanine DNA methyltransferase) family protein similar to MGMT, also called methylated-DNA--[protein]-cysteine S-methyltransferase, that repairs alkylated guanine in DNA by stoichiometrically transferring the alkyl group at the O-6 position to a cysteine residue in the enzyme, resulting in its irreversible inactivation

CATH:  1.10.10.10
EC:  2.1.1.63
Gene Ontology:  GO:0006281|GO:0003824|GO:0003908|GO:0003677

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Atl1 COG3695
Alkylated DNA nucleotide flippase Atl1, participates in nucleotide excision repair, Ada-like ...
 1-113 9.22e-44

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


:

Pssm-ID: 442910  Cd Length: 104  Bit Score: 138.01  E-value: 9.22e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705454223   1 MVESFNAAVYQVVQRIPAGKVATYGQVAALAGNPHSARFVGYALHSNPSPGVIPCHRVVFRDGSLAPGFAFgGPDRQRGL 80
Cdd:COG3695    2 EMEEFYERVYEVVAQIPPGRVATYGDIAALAGLPRGARQVGRALRALPEGSDLPWHRVVNADGRLSPGHAG-GAEEQREL 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 705454223  81 LEEEGVLFippvsghrnagDPGWCVDMEHCQWQ 113
Cdd:COG3695   81 LEAEGVPV-----------VDDGRVDLKRYRWD 102
 
Name Accession Description Interval E-value
Atl1 COG3695
Alkylated DNA nucleotide flippase Atl1, participates in nucleotide excision repair, Ada-like ...
 1-113 9.22e-44

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


Pssm-ID: 442910  Cd Length: 104  Bit Score: 138.01  E-value: 9.22e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705454223   1 MVESFNAAVYQVVQRIPAGKVATYGQVAALAGNPHSARFVGYALHSNPSPGVIPCHRVVFRDGSLAPGFAFgGPDRQRGL 80
Cdd:COG3695    2 EMEEFYERVYEVVAQIPPGRVATYGDIAALAGLPRGARQVGRALRALPEGSDLPWHRVVNADGRLSPGHAG-GAEEQREL 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 705454223  81 LEEEGVLFippvsghrnagDPGWCVDMEHCQWQ 113
Cdd:COG3695   81 LEAEGVPV-----------VDDGRVDLKRYRWD 102
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
 4-86 2.09e-37

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: 121.31  E-value: 2.09e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705454223    4 SFNAAVYQVVQRIPAGKVATYGQVAALAGNPHSARFVGYALHSNPSPGVIPCHRVVFRDGSLapGFAFGGPDRQRGLLEE 83
Cdd:pfam01035   1 PFQRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSL--GGYAGGLERKRALLEL 78


                  ...
gi 705454223   84 EGV 86
Cdd:pfam01035  79 EGV 81
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
 5-85 2.98e-34

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: 113.35  E-value: 2.98e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705454223   5 FNAAVYQVVQRIPAGKVATYGQVAALAGNPHSARFVGYALHSNPSPGVIPCHRVVFRDGSLaPGFAfGGPDRQRGLLEEE 84
Cdd:cd06445    1 FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGL-GGYR-GGLERKRELLELE 78


                 .
gi 705454223  85 G 85
Cdd:cd06445   79 G 79
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
 5-84 4.16e-22

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: 82.36  E-value: 4.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705454223    5 FNAAVYQVVQRIPAGKVATYGQVAALAGNPHSARFVGYALHSNPSPGVIPCHRVVFRDGSLApGFAfGGPDRQRGLLEEE 84
Cdd:TIGR00589   3 FQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLT-GYG-GGLERKEFLLEHE 80
PRK10286 PRK10286
methylated-DNA--[protein]-cysteine S-methyltransferase;
5-89 3.15e-18

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


Pssm-ID: 182355 [Multi-domain]  Cd Length: 171  Bit Score: 75.29  E-value: 3.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705454223   5 FNAAVYQVVQRIPAGKVATYGQVAALAGNPHSARFVGYALHSNPSPGVIPCHRVVFRDGSLApGFAfGGPDRQRGLLEEE 84
Cdd:PRK10286  89 FQREVWQTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIGRNGTMT-GYA-GGVQRKEWLLRHE 166


                 ....*
gi 705454223  85 GVLFI 89
Cdd:PRK10286 167 GYLLL 171
 
Name Accession Description Interval E-value
Atl1 COG3695
Alkylated DNA nucleotide flippase Atl1, participates in nucleotide excision repair, Ada-like ...
 1-113 9.22e-44

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


Pssm-ID: 442910  Cd Length: 104  Bit Score: 138.01  E-value: 9.22e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705454223   1 MVESFNAAVYQVVQRIPAGKVATYGQVAALAGNPHSARFVGYALHSNPSPGVIPCHRVVFRDGSLAPGFAFgGPDRQRGL 80
Cdd:COG3695    2 EMEEFYERVYEVVAQIPPGRVATYGDIAALAGLPRGARQVGRALRALPEGSDLPWHRVVNADGRLSPGHAG-GAEEQREL 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 705454223  81 LEEEGVLFippvsghrnagDPGWCVDMEHCQWQ 113
Cdd:COG3695   81 LEAEGVPV-----------VDDGRVDLKRYRWD 102
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
 4-86 2.09e-37

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: 121.31  E-value: 2.09e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705454223    4 SFNAAVYQVVQRIPAGKVATYGQVAALAGNPHSARFVGYALHSNPSPGVIPCHRVVFRDGSLapGFAFGGPDRQRGLLEE 83
Cdd:pfam01035   1 PFQRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSL--GGYAGGLERKRALLEL 78


                  ...
gi 705454223   84 EGV 86
Cdd:pfam01035  79 EGV 81
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
 5-85 2.98e-34

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: 113.35  E-value: 2.98e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705454223   5 FNAAVYQVVQRIPAGKVATYGQVAALAGNPHSARFVGYALHSNPSPGVIPCHRVVFRDGSLaPGFAfGGPDRQRGLLEEE 84
Cdd:cd06445    1 FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGL-GGYR-GGLERKRELLELE 78


                 .
gi 705454223  85 G 85
Cdd:cd06445   79 G 79
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
 5-88 2.09e-28

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


Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 101.10  E-value: 2.09e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705454223   5 FNAAVYQVVQRIPAGKVATYGQVAALAGNPHSARFVGYALHSNPSPGVIPCHRVVFRDGSLApGFAfGGPDRQRGLLEEE 84
Cdd:COG0350   80 FQRRVWEALRKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSLG-GYA-GGLERKRALLELE 157


                 ....
gi 705454223  85 GVLF 88
Cdd:COG0350  158 GALA 161
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
 5-84 4.16e-22

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: 82.36  E-value: 4.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705454223    5 FNAAVYQVVQRIPAGKVATYGQVAALAGNPHSARFVGYALHSNPSPGVIPCHRVVFRDGSLApGFAfGGPDRQRGLLEEE 84
Cdd:TIGR00589   3 FQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLT-GYG-GGLERKEFLLEHE 80
PRK10286 PRK10286
methylated-DNA--[protein]-cysteine S-methyltransferase;
5-89 3.15e-18

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


Pssm-ID: 182355 [Multi-domain]  Cd Length: 171  Bit Score: 75.29  E-value: 3.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705454223   5 FNAAVYQVVQRIPAGKVATYGQVAALAGNPHSARFVGYALHSNPSPGVIPCHRVVFRDGSLApGFAfGGPDRQRGLLEEE 84
Cdd:PRK10286  89 FQREVWQTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIGRNGTMT-GYA-GGVQRKEWLLRHE 166


                 ....*
gi 705454223  85 GVLFI 89
Cdd:PRK10286 167 GYLLL 171
PRK00901 PRK00901
methylated-DNA--protein-cysteine methyltransferase; Provisional
 5-85 9.58e-18

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 234860 [Multi-domain]  Cd Length: 155  Bit Score: 73.55  E-value: 9.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705454223   5 FNAAVYQVVQRIPAGKVATYGQVAALAGNPHSARFVGYALHSNPSPGVIPCHRVVFRDGSLApGFAfGGPDRQRGLLEEE 84
Cdd:PRK00901  74 FQKKVWKALQEIPYGETRSYKEIAVNIGNPKACRAVGLANNKNPIPIFIPCHRVIGANGKLV-GYA-GGLDIKEKLLKLE 151


                 .
gi 705454223  85 G 85
Cdd:PRK00901 152 K 152
PRK03887 PRK03887
methylated-DNA--protein-cysteine methyltransferase; Provisional
 2-86 2.10e-14

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 167628 [Multi-domain]  Cd Length: 175  Bit Score: 65.14  E-value: 2.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705454223   2 VESFNAAVYQ-VVQRIPAGKVATYGQVAALAGNphSARFVGYALHSNPSPGVIPCHRVVFRDGslaPGFAFGGPDRQRGL 80
Cdd:PRK03887  90 LTPFERKVYEwLTKNVKRGEVITYGELAKALNT--SPRAVGGAMKRNPYPIIVPCHRVVGRKN---PGLYTPKPEYKKFL 164


                 ....*.
gi 705454223  81 LEEEGV 86
Cdd:PRK03887 165 LEVEGV 170
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
4-84 2.71e-14

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


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 67.13  E-value: 2.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705454223   4 SFNAAVYQVVQRIPAGKVATYGQVAALAGNPHSARFVGYALHSNPSPGVIPCHRVVFRDGSLApGFAFgGPDRQRGLLEE 83
Cdd:PRK15435 270 AFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIVIPCHRVVRGDGALS-GYRW-GVSRKAQLLRR 347


                 .
gi 705454223  84 E 84
Cdd:PRK15435 348 E 348
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 5-84 1.40e-09

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: 53.90  E-value: 1.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705454223   5 FNAAVYQVVQRIPAGKVATYGQVAALAGNPHSARFVGYALHSNPSPGVIPCHRVVFRDGSLAPGfaFGGPDRQRGLLEEE 84
Cdd:COG2169  272 FQQRVWQALRAIPAGETASYAEIAARIGAPKAVRAVAAACAANQLAVAIPCHRVVRADGALSGY--RWGVERKRALLERE 349
 
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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