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Conserved domains on  [gi|503622368|ref|WP_013856444|]
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MULTISPECIES: MGMT family protein [Vibrio]

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 ...
 1-100 1.50e-46

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


:

Pssm-ID: 442910  Cd Length: 104  Bit Score: 144.56  E-value: 1.50e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503622368   1 MNQFLAQIFAVIHQIPAGKVTTYGEIARLAGYPGYARHVGKALGNLPQNSRLPWFRVINSKGEISLK-GEDLLRQRQKLI 79
Cdd:COG3695    3 MEEFYERVYEVVAQIPPGRVATYGDIAALAGLPRGARQVGRALRALPEGSDLPWHRVVNADGRLSPGhAGGAEEQRELLE 82

                         90       100
                 ....*....|....*....|.
gi 503622368  80 AEGVEVNEHGKIKLRLYQWRP 100
Cdd:COG3695   83 AEGVPVVDDGRVDLKRYRWDP 103
 
Name Accession Description Interval E-value
Atl1 COG3695
Alkylated DNA nucleotide flippase Atl1, participates in nucleotide excision repair, Ada-like ...
 1-100 1.50e-46

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


Pssm-ID: 442910  Cd Length: 104  Bit Score: 144.56  E-value: 1.50e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503622368   1 MNQFLAQIFAVIHQIPAGKVTTYGEIARLAGYPGYARHVGKALGNLPQNSRLPWFRVINSKGEISLK-GEDLLRQRQKLI 79
Cdd:COG3695    3 MEEFYERVYEVVAQIPPGRVATYGDIAALAGLPRGARQVGRALRALPEGSDLPWHRVVNADGRLSPGhAGGAEEQRELLE 82

                         90       100
                 ....*....|....*....|.
gi 503622368  80 AEGVEVNEHGKIKLRLYQWRP 100
Cdd:COG3695   83 AEGVPVVDDGRVDLKRYRWDP 103
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
 4-83 1.77e-27

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: 95.50  E-value: 1.77e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503622368    4 FLAQIFAVIHQIPAGKVTTYGEIARLAGYPGYARHVGKALGNLPQNSRLPWFRVINSKGEISLKGEDLLRQRQKLIAEGV 83
Cdd:pfam01035   2 FQRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSLGGYAGGLERKRALLELEGV 81
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
 4-82 1.49e-24

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: 87.92  E-value: 1.49e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503622368   4 FLAQIFAVIHQIPAGKVTTYGEIARLAGYPGYARHVGKALGNLPQNSRLPWFRVINSKGEISLKGEDLLRQRQKLIAEG 82
Cdd:cd06445    1 FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGLGGYRGGLERKRELLELEG 79
PRK10286 PRK10286
methylated-DNA--[protein]-cysteine S-methyltransferase;
4-82 2.92e-07

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


Pssm-ID: 182355 [Multi-domain]  Cd Length: 171  Bit Score: 45.63  E-value: 2.92e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503622368   4 FLAQIFAVIHQIPAGKVTTYGEIARLAGYPGYARHVGKALGNLPQNSRLPWFRVINSKGEISLKGEDLLRQRQKLIAEG 82
Cdd:PRK10286  89 FQREVWQTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIGRNGTMTGYAGGVQRKEWLLRHEG 167
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
 3-65 7.28e-07

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: 43.07  E-value: 7.28e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503622368    3 QFLAQIFAVIHQIPAGKVTTYGEIARLAGYPGYARHVGKALGNLPQNSRLPWFRVINSKGEIS 65
Cdd:TIGR00589   2 PFQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLT 64
 
Name Accession Description Interval E-value
Atl1 COG3695
Alkylated DNA nucleotide flippase Atl1, participates in nucleotide excision repair, Ada-like ...
 1-100 1.50e-46

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


Pssm-ID: 442910  Cd Length: 104  Bit Score: 144.56  E-value: 1.50e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503622368   1 MNQFLAQIFAVIHQIPAGKVTTYGEIARLAGYPGYARHVGKALGNLPQNSRLPWFRVINSKGEISLK-GEDLLRQRQKLI 79
Cdd:COG3695    3 MEEFYERVYEVVAQIPPGRVATYGDIAALAGLPRGARQVGRALRALPEGSDLPWHRVVNADGRLSPGhAGGAEEQRELLE 82

                         90       100
                 ....*....|....*....|.
gi 503622368  80 AEGVEVNEHGKIKLRLYQWRP 100
Cdd:COG3695   83 AEGVPVVDDGRVDLKRYRWDP 103
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
 4-83 1.77e-27

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: 95.50  E-value: 1.77e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503622368    4 FLAQIFAVIHQIPAGKVTTYGEIARLAGYPGYARHVGKALGNLPQNSRLPWFRVINSKGEISLKGEDLLRQRQKLIAEGV 83
Cdd:pfam01035   2 FQRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSLGGYAGGLERKRALLELEGV 81
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
 4-82 1.49e-24

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: 87.92  E-value: 1.49e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503622368   4 FLAQIFAVIHQIPAGKVTTYGEIARLAGYPGYARHVGKALGNLPQNSRLPWFRVINSKGEISLKGEDLLRQRQKLIAEG 82
Cdd:cd06445    1 FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGLGGYRGGLERKRELLELEG 79
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
 4-64 1.53e-10

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


Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 54.49  E-value: 1.53e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503622368   4 FLAQIFAVIHQIPAGKVTTYGEIARLAGYPGYARHVGKALGNLPqnsrLPWF----RVINSKGEI 64
Cdd:COG0350   80 FQRRVWEALRKIPYGETVTYGELARAIGRPKAARAVGSACGANP----IPIIipchRVIGADGSL 140
PRK10286 PRK10286
methylated-DNA--[protein]-cysteine S-methyltransferase;
4-82 2.92e-07

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


Pssm-ID: 182355 [Multi-domain]  Cd Length: 171  Bit Score: 45.63  E-value: 2.92e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503622368   4 FLAQIFAVIHQIPAGKVTTYGEIARLAGYPGYARHVGKALGNLPQNSRLPWFRVINSKGEISLKGEDLLRQRQKLIAEG 82
Cdd:PRK10286  89 FQREVWQTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIGRNGTMTGYAGGVQRKEWLLRHEG 167
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
 3-65 7.28e-07

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: 43.07  E-value: 7.28e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503622368    3 QFLAQIFAVIHQIPAGKVTTYGEIARLAGYPGYARHVGKALGNLPQNSRLPWFRVINSKGEIS 65
Cdd:TIGR00589   2 PFQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLT 64
PRK00901 PRK00901
methylated-DNA--protein-cysteine methyltransferase; Provisional
 3-62 3.11e-04

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 234860 [Multi-domain]  Cd Length: 155  Bit Score: 37.34  E-value: 3.11e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503622368   3 QFLAQIFAVIHQIPAGKVTTYGEIARLAGYPGYARHVGKALGNLPQNSRLPWFRVINSKG 62
Cdd:PRK00901  73 EFQKKVWKALQEIPYGETRSYKEIAVNIGNPKACRAVGLANNKNPIPIFIPCHRVIGANG 132
 
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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