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Conserved domains on  [gi|446299469|ref|WP_000377324|]
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MULTISPECIES: MGMT family protein [Acinetobacter]

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

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 ...
10-109 4.48e-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: 143.79  E-value: 4.48e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446299469  10 ELHRQILEVIALIPYGKVATYGQVARMAGLPKHARLVGYVLKHLEADHQVPWHRVINSQGKISLSKfnEKGENIQQLKLE 89
Cdd:COG3695    5 EFYERVYEVVAQIPPGRVATYGDIAALAGLPRGARQVGRALRALPEGSDLPWHRVVNADGRLSPGH--AGGAEEQRELLE 82
                         90       100
                 ....*....|....*....|.
gi 446299469  90 TEGIYLL-NGKVNLKQFAWQP 109
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 ...
10-109 4.48e-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: 143.79  E-value: 4.48e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446299469  10 ELHRQILEVIALIPYGKVATYGQVARMAGLPKHARLVGYVLKHLEADHQVPWHRVINSQGKISLSKfnEKGENIQQLKLE 89
Cdd:COG3695    5 EFYERVYEVVAQIPPGRVATYGDIAALAGLPRGARQVGRALRALPEGSDLPWHRVVNADGRLSPGH--AGGAEEQRELLE 82
                         90       100
                 ....*....|....*....|.
gi 446299469  90 TEGIYLL-NGKVNLKQFAWQP 109
Cdd:COG3695   83 AEGVPVVdDGRVDLKRYRWDP 103
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
10-93 5.97e-30

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: 102.05  E-value: 5.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446299469   10 ELHRQILEVIALIPYGKVATYGQVARMAGLPKHARLVGYVLKHLEADHQVPWHRVINSQGKISLSKFnekGENIQQLKLE 89
Cdd:pfam01035   1 PFQRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSLGGYAG---GLERKRALLE 77

                  ....
gi 446299469   90 TEGI 93
Cdd:pfam01035  78 LEGV 81
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
11-92 2.22e-28

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: 97.94  E-value: 2.22e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446299469  11 LHRQILEVIALIPYGKVATYGQVARMAGLPKHARLVGYVLKHLEADHQVPWHRVINSQGKisLSKFNEkGENIQQLKLET 90
Cdd:cd06445    1 FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGG--LGGYRG-GLERKRELLEL 77

                 ..
gi 446299469  91 EG 92
Cdd:cd06445   78 EG 79
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
22-72 6.57e-09

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: 48.46  E-value: 6.57e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446299469   22 IPYGKVATYGQVARMAGLPKHARLVGYVLKHLEADHQVPWHRVINSQGKIS 72
Cdd:TIGR00589  14 IPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLT 64
PRK00901 PRK00901
methylated-DNA--protein-cysteine methyltransferase; Provisional
22-71 8.17e-07

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 234860 [Multi-domain]  Cd Length: 155  Bit Score: 44.66  E-value: 8.17e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446299469  22 IPYGKVATYGQVARMAGLPKHARLVGYvlkhleADHQ------VPWHRVINSQGKI 71
Cdd:PRK00901  85 IPYGETRSYKEIAVNIGNPKACRAVGL------ANNKnpipifIPCHRVIGANGKL 134
 
Name Accession Description Interval E-value
Atl1 COG3695
Alkylated DNA nucleotide flippase Atl1, participates in nucleotide excision repair, Ada-like ...
10-109 4.48e-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: 143.79  E-value: 4.48e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446299469  10 ELHRQILEVIALIPYGKVATYGQVARMAGLPKHARLVGYVLKHLEADHQVPWHRVINSQGKISLSKfnEKGENIQQLKLE 89
Cdd:COG3695    5 EFYERVYEVVAQIPPGRVATYGDIAALAGLPRGARQVGRALRALPEGSDLPWHRVVNADGRLSPGH--AGGAEEQRELLE 82
                         90       100
                 ....*....|....*....|.
gi 446299469  90 TEGIYLL-NGKVNLKQFAWQP 109
Cdd:COG3695   83 AEGVPVVdDGRVDLKRYRWDP 103
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
10-93 5.97e-30

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: 102.05  E-value: 5.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446299469   10 ELHRQILEVIALIPYGKVATYGQVARMAGLPKHARLVGYVLKHLEADHQVPWHRVINSQGKISLSKFnekGENIQQLKLE 89
Cdd:pfam01035   1 PFQRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSLGGYAG---GLERKRALLE 77

                  ....
gi 446299469   90 TEGI 93
Cdd:pfam01035  78 LEGV 81
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
11-92 2.22e-28

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: 97.94  E-value: 2.22e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446299469  11 LHRQILEVIALIPYGKVATYGQVARMAGLPKHARLVGYVLKHLEADHQVPWHRVINSQGKisLSKFNEkGENIQQLKLET 90
Cdd:cd06445    1 FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGG--LGGYRG-GLERKRELLEL 77

                 ..
gi 446299469  91 EG 92
Cdd:cd06445   78 EG 79
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
10-71 8.09e-13

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


Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 60.66  E-value: 8.09e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446299469  10 ELHRQILEVIALIPYGKVATYGQVARMAGLPKHARLVGYVLKH-----LeadhqVPWHRVINSQGKI 71
Cdd:COG0350   79 PFQRRVWEALRKIPYGETVTYGELARAIGRPKAARAVGSACGAnpipiI-----IPCHRVIGADGSL 140
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
22-72 6.57e-09

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: 48.46  E-value: 6.57e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446299469   22 IPYGKVATYGQVARMAGLPKHARLVGYVLKHLEADHQVPWHRVINSQGKIS 72
Cdd:TIGR00589  14 IPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLT 64
PRK00901 PRK00901
methylated-DNA--protein-cysteine methyltransferase; Provisional
22-71 8.17e-07

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 234860 [Multi-domain]  Cd Length: 155  Bit Score: 44.66  E-value: 8.17e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446299469  22 IPYGKVATYGQVARMAGLPKHARLVGYvlkhleADHQ------VPWHRVINSQGKI 71
Cdd:PRK00901  85 IPYGETRSYKEIAVNIGNPKACRAVGL------ANNKnpipifIPCHRVIGANGKL 134
PRK10286 PRK10286
methylated-DNA--[protein]-cysteine S-methyltransferase;
11-72 3.76e-05

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


Pssm-ID: 182355 [Multi-domain]  Cd Length: 171  Bit Score: 40.24  E-value: 3.76e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446299469  11 LHRQILEVIALIPYGKVATYGQVARMAGLPKHARLVGYVLKHLEADHQVPWHRVINSQGKIS 72
Cdd:PRK10286  89 FQREVWQTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIGRNGTMT 150
MutS COG0249
DNA mismatch repair ATPase MutS [Replication, recombination and repair];
30-93 1.78e-03

DNA mismatch repair ATPase MutS [Replication, recombination and repair];


Pssm-ID: 440019 [Multi-domain]  Cd Length: 861  Bit Score: 36.19  E-value: 1.78e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446299469  30 YG-QVARMAGLPK----HARlvgYVLKHLEADHQVPWHRVINSQgkisLSKFNEKGENIQQLKLETEGI 93
Cdd:COG0249  777 YGiHVAKLAGLPAsvieRAR---EILAELEKGEAAAAGKAAPDQ----LSLFAAADPEPSPVLEELKAL 838
 
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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