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Conserved domains on  [gi|446867764|ref|WP_000945020|]
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MULTISPECIES: methylated-DNA--[protein]-cysteine S-methyltransferase [Enterobacteriaceae]

Protein Classification

methylated-DNA--[protein]-cysteine S-methyltransferase( domain architecture ID 11484647)

methylated-DNA--[protein]-cysteine S-methyltransferase 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
PRK10286 PRK10286
methylated-DNA--[protein]-cysteine S-methyltransferase;
1-171 1.10e-132

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


:

Pssm-ID: 182355 [Multi-domain]  Cd Length: 171  Bit Score: 367.66  E-value: 1.10e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867764   1 MLRLLEEKIATPLGPLWVICDEQFRLRAVEWEEYSERMVQLLDIHYRKESYERISATNPGGLSDKLREYFAGNLSIIDTL 80
Cdd:PRK10286   1 MLRLLEEKIATPLGPLWVICDEQFRLRAVEWEEYSERMVQLLDIHYRKEGYERISATNPGGLSDKLRDYFAGNLSIIDTL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867764  81 PTATGGTQFQREVWKTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIGRNGTMTGYAGGVQRKE 160
Cdd:PRK10286  81 PTATGGTPFQREVWQTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIGRNGTMTGYAGGVQRKE 160

                        170
                 ....*....|.
gi 446867764 161 WLLRHEGYLLL 171
Cdd:PRK10286 161 WLLRHEGYLLL 171
 
Name Accession Description Interval E-value
PRK10286 PRK10286
methylated-DNA--[protein]-cysteine S-methyltransferase;
1-171 1.10e-132

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


Pssm-ID: 182355 [Multi-domain]  Cd Length: 171  Bit Score: 367.66  E-value: 1.10e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867764   1 MLRLLEEKIATPLGPLWVICDEQFRLRAVEWEEYSERMVQLLDIHYRKESYERISATNPGGLSDKLREYFAGNLSIIDTL 80
Cdd:PRK10286   1 MLRLLEEKIATPLGPLWVICDEQFRLRAVEWEEYSERMVQLLDIHYRKEGYERISATNPGGLSDKLRDYFAGNLSIIDTL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867764  81 PTATGGTQFQREVWKTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIGRNGTMTGYAGGVQRKE 160
Cdd:PRK10286  81 PTATGGTPFQREVWQTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIGRNGTMTGYAGGVQRKE 160

                        170
                 ....*....|.
gi 446867764 161 WLLRHEGYLLL 171
Cdd:PRK10286 161 WLLRHEGYLLL 171
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
 9-167 1.05e-62

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


Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 190.47  E-value: 1.05e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867764   9 IATPLGPLWVICDEQfRLRAVEWEEYSERmvqLLDIHYRKESYERISATNPggLSDKLREYFAGNLSIIDtLPTATGGTQ 88
Cdd:COG0350    7 FDTPLGPLLIAATDR-GLCALSFGDDREE---ALLARFPAALREDPPLLAE--AARQLDAYFAGERKDFD-LPLDLRGTP 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446867764  89 FQREVWKTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIGRNGTMTGYAGGVQRKEWLLRHEG 167
Cdd:COG0350   80 FQRRVWEALRKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSLGGYAGGLERKRALLELEG 158
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
 87-166 1.53e-49

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: 154.39  E-value: 1.53e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867764   87 TQFQREVWKTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIGRNGTMTGYAGGVQRKEWLLRHE 166
Cdd:TIGR00589   1 TPFQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLTGYGGGLERKEFLLEHE 80
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
 89-167 3.05e-47

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: 148.28  E-value: 3.05e-47
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446867764   89 FQREVWKTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIGRNGTMTGYAGGVQRKEWLLRHEG 167
Cdd:pfam01035   2 FQRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSLGGYAGGLERKRALLELEG 80
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
 89-167 3.08e-42

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: 135.69  E-value: 3.08e-42
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446867764  89 FQREVWKTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIGRNGTMTGYAGGVQRKEWLLRHEG 167
Cdd:cd06445    1 FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGLGGYRGGLERKRELLELEG 79
 
Name Accession Description Interval E-value
PRK10286 PRK10286
methylated-DNA--[protein]-cysteine S-methyltransferase;
1-171 1.10e-132

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


Pssm-ID: 182355 [Multi-domain]  Cd Length: 171  Bit Score: 367.66  E-value: 1.10e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867764   1 MLRLLEEKIATPLGPLWVICDEQFRLRAVEWEEYSERMVQLLDIHYRKESYERISATNPGGLSDKLREYFAGNLSIIDTL 80
Cdd:PRK10286   1 MLRLLEEKIATPLGPLWVICDEQFRLRAVEWEEYSERMVQLLDIHYRKEGYERISATNPGGLSDKLRDYFAGNLSIIDTL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867764  81 PTATGGTQFQREVWKTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIGRNGTMTGYAGGVQRKE 160
Cdd:PRK10286  81 PTATGGTPFQREVWQTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIGRNGTMTGYAGGVQRKE 160

                        170
                 ....*....|.
gi 446867764 161 WLLRHEGYLLL 171
Cdd:PRK10286 161 WLLRHEGYLLL 171
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
 9-167 1.05e-62

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


Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 190.47  E-value: 1.05e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867764   9 IATPLGPLWVICDEQfRLRAVEWEEYSERmvqLLDIHYRKESYERISATNPggLSDKLREYFAGNLSIIDtLPTATGGTQ 88
Cdd:COG0350    7 FDTPLGPLLIAATDR-GLCALSFGDDREE---ALLARFPAALREDPPLLAE--AARQLDAYFAGERKDFD-LPLDLRGTP 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446867764  89 FQREVWKTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIGRNGTMTGYAGGVQRKEWLLRHEG 167
Cdd:COG0350   80 FQRRVWEALRKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSLGGYAGGLERKRALLELEG 158
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
 87-166 1.53e-49

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: 154.39  E-value: 1.53e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867764   87 TQFQREVWKTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIGRNGTMTGYAGGVQRKEWLLRHE 166
Cdd:TIGR00589   1 TPFQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLTGYGGGLERKEFLLEHE 80
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
 89-167 3.05e-47

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: 148.28  E-value: 3.05e-47
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446867764   89 FQREVWKTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIGRNGTMTGYAGGVQRKEWLLRHEG 167
Cdd:pfam01035   2 FQRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSLGGYAGGLERKRALLELEG 80
PRK00901 PRK00901
methylated-DNA--protein-cysteine methyltransferase; Provisional
 63-167 5.54e-44

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 234860 [Multi-domain]  Cd Length: 155  Bit Score: 142.88  E-value: 5.54e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867764  63 SDKLREYFAGNLSIIDtLPTATGGTQFQREVWKTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRV 142
Cdd:PRK00901  49 NKQLEEYFEGKRKKFD-LPLAPQGTEFQKKVWKALQEIPYGETRSYKEIAVNIGNPKACRAVGLANNKNPIPIFIPCHRV 127

                         90       100
                 ....*....|....*....|....*
gi 446867764 143 IGRNGTMTGYAGGVQRKEWLLRHEG 167
Cdd:PRK00901 128 IGANGKLVGYAGGLDIKEKLLKLEK 152
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
 89-167 3.08e-42

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: 135.69  E-value: 3.08e-42
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446867764  89 FQREVWKTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIGRNGTMTGYAGGVQRKEWLLRHEG 167
Cdd:cd06445    1 FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGLGGYRGGLERKRELLELEG 79
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
79-166 4.54e-31

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


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 114.89  E-value: 4.54e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867764  79 TLPTATGGTQFQREVWKTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIGRNGTMTGYAGGVQR 158
Cdd:PRK15435 261 TLPLDIRGTAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIVIPCHRVVRGDGALSGYRWGVSR 340


                 ....*...
gi 446867764 159 KEWLLRHE 166
Cdd:PRK15435 341 KAQLLRRE 348
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 11-166 1.00e-24

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: 97.82  E-value: 1.00e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867764  11 TPLGPLWVICDEQFRLR-AVEWEEYSERMVQLLdiHYRKESYERISATNPGGLSDKLREYFAGNLSIIDTLPTATGGTQF 89
Cdd:COG2169  195 TPCSLGLLLVAASARGVcAILLGDDPEALLRDL--QDRFPAAELIGGDAAFEQLVAEVVGFVEGPLLGLDLPLDLRGTAF 272

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446867764  90 QREVWKTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIGRNGTMTGYAGGVQRKEWLLRHE 166
Cdd:COG2169  273 QQRVWQALRAIPAGETASYAEIAARIGAPKAVRAVAAACAANQLAVAIPCHRVVRADGALSGYRWGVERKRALLERE 349
Atl1 COG3695
Alkylated DNA nucleotide flippase Atl1, participates in nucleotide excision repair, Ada-like ...
 89-167 2.65e-21

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


Pssm-ID: 442910  Cd Length: 104  Bit Score: 82.93  E-value: 2.65e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867764  89 FQREVWKTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIGRNGTMT-GYAGGVQRKEWLLRHEG 167
Cdd:COG3695    6 FYERVYEVVAQIPPGRVATYGDIAALAGLPRGARQVGRALRALPEGSDLPWHRVVNADGRLSpGHAGGAEEQRELLEAEG 85
Methyltransf_1N pfam02870
6-O-methylguanine DNA methyltransferase, ribonuclease-like domain; This entry represents the ...
 3-84 2.69e-17

6-O-methylguanine DNA methyltransferase, ribonuclease-like domain; This entry represents the N-terminal ribonuclease-like domain associated with 6-O-methylguanine DNA methyltransferase activity. The repair of DNA containing O6-alkylated guanine is carried out by DNA-[protein]-cysteine S-methyltransferase (also known as O-6-methylguanine-DNA-alkyltransferase)


Pssm-ID: 397139 [Multi-domain]  Cd Length: 77  Bit Score: 72.01  E-value: 2.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867764    3 RLLEEKIATPLGPLWVICDEQFrLRAVEWEEYSER-MVQLLDIHYRKESyerisATNPGGLSDKLREYFAGNLSIIDTLP 81
Cdd:pfam02870   1 ALYYTLIDSPLGRLLLAGDERG-LTAIDFLDKDYAlRKELPKVLPQPEL-----LPALALLVQALEEYFAGELKPEFTLP 74


                  ...
gi 446867764   82 TAT 84
Cdd:pfam02870  75 LDQ 77
PRK03887 PRK03887
methylated-DNA--protein-cysteine methyltransferase; Provisional
 59-167 6.92e-15

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 167628 [Multi-domain]  Cd Length: 175  Bit Score: 68.22  E-value: 6.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867764  59 PGGLSDKLREYFAGNLSIIDTLP--TATGGTQFQREVWKTL-RTIPCGQVMHYGQLAEQLGRpgAARAVGAANGSNPISI 135
Cdd:PRK03887  61 PSDYPELVFKVLIGKISNEEGLEelSFEGLTPFERKVYEWLtKNVKRGEVITYGELAKALNT--SPRAVGGAMKRNPYPI 138

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446867764 136 VVPCHRVIGRNGTMTgYAGGVQRKEWLLRHEG 167
Cdd:PRK03887 139 IVPCHRVVGRKNPGL-YTPKPEYKKFLLEVEG 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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