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Conserved domains on  [gi|2215770214|ref|WP_243215699|]
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methylated-DNA--[protein]-cysteine S-methyltransferase [Frigoribacterium faeni]

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, ...
 12-167 9.22e-73

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


:

Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 216.28  E-value: 9.22e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215770214  12 HTTVPSPLGDLTLVASEDGLAGLYFAEHRNLPDPAGFGRASPTGVGVvdFDEVEHQLGEYFAGERRRFDLPLAPRGNEFR 91
Cdd:COG0350     4 YAIFDTPLGPLLIAATDRGLCALSFGDDREEALLARFPAALREDPPL--LAEAARQLDAYFAGERKDFDLPLDLRGTPFQ 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2215770214  92 RRVWALLRDIPYGETRSYGQLARELGDVGLARAVGAANGLNPLSIVVPCHRVVGAAGALVGYAGGLDRKRRLLDLE 167
Cdd:COG0350    82 RRVWEALRKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSLGGYAGGLERKRALLELE 157
 
Name Accession Description Interval E-value
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
 12-167 9.22e-73

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


Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 216.28  E-value: 9.22e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215770214  12 HTTVPSPLGDLTLVASEDGLAGLYFAEHRNLPDPAGFGRASPTGVGVvdFDEVEHQLGEYFAGERRRFDLPLAPRGNEFR 91
Cdd:COG0350     4 YAIFDTPLGPLLIAATDRGLCALSFGDDREEALLARFPAALREDPPL--LAEAARQLDAYFAGERKDFDLPLDLRGTPFQ 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2215770214  92 RRVWALLRDIPYGETRSYGQLARELGDVGLARAVGAANGLNPLSIVVPCHRVVGAAGALVGYAGGLDRKRRLLDLE 167
Cdd:COG0350    82 RRVWEALRKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSLGGYAGGLERKRALLELE 157
PRK00901 PRK00901
methylated-DNA--protein-cysteine methyltransferase; Provisional
 17-168 3.13e-54

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 234860 [Multi-domain]  Cd Length: 155  Bit Score: 169.08  E-value: 3.13e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215770214  17 SPLGDLTLVASEDGLAGLYFAEHRNLPDpagfgrasptgVGVVD---FDEVEHQLGEYFAGERRRFDLPLAPRGNEFRRR 93
Cdd:PRK00901    9 TPIGKIGIAENGTAITHLCFGEDKIPKD-----------VTILEtdlLKEANKQLEEYFEGKRKKFDLPLAPQGTEFQKK 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2215770214  94 VWALLRDIPYGETRSYGQLARELGDVGLARAVGAANGLNPLSIVVPCHRVVGAAGALVGYAGGLDRKRRLLDLEE 168
Cdd:PRK00901   78 VWKALQEIPYGETRSYKEIAVNIGNPKACRAVGLANNKNPIPIFIPCHRVIGANGKLVGYAGGLDIKEKLLKLEK 152
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
 89-167 3.76e-43

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: 138.26  E-value: 3.76e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2215770214  89 EFRRRVWALLRDIPYGETRSYGQLARELGDVGLARAVGAANGLNPLSIVVPCHRVVGAAGALVGYAGGLDRKRRLLDLE 167
Cdd:pfam01035   1 PFQRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSLGGYAGGLERKRALLELE 79
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
 90-167 2.31e-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: 2.31e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2215770214  90 FRRRVWALLRDIPYGETRSYGQLARELGDVGLARAVGAANGLNPLSIVVPCHRVVGAAGALVGYAGGLDRKRRLLDLE 167
Cdd:cd06445     1 FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGLGGYRGGLERKRELLELE 78
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
 89-167 3.96e-37

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: 123.19  E-value: 3.96e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2215770214  89 EFRRRVWALLRDIPYGETRSYGQLARELGDVGLARAVGAANGLNPLSIVVPCHRVVGAAGALVGYAGGLDRKRRLLDLE 167
Cdd:TIGR00589   2 PFQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLTGYGGGLERKEFLLEHE 80
 
Name Accession Description Interval E-value
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
 12-167 9.22e-73

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


Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 216.28  E-value: 9.22e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215770214  12 HTTVPSPLGDLTLVASEDGLAGLYFAEHRNLPDPAGFGRASPTGVGVvdFDEVEHQLGEYFAGERRRFDLPLAPRGNEFR 91
Cdd:COG0350     4 YAIFDTPLGPLLIAATDRGLCALSFGDDREEALLARFPAALREDPPL--LAEAARQLDAYFAGERKDFDLPLDLRGTPFQ 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2215770214  92 RRVWALLRDIPYGETRSYGQLARELGDVGLARAVGAANGLNPLSIVVPCHRVVGAAGALVGYAGGLDRKRRLLDLE 167
Cdd:COG0350    82 RRVWEALRKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSLGGYAGGLERKRALLELE 157
PRK00901 PRK00901
methylated-DNA--protein-cysteine methyltransferase; Provisional
 17-168 3.13e-54

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 234860 [Multi-domain]  Cd Length: 155  Bit Score: 169.08  E-value: 3.13e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215770214  17 SPLGDLTLVASEDGLAGLYFAEHRNLPDpagfgrasptgVGVVD---FDEVEHQLGEYFAGERRRFDLPLAPRGNEFRRR 93
Cdd:PRK00901    9 TPIGKIGIAENGTAITHLCFGEDKIPKD-----------VTILEtdlLKEANKQLEEYFEGKRKKFDLPLAPQGTEFQKK 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2215770214  94 VWALLRDIPYGETRSYGQLARELGDVGLARAVGAANGLNPLSIVVPCHRVVGAAGALVGYAGGLDRKRRLLDLEE 168
Cdd:PRK00901   78 VWKALQEIPYGETRSYKEIAVNIGNPKACRAVGLANNKNPIPIFIPCHRVIGANGKLVGYAGGLDIKEKLLKLEK 152
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
 89-167 3.76e-43

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: 138.26  E-value: 3.76e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2215770214  89 EFRRRVWALLRDIPYGETRSYGQLARELGDVGLARAVGAANGLNPLSIVVPCHRVVGAAGALVGYAGGLDRKRRLLDLE 167
Cdd:pfam01035   1 PFQRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSLGGYAGGLERKRALLELE 79
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
 90-167 2.31e-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: 2.31e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2215770214  90 FRRRVWALLRDIPYGETRSYGQLARELGDVGLARAVGAANGLNPLSIVVPCHRVVGAAGALVGYAGGLDRKRRLLDLE 167
Cdd:cd06445     1 FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGLGGYRGGLERKRELLELE 78
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
 89-167 3.96e-37

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: 123.19  E-value: 3.96e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2215770214  89 EFRRRVWALLRDIPYGETRSYGQLARELGDVGLARAVGAANGLNPLSIVVPCHRVVGAAGALVGYAGGLDRKRRLLDLE 167
Cdd:TIGR00589   2 PFQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLTGYGGGLERKEFLLEHE 80
PRK10286 PRK10286
methylated-DNA--[protein]-cysteine S-methyltransferase;
15-167 3.96e-36

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


Pssm-ID: 182355 [Multi-domain]  Cd Length: 171  Bit Score: 123.44  E-value: 3.96e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215770214  15 VPSPLGDLTLVASED-GLAGLYFAEHRN----LPD----PAGFGRASPTGVGvvdfdEVEHQLGEYFAGERRRFD-LPLA 84
Cdd:PRK10286    9 IATPLGPLWVICDEQfRLRAVEWEEYSErmvqLLDihyrKEGYERISATNPG-----GLSDKLRDYFAGNLSIIDtLPTA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215770214  85 PRGNEFRRRVWALLRDIPYGETRSYGQLARELGDVGLARAVGAANGLNPLSIVVPCHRVVGAAGALVGYAGGLDRKRRLL 164
Cdd:PRK10286   84 TGGTPFQREVWQTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIGRNGTMTGYAGGVQRKEWLL 163


                  ...
gi 2215770214 165 DLE 167
Cdd:PRK10286  164 RHE 166
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 16-172 1.50e-29

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: 110.91  E-value: 1.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215770214  16 PSPLGDLTLVASEDGLAGLYF---AEHRNLPDPAGFGRASPTGvGVVDFDEVEHQLGEYFAGERRRFDLPLAPRGNEFRR 92
Cdd:COG2169   196 PCSLGLLLVAASARGVCAILLgddPEALLRDLQDRFPAAELIG-GDAAFEQLVAEVVGFVEGPLLGLDLPLDLRGTAFQQ 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215770214  93 RVWALLRDIPYGETRSYGQLARELGDVGLARAVGAANGLNPLSIVVPCHRVVGAAGALVGYAGGLDRKRRLLDLEEPESA 172
Cdd:COG2169   275 RVWQALRAIPAGETASYAEIAARIGAPKAVRAVAAACAANQLAVAIPCHRVVRADGALSGYRWGVERKRALLEREAAAAA 354
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
81-167 4.85e-26

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


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 101.79  E-value: 4.85e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215770214  81 LPLAPRGNEFRRRVWALLRDIPYGETRSYGQLARELGDVGLARAVGAANGLNPLSIVVPCHRVVGAAGALVGYAGGLDRK 160
Cdd:PRK15435  262 LPLDIRGTAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIVIPCHRVVRGDGALSGYRWGVSRK 341


                  ....*..
gi 2215770214 161 RRLLDLE 167
Cdd:PRK15435  342 AQLLRRE 348
Atl1 COG3695
Alkylated DNA nucleotide flippase Atl1, participates in nucleotide excision repair, Ada-like ...
 88-167 1.51e-17

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


Pssm-ID: 442910  Cd Length: 104  Bit Score: 73.68  E-value: 1.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215770214  88 NEFRRRVWALLRDIPYGETRSYGQLARELGDVGLARAVGAANGLNPLSIVVPCHRVVGAAGAL-VGYAGGLDRKRRLLDL 166
Cdd:COG3695     4 EEFYERVYEVVAQIPPGRVATYGDIAALAGLPRGARQVGRALRALPEGSDLPWHRVVNADGRLsPGHAGGAEEQRELLEA 83


                  .
gi 2215770214 167 E 167
Cdd:COG3695    84 E 84
PRK03887 PRK03887
methylated-DNA--protein-cysteine methyltransferase; Provisional
 90-167 3.35e-12

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 167628 [Multi-domain]  Cd Length: 175  Bit Score: 61.29  E-value: 3.35e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2215770214  90 FRRRVWA-LLRDIPYGETRSYGQLARELGDVglARAVGAANGLNPLSIVVPCHRVVGAAGALVgYAGGLDRKRRLLDLE 167
Cdd:PRK03887   93 FERKVYEwLTKNVKRGEVITYGELAKALNTS--PRAVGGAMKRNPYPIIVPCHRVVGRKNPGL-YTPKPEYKKFLLEVE 168
 
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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