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Conserved domains on  [gi|1085371892|gb|OGV42981|]
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MAG: hypothetical protein A2X46_00055 [Lentisphaerae bacterium GWF2_57_35]

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, ...
 1-158 1.42e-43

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


:

Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 141.55  E-value: 1.42e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085371892   1 MESSWGVLVVKSRNALITACELPflssepHEKFEWGRSDIKANNSRDEAVLRKAERFVRGLFGGK-ESPSPELDWpKASV 79
Cdd:COG0350     7 FDTPLGPLLIAATDRGLCALSFG------DDREEALLARFPAALREDPPLLAEAARQLDAYFAGErKDFDLPLDL-RGTP 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085371892  80 FTVSVWKGLAAIPKGQTAEYGELARTVGCPGGARAVGRACGANPLPLFIPCHRAVARHGTLGGFSCGLPWKRLLLEVEK 158
Cdd:COG0350    80 FQRRVWEALRKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSLGGYAGGLERKRALLELEG 158
 
Name Accession Description Interval E-value
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
 1-158 1.42e-43

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


Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 141.55  E-value: 1.42e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085371892   1 MESSWGVLVVKSRNALITACELPflssepHEKFEWGRSDIKANNSRDEAVLRKAERFVRGLFGGK-ESPSPELDWpKASV 79
Cdd:COG0350     7 FDTPLGPLLIAATDRGLCALSFG------DDREEALLARFPAALREDPPLLAEAARQLDAYFAGErKDFDLPLDL-RGTP 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085371892  80 FTVSVWKGLAAIPKGQTAEYGELARTVGCPGGARAVGRACGANPLPLFIPCHRAVARHGTLGGFSCGLPWKRLLLEVEK 158
Cdd:COG0350    80 FQRRVWEALRKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSLGGYAGGLERKRALLELEG 158
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
 80-158 2.50e-34

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: 115.15  E-value: 2.50e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085371892  80 FTVSVWKGLAAIPKGQTAEYGELARTVGCPGGARAVGRACGANPLPLFIPCHRAVARHGTLGGFSCGLPWKRLLLEVEK 158
Cdd:pfam01035   2 FQRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSLGGYAGGLERKRALLELEG 80
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
 80-158 1.27e-33

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: 1.27e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085371892  80 FTVSVWKGLAAIPKGQTAEYGELARTVGCPGGARAVGRACGANPLPLFIPCHRAVARHGTLGGFSCGLPWKRLLLEVEK 158
Cdd:cd06445     1 FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGLGGYRGGLERKRELLELEG 79
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
 80-157 2.68e-30

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: 105.09  E-value: 2.68e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1085371892  80 FTVSVWKGLAAIPKGQTAEYGELARTVGCPGGARAVGRACGANPLPLFIPCHRAVARHGTLGGFSCGLPWKRLLLEVE 157
Cdd:TIGR00589   3 FQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLTGYGGGLERKEFLLEHE 80
PRK00901 PRK00901
methylated-DNA--protein-cysteine methyltransferase; Provisional
 39-158 4.95e-27

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 234860 [Multi-domain]  Cd Length: 155  Bit Score: 98.97  E-value: 4.95e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085371892  39 DIKANNsrdEAVLRKAERFVRGLFGGK-ESPSPELDwPKASVFTVSVWKGLAAIPKGQTAEYGELARTVGCPGGARAVGR 117
Cdd:PRK00901   36 DVTILE---TDLLKEANKQLEEYFEGKrKKFDLPLA-PQGTEFQKKVWKALQEIPYGETRSYKEIAVNIGNPKACRAVGL 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1085371892 118 ACGANPLPLFIPCHRAVARHGTLGGFSCGLPWKRLLLEVEK 158
Cdd:PRK00901  112 ANNKNPIPIFIPCHRVIGANGKLVGYAGGLDIKEKLLKLEK 152
 
Name Accession Description Interval E-value
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
 1-158 1.42e-43

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


Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 141.55  E-value: 1.42e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085371892   1 MESSWGVLVVKSRNALITACELPflssepHEKFEWGRSDIKANNSRDEAVLRKAERFVRGLFGGK-ESPSPELDWpKASV 79
Cdd:COG0350     7 FDTPLGPLLIAATDRGLCALSFG------DDREEALLARFPAALREDPPLLAEAARQLDAYFAGErKDFDLPLDL-RGTP 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085371892  80 FTVSVWKGLAAIPKGQTAEYGELARTVGCPGGARAVGRACGANPLPLFIPCHRAVARHGTLGGFSCGLPWKRLLLEVEK 158
Cdd:COG0350    80 FQRRVWEALRKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSLGGYAGGLERKRALLELEG 158
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
 80-158 2.50e-34

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: 115.15  E-value: 2.50e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085371892  80 FTVSVWKGLAAIPKGQTAEYGELARTVGCPGGARAVGRACGANPLPLFIPCHRAVARHGTLGGFSCGLPWKRLLLEVEK 158
Cdd:pfam01035   2 FQRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSLGGYAGGLERKRALLELEG 80
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
 80-158 1.27e-33

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: 1.27e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085371892  80 FTVSVWKGLAAIPKGQTAEYGELARTVGCPGGARAVGRACGANPLPLFIPCHRAVARHGTLGGFSCGLPWKRLLLEVEK 158
Cdd:cd06445     1 FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGLGGYRGGLERKRELLELEG 79
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
 80-157 2.68e-30

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: 105.09  E-value: 2.68e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1085371892  80 FTVSVWKGLAAIPKGQTAEYGELARTVGCPGGARAVGRACGANPLPLFIPCHRAVARHGTLGGFSCGLPWKRLLLEVE 157
Cdd:TIGR00589   3 FQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLTGYGGGLERKEFLLEHE 80
PRK00901 PRK00901
methylated-DNA--protein-cysteine methyltransferase; Provisional
 39-158 4.95e-27

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 234860 [Multi-domain]  Cd Length: 155  Bit Score: 98.97  E-value: 4.95e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085371892  39 DIKANNsrdEAVLRKAERFVRGLFGGK-ESPSPELDwPKASVFTVSVWKGLAAIPKGQTAEYGELARTVGCPGGARAVGR 117
Cdd:PRK00901   36 DVTILE---TDLLKEANKQLEEYFEGKrKKFDLPLA-PQGTEFQKKVWKALQEIPYGETRSYKEIAVNIGNPKACRAVGL 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1085371892 118 ACGANPLPLFIPCHRAVARHGTLGGFSCGLPWKRLLLEVEK 158
Cdd:PRK00901  112 ANNKNPIPIFIPCHRVIGANGKLVGYAGGLDIKEKLLKLEK 152
PRK10286 PRK10286
methylated-DNA--[protein]-cysteine S-methyltransferase;
80-157 8.43e-22

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


Pssm-ID: 182355 [Multi-domain]  Cd Length: 171  Bit Score: 86.08  E-value: 8.43e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1085371892  80 FTVSVWKGLAAIPKGQTAEYGELARTVGCPGGARAVGRACGANPLPLFIPCHRAVARHGTLGGFSCGLPWKRLLLEVE 157
Cdd:PRK10286   89 FQREVWQTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIGRNGTMTGYAGGVQRKEWLLRHE 166
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
44-157 3.44e-20

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


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 85.23  E-value: 3.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085371892  44 NSRDEAVLRKAERFVRGLFGGKESPSPELDWP---KASVFTVSVWKGLAAIPKGQTAEYGELARTVGCPGGARAVGRACG 120
Cdd:PRK15435  232 AADNAPADLTFQQHVREVIASLNQRDTPLTLPldiRGTAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACA 311

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1085371892 121 ANPLPLFIPCHRAVARHGTLGGFSCGLPWKRLLLEVE 157
Cdd:PRK15435  312 ANKLAIVIPCHRVVRGDGALSGYRWGVSRKAQLLRRE 348
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 2-157 2.30e-16

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: 74.70  E-value: 2.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085371892   2 ESSWGVLVVKSRNALItaCELPFLSSEPHEKFEWGRSDIKANNSRDEAVLRKAERFVRGLFggkESPSPELDWP---KAS 78
Cdd:COG2169   196 PCSLGLLLVAASARGV--CAILLGDDPEALLRDLQDRFPAAELIGGDAAFEQLVAEVVGFV---EGPLLGLDLPldlRGT 270

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085371892  79 VFTVSVWKGLAAIPKGQTAEYGELARTVGCPGGARAVGRACGANPLPLFIPCHRAVARHGTLGGFSCGLPWKRLLLEVE 157
Cdd:COG2169   271 AFQQRVWQALRAIPAGETASYAEIAARIGAPKAVRAVAAACAANQLAVAIPCHRVVRADGALSGYRWGVERKRALLERE 349
Atl1 COG3695
Alkylated DNA nucleotide flippase Atl1, participates in nucleotide excision repair, Ada-like ...
 84-157 3.01e-14

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


Pssm-ID: 442910  Cd Length: 104  Bit Score: 64.44  E-value: 3.01e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1085371892  84 VWKGLAAIPKGQTAEYGELARTVGCPGGARAVGRACGANPLPLFIPCHRAVARHGTL-GGFSCGLPWKRLLLEVE 157
Cdd:COG3695    10 VYEVVAQIPPGRVATYGDIAALAGLPRGARQVGRALRALPEGSDLPWHRVVNADGRLsPGHAGGAEEQRELLEAE 84
PRK03887 PRK03887
methylated-DNA--protein-cysteine methyltransferase; Provisional
 64-157 7.83e-11

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 167628 [Multi-domain]  Cd Length: 175  Bit Score: 57.44  E-value: 7.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085371892  64 GKESPSPELDWPKASVFTVSVWKGLAA-IPKGQTAEYGELARTVGCpgGARAVGRACGANPLPLFIPCHRAVARHGtLGG 142
Cdd:PRK03887   77 SNEEGLEELSFEGLTPFERKVYEWLTKnVKRGEVITYGELAKALNT--SPRAVGGAMKRNPYPIIVPCHRVVGRKN-PGL 153

                          90
                  ....*....|....*
gi 1085371892 143 FSCGLPWKRLLLEVE 157
Cdd:PRK03887  154 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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