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Conserved domains on  [gi|15597314|ref|NP_250808|]
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O6-methylguanine-DNA methyltransferase [Pseudomonas aeruginosa PAO1]

Protein Classification

Ada family protein( domain architecture ID 1002941)

Ada family protein such as the bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada, which has a functional switch mechanism between acting as a DNA methyltransferase and a transcriptional regulator

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK15435 super family cl33145
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
9-357 6.85e-142

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


The actual alignment was detected with superfamily member PRK15435:

Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 406.10  E-value: 6.85e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314    9 NAYHTDEQRWAAVLARDAAADGAFVYAVKTTGVYCRPSSSARRPRRENVEFFATAEAAEAAGYRPSRRAAGDRSLAAEQR 88
Cdd:PRK15435   4 ATCLTDDQRWQSVLARDPNADGEFVFAVRTTGIFCRPSCRARHALRENVRFYANASEALAAGFRPCKRCQPDKANPQQHR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314   89 AERVAQACRMIETaETPPALEALAARLGMSPFHFHRLFKAETGLTPKAYASAYRARRLRERLGQASaSVTEAIYDSGFNS 168
Cdd:PRK15435  84 LDKITHACRLLEQ-ETPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLREALAKGE-SVTTSILNAGFPD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314  169 NSRFYESSSQRLGMRPRDYRDGGAGAAIRFAIGQCSLGAILVAQSQRGICAILLGEEPEPLLRELQDQFPRAQLLGGDAD 248
Cdd:PRK15435 162 SSSYYRKADETLGMTAKQFRHGGENLAVRYALADCELGRCLVAESERGICAILLGDDDAALISELQQMFPAADNAPADLT 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314  249 FERLVAQVVGFVESPQLGLDLPLDVRGTAFQERVWQALREIPPGSTASYAQVAERIGAPRAVRAVAQACAANRIAVAIPC 328
Cdd:PRK15435 242 FQQHVREVIASLNQRDTPLTLPLDIRGTAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIVIPC 321

                        330       340
                 ....*....|....*....|....*....
gi 15597314  329 HRVVRRDGDISGYRWGVERKRELLRREER 357
Cdd:PRK15435 322 HRVVRGDGALSGYRWGVSRKAQLLRREAE 350
 
Name Accession Description Interval E-value
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
9-357 6.85e-142

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


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 406.10  E-value: 6.85e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314    9 NAYHTDEQRWAAVLARDAAADGAFVYAVKTTGVYCRPSSSARRPRRENVEFFATAEAAEAAGYRPSRRAAGDRSLAAEQR 88
Cdd:PRK15435   4 ATCLTDDQRWQSVLARDPNADGEFVFAVRTTGIFCRPSCRARHALRENVRFYANASEALAAGFRPCKRCQPDKANPQQHR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314   89 AERVAQACRMIETaETPPALEALAARLGMSPFHFHRLFKAETGLTPKAYASAYRARRLRERLGQASaSVTEAIYDSGFNS 168
Cdd:PRK15435  84 LDKITHACRLLEQ-ETPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLREALAKGE-SVTTSILNAGFPD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314  169 NSRFYESSSQRLGMRPRDYRDGGAGAAIRFAIGQCSLGAILVAQSQRGICAILLGEEPEPLLRELQDQFPRAQLLGGDAD 248
Cdd:PRK15435 162 SSSYYRKADETLGMTAKQFRHGGENLAVRYALADCELGRCLVAESERGICAILLGDDDAALISELQQMFPAADNAPADLT 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314  249 FERLVAQVVGFVESPQLGLDLPLDVRGTAFQERVWQALREIPPGSTASYAQVAERIGAPRAVRAVAQACAANRIAVAIPC 328
Cdd:PRK15435 242 FQQHVREVIASLNQRDTPLTLPLDIRGTAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIVIPC 321

                        330       340
                 ....*....|....*....|....*....
gi 15597314  329 HRVVRRDGDISGYRWGVERKRELLRREER 357
Cdd:PRK15435 322 HRVVRGDGALSGYRWGVSRKAQLLRREAE 350
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 13-357 7.93e-134

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: 385.95  E-value: 7.93e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314  13 TDEQRWAAVLARDAAADGAFVYAVKTTGVYCRPSSSARRPRRENVEFFATAEAAEAAGYRPSRRAAGDRSLAAEQRAERV 92
Cdd:COG2169   7 DDDERWQAVLARDARFDGRFFYGVKTTGIYCRPSCPARKPKRENVRFFATAAAAEAAGFRPCKRCRPDLAPGSPPRADLV 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314  93 AQACRMIET-AETPPALEALAARLGMSPFHFHRLFKAETGLTPKAYASAYRARRLRERLgQASASVTEAIYDSGFNSNSR 171
Cdd:COG2169  87 ARACRLIEAgAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLL-QTGLSVTDAAYAAGFGSLSR 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314 172 FYESSSQRLGMRPRDYRDGGAGAAIRFAIGQCSLGAILVAQSQRGICAILLGEEPEPLLRELQDQFPRAQLLGGDADFER 251
Cdd:COG2169 166 FYEAFKKLLGMTPSAYRRGGAGAAIRFAPTPCSLGLLLVAASARGVCAILLGDDPEALLRDLQDRFPAAELIGGDAAFEQ 245

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314 252 LVAQVVGFVESPQLGLDLPLDVRGTAFQERVWQALREIPPGSTASYAQVAERIGAPRAVRAVAQACAANRIAVAIPCHRV 331
Cdd:COG2169 246 LVAEVVGFVEGPLLGLDLPLDLRGTAFQQRVWQALRAIPAGETASYAEIAARIGAPKAVRAVAAACAANQLAVAIPCHRV 325

                       330       340
                ....*....|....*....|....*.
gi 15597314 332 VRRDGDISGYRWGVERKRELLRREER 357
Cdd:COG2169 326 VRADGALSGYRWGVERKRALLEREAA 351
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
 277-355 3.85e-42

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: 141.73  E-value: 3.85e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597314   277 AFQERVWQALREIPPGSTASYAQVAERIGAPRAVRAVAQACAANRIAVAIPCHRVVRRDGDISGYRWGVERKRELLRRE 355
Cdd:pfam01035   1 PFQRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSLGGYAGGLERKRALLELE 79
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
 278-355 2.17e-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: 131.83  E-value: 2.17e-38
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597314 278 FQERVWQALREIPPGSTASYAQVAERIGAPRAVRAVAQACAANRIAVAIPCHRVVRRDGDISGYRWGVERKRELLRRE 355
Cdd:cd06445   1 FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGLGGYRGGLERKRELLELE 78
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
 276-355 1.29e-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: 129.74  E-value: 1.29e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314   276 TAFQERVWQALREIPPGSTASYAQVAERIGAPRAVRAVAQACAANRIAVAIPCHRVVRRDGDISGYRWGVERKRELLRRE 355
Cdd:TIGR00589   1 TPFQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLTGYGGGLERKEFLLEHE 80
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
105-188 1.17e-19

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 82.22  E-value: 1.17e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314    105 PPALEALAARLGMSPFHFHRLFKAETGLTPKAYASAYRARRLRERLGQASASVTEAIYDSGFNSNSRFYESSSQRLGMRP 184
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 15597314    185 RDYR 188
Cdd:smart00342  81 SEYR 84
 
Name Accession Description Interval E-value
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
9-357 6.85e-142

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


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 406.10  E-value: 6.85e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314    9 NAYHTDEQRWAAVLARDAAADGAFVYAVKTTGVYCRPSSSARRPRRENVEFFATAEAAEAAGYRPSRRAAGDRSLAAEQR 88
Cdd:PRK15435   4 ATCLTDDQRWQSVLARDPNADGEFVFAVRTTGIFCRPSCRARHALRENVRFYANASEALAAGFRPCKRCQPDKANPQQHR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314   89 AERVAQACRMIETaETPPALEALAARLGMSPFHFHRLFKAETGLTPKAYASAYRARRLRERLGQASaSVTEAIYDSGFNS 168
Cdd:PRK15435  84 LDKITHACRLLEQ-ETPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLREALAKGE-SVTTSILNAGFPD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314  169 NSRFYESSSQRLGMRPRDYRDGGAGAAIRFAIGQCSLGAILVAQSQRGICAILLGEEPEPLLRELQDQFPRAQLLGGDAD 248
Cdd:PRK15435 162 SSSYYRKADETLGMTAKQFRHGGENLAVRYALADCELGRCLVAESERGICAILLGDDDAALISELQQMFPAADNAPADLT 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314  249 FERLVAQVVGFVESPQLGLDLPLDVRGTAFQERVWQALREIPPGSTASYAQVAERIGAPRAVRAVAQACAANRIAVAIPC 328
Cdd:PRK15435 242 FQQHVREVIASLNQRDTPLTLPLDIRGTAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIVIPC 321

                        330       340
                 ....*....|....*....|....*....
gi 15597314  329 HRVVRRDGDISGYRWGVERKRELLRREER 357
Cdd:PRK15435 322 HRVVRGDGALSGYRWGVSRKAQLLRREAE 350
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 13-357 7.93e-134

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: 385.95  E-value: 7.93e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314  13 TDEQRWAAVLARDAAADGAFVYAVKTTGVYCRPSSSARRPRRENVEFFATAEAAEAAGYRPSRRAAGDRSLAAEQRAERV 92
Cdd:COG2169   7 DDDERWQAVLARDARFDGRFFYGVKTTGIYCRPSCPARKPKRENVRFFATAAAAEAAGFRPCKRCRPDLAPGSPPRADLV 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314  93 AQACRMIET-AETPPALEALAARLGMSPFHFHRLFKAETGLTPKAYASAYRARRLRERLgQASASVTEAIYDSGFNSNSR 171
Cdd:COG2169  87 ARACRLIEAgAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLL-QTGLSVTDAAYAAGFGSLSR 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314 172 FYESSSQRLGMRPRDYRDGGAGAAIRFAIGQCSLGAILVAQSQRGICAILLGEEPEPLLRELQDQFPRAQLLGGDADFER 251
Cdd:COG2169 166 FYEAFKKLLGMTPSAYRRGGAGAAIRFAPTPCSLGLLLVAASARGVCAILLGDDPEALLRDLQDRFPAAELIGGDAAFEQ 245

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314 252 LVAQVVGFVESPQLGLDLPLDVRGTAFQERVWQALREIPPGSTASYAQVAERIGAPRAVRAVAQACAANRIAVAIPCHRV 331
Cdd:COG2169 246 LVAEVVGFVEGPLLGLDLPLDLRGTAFQQRVWQALRAIPAGETASYAEIAARIGAPKAVRAVAAACAANQLAVAIPCHRV 325

                       330       340
                ....*....|....*....|....*.
gi 15597314 332 VRRDGDISGYRWGVERKRELLRREER 357
Cdd:COG2169 326 VRADGALSGYRWGVERKRALLEREAA 351
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
 195-355 3.76e-65

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


Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 203.57  E-value: 3.76e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314 195 AIRFAIGQCSLGAILVAQSQRGICAILLGEEPEpllRELQDQFPRAqLLGGDADFERLVAQVVGFVESPQLGLDLPLDVR 274
Cdd:COG0350   1 TIRYAIFDTPLGPLLIAATDRGLCALSFGDDRE---EALLARFPAA-LREDPPLLAEAARQLDAYFAGERKDFDLPLDLR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314 275 GTAFQERVWQALREIPPGSTASYAQVAERIGAPRAVRAVAQACAANRIAVAIPCHRVVRRDGDISGYRWGVERKRELLRR 354
Cdd:COG0350  77 GTPFQRRVWEALRKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSLGGYAGGLERKRALLEL 156


                .
gi 15597314 355 E 355
Cdd:COG0350 157 E 157
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
 277-355 3.85e-42

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: 141.73  E-value: 3.85e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597314   277 AFQERVWQALREIPPGSTASYAQVAERIGAPRAVRAVAQACAANRIAVAIPCHRVVRRDGDISGYRWGVERKRELLRRE 355
Cdd:pfam01035   1 PFQRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSLGGYAGGLERKRALLELE 79
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
 278-355 2.17e-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: 131.83  E-value: 2.17e-38
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597314 278 FQERVWQALREIPPGSTASYAQVAERIGAPRAVRAVAQACAANRIAVAIPCHRVVRRDGDISGYRWGVERKRELLRRE 355
Cdd:cd06445   1 FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGLGGYRGGLERKRELLELE 78
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
 276-355 1.29e-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: 129.74  E-value: 1.29e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314   276 TAFQERVWQALREIPPGSTASYAQVAERIGAPRAVRAVAQACAANRIAVAIPCHRVVRRDGDISGYRWGVERKRELLRRE 355
Cdd:TIGR00589   1 TPFQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLTGYGGGLERKEFLLEHE 80
PRK00901 PRK00901
methylated-DNA--protein-cysteine methyltransferase; Provisional
 202-356 6.15e-30

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 234860 [Multi-domain]  Cd Length: 155  Bit Score: 112.07  E-value: 6.15e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314  202 QCSLGAILVAQSQRGICAILLGEEP---------EPLLRELQDQFpRAQLLGGDADFerlvaqvvgfvespqlglDLPLD 272
Cdd:PRK00901   8 ETPIGKIGIAENGTAITHLCFGEDKipkdvtileTDLLKEANKQL-EEYFEGKRKKF------------------DLPLA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314  273 VRGTAFQERVWQALREIPPGSTASYAQVAERIGAPRAVRAVAQACAANRIAVAIPCHRVVRRDGDISGYRWGVERKRELL 352
Cdd:PRK00901  69 PQGTEFQKKVWKALQEIPYGETRSYKEIAVNIGNPKACRAVGLANNKNPIPIFIPCHRVIGANGKLVGYAGGLDIKEKLL 148


                 ....
gi 15597314  353 RREE 356
Cdd:PRK00901 149 KLEK 152
PRK10286 PRK10286
methylated-DNA--[protein]-cysteine S-methyltransferase;
268-355 3.05e-25

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


Pssm-ID: 182355 [Multi-domain]  Cd Length: 171  Bit Score: 100.33  E-value: 3.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314  268 DLPLDVRGTAFQERVWQALREIPPGSTASYAQVAERIGAPRAVRAVAQACAANRIAVAIPCHRVVRRDGDISGYRWGVER 347
Cdd:PRK10286  79 TLPTATGGTPFQREVWQTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIGRNGTMTGYAGGVQR 158


                 ....*...
gi 15597314  348 KRELLRRE 355
Cdd:PRK10286 159 KEWLLRHE 166
Atl1 COG3695
Alkylated DNA nucleotide flippase Atl1, participates in nucleotide excision repair, Ada-like ...
 278-355 4.74e-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: 86.78  E-value: 4.74e-21
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597314 278 FQERVWQALREIPPGSTASYAQVAERIGAPRAVRAVAQACAANRIAVAIPCHRVVRRDGDIS-GYRWGVERKRELLRRE 355
Cdd:COG3695   6 FYERVYEVVAQIPPGRVATYGDIAALAGLPRGARQVGRALRALPEGSDLPWHRVVNADGRLSpGHAGGAEEQRELLEAE 84
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
105-188 1.17e-19

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 82.22  E-value: 1.17e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314    105 PPALEALAARLGMSPFHFHRLFKAETGLTPKAYASAYRARRLRERLGQASASVTEAIYDSGFNSNSRFYESSSQRLGMRP 184
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 15597314    185 RDYR 188
Cdd:smart00342  81 SEYR 84
HTH_18 pfam12833
Helix-turn-helix domain;
111-188 6.82e-18

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 77.24  E-value: 6.82e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597314   111 LAARLGMSPFHFHRLFKAETGLTPKAYASAYRARRLRERLGQASA-SVTEAIYDSGFNSNSRFYESSSQRLGMRPRDYR 188
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEDTGlSVAEIALALGFSDASHFSRAFRRLFGLTPSEYR 79
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
108-188 2.35e-16

AraC-type DNA-binding domain and AraC-containing proteins [Transcription];


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 77.90  E-value: 2.35e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314 108 LEALAARLGMSPFHFHRLFKAETGLTPKAYASAYRARRLRERLGQASASVTEAIYDSGFNSNSRFYESSSQRLGMRPRDY 187
Cdd:COG2207 171 LEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEY 250


                .
gi 15597314 188 R 188
Cdd:COG2207 251 R 251
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 73-195 3.53e-16

Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];


Pssm-ID: 444002 [Multi-domain]  Cd Length: 318  Bit Score: 78.28  E-value: 3.53e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314  73 PSRRAAGD-----RSLAAEQRAERVAQACRMIETA-ETPPALEALAARLGMSPFHFHRLFKAETGLTPKAYASAYRARRL 146
Cdd:COG4977 188 DPRRPGGQaqfspLLVPLGHRDPRLARAQAWMEANlEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERA 267

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15597314 147 RERLGQASASVTEAIYDSGFNSNSRFYESSSQRLGMRPRDYRDGGAGAA 195
Cdd:COG4977 268 RRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRRRFRARA 316
Ada_Zn_binding pfam02805
Metal binding domain of Ada; The Escherichia coli Ada protein repairs O6-methylguanine ...
 29-76 3.68e-15

Metal binding domain of Ada; The Escherichia coli Ada protein repairs O6-methylguanine residues and methyl phosphotriesters in DNA by direct transfer of the methyl group to a cysteine residue. This domain contains four conserved cysteines that form a zinc binding site. One of these cysteines is a methyl group acceptor. The methylated domain can then specifically bind to the ada box on a DNA duplex.


Pssm-ID: 460701 [Multi-domain]  Cd Length: 62  Bit Score: 69.01  E-value: 3.68e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 15597314    29 DGAFVYAVKTTGVYCRPSSSARRPRRENVEFFATAEAAEAAGYRPSRR 76
Cdd:pfam02805  14 DGSFFYAVKTTGIYCRPSCPARLPKRENVRFFDTAAEAEAAGFRPCKR 61
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 98-137 1.95e-08

Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the N-terminal arm of AraC binds to the DNA binding domain (pfam00165) and helps to hold the two DNA binding domains in a relative orientation that favours DNA looping. In the presence of arabinose, the arms bind over the arabinose on the dimerization domain, thus freeing the DNA-binding domains. The freed DNA-binding domains are then able to assume a conformation suitable for binding to the adjacent DNA sites that are utilized when AraC activates transcription, and hence AraC ceases looping the DNA when arabinose is added.


Pssm-ID: 425497 [Multi-domain]  Cd Length: 42  Bit Score: 49.84  E-value: 1.95e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 15597314    98 MIETAETPPALEALAARLGMSPFHFHRLFKAETGLTPKAY 137
Cdd:pfam00165   1 LRENLSTNLTIADIADELGFSRSYFSRLFKKYTGVTPSQY 40
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
109-190 5.80e-08

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 53.53  E-value: 5.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314  109 EALAARLGMSPFHFHRLFKAETGLTPKAYASAYRARRLRERLGQASASVTEAIYDSGFNSNSRFYESSSQRLGMRPRDYR 188
Cdd:PRK13503 191 EALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCGFGDSNHFSTLFRREFSWSPRDIR 270


                 ..
gi 15597314  189 DG 190
Cdd:PRK13503 271 QG 272
PRK10371 PRK10371
transcriptional regulator MelR;
108-188 7.92e-08

transcriptional regulator MelR;


Pssm-ID: 182416 [Multi-domain]  Cd Length: 302  Bit Score: 53.28  E-value: 7.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314  108 LEALAARLGMSPFHFHRLFKAETGLTPKAYASAYRARRLRERLGQASASVTEAIYDSGFNSNSRFYESSSQRLGMRPRDY 187
Cdd:PRK10371 210 INDVAEHVKLNANYAMGIFQRVMQLTMKQYITAMRINHVRALLSDTDKSILDIALTAGFRSSSRFYSTFGKYVGMSPQQY 289


                 .
gi 15597314  188 R 188
Cdd:PRK10371 290 R 290
ftrA PRK09393
transcriptional activator FtrA; Provisional
 97-188 3.28e-07

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 51.50  E-value: 3.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314   97 RMIETAETPPALEALAARLGMSPFHFHRLFKAETGLTPKAYASAYRARRLRERLGQASASVTEAIYDSGFNSNSRFYESS 176
Cdd:PRK09393 226 WMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEESLRHHF 305

                         90
                 ....*....|..
gi 15597314  177 SQRLGMRPRDYR 188
Cdd:PRK09393 306 RRRAATSPAAYR 317
PRK11511 PRK11511
MDR efflux pump AcrAB transcriptional activator MarA;
103-188 4.52e-06

MDR efflux pump AcrAB transcriptional activator MarA;


Pssm-ID: 236920 [Multi-domain]  Cd Length: 127  Bit Score: 45.48  E-value: 4.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314  103 ETPPALEALAARLGMSPFHFHRLFKAETGLTPKAYASAYRARRLRERLGQASASVTEAIYDSGFNSNSRFYESSSQRLGM 182
Cdd:PRK11511  23 ESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKLKESNEPILYLAERYGFESQQTLTRTFKNYFDV 102


                 ....*.
gi 15597314  183 RPRDYR 188
Cdd:PRK11511 103 PPHKYR 108
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
 74-188 7.43e-06

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 46.95  E-value: 7.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314   74 SRRAAGDRSLAAEQRAERVaqacrmIETAETPPAL--EALAARLGMSPFHFHRLFkAETGLTPKAYASAYRARRLRERLG 151
Cdd:PRK09685 187 QRESVQPRRERQFQKVVAL------IDQSIQEEILrpEWIAGELGISVRSLYRLF-AEQGLVVAQYIRNRRLDRCADDLR 259

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 15597314  152 QASA--SVTEAIYDSGFNSNSRFYESSSQRLGMRPRDYR 188
Cdd:PRK09685 260 PAADdeKITSIAYKWGFSDSSHFSTAFKQRFGVSPGEYR 298
PRK03887 PRK03887
methylated-DNA--protein-cysteine methyltransferase; Provisional
 239-355 1.72e-05

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 167628 [Multi-domain]  Cd Length: 175  Bit Score: 44.72  E-value: 1.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597314  239 RAQLLGGDADFERLVAQV-VGFVESPQLgldLP-LDVRG-TAFQERVWQAL-REIPPGSTASYAQVAERIGAprAVRAVA 314
Cdd:PRK03887  54 KVSLKERPSDYPELVFKVlIGKISNEEG---LEeLSFEGlTPFERKVYEWLtKNVKRGEVITYGELAKALNT--SPRAVG 128

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 15597314  315 QACAANRIAVAIPCHRVVRRDGdISGYRWGVERKRELLRRE 355
Cdd:PRK03887 129 GAMKRNPYPIIVPCHRVVGRKN-PGLYTPKPEYKKFLLEVE 168
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
76-145 3.41e-05

AraC-type DNA-binding domain and AraC-containing proteins [Transcription];


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 44.77  E-value: 3.41e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597314  76 RAAGDRSLAAEQRAERVAQACRMIETAETPpaLEALAARLGM-SPFHFHRLFKAETGLTPKAYASAYRARR 145
Cdd:COG2207 190 KEETGTSPKQYLRELRLERAKRLLAETDLS--ISEIAYELGFsSQSHFSRAFKKRFGVTPSEYRKRLRARA 258
Methyltransf_1N pfam02870
6-O-methylguanine DNA methyltransferase, ribonuclease-like domain; This entry represents the ...
 195-272 1.01e-04

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: 40.43  E-value: 1.01e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597314   195 AIRFAIGQCSLGAILVAQSQRGICAILLGEEPEPLLRELQDQFPRAQLLGGDADFERLVAQVVGFVESPQlgLDLPLD 272
Cdd:pfam02870   1 ALYYTLIDSPLGRLLLAGDERGLTAIDFLDKDYALRKELPKVLPQPELLPALALLVQALEEYFAGELKPE--FTLPLD 76
 
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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