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Conserved domains on  [gi|1004664661|ref|WP_061548529|]
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MULTISPECIES: bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada [Citrobacter]

Protein Classification

bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada( domain architecture ID 11487795)

bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada has a functional switch mechanism from a DNA methyltransferase to a transcriptional regulator

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
1-353 0e+00

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


:

Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 660.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661   1 MKNRLRITDDDRWQSVLARDADADGQFVFAVQTTGIFCRPSCRAKHALRKNVCFFSDAQQAQAAGFRPCKRCQPDKDSAQ 80
Cdd:PRK15435    1 MKNATCLTDDQRWQSVLARDPNADGEFVFAVRTTGIFCRPSCRARHALRENVRFYANASEALAAGFRPCKRCQPDKANPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661  81 QHRLDKIARACQLLEHESPLTLDELAQQVAMSPYHLHRLFKATTGMTPKAWQQSWRARRLRDALAKGVPVTQAILNAGFP 160
Cdd:PRK15435   81 QHRLDKITHACRLLEQETPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLREALAKGESVTTSILNAGFP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661 161 DSSSYYRKADQTLGMTAKQFRKGGDNVFVRYTLADCALGRCLVAESERGICAILLGDDDATLVADLHELFPAAQDVPADA 240
Cdd:PRK15435  161 DSSSYYRKADETLGMTAKQFRHGGENLAVRYALADCELGRCLVAESERGICAILLGDDDAALISELQQMFPAADNAPADL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661 241 DFQQHVREVIAAINSRDASLSLPLDIRGTAFQQQVWQALRAIPCGETMSYQQLASAIGKPKAVRAVASACGANKLAIVIP 320
Cdd:PRK15435  241 TFQQHVREVIASLNQRDTPLTLPLDIRGTAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIVIP 320

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1004664661 321 CHRVIRGDGALSGYRWGIARKAQLLQRETTGEE 353
Cdd:PRK15435  321 CHRVVRGDGALSGYRWGVSRKAQLLRREAENEE 353
 
Name Accession Description Interval E-value
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
1-353 0e+00

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


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 660.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661   1 MKNRLRITDDDRWQSVLARDADADGQFVFAVQTTGIFCRPSCRAKHALRKNVCFFSDAQQAQAAGFRPCKRCQPDKDSAQ 80
Cdd:PRK15435    1 MKNATCLTDDQRWQSVLARDPNADGEFVFAVRTTGIFCRPSCRARHALRENVRFYANASEALAAGFRPCKRCQPDKANPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661  81 QHRLDKIARACQLLEHESPLTLDELAQQVAMSPYHLHRLFKATTGMTPKAWQQSWRARRLRDALAKGVPVTQAILNAGFP 160
Cdd:PRK15435   81 QHRLDKITHACRLLEQETPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLREALAKGESVTTSILNAGFP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661 161 DSSSYYRKADQTLGMTAKQFRKGGDNVFVRYTLADCALGRCLVAESERGICAILLGDDDATLVADLHELFPAAQDVPADA 240
Cdd:PRK15435  161 DSSSYYRKADETLGMTAKQFRHGGENLAVRYALADCELGRCLVAESERGICAILLGDDDAALISELQQMFPAADNAPADL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661 241 DFQQHVREVIAAINSRDASLSLPLDIRGTAFQQQVWQALRAIPCGETMSYQQLASAIGKPKAVRAVASACGANKLAIVIP 320
Cdd:PRK15435  241 TFQQHVREVIASLNQRDTPLTLPLDIRGTAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIVIP 320

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1004664661 321 CHRVIRGDGALSGYRWGIARKAQLLQRETTGEE 353
Cdd:PRK15435  321 CHRVVRGDGALSGYRWGVSRKAQLLRREAENEE 353
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 3-354 9.69e-151

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: 428.70  E-value: 9.69e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661   3 NRLRITDDDRWQSVLARDADADGQFVFAVQTTGIFCRPSCRAKHALRKNVCFFSDAQQAQAAGFRPCKRCQPDKDSAQQH 82
Cdd:COG2169     2 TTDLLDDDERWQAVLARDARFDGRFFYGVKTTGIYCRPSCPARKPKRENVRFFATAAAAEAAGFRPCKRCRPDLAPGSPP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661  83 RLDKIARACQLLEH--ESPLTLDELAQQVAMSPYHLHRLFKATTGMTPKAWQQSWRARRLRDALAKGVPVTQAILNAGFP 160
Cdd:COG2169    82 RADLVARACRLIEAgaEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLLQTGLSVTDAAYAAGFG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661 161 DSSSYYRKADQTLGMTAKQFRKGGDNVFVRYTLADCALGRCLVAESERGICAILLGDDDATLVADLHELFPAAQDVPADA 240
Cdd:COG2169   162 SLSRFYEAFKKLLGMTPSAYRRGGAGAAIRFAPTPCSLGLLLVAASARGVCAILLGDDPEALLRDLQDRFPAAELIGGDA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661 241 DFQQHVREVIAAINSRDASLSLPLDIRGTAFQQQVWQALRAIPCGETMSYQQLASAIGKPKAVRAVASACGANKLAIVIP 320
Cdd:COG2169   242 AFEQLVAEVVGFVEGPLLGLDLPLDLRGTAFQQRVWQALRAIPAGETASYAEIAARIGAPKAVRAVAAACAANQLAVAIP 321

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1004664661 321 CHRVIRGDGALSGYRWGIARKAQLLQRETTGEET 354
Cdd:COG2169   322 CHRVVRADGALSGYRWGVERKRALLEREAAAAAA 355
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
 269-348 1.09e-45

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: 150.54  E-value: 1.09e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661 269 TAFQQQVWQALRAIPCGETMSYQQLASAIGKPKAVRAVASACGANKLAIVIPCHRVIRGDGALSGYRWGIARKAQLLQRE 348
Cdd:TIGR00589   1 TPFQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLTGYGGGLERKEFLLEHE 80
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
 270-348 5.57e-44

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: 146.35  E-value: 5.57e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1004664661 270 AFQQQVWQALRAIPCGETMSYQQLASAIGKPKAVRAVASACGANKLAIVIPCHRVIRGDGALSGYRWGIARKAQLLQRE 348
Cdd:pfam01035   1 PFQRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSLGGYAGGLERKRALLELE 79
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
 271-348 8.44e-41

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: 138.00  E-value: 8.44e-41
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1004664661 271 FQQQVWQALRAIPCGETMSYQQLASAIGKPKAVRAVASACGANKLAIVIPCHRVIRGDGALSGYRWGIARKAQLLQRE 348
Cdd:cd06445     1 FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGLGGYRGGLERKRELLELE 78
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
99-181 1.94e-22

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 89.53  E-value: 1.94e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661   99 PLTLDELAQQVAMSPYHLHRLFKATTGMTPKAWQQSWRARRLRDALAKG-VPVTQAILNAGFPDSSSYYRKADQTLGMTA 177
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTdLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 1004664661  178 KQFR 181
Cdd:smart00342  81 SEYR 84
 
Name Accession Description Interval E-value
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
1-353 0e+00

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


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 660.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661   1 MKNRLRITDDDRWQSVLARDADADGQFVFAVQTTGIFCRPSCRAKHALRKNVCFFSDAQQAQAAGFRPCKRCQPDKDSAQ 80
Cdd:PRK15435    1 MKNATCLTDDQRWQSVLARDPNADGEFVFAVRTTGIFCRPSCRARHALRENVRFYANASEALAAGFRPCKRCQPDKANPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661  81 QHRLDKIARACQLLEHESPLTLDELAQQVAMSPYHLHRLFKATTGMTPKAWQQSWRARRLRDALAKGVPVTQAILNAGFP 160
Cdd:PRK15435   81 QHRLDKITHACRLLEQETPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLREALAKGESVTTSILNAGFP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661 161 DSSSYYRKADQTLGMTAKQFRKGGDNVFVRYTLADCALGRCLVAESERGICAILLGDDDATLVADLHELFPAAQDVPADA 240
Cdd:PRK15435  161 DSSSYYRKADETLGMTAKQFRHGGENLAVRYALADCELGRCLVAESERGICAILLGDDDAALISELQQMFPAADNAPADL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661 241 DFQQHVREVIAAINSRDASLSLPLDIRGTAFQQQVWQALRAIPCGETMSYQQLASAIGKPKAVRAVASACGANKLAIVIP 320
Cdd:PRK15435  241 TFQQHVREVIASLNQRDTPLTLPLDIRGTAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIVIP 320

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1004664661 321 CHRVIRGDGALSGYRWGIARKAQLLQRETTGEE 353
Cdd:PRK15435  321 CHRVVRGDGALSGYRWGVSRKAQLLRREAENEE 353
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 3-354 9.69e-151

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: 428.70  E-value: 9.69e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661   3 NRLRITDDDRWQSVLARDADADGQFVFAVQTTGIFCRPSCRAKHALRKNVCFFSDAQQAQAAGFRPCKRCQPDKDSAQQH 82
Cdd:COG2169     2 TTDLLDDDERWQAVLARDARFDGRFFYGVKTTGIYCRPSCPARKPKRENVRFFATAAAAEAAGFRPCKRCRPDLAPGSPP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661  83 RLDKIARACQLLEH--ESPLTLDELAQQVAMSPYHLHRLFKATTGMTPKAWQQSWRARRLRDALAKGVPVTQAILNAGFP 160
Cdd:COG2169    82 RADLVARACRLIEAgaEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLLQTGLSVTDAAYAAGFG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661 161 DSSSYYRKADQTLGMTAKQFRKGGDNVFVRYTLADCALGRCLVAESERGICAILLGDDDATLVADLHELFPAAQDVPADA 240
Cdd:COG2169   162 SLSRFYEAFKKLLGMTPSAYRRGGAGAAIRFAPTPCSLGLLLVAASARGVCAILLGDDPEALLRDLQDRFPAAELIGGDA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661 241 DFQQHVREVIAAINSRDASLSLPLDIRGTAFQQQVWQALRAIPCGETMSYQQLASAIGKPKAVRAVASACGANKLAIVIP 320
Cdd:COG2169   242 AFEQLVAEVVGFVEGPLLGLDLPLDLRGTAFQQRVWQALRAIPAGETASYAEIAARIGAPKAVRAVAAACAANQLAVAIP 321

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1004664661 321 CHRVIRGDGALSGYRWGIARKAQLLQRETTGEET 354
Cdd:COG2169   322 CHRVVRADGALSGYRWGVERKRALLEREAAAAAA 355
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
 189-348 6.33e-70

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


Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 215.89  E-value: 6.33e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661 189 VRYTLADCALGRCLVAESERGICAILLGDDDAtlvADLHELFPAAqDVPADADFQQHVREVIAAINSRDASLSLPLDIRG 268
Cdd:COG0350     2 IRYAIFDTPLGPLLIAATDRGLCALSFGDDRE---EALLARFPAA-LREDPPLLAEAARQLDAYFAGERKDFDLPLDLRG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661 269 TAFQQQVWQALRAIPCGETMSYQQLASAIGKPKAVRAVASACGANKLAIVIPCHRVIRGDGALSGYRWGIARKAQLLQRE 348
Cdd:COG0350    78 TPFQRRVWEALRKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSLGGYAGGLERKRALLELE 157
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
 269-348 1.09e-45

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: 150.54  E-value: 1.09e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661 269 TAFQQQVWQALRAIPCGETMSYQQLASAIGKPKAVRAVASACGANKLAIVIPCHRVIRGDGALSGYRWGIARKAQLLQRE 348
Cdd:TIGR00589   1 TPFQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLTGYGGGLERKEFLLEHE 80
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
 270-348 5.57e-44

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: 146.35  E-value: 5.57e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1004664661 270 AFQQQVWQALRAIPCGETMSYQQLASAIGKPKAVRAVASACGANKLAIVIPCHRVIRGDGALSGYRWGIARKAQLLQRE 348
Cdd:pfam01035   1 PFQRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSLGGYAGGLERKRALLELE 79
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
 271-348 8.44e-41

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: 138.00  E-value: 8.44e-41
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1004664661 271 FQQQVWQALRAIPCGETMSYQQLASAIGKPKAVRAVASACGANKLAIVIPCHRVIRGDGALSGYRWGIARKAQLLQRE 348
Cdd:cd06445     1 FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGLGGYRGGLERKRELLELE 78
Ada_Zn_binding pfam02805
Metal binding domain of Ada; The Escherichia coli Ada protein repairs O6-methylguanine ...
 12-72 8.90e-34

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: 119.09  E-value: 8.90e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1004664661  12 RWQSVLARDADADGQFVFAVQTTGIFCRPSCRAKHALRKNVCFFSDAQQAQAAGFRPCKRC 72
Cdd:pfam02805   2 RWQAVLARDPRADGSFFYAVKTTGIYCRPSCPARLPKRENVRFFDTAAEAEAAGFRPCKRC 62
PRK10286 PRK10286
methylated-DNA--[protein]-cysteine S-methyltransferase;
261-348 3.61e-31

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


Pssm-ID: 182355 [Multi-domain]  Cd Length: 171  Bit Score: 115.74  E-value: 3.61e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661 261 SLPLDIRGTAFQQQVWQALRAIPCGETMSYQQLASAIGKPKAVRAVASACGANKLAIVIPCHRVIRGDGALSGYRWGIAR 340
Cdd:PRK10286   79 TLPTATGGTPFQREVWQTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIGRNGTMTGYAGGVQR 158


                  ....*...
gi 1004664661 341 KAQLLQRE 348
Cdd:PRK10286  159 KEWLLRHE 166
PRK00901 PRK00901
methylated-DNA--protein-cysteine methyltransferase; Provisional
 262-348 5.35e-31

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 234860 [Multi-domain]  Cd Length: 155  Bit Score: 114.76  E-value: 5.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661 262 LPLDIRGTAFQQQVWQALRAIPCGETMSYQQLASAIGKPKAVRAVASACGANKLAIVIPCHRVIRGDGALSGYRWGIARK 341
Cdd:PRK00901   65 LPLAPQGTEFQKKVWKALQEIPYGETRSYKEIAVNIGNPKACRAVGLANNKNPIPIFIPCHRVIGANGKLVGYAGGLDIK 144


                  ....*..
gi 1004664661 342 AQLLQRE 348
Cdd:PRK00901  145 EKLLKLE 151
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
99-181 1.94e-22

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 89.53  E-value: 1.94e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661   99 PLTLDELAQQVAMSPYHLHRLFKATTGMTPKAWQQSWRARRLRDALAKG-VPVTQAILNAGFPDSSSYYRKADQTLGMTA 177
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTdLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 1004664661  178 KQFR 181
Cdd:smart00342  81 SEYR 84
Methyltransf_1N pfam02870
6-O-methylguanine DNA methyltransferase, ribonuclease-like domain; This entry represents the ...
 189-266 2.17e-19

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: 81.26  E-value: 2.17e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1004664661 189 VRYTLADCALGRCLVAESERGICAILLGDDDATLVADLHELFPAAQDVPADADFQQHVREVIAAINSrdASLSLPLDI 266
Cdd:pfam02870   2 LYYTLIDSPLGRLLLAGDERGLTAIDFLDKDYALRKELPKVLPQPELLPALALLVQALEEYFAGELK--PEFTLPLDQ 77
Atl1 COG3695
Alkylated DNA nucleotide flippase Atl1, participates in nucleotide excision repair, Ada-like ...
 271-348 1.46e-16

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


Pssm-ID: 442910  Cd Length: 104  Bit Score: 74.45  E-value: 1.46e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1004664661 271 FQQQVWQALRAIPCGETMSYQQLASAIGKPKAVRAVASACGANKLAIVIPCHRVIRGDGALS-GYRWGIARKAQLLQRE 348
Cdd:COG3695     6 FYERVYEVVAQIPPGRVATYGDIAALAGLPRGARQVGRALRALPEGSDLPWHRVVNADGRLSpGHAGGAEEQRELLEAE 84
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
79-183 1.76e-16

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 78.28  E-value: 1.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661  79 AQQHRLDKIARACQLLEHESPLTLDELAQQVAMSPYHLHRLFKATTGMTPKAWQQSWRARRLRDALAKG-VPVTQAILNA 157
Cdd:COG2207   148 LLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETdLSISEIAYEL 227

                          90       100
                  ....*....|....*....|....*.
gi 1004664661 158 GFPDSSSYYRKADQTLGMTAKQFRKG 183
Cdd:COG2207   228 GFSSQSHFSRAFKKRFGVTPSEYRKR 253
HTH_18 pfam12833
Helix-turn-helix domain;
105-182 1.22e-15

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 71.08  E-value: 1.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661 105 LAQQVAMSPYHLHRLFKATTGMTPKAWQQSWRARRLRDALAK--GVPVTQAILNAGFPDSSSYYRKADQTLGMTAKQFRK 182
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEdtGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 57-182 2.83e-15

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: 75.58  E-value: 2.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661  57 DAQQAQAAGFRPckrcqpdkdsAQQHRLDKIARACQLLEH--ESPLTLDELAQQVAMSPYHLHRLFKATTGMTPKAWQQS 134
Cdd:COG4977   192 PGGQAQFSPLLV----------PLGHRDPRLARAQAWMEAnlEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQR 261

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1004664661 135 WRARRLRDALAKG-VPVTQAILNAGFPDSSSY---YRKAdqtLGMTAKQFRK 182
Cdd:COG4977   262 LRLERARRLLETTdLSIEEIAAACGFGSASHFrraFRRR---FGVSPSAYRR 310
ftrA PRK09393
transcriptional activator FtrA; Provisional
 99-182 1.11e-10

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 61.90  E-value: 1.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661  99 PLTLDELAQQVAMSPYHLHRLFKATTGMTPKAWQQSWRARRLRDALAK-GVPVTQAILNAGFPDSSSYYRKADQTLGMTA 177
Cdd:PRK09393  234 PHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESsALSIDQIAERAGFGSEESLRHHFRRRAATSP 313


                  ....*
gi 1004664661 178 KQFRK 182
Cdd:PRK09393  314 AAYRK 318
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 93-133 1.89e-10

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: 55.24  E-value: 1.89e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1004664661  93 LLEHES-PLTLDELAQQVAMSPYHLHRLFKATTGMTPKAWQQ 133
Cdd:pfam00165   1 LRENLStNLTIADIADELGFSRSYFSRLFKKYTGVTPSQYRH 42
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
71-183 5.17e-06

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 47.66  E-value: 5.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661  71 RC-QPDKDSAQQHRLDKIARACQLL-EH-ESPLTLDELAQQVAMSPYHLHRLFKATTGMTPKAWQQSWRARRLRDALAK- 146
Cdd:PRK10572  168 RCmEAIPESLHPPMDPRVREACQYIsDHlASEFDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTt 247

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1004664661 147 GVPVTQAILNAGFPDS---SSYYRKadqTLGMTAKQFRKG 183
Cdd:PRK10572  248 RMPIATIGRNVGYDDQlyfSRVFKK---CTGASPSEFRAR 284
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
86-139 2.62e-05

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 45.16  E-value: 2.62e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1004664661  86 KIARACQLLEHeSPLTLDELAQQVAM-SPYHLHRLFKATTGMTPKAWQQSWRARR 139
Cdd:COG2207   205 RLERAKRLLAE-TDLSISEIAYELGFsSQSHFSRAFKKRFGVTPSEYRKRLRARA 258
PRK03887 PRK03887
methylated-DNA--protein-cysteine methyltransferase; Provisional
 269-354 3.78e-05

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 167628 [Multi-domain]  Cd Length: 175  Bit Score: 43.57  E-value: 3.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661 269 TAFQQQVWQAL-RAIPCGETMSYQQLASAIGKpkAVRAVASACGANKLAIVIPCHRVIRGDGaLSGYRWGIARKAQLLQR 347
Cdd:PRK03887   91 TPFERKVYEWLtKNVKRGEVITYGELAKALNT--SPRAVGGAMKRNPYPIIVPCHRVVGRKN-PGLYTPKPEYKKFLLEV 167


                  ....*..
gi 1004664661 348 ETTGEET 354
Cdd:PRK03887  168 EGVKEWT 174
HTH_18 pfam12833
Helix-turn-helix domain;
80-134 4.44e-05

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 41.42  E-value: 4.44e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1004664661  80 QQHRLDkiaRACQLLEHESPLTLDELAQQVAM-SPYHLHRLFKATTGMTPKAWQQS 134
Cdd:pfam12833  29 RRLRLE---RARRLLLEDTGLSVAEIALALGFsDASHFSRAFRRLFGLTPSEYRRR 81
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 80-139 5.35e-05

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: 44.38  E-value: 5.35e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1004664661  80 QQHRLDkiaRACQLLEHeSPLTLDELAQQVAM-SPYHLHRLFKATTGMTPKAWQQSWRARR 139
Cdd:COG4977   260 QRLRLE---RARRLLET-TDLSIEEIAAACGFgSASHFRRAFRRRFGVSPSAYRRRFRARA 316
PRK10371 PRK10371
transcriptional regulator MelR;
96-182 3.57e-04

transcriptional regulator MelR;


Pssm-ID: 182416 [Multi-domain]  Cd Length: 302  Bit Score: 41.73  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661  96 HESPLTLDELAQQVAMSPYHLHRLFKATTGMTPKAWQQSWRARRLRDALAK-GVPVTQAILNAGFPDSSSYYRKADQTLG 174
Cdd:PRK10371  204 YDQALTINDVAEHVKLNANYAMGIFQRVMQLTMKQYITAMRINHVRALLSDtDKSILDIALTAGFRSSSRFYSTFGKYVG 283


                  ....*...
gi 1004664661 175 MTAKQFRK 182
Cdd:PRK10371  284 MSPQQYRK 291
PRK11511 PRK11511
MDR efflux pump AcrAB transcriptional activator MarA;
97-180 5.74e-04

MDR efflux pump AcrAB transcriptional activator MarA;


Pssm-ID: 236920 [Multi-domain]  Cd Length: 127  Bit Score: 39.31  E-value: 5.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004664661  97 ESPLTLDELAQQVAMSPYHLHRLFKATTGmtpKAWQQSWRARRLRDALAKGVPVTQAILNAgfpdSSSYYRKADQTLGMT 176
Cdd:PRK11511   23 ESPLSLEKVSERSGYSKWHLQRMFKKETG---HSLGQYIRSRKMTEIAQKLKESNEPILYL----AERYGFESQQTLTRT 95


                  ....
gi 1004664661 177 AKQF 180
Cdd:PRK11511   96 FKNY 99
PRK15121 PRK15121
MDR efflux pump AcrAB transcriptional activator RobA;
99-143 3.49e-03

MDR efflux pump AcrAB transcriptional activator RobA;


Pssm-ID: 185076 [Multi-domain]  Cd Length: 289  Bit Score: 38.84  E-value: 3.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1004664661  99 PLTLDELAQQVAMSPYHLHRLFKATTGMTPKAWqqsWRARRLRDA 143
Cdd:PRK15121   21 PLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAY---IRARRLSKA 62
 
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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