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Conserved domains on  [gi|446633029|ref|WP_000710375|]
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MULTISPECIES: bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada [Enterobacteriaceae]

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: 691.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029   1 MKKATCLTDDQRWQSVLARDPNADGEFVFAVRTTGIFCRPSCRARHALRENVSFYANASEALAAGFRPCKRCQPEKANAQ 80
Cdd:PRK15435   1 MKNATCLTDDQRWQSVLARDPNADGEFVFAVRTTGIFCRPSCRARHALRENVRFYANASEALAAGFRPCKRCQPDKANPQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029  81 QHRLDKITHACRLLEQETPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLRESLAKGESVTTSILNAGFP 160
Cdd:PRK15435  81 QHRLDKITHACRLLEQETPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLREALAKGESVTTSILNAGFP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029 161 DSSSYYRKADETLGMTAKQFRHGGENLAVRYALADCELGRCLVAESERGICAILLGDDDATLISELQQMFPAADNAPADL 240
Cdd:PRK15435 161 DSSSYYRKADETLGMTAKQFRHGGENLAVRYALADCELGRCLVAESERGICAILLGDDDAALISELQQMFPAADNAPADL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029 241 MFQQHVREVIASLNQRDTPLTLPLDIRGTAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIIIP 320
Cdd:PRK15435 241 TFQQHVREVIASLNQRDTPLTLPLDIRGTAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIVIP 320

                        330       340       350
                 ....*....|....*....|....*....|...
gi 446633029 321 CHRVVRGDGTLSGYRWGVSRKAQLLRREAENEE 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: 691.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029   1 MKKATCLTDDQRWQSVLARDPNADGEFVFAVRTTGIFCRPSCRARHALRENVSFYANASEALAAGFRPCKRCQPEKANAQ 80
Cdd:PRK15435   1 MKNATCLTDDQRWQSVLARDPNADGEFVFAVRTTGIFCRPSCRARHALRENVRFYANASEALAAGFRPCKRCQPDKANPQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029  81 QHRLDKITHACRLLEQETPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLRESLAKGESVTTSILNAGFP 160
Cdd:PRK15435  81 QHRLDKITHACRLLEQETPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLREALAKGESVTTSILNAGFP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029 161 DSSSYYRKADETLGMTAKQFRHGGENLAVRYALADCELGRCLVAESERGICAILLGDDDATLISELQQMFPAADNAPADL 240
Cdd:PRK15435 161 DSSSYYRKADETLGMTAKQFRHGGENLAVRYALADCELGRCLVAESERGICAILLGDDDAALISELQQMFPAADNAPADL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029 241 MFQQHVREVIASLNQRDTPLTLPLDIRGTAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIIIP 320
Cdd:PRK15435 241 TFQQHVREVIASLNQRDTPLTLPLDIRGTAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIVIP 320

                        330       340       350
                 ....*....|....*....|....*....|...
gi 446633029 321 CHRVVRGDGTLSGYRWGVSRKAQLLRREAENEE 353
Cdd:PRK15435 321 CHRVVRGDGALSGYRWGVSRKAQLLRREAENEE 353
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 1-353 1.40e-149

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: 425.62  E-value: 1.40e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029   1 MKKATcLTDDQRWQSVLARDPNADGEFVFAVRTTGIFCRPSCRARHALRENVSFYANASEALAAGFRPCKRCQPEKANAQ 80
Cdd:COG2169    1 MTTDL-LDDDERWQAVLARDARFDGRFFYGVKTTGIYCRPSCPARKPKRENVRFFATAAAAEAAGFRPCKRCRPDLAPGS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029  81 QHRLDKITHACRLLEQ--ETPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLRESLAKGESVTTSILNAG 158
Cdd:COG2169   80 PPRADLVARACRLIEAgaEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLLQTGLSVTDAAYAAG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029 159 FPDSSSYYRKADETLGMTAKQFRHGGENLAVRYALADCELGRCLVAESERGICAILLGDDDATLISELQQMFPAADNAPA 238
Cdd:COG2169  160 FGSLSRFYEAFKKLLGMTPSAYRRGGAGAAIRFAPTPCSLGLLLVAASARGVCAILLGDDPEALLRDLQDRFPAAELIGG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029 239 DLMFQQHVREVIASLNQRDTPLTLPLDIRGTAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAII 318
Cdd:COG2169  240 DAAFEQLVAEVVGFVEGPLLGLDLPLDLRGTAFQQRVWQALRAIPAGETASYAEIAARIGAPKAVRAVAAACAANQLAVA 319

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 446633029 319 IPCHRVVRGDGTLSGYRWGVSRKAQLLRREAENEE 353
Cdd:COG2169  320 IPCHRVVRADGALSGYRWGVERKRALLEREAAAAA 354
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
 269-348 2.35e-46

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: 152.47  E-value: 2.35e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029  269 TAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIIIPCHRVVRGDGTLSGYRWGVSRKAQLLRRE 348
Cdd:TIGR00589   1 TPFQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLTGYGGGLERKEFLLEHE 80
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
 270-349 3.26e-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: 146.74  E-value: 3.26e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029  270 AFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIIIPCHRVVRGDGTLSGYRWGVSRKAQLLRREA 349
Cdd:pfam01035   1 PFQRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSLGGYAGGLERKRALLELEG 80
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
 271-348 1.62e-40

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: 137.23  E-value: 1.62e-40
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446633029 271 FQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIIIPCHRVVRGDGTLSGYRWGVSRKAQLLRRE 348
Cdd:cd06445    1 FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGLGGYRGGLERKRELLELE 78
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
99-181 1.19e-21

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 87.61  E-value: 1.19e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029    99 PVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLRESLAKGE-SVTTSILNAGFPDSSSYYRKADETLGMTA 177
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDlSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 446633029   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: 691.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029   1 MKKATCLTDDQRWQSVLARDPNADGEFVFAVRTTGIFCRPSCRARHALRENVSFYANASEALAAGFRPCKRCQPEKANAQ 80
Cdd:PRK15435   1 MKNATCLTDDQRWQSVLARDPNADGEFVFAVRTTGIFCRPSCRARHALRENVRFYANASEALAAGFRPCKRCQPDKANPQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029  81 QHRLDKITHACRLLEQETPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLRESLAKGESVTTSILNAGFP 160
Cdd:PRK15435  81 QHRLDKITHACRLLEQETPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLREALAKGESVTTSILNAGFP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029 161 DSSSYYRKADETLGMTAKQFRHGGENLAVRYALADCELGRCLVAESERGICAILLGDDDATLISELQQMFPAADNAPADL 240
Cdd:PRK15435 161 DSSSYYRKADETLGMTAKQFRHGGENLAVRYALADCELGRCLVAESERGICAILLGDDDAALISELQQMFPAADNAPADL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029 241 MFQQHVREVIASLNQRDTPLTLPLDIRGTAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIIIP 320
Cdd:PRK15435 241 TFQQHVREVIASLNQRDTPLTLPLDIRGTAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIVIP 320

                        330       340       350
                 ....*....|....*....|....*....|...
gi 446633029 321 CHRVVRGDGTLSGYRWGVSRKAQLLRREAENEE 353
Cdd:PRK15435 321 CHRVVRGDGALSGYRWGVSRKAQLLRREAENEE 353
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 1-353 1.40e-149

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: 425.62  E-value: 1.40e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029   1 MKKATcLTDDQRWQSVLARDPNADGEFVFAVRTTGIFCRPSCRARHALRENVSFYANASEALAAGFRPCKRCQPEKANAQ 80
Cdd:COG2169    1 MTTDL-LDDDERWQAVLARDARFDGRFFYGVKTTGIYCRPSCPARKPKRENVRFFATAAAAEAAGFRPCKRCRPDLAPGS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029  81 QHRLDKITHACRLLEQ--ETPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLRESLAKGESVTTSILNAG 158
Cdd:COG2169   80 PPRADLVARACRLIEAgaEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLLQTGLSVTDAAYAAG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029 159 FPDSSSYYRKADETLGMTAKQFRHGGENLAVRYALADCELGRCLVAESERGICAILLGDDDATLISELQQMFPAADNAPA 238
Cdd:COG2169  160 FGSLSRFYEAFKKLLGMTPSAYRRGGAGAAIRFAPTPCSLGLLLVAASARGVCAILLGDDPEALLRDLQDRFPAAELIGG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029 239 DLMFQQHVREVIASLNQRDTPLTLPLDIRGTAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAII 318
Cdd:COG2169  240 DAAFEQLVAEVVGFVEGPLLGLDLPLDLRGTAFQQRVWQALRAIPAGETASYAEIAARIGAPKAVRAVAAACAANQLAVA 319

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 446633029 319 IPCHRVVRGDGTLSGYRWGVSRKAQLLRREAENEE 353
Cdd:COG2169  320 IPCHRVVRADGALSGYRWGVERKRALLEREAAAAA 354
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
 188-354 7.70e-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: 215.51  E-value: 7.70e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029 188 AVRYALADCELGRCLVAESERGICAILLGDDDAtliSELQQMFPAADNAPADLmFQQHVREVIASLNQRDTPLTLPLDIR 267
Cdd:COG0350    1 TIRYAIFDTPLGPLLIAATDRGLCALSFGDDRE---EALLARFPAALREDPPL-LAEAARQLDAYFAGERKDFDLPLDLR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029 268 GTAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIIIPCHRVVRGDGTLSGYRWGVSRKAQLLRR 347
Cdd:COG0350   77 GTPFQRRVWEALRKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSLGGYAGGLERKRALLEL 156


                 ....*..
gi 446633029 348 EAENEER 354
Cdd:COG0350  157 EGALAAA 163
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
 269-348 2.35e-46

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: 152.47  E-value: 2.35e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029  269 TAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIIIPCHRVVRGDGTLSGYRWGVSRKAQLLRRE 348
Cdd:TIGR00589   1 TPFQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLTGYGGGLERKEFLLEHE 80
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
 270-349 3.26e-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: 146.74  E-value: 3.26e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029  270 AFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIIIPCHRVVRGDGTLSGYRWGVSRKAQLLRREA 349
Cdd:pfam01035   1 PFQRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSLGGYAGGLERKRALLELEG 80
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
 271-348 1.62e-40

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: 137.23  E-value: 1.62e-40
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446633029 271 FQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIIIPCHRVVRGDGTLSGYRWGVSRKAQLLRRE 348
Cdd:cd06445    1 FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGLGGYRGGLERKRELLELE 78
Ada_Zn_binding pfam02805
Metal binding domain of Ada; The Escherichia coli Ada protein repairs O6-methylguanine ...
 11-72 4.40e-36

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: 125.25  E-value: 4.40e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446633029   11 QRWQSVLARDPNADGEFVFAVRTTGIFCRPSCRARHALRENVSFYANASEALAAGFRPCKRC 72
Cdd:pfam02805   1 ARWQAVLARDPRADGSFFYAVKTTGIYCRPSCPARLPKRENVRFFDTAAEAEAAGFRPCKRC 62
PRK00901 PRK00901
methylated-DNA--protein-cysteine methyltransferase; Provisional
 261-351 8.34e-32

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 234860 [Multi-domain]  Cd Length: 155  Bit Score: 117.08  E-value: 8.34e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029 261 TLPLDIRGTAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIIIPCHRVVRGDGTLSGYRWGVSR 340
Cdd:PRK00901  64 DLPLAPQGTEFQKKVWKALQEIPYGETRSYKEIAVNIGNPKACRAVGLANNKNPIPIFIPCHRVIGANGKLVGYAGGLDI 143

                         90
                 ....*....|.
gi 446633029 341 KAQLLRREAEN 351
Cdd:PRK00901 144 KEKLLKLEKEN 154
PRK10286 PRK10286
methylated-DNA--[protein]-cysteine S-methyltransferase;
261-348 1.10e-30

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


Pssm-ID: 182355 [Multi-domain]  Cd Length: 171  Bit Score: 114.58  E-value: 1.10e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029 261 TLPLDIRGTAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIIIPCHRVVRGDGTLSGYRWGVSR 340
Cdd:PRK10286  79 TLPTATGGTPFQREVWQTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIGRNGTMTGYAGGVQR 158


                 ....*...
gi 446633029 341 KAQLLRRE 348
Cdd:PRK10286 159 KEWLLRHE 166
Methyltransf_1N pfam02870
6-O-methylguanine DNA methyltransferase, ribonuclease-like domain; This entry represents the ...
 188-266 2.47e-23

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: 92.04  E-value: 2.47e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446633029  188 AVRYALADCELGRCLVAESERGICAILLGDDDATLISELQQMFPAADNAPADLMFQQHVREVIASLNQrdTPLTLPLDI 266
Cdd:pfam02870   1 ALYYTLIDSPLGRLLLAGDERGLTAIDFLDKDYALRKELPKVLPQPELLPALALLVQALEEYFAGELK--PEFTLPLDQ 77
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
99-181 1.19e-21

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 87.61  E-value: 1.19e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029    99 PVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLRESLAKGE-SVTTSILNAGFPDSSSYYRKADETLGMTA 177
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDlSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 446633029   178 KQFR 181
Cdd:smart00342  81 SEYR 84
Atl1 COG3695
Alkylated DNA nucleotide flippase Atl1, participates in nucleotide excision repair, Ada-like ...
 271-348 1.88e-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: 74.07  E-value: 1.88e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446633029 271 FQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIIIPCHRVVRGDGTLS-GYRWGVSRKAQLLRRE 348
Cdd:COG3695    6 FYERVYEVVAQIPPGRVATYGDIAALAGLPRGARQVGRALRALPEGSDLPWHRVVNADGRLSpGHAGGAEEQRELLEAE 84
HTH_18 pfam12833
Helix-turn-helix domain;
105-181 7.60e-14

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 66.07  E-value: 7.60e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446633029  105 LADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLRESLAK--GESVTTSILNAGFPDSSSYYRKADETLGMTAKQFR 181
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEdtGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYR 79
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
79-188 4.38e-13

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 68.27  E-value: 4.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029  79 AQQHRLDKITHACRLLEQETPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLRESLAKGE-SVTTSILNA 157
Cdd:COG2207  148 LLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDlSISEIAYEL 227

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446633029 158 GFPDSSSYYRKADETLGMTAKQFRHGGENLA 188
Cdd:COG2207  228 GFSSQSHFSRAFKKRFGVTPSEYRKRLRARA 258
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 79-181 9.15e-13

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: 68.26  E-value: 9.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029  79 AQQHRLDKITHACRLLEQ--ETPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLRESLAKGE-SVTTSIL 155
Cdd:COG4977  204 PLGHRDPRLARAQAWMEAnlEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDlSIEEIAA 283

                         90       100
                 ....*....|....*....|....*....
gi 446633029 156 NAGFPDSSSY---YRKAdetLGMTAKQFR 181
Cdd:COG4977  284 ACGFGSASHFrraFRRR---FGVSPSAYR 309
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 98-133 9.11e-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: 53.31  E-value: 9.11e-10
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 446633029   98 TPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQ 133
Cdd:pfam00165   7 TNLTIADIADELGFSRSYFSRLFKKYTGVTPSQYRH 42
ftrA PRK09393
transcriptional activator FtrA; Provisional
 99-181 8.99e-08

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 53.04  E-value: 8.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029  99 PVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLRESLakgESVTTSI----LNAGFPDSSSYYRKADETLG 174
Cdd:PRK09393 234 PHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLL---ESSALSIdqiaERAGFGSEESLRHHFRRRAA 310


                 ....*..
gi 446633029 175 MTAKQFR 181
Cdd:PRK09393 311 TSPAAYR 317
PRK03887 PRK03887
methylated-DNA--protein-cysteine methyltransferase; Provisional
 269-352 1.16e-05

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 167628 [Multi-domain]  Cd Length: 175  Bit Score: 45.11  E-value: 1.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029 269 TAFQQQVWQAL-RTIPCGETVSYQQLANAIGKpkAVRAVASACAANKLAIIIPCHRVVRGDGtLSGYRWGVSRKAQLLRR 347
Cdd:PRK03887  91 TPFERKVYEWLtKNVKRGEVITYGELAKALNT--SPRAVGGAMKRNPYPIIVPCHRVVGRKN-PGLYTPKPEYKKFLLEV 167


                 ....*
gi 446633029 348 EAENE 352
Cdd:PRK03887 168 EGVKE 172
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
100-183 2.91e-05

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 45.05  E-value: 2.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029 100 VTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWR---ARR-LRESlakGESVTTSILNAGFPDS---SSYYRKAdet 172
Cdd:PRK13503 188 VNWEALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRllkARHlLRHS---DASVTDIAYRCGFGDSnhfSTLFRRE--- 261

                         90
                 ....*....|.
gi 446633029 173 LGMTAKQFRHG 183
Cdd:PRK13503 262 FSWSPRDIRQG 272
HTH_18 pfam12833
Helix-turn-helix domain;
80-134 9.44e-05

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 40.27  E-value: 9.44e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446633029   80 QQHRLDkitHACRLLEQETPVTLEALADQVAM-SPFHLHRLFKATTGMTPKAWQQA 134
Cdd:pfam12833  29 RRLRLE---RARRLLLEDTGLSVAEIALALGFsDASHFSRAFRRLFGLTPSEYRRR 81
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
59-168 9.86e-05

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 43.42  E-value: 9.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029  59 SEALAAGF--RPCKRCQPEKANAQQHRLD-KITHACRL----LEQEtpVTLEALADQVAMSPFHLHRLFKATTGMTPKAW 131
Cdd:PRK10572 154 SELLAMNLleRLLLRCMEAIPESLHPPMDpRVREACQYisdhLASE--FDIESVAQHVCLSPSRLAHLFRQQLGISVLRW 231

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446633029 132 ---QQAWRARRLRESlaKGESVTTSILNAGFPDS---SSYYRK 168
Cdd:PRK10572 232 redQRISRAKLLLQT--TRMPIATIGRNVGYDDQlyfSRVFKK 272
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 80-139 5.71e-04

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: 41.30  E-value: 5.71e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446633029  80 QQHRLDkitHACRLLEQeTPVTLEALADQVAM-SPFHLHRLFKATTGMTPKAWQQAWRARR 139
Cdd:COG4977  260 QRLRLE---RARRLLET-TDLSIEEIAAACGFgSASHFRRAFRRRFGVSPSAYRRRFRARA 316
PRK10371 PRK10371
transcriptional regulator MelR;
99-181 8.27e-04

transcriptional regulator MelR;


Pssm-ID: 182416 [Multi-domain]  Cd Length: 302  Bit Score: 40.57  E-value: 8.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633029  99 PVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLRESLAKGE-SVTTSILNAGFPDSSSYYRKADETLGMTA 177
Cdd:PRK10371 207 ALTINDVAEHVKLNANYAMGIFQRVMQLTMKQYITAMRINHVRALLSDTDkSILDIALTAGFRSSSRFYSTFGKYVGMSP 286


                 ....
gi 446633029 178 KQFR 181
Cdd:PRK10371 287 QQYR 290
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 140-182 5.74e-03

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: 34.44  E-value: 5.74e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 446633029  140 LRESLAKGESVTTSILNAGFpDSSSYYRKADETLGMTAKQFRH 182
Cdd:pfam00165   1 LRENLSTNLTIADIADELGF-SRSYFSRLFKKYTGVTPSQYRH 42
 
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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