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Conserved domains on  [gi|939620267|ref|NP_001303422|]
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O-6-alkylguanine-DNA alkyltransferase, isoform B [Drosophila melanogaster]

Protein Classification

methylated-DNA--[protein]-cysteine S-methyltransferase; MGMT family protein( domain architecture ID 12776258)

methylated-DNA--[protein]-cysteine S-methyltransferase is involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA; it repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme| MGMT (O-6-methylguanine DNA methyltransferase) family protein similar to Vibrio parahaemolyticus DNA base-flipping protein, which binds to the damaged base O(6)-methylguanine and flips the base out of the DNA duplex into an extrahelical conformation to allow processing by repair proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATase super family cl29527
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
 111-189 1.91e-33

The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT and MGMT) reverses O6-alkylation DNA damage by transferring O6-alkyl adducts to an active site cysteine irreversibly, without inducing DNA strand breaks. ATases are specific for repair of guanines with O6-alkyl adducts, however human ATase is not limited to O6-methylguanine, repairing many other adducts at the O6-position of guanine as well. ATase is widely distributed among species. Most ATases have N- and C-terminal domains. The C-terminal domain contains the conserved active-site cysteine motif (PCHR), the O6-alkylguanine binding channel, and the helix-turn-helix (HTH) DNA-binding motif. The active site is located near the recognition helix of the HTH motif. While the C-terminal domain of ATase contains residues that are necessary for DNA binding and alkyl transfer, the function of the N-terminal domain is still unknown. Removal of the N-terminal domain abolishes the activity of the C-terminal domain, suggesting an important structural role for the N-terminal domain in orienting the C-terminal domain for proper catalysis. Some ATase C-terminal domain homologs are either single-domain proteins that lack an N-terminal domain, or have a tryptophan substituted in place of the acceptor cysteine (i.e. the motif PCHR is replaced by PWHR). ATase null mutant mice are viable, fertile, and have a normal lifespan.


The actual alignment was detected with superfamily member TIGR00589:

Pssm-ID: 475221  Cd Length: 80  Bit Score: 114.33  E-value: 1.91e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620267  111 TDFQLSVWRALVHMKRGETCTYSQLAERMGRPTAVRAVASAVAKNELAILIPCHRVVSQNGA-SKYHWGAALKQLLLADE 189
Cdd:TIGR00589   1 TPFQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTlTGYGGGLERKEFLLEHE 80
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
 22-190 9.73e-31

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


:

Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 109.96  E-value: 9.73e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620267  22 TIRYSFLATKFGQMMmgvinpISGDSKdqvaiGVLHFVIKDnvSTYNEVQERWPKSELwKDDDAVKLVADKLFE--SDKE 99
Cdd:COG0350    1 TIRYAIFDTPLGPLL------IAATDR-----GLCALSFGD--DREEALLARFPAALR-EDPPLLAEAARQLDAyfAGER 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620267 100 NSQAIPIAIYGTDFQLSVWRALVHMKRGETCTYSQLAERMGRPTAVRAVASAVAKNELAILIPCHRVVSQNGA-SKYHWG 178
Cdd:COG0350   67 KDFDLPLDLRGTPFQRRVWEALRKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSlGGYAGG 146

                        170
                 ....*....|..
gi 939620267 179 AALKQLLLADEK 190
Cdd:COG0350  147 LERKRALLELEG 158
 
Name Accession Description Interval E-value
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
 111-189 1.91e-33

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: 114.33  E-value: 1.91e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620267  111 TDFQLSVWRALVHMKRGETCTYSQLAERMGRPTAVRAVASAVAKNELAILIPCHRVVSQNGA-SKYHWGAALKQLLLADE 189
Cdd:TIGR00589   1 TPFQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTlTGYGGGLERKEFLLEHE 80
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
 22-190 9.73e-31

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


Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 109.96  E-value: 9.73e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620267  22 TIRYSFLATKFGQMMmgvinpISGDSKdqvaiGVLHFVIKDnvSTYNEVQERWPKSELwKDDDAVKLVADKLFE--SDKE 99
Cdd:COG0350    1 TIRYAIFDTPLGPLL------IAATDR-----GLCALSFGD--DREEALLARFPAALR-EDPPLLAEAARQLDAyfAGER 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620267 100 NSQAIPIAIYGTDFQLSVWRALVHMKRGETCTYSQLAERMGRPTAVRAVASAVAKNELAILIPCHRVVSQNGA-SKYHWG 178
Cdd:COG0350   67 KDFDLPLDLRGTPFQRRVWEALRKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSlGGYAGG 146

                        170
                 ....*....|..
gi 939620267 179 AALKQLLLADEK 190
Cdd:COG0350  147 LERKRALLELEG 158
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
62-192 1.21e-24

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


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 98.33  E-value: 1.21e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620267  62 DNVSTYNEVQERWPKSELWKDDDAVKLVADKLFES--DKENSQAIPIAIYGTDFQLSVWRALVHMKRGETCTYSQLAERM 139
Cdd:PRK15435 218 DDAALISELQQMFPAADNAPADLTFQQHVREVIASlnQRDTPLTLPLDIRGTAFQQQVWQALRTIPCGETVSYQQLANAI 297

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 939620267 140 GRPTAVRAVASAVAKNELAILIPCHRVVSQNGA-SKYHWGAALKQLLLADEKSK 192
Cdd:PRK15435 298 GKPKAVRAVASACAANKLAIVIPCHRVVRGDGAlSGYRWGVSRKAQLLRREAEN 351
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
 112-190 1.54e-22

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: 86.26  E-value: 1.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620267  112 DFQLSVWRALVHMKRGETCTYSQLAERMGRPTAVRAVASAVAKNELAILIPCHRVVSQNGA-SKYHWGAALKQLLLADEK 190
Cdd:pfam01035   1 PFQRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSlGGYAGGLERKRALLELEG 80
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
 113-190 4.25e-22

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: 85.23  E-value: 4.25e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939620267 113 FQLSVWRALVHMKRGETCTYSQLAERMGRPTAVRAVASAVAKNELAILIPCHRVVSQNGA-SKYHWGAALKQLLLADEK 190
Cdd:cd06445    1 FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGlGGYRGGLERKRELLELEG 79
Atl1 COG3695
Alkylated DNA nucleotide flippase Atl1, participates in nucleotide excision repair, Ada-like ...
 111-189 7.74e-03

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


Pssm-ID: 442910  Cd Length: 104  Bit Score: 34.78  E-value: 7.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620267 111 TDFQLSVWRALVHMKRGETCTYSQLAERMGRPTAvravasavaknelA-----IL--------IPCHRVVSQNG--ASKY 175
Cdd:COG3695    4 EEFYERVYEVVAQIPPGRVATYGDIAALAGLPRG-------------ArqvgrALralpegsdLPWHRVVNADGrlSPGH 70

                         90
                 ....*....|....
gi 939620267 176 HWGAALKQLLLADE 189
Cdd:COG3695   71 AGGAEEQRELLEAE 84
 
Name Accession Description Interval E-value
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
 111-189 1.91e-33

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: 114.33  E-value: 1.91e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620267  111 TDFQLSVWRALVHMKRGETCTYSQLAERMGRPTAVRAVASAVAKNELAILIPCHRVVSQNGA-SKYHWGAALKQLLLADE 189
Cdd:TIGR00589   1 TPFQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTlTGYGGGLERKEFLLEHE 80
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
 22-190 9.73e-31

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


Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 109.96  E-value: 9.73e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620267  22 TIRYSFLATKFGQMMmgvinpISGDSKdqvaiGVLHFVIKDnvSTYNEVQERWPKSELwKDDDAVKLVADKLFE--SDKE 99
Cdd:COG0350    1 TIRYAIFDTPLGPLL------IAATDR-----GLCALSFGD--DREEALLARFPAALR-EDPPLLAEAARQLDAyfAGER 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620267 100 NSQAIPIAIYGTDFQLSVWRALVHMKRGETCTYSQLAERMGRPTAVRAVASAVAKNELAILIPCHRVVSQNGA-SKYHWG 178
Cdd:COG0350   67 KDFDLPLDLRGTPFQRRVWEALRKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSlGGYAGG 146

                        170
                 ....*....|..
gi 939620267 179 AALKQLLLADEK 190
Cdd:COG0350  147 LERKRALLELEG 158
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
62-192 1.21e-24

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


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 98.33  E-value: 1.21e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620267  62 DNVSTYNEVQERWPKSELWKDDDAVKLVADKLFES--DKENSQAIPIAIYGTDFQLSVWRALVHMKRGETCTYSQLAERM 139
Cdd:PRK15435 218 DDAALISELQQMFPAADNAPADLTFQQHVREVIASlnQRDTPLTLPLDIRGTAFQQQVWQALRTIPCGETVSYQQLANAI 297

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 939620267 140 GRPTAVRAVASAVAKNELAILIPCHRVVSQNGA-SKYHWGAALKQLLLADEKSK 192
Cdd:PRK15435 298 GKPKAVRAVASACAANKLAIVIPCHRVVRGDGAlSGYRWGVSRKAQLLRREAEN 351
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
 112-190 1.54e-22

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: 86.26  E-value: 1.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620267  112 DFQLSVWRALVHMKRGETCTYSQLAERMGRPTAVRAVASAVAKNELAILIPCHRVVSQNGA-SKYHWGAALKQLLLADEK 190
Cdd:pfam01035   1 PFQRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSlGGYAGGLERKRALLELEG 80
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
 113-190 4.25e-22

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: 85.23  E-value: 4.25e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939620267 113 FQLSVWRALVHMKRGETCTYSQLAERMGRPTAVRAVASAVAKNELAILIPCHRVVSQNGA-SKYHWGAALKQLLLADEK 190
Cdd:cd06445    1 FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGlGGYRGGLERKRELLELEG 79
PRK00901 PRK00901
methylated-DNA--protein-cysteine methyltransferase; Provisional
 98-193 4.25e-21

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 234860 [Multi-domain]  Cd Length: 155  Bit Score: 84.72  E-value: 4.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620267  98 KENSQAIPIAIYGTDFQLSVWRALVHMKRGETCTYSQLAERMGRPTAVRAVASAVAKNELAILIPCHRVVSQNGA-SKYH 176
Cdd:PRK00901  59 KRKKFDLPLAPQGTEFQKKVWKALQEIPYGETRSYKEIAVNIGNPKACRAVGLANNKNPIPIFIPCHRVIGANGKlVGYA 138

                         90
                 ....*....|....*..
gi 939620267 177 WGAALKQLLLADEKSKN 193
Cdd:PRK00901 139 GGLDIKEKLLKLEKENS 155
PRK10286 PRK10286
methylated-DNA--[protein]-cysteine S-methyltransferase;
89-189 9.56e-16

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


Pssm-ID: 182355 [Multi-domain]  Cd Length: 171  Bit Score: 71.44  E-value: 9.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620267  89 VADKL---FESDKENSQAIPIAIYGTDFQLSVWRALVHMKRGETCTYSQLAERMGRPTAVRAVASAVAKNELAILIPCHR 165
Cdd:PRK10286  62 LSDKLrdyFAGNLSIIDTLPTATGGTPFQREVWQTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHR 141

                         90       100
                 ....*....|....*....|....*
gi 939620267 166 VVSQNGA-SKYHWGAALKQLLLADE 189
Cdd:PRK10286 142 VIGRNGTmTGYAGGVQRKEWLLRHE 166
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 24-189 4.42e-15

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: 72.01  E-value: 4.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620267  24 RYSFLATKFGQMMMGVinpisgdskDQVAIGVLHFVI-KDNVSTYNEVQERWPKSELWKDDDAVKLVADKL--FESDKEN 100
Cdd:COG2169  189 AIRFAPTPCSLGLLLV---------AASARGVCAILLgDDPEALLRDLQDRFPAAELIGGDAAFEQLVAEVvgFVEGPLL 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620267 101 SQAIPIAIYGTDFQLSVWRALVHMKRGETCTYSQLAERMGRPTAVRAVASAVAKNELAILIPCHRVVSQNGA-SKYHWGA 179
Cdd:COG2169  260 GLDLPLDLRGTAFQQRVWQALRAIPAGETASYAEIAARIGAPKAVRAVAAACAANQLAVAIPCHRVVRADGAlSGYRWGV 339

                        170
                 ....*....|
gi 939620267 180 ALKQLLLADE 189
Cdd:COG2169  340 ERKRALLERE 349
PRK03887 PRK03887
methylated-DNA--protein-cysteine methyltransferase; Provisional
 111-194 3.05e-07

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 167628 [Multi-domain]  Cd Length: 175  Bit Score: 48.19  E-value: 3.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620267 111 TDFQLSVWRALV-HMKRGETCTYSQLAERMGrpTAVRAVASAVAKNELAILIPCHRVVSQNGASKYHWGAALKQLLLADE 189
Cdd:PRK03887  91 TPFERKVYEWLTkNVKRGEVITYGELAKALN--TSPRAVGGAMKRNPYPIIVPCHRVVGRKNPGLYTPKPEYKKFLLEVE 168


                 ....*
gi 939620267 190 KSKNY 194
Cdd:PRK03887 169 GVKEW 173
Atl1 COG3695
Alkylated DNA nucleotide flippase Atl1, participates in nucleotide excision repair, Ada-like ...
 111-189 7.74e-03

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


Pssm-ID: 442910  Cd Length: 104  Bit Score: 34.78  E-value: 7.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620267 111 TDFQLSVWRALVHMKRGETCTYSQLAERMGRPTAvravasavaknelA-----IL--------IPCHRVVSQNG--ASKY 175
Cdd:COG3695    4 EEFYERVYEVVAQIPPGRVATYGDIAALAGLPRG-------------ArqvgrALralpegsdLPWHRVVNADGrlSPGH 70

                         90
                 ....*....|....
gi 939620267 176 HWGAALKQLLLADE 189
Cdd:COG3695   71 AGGAEEQRELLEAE 84
 
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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