NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1304178124|gb|PKC50036|]
View 

DNA-3-methyladenine glycosylase [Plasmodium falciparum NF54]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Mpg super family cl43601
3-methyladenine DNA glycosylase Mpg [Replication, recombination and repair];
90-218 1.66e-33

3-methyladenine DNA glycosylase Mpg [Replication, recombination and repair];


The actual alignment was detected with superfamily member COG2094:

Pssm-ID: 441697  Cd Length: 193  Bit Score: 125.23  E-value: 1.66e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304178124  90 KILNENFYLKDdVLYITEILIGHILwVFDEKQNKLYGsRIIELESYNGVNDKASHAYNNRkTNRNMSMFEKGGISYVYLC 169
Cdd:COG2094     3 RPLPRDFFARD-ALEVARDLLGKVL-VRETDGGTVAG-RIVETEAYLGPDDPASHAYRGR-TPRNAVMFGPPGHAYVYFI 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1304178124 170 YGIHNCLNIVTNIQNIPDAILVRSTEPLYNIEYFLSNKFEKISQYLLSN 218
Cdd:COG2094    79 YGMHWCLNVVTGPEGEPSAVLIRAGEPVEGIELMRARRGKARKDRDLAN 127
 
Name Accession Description Interval E-value
Mpg COG2094
3-methyladenine DNA glycosylase Mpg [Replication, recombination and repair];
90-218 1.66e-33

3-methyladenine DNA glycosylase Mpg [Replication, recombination and repair];


Pssm-ID: 441697  Cd Length: 193  Bit Score: 125.23  E-value: 1.66e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304178124  90 KILNENFYLKDdVLYITEILIGHILwVFDEKQNKLYGsRIIELESYNGVNDKASHAYNNRkTNRNMSMFEKGGISYVYLC 169
Cdd:COG2094     3 RPLPRDFFARD-ALEVARDLLGKVL-VRETDGGTVAG-RIVETEAYLGPDDPASHAYRGR-TPRNAVMFGPPGHAYVYFI 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1304178124 170 YGIHNCLNIVTNIQNIPDAILVRSTEPLYNIEYFLSNKFEKISQYLLSN 218
Cdd:COG2094    79 YGMHWCLNVVTGPEGEPSAVLIRAGEPVEGIELMRARRGKARKDRDLAN 127
Pur_DNA_glyco pfam02245
Methylpurine-DNA glycosylase (MPG); Methylpurine-DNA glycosylase is a base excision-repair ...
109-218 1.87e-30

Methylpurine-DNA glycosylase (MPG); Methylpurine-DNA glycosylase is a base excision-repair protein. It is responsible for the hydrolysis of the deoxyribose N-glycosidic bond, excising 3-methyladenine and 3-methylguanine from damaged DNA.


Pssm-ID: 460506  Cd Length: 182  Bit Score: 116.78  E-value: 1.87e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304178124 109 LIGHILWVfdeKQNKLYGsRIIELESYNGVNDKASHAYNNRkTNRNMSMFEKGGISYVYLCYGIHNCLNIVTNIQNIPDA 188
Cdd:pfam02245  14 LLGKVLVR---RLPRLAG-RIVETEAYLGPEDPASHAYRGR-TPRNAVMFGPPGHAYVYLIYGMHHCLNVVTGPEGVPAA 88
                          90       100       110
                  ....*....|....*....|....*....|
gi 1304178124 189 ILVRSTEPLYNIEYFLSNKFEKISQYLLSN 218
Cdd:pfam02245  89 VLIRALEPVEGLELMRARRGGARKDRDLTN 118
AAG cd00540
Alkyladenine DNA glycosylase catalyzes the first step in base excision repair; Alkyladenine ...
109-201 2.87e-30

Alkyladenine DNA glycosylase catalyzes the first step in base excision repair; Alkyladenine DNA glycosylase (AAG), also known as 3-methyladenine DNA glycosylase, catalyzes the first step in base excision repair (BER) by cleaving damaged DNA bases within double-stranded DNA to produce an abasic site. AAG bends DNA by intercalating between the base pairs, causing the damaged base to flip out of the double helix and into the enzyme active site for cleavage. Although AAG represents one of six DNA glycosylase classes, it lacks the helix-hairpin-helix active site motif associated with other BER glycosylases and is structurally distinct from them.


Pssm-ID: 187726  Cd Length: 187  Bit Score: 116.47  E-value: 2.87e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304178124 109 LIGHILWVfdEKQNKLYGSRIIELESYNGVNDKASHAYNNRKTnRNMSMFEKGGISYVYLCYGIHNCLNIVTNIQNIPDA 188
Cdd:cd00540    13 LLGKVLVR--RLPGGVLSGRIVETEAYLGPDDPASHAYRGRTT-RREAMFGPPGTAYVYLIYGMHHCLNVVTGPEGEPAA 89
                          90
                  ....*....|...
gi 1304178124 189 ILVRSTEPLYNIE 201
Cdd:cd00540    90 VLIRALEPLEGLD 102
PRK00802 PRK00802
DNA-3-methyladenine glycosylase;
88-218 1.28e-27

DNA-3-methyladenine glycosylase;


Pssm-ID: 234840  Cd Length: 188  Bit Score: 109.15  E-value: 1.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304178124  88 PLKILNENFYLKDdVLYITEILIGHILWVfdekQNKLYGsRIIELESYNGVNDKASHAYNNRkTNRNMSMFEKGGISYVY 167
Cdd:PRK00802    1 MGMPLPREFFARD-ALEVARDLLGKVLVH----EGGVSG-RIVETEAYIGADDPASHSYRGR-TPRTEVMFGPPGHAYVY 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1304178124 168 LCYGIHNCLNIVTNIQNIPDAILVRSTEPLYNIEYFLSNKFEKISQYLLSN 218
Cdd:PRK00802   74 FIYGMHHCLNVVCGPEGTGAAVLIRALEPLEGIALMRRRRGGKRPEKNLCN 124
3mg TIGR00567
DNA-3-methyladenine glycosylase; This families are based on the phylogenomic analysis of JA ...
92-201 9.92e-25

DNA-3-methyladenine glycosylase; This families are based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). All proteins in this family for which the function is known are involved in the base excision repair of alkylation damage to DNA. The exact specificty of the type of alkylation damage repaired by each of these varies somewhat between species. Substrates include 3-methyl adenine, 7-methyl-guanaine, and 3-methyl-guanine. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273145  Cd Length: 192  Bit Score: 101.04  E-value: 9.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304178124  92 LNENFYLKDdVLYITEILIGHILWVFDEKQNKLYGsRIIELESYNGVNDKASHAYNNRKTNRNMSMFEKGGISYVYLCYG 171
Cdd:TIGR00567   1 MPPEFFQID-AVTLAPRLLGALLVRRLDDGTGVRG-RIVETEAYMGPPDSAAHSYGGRQTPRTDVMFGPPGRLYVYLIYG 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 1304178124 172 IHNCLNIVTNIQNIPDAILVRSTEPLYNIE 201
Cdd:TIGR00567  79 IHYMLNVVAAPEGVPAAVLIRAAEPESGAE 108
 
Name Accession Description Interval E-value
Mpg COG2094
3-methyladenine DNA glycosylase Mpg [Replication, recombination and repair];
90-218 1.66e-33

3-methyladenine DNA glycosylase Mpg [Replication, recombination and repair];


Pssm-ID: 441697  Cd Length: 193  Bit Score: 125.23  E-value: 1.66e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304178124  90 KILNENFYLKDdVLYITEILIGHILwVFDEKQNKLYGsRIIELESYNGVNDKASHAYNNRkTNRNMSMFEKGGISYVYLC 169
Cdd:COG2094     3 RPLPRDFFARD-ALEVARDLLGKVL-VRETDGGTVAG-RIVETEAYLGPDDPASHAYRGR-TPRNAVMFGPPGHAYVYFI 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1304178124 170 YGIHNCLNIVTNIQNIPDAILVRSTEPLYNIEYFLSNKFEKISQYLLSN 218
Cdd:COG2094    79 YGMHWCLNVVTGPEGEPSAVLIRAGEPVEGIELMRARRGKARKDRDLAN 127
Pur_DNA_glyco pfam02245
Methylpurine-DNA glycosylase (MPG); Methylpurine-DNA glycosylase is a base excision-repair ...
109-218 1.87e-30

Methylpurine-DNA glycosylase (MPG); Methylpurine-DNA glycosylase is a base excision-repair protein. It is responsible for the hydrolysis of the deoxyribose N-glycosidic bond, excising 3-methyladenine and 3-methylguanine from damaged DNA.


Pssm-ID: 460506  Cd Length: 182  Bit Score: 116.78  E-value: 1.87e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304178124 109 LIGHILWVfdeKQNKLYGsRIIELESYNGVNDKASHAYNNRkTNRNMSMFEKGGISYVYLCYGIHNCLNIVTNIQNIPDA 188
Cdd:pfam02245  14 LLGKVLVR---RLPRLAG-RIVETEAYLGPEDPASHAYRGR-TPRNAVMFGPPGHAYVYLIYGMHHCLNVVTGPEGVPAA 88
                          90       100       110
                  ....*....|....*....|....*....|
gi 1304178124 189 ILVRSTEPLYNIEYFLSNKFEKISQYLLSN 218
Cdd:pfam02245  89 VLIRALEPVEGLELMRARRGGARKDRDLTN 118
AAG cd00540
Alkyladenine DNA glycosylase catalyzes the first step in base excision repair; Alkyladenine ...
109-201 2.87e-30

Alkyladenine DNA glycosylase catalyzes the first step in base excision repair; Alkyladenine DNA glycosylase (AAG), also known as 3-methyladenine DNA glycosylase, catalyzes the first step in base excision repair (BER) by cleaving damaged DNA bases within double-stranded DNA to produce an abasic site. AAG bends DNA by intercalating between the base pairs, causing the damaged base to flip out of the double helix and into the enzyme active site for cleavage. Although AAG represents one of six DNA glycosylase classes, it lacks the helix-hairpin-helix active site motif associated with other BER glycosylases and is structurally distinct from them.


Pssm-ID: 187726  Cd Length: 187  Bit Score: 116.47  E-value: 2.87e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304178124 109 LIGHILWVfdEKQNKLYGSRIIELESYNGVNDKASHAYNNRKTnRNMSMFEKGGISYVYLCYGIHNCLNIVTNIQNIPDA 188
Cdd:cd00540    13 LLGKVLVR--RLPGGVLSGRIVETEAYLGPDDPASHAYRGRTT-RREAMFGPPGTAYVYLIYGMHHCLNVVTGPEGEPAA 89
                          90
                  ....*....|...
gi 1304178124 189 ILVRSTEPLYNIE 201
Cdd:cd00540    90 VLIRALEPLEGLD 102
PRK00802 PRK00802
DNA-3-methyladenine glycosylase;
88-218 1.28e-27

DNA-3-methyladenine glycosylase;


Pssm-ID: 234840  Cd Length: 188  Bit Score: 109.15  E-value: 1.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304178124  88 PLKILNENFYLKDdVLYITEILIGHILWVfdekQNKLYGsRIIELESYNGVNDKASHAYNNRkTNRNMSMFEKGGISYVY 167
Cdd:PRK00802    1 MGMPLPREFFARD-ALEVARDLLGKVLVH----EGGVSG-RIVETEAYIGADDPASHSYRGR-TPRTEVMFGPPGHAYVY 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1304178124 168 LCYGIHNCLNIVTNIQNIPDAILVRSTEPLYNIEYFLSNKFEKISQYLLSN 218
Cdd:PRK00802   74 FIYGMHHCLNVVCGPEGTGAAVLIRALEPLEGIALMRRRRGGKRPEKNLCN 124
3mg TIGR00567
DNA-3-methyladenine glycosylase; This families are based on the phylogenomic analysis of JA ...
92-201 9.92e-25

DNA-3-methyladenine glycosylase; This families are based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). All proteins in this family for which the function is known are involved in the base excision repair of alkylation damage to DNA. The exact specificty of the type of alkylation damage repaired by each of these varies somewhat between species. Substrates include 3-methyl adenine, 7-methyl-guanaine, and 3-methyl-guanine. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273145  Cd Length: 192  Bit Score: 101.04  E-value: 9.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304178124  92 LNENFYLKDdVLYITEILIGHILWVFDEKQNKLYGsRIIELESYNGVNDKASHAYNNRKTNRNMSMFEKGGISYVYLCYG 171
Cdd:TIGR00567   1 MPPEFFQID-AVTLAPRLLGALLVRRLDDGTGVRG-RIVETEAYMGPPDSAAHSYGGRQTPRTDVMFGPPGRLYVYLIYG 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 1304178124 172 IHNCLNIVTNIQNIPDAILVRSTEPLYNIE 201
Cdd:TIGR00567  79 IHYMLNVVAAPEGVPAAVLIRAAEPESGAE 108
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH