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Conserved domains on  [gi|2687195389|ref|WP_334019437|]
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MGMT family protein [Alteromonas sp. F363]

Protein Classification

MGMT family protein( domain architecture ID 10790320)

MGMT (O-6-methylguanine DNA methyltransferase) family protein similar to MGMT, also called methylated-DNA--[protein]-cysteine S-methyltransferase, that repairs alkylated guanine in DNA by stoichiometrically transferring the alkyl group at the O-6 position to a cysteine residue in the enzyme, resulting in its irreversible inactivation

CATH:  1.10.10.10
EC:  2.1.1.63
Gene Ontology:  GO:0006281|GO:0003824|GO:0003908|GO:0003677

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Atl1 COG3695
Alkylated DNA nucleotide flippase Atl1, participates in nucleotide excision repair, Ada-like ...
 1-102 1.59e-30

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


:

Pssm-ID: 442910  Cd Length: 104  Bit Score: 104.50  E-value: 1.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2687195389   1 MPNKAVQSRVEKTLSLVPEGQVISYALLADLCGLPGRARMMGKCLREISADCH--WHRVLRSDGKIAFPVGSDkADEQRE 78
Cdd:COG3695     1 MEMEEFYERVYEVVAQIPPGRVATYGDIAALAGLPRGARQVGRALRALPEGSDlpWHRVVNADGRLSPGHAGG-AEEQRE 79

                          90       100
                  ....*....|....*....|....*
gi 2687195389  79 RLTVEGVVVK-HYRVNMTKFGWKPD 102
Cdd:COG3695    80 LLEAEGVPVVdDGRVDLKRYRWDPD 104
 
Name Accession Description Interval E-value
Atl1 COG3695
Alkylated DNA nucleotide flippase Atl1, participates in nucleotide excision repair, Ada-like ...
 1-102 1.59e-30

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


Pssm-ID: 442910  Cd Length: 104  Bit Score: 104.50  E-value: 1.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2687195389   1 MPNKAVQSRVEKTLSLVPEGQVISYALLADLCGLPGRARMMGKCLREISADCH--WHRVLRSDGKIAFPVGSDkADEQRE 78
Cdd:COG3695     1 MEMEEFYERVYEVVAQIPPGRVATYGDIAALAGLPRGARQVGRALRALPEGSDlpWHRVVNADGRLSPGHAGG-AEEQRE 79

                          90       100
                  ....*....|....*....|....*
gi 2687195389  79 RLTVEGVVVK-HYRVNMTKFGWKPD 102
Cdd:COG3695    80 LLEAEGVPVVdDGRVDLKRYRWDPD 104
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
 7-84 1.55e-16

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: 68.28  E-value: 1.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2687195389   7 QSRVEKTLSLVPEGQVISYALLADLCGLPGRARMMGKCLRE--ISADCHWHRVLRSDGKI-AFPVGsdkADEQRERLTVE 83
Cdd:cd06445     2 QRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARnpIPILIPCHRVVRSDGGLgGYRGG---LERKRELLELE 78


                  .
gi 2687195389  84 G 84
Cdd:cd06445    79 G 79
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
 7-85 7.16e-16

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: 66.61  E-value: 7.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2687195389   7 QSRVEKTLSLVPEGQVISYALLADLCGLPGRARMMGKCLRE--ISADCHWHRVLRSDGKIAFPVGSdkADEQRERLTVEG 84
Cdd:pfam01035   3 QRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGAnpIPIIVPCHRVVGSDGSLGGYAGG--LERKRALLELEG 80


                  .
gi 2687195389  85 V 85
Cdd:pfam01035  81 V 81
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
5-62 1.31e-03

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


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 36.69  E-value: 1.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2687195389   5 AVQSRVEKTLSLVPEGQVISYALLADLCGLPGRAR-MMGKCLRE---ISADChwHRVLRSDG 62
Cdd:PRK15435  270 AFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRaVASACAANklaIVIPC--HRVVRGDG 329
 
Name Accession Description Interval E-value
Atl1 COG3695
Alkylated DNA nucleotide flippase Atl1, participates in nucleotide excision repair, Ada-like ...
 1-102 1.59e-30

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


Pssm-ID: 442910  Cd Length: 104  Bit Score: 104.50  E-value: 1.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2687195389   1 MPNKAVQSRVEKTLSLVPEGQVISYALLADLCGLPGRARMMGKCLREISADCH--WHRVLRSDGKIAFPVGSDkADEQRE 78
Cdd:COG3695     1 MEMEEFYERVYEVVAQIPPGRVATYGDIAALAGLPRGARQVGRALRALPEGSDlpWHRVVNADGRLSPGHAGG-AEEQRE 79

                          90       100
                  ....*....|....*....|....*
gi 2687195389  79 RLTVEGVVVK-HYRVNMTKFGWKPD 102
Cdd:COG3695    80 LLEAEGVPVVdDGRVDLKRYRWDPD 104
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
 7-84 1.55e-16

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: 68.28  E-value: 1.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2687195389   7 QSRVEKTLSLVPEGQVISYALLADLCGLPGRARMMGKCLRE--ISADCHWHRVLRSDGKI-AFPVGsdkADEQRERLTVE 83
Cdd:cd06445     2 QRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARnpIPILIPCHRVVRSDGGLgGYRGG---LERKRELLELE 78


                  .
gi 2687195389  84 G 84
Cdd:cd06445    79 G 79
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
 7-85 7.16e-16

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: 66.61  E-value: 7.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2687195389   7 QSRVEKTLSLVPEGQVISYALLADLCGLPGRARMMGKCLRE--ISADCHWHRVLRSDGKIAFPVGSdkADEQRERLTVEG 84
Cdd:pfam01035   3 QRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGAnpIPIIVPCHRVVGSDGSLGGYAGG--LERKRALLELEG 80


                  .
gi 2687195389  85 V 85
Cdd:pfam01035  81 V 81
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
 7-64 9.72e-06

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


Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 41.78  E-value: 9.72e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2687195389   7 QSRVEKTLSLVPEGQVISYALLADLCGLPGRAR----MMGK--------ClreisadchwHRVLRSDGKI 64
Cdd:COG0350    81 QRRVWEALRKIPYGETVTYGELARAIGRPKAARavgsACGAnpipiiipC----------HRVIGADGSL 140
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
5-62 1.31e-03

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


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 36.69  E-value: 1.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2687195389   5 AVQSRVEKTLSLVPEGQVISYALLADLCGLPGRAR-MMGKCLRE---ISADChwHRVLRSDG 62
Cdd:PRK15435  270 AFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRaVASACAANklaIVIPC--HRVVRGDG 329
 
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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