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Conserved domains on  [gi|490440037|ref|WP_004311039|]
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MULTISPECIES: class I SAM-dependent methyltransferase [Bacteroides]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10614797)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

CATH:  2.20.25.110
EC:  2.1.-.-|2.1.1.-
Gene Ontology:  GO:0032259|GO:0008757|GO:0008168|GO:1904047
PubMed:  12504684|12826405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 185-276 1.91e-05

Methyltransferase domain; This family appears to be a methyltransferase domain.


:

Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 42.94  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490440037  185 LDVGGNTGRWATKCVSYDDAvEVTIMDL-PQQLEMMRQQTKDLPGAMR-IHGYGANLldpevPFPTG-FDAIWMSQFLDC 261
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGA-RVTGVDLsPEMLERARERAAEAGLNVEfVQGDAEDL-----PFPDGsFDLVVSSGVLHH 75

                          90
                  ....*....|....*
gi 490440037  262 FSEEEVTSILTRAAR 276
Cdd:pfam13649  76 LPDPDLEAALREIAR 90
 
Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 185-276 1.91e-05

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 42.94  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490440037  185 LDVGGNTGRWATKCVSYDDAvEVTIMDL-PQQLEMMRQQTKDLPGAMR-IHGYGANLldpevPFPTG-FDAIWMSQFLDC 261
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGA-RVTGVDLsPEMLERARERAAEAGLNVEfVQGDAEDL-----PFPDGsFDLVVSSGVLHH 75

                          90
                  ....*....|....*
gi 490440037  262 FSEEEVTSILTRAAR 276
Cdd:pfam13649  76 LPDPDLEAALREIAR 90
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 183-287 5.85e-03

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 36.25  E-value: 5.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490440037 183 TLLDVGGNTGRWATKCVSYDDAvEVTIMDL-PQQLEMMRQQtKDLPGAMRIHGYGANLLDPEVPFPTGFDAIWMSQFLdC 261
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGA-RVTGVDIsPVALELARKA-AAALLADNVEVLKGDAEELPPEADESFDVIISDPPL-H 77

                         90       100
                 ....*....|....*....|....*.
gi 490440037 262 FSEEEVTSILTRAARSMSGESRLYIM 287
Cdd:cd02440   78 HLVEDLARFLEEARRLLKPGGVLVLT 103
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 157-308 5.98e-03

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 37.59  E-value: 5.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490440037 157 WFGFDHYYSDCSFDEALAIVFA-RHPKTLLDVGGNTGRWATKCVSYDDAvEVTIMDL-PQQLEMMRQQTKDLpGAMRIHG 234
Cdd:COG0500    2 WDSYYSDELLPGLAALLALLERlPKGGRVLDLGCGTGRNLLALAARFGG-RVIGIDLsPEAIALARARAAKA-GLGNVEF 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490440037 235 YGANLLDPEVPFPTGFDAIWMSQFLDCFSEEEVTSILTRAARSMSGESRLYIMETFWNRQKFDTAAYCLTQISL 308
Cdd:COG0500   80 LVADLAELDPLPAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLLSASDAAAALSLARLLLLATASL 153
 
Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 185-276 1.91e-05

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 42.94  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490440037  185 LDVGGNTGRWATKCVSYDDAvEVTIMDL-PQQLEMMRQQTKDLPGAMR-IHGYGANLldpevPFPTG-FDAIWMSQFLDC 261
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGA-RVTGVDLsPEMLERARERAAEAGLNVEfVQGDAEDL-----PFPDGsFDLVVSSGVLHH 75

                          90
                  ....*....|....*
gi 490440037  262 FSEEEVTSILTRAAR 276
Cdd:pfam13649  76 LPDPDLEAALREIAR 90
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 185-278 6.76e-04

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 38.50  E-value: 6.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490440037  185 LDVGGNTGRWATKCVSYDDAVEVTIMDL-PQQLEMMRQQTKDLPGAmRIHGYGANLLDPEVPFPTGFDAIWMSQFLDCFs 263
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDIsPAALEAARERLAALGLL-NAVRVELFQLDLGELDPGSFDVVVASNVLHHL- 78

                          90
                  ....*....|....*
gi 490440037  264 eEEVTSILTRAARSM 278
Cdd:pfam08242  79 -ADPRAVLRNIRRLL 92
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 183-287 5.85e-03

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 36.25  E-value: 5.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490440037 183 TLLDVGGNTGRWATKCVSYDDAvEVTIMDL-PQQLEMMRQQtKDLPGAMRIHGYGANLLDPEVPFPTGFDAIWMSQFLdC 261
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGA-RVTGVDIsPVALELARKA-AAALLADNVEVLKGDAEELPPEADESFDVIISDPPL-H 77

                         90       100
                 ....*....|....*....|....*.
gi 490440037 262 FSEEEVTSILTRAARSMSGESRLYIM 287
Cdd:cd02440   78 HLVEDLARFLEEARRLLKPGGVLVLT 103
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 157-308 5.98e-03

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 37.59  E-value: 5.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490440037 157 WFGFDHYYSDCSFDEALAIVFA-RHPKTLLDVGGNTGRWATKCVSYDDAvEVTIMDL-PQQLEMMRQQTKDLpGAMRIHG 234
Cdd:COG0500    2 WDSYYSDELLPGLAALLALLERlPKGGRVLDLGCGTGRNLLALAARFGG-RVIGIDLsPEAIALARARAAKA-GLGNVEF 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490440037 235 YGANLLDPEVPFPTGFDAIWMSQFLDCFSEEEVTSILTRAARSMSGESRLYIMETFWNRQKFDTAAYCLTQISL 308
Cdd:COG0500   80 LVADLAELDPLPAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLLSASDAAAALSLARLLLLATASL 153
 
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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